data_8RRJ
# 
_entry.id   8RRJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8RRJ         pdb_00008rrj 10.2210/pdb8rrj/pdb 
WWPDB D_1292135902 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-14 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RRJ 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-22 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
4 edward.petri@dbe.uns.ac.rs    Edward  Petri    T 'principal investigator/group leader' 0000-0002-3650-1523 
5 pavlina.rezacova@uochb.cas.cz Pavlina Rezacova M 'principal investigator/group leader' 0000-0001-9626-346X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Petri, E.T.'     1 0000-0002-3650-1523 
'Skerlova, J.'    2 0000-0002-9579-4047 
'Plavsa, J.J.'    3 ?                   
'Brynda, J.'      4 ?                   
'Ajdukovic, J.J.' 5 0000-0003-0218-3640 
'Bekic, S.'       6 0000-0002-9020-698X 
'Celic, A.S.'     7 0000-0002-1058-6872 
'Rezacova, P.'    8 0000-0001-9626-346X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'The structural basis of aldo-keto reductase 1C3 inhibition by 17alpha-picolyl and 17(E)-picolinylidene androstane derivatives' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Plavsa, J.J.'    1 ?                   
primary 'Skerlova, J.'    2 0000-0002-9579-4047 
primary 'Brynda, J.'      3 ?                   
primary 'Ajdukovic, J.J.' 4 0000-0003-0218-3640 
primary 'Bekic, S.'       5 0000-0002-9020-698X 
primary 'Celic, A.S.'     6 0000-0002-1058-6872 
primary 'Rezacova, P.'    7 0000-0001-9626-346X 
primary 'Petri, E.T.'     8 0000-0002-3650-1523 
# 
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 'Aldo-keto reductase family 1 member C3' 37188.508 2   
1.1.1.-,1.1.1.210,1.1.1.53,1.1.1.62,1.1.1.357,1.1.1.188,1.1.1.239,1.1.1.64 ? ? ? 
2 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 743.405   2   ? ? ? ? 
3 non-polymer syn 
;(3~{Z},8~{R},9~{S},10~{R},13~{S},14~{S},17~{R})-3-hydroxyimino-10,13-dimethyl-17-(pyridin-2-ylmethyl)-2,6,7,8,9,11,12,14,15,16-decahydro-1~{H}-cyclopenta[a]phenanthren-17-ol
;
394.550   2   ?                                                                          ? ? ? 
4 non-polymer syn 'SODIUM ION' 22.990    11  ?                                                                          ? ? ? 
5 water       nat water 18.015    581 ?                                                                          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;17-beta-hydroxysteroid dehydrogenase type 5,17-beta-HSD 5,3-alpha-HSD type II,brain,3-alpha-hydroxysteroid dehydrogenase type 2,3-alpha-HSD type 2,Chlordecone reductase homolog HAKRb,Dihydrodiol dehydrogenase 3,DD-3,DD3,Dihydrodiol dehydrogenase type I,HA1753,Prostaglandin F synthase,PGFS,Testosterone 17-beta-dehydrogenase 5
;
# 
_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       
;GSHMDSKHQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKRE
DIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDA
GLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLE
DPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFASHPNY
PYSDEY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSHMDSKHQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKRE
DIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDA
GLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLE
DPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFASHPNY
PYSDEY
;
_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 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NAP   
3 
;(3~{Z},8~{R},9~{S},10~{R},13~{S},14~{S},17~{R})-3-hydroxyimino-10,13-dimethyl-17-(pyridin-2-ylmethyl)-2,6,7,8,9,11,12,14,15,16-decahydro-1~{H}-cyclopenta[a]phenanthren-17-ol
;
A1H2U 
4 'SODIUM ION' NA    
5 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   HIS n 
1 4   MET n 
1 5   ASP n 
1 6   SER n 
1 7   LYS n 
1 8   HIS n 
1 9   GLN n 
1 10  CYS n 
1 11  VAL n 
1 12  LYS n 
1 13  LEU n 
1 14  ASN n 
1 15  ASP n 
1 16  GLY n 
1 17  HIS n 
1 18  PHE n 
1 19  MET n 
1 20  PRO n 
1 21  VAL n 
1 22  LEU n 
1 23  GLY n 
1 24  PHE n 
1 25  GLY n 
1 26  THR n 
1 27  TYR n 
1 28  ALA n 
1 29  PRO n 
1 30  PRO n 
1 31  GLU n 
1 32  VAL n 
1 33  PRO n 
1 34  ARG n 
1 35  SER n 
1 36  LYS n 
1 37  ALA n 
1 38  LEU n 
1 39  GLU n 
1 40  VAL n 
1 41  THR n 
1 42  LYS n 
1 43  LEU n 
1 44  ALA n 
1 45  ILE n 
1 46  GLU n 
1 47  ALA n 
1 48  GLY n 
1 49  PHE n 
1 50  ARG n 
1 51  HIS n 
1 52  ILE n 
1 53  ASP n 
1 54  SER n 
1 55  ALA n 
1 56  HIS n 
1 57  LEU n 
1 58  TYR n 
1 59  ASN n 
1 60  ASN n 
1 61  GLU n 
1 62  GLU n 
1 63  GLN n 
1 64  VAL n 
1 65  GLY n 
1 66  LEU n 
1 67  ALA n 
1 68  ILE n 
1 69  ARG n 
1 70  SER n 
1 71  LYS n 
1 72  ILE n 
1 73  ALA n 
1 74  ASP n 
1 75  GLY n 
1 76  SER n 
1 77  VAL n 
1 78  LYS n 
1 79  ARG n 
1 80  GLU n 
1 81  ASP n 
1 82  ILE n 
1 83  PHE n 
1 84  TYR n 
1 85  THR n 
1 86  SER n 
1 87  LYS n 
1 88  LEU n 
1 89  TRP n 
1 90  SER n 
1 91  THR n 
1 92  PHE n 
1 93  HIS n 
1 94  ARG n 
1 95  PRO n 
1 96  GLU n 
1 97  LEU n 
1 98  VAL n 
1 99  ARG n 
1 100 PRO n 
1 101 ALA n 
1 102 LEU n 
1 103 GLU n 
1 104 ASN n 
1 105 SER n 
1 106 LEU n 
1 107 LYS n 
1 108 LYS n 
1 109 ALA n 
1 110 GLN n 
1 111 LEU n 
1 112 ASP n 
1 113 TYR n 
1 114 VAL n 
1 115 ASP n 
1 116 LEU n 
1 117 TYR n 
1 118 LEU n 
1 119 ILE n 
1 120 HIS n 
1 121 SER n 
1 122 PRO n 
1 123 MET n 
1 124 SER n 
1 125 LEU n 
1 126 LYS n 
1 127 PRO n 
1 128 GLY n 
1 129 GLU n 
1 130 GLU n 
1 131 LEU n 
1 132 SER n 
1 133 PRO n 
1 134 THR n 
1 135 ASP n 
1 136 GLU n 
1 137 ASN n 
1 138 GLY n 
1 139 LYS n 
1 140 VAL n 
1 141 ILE n 
1 142 PHE n 
1 143 ASP n 
1 144 ILE n 
1 145 VAL n 
1 146 ASP n 
1 147 LEU n 
1 148 CYS n 
1 149 THR n 
1 150 THR n 
1 151 TRP n 
1 152 GLU n 
1 153 ALA n 
1 154 MET n 
1 155 GLU n 
1 156 LYS n 
1 157 CYS n 
1 158 LYS n 
1 159 ASP n 
1 160 ALA n 
1 161 GLY n 
1 162 LEU n 
1 163 ALA n 
1 164 LYS n 
1 165 SER n 
1 166 ILE n 
1 167 GLY n 
1 168 VAL n 
1 169 SER n 
1 170 ASN n 
1 171 PHE n 
1 172 ASN n 
1 173 ARG n 
1 174 ARG n 
1 175 GLN n 
1 176 LEU n 
1 177 GLU n 
1 178 MET n 
1 179 ILE n 
1 180 LEU n 
1 181 ASN n 
1 182 LYS n 
1 183 PRO n 
1 184 GLY n 
1 185 LEU n 
1 186 LYS n 
1 187 TYR n 
1 188 LYS n 
1 189 PRO n 
1 190 VAL n 
1 191 CYS n 
1 192 ASN n 
1 193 GLN n 
1 194 VAL n 
1 195 GLU n 
1 196 CYS n 
1 197 HIS n 
1 198 PRO n 
1 199 TYR n 
1 200 PHE n 
1 201 ASN n 
1 202 ARG n 
1 203 SER n 
1 204 LYS n 
1 205 LEU n 
1 206 LEU n 
1 207 ASP n 
1 208 PHE n 
1 209 CYS n 
1 210 LYS n 
1 211 SER n 
1 212 LYS n 
1 213 ASP n 
1 214 ILE n 
1 215 VAL n 
1 216 LEU n 
1 217 VAL n 
1 218 ALA n 
1 219 TYR n 
1 220 SER n 
1 221 ALA n 
1 222 LEU n 
1 223 GLY n 
1 224 SER n 
1 225 GLN n 
1 226 ARG n 
1 227 ASP n 
1 228 LYS n 
1 229 ARG n 
1 230 TRP n 
1 231 VAL n 
1 232 ASP n 
1 233 PRO n 
1 234 ASN n 
1 235 SER n 
1 236 PRO n 
1 237 VAL n 
1 238 LEU n 
1 239 LEU n 
1 240 GLU n 
1 241 ASP n 
1 242 PRO n 
1 243 VAL n 
1 244 LEU n 
1 245 CYS n 
1 246 ALA n 
1 247 LEU n 
1 248 ALA n 
1 249 LYS n 
1 250 LYS n 
1 251 HIS n 
1 252 LYS n 
1 253 ARG n 
1 254 THR n 
1 255 PRO n 
1 256 ALA n 
1 257 LEU n 
1 258 ILE n 
1 259 ALA n 
1 260 LEU n 
1 261 ARG n 
1 262 TYR n 
1 263 GLN n 
1 264 LEU n 
1 265 GLN n 
1 266 ARG n 
1 267 GLY n 
1 268 VAL n 
1 269 VAL n 
1 270 VAL n 
1 271 LEU n 
1 272 ALA n 
1 273 LYS n 
1 274 SER n 
1 275 TYR n 
1 276 ASN n 
1 277 GLU n 
1 278 GLN n 
1 279 ARG n 
1 280 ILE n 
1 281 ARG n 
1 282 GLN n 
1 283 ASN n 
1 284 VAL n 
1 285 GLN n 
1 286 VAL n 
1 287 PHE n 
1 288 GLU n 
1 289 PHE n 
1 290 GLN n 
1 291 LEU n 
1 292 THR n 
1 293 ALA n 
1 294 GLU n 
1 295 ASP n 
1 296 MET n 
1 297 LYS n 
1 298 ALA n 
1 299 ILE n 
1 300 ASP n 
1 301 GLY n 
1 302 LEU n 
1 303 ASP n 
1 304 ARG n 
1 305 ASN n 
1 306 LEU n 
1 307 HIS n 
1 308 TYR n 
1 309 PHE n 
1 310 ASN n 
1 311 SER n 
1 312 ASP n 
1 313 SER n 
1 314 PHE n 
1 315 ALA n 
1 316 SER n 
1 317 HIS n 
1 318 PRO n 
1 319 ASN n 
1 320 TYR n 
1 321 PRO n 
1 322 TYR n 
1 323 SER n 
1 324 ASP n 
1 325 GLU n 
1 326 TYR 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                   326 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'AKR1C3, DDH1, HSD17B5, KIAA0119, PGFS' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'PET28B(+)' 
_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 
A1H2U non-polymer         . 
;(3~{Z},8~{R},9~{S},10~{R},13~{S},14~{S},17~{R})-3-hydroxyimino-10,13-dimethyl-17-(pyridin-2-ylmethyl)-2,6,7,8,9,11,12,14,15,16-decahydro-1~{H}-cyclopenta[a]phenanthren-17-ol
;
'17beta-Hydroxy-17alpha-picolyl-androst-4-en-(3Z)-one oxime' 'C25 H34 N2 O2'     394.550 
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 
NA    non-polymer         . 'SODIUM ION' ?                                                            'Na 1'              22.990  
NAP   non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3' 743.405 
PHE   'L-peptide linking' y PHENYLALANINE ?                                                            'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ?                                                            'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ?                                                            'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ?                                                            'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                                                            'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ?                                                            'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ?                                                            'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   SER 2   -1  ?   ?   ?   A . n 
A 1 3   HIS 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   ?   ?   ?   A . n 
A 1 5   ASP 5   2   ?   ?   ?   A . n 
A 1 6   SER 6   3   ?   ?   ?   A . n 
A 1 7   LYS 7   4   ?   ?   ?   A . n 
A 1 8   HIS 8   5   ?   ?   ?   A . n 
A 1 9   GLN 9   6   6   GLN GLN A . n 
A 1 10  CYS 10  7   7   CYS CYS A . n 
A 1 11  VAL 11  8   8   VAL VAL A . n 
A 1 12  LYS 12  9   9   LYS LYS A . n 
A 1 13  LEU 13  10  10  LEU LEU A . n 
A 1 14  ASN 14  11  11  ASN ASN A . n 
A 1 15  ASP 15  12  12  ASP ASP A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  HIS 17  14  14  HIS HIS A . n 
A 1 18  PHE 18  15  15  PHE PHE A . n 
A 1 19  MET 19  16  16  MET MET A . n 
A 1 20  PRO 20  17  17  PRO PRO A . n 
A 1 21  VAL 21  18  18  VAL VAL A . n 
A 1 22  LEU 22  19  19  LEU LEU A . n 
A 1 23  GLY 23  20  20  GLY GLY A . n 
A 1 24  PHE 24  21  21  PHE PHE A . n 
A 1 25  GLY 25  22  22  GLY GLY A . n 
A 1 26  THR 26  23  23  THR THR A . n 
A 1 27  TYR 27  24  24  TYR TYR A . n 
A 1 28  ALA 28  25  25  ALA ALA A . n 
A 1 29  PRO 29  26  26  PRO PRO A . n 
A 1 30  PRO 30  27  27  PRO PRO A . n 
A 1 31  GLU 31  28  28  GLU GLU A . n 
A 1 32  VAL 32  29  29  VAL VAL A . n 
A 1 33  PRO 33  30  30  PRO PRO A . n 
A 1 34  ARG 34  31  31  ARG ARG A . n 
A 1 35  SER 35  32  32  SER SER A . n 
A 1 36  LYS 36  33  33  LYS LYS A . n 
A 1 37  ALA 37  34  34  ALA ALA A . n 
A 1 38  LEU 38  35  35  LEU LEU A . n 
A 1 39  GLU 39  36  36  GLU GLU A . n 
A 1 40  VAL 40  37  37  VAL VAL A . n 
A 1 41  THR 41  38  38  THR THR A . n 
A 1 42  LYS 42  39  39  LYS LYS A . n 
A 1 43  LEU 43  40  40  LEU LEU A . n 
A 1 44  ALA 44  41  41  ALA ALA A . n 
A 1 45  ILE 45  42  42  ILE ILE A . n 
A 1 46  GLU 46  43  43  GLU GLU A . n 
A 1 47  ALA 47  44  44  ALA ALA A . n 
A 1 48  GLY 48  45  45  GLY GLY A . n 
A 1 49  PHE 49  46  46  PHE PHE A . n 
A 1 50  ARG 50  47  47  ARG ARG A . n 
A 1 51  HIS 51  48  48  HIS HIS A . n 
A 1 52  ILE 52  49  49  ILE ILE A . n 
A 1 53  ASP 53  50  50  ASP ASP A . n 
A 1 54  SER 54  51  51  SER SER A . n 
A 1 55  ALA 55  52  52  ALA ALA A . n 
A 1 56  HIS 56  53  53  HIS HIS A . n 
A 1 57  LEU 57  54  54  LEU LEU A . n 
A 1 58  TYR 58  55  55  TYR TYR A . n 
A 1 59  ASN 59  56  56  ASN ASN A . n 
A 1 60  ASN 60  57  57  ASN ASN A . n 
A 1 61  GLU 61  58  58  GLU GLU A . n 
A 1 62  GLU 62  59  59  GLU GLU A . n 
A 1 63  GLN 63  60  60  GLN GLN A . n 
A 1 64  VAL 64  61  61  VAL VAL A . n 
A 1 65  GLY 65  62  62  GLY GLY A . n 
A 1 66  LEU 66  63  63  LEU LEU A . n 
A 1 67  ALA 67  64  64  ALA ALA A . n 
A 1 68  ILE 68  65  65  ILE ILE A . n 
A 1 69  ARG 69  66  66  ARG ARG A . n 
A 1 70  SER 70  67  67  SER SER A . n 
A 1 71  LYS 71  68  68  LYS LYS A . n 
A 1 72  ILE 72  69  69  ILE ILE A . n 
A 1 73  ALA 73  70  70  ALA ALA A . n 
A 1 74  ASP 74  71  71  ASP ASP A . n 
A 1 75  GLY 75  72  72  GLY GLY A . n 
A 1 76  SER 76  73  73  SER SER A . n 
A 1 77  VAL 77  74  74  VAL VAL A . n 
A 1 78  LYS 78  75  75  LYS LYS A . n 
A 1 79  ARG 79  76  76  ARG ARG A . n 
A 1 80  GLU 80  77  77  GLU GLU A . n 
A 1 81  ASP 81  78  78  ASP ASP A . n 
A 1 82  ILE 82  79  79  ILE ILE A . n 
A 1 83  PHE 83  80  80  PHE PHE A . n 
A 1 84  TYR 84  81  81  TYR TYR A . n 
A 1 85  THR 85  82  82  THR THR A . n 
A 1 86  SER 86  83  83  SER SER A . n 
A 1 87  LYS 87  84  84  LYS LYS A . n 
A 1 88  LEU 88  85  85  LEU LEU A . n 
A 1 89  TRP 89  86  86  TRP TRP A . n 
A 1 90  SER 90  87  87  SER SER A . n 
A 1 91  THR 91  88  88  THR THR A . n 
A 1 92  PHE 92  89  89  PHE PHE A . n 
A 1 93  HIS 93  90  90  HIS HIS A . n 
A 1 94  ARG 94  91  91  ARG ARG A . n 
A 1 95  PRO 95  92  92  PRO PRO A . n 
A 1 96  GLU 96  93  93  GLU GLU A . n 
A 1 97  LEU 97  94  94  LEU LEU A . n 
A 1 98  VAL 98  95  95  VAL VAL A . n 
A 1 99  ARG 99  96  96  ARG ARG A . n 
A 1 100 PRO 100 97  97  PRO PRO A . n 
A 1 101 ALA 101 98  98  ALA ALA A . n 
A 1 102 LEU 102 99  99  LEU LEU A . n 
A 1 103 GLU 103 100 100 GLU GLU A . n 
A 1 104 ASN 104 101 101 ASN ASN A . n 
A 1 105 SER 105 102 102 SER SER A . n 
A 1 106 LEU 106 103 103 LEU LEU A . n 
A 1 107 LYS 107 104 104 LYS LYS A . n 
A 1 108 LYS 108 105 105 LYS LYS A . n 
A 1 109 ALA 109 106 106 ALA ALA A . n 
A 1 110 GLN 110 107 107 GLN GLN A . n 
A 1 111 LEU 111 108 108 LEU LEU A . n 
A 1 112 ASP 112 109 109 ASP ASP A . n 
A 1 113 TYR 113 110 110 TYR TYR A . n 
A 1 114 VAL 114 111 111 VAL VAL A . n 
A 1 115 ASP 115 112 112 ASP ASP A . n 
A 1 116 LEU 116 113 113 LEU LEU A . n 
A 1 117 TYR 117 114 114 TYR TYR A . n 
A 1 118 LEU 118 115 115 LEU LEU A . n 
A 1 119 ILE 119 116 116 ILE ILE A . n 
A 1 120 HIS 120 117 117 HIS HIS A . n 
A 1 121 SER 121 118 118 SER SER A . n 
A 1 122 PRO 122 119 119 PRO PRO A . n 
A 1 123 MET 123 120 120 MET MET A . n 
A 1 124 SER 124 121 121 SER SER A . n 
A 1 125 LEU 125 122 122 LEU LEU A . n 
A 1 126 LYS 126 123 123 LYS LYS A . n 
A 1 127 PRO 127 124 124 PRO PRO A . n 
A 1 128 GLY 128 125 125 GLY GLY A . n 
A 1 129 GLU 129 126 126 GLU GLU A . n 
A 1 130 GLU 130 127 127 GLU GLU A . n 
A 1 131 LEU 131 128 128 LEU LEU A . n 
A 1 132 SER 132 129 129 SER SER A . n 
A 1 133 PRO 133 130 130 PRO PRO A . n 
A 1 134 THR 134 131 131 THR THR A . n 
A 1 135 ASP 135 132 132 ASP ASP A . n 
A 1 136 GLU 136 133 133 GLU GLU A . n 
A 1 137 ASN 137 134 134 ASN ASN A . n 
A 1 138 GLY 138 135 135 GLY GLY A . n 
A 1 139 LYS 139 136 136 LYS LYS A . n 
A 1 140 VAL 140 137 137 VAL VAL A . n 
A 1 141 ILE 141 138 138 ILE ILE A . n 
A 1 142 PHE 142 139 139 PHE PHE A . n 
A 1 143 ASP 143 140 140 ASP ASP A . n 
A 1 144 ILE 144 141 141 ILE ILE A . n 
A 1 145 VAL 145 142 142 VAL VAL A . n 
A 1 146 ASP 146 143 143 ASP ASP A . n 
A 1 147 LEU 147 144 144 LEU LEU A . n 
A 1 148 CYS 148 145 145 CYS CYS A . n 
A 1 149 THR 149 146 146 THR THR A . n 
A 1 150 THR 150 147 147 THR THR A . n 
A 1 151 TRP 151 148 148 TRP TRP A . n 
A 1 152 GLU 152 149 149 GLU GLU A . n 
A 1 153 ALA 153 150 150 ALA ALA A . n 
A 1 154 MET 154 151 151 MET MET A . n 
A 1 155 GLU 155 152 152 GLU GLU A . n 
A 1 156 LYS 156 153 153 LYS LYS A . n 
A 1 157 CYS 157 154 154 CYS CYS A . n 
A 1 158 LYS 158 155 155 LYS LYS A . n 
A 1 159 ASP 159 156 156 ASP ASP A . n 
A 1 160 ALA 160 157 157 ALA ALA A . n 
A 1 161 GLY 161 158 158 GLY GLY A . n 
A 1 162 LEU 162 159 159 LEU LEU A . n 
A 1 163 ALA 163 160 160 ALA ALA A . n 
A 1 164 LYS 164 161 161 LYS LYS A . n 
A 1 165 SER 165 162 162 SER SER A . n 
A 1 166 ILE 166 163 163 ILE ILE A . n 
A 1 167 GLY 167 164 164 GLY GLY A . n 
A 1 168 VAL 168 165 165 VAL VAL A . n 
A 1 169 SER 169 166 166 SER SER A . n 
A 1 170 ASN 170 167 167 ASN ASN A . n 
A 1 171 PHE 171 168 168 PHE PHE A . n 
A 1 172 ASN 172 169 169 ASN ASN A . n 
A 1 173 ARG 173 170 170 ARG ARG A . n 
A 1 174 ARG 174 171 171 ARG ARG A . n 
A 1 175 GLN 175 172 172 GLN GLN A . n 
A 1 176 LEU 176 173 173 LEU LEU A . n 
A 1 177 GLU 177 174 174 GLU GLU A . n 
A 1 178 MET 178 175 175 MET MET A . n 
A 1 179 ILE 179 176 176 ILE ILE A . n 
A 1 180 LEU 180 177 177 LEU LEU A . n 
A 1 181 ASN 181 178 178 ASN ASN A . n 
A 1 182 LYS 182 179 179 LYS LYS A . n 
A 1 183 PRO 183 180 180 PRO PRO A . n 
A 1 184 GLY 184 181 181 GLY GLY A . n 
A 1 185 LEU 185 182 182 LEU LEU A . n 
A 1 186 LYS 186 183 183 LYS LYS A . n 
A 1 187 TYR 187 184 184 TYR TYR A . n 
A 1 188 LYS 188 185 185 LYS LYS A . n 
A 1 189 PRO 189 186 186 PRO PRO A . n 
A 1 190 VAL 190 187 187 VAL VAL A . n 
A 1 191 CYS 191 188 188 CYS CYS A . n 
A 1 192 ASN 192 189 189 ASN ASN A . n 
A 1 193 GLN 193 190 190 GLN GLN A . n 
A 1 194 VAL 194 191 191 VAL VAL A . n 
A 1 195 GLU 195 192 192 GLU GLU A . n 
A 1 196 CYS 196 193 193 CYS CYS A . n 
A 1 197 HIS 197 194 194 HIS HIS A . n 
A 1 198 PRO 198 195 195 PRO PRO A . n 
A 1 199 TYR 199 196 196 TYR TYR A . n 
A 1 200 PHE 200 197 197 PHE PHE A . n 
A 1 201 ASN 201 198 198 ASN ASN A . n 
A 1 202 ARG 202 199 199 ARG ARG A . n 
A 1 203 SER 203 200 200 SER SER A . n 
A 1 204 LYS 204 201 201 LYS LYS A . n 
A 1 205 LEU 205 202 202 LEU LEU A . n 
A 1 206 LEU 206 203 203 LEU LEU A . n 
A 1 207 ASP 207 204 204 ASP ASP A . n 
A 1 208 PHE 208 205 205 PHE PHE A . n 
A 1 209 CYS 209 206 206 CYS CYS A . n 
A 1 210 LYS 210 207 207 LYS LYS A . n 
A 1 211 SER 211 208 208 SER SER A . n 
A 1 212 LYS 212 209 209 LYS LYS A . n 
A 1 213 ASP 213 210 210 ASP ASP A . n 
A 1 214 ILE 214 211 211 ILE ILE A . n 
A 1 215 VAL 215 212 212 VAL VAL A . n 
A 1 216 LEU 216 213 213 LEU LEU A . n 
A 1 217 VAL 217 214 214 VAL VAL A . n 
A 1 218 ALA 218 215 215 ALA ALA A . n 
A 1 219 TYR 219 216 216 TYR TYR A . n 
A 1 220 SER 220 217 217 SER SER A . n 
A 1 221 ALA 221 218 218 ALA ALA A . n 
A 1 222 LEU 222 219 219 LEU LEU A . n 
A 1 223 GLY 223 220 220 GLY GLY A . n 
A 1 224 SER 224 221 221 SER SER A . n 
A 1 225 GLN 225 222 222 GLN GLN A . n 
A 1 226 ARG 226 223 223 ARG ARG A . n 
A 1 227 ASP 227 224 224 ASP ASP A . n 
A 1 228 LYS 228 225 225 LYS LYS A . n 
A 1 229 ARG 229 226 226 ARG ARG A . n 
A 1 230 TRP 230 227 227 TRP TRP A . n 
A 1 231 VAL 231 228 228 VAL VAL A . n 
A 1 232 ASP 232 229 229 ASP ASP A . n 
A 1 233 PRO 233 230 230 PRO PRO A . n 
A 1 234 ASN 234 231 231 ASN ASN A . n 
A 1 235 SER 235 232 232 SER SER A . n 
A 1 236 PRO 236 233 233 PRO PRO A . n 
A 1 237 VAL 237 234 234 VAL VAL A . n 
A 1 238 LEU 238 235 235 LEU LEU A . n 
A 1 239 LEU 239 236 236 LEU LEU A . n 
A 1 240 GLU 240 237 237 GLU GLU A . n 
A 1 241 ASP 241 238 238 ASP ASP A . n 
A 1 242 PRO 242 239 239 PRO PRO A . n 
A 1 243 VAL 243 240 240 VAL VAL A . n 
A 1 244 LEU 244 241 241 LEU LEU A . n 
A 1 245 CYS 245 242 242 CYS CYS A . n 
A 1 246 ALA 246 243 243 ALA ALA A . n 
A 1 247 LEU 247 244 244 LEU LEU A . n 
A 1 248 ALA 248 245 245 ALA ALA A . n 
A 1 249 LYS 249 246 246 LYS LYS A . n 
A 1 250 LYS 250 247 247 LYS LYS A . n 
A 1 251 HIS 251 248 248 HIS HIS A . n 
A 1 252 LYS 252 249 249 LYS LYS A . n 
A 1 253 ARG 253 250 250 ARG ARG A . n 
A 1 254 THR 254 251 251 THR THR A . n 
A 1 255 PRO 255 252 252 PRO PRO A . n 
A 1 256 ALA 256 253 253 ALA ALA A . n 
A 1 257 LEU 257 254 254 LEU LEU A . n 
A 1 258 ILE 258 255 255 ILE ILE A . n 
A 1 259 ALA 259 256 256 ALA ALA A . n 
A 1 260 LEU 260 257 257 LEU LEU A . n 
A 1 261 ARG 261 258 258 ARG ARG A . n 
A 1 262 TYR 262 259 259 TYR TYR A . n 
A 1 263 GLN 263 260 260 GLN GLN A . n 
A 1 264 LEU 264 261 261 LEU LEU A . n 
A 1 265 GLN 265 262 262 GLN GLN A . n 
A 1 266 ARG 266 263 263 ARG ARG A . n 
A 1 267 GLY 267 264 264 GLY GLY A . n 
A 1 268 VAL 268 265 265 VAL VAL A . n 
A 1 269 VAL 269 266 266 VAL VAL A . n 
A 1 270 VAL 270 267 267 VAL VAL A . n 
A 1 271 LEU 271 268 268 LEU LEU A . n 
A 1 272 ALA 272 269 269 ALA ALA A . n 
A 1 273 LYS 273 270 270 LYS LYS A . n 
A 1 274 SER 274 271 271 SER SER A . n 
A 1 275 TYR 275 272 272 TYR TYR A . n 
A 1 276 ASN 276 273 273 ASN ASN A . n 
A 1 277 GLU 277 274 274 GLU GLU A . n 
A 1 278 GLN 278 275 275 GLN GLN A . n 
A 1 279 ARG 279 276 276 ARG ARG A . n 
A 1 280 ILE 280 277 277 ILE ILE A . n 
A 1 281 ARG 281 278 278 ARG ARG A . n 
A 1 282 GLN 282 279 279 GLN GLN A . n 
A 1 283 ASN 283 280 280 ASN ASN A . n 
A 1 284 VAL 284 281 281 VAL VAL A . n 
A 1 285 GLN 285 282 282 GLN GLN A . n 
A 1 286 VAL 286 283 283 VAL VAL A . n 
A 1 287 PHE 287 284 284 PHE PHE A . n 
A 1 288 GLU 288 285 285 GLU GLU A . n 
A 1 289 PHE 289 286 286 PHE PHE A . n 
A 1 290 GLN 290 287 287 GLN GLN A . n 
A 1 291 LEU 291 288 288 LEU LEU A . n 
A 1 292 THR 292 289 289 THR THR A . n 
A 1 293 ALA 293 290 290 ALA ALA A . n 
A 1 294 GLU 294 291 291 GLU GLU A . n 
A 1 295 ASP 295 292 292 ASP ASP A . n 
A 1 296 MET 296 293 293 MET MET A . n 
A 1 297 LYS 297 294 294 LYS LYS A . n 
A 1 298 ALA 298 295 295 ALA ALA A . n 
A 1 299 ILE 299 296 296 ILE ILE A . n 
A 1 300 ASP 300 297 297 ASP ASP A . n 
A 1 301 GLY 301 298 298 GLY GLY A . n 
A 1 302 LEU 302 299 299 LEU LEU A . n 
A 1 303 ASP 303 300 300 ASP ASP A . n 
A 1 304 ARG 304 301 301 ARG ARG A . n 
A 1 305 ASN 305 302 302 ASN ASN A . n 
A 1 306 LEU 306 303 303 LEU LEU A . n 
A 1 307 HIS 307 304 304 HIS HIS A . n 
A 1 308 TYR 308 305 305 TYR TYR A . n 
A 1 309 PHE 309 306 306 PHE PHE A . n 
A 1 310 ASN 310 307 307 ASN ASN A . n 
A 1 311 SER 311 308 308 SER SER A . n 
A 1 312 ASP 312 309 309 ASP ASP A . n 
A 1 313 SER 313 310 310 SER SER A . n 
A 1 314 PHE 314 311 311 PHE PHE A . n 
A 1 315 ALA 315 312 312 ALA ALA A . n 
A 1 316 SER 316 313 313 SER SER A . n 
A 1 317 HIS 317 314 314 HIS HIS A . n 
A 1 318 PRO 318 315 315 PRO PRO A . n 
A 1 319 ASN 319 316 316 ASN ASN A . n 
A 1 320 TYR 320 317 317 TYR TYR A . n 
A 1 321 PRO 321 318 318 PRO PRO A . n 
A 1 322 TYR 322 319 319 TYR TYR A . n 
A 1 323 SER 323 320 320 SER SER A . n 
A 1 324 ASP 324 321 321 ASP ASP A . n 
A 1 325 GLU 325 322 322 GLU GLU A . n 
A 1 326 TYR 326 323 323 TYR TYR A . n 
B 1 1   GLY 1   -2  ?   ?   ?   B . n 
B 1 2   SER 2   -1  ?   ?   ?   B . n 
B 1 3   HIS 3   0   ?   ?   ?   B . n 
B 1 4   MET 4   1   ?   ?   ?   B . n 
B 1 5   ASP 5   2   ?   ?   ?   B . n 
B 1 6   SER 6   3   ?   ?   ?   B . n 
B 1 7   LYS 7   4   ?   ?   ?   B . n 
B 1 8   HIS 8   5   ?   ?   ?   B . n 
B 1 9   GLN 9   6   6   GLN GLN B . n 
B 1 10  CYS 10  7   7   CYS CYS B . n 
B 1 11  VAL 11  8   8   VAL VAL B . n 
B 1 12  LYS 12  9   9   LYS LYS B . n 
B 1 13  LEU 13  10  10  LEU LEU B . n 
B 1 14  ASN 14  11  11  ASN ASN B . n 
B 1 15  ASP 15  12  12  ASP ASP B . n 
B 1 16  GLY 16  13  13  GLY GLY B . n 
B 1 17  HIS 17  14  14  HIS HIS B . n 
B 1 18  PHE 18  15  15  PHE PHE B . n 
B 1 19  MET 19  16  16  MET MET B . n 
B 1 20  PRO 20  17  17  PRO PRO B . n 
B 1 21  VAL 21  18  18  VAL VAL B . n 
B 1 22  LEU 22  19  19  LEU LEU B . n 
B 1 23  GLY 23  20  20  GLY GLY B . n 
B 1 24  PHE 24  21  21  PHE PHE B . n 
B 1 25  GLY 25  22  22  GLY GLY B . n 
B 1 26  THR 26  23  23  THR THR B . n 
B 1 27  TYR 27  24  24  TYR TYR B . n 
B 1 28  ALA 28  25  25  ALA ALA B . n 
B 1 29  PRO 29  26  26  PRO PRO B . n 
B 1 30  PRO 30  27  27  PRO PRO B . n 
B 1 31  GLU 31  28  28  GLU GLU B . n 
B 1 32  VAL 32  29  29  VAL VAL B . n 
B 1 33  PRO 33  30  30  PRO PRO B . n 
B 1 34  ARG 34  31  31  ARG ARG B . n 
B 1 35  SER 35  32  32  SER SER B . n 
B 1 36  LYS 36  33  33  LYS LYS B . n 
B 1 37  ALA 37  34  34  ALA ALA B . n 
B 1 38  LEU 38  35  35  LEU LEU B . n 
B 1 39  GLU 39  36  36  GLU GLU B . n 
B 1 40  VAL 40  37  37  VAL VAL B . n 
B 1 41  THR 41  38  38  THR THR B . n 
B 1 42  LYS 42  39  39  LYS LYS B . n 
B 1 43  LEU 43  40  40  LEU LEU B . n 
B 1 44  ALA 44  41  41  ALA ALA B . n 
B 1 45  ILE 45  42  42  ILE ILE B . n 
B 1 46  GLU 46  43  43  GLU GLU B . n 
B 1 47  ALA 47  44  44  ALA ALA B . n 
B 1 48  GLY 48  45  45  GLY GLY B . n 
B 1 49  PHE 49  46  46  PHE PHE B . n 
B 1 50  ARG 50  47  47  ARG ARG B . n 
B 1 51  HIS 51  48  48  HIS HIS B . n 
B 1 52  ILE 52  49  49  ILE ILE B . n 
B 1 53  ASP 53  50  50  ASP ASP B . n 
B 1 54  SER 54  51  51  SER SER B . n 
B 1 55  ALA 55  52  52  ALA ALA B . n 
B 1 56  HIS 56  53  53  HIS HIS B . n 
B 1 57  LEU 57  54  54  LEU LEU B . n 
B 1 58  TYR 58  55  55  TYR TYR B . n 
B 1 59  ASN 59  56  56  ASN ASN B . n 
B 1 60  ASN 60  57  57  ASN ASN B . n 
B 1 61  GLU 61  58  58  GLU GLU B . n 
B 1 62  GLU 62  59  59  GLU GLU B . n 
B 1 63  GLN 63  60  60  GLN GLN B . n 
B 1 64  VAL 64  61  61  VAL VAL B . n 
B 1 65  GLY 65  62  62  GLY GLY B . n 
B 1 66  LEU 66  63  63  LEU LEU B . n 
B 1 67  ALA 67  64  64  ALA ALA B . n 
B 1 68  ILE 68  65  65  ILE ILE B . n 
B 1 69  ARG 69  66  66  ARG ARG B . n 
B 1 70  SER 70  67  67  SER SER B . n 
B 1 71  LYS 71  68  68  LYS LYS B . n 
B 1 72  ILE 72  69  69  ILE ILE B . n 
B 1 73  ALA 73  70  70  ALA ALA B . n 
B 1 74  ASP 74  71  71  ASP ASP B . n 
B 1 75  GLY 75  72  72  GLY GLY B . n 
B 1 76  SER 76  73  73  SER SER B . n 
B 1 77  VAL 77  74  74  VAL VAL B . n 
B 1 78  LYS 78  75  75  LYS LYS B . n 
B 1 79  ARG 79  76  76  ARG ARG B . n 
B 1 80  GLU 80  77  77  GLU GLU B . n 
B 1 81  ASP 81  78  78  ASP ASP B . n 
B 1 82  ILE 82  79  79  ILE ILE B . n 
B 1 83  PHE 83  80  80  PHE PHE B . n 
B 1 84  TYR 84  81  81  TYR TYR B . n 
B 1 85  THR 85  82  82  THR THR B . n 
B 1 86  SER 86  83  83  SER SER B . n 
B 1 87  LYS 87  84  84  LYS LYS B . n 
B 1 88  LEU 88  85  85  LEU LEU B . n 
B 1 89  TRP 89  86  86  TRP TRP B . n 
B 1 90  SER 90  87  87  SER SER B . n 
B 1 91  THR 91  88  88  THR THR B . n 
B 1 92  PHE 92  89  89  PHE PHE B . n 
B 1 93  HIS 93  90  90  HIS HIS B . n 
B 1 94  ARG 94  91  91  ARG ARG B . n 
B 1 95  PRO 95  92  92  PRO PRO B . n 
B 1 96  GLU 96  93  93  GLU GLU B . n 
B 1 97  LEU 97  94  94  LEU LEU B . n 
B 1 98  VAL 98  95  95  VAL VAL B . n 
B 1 99  ARG 99  96  96  ARG ARG B . n 
B 1 100 PRO 100 97  97  PRO PRO B . n 
B 1 101 ALA 101 98  98  ALA ALA B . n 
B 1 102 LEU 102 99  99  LEU LEU B . n 
B 1 103 GLU 103 100 100 GLU GLU B . n 
B 1 104 ASN 104 101 101 ASN ASN B . n 
B 1 105 SER 105 102 102 SER SER B . n 
B 1 106 LEU 106 103 103 LEU LEU B . n 
B 1 107 LYS 107 104 104 LYS LYS B . n 
B 1 108 LYS 108 105 105 LYS LYS B . n 
B 1 109 ALA 109 106 106 ALA ALA B . n 
B 1 110 GLN 110 107 107 GLN GLN B . n 
B 1 111 LEU 111 108 108 LEU LEU B . n 
B 1 112 ASP 112 109 109 ASP ASP B . n 
B 1 113 TYR 113 110 110 TYR TYR B . n 
B 1 114 VAL 114 111 111 VAL VAL B . n 
B 1 115 ASP 115 112 112 ASP ASP B . n 
B 1 116 LEU 116 113 113 LEU LEU B . n 
B 1 117 TYR 117 114 114 TYR TYR B . n 
B 1 118 LEU 118 115 115 LEU LEU B . n 
B 1 119 ILE 119 116 116 ILE ILE B . n 
B 1 120 HIS 120 117 117 HIS HIS B . n 
B 1 121 SER 121 118 118 SER SER B . n 
B 1 122 PRO 122 119 119 PRO PRO B . n 
B 1 123 MET 123 120 120 MET MET B . n 
B 1 124 SER 124 121 121 SER SER B . n 
B 1 125 LEU 125 122 122 LEU LEU B . n 
B 1 126 LYS 126 123 123 LYS LYS B . n 
B 1 127 PRO 127 124 124 PRO PRO B . n 
B 1 128 GLY 128 125 125 GLY GLY B . n 
B 1 129 GLU 129 126 126 GLU GLU B . n 
B 1 130 GLU 130 127 127 GLU GLU B . n 
B 1 131 LEU 131 128 128 LEU LEU B . n 
B 1 132 SER 132 129 129 SER SER B . n 
B 1 133 PRO 133 130 130 PRO PRO B . n 
B 1 134 THR 134 131 131 THR THR B . n 
B 1 135 ASP 135 132 132 ASP ASP B . n 
B 1 136 GLU 136 133 133 GLU GLU B . n 
B 1 137 ASN 137 134 134 ASN ASN B . n 
B 1 138 GLY 138 135 135 GLY GLY B . n 
B 1 139 LYS 139 136 136 LYS LYS B . n 
B 1 140 VAL 140 137 137 VAL VAL B . n 
B 1 141 ILE 141 138 138 ILE ILE B . n 
B 1 142 PHE 142 139 139 PHE PHE B . n 
B 1 143 ASP 143 140 140 ASP ASP B . n 
B 1 144 ILE 144 141 141 ILE ILE B . n 
B 1 145 VAL 145 142 142 VAL VAL B . n 
B 1 146 ASP 146 143 143 ASP ASP B . n 
B 1 147 LEU 147 144 144 LEU LEU B . n 
B 1 148 CYS 148 145 145 CYS CYS B . n 
B 1 149 THR 149 146 146 THR THR B . n 
B 1 150 THR 150 147 147 THR THR B . n 
B 1 151 TRP 151 148 148 TRP TRP B . n 
B 1 152 GLU 152 149 149 GLU GLU B . n 
B 1 153 ALA 153 150 150 ALA ALA B . n 
B 1 154 MET 154 151 151 MET MET B . n 
B 1 155 GLU 155 152 152 GLU GLU B . n 
B 1 156 LYS 156 153 153 LYS LYS B . n 
B 1 157 CYS 157 154 154 CYS CYS B . n 
B 1 158 LYS 158 155 155 LYS LYS B . n 
B 1 159 ASP 159 156 156 ASP ASP B . n 
B 1 160 ALA 160 157 157 ALA ALA B . n 
B 1 161 GLY 161 158 158 GLY GLY B . n 
B 1 162 LEU 162 159 159 LEU LEU B . n 
B 1 163 ALA 163 160 160 ALA ALA B . n 
B 1 164 LYS 164 161 161 LYS LYS B . n 
B 1 165 SER 165 162 162 SER SER B . n 
B 1 166 ILE 166 163 163 ILE ILE B . n 
B 1 167 GLY 167 164 164 GLY GLY B . n 
B 1 168 VAL 168 165 165 VAL VAL B . n 
B 1 169 SER 169 166 166 SER SER B . n 
B 1 170 ASN 170 167 167 ASN ASN B . n 
B 1 171 PHE 171 168 168 PHE PHE B . n 
B 1 172 ASN 172 169 169 ASN ASN B . n 
B 1 173 ARG 173 170 170 ARG ARG B . n 
B 1 174 ARG 174 171 171 ARG ARG B . n 
B 1 175 GLN 175 172 172 GLN GLN B . n 
B 1 176 LEU 176 173 173 LEU LEU B . n 
B 1 177 GLU 177 174 174 GLU GLU B . n 
B 1 178 MET 178 175 175 MET MET B . n 
B 1 179 ILE 179 176 176 ILE ILE B . n 
B 1 180 LEU 180 177 177 LEU LEU B . n 
B 1 181 ASN 181 178 178 ASN ASN B . n 
B 1 182 LYS 182 179 179 LYS LYS B . n 
B 1 183 PRO 183 180 180 PRO PRO B . n 
B 1 184 GLY 184 181 181 GLY GLY B . n 
B 1 185 LEU 185 182 182 LEU LEU B . n 
B 1 186 LYS 186 183 183 LYS LYS B . n 
B 1 187 TYR 187 184 184 TYR TYR B . n 
B 1 188 LYS 188 185 185 LYS LYS B . n 
B 1 189 PRO 189 186 186 PRO PRO B . n 
B 1 190 VAL 190 187 187 VAL VAL B . n 
B 1 191 CYS 191 188 188 CYS CYS B . n 
B 1 192 ASN 192 189 189 ASN ASN B . n 
B 1 193 GLN 193 190 190 GLN GLN B . n 
B 1 194 VAL 194 191 191 VAL VAL B . n 
B 1 195 GLU 195 192 192 GLU GLU B . n 
B 1 196 CYS 196 193 193 CYS CYS B . n 
B 1 197 HIS 197 194 194 HIS HIS B . n 
B 1 198 PRO 198 195 195 PRO PRO B . n 
B 1 199 TYR 199 196 196 TYR TYR B . n 
B 1 200 PHE 200 197 197 PHE PHE B . n 
B 1 201 ASN 201 198 198 ASN ASN B . n 
B 1 202 ARG 202 199 199 ARG ARG B . n 
B 1 203 SER 203 200 200 SER SER B . n 
B 1 204 LYS 204 201 201 LYS LYS B . n 
B 1 205 LEU 205 202 202 LEU LEU B . n 
B 1 206 LEU 206 203 203 LEU LEU B . n 
B 1 207 ASP 207 204 204 ASP ASP B . n 
B 1 208 PHE 208 205 205 PHE PHE B . n 
B 1 209 CYS 209 206 206 CYS CYS B . n 
B 1 210 LYS 210 207 207 LYS LYS B . n 
B 1 211 SER 211 208 208 SER SER B . n 
B 1 212 LYS 212 209 209 LYS LYS B . n 
B 1 213 ASP 213 210 210 ASP ASP B . n 
B 1 214 ILE 214 211 211 ILE ILE B . n 
B 1 215 VAL 215 212 212 VAL VAL B . n 
B 1 216 LEU 216 213 213 LEU LEU B . n 
B 1 217 VAL 217 214 214 VAL VAL B . n 
B 1 218 ALA 218 215 215 ALA ALA B . n 
B 1 219 TYR 219 216 216 TYR TYR B . n 
B 1 220 SER 220 217 217 SER SER B . n 
B 1 221 ALA 221 218 218 ALA ALA B . n 
B 1 222 LEU 222 219 219 LEU LEU B . n 
B 1 223 GLY 223 220 220 GLY GLY B . n 
B 1 224 SER 224 221 221 SER SER B . n 
B 1 225 GLN 225 222 222 GLN GLN B . n 
B 1 226 ARG 226 223 223 ARG ARG B . n 
B 1 227 ASP 227 224 224 ASP ASP B . n 
B 1 228 LYS 228 225 225 LYS LYS B . n 
B 1 229 ARG 229 226 226 ARG ARG B . n 
B 1 230 TRP 230 227 227 TRP TRP B . n 
B 1 231 VAL 231 228 228 VAL VAL B . n 
B 1 232 ASP 232 229 229 ASP ASP B . n 
B 1 233 PRO 233 230 230 PRO PRO B . n 
B 1 234 ASN 234 231 231 ASN ASN B . n 
B 1 235 SER 235 232 232 SER SER B . n 
B 1 236 PRO 236 233 233 PRO PRO B . n 
B 1 237 VAL 237 234 234 VAL VAL B . n 
B 1 238 LEU 238 235 235 LEU LEU B . n 
B 1 239 LEU 239 236 236 LEU LEU B . n 
B 1 240 GLU 240 237 237 GLU GLU B . n 
B 1 241 ASP 241 238 238 ASP ASP B . n 
B 1 242 PRO 242 239 239 PRO PRO B . n 
B 1 243 VAL 243 240 240 VAL VAL B . n 
B 1 244 LEU 244 241 241 LEU LEU B . n 
B 1 245 CYS 245 242 242 CYS CYS B . n 
B 1 246 ALA 246 243 243 ALA ALA B . n 
B 1 247 LEU 247 244 244 LEU LEU B . n 
B 1 248 ALA 248 245 245 ALA ALA B . n 
B 1 249 LYS 249 246 246 LYS LYS B . n 
B 1 250 LYS 250 247 247 LYS LYS B . n 
B 1 251 HIS 251 248 248 HIS HIS B . n 
B 1 252 LYS 252 249 249 LYS LYS B . n 
B 1 253 ARG 253 250 250 ARG ARG B . n 
B 1 254 THR 254 251 251 THR THR B . n 
B 1 255 PRO 255 252 252 PRO PRO B . n 
B 1 256 ALA 256 253 253 ALA ALA B . n 
B 1 257 LEU 257 254 254 LEU LEU B . n 
B 1 258 ILE 258 255 255 ILE ILE B . n 
B 1 259 ALA 259 256 256 ALA ALA B . n 
B 1 260 LEU 260 257 257 LEU LEU B . n 
B 1 261 ARG 261 258 258 ARG ARG B . n 
B 1 262 TYR 262 259 259 TYR TYR B . n 
B 1 263 GLN 263 260 260 GLN GLN B . n 
B 1 264 LEU 264 261 261 LEU LEU B . n 
B 1 265 GLN 265 262 262 GLN GLN B . n 
B 1 266 ARG 266 263 263 ARG ARG B . n 
B 1 267 GLY 267 264 264 GLY GLY B . n 
B 1 268 VAL 268 265 265 VAL VAL B . n 
B 1 269 VAL 269 266 266 VAL VAL B . n 
B 1 270 VAL 270 267 267 VAL VAL B . n 
B 1 271 LEU 271 268 268 LEU LEU B . n 
B 1 272 ALA 272 269 269 ALA ALA B . n 
B 1 273 LYS 273 270 270 LYS LYS B . n 
B 1 274 SER 274 271 271 SER SER B . n 
B 1 275 TYR 275 272 272 TYR TYR B . n 
B 1 276 ASN 276 273 273 ASN ASN B . n 
B 1 277 GLU 277 274 274 GLU GLU B . n 
B 1 278 GLN 278 275 275 GLN GLN B . n 
B 1 279 ARG 279 276 276 ARG ARG B . n 
B 1 280 ILE 280 277 277 ILE ILE B . n 
B 1 281 ARG 281 278 278 ARG ARG B . n 
B 1 282 GLN 282 279 279 GLN GLN B . n 
B 1 283 ASN 283 280 280 ASN ASN B . n 
B 1 284 VAL 284 281 281 VAL VAL B . n 
B 1 285 GLN 285 282 282 GLN GLN B . n 
B 1 286 VAL 286 283 283 VAL VAL B . n 
B 1 287 PHE 287 284 284 PHE PHE B . n 
B 1 288 GLU 288 285 285 GLU GLU B . n 
B 1 289 PHE 289 286 286 PHE PHE B . n 
B 1 290 GLN 290 287 287 GLN GLN B . n 
B 1 291 LEU 291 288 288 LEU LEU B . n 
B 1 292 THR 292 289 289 THR THR B . n 
B 1 293 ALA 293 290 290 ALA ALA B . n 
B 1 294 GLU 294 291 291 GLU GLU B . n 
B 1 295 ASP 295 292 292 ASP ASP B . n 
B 1 296 MET 296 293 293 MET MET B . n 
B 1 297 LYS 297 294 294 LYS LYS B . n 
B 1 298 ALA 298 295 295 ALA ALA B . n 
B 1 299 ILE 299 296 296 ILE ILE B . n 
B 1 300 ASP 300 297 297 ASP ASP B . n 
B 1 301 GLY 301 298 298 GLY GLY B . n 
B 1 302 LEU 302 299 299 LEU LEU B . n 
B 1 303 ASP 303 300 300 ASP ASP B . n 
B 1 304 ARG 304 301 301 ARG ARG B . n 
B 1 305 ASN 305 302 302 ASN ASN B . n 
B 1 306 LEU 306 303 303 LEU LEU B . n 
B 1 307 HIS 307 304 304 HIS HIS B . n 
B 1 308 TYR 308 305 305 TYR TYR B . n 
B 1 309 PHE 309 306 306 PHE PHE B . n 
B 1 310 ASN 310 307 307 ASN ASN B . n 
B 1 311 SER 311 308 308 SER SER B . n 
B 1 312 ASP 312 309 309 ASP ASP B . n 
B 1 313 SER 313 310 310 SER SER B . n 
B 1 314 PHE 314 311 311 PHE PHE B . n 
B 1 315 ALA 315 312 312 ALA ALA B . n 
B 1 316 SER 316 313 313 SER SER B . n 
B 1 317 HIS 317 314 314 HIS HIS B . n 
B 1 318 PRO 318 315 315 PRO PRO B . n 
B 1 319 ASN 319 316 316 ASN ASN B . n 
B 1 320 TYR 320 317 317 TYR TYR B . n 
B 1 321 PRO 321 318 318 PRO PRO B . n 
B 1 322 TYR 322 319 319 TYR TYR B . n 
B 1 323 SER 323 320 320 SER SER B . n 
B 1 324 ASP 324 321 321 ASP ASP B . n 
B 1 325 GLU 325 322 322 GLU GLU B . n 
B 1 326 TYR 326 323 323 TYR TYR B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1H2U ? ? A1H2U ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAP   ? ? NAP   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 NAP   1   401 600 NAP   NAP A . 
D 3 A1H2U 1   402 1   A1H2U LIG A . 
E 4 NA    1   403 2   NA    NA  A . 
F 4 NA    1   404 4   NA    NA  A . 
G 4 NA    1   405 9   NA    NA  A . 
H 4 NA    1   406 10  NA    NA  A . 
I 4 NA    1   407 12  NA    NA  A . 
J 2 NAP   1   401 600 NAP   NAP B . 
K 3 A1H2U 1   402 2   A1H2U LIG B . 
L 4 NA    1   403 1   NA    NA  B . 
M 4 NA    1   404 3   NA    NA  B . 
N 4 NA    1   405 5   NA    NA  B . 
O 4 NA    1   406 6   NA    NA  B . 
P 4 NA    1   407 8   NA    NA  B . 
Q 4 NA    1   408 11  NA    NA  B . 
R 5 HOH   1   501 334 HOH   HOH A . 
R 5 HOH   2   502 444 HOH   HOH A . 
R 5 HOH   3   503 339 HOH   HOH A . 
R 5 HOH   4   504 512 HOH   HOH A . 
R 5 HOH   5   505 45  HOH   HOH A . 
R 5 HOH   6   506 6   HOH   HOH A . 
R 5 HOH   7   507 333 HOH   HOH A . 
R 5 HOH   8   508 256 HOH   HOH A . 
R 5 HOH   9   509 452 HOH   HOH A . 
R 5 HOH   10  510 230 HOH   HOH A . 
R 5 HOH   11  511 647 HOH   HOH A . 
R 5 HOH   12  512 584 HOH   HOH A . 
R 5 HOH   13  513 379 HOH   HOH A . 
R 5 HOH   14  514 597 HOH   HOH A . 
R 5 HOH   15  515 273 HOH   HOH A . 
R 5 HOH   16  516 665 HOH   HOH A . 
R 5 HOH   17  517 51  HOH   HOH A . 
R 5 HOH   18  518 271 HOH   HOH A . 
R 5 HOH   19  519 67  HOH   HOH A . 
R 5 HOH   20  520 585 HOH   HOH A . 
R 5 HOH   21  521 498 HOH   HOH A . 
R 5 HOH   22  522 82  HOH   HOH A . 
R 5 HOH   23  523 118 HOH   HOH A . 
R 5 HOH   24  524 356 HOH   HOH A . 
R 5 HOH   25  525 148 HOH   HOH A . 
R 5 HOH   26  526 96  HOH   HOH A . 
R 5 HOH   27  527 249 HOH   HOH A . 
R 5 HOH   28  528 10  HOH   HOH A . 
R 5 HOH   29  529 578 HOH   HOH A . 
R 5 HOH   30  530 138 HOH   HOH A . 
R 5 HOH   31  531 543 HOH   HOH A . 
R 5 HOH   32  532 18  HOH   HOH A . 
R 5 HOH   33  533 40  HOH   HOH A . 
R 5 HOH   34  534 310 HOH   HOH A . 
R 5 HOH   35  535 488 HOH   HOH A . 
R 5 HOH   36  536 398 HOH   HOH A . 
R 5 HOH   37  537 562 HOH   HOH A . 
R 5 HOH   38  538 109 HOH   HOH A . 
R 5 HOH   39  539 182 HOH   HOH A . 
R 5 HOH   40  540 228 HOH   HOH A . 
R 5 HOH   41  541 199 HOH   HOH A . 
R 5 HOH   42  542 243 HOH   HOH A . 
R 5 HOH   43  543 126 HOH   HOH A . 
R 5 HOH   44  544 515 HOH   HOH A . 
R 5 HOH   45  545 352 HOH   HOH A . 
R 5 HOH   46  546 341 HOH   HOH A . 
R 5 HOH   47  547 153 HOH   HOH A . 
R 5 HOH   48  548 26  HOH   HOH A . 
R 5 HOH   49  549 354 HOH   HOH A . 
R 5 HOH   50  550 170 HOH   HOH A . 
R 5 HOH   51  551 335 HOH   HOH A . 
R 5 HOH   52  552 257 HOH   HOH A . 
R 5 HOH   53  553 440 HOH   HOH A . 
R 5 HOH   54  554 357 HOH   HOH A . 
R 5 HOH   55  555 68  HOH   HOH A . 
R 5 HOH   56  556 418 HOH   HOH A . 
R 5 HOH   57  557 568 HOH   HOH A . 
R 5 HOH   58  558 205 HOH   HOH A . 
R 5 HOH   59  559 71  HOH   HOH A . 
R 5 HOH   60  560 300 HOH   HOH A . 
R 5 HOH   61  561 134 HOH   HOH A . 
R 5 HOH   62  562 179 HOH   HOH A . 
R 5 HOH   63  563 64  HOH   HOH A . 
R 5 HOH   64  564 212 HOH   HOH A . 
R 5 HOH   65  565 59  HOH   HOH A . 
R 5 HOH   66  566 14  HOH   HOH A . 
R 5 HOH   67  567 1   HOH   HOH A . 
R 5 HOH   68  568 103 HOH   HOH A . 
R 5 HOH   69  569 225 HOH   HOH A . 
R 5 HOH   70  570 278 HOH   HOH A . 
R 5 HOH   71  571 120 HOH   HOH A . 
R 5 HOH   72  572 61  HOH   HOH A . 
R 5 HOH   73  573 81  HOH   HOH A . 
R 5 HOH   74  574 508 HOH   HOH A . 
R 5 HOH   75  575 258 HOH   HOH A . 
R 5 HOH   76  576 100 HOH   HOH A . 
R 5 HOH   77  577 606 HOH   HOH A . 
R 5 HOH   78  578 156 HOH   HOH A . 
R 5 HOH   79  579 405 HOH   HOH A . 
R 5 HOH   80  580 181 HOH   HOH A . 
R 5 HOH   81  581 422 HOH   HOH A . 
R 5 HOH   82  582 117 HOH   HOH A . 
R 5 HOH   83  583 4   HOH   HOH A . 
R 5 HOH   84  584 525 HOH   HOH A . 
R 5 HOH   85  585 453 HOH   HOH A . 
R 5 HOH   86  586 610 HOH   HOH A . 
R 5 HOH   87  587 23  HOH   HOH A . 
R 5 HOH   88  588 268 HOH   HOH A . 
R 5 HOH   89  589 29  HOH   HOH A . 
R 5 HOH   90  590 162 HOH   HOH A . 
R 5 HOH   91  591 54  HOH   HOH A . 
R 5 HOH   92  592 505 HOH   HOH A . 
R 5 HOH   93  593 116 HOH   HOH A . 
R 5 HOH   94  594 119 HOH   HOH A . 
R 5 HOH   95  595 83  HOH   HOH A . 
R 5 HOH   96  596 19  HOH   HOH A . 
R 5 HOH   97  597 22  HOH   HOH A . 
R 5 HOH   98  598 431 HOH   HOH A . 
R 5 HOH   99  599 58  HOH   HOH A . 
R 5 HOH   100 600 344 HOH   HOH A . 
R 5 HOH   101 601 34  HOH   HOH A . 
R 5 HOH   102 602 477 HOH   HOH A . 
R 5 HOH   103 603 33  HOH   HOH A . 
R 5 HOH   104 604 644 HOH   HOH A . 
R 5 HOH   105 605 24  HOH   HOH A . 
R 5 HOH   106 606 145 HOH   HOH A . 
R 5 HOH   107 607 37  HOH   HOH A . 
R 5 HOH   108 608 570 HOH   HOH A . 
R 5 HOH   109 609 552 HOH   HOH A . 
R 5 HOH   110 610 35  HOH   HOH A . 
R 5 HOH   111 611 611 HOH   HOH A . 
R 5 HOH   112 612 556 HOH   HOH A . 
R 5 HOH   113 613 173 HOH   HOH A . 
R 5 HOH   114 614 359 HOH   HOH A . 
R 5 HOH   115 615 9   HOH   HOH A . 
R 5 HOH   116 616 30  HOH   HOH A . 
R 5 HOH   117 617 20  HOH   HOH A . 
R 5 HOH   118 618 104 HOH   HOH A . 
R 5 HOH   119 619 2   HOH   HOH A . 
R 5 HOH   120 620 17  HOH   HOH A . 
R 5 HOH   121 621 459 HOH   HOH A . 
R 5 HOH   122 622 306 HOH   HOH A . 
R 5 HOH   123 623 305 HOH   HOH A . 
R 5 HOH   124 624 38  HOH   HOH A . 
R 5 HOH   125 625 565 HOH   HOH A . 
R 5 HOH   126 626 436 HOH   HOH A . 
R 5 HOH   127 627 337 HOH   HOH A . 
R 5 HOH   128 628 426 HOH   HOH A . 
R 5 HOH   129 629 48  HOH   HOH A . 
R 5 HOH   130 630 332 HOH   HOH A . 
R 5 HOH   131 631 43  HOH   HOH A . 
R 5 HOH   132 632 149 HOH   HOH A . 
R 5 HOH   133 633 207 HOH   HOH A . 
R 5 HOH   134 634 475 HOH   HOH A . 
R 5 HOH   135 635 594 HOH   HOH A . 
R 5 HOH   136 636 131 HOH   HOH A . 
R 5 HOH   137 637 366 HOH   HOH A . 
R 5 HOH   138 638 487 HOH   HOH A . 
R 5 HOH   139 639 316 HOH   HOH A . 
R 5 HOH   140 640 91  HOH   HOH A . 
R 5 HOH   141 641 292 HOH   HOH A . 
R 5 HOH   142 642 291 HOH   HOH A . 
R 5 HOH   143 643 323 HOH   HOH A . 
R 5 HOH   144 644 313 HOH   HOH A . 
R 5 HOH   145 645 72  HOH   HOH A . 
R 5 HOH   146 646 548 HOH   HOH A . 
R 5 HOH   147 647 193 HOH   HOH A . 
R 5 HOH   148 648 483 HOH   HOH A . 
R 5 HOH   149 649 187 HOH   HOH A . 
R 5 HOH   150 650 441 HOH   HOH A . 
R 5 HOH   151 651 298 HOH   HOH A . 
R 5 HOH   152 652 412 HOH   HOH A . 
R 5 HOH   153 653 224 HOH   HOH A . 
R 5 HOH   154 654 282 HOH   HOH A . 
R 5 HOH   155 655 551 HOH   HOH A . 
R 5 HOH   156 656 129 HOH   HOH A . 
R 5 HOH   157 657 167 HOH   HOH A . 
R 5 HOH   158 658 303 HOH   HOH A . 
R 5 HOH   159 659 55  HOH   HOH A . 
R 5 HOH   160 660 338 HOH   HOH A . 
R 5 HOH   161 661 92  HOH   HOH A . 
R 5 HOH   162 662 600 HOH   HOH A . 
R 5 HOH   163 663 387 HOH   HOH A . 
R 5 HOH   164 664 439 HOH   HOH A . 
R 5 HOH   165 665 176 HOH   HOH A . 
R 5 HOH   166 666 144 HOH   HOH A . 
R 5 HOH   167 667 234 HOH   HOH A . 
R 5 HOH   168 668 95  HOH   HOH A . 
R 5 HOH   169 669 154 HOH   HOH A . 
R 5 HOH   170 670 343 HOH   HOH A . 
R 5 HOH   171 671 130 HOH   HOH A . 
R 5 HOH   172 672 372 HOH   HOH A . 
R 5 HOH   173 673 195 HOH   HOH A . 
R 5 HOH   174 674 572 HOH   HOH A . 
R 5 HOH   175 675 233 HOH   HOH A . 
R 5 HOH   176 676 11  HOH   HOH A . 
R 5 HOH   177 677 401 HOH   HOH A . 
R 5 HOH   178 678 108 HOH   HOH A . 
R 5 HOH   179 679 367 HOH   HOH A . 
R 5 HOH   180 680 192 HOH   HOH A . 
R 5 HOH   181 681 216 HOH   HOH A . 
R 5 HOH   182 682 462 HOH   HOH A . 
R 5 HOH   183 683 374 HOH   HOH A . 
R 5 HOH   184 684 538 HOH   HOH A . 
R 5 HOH   185 685 267 HOH   HOH A . 
R 5 HOH   186 686 79  HOH   HOH A . 
R 5 HOH   187 687 201 HOH   HOH A . 
R 5 HOH   188 688 489 HOH   HOH A . 
R 5 HOH   189 689 98  HOH   HOH A . 
R 5 HOH   190 690 598 HOH   HOH A . 
R 5 HOH   191 691 106 HOH   HOH A . 
R 5 HOH   192 692 423 HOH   HOH A . 
R 5 HOH   193 693 450 HOH   HOH A . 
R 5 HOH   194 694 280 HOH   HOH A . 
R 5 HOH   195 695 521 HOH   HOH A . 
R 5 HOH   196 696 348 HOH   HOH A . 
R 5 HOH   197 697 307 HOH   HOH A . 
R 5 HOH   198 698 301 HOH   HOH A . 
R 5 HOH   199 699 591 HOH   HOH A . 
R 5 HOH   200 700 105 HOH   HOH A . 
R 5 HOH   201 701 73  HOH   HOH A . 
R 5 HOH   202 702 555 HOH   HOH A . 
R 5 HOH   203 703 177 HOH   HOH A . 
R 5 HOH   204 704 194 HOH   HOH A . 
R 5 HOH   205 705 161 HOH   HOH A . 
R 5 HOH   206 706 253 HOH   HOH A . 
R 5 HOH   207 707 668 HOH   HOH A . 
R 5 HOH   208 708 541 HOH   HOH A . 
R 5 HOH   209 709 12  HOH   HOH A . 
R 5 HOH   210 710 200 HOH   HOH A . 
R 5 HOH   211 711 537 HOH   HOH A . 
R 5 HOH   212 712 180 HOH   HOH A . 
R 5 HOH   213 713 409 HOH   HOH A . 
R 5 HOH   214 714 183 HOH   HOH A . 
R 5 HOH   215 715 215 HOH   HOH A . 
R 5 HOH   216 716 373 HOH   HOH A . 
R 5 HOH   217 717 492 HOH   HOH A . 
R 5 HOH   218 718 295 HOH   HOH A . 
R 5 HOH   219 719 629 HOH   HOH A . 
R 5 HOH   220 720 391 HOH   HOH A . 
R 5 HOH   221 721 381 HOH   HOH A . 
R 5 HOH   222 722 666 HOH   HOH A . 
R 5 HOH   223 723 252 HOH   HOH A . 
R 5 HOH   224 724 284 HOH   HOH A . 
R 5 HOH   225 725 151 HOH   HOH A . 
R 5 HOH   226 726 545 HOH   HOH A . 
R 5 HOH   227 727 191 HOH   HOH A . 
R 5 HOH   228 728 474 HOH   HOH A . 
R 5 HOH   229 729 485 HOH   HOH A . 
R 5 HOH   230 730 493 HOH   HOH A . 
R 5 HOH   231 731 213 HOH   HOH A . 
R 5 HOH   232 732 632 HOH   HOH A . 
R 5 HOH   233 733 457 HOH   HOH A . 
R 5 HOH   234 734 254 HOH   HOH A . 
R 5 HOH   235 735 657 HOH   HOH A . 
R 5 HOH   236 736 378 HOH   HOH A . 
R 5 HOH   237 737 244 HOH   HOH A . 
R 5 HOH   238 738 389 HOH   HOH A . 
R 5 HOH   239 739 219 HOH   HOH A . 
R 5 HOH   240 740 530 HOH   HOH A . 
R 5 HOH   241 741 506 HOH   HOH A . 
R 5 HOH   242 742 573 HOH   HOH A . 
R 5 HOH   243 743 633 HOH   HOH A . 
R 5 HOH   244 744 358 HOH   HOH A . 
R 5 HOH   245 745 203 HOH   HOH A . 
R 5 HOH   246 746 76  HOH   HOH A . 
R 5 HOH   247 747 246 HOH   HOH A . 
R 5 HOH   248 748 580 HOH   HOH A . 
R 5 HOH   249 749 623 HOH   HOH A . 
R 5 HOH   250 750 531 HOH   HOH A . 
R 5 HOH   251 751 646 HOH   HOH A . 
R 5 HOH   252 752 360 HOH   HOH A . 
R 5 HOH   253 753 186 HOH   HOH A . 
R 5 HOH   254 754 535 HOH   HOH A . 
R 5 HOH   255 755 304 HOH   HOH A . 
R 5 HOH   256 756 517 HOH   HOH A . 
R 5 HOH   257 757 540 HOH   HOH A . 
R 5 HOH   258 758 664 HOH   HOH A . 
R 5 HOH   259 759 110 HOH   HOH A . 
R 5 HOH   260 760 189 HOH   HOH A . 
R 5 HOH   261 761 403 HOH   HOH A . 
R 5 HOH   262 762 599 HOH   HOH A . 
R 5 HOH   263 763 607 HOH   HOH A . 
R 5 HOH   264 764 204 HOH   HOH A . 
R 5 HOH   265 765 321 HOH   HOH A . 
R 5 HOH   266 766 196 HOH   HOH A . 
R 5 HOH   267 767 408 HOH   HOH A . 
R 5 HOH   268 768 470 HOH   HOH A . 
R 5 HOH   269 769 380 HOH   HOH A . 
R 5 HOH   270 770 445 HOH   HOH A . 
R 5 HOH   271 771 413 HOH   HOH A . 
R 5 HOH   272 772 425 HOH   HOH A . 
R 5 HOH   273 773 510 HOH   HOH A . 
R 5 HOH   274 774 232 HOH   HOH A . 
R 5 HOH   275 775 302 HOH   HOH A . 
R 5 HOH   276 776 346 HOH   HOH A . 
R 5 HOH   277 777 455 HOH   HOH A . 
R 5 HOH   278 778 433 HOH   HOH A . 
R 5 HOH   279 779 593 HOH   HOH A . 
R 5 HOH   280 780 396 HOH   HOH A . 
R 5 HOH   281 781 532 HOH   HOH A . 
R 5 HOH   282 782 317 HOH   HOH A . 
R 5 HOH   283 783 361 HOH   HOH A . 
R 5 HOH   284 784 369 HOH   HOH A . 
R 5 HOH   285 785 527 HOH   HOH A . 
R 5 HOH   286 786 152 HOH   HOH A . 
R 5 HOH   287 787 550 HOH   HOH A . 
R 5 HOH   288 788 206 HOH   HOH A . 
R 5 HOH   289 789 329 HOH   HOH A . 
R 5 HOH   290 790 342 HOH   HOH A . 
R 5 HOH   291 791 353 HOH   HOH A . 
R 5 HOH   292 792 618 HOH   HOH A . 
R 5 HOH   293 793 294 HOH   HOH A . 
R 5 HOH   294 794 533 HOH   HOH A . 
R 5 HOH   295 795 434 HOH   HOH A . 
R 5 HOH   296 796 526 HOH   HOH A . 
R 5 HOH   297 797 147 HOH   HOH A . 
R 5 HOH   298 798 137 HOH   HOH A . 
R 5 HOH   299 799 603 HOH   HOH A . 
R 5 HOH   300 800 417 HOH   HOH A . 
R 5 HOH   301 801 133 HOH   HOH A . 
R 5 HOH   302 802 89  HOH   HOH A . 
R 5 HOH   303 803 404 HOH   HOH A . 
R 5 HOH   304 804 476 HOH   HOH A . 
R 5 HOH   305 805 542 HOH   HOH A . 
R 5 HOH   306 806 388 HOH   HOH A . 
R 5 HOH   307 807 520 HOH   HOH A . 
R 5 HOH   308 808 272 HOH   HOH A . 
R 5 HOH   309 809 269 HOH   HOH A . 
R 5 HOH   310 810 468 HOH   HOH A . 
R 5 HOH   311 811 509 HOH   HOH A . 
R 5 HOH   312 812 478 HOH   HOH A . 
R 5 HOH   313 813 481 HOH   HOH A . 
R 5 HOH   314 814 471 HOH   HOH A . 
R 5 HOH   315 815 503 HOH   HOH A . 
R 5 HOH   316 816 330 HOH   HOH A . 
R 5 HOH   317 817 499 HOH   HOH A . 
R 5 HOH   318 818 451 HOH   HOH A . 
R 5 HOH   319 819 504 HOH   HOH A . 
R 5 HOH   320 820 325 HOH   HOH A . 
R 5 HOH   321 821 546 HOH   HOH A . 
R 5 HOH   322 822 174 HOH   HOH A . 
R 5 HOH   323 823 446 HOH   HOH A . 
R 5 HOH   324 824 559 HOH   HOH A . 
R 5 HOH   325 825 522 HOH   HOH A . 
R 5 HOH   326 826 467 HOH   HOH A . 
R 5 HOH   327 827 560 HOH   HOH A . 
R 5 HOH   328 828 595 HOH   HOH A . 
S 5 HOH   1   501 589 HOH   HOH B . 
S 5 HOH   2   502 32  HOH   HOH B . 
S 5 HOH   3   503 406 HOH   HOH B . 
S 5 HOH   4   504 226 HOH   HOH B . 
S 5 HOH   5   505 469 HOH   HOH B . 
S 5 HOH   6   506 627 HOH   HOH B . 
S 5 HOH   7   507 217 HOH   HOH B . 
S 5 HOH   8   508 283 HOH   HOH B . 
S 5 HOH   9   509 319 HOH   HOH B . 
S 5 HOH   10  510 112 HOH   HOH B . 
S 5 HOH   11  511 463 HOH   HOH B . 
S 5 HOH   12  512 208 HOH   HOH B . 
S 5 HOH   13  513 7   HOH   HOH B . 
S 5 HOH   14  514 70  HOH   HOH B . 
S 5 HOH   15  515 365 HOH   HOH B . 
S 5 HOH   16  516 155 HOH   HOH B . 
S 5 HOH   17  517 500 HOH   HOH B . 
S 5 HOH   18  518 221 HOH   HOH B . 
S 5 HOH   19  519 639 HOH   HOH B . 
S 5 HOH   20  520 86  HOH   HOH B . 
S 5 HOH   21  521 368 HOH   HOH B . 
S 5 HOH   22  522 652 HOH   HOH B . 
S 5 HOH   23  523 121 HOH   HOH B . 
S 5 HOH   24  524 375 HOH   HOH B . 
S 5 HOH   25  525 75  HOH   HOH B . 
S 5 HOH   26  526 27  HOH   HOH B . 
S 5 HOH   27  527 386 HOH   HOH B . 
S 5 HOH   28  528 157 HOH   HOH B . 
S 5 HOH   29  529 46  HOH   HOH B . 
S 5 HOH   30  530 328 HOH   HOH B . 
S 5 HOH   31  531 141 HOH   HOH B . 
S 5 HOH   32  532 150 HOH   HOH B . 
S 5 HOH   33  533 673 HOH   HOH B . 
S 5 HOH   34  534 490 HOH   HOH B . 
S 5 HOH   35  535 41  HOH   HOH B . 
S 5 HOH   36  536 430 HOH   HOH B . 
S 5 HOH   37  537 127 HOH   HOH B . 
S 5 HOH   38  538 247 HOH   HOH B . 
S 5 HOH   39  539 36  HOH   HOH B . 
S 5 HOH   40  540 184 HOH   HOH B . 
S 5 HOH   41  541 442 HOH   HOH B . 
S 5 HOH   42  542 443 HOH   HOH B . 
S 5 HOH   43  543 80  HOH   HOH B . 
S 5 HOH   44  544 124 HOH   HOH B . 
S 5 HOH   45  545 163 HOH   HOH B . 
S 5 HOH   46  546 74  HOH   HOH B . 
S 5 HOH   47  547 190 HOH   HOH B . 
S 5 HOH   48  548 5   HOH   HOH B . 
S 5 HOH   49  549 370 HOH   HOH B . 
S 5 HOH   50  550 142 HOH   HOH B . 
S 5 HOH   51  551 139 HOH   HOH B . 
S 5 HOH   52  552 473 HOH   HOH B . 
S 5 HOH   53  553 47  HOH   HOH B . 
S 5 HOH   54  554 146 HOH   HOH B . 
S 5 HOH   55  555 241 HOH   HOH B . 
S 5 HOH   56  556 248 HOH   HOH B . 
S 5 HOH   57  557 63  HOH   HOH B . 
S 5 HOH   58  558 8   HOH   HOH B . 
S 5 HOH   59  559 315 HOH   HOH B . 
S 5 HOH   60  560 223 HOH   HOH B . 
S 5 HOH   61  561 28  HOH   HOH B . 
S 5 HOH   62  562 85  HOH   HOH B . 
S 5 HOH   63  563 265 HOH   HOH B . 
S 5 HOH   64  564 288 HOH   HOH B . 
S 5 HOH   65  565 218 HOH   HOH B . 
S 5 HOH   66  566 658 HOH   HOH B . 
S 5 HOH   67  567 50  HOH   HOH B . 
S 5 HOH   68  568 101 HOH   HOH B . 
S 5 HOH   69  569 227 HOH   HOH B . 
S 5 HOH   70  570 175 HOH   HOH B . 
S 5 HOH   71  571 94  HOH   HOH B . 
S 5 HOH   72  572 52  HOH   HOH B . 
S 5 HOH   73  573 69  HOH   HOH B . 
S 5 HOH   74  574 3   HOH   HOH B . 
S 5 HOH   75  575 60  HOH   HOH B . 
S 5 HOH   76  576 245 HOH   HOH B . 
S 5 HOH   77  577 324 HOH   HOH B . 
S 5 HOH   78  578 331 HOH   HOH B . 
S 5 HOH   79  579 77  HOH   HOH B . 
S 5 HOH   80  580 458 HOH   HOH B . 
S 5 HOH   81  581 362 HOH   HOH B . 
S 5 HOH   82  582 465 HOH   HOH B . 
S 5 HOH   83  583 229 HOH   HOH B . 
S 5 HOH   84  584 411 HOH   HOH B . 
S 5 HOH   85  585 427 HOH   HOH B . 
S 5 HOH   86  586 571 HOH   HOH B . 
S 5 HOH   87  587 166 HOH   HOH B . 
S 5 HOH   88  588 242 HOH   HOH B . 
S 5 HOH   89  589 420 HOH   HOH B . 
S 5 HOH   90  590 57  HOH   HOH B . 
S 5 HOH   91  591 393 HOH   HOH B . 
S 5 HOH   92  592 159 HOH   HOH B . 
S 5 HOH   93  593 87  HOH   HOH B . 
S 5 HOH   94  594 311 HOH   HOH B . 
S 5 HOH   95  595 514 HOH   HOH B . 
S 5 HOH   96  596 544 HOH   HOH B . 
S 5 HOH   97  597 336 HOH   HOH B . 
S 5 HOH   98  598 140 HOH   HOH B . 
S 5 HOH   99  599 250 HOH   HOH B . 
S 5 HOH   100 600 624 HOH   HOH B . 
S 5 HOH   101 601 220 HOH   HOH B . 
S 5 HOH   102 602 13  HOH   HOH B . 
S 5 HOH   103 603 264 HOH   HOH B . 
S 5 HOH   104 604 363 HOH   HOH B . 
S 5 HOH   105 605 667 HOH   HOH B . 
S 5 HOH   106 606 136 HOH   HOH B . 
S 5 HOH   107 607 518 HOH   HOH B . 
S 5 HOH   108 608 178 HOH   HOH B . 
S 5 HOH   109 609 25  HOH   HOH B . 
S 5 HOH   110 610 400 HOH   HOH B . 
S 5 HOH   111 611 66  HOH   HOH B . 
S 5 HOH   112 612 438 HOH   HOH B . 
S 5 HOH   113 613 235 HOH   HOH B . 
S 5 HOH   114 614 62  HOH   HOH B . 
S 5 HOH   115 615 49  HOH   HOH B . 
S 5 HOH   116 616 309 HOH   HOH B . 
S 5 HOH   117 617 236 HOH   HOH B . 
S 5 HOH   118 618 507 HOH   HOH B . 
S 5 HOH   119 619 111 HOH   HOH B . 
S 5 HOH   120 620 399 HOH   HOH B . 
S 5 HOH   121 621 115 HOH   HOH B . 
S 5 HOH   122 622 102 HOH   HOH B . 
S 5 HOH   123 623 587 HOH   HOH B . 
S 5 HOH   124 624 238 HOH   HOH B . 
S 5 HOH   125 625 547 HOH   HOH B . 
S 5 HOH   126 626 672 HOH   HOH B . 
S 5 HOH   127 627 276 HOH   HOH B . 
S 5 HOH   128 628 482 HOH   HOH B . 
S 5 HOH   129 629 263 HOH   HOH B . 
S 5 HOH   130 630 209 HOH   HOH B . 
S 5 HOH   131 631 577 HOH   HOH B . 
S 5 HOH   132 632 31  HOH   HOH B . 
S 5 HOH   133 633 44  HOH   HOH B . 
S 5 HOH   134 634 15  HOH   HOH B . 
S 5 HOH   135 635 491 HOH   HOH B . 
S 5 HOH   136 636 351 HOH   HOH B . 
S 5 HOH   137 637 185 HOH   HOH B . 
S 5 HOH   138 638 628 HOH   HOH B . 
S 5 HOH   139 639 197 HOH   HOH B . 
S 5 HOH   140 640 39  HOH   HOH B . 
S 5 HOH   141 641 122 HOH   HOH B . 
S 5 HOH   142 642 534 HOH   HOH B . 
S 5 HOH   143 643 281 HOH   HOH B . 
S 5 HOH   144 644 88  HOH   HOH B . 
S 5 HOH   145 645 53  HOH   HOH B . 
S 5 HOH   146 646 262 HOH   HOH B . 
S 5 HOH   147 647 99  HOH   HOH B . 
S 5 HOH   148 648 428 HOH   HOH B . 
S 5 HOH   149 649 293 HOH   HOH B . 
S 5 HOH   150 650 90  HOH   HOH B . 
S 5 HOH   151 651 529 HOH   HOH B . 
S 5 HOH   152 652 466 HOH   HOH B . 
S 5 HOH   153 653 132 HOH   HOH B . 
S 5 HOH   154 654 260 HOH   HOH B . 
S 5 HOH   155 655 519 HOH   HOH B . 
S 5 HOH   156 656 308 HOH   HOH B . 
S 5 HOH   157 657 97  HOH   HOH B . 
S 5 HOH   158 658 210 HOH   HOH B . 
S 5 HOH   159 659 645 HOH   HOH B . 
S 5 HOH   160 660 576 HOH   HOH B . 
S 5 HOH   161 661 286 HOH   HOH B . 
S 5 HOH   162 662 65  HOH   HOH B . 
S 5 HOH   163 663 502 HOH   HOH B . 
S 5 HOH   164 664 123 HOH   HOH B . 
S 5 HOH   165 665 523 HOH   HOH B . 
S 5 HOH   166 666 211 HOH   HOH B . 
S 5 HOH   167 667 424 HOH   HOH B . 
S 5 HOH   168 668 582 HOH   HOH B . 
S 5 HOH   169 669 114 HOH   HOH B . 
S 5 HOH   170 670 290 HOH   HOH B . 
S 5 HOH   171 671 454 HOH   HOH B . 
S 5 HOH   172 672 464 HOH   HOH B . 
S 5 HOH   173 673 135 HOH   HOH B . 
S 5 HOH   174 674 376 HOH   HOH B . 
S 5 HOH   175 675 377 HOH   HOH B . 
S 5 HOH   176 676 239 HOH   HOH B . 
S 5 HOH   177 677 392 HOH   HOH B . 
S 5 HOH   178 678 349 HOH   HOH B . 
S 5 HOH   179 679 255 HOH   HOH B . 
S 5 HOH   180 680 340 HOH   HOH B . 
S 5 HOH   181 681 326 HOH   HOH B . 
S 5 HOH   182 682 630 HOH   HOH B . 
S 5 HOH   183 683 479 HOH   HOH B . 
S 5 HOH   184 684 516 HOH   HOH B . 
S 5 HOH   185 685 289 HOH   HOH B . 
S 5 HOH   186 686 435 HOH   HOH B . 
S 5 HOH   187 687 384 HOH   HOH B . 
S 5 HOH   188 688 279 HOH   HOH B . 
S 5 HOH   189 689 650 HOH   HOH B . 
S 5 HOH   190 690 261 HOH   HOH B . 
S 5 HOH   191 691 320 HOH   HOH B . 
S 5 HOH   192 692 421 HOH   HOH B . 
S 5 HOH   193 693 168 HOH   HOH B . 
S 5 HOH   194 694 171 HOH   HOH B . 
S 5 HOH   195 695 56  HOH   HOH B . 
S 5 HOH   196 696 642 HOH   HOH B . 
S 5 HOH   197 697 586 HOH   HOH B . 
S 5 HOH   198 698 240 HOH   HOH B . 
S 5 HOH   199 699 299 HOH   HOH B . 
S 5 HOH   200 700 347 HOH   HOH B . 
S 5 HOH   201 701 158 HOH   HOH B . 
S 5 HOH   202 702 472 HOH   HOH B . 
S 5 HOH   203 703 539 HOH   HOH B . 
S 5 HOH   204 704 549 HOH   HOH B . 
S 5 HOH   205 705 385 HOH   HOH B . 
S 5 HOH   206 706 93  HOH   HOH B . 
S 5 HOH   207 707 251 HOH   HOH B . 
S 5 HOH   208 708 567 HOH   HOH B . 
S 5 HOH   209 709 592 HOH   HOH B . 
S 5 HOH   210 710 579 HOH   HOH B . 
S 5 HOH   211 711 621 HOH   HOH B . 
S 5 HOH   212 712 536 HOH   HOH B . 
S 5 HOH   213 713 296 HOH   HOH B . 
S 5 HOH   214 714 640 HOH   HOH B . 
S 5 HOH   215 715 128 HOH   HOH B . 
S 5 HOH   216 716 143 HOH   HOH B . 
S 5 HOH   217 717 496 HOH   HOH B . 
S 5 HOH   218 718 345 HOH   HOH B . 
S 5 HOH   219 719 231 HOH   HOH B . 
S 5 HOH   220 720 596 HOH   HOH B . 
S 5 HOH   221 721 318 HOH   HOH B . 
S 5 HOH   222 722 419 HOH   HOH B . 
S 5 HOH   223 723 661 HOH   HOH B . 
S 5 HOH   224 724 581 HOH   HOH B . 
S 5 HOH   225 725 78  HOH   HOH B . 
S 5 HOH   226 726 415 HOH   HOH B . 
S 5 HOH   227 727 449 HOH   HOH B . 
S 5 HOH   228 728 480 HOH   HOH B . 
S 5 HOH   229 729 125 HOH   HOH B . 
S 5 HOH   230 730 322 HOH   HOH B . 
S 5 HOH   231 731 397 HOH   HOH B . 
S 5 HOH   232 732 169 HOH   HOH B . 
S 5 HOH   233 733 460 HOH   HOH B . 
S 5 HOH   234 734 447 HOH   HOH B . 
S 5 HOH   235 735 287 HOH   HOH B . 
S 5 HOH   236 736 364 HOH   HOH B . 
S 5 HOH   237 737 501 HOH   HOH B . 
S 5 HOH   238 738 456 HOH   HOH B . 
S 5 HOH   239 739 410 HOH   HOH B . 
S 5 HOH   240 740 172 HOH   HOH B . 
S 5 HOH   241 741 164 HOH   HOH B . 
S 5 HOH   242 742 604 HOH   HOH B . 
S 5 HOH   243 743 566 HOH   HOH B . 
S 5 HOH   244 744 327 HOH   HOH B . 
S 5 HOH   245 745 414 HOH   HOH B . 
S 5 HOH   246 746 350 HOH   HOH B . 
S 5 HOH   247 747 494 HOH   HOH B . 
S 5 HOH   248 748 402 HOH   HOH B . 
S 5 HOH   249 749 561 HOH   HOH B . 
S 5 HOH   250 750 524 HOH   HOH B . 
S 5 HOH   251 751 214 HOH   HOH B . 
S 5 HOH   252 752 583 HOH   HOH B . 
S 5 HOH   253 753 497 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction'  ? ? 'Wolfgang Kabsch'    Wolfgang.Kabsch@mpimf-heidelberg.mpg.de ?               ? ? ? ?          
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/                             ? XDS         ? ? package .        1 
? 'data scaling'    ? ? 'Wolfgang Kabsch'    ?                                       ?               ? ? ? ?          
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/html_doc/xscale_program.html ? XSCALE      ? ? package .        2 
? phasing           ? ? 'Randy J. Read'      cimr-phaser@lists.cam.ac.uk             ?               ? ? ? ?          
http://www-structmed.cimr.cam.ac.uk/phaser/                                 ? PHASER      ? ? program .        3 
? refinement        ? ? 'Garib N. Murshudov' garib@ysbl.york.ac.uk                   ?               ? ? ? Fortran_77 
http://www.ccp4.ac.uk/dist/html/refmac5.html                                ? REFMAC      ? ? program 5.8.0232 4 
? 'data extraction' ? ? PDB                  deposit@deposit.rcsb.org                'Oct. 31, 2020' ? ? ? C++        
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                   ? PDB_EXTRACT ? ? package 3.27     5 
# 
_cell.angle_alpha                  77.710 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   85.610 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  76.060 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RRJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.170 
_cell.length_a_esd                 ? 
_cell.length_b                     53.520 
_cell.length_b_esd                 ? 
_cell.length_c                     75.620 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8RRJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8RRJ 
_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             2.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.08 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    
;10% w/v PEG 20 000, 20% v/v PEG MME 550, 0.1 M MES/imidazole pH 6.5, 0.03 M of each halide (sodium fluoride, sodium bromide and sodium iodide)
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      'VariMax VHF Arc Sec confocal optical system' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 300K' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-07-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54187 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54187 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          28.445 
_reflns.entry_id                                       8RRJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.700 
_reflns.d_resolution_low                               46.490 
_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                                     55988 
_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                           83.100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.340 
_reflns.pdbx_netI_over_av_sigmaI                       8.70 
_reflns.pdbx_netI_over_sigmaI                          8.700 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.951 
_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                                0.099 
_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                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.084 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.700 1.740  ? 1.010  ? ? ? ? 4900 ? ? ? ? ? ? ? ? ? ? ? 1.858 ? ? ? 1.103 ? ? 1  1 0.475 ? ? 98.100 ? 0.832 ? ? ? ? ? ? ? ? ? 
1.740 1.790  ? 1.240  ? ? ? ? 4809 ? ? ? ? ? ? ? ? ? ? ? 2.063 ? ? ? 0.924 ? ? 2  1 0.577 ? ? 98.400 ? 0.713 ? ? ? ? ? ? ? ? ? 
1.790 1.840  ? 1.450  ? ? ? ? 4686 ? ? ? ? ? ? ? ? ? ? ? 2.397 ? ? ? 0.829 ? ? 3  1 0.661 ? ? 99.000 ? 0.659 ? ? ? ? ? ? ? ? ? 
1.840 1.900  ? 1.160  ? ? ? ? 3409 ? ? ? ? ? ? ? ? ? ? ? 2.681 ? ? ? 1.284 ? ? 4  1 0.707 ? ? 74.800 ? 1.049 ? ? ? ? ? ? ? ? ? 
1.900 1.960  ? 2.960  ? ? ? ? 847  ? ? ? ? ? ? ? ? ? ? ? 2.845 ? ? ? 0.404 ? ? 5  1 0.898 ? ? 19.000 ? 0.340 ? ? ? ? ? ? ? ? ? 
1.960 2.030  ? 4.110  ? ? ? ? 4284 ? ? ? ? ? ? ? ? ? ? ? 4.068 ? ? ? 0.372 ? ? 6  1 0.929 ? ? 99.900 ? 0.323 ? ? ? ? ? ? ? ? ? 
2.030 2.110  ? 3.130  ? ? ? ? 687  ? ? ? ? ? ? ? ? ? ? ? 2.415 ? ? ? 0.339 ? ? 7  1 0.906 ? ? 16.600 ? 0.276 ? ? ? ? ? ? ? ? ? 
2.110 2.190  ? 5.890  ? ? ? ? 3911 ? ? ? ? ? ? ? ? ? ? ? 4.006 ? ? ? 0.262 ? ? 8  1 0.967 ? ? 97.600 ? 0.227 ? ? ? ? ? ? ? ? ? 
2.190 2.290  ? 4.350  ? ? ? ? 1231 ? ? ? ? ? ? ? ? ? ? ? 3.080 ? ? ? 0.394 ? ? 9  1 0.953 ? ? 31.900 ? 0.334 ? ? ? ? ? ? ? ? ? 
2.290 2.400  ? 8.170  ? ? ? ? 3624 ? ? ? ? ? ? ? ? ? ? ? 3.963 ? ? ? 0.169 ? ? 10 1 0.981 ? ? 99.900 ? 0.146 ? ? ? ? ? ? ? ? ? 
2.400 2.530  ? 9.580  ? ? ? ? 3491 ? ? ? ? ? ? ? ? ? ? ? 3.719 ? ? ? 0.141 ? ? 11 1 0.984 ? ? 99.900 ? 0.121 ? ? ? ? ? ? ? ? ? 
2.530 2.690  ? 10.620 ? ? ? ? 3289 ? ? ? ? ? ? ? ? ? ? ? 3.409 ? ? ? 0.114 ? ? 12 1 0.989 ? ? 99.500 ? 0.097 ? ? ? ? ? ? ? ? ? 
2.690 2.870  ? 13.000 ? ? ? ? 3058 ? ? ? ? ? ? ? ? ? ? ? 3.976 ? ? ? 0.097 ? ? 13 1 0.993 ? ? 99.800 ? 0.084 ? ? ? ? ? ? ? ? ? 
2.870 3.100  ? 16.020 ? ? ? ? 2902 ? ? ? ? ? ? ? ? ? ? ? 4.382 ? ? ? 0.078 ? ? 14 1 0.996 ? ? 100    ? 0.068 ? ? ? ? ? ? ? ? ? 
3.100 3.400  ? 18.600 ? ? ? ? 2636 ? ? ? ? ? ? ? ? ? ? ? 4.365 ? ? ? 0.064 ? ? 15 1 0.997 ? ? 99.600 ? 0.056 ? ? ? ? ? ? ? ? ? 
3.400 3.800  ? 20.630 ? ? ? ? 2262 ? ? ? ? ? ? ? ? ? ? ? 3.782 ? ? ? 0.084 ? ? 16 1 0.991 ? ? 94.500 ? 0.072 ? ? ? ? ? ? ? ? ? 
3.800 4.390  ? 22.450 ? ? ? ? 2070 ? ? ? ? ? ? ? ? ? ? ? 3.921 ? ? ? 0.056 ? ? 17 1 0.997 ? ? 98.300 ? 0.049 ? ? ? ? ? ? ? ? ? 
4.390 5.380  ? 21.250 ? ? ? ? 1789 ? ? ? ? ? ? ? ? ? ? ? 3.400 ? ? ? 0.052 ? ? 18 1 0.997 ? ? 99.700 ? 0.044 ? ? ? ? ? ? ? ? ? 
5.380 7.600  ? 21.900 ? ? ? ? 1365 ? ? ? ? ? ? ? ? ? ? ? 4.224 ? ? ? 0.060 ? ? 19 1 0.996 ? ? 99.600 ? 0.052 ? ? ? ? ? ? ? ? ? 
7.600 46.490 ? 27.760 ? ? ? ? 738  ? ? ? ? ? ? ? ? ? ? ? 4.305 ? ? ? 0.049 ? ? 20 1 0.997 ? ? 97.900 ? 0.043 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.5700 
_refine.aniso_B[1][2]                            0.3500 
_refine.aniso_B[1][3]                            -0.0300 
_refine.aniso_B[2][2]                            0.7600 
_refine.aniso_B[2][3]                            -0.2000 
_refine.aniso_B[3][3]                            -0.1800 
_refine.B_iso_max                                119.750 
_refine.B_iso_mean                               23.608 
_refine.B_iso_min                                9.300 
_refine.correlation_coeff_Fo_to_Fc               0.9580 
_refine.correlation_coeff_Fo_to_Fc_free          0.9400 
_refine.details                                  
;HYDROGENS HAVE BEEN ADDED IN THE RIDING   
POSITIONS U VALUES REFINED INDIVIDUALLY
;
_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                                 8RRJ 
_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                            1.7000 
_refine.ls_d_res_low                             46.4900 
_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                     54868 
_refine.ls_number_reflns_R_free                  1120 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    83.1500 
_refine.ls_percent_reflns_R_free                 2.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1869 
_refine.ls_R_factor_R_free                       0.2212 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1862 
_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                    MASK 
_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       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.1470 
_refine.pdbx_overall_ESU_R_Free                  0.1320 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.1473 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.7000 
_refine_hist.d_res_low                        46.4900 
_refine_hist.number_atoms_solvent             581 
_refine_hist.number_atoms_total               5854 
_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       636 
_refine_hist.pdbx_B_iso_mean_ligand           21.25 
_refine_hist.pdbx_B_iso_mean_solvent          31.47 
_refine_hist.pdbx_number_atoms_protein        5108 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         165 
_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  0.013  5455  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.034  0.017  5035  ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.733  1.692  7431  ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 2.292  1.611  11728 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 6.778  5.000  650   ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.547 22.404 287   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.728 15.000 940   ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 16.463 15.000 35    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.088  0.200  692   ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  6006  ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.020  1143  ? r_gen_planes_other     ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.7000 
_refine_ls_shell.d_res_low                        1.7440 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             98 
_refine_ls_shell.number_reflns_R_work             4798 
_refine_ls_shell.percent_reflns_obs               98.1800 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.3050 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.3130 
# 
_struct.entry_id                     8RRJ 
_struct.title                        
'The structural basis of aldo-keto reductase 1C3 inhibition by 17alpha-picolyl and 17(E)-picolinylidene androstane derivatives' 
_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        8RRJ 
_struct_keywords.text            
'aldo-keto reductase, oxidoreductase, AKR1C3, inhibitor, steroid, 3-Alpha Hydroxysteroid Dehydrogenase' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
P N N 4 ? 
Q N N 4 ? 
R N N 5 ? 
S N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    AK1C3_HUMAN 
_struct_ref.pdbx_db_accession          P42330 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDSKHQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIF
YTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLA
KSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFASHPNYPYS
DEY
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8RRJ A 4 ? 326 ? P42330 1 ? 323 ? 1 323 
2 1 8RRJ B 4 ? 326 ? P42330 1 ? 323 ? 1 323 
# 
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 8RRJ GLY A 1 ? UNP P42330 ? ? 'expression tag' -2 1 
1 8RRJ SER A 2 ? UNP P42330 ? ? 'expression tag' -1 2 
1 8RRJ HIS A 3 ? UNP P42330 ? ? 'expression tag' 0  3 
2 8RRJ GLY B 1 ? UNP P42330 ? ? 'expression tag' -2 4 
2 8RRJ SER B 2 ? UNP P42330 ? ? 'expression tag' -1 5 
2 8RRJ HIS B 3 ? UNP P42330 ? ? 'expression tag' 0  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,H,I,R   
2 1 B,J,K,L,M,N,O,P,Q,S 
# 
_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 ARG A 34  ? GLY A 48  ? ARG A 31  GLY A 45  1 ? 15 
HELX_P HELX_P2  AA2 ALA A 55  ? ASN A 59  ? ALA A 52  ASN A 56  5 ? 5  
HELX_P HELX_P3  AA3 ASN A 60  ? ASP A 74  ? ASN A 57  ASP A 71  1 ? 15 
HELX_P HELX_P4  AA4 LYS A 78  ? ILE A 82  ? LYS A 75  ILE A 79  5 ? 5  
HELX_P HELX_P5  AA5 TRP A 89  ? HIS A 93  ? TRP A 86  HIS A 90  5 ? 5  
HELX_P HELX_P6  AA6 ARG A 94  ? GLN A 110 ? ARG A 91  GLN A 107 1 ? 17 
HELX_P HELX_P7  AA7 ASP A 146 ? ALA A 160 ? ASP A 143 ALA A 157 1 ? 15 
HELX_P HELX_P8  AA8 ASN A 172 ? ASN A 181 ? ASN A 169 ASN A 178 1 ? 10 
HELX_P HELX_P9  AA9 ARG A 202 ? LYS A 212 ? ARG A 199 LYS A 209 1 ? 11 
HELX_P HELX_P10 AB1 VAL A 237 ? GLU A 240 ? VAL A 234 GLU A 237 5 ? 4  
HELX_P HELX_P11 AB2 ASP A 241 ? LYS A 252 ? ASP A 238 LYS A 249 1 ? 12 
HELX_P HELX_P12 AB3 THR A 254 ? ARG A 266 ? THR A 251 ARG A 263 1 ? 13 
HELX_P HELX_P13 AB4 ASN A 276 ? VAL A 284 ? ASN A 273 VAL A 281 1 ? 9  
HELX_P HELX_P14 AB5 GLN A 285 ? PHE A 289 ? GLN A 282 PHE A 286 5 ? 5  
HELX_P HELX_P15 AB6 THR A 292 ? GLY A 301 ? THR A 289 GLY A 298 1 ? 10 
HELX_P HELX_P16 AB7 SER A 311 ? SER A 316 ? SER A 308 SER A 313 1 ? 6  
HELX_P HELX_P17 AB8 ARG B 34  ? GLY B 48  ? ARG B 31  GLY B 45  1 ? 15 
HELX_P HELX_P18 AB9 ALA B 55  ? ASN B 59  ? ALA B 52  ASN B 56  5 ? 5  
HELX_P HELX_P19 AC1 ASN B 60  ? ASP B 74  ? ASN B 57  ASP B 71  1 ? 15 
HELX_P HELX_P20 AC2 LYS B 78  ? ILE B 82  ? LYS B 75  ILE B 79  5 ? 5  
HELX_P HELX_P21 AC3 ARG B 94  ? GLU B 96  ? ARG B 91  GLU B 93  5 ? 3  
HELX_P HELX_P22 AC4 LEU B 97  ? GLN B 110 ? LEU B 94  GLN B 107 1 ? 14 
HELX_P HELX_P23 AC5 ASP B 146 ? ALA B 160 ? ASP B 143 ALA B 157 1 ? 15 
HELX_P HELX_P24 AC6 ASN B 172 ? ASN B 181 ? ASN B 169 ASN B 178 1 ? 10 
HELX_P HELX_P25 AC7 ARG B 202 ? LYS B 212 ? ARG B 199 LYS B 209 1 ? 11 
HELX_P HELX_P26 AC8 VAL B 237 ? GLU B 240 ? VAL B 234 GLU B 237 5 ? 4  
HELX_P HELX_P27 AC9 ASP B 241 ? LYS B 252 ? ASP B 238 LYS B 249 1 ? 12 
HELX_P HELX_P28 AD1 THR B 254 ? ARG B 266 ? THR B 251 ARG B 263 1 ? 13 
HELX_P HELX_P29 AD2 ASN B 276 ? VAL B 284 ? ASN B 273 VAL B 281 1 ? 9  
HELX_P HELX_P30 AD3 GLN B 285 ? PHE B 289 ? GLN B 282 PHE B 286 5 ? 5  
HELX_P HELX_P31 AD4 THR B 292 ? GLY B 301 ? THR B 289 GLY B 298 1 ? 10 
HELX_P HELX_P32 AD5 SER B 311 ? SER B 316 ? SER B 308 SER B 313 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A TYR 58  OH  ? ? ? 1_555 E NA  . NA ? ? A TYR 55  A NA  403 1_555 ? ? ? ? ? ? ? 2.236 ? ? 
metalc2  metalc ? ? A GLU 177 OE1 ? ? ? 1_555 F NA  . NA ? ? A GLU 174 A NA  404 1_555 ? ? ? ? ? ? ? 2.511 ? ? 
metalc3  metalc ? ? A TYR 308 O   ? ? ? 1_555 G NA  . NA ? ? A TYR 305 A NA  405 1_555 ? ? ? ? ? ? ? 2.599 ? ? 
metalc4  metalc ? ? A GLU 325 OE1 ? ? ? 1_555 I NA  . NA ? ? A GLU 322 A NA  407 1_555 ? ? ? ? ? ? ? 2.427 ? ? 
metalc5  metalc ? ? A TYR 326 O   ? ? ? 1_555 H NA  . NA ? ? A TYR 323 A NA  406 1_555 ? ? ? ? ? ? ? 2.228 ? ? 
metalc6  metalc ? ? F NA  .   NA  ? ? ? 1_555 R HOH . O  ? ? A NA  404 A HOH 539 1_555 ? ? ? ? ? ? ? 2.973 ? ? 
metalc7  metalc ? ? R HOH .   O   ? ? ? 1_554 P NA  . NA ? ? A HOH 725 B NA  407 1_555 ? ? ? ? ? ? ? 2.905 ? ? 
metalc8  metalc ? ? B TYR 58  OH  ? ? ? 1_555 L NA  . NA ? ? B TYR 55  B NA  403 1_555 ? ? ? ? ? ? ? 2.093 ? ? 
metalc9  metalc ? ? B ASP 81  OD2 ? ? ? 1_555 Q NA  . NA ? ? B ASP 78  B NA  408 1_555 ? ? ? ? ? ? ? 2.564 ? ? 
metalc10 metalc ? ? B THR 91  OG1 ? ? ? 1_555 N NA  . NA ? ? B THR 88  B NA  405 1_555 ? ? ? ? ? ? ? 3.053 ? ? 
metalc11 metalc ? ? B GLU 103 OE2 ? ? ? 1_555 P NA  . NA ? ? B GLU 100 B NA  407 1_555 ? ? ? ? ? ? ? 2.465 ? ? 
metalc12 metalc ? ? B GLY 128 O   ? ? ? 1_555 N NA  . NA ? ? B GLY 125 B NA  405 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc13 metalc ? ? B GLU 240 O   ? ? ? 1_555 O NA  . NA ? ? B GLU 237 B NA  406 1_555 ? ? ? ? ? ? ? 2.384 ? ? 
metalc14 metalc ? ? B HIS 251 O   ? ? ? 1_555 M NA  . NA ? ? B HIS 248 B NA  404 1_555 ? ? ? ? ? ? ? 2.370 ? ? 
metalc15 metalc ? ? M NA  .   NA  ? ? ? 1_555 S HOH . O  ? ? B NA  404 B HOH 503 1_555 ? ? ? ? ? ? ? 2.412 ? ? 
metalc16 metalc ? ? N NA  .   NA  ? ? ? 1_555 S HOH . O  ? ? B NA  405 B HOH 509 1_555 ? ? ? ? ? ? ? 2.746 ? ? 
metalc17 metalc ? ? N NA  .   NA  ? ? ? 1_555 S HOH . O  ? ? B NA  405 B HOH 588 1_555 ? ? ? ? ? ? ? 2.714 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OE1 ? A GLU 177 ? A GLU 174 ? 1_555 NA ? F NA . ? A NA 404 ? 1_555 O   ? R HOH .   ? A HOH 539 ? 1_555 103.9 ? 
2 O   ? R HOH .   ? A HOH 725 ? 1_554 NA ? P NA . ? B NA 407 ? 1_555 OE2 ? B GLU 103 ? B GLU 100 ? 1_555 109.8 ? 
3 OG1 ? B THR 91  ? B THR 88  ? 1_555 NA ? N NA . ? B NA 405 ? 1_555 O   ? B GLY 128 ? B GLY 125 ? 1_555 142.5 ? 
4 OG1 ? B THR 91  ? B THR 88  ? 1_555 NA ? N NA . ? B NA 405 ? 1_555 O   ? S HOH .   ? B HOH 509 ? 1_555 130.2 ? 
5 O   ? B GLY 128 ? B GLY 125 ? 1_555 NA ? N NA . ? B NA 405 ? 1_555 O   ? S HOH .   ? B HOH 509 ? 1_555 86.7  ? 
6 OG1 ? B THR 91  ? B THR 88  ? 1_555 NA ? N NA . ? B NA 405 ? 1_555 O   ? S HOH .   ? B HOH 588 ? 1_555 84.3  ? 
7 O   ? B GLY 128 ? B GLY 125 ? 1_555 NA ? N NA . ? B NA 405 ? 1_555 O   ? S HOH .   ? B HOH 588 ? 1_555 75.0  ? 
8 O   ? S HOH .   ? B HOH 509 ? 1_555 NA ? N NA . ? B NA 405 ? 1_555 O   ? S HOH .   ? B HOH 588 ? 1_555 128.0 ? 
9 O   ? B HIS 251 ? B HIS 248 ? 1_555 NA ? M NA . ? B NA 404 ? 1_555 O   ? S HOH .   ? B HOH 503 ? 1_555 101.9 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 9 ? 
AA3 ? 2 ? 
AA4 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA2 8 9 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA4 6 7 ? parallel      
AA4 7 8 ? parallel      
AA4 8 9 ? 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 CYS A 10  ? LYS A 12  ? CYS A 7   LYS A 9   
AA1 2 PHE A 18  ? PRO A 20  ? PHE A 15  PRO A 17  
AA2 1 LEU A 22  ? GLY A 25  ? LEU A 19  GLY A 22  
AA2 2 HIS A 51  ? ASP A 53  ? HIS A 48  ASP A 50  
AA2 3 PHE A 83  ? LEU A 88  ? PHE A 80  LEU A 85  
AA2 4 VAL A 114 ? ILE A 119 ? VAL A 111 ILE A 116 
AA2 5 ALA A 163 ? SER A 169 ? ALA A 160 SER A 166 
AA2 6 CYS A 191 ? GLU A 195 ? CYS A 188 GLU A 192 
AA2 7 VAL A 215 ? TYR A 219 ? VAL A 212 TYR A 216 
AA2 8 VAL A 269 ? LYS A 273 ? VAL A 266 LYS A 270 
AA2 9 LEU A 22  ? GLY A 25  ? LEU A 19  GLY A 22  
AA3 1 CYS B 10  ? LYS B 12  ? CYS B 7   LYS B 9   
AA3 2 PHE B 18  ? PRO B 20  ? PHE B 15  PRO B 17  
AA4 1 LEU B 22  ? GLY B 25  ? LEU B 19  GLY B 22  
AA4 2 HIS B 51  ? ASP B 53  ? HIS B 48  ASP B 50  
AA4 3 PHE B 83  ? LEU B 88  ? PHE B 80  LEU B 85  
AA4 4 VAL B 114 ? ILE B 119 ? VAL B 111 ILE B 116 
AA4 5 ALA B 163 ? SER B 169 ? ALA B 160 SER B 166 
AA4 6 CYS B 191 ? GLU B 195 ? CYS B 188 GLU B 192 
AA4 7 VAL B 215 ? TYR B 219 ? VAL B 212 TYR B 216 
AA4 8 VAL B 269 ? LYS B 273 ? VAL B 266 LYS B 270 
AA4 9 LEU B 22  ? GLY B 25  ? LEU B 19  GLY B 22  
# 
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 VAL A 11  ? N VAL A 8   O MET A 19  ? O MET A 16  
AA2 1 2 N PHE A 24  ? N PHE A 21  O ASP A 53  ? O ASP A 50  
AA2 2 3 N ILE A 52  ? N ILE A 49  O PHE A 83  ? O PHE A 80  
AA2 3 4 N LEU A 88  ? N LEU A 85  O LEU A 118 ? O LEU A 115 
AA2 4 5 N VAL A 114 ? N VAL A 111 O LYS A 164 ? O LYS A 161 
AA2 5 6 N VAL A 168 ? N VAL A 165 O CYS A 191 ? O CYS A 188 
AA2 6 7 N VAL A 194 ? N VAL A 191 O TYR A 219 ? O TYR A 216 
AA2 7 8 N ALA A 218 ? N ALA A 215 O VAL A 269 ? O VAL A 266 
AA2 8 9 O VAL A 270 ? O VAL A 267 N GLY A 23  ? N GLY A 20  
AA3 1 2 N VAL B 11  ? N VAL B 8   O MET B 19  ? O MET B 16  
AA4 1 2 N PHE B 24  ? N PHE B 21  O ASP B 53  ? O ASP B 50  
AA4 2 3 N ILE B 52  ? N ILE B 49  O PHE B 83  ? O PHE B 80  
AA4 3 4 N LEU B 88  ? N LEU B 85  O LEU B 118 ? O LEU B 115 
AA4 4 5 N VAL B 114 ? N VAL B 111 O LYS B 164 ? O LYS B 161 
AA4 5 6 N VAL B 168 ? N VAL B 165 O CYS B 191 ? O CYS B 188 
AA4 6 7 N VAL B 194 ? N VAL B 191 O VAL B 217 ? O VAL B 214 
AA4 7 8 N ALA B 218 ? N ALA B 215 O VAL B 269 ? O VAL B 266 
AA4 8 9 O VAL B 270 ? O VAL B 267 N GLY B 23  ? N GLY B 20  
# 
_pdbx_entry_details.entry_id                   8RRJ 
_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 PHE A 197 ? ? -154.20 76.09   
2  1 SER A 221 ? ? 74.92   165.89  
3  1 ARG A 250 ? ? -120.34 -152.55 
4  1 ARG A 301 ? ? -140.51 19.12   
5  1 PHE B 197 ? ? -157.59 78.36   
6  1 SER B 221 ? ? 75.11   169.02  
7  1 ARG B 250 ? ? -122.91 -156.92 
8  1 GLN B 282 ? ? -63.87  1.00    
9  1 ARG B 301 ? ? -144.75 21.34   
10 1 SER B 308 ? ? -167.11 109.32  
11 1 SER B 310 ? ? -26.01  -54.95  
# 
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 9.4290   11.6040 31.5490  0.1327 ? -0.0297 ? -0.0349 ? 0.0295 ? 0.0215 ? 0.0221 ? 0.6919 ? 0.0060  
? 0.1058  ? 0.7378 ? 0.0620  ? 1.3268  ? -0.0067 ? -0.0572 ? -0.0656 ? 0.1007  ? -0.0188 ? -0.0684 ? 0.1249  ? 0.1081  ? 0.0256  ? 
2 'X-RAY DIFFRACTION' ? refined 23.7000  10.1140 11.3950  0.1424 ? -0.0485 ? -0.0585 ? 0.1967 ? 0.0144 ? 0.2419 ? 3.6600 ? 1.0301  
? -6.2361 ? 3.9947 ? -5.7014 ? 14.9431 ? -0.1419 ? -0.2444 ? 0.0579  ? -0.6389 ? -0.0200 ? -0.0844 ? 0.8424  ? 0.3979  ? 0.1619  ? 
3 'X-RAY DIFFRACTION' ? refined 1.2870   22.5320 22.5520  0.1133 ? -0.0411 ? -0.0250 ? 0.0287 ? 0.0136 ? 0.0091 ? 0.6550 ? -0.0746 
? 0.0608  ? 1.1027 ? 0.0407  ? 1.0844  ? -0.0019 ? 0.0700  ? 0.0478  ? -0.0180 ? -0.0190 ? 0.0105  ? -0.0599 ? -0.0532 ? 0.0209  ? 
4 'X-RAY DIFFRACTION' ? refined 7.8960   18.0510 7.5690   0.1968 ? -0.0548 ? 0.0031  ? 0.1507 ? 0.0418 ? 0.0336 ? 4.6540 ? -3.8765 
? 0.6904  ? 3.7419 ? 0.8169  ? 3.9764  ? 0.3194  ? 0.4575  ? 0.0621  ? -0.3704 ? -0.2514 ? -0.0698 ? -0.1672 ? 0.3465  ? -0.0680 ? 
5 'X-RAY DIFFRACTION' ? refined -8.8110  37.4390 -20.7400 0.1600 ? -0.0455 ? -0.0434 ? 0.0646 ? 0.0091 ? 0.0153 ? 0.9264 ? -0.4247 
? 0.4751  ? 0.8276 ? -0.1817 ? 1.5316  ? -0.0811 ? 0.0817  ? 0.0398  ? -0.1061 ? -0.0049 ? 0.0096  ? -0.0593 ? -0.0111 ? 0.0860  ? 
6 'X-RAY DIFFRACTION' ? refined -12.9610 18.9100 -14.2500 0.1846 ? -0.0492 ? -0.0415 ? 0.0452 ? 0.0137 ? 0.0449 ? 4.5030 ? 0.1085  
? -1.5367 ? 0.9833 ? -0.4792 ? 3.8093  ? -0.0383 ? -0.1217 ? -0.2455 ? -0.0076 ? 0.1179  ? 0.0493  ? 0.4025  ? -0.2074 ? -0.0796 ? 
7 'X-RAY DIFFRACTION' ? refined 0.1790   38.7620 -5.6110  0.1553 ? -0.0375 ? -0.0619 ? 0.0451 ? 0.0064 ? 0.0410 ? 1.2351 ? -0.2426 
? 0.8598  ? 0.9865 ? -0.0099 ? 1.7505  ? -0.1700 ? -0.0606 ? 0.1272  ? 0.1102  ? 0.0181  ? -0.1283 ? -0.1176 ? 0.0284  ? 0.1518  ? 
8 'X-RAY DIFFRACTION' ? refined -7.7200  23.1150 -1.1670  0.2743 ? -0.0749 ? 0.0348  ? 0.1925 ? 0.0390 ? 0.0288 ? 4.9197 ? -1.6440 
? 3.7283  ? 4.9740 ? -0.7899 ? 2.8796  ? 0.0773  ? -0.3833 ? -0.2391 ? 0.7233  ? 0.0768  ? 0.3139  ? 0.1412  ? -0.2704 ? -0.1541 ? 
# 
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 6   ? ? ? A 124 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 125 ? ? ? A 137 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? A 138 ? ? ? A 306 ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? A 307 ? ? ? A 323 ? ? ? 
5 'X-RAY DIFFRACTION' 5 ? ? B 6   ? ? ? B 124 ? ? ? 
6 'X-RAY DIFFRACTION' 6 ? ? B 125 ? ? ? B 153 ? ? ? 
7 'X-RAY DIFFRACTION' 7 ? ? B 154 ? ? ? B 305 ? ? ? 
8 'X-RAY DIFFRACTION' 8 ? ? B 306 ? ? ? B 323 ? ? ? 
# 
_phasing.method   MR 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       828 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.84 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -2 ? A GLY 1 
2  1 Y 1 A SER -1 ? A SER 2 
3  1 Y 1 A HIS 0  ? A HIS 3 
4  1 Y 1 A MET 1  ? A MET 4 
5  1 Y 1 A ASP 2  ? A ASP 5 
6  1 Y 1 A SER 3  ? A SER 6 
7  1 Y 1 A LYS 4  ? A LYS 7 
8  1 Y 1 A HIS 5  ? A HIS 8 
9  1 Y 1 B GLY -2 ? B GLY 1 
10 1 Y 1 B SER -1 ? B SER 2 
11 1 Y 1 B HIS 0  ? B HIS 3 
12 1 Y 1 B MET 1  ? B MET 4 
13 1 Y 1 B ASP 2  ? B ASP 5 
14 1 Y 1 B SER 3  ? B SER 6 
15 1 Y 1 B LYS 4  ? B LYS 7 
16 1 Y 1 B HIS 5  ? B HIS 8 
# 
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 
A1H2U N1   N  Y N 1   
A1H2U C4   C  N N 2   
A1H2U C5   C  N N 3   
A1H2U C6   C  N N 4   
A1H2U C7   C  N N 5   
A1H2U C8   C  N S 6   
A1H2U C10  C  N R 7   
A1H2U C13  C  N N 8   
A1H2U C15  C  N N 9   
A1H2U C17  C  N N 10  
A1H2U C20  C  Y N 11  
A1H2U C21  C  Y N 12  
A1H2U C22  C  Y N 13  
A1H2U C24  C  Y N 14  
A1H2U O1   O  N N 15  
A1H2U N    N  N N 16  
A1H2U C11  C  N N 17  
A1H2U C16  C  N N 18  
A1H2U C9   C  N S 19  
A1H2U C3   C  N N 20  
A1H2U C18  C  N R 21  
A1H2U C14  C  N N 22  
A1H2U C12  C  N N 23  
A1H2U C    C  N S 24  
A1H2U C1   C  N N 25  
A1H2U C2   C  N R 26  
A1H2U O    O  N N 27  
A1H2U C19  C  N N 28  
A1H2U C23  C  Y N 29  
A1H2U H1   H  N N 30  
A1H2U H2   H  N N 31  
A1H2U H3   H  N N 32  
A1H2U H4   H  N N 33  
A1H2U H5   H  N N 34  
A1H2U H6   H  N N 35  
A1H2U H7   H  N N 36  
A1H2U H8   H  N N 37  
A1H2U H9   H  N N 38  
A1H2U H10  H  N N 39  
A1H2U H11  H  N N 40  
A1H2U H12  H  N N 41  
A1H2U H13  H  N N 42  
A1H2U H14  H  N N 43  
A1H2U H15  H  N N 44  
A1H2U H16  H  N N 45  
A1H2U H17  H  N N 46  
A1H2U H18  H  N N 47  
A1H2U H19  H  N N 48  
A1H2U H20  H  N N 49  
A1H2U H21  H  N N 50  
A1H2U H22  H  N N 51  
A1H2U H23  H  N N 52  
A1H2U H24  H  N N 53  
A1H2U H25  H  N N 54  
A1H2U H26  H  N N 55  
A1H2U H27  H  N N 56  
A1H2U H28  H  N N 57  
A1H2U H29  H  N N 58  
A1H2U H30  H  N N 59  
A1H2U H31  H  N N 60  
A1H2U H32  H  N N 61  
A1H2U H33  H  N N 62  
A1H2U H34  H  N N 63  
ALA   N    N  N N 64  
ALA   CA   C  N S 65  
ALA   C    C  N N 66  
ALA   O    O  N N 67  
ALA   CB   C  N N 68  
ALA   OXT  O  N N 69  
ALA   H    H  N N 70  
ALA   H2   H  N N 71  
ALA   HA   H  N N 72  
ALA   HB1  H  N N 73  
ALA   HB2  H  N N 74  
ALA   HB3  H  N N 75  
ALA   HXT  H  N N 76  
ARG   N    N  N N 77  
ARG   CA   C  N S 78  
ARG   C    C  N N 79  
ARG   O    O  N N 80  
ARG   CB   C  N N 81  
ARG   CG   C  N N 82  
ARG   CD   C  N N 83  
ARG   NE   N  N N 84  
ARG   CZ   C  N N 85  
ARG   NH1  N  N N 86  
ARG   NH2  N  N N 87  
ARG   OXT  O  N N 88  
ARG   H    H  N N 89  
ARG   H2   H  N N 90  
ARG   HA   H  N N 91  
ARG   HB2  H  N N 92  
ARG   HB3  H  N N 93  
ARG   HG2  H  N N 94  
ARG   HG3  H  N N 95  
ARG   HD2  H  N N 96  
ARG   HD3  H  N N 97  
ARG   HE   H  N N 98  
ARG   HH11 H  N N 99  
ARG   HH12 H  N N 100 
ARG   HH21 H  N N 101 
ARG   HH22 H  N N 102 
ARG   HXT  H  N N 103 
ASN   N    N  N N 104 
ASN   CA   C  N S 105 
ASN   C    C  N N 106 
ASN   O    O  N N 107 
ASN   CB   C  N N 108 
ASN   CG   C  N N 109 
ASN   OD1  O  N N 110 
ASN   ND2  N  N N 111 
ASN   OXT  O  N N 112 
ASN   H    H  N N 113 
ASN   H2   H  N N 114 
ASN   HA   H  N N 115 
ASN   HB2  H  N N 116 
ASN   HB3  H  N N 117 
ASN   HD21 H  N N 118 
ASN   HD22 H  N N 119 
ASN   HXT  H  N N 120 
ASP   N    N  N N 121 
ASP   CA   C  N S 122 
ASP   C    C  N N 123 
ASP   O    O  N N 124 
ASP   CB   C  N N 125 
ASP   CG   C  N N 126 
ASP   OD1  O  N N 127 
ASP   OD2  O  N N 128 
ASP   OXT  O  N N 129 
ASP   H    H  N N 130 
ASP   H2   H  N N 131 
ASP   HA   H  N N 132 
ASP   HB2  H  N N 133 
ASP   HB3  H  N N 134 
ASP   HD2  H  N N 135 
ASP   HXT  H  N N 136 
CYS   N    N  N N 137 
CYS   CA   C  N R 138 
CYS   C    C  N N 139 
CYS   O    O  N N 140 
CYS   CB   C  N N 141 
CYS   SG   S  N N 142 
CYS   OXT  O  N N 143 
CYS   H    H  N N 144 
CYS   H2   H  N N 145 
CYS   HA   H  N N 146 
CYS   HB2  H  N N 147 
CYS   HB3  H  N N 148 
CYS   HG   H  N N 149 
CYS   HXT  H  N N 150 
GLN   N    N  N N 151 
GLN   CA   C  N S 152 
GLN   C    C  N N 153 
GLN   O    O  N N 154 
GLN   CB   C  N N 155 
GLN   CG   C  N N 156 
GLN   CD   C  N N 157 
GLN   OE1  O  N N 158 
GLN   NE2  N  N N 159 
GLN   OXT  O  N N 160 
GLN   H    H  N N 161 
GLN   H2   H  N N 162 
GLN   HA   H  N N 163 
GLN   HB2  H  N N 164 
GLN   HB3  H  N N 165 
GLN   HG2  H  N N 166 
GLN   HG3  H  N N 167 
GLN   HE21 H  N N 168 
GLN   HE22 H  N N 169 
GLN   HXT  H  N N 170 
GLU   N    N  N N 171 
GLU   CA   C  N S 172 
GLU   C    C  N N 173 
GLU   O    O  N N 174 
GLU   CB   C  N N 175 
GLU   CG   C  N N 176 
GLU   CD   C  N N 177 
GLU   OE1  O  N N 178 
GLU   OE2  O  N N 179 
GLU   OXT  O  N N 180 
GLU   H    H  N N 181 
GLU   H2   H  N N 182 
GLU   HA   H  N N 183 
GLU   HB2  H  N N 184 
GLU   HB3  H  N N 185 
GLU   HG2  H  N N 186 
GLU   HG3  H  N N 187 
GLU   HE2  H  N N 188 
GLU   HXT  H  N N 189 
GLY   N    N  N N 190 
GLY   CA   C  N N 191 
GLY   C    C  N N 192 
GLY   O    O  N N 193 
GLY   OXT  O  N N 194 
GLY   H    H  N N 195 
GLY   H2   H  N N 196 
GLY   HA2  H  N N 197 
GLY   HA3  H  N N 198 
GLY   HXT  H  N N 199 
HIS   N    N  N N 200 
HIS   CA   C  N S 201 
HIS   C    C  N N 202 
HIS   O    O  N N 203 
HIS   CB   C  N N 204 
HIS   CG   C  Y N 205 
HIS   ND1  N  Y N 206 
HIS   CD2  C  Y N 207 
HIS   CE1  C  Y N 208 
HIS   NE2  N  Y N 209 
HIS   OXT  O  N N 210 
HIS   H    H  N N 211 
HIS   H2   H  N N 212 
HIS   HA   H  N N 213 
HIS   HB2  H  N N 214 
HIS   HB3  H  N N 215 
HIS   HD1  H  N N 216 
HIS   HD2  H  N N 217 
HIS   HE1  H  N N 218 
HIS   HE2  H  N N 219 
HIS   HXT  H  N N 220 
HOH   O    O  N N 221 
HOH   H1   H  N N 222 
HOH   H2   H  N N 223 
ILE   N    N  N N 224 
ILE   CA   C  N S 225 
ILE   C    C  N N 226 
ILE   O    O  N N 227 
ILE   CB   C  N S 228 
ILE   CG1  C  N N 229 
ILE   CG2  C  N N 230 
ILE   CD1  C  N N 231 
ILE   OXT  O  N N 232 
ILE   H    H  N N 233 
ILE   H2   H  N N 234 
ILE   HA   H  N N 235 
ILE   HB   H  N N 236 
ILE   HG12 H  N N 237 
ILE   HG13 H  N N 238 
ILE   HG21 H  N N 239 
ILE   HG22 H  N N 240 
ILE   HG23 H  N N 241 
ILE   HD11 H  N N 242 
ILE   HD12 H  N N 243 
ILE   HD13 H  N N 244 
ILE   HXT  H  N N 245 
LEU   N    N  N N 246 
LEU   CA   C  N S 247 
LEU   C    C  N N 248 
LEU   O    O  N N 249 
LEU   CB   C  N N 250 
LEU   CG   C  N N 251 
LEU   CD1  C  N N 252 
LEU   CD2  C  N N 253 
LEU   OXT  O  N N 254 
LEU   H    H  N N 255 
LEU   H2   H  N N 256 
LEU   HA   H  N N 257 
LEU   HB2  H  N N 258 
LEU   HB3  H  N N 259 
LEU   HG   H  N N 260 
LEU   HD11 H  N N 261 
LEU   HD12 H  N N 262 
LEU   HD13 H  N N 263 
LEU   HD21 H  N N 264 
LEU   HD22 H  N N 265 
LEU   HD23 H  N N 266 
LEU   HXT  H  N N 267 
LYS   N    N  N N 268 
LYS   CA   C  N S 269 
LYS   C    C  N N 270 
LYS   O    O  N N 271 
LYS   CB   C  N N 272 
LYS   CG   C  N N 273 
LYS   CD   C  N N 274 
LYS   CE   C  N N 275 
LYS   NZ   N  N N 276 
LYS   OXT  O  N N 277 
LYS   H    H  N N 278 
LYS   H2   H  N N 279 
LYS   HA   H  N N 280 
LYS   HB2  H  N N 281 
LYS   HB3  H  N N 282 
LYS   HG2  H  N N 283 
LYS   HG3  H  N N 284 
LYS   HD2  H  N N 285 
LYS   HD3  H  N N 286 
LYS   HE2  H  N N 287 
LYS   HE3  H  N N 288 
LYS   HZ1  H  N N 289 
LYS   HZ2  H  N N 290 
LYS   HZ3  H  N N 291 
LYS   HXT  H  N N 292 
MET   N    N  N N 293 
MET   CA   C  N S 294 
MET   C    C  N N 295 
MET   O    O  N N 296 
MET   CB   C  N N 297 
MET   CG   C  N N 298 
MET   SD   S  N N 299 
MET   CE   C  N N 300 
MET   OXT  O  N N 301 
MET   H    H  N N 302 
MET   H2   H  N N 303 
MET   HA   H  N N 304 
MET   HB2  H  N N 305 
MET   HB3  H  N N 306 
MET   HG2  H  N N 307 
MET   HG3  H  N N 308 
MET   HE1  H  N N 309 
MET   HE2  H  N N 310 
MET   HE3  H  N N 311 
MET   HXT  H  N N 312 
NA    NA   NA N N 313 
NAP   PA   P  N R 314 
NAP   O1A  O  N N 315 
NAP   O2A  O  N N 316 
NAP   O5B  O  N N 317 
NAP   C5B  C  N N 318 
NAP   C4B  C  N R 319 
NAP   O4B  O  N N 320 
NAP   C3B  C  N R 321 
NAP   O3B  O  N N 322 
NAP   C2B  C  N R 323 
NAP   O2B  O  N N 324 
NAP   C1B  C  N R 325 
NAP   N9A  N  Y N 326 
NAP   C8A  C  Y N 327 
NAP   N7A  N  Y N 328 
NAP   C5A  C  Y N 329 
NAP   C6A  C  Y N 330 
NAP   N6A  N  N N 331 
NAP   N1A  N  Y N 332 
NAP   C2A  C  Y N 333 
NAP   N3A  N  Y N 334 
NAP   C4A  C  Y N 335 
NAP   O3   O  N N 336 
NAP   PN   P  N N 337 
NAP   O1N  O  N N 338 
NAP   O2N  O  N N 339 
NAP   O5D  O  N N 340 
NAP   C5D  C  N N 341 
NAP   C4D  C  N R 342 
NAP   O4D  O  N N 343 
NAP   C3D  C  N S 344 
NAP   O3D  O  N N 345 
NAP   C2D  C  N R 346 
NAP   O2D  O  N N 347 
NAP   C1D  C  N R 348 
NAP   N1N  N  Y N 349 
NAP   C2N  C  Y N 350 
NAP   C3N  C  Y N 351 
NAP   C7N  C  N N 352 
NAP   O7N  O  N N 353 
NAP   N7N  N  N N 354 
NAP   C4N  C  Y N 355 
NAP   C5N  C  Y N 356 
NAP   C6N  C  Y N 357 
NAP   P2B  P  N N 358 
NAP   O1X  O  N N 359 
NAP   O2X  O  N N 360 
NAP   O3X  O  N N 361 
NAP   HOA2 H  N N 362 
NAP   H51A H  N N 363 
NAP   H52A H  N N 364 
NAP   H4B  H  N N 365 
NAP   H3B  H  N N 366 
NAP   HO3A H  N N 367 
NAP   H2B  H  N N 368 
NAP   H1B  H  N N 369 
NAP   H8A  H  N N 370 
NAP   H61A H  N N 371 
NAP   H62A H  N N 372 
NAP   H2A  H  N N 373 
NAP   H51N H  N N 374 
NAP   H52N H  N N 375 
NAP   H4D  H  N N 376 
NAP   H3D  H  N N 377 
NAP   HO3N H  N N 378 
NAP   H2D  H  N N 379 
NAP   HO2N H  N N 380 
NAP   H1D  H  N N 381 
NAP   H2N  H  N N 382 
NAP   H71N H  N N 383 
NAP   H72N H  N N 384 
NAP   H4N  H  N N 385 
NAP   H5N  H  N N 386 
NAP   H6N  H  N N 387 
NAP   HOP2 H  N N 388 
NAP   HOP3 H  N N 389 
PHE   N    N  N N 390 
PHE   CA   C  N S 391 
PHE   C    C  N N 392 
PHE   O    O  N N 393 
PHE   CB   C  N N 394 
PHE   CG   C  Y N 395 
PHE   CD1  C  Y N 396 
PHE   CD2  C  Y N 397 
PHE   CE1  C  Y N 398 
PHE   CE2  C  Y N 399 
PHE   CZ   C  Y N 400 
PHE   OXT  O  N N 401 
PHE   H    H  N N 402 
PHE   H2   H  N N 403 
PHE   HA   H  N N 404 
PHE   HB2  H  N N 405 
PHE   HB3  H  N N 406 
PHE   HD1  H  N N 407 
PHE   HD2  H  N N 408 
PHE   HE1  H  N N 409 
PHE   HE2  H  N N 410 
PHE   HZ   H  N N 411 
PHE   HXT  H  N N 412 
PRO   N    N  N N 413 
PRO   CA   C  N S 414 
PRO   C    C  N N 415 
PRO   O    O  N N 416 
PRO   CB   C  N N 417 
PRO   CG   C  N N 418 
PRO   CD   C  N N 419 
PRO   OXT  O  N N 420 
PRO   H    H  N N 421 
PRO   HA   H  N N 422 
PRO   HB2  H  N N 423 
PRO   HB3  H  N N 424 
PRO   HG2  H  N N 425 
PRO   HG3  H  N N 426 
PRO   HD2  H  N N 427 
PRO   HD3  H  N N 428 
PRO   HXT  H  N N 429 
SER   N    N  N N 430 
SER   CA   C  N S 431 
SER   C    C  N N 432 
SER   O    O  N N 433 
SER   CB   C  N N 434 
SER   OG   O  N N 435 
SER   OXT  O  N N 436 
SER   H    H  N N 437 
SER   H2   H  N N 438 
SER   HA   H  N N 439 
SER   HB2  H  N N 440 
SER   HB3  H  N N 441 
SER   HG   H  N N 442 
SER   HXT  H  N N 443 
THR   N    N  N N 444 
THR   CA   C  N S 445 
THR   C    C  N N 446 
THR   O    O  N N 447 
THR   CB   C  N R 448 
THR   OG1  O  N N 449 
THR   CG2  C  N N 450 
THR   OXT  O  N N 451 
THR   H    H  N N 452 
THR   H2   H  N N 453 
THR   HA   H  N N 454 
THR   HB   H  N N 455 
THR   HG1  H  N N 456 
THR   HG21 H  N N 457 
THR   HG22 H  N N 458 
THR   HG23 H  N N 459 
THR   HXT  H  N N 460 
TRP   N    N  N N 461 
TRP   CA   C  N S 462 
TRP   C    C  N N 463 
TRP   O    O  N N 464 
TRP   CB   C  N N 465 
TRP   CG   C  Y N 466 
TRP   CD1  C  Y N 467 
TRP   CD2  C  Y N 468 
TRP   NE1  N  Y N 469 
TRP   CE2  C  Y N 470 
TRP   CE3  C  Y N 471 
TRP   CZ2  C  Y N 472 
TRP   CZ3  C  Y N 473 
TRP   CH2  C  Y N 474 
TRP   OXT  O  N N 475 
TRP   H    H  N N 476 
TRP   H2   H  N N 477 
TRP   HA   H  N N 478 
TRP   HB2  H  N N 479 
TRP   HB3  H  N N 480 
TRP   HD1  H  N N 481 
TRP   HE1  H  N N 482 
TRP   HE3  H  N N 483 
TRP   HZ2  H  N N 484 
TRP   HZ3  H  N N 485 
TRP   HH2  H  N N 486 
TRP   HXT  H  N N 487 
TYR   N    N  N N 488 
TYR   CA   C  N S 489 
TYR   C    C  N N 490 
TYR   O    O  N N 491 
TYR   CB   C  N N 492 
TYR   CG   C  Y N 493 
TYR   CD1  C  Y N 494 
TYR   CD2  C  Y N 495 
TYR   CE1  C  Y N 496 
TYR   CE2  C  Y N 497 
TYR   CZ   C  Y N 498 
TYR   OH   O  N N 499 
TYR   OXT  O  N N 500 
TYR   H    H  N N 501 
TYR   H2   H  N N 502 
TYR   HA   H  N N 503 
TYR   HB2  H  N N 504 
TYR   HB3  H  N N 505 
TYR   HD1  H  N N 506 
TYR   HD2  H  N N 507 
TYR   HE1  H  N N 508 
TYR   HE2  H  N N 509 
TYR   HH   H  N N 510 
TYR   HXT  H  N N 511 
VAL   N    N  N N 512 
VAL   CA   C  N S 513 
VAL   C    C  N N 514 
VAL   O    O  N N 515 
VAL   CB   C  N N 516 
VAL   CG1  C  N N 517 
VAL   CG2  C  N N 518 
VAL   OXT  O  N N 519 
VAL   H    H  N N 520 
VAL   H2   H  N N 521 
VAL   HA   H  N N 522 
VAL   HB   H  N N 523 
VAL   HG11 H  N N 524 
VAL   HG12 H  N N 525 
VAL   HG13 H  N N 526 
VAL   HG21 H  N N 527 
VAL   HG22 H  N N 528 
VAL   HG23 H  N N 529 
VAL   HXT  H  N N 530 
# 
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 
A1H2U C21 C22  doub Y N 1   
A1H2U C21 N1   sing Y N 2   
A1H2U C22 C23  sing Y N 3   
A1H2U N1  C20  doub Y N 4   
A1H2U C23 C24  doub Y N 5   
A1H2U C20 C24  sing Y N 6   
A1H2U C20 C19  sing N N 7   
A1H2U O   C2   sing N N 8   
A1H2U C19 C2   sing N N 9   
A1H2U C2  C    sing N N 10  
A1H2U C2  C3   sing N N 11  
A1H2U C1  C    sing N N 12  
A1H2U C12 C    sing N N 13  
A1H2U C12 C14  sing N N 14  
A1H2U C   C9   sing N N 15  
A1H2U C3  C7   sing N N 16  
A1H2U C14 C8   sing N N 17  
A1H2U C9  C7   sing N N 18  
A1H2U C9  C10  sing N N 19  
A1H2U C8  C10  sing N N 20  
A1H2U C8  C18  sing N N 21  
A1H2U C10 C13  sing N N 22  
A1H2U C5  C18  sing N N 23  
A1H2U C5  C16  sing N N 24  
A1H2U C4  C18  sing N N 25  
A1H2U C18 C17  sing N N 26  
A1H2U C13 C15  sing N N 27  
A1H2U C16 C11  sing N N 28  
A1H2U C17 C15  sing N N 29  
A1H2U C17 C6   doub N N 30  
A1H2U C11 C6   sing N N 31  
A1H2U C11 N    doub N Z 32  
A1H2U N   O1   sing N N 33  
A1H2U C4  H1   sing N N 34  
A1H2U C4  H2   sing N N 35  
A1H2U C4  H3   sing N N 36  
A1H2U C5  H4   sing N N 37  
A1H2U C5  H5   sing N N 38  
A1H2U C6  H6   sing N N 39  
A1H2U C7  H7   sing N N 40  
A1H2U C7  H8   sing N N 41  
A1H2U C8  H9   sing N N 42  
A1H2U C10 H10  sing N N 43  
A1H2U C13 H11  sing N N 44  
A1H2U C13 H12  sing N N 45  
A1H2U C15 H13  sing N N 46  
A1H2U C15 H14  sing N N 47  
A1H2U C21 H15  sing N N 48  
A1H2U C22 H16  sing N N 49  
A1H2U C24 H17  sing N N 50  
A1H2U O1  H18  sing N N 51  
A1H2U C16 H19  sing N N 52  
A1H2U C16 H20  sing N N 53  
A1H2U C9  H21  sing N N 54  
A1H2U C3  H22  sing N N 55  
A1H2U C3  H23  sing N N 56  
A1H2U C14 H24  sing N N 57  
A1H2U C14 H25  sing N N 58  
A1H2U C12 H26  sing N N 59  
A1H2U C12 H27  sing N N 60  
A1H2U C1  H28  sing N N 61  
A1H2U C1  H29  sing N N 62  
A1H2U C1  H30  sing N N 63  
A1H2U O   H31  sing N N 64  
A1H2U C19 H32  sing N N 65  
A1H2U C19 H33  sing N N 66  
A1H2U C23 H34  sing N N 67  
ALA   N   CA   sing N N 68  
ALA   N   H    sing N N 69  
ALA   N   H2   sing N N 70  
ALA   CA  C    sing N N 71  
ALA   CA  CB   sing N N 72  
ALA   CA  HA   sing N N 73  
ALA   C   O    doub N N 74  
ALA   C   OXT  sing N N 75  
ALA   CB  HB1  sing N N 76  
ALA   CB  HB2  sing N N 77  
ALA   CB  HB3  sing N N 78  
ALA   OXT HXT  sing N N 79  
ARG   N   CA   sing N N 80  
ARG   N   H    sing N N 81  
ARG   N   H2   sing N N 82  
ARG   CA  C    sing N N 83  
ARG   CA  CB   sing N N 84  
ARG   CA  HA   sing N N 85  
ARG   C   O    doub N N 86  
ARG   C   OXT  sing N N 87  
ARG   CB  CG   sing N N 88  
ARG   CB  HB2  sing N N 89  
ARG   CB  HB3  sing N N 90  
ARG   CG  CD   sing N N 91  
ARG   CG  HG2  sing N N 92  
ARG   CG  HG3  sing N N 93  
ARG   CD  NE   sing N N 94  
ARG   CD  HD2  sing N N 95  
ARG   CD  HD3  sing N N 96  
ARG   NE  CZ   sing N N 97  
ARG   NE  HE   sing N N 98  
ARG   CZ  NH1  sing N N 99  
ARG   CZ  NH2  doub N N 100 
ARG   NH1 HH11 sing N N 101 
ARG   NH1 HH12 sing N N 102 
ARG   NH2 HH21 sing N N 103 
ARG   NH2 HH22 sing N N 104 
ARG   OXT HXT  sing N N 105 
ASN   N   CA   sing N N 106 
ASN   N   H    sing N N 107 
ASN   N   H2   sing N N 108 
ASN   CA  C    sing N N 109 
ASN   CA  CB   sing N N 110 
ASN   CA  HA   sing N N 111 
ASN   C   O    doub N N 112 
ASN   C   OXT  sing N N 113 
ASN   CB  CG   sing N N 114 
ASN   CB  HB2  sing N N 115 
ASN   CB  HB3  sing N N 116 
ASN   CG  OD1  doub N N 117 
ASN   CG  ND2  sing N N 118 
ASN   ND2 HD21 sing N N 119 
ASN   ND2 HD22 sing N N 120 
ASN   OXT HXT  sing N N 121 
ASP   N   CA   sing N N 122 
ASP   N   H    sing N N 123 
ASP   N   H2   sing N N 124 
ASP   CA  C    sing N N 125 
ASP   CA  CB   sing N N 126 
ASP   CA  HA   sing N N 127 
ASP   C   O    doub N N 128 
ASP   C   OXT  sing N N 129 
ASP   CB  CG   sing N N 130 
ASP   CB  HB2  sing N N 131 
ASP   CB  HB3  sing N N 132 
ASP   CG  OD1  doub N N 133 
ASP   CG  OD2  sing N N 134 
ASP   OD2 HD2  sing N N 135 
ASP   OXT HXT  sing N N 136 
CYS   N   CA   sing N N 137 
CYS   N   H    sing N N 138 
CYS   N   H2   sing N N 139 
CYS   CA  C    sing N N 140 
CYS   CA  CB   sing N N 141 
CYS   CA  HA   sing N N 142 
CYS   C   O    doub N N 143 
CYS   C   OXT  sing N N 144 
CYS   CB  SG   sing N N 145 
CYS   CB  HB2  sing N N 146 
CYS   CB  HB3  sing N N 147 
CYS   SG  HG   sing N N 148 
CYS   OXT HXT  sing N N 149 
GLN   N   CA   sing N N 150 
GLN   N   H    sing N N 151 
GLN   N   H2   sing N N 152 
GLN   CA  C    sing N N 153 
GLN   CA  CB   sing N N 154 
GLN   CA  HA   sing N N 155 
GLN   C   O    doub N N 156 
GLN   C   OXT  sing N N 157 
GLN   CB  CG   sing N N 158 
GLN   CB  HB2  sing N N 159 
GLN   CB  HB3  sing N N 160 
GLN   CG  CD   sing N N 161 
GLN   CG  HG2  sing N N 162 
GLN   CG  HG3  sing N N 163 
GLN   CD  OE1  doub N N 164 
GLN   CD  NE2  sing N N 165 
GLN   NE2 HE21 sing N N 166 
GLN   NE2 HE22 sing N N 167 
GLN   OXT HXT  sing N N 168 
GLU   N   CA   sing N N 169 
GLU   N   H    sing N N 170 
GLU   N   H2   sing N N 171 
GLU   CA  C    sing N N 172 
GLU   CA  CB   sing N N 173 
GLU   CA  HA   sing N N 174 
GLU   C   O    doub N N 175 
GLU   C   OXT  sing N N 176 
GLU   CB  CG   sing N N 177 
GLU   CB  HB2  sing N N 178 
GLU   CB  HB3  sing N N 179 
GLU   CG  CD   sing N N 180 
GLU   CG  HG2  sing N N 181 
GLU   CG  HG3  sing N N 182 
GLU   CD  OE1  doub N N 183 
GLU   CD  OE2  sing N N 184 
GLU   OE2 HE2  sing N N 185 
GLU   OXT HXT  sing N N 186 
GLY   N   CA   sing N N 187 
GLY   N   H    sing N N 188 
GLY   N   H2   sing N N 189 
GLY   CA  C    sing N N 190 
GLY   CA  HA2  sing N N 191 
GLY   CA  HA3  sing N N 192 
GLY   C   O    doub N N 193 
GLY   C   OXT  sing N N 194 
GLY   OXT HXT  sing N N 195 
HIS   N   CA   sing N N 196 
HIS   N   H    sing N N 197 
HIS   N   H2   sing N N 198 
HIS   CA  C    sing N N 199 
HIS   CA  CB   sing N N 200 
HIS   CA  HA   sing N N 201 
HIS   C   O    doub N N 202 
HIS   C   OXT  sing N N 203 
HIS   CB  CG   sing N N 204 
HIS   CB  HB2  sing N N 205 
HIS   CB  HB3  sing N N 206 
HIS   CG  ND1  sing Y N 207 
HIS   CG  CD2  doub Y N 208 
HIS   ND1 CE1  doub Y N 209 
HIS   ND1 HD1  sing N N 210 
HIS   CD2 NE2  sing Y N 211 
HIS   CD2 HD2  sing N N 212 
HIS   CE1 NE2  sing Y N 213 
HIS   CE1 HE1  sing N N 214 
HIS   NE2 HE2  sing N N 215 
HIS   OXT HXT  sing N N 216 
HOH   O   H1   sing N N 217 
HOH   O   H2   sing N N 218 
ILE   N   CA   sing N N 219 
ILE   N   H    sing N N 220 
ILE   N   H2   sing N N 221 
ILE   CA  C    sing N N 222 
ILE   CA  CB   sing N N 223 
ILE   CA  HA   sing N N 224 
ILE   C   O    doub N N 225 
ILE   C   OXT  sing N N 226 
ILE   CB  CG1  sing N N 227 
ILE   CB  CG2  sing N N 228 
ILE   CB  HB   sing N N 229 
ILE   CG1 CD1  sing N N 230 
ILE   CG1 HG12 sing N N 231 
ILE   CG1 HG13 sing N N 232 
ILE   CG2 HG21 sing N N 233 
ILE   CG2 HG22 sing N N 234 
ILE   CG2 HG23 sing N N 235 
ILE   CD1 HD11 sing N N 236 
ILE   CD1 HD12 sing N N 237 
ILE   CD1 HD13 sing N N 238 
ILE   OXT HXT  sing N N 239 
LEU   N   CA   sing N N 240 
LEU   N   H    sing N N 241 
LEU   N   H2   sing N N 242 
LEU   CA  C    sing N N 243 
LEU   CA  CB   sing N N 244 
LEU   CA  HA   sing N N 245 
LEU   C   O    doub N N 246 
LEU   C   OXT  sing N N 247 
LEU   CB  CG   sing N N 248 
LEU   CB  HB2  sing N N 249 
LEU   CB  HB3  sing N N 250 
LEU   CG  CD1  sing N N 251 
LEU   CG  CD2  sing N N 252 
LEU   CG  HG   sing N N 253 
LEU   CD1 HD11 sing N N 254 
LEU   CD1 HD12 sing N N 255 
LEU   CD1 HD13 sing N N 256 
LEU   CD2 HD21 sing N N 257 
LEU   CD2 HD22 sing N N 258 
LEU   CD2 HD23 sing N N 259 
LEU   OXT HXT  sing N N 260 
LYS   N   CA   sing N N 261 
LYS   N   H    sing N N 262 
LYS   N   H2   sing N N 263 
LYS   CA  C    sing N N 264 
LYS   CA  CB   sing N N 265 
LYS   CA  HA   sing N N 266 
LYS   C   O    doub N N 267 
LYS   C   OXT  sing N N 268 
LYS   CB  CG   sing N N 269 
LYS   CB  HB2  sing N N 270 
LYS   CB  HB3  sing N N 271 
LYS   CG  CD   sing N N 272 
LYS   CG  HG2  sing N N 273 
LYS   CG  HG3  sing N N 274 
LYS   CD  CE   sing N N 275 
LYS   CD  HD2  sing N N 276 
LYS   CD  HD3  sing N N 277 
LYS   CE  NZ   sing N N 278 
LYS   CE  HE2  sing N N 279 
LYS   CE  HE3  sing N N 280 
LYS   NZ  HZ1  sing N N 281 
LYS   NZ  HZ2  sing N N 282 
LYS   NZ  HZ3  sing N N 283 
LYS   OXT HXT  sing N N 284 
MET   N   CA   sing N N 285 
MET   N   H    sing N N 286 
MET   N   H2   sing N N 287 
MET   CA  C    sing N N 288 
MET   CA  CB   sing N N 289 
MET   CA  HA   sing N N 290 
MET   C   O    doub N N 291 
MET   C   OXT  sing N N 292 
MET   CB  CG   sing N N 293 
MET   CB  HB2  sing N N 294 
MET   CB  HB3  sing N N 295 
MET   CG  SD   sing N N 296 
MET   CG  HG2  sing N N 297 
MET   CG  HG3  sing N N 298 
MET   SD  CE   sing N N 299 
MET   CE  HE1  sing N N 300 
MET   CE  HE2  sing N N 301 
MET   CE  HE3  sing N N 302 
MET   OXT HXT  sing N N 303 
NAP   PA  O1A  doub N N 304 
NAP   PA  O2A  sing N N 305 
NAP   PA  O5B  sing N N 306 
NAP   PA  O3   sing N N 307 
NAP   O2A HOA2 sing N N 308 
NAP   O5B C5B  sing N N 309 
NAP   C5B C4B  sing N N 310 
NAP   C5B H51A sing N N 311 
NAP   C5B H52A sing N N 312 
NAP   C4B O4B  sing N N 313 
NAP   C4B C3B  sing N N 314 
NAP   C4B H4B  sing N N 315 
NAP   O4B C1B  sing N N 316 
NAP   C3B O3B  sing N N 317 
NAP   C3B C2B  sing N N 318 
NAP   C3B H3B  sing N N 319 
NAP   O3B HO3A sing N N 320 
NAP   C2B O2B  sing N N 321 
NAP   C2B C1B  sing N N 322 
NAP   C2B H2B  sing N N 323 
NAP   O2B P2B  sing N N 324 
NAP   C1B N9A  sing N N 325 
NAP   C1B H1B  sing N N 326 
NAP   N9A C8A  sing Y N 327 
NAP   N9A C4A  sing Y N 328 
NAP   C8A N7A  doub Y N 329 
NAP   C8A H8A  sing N N 330 
NAP   N7A C5A  sing Y N 331 
NAP   C5A C6A  sing Y N 332 
NAP   C5A C4A  doub Y N 333 
NAP   C6A N6A  sing N N 334 
NAP   C6A N1A  doub Y N 335 
NAP   N6A H61A sing N N 336 
NAP   N6A H62A sing N N 337 
NAP   N1A C2A  sing Y N 338 
NAP   C2A N3A  doub Y N 339 
NAP   C2A H2A  sing N N 340 
NAP   N3A C4A  sing Y N 341 
NAP   O3  PN   sing N N 342 
NAP   PN  O1N  doub N N 343 
NAP   PN  O2N  sing N N 344 
NAP   PN  O5D  sing N N 345 
NAP   O5D C5D  sing N N 346 
NAP   C5D C4D  sing N N 347 
NAP   C5D H51N sing N N 348 
NAP   C5D H52N sing N N 349 
NAP   C4D O4D  sing N N 350 
NAP   C4D C3D  sing N N 351 
NAP   C4D H4D  sing N N 352 
NAP   O4D C1D  sing N N 353 
NAP   C3D O3D  sing N N 354 
NAP   C3D C2D  sing N N 355 
NAP   C3D H3D  sing N N 356 
NAP   O3D HO3N sing N N 357 
NAP   C2D O2D  sing N N 358 
NAP   C2D C1D  sing N N 359 
NAP   C2D H2D  sing N N 360 
NAP   O2D HO2N sing N N 361 
NAP   C1D N1N  sing N N 362 
NAP   C1D H1D  sing N N 363 
NAP   N1N C2N  sing Y N 364 
NAP   N1N C6N  doub Y N 365 
NAP   C2N C3N  doub Y N 366 
NAP   C2N H2N  sing N N 367 
NAP   C3N C7N  sing N N 368 
NAP   C3N C4N  sing Y N 369 
NAP   C7N O7N  doub N N 370 
NAP   C7N N7N  sing N N 371 
NAP   N7N H71N sing N N 372 
NAP   N7N H72N sing N N 373 
NAP   C4N C5N  doub Y N 374 
NAP   C4N H4N  sing N N 375 
NAP   C5N C6N  sing Y N 376 
NAP   C5N H5N  sing N N 377 
NAP   C6N H6N  sing N N 378 
NAP   P2B O1X  doub N N 379 
NAP   P2B O2X  sing N N 380 
NAP   P2B O3X  sing N N 381 
NAP   O2X HOP2 sing N N 382 
NAP   O3X HOP3 sing N N 383 
PHE   N   CA   sing N N 384 
PHE   N   H    sing N N 385 
PHE   N   H2   sing N N 386 
PHE   CA  C    sing N N 387 
PHE   CA  CB   sing N N 388 
PHE   CA  HA   sing N N 389 
PHE   C   O    doub N N 390 
PHE   C   OXT  sing N N 391 
PHE   CB  CG   sing N N 392 
PHE   CB  HB2  sing N N 393 
PHE   CB  HB3  sing N N 394 
PHE   CG  CD1  doub Y N 395 
PHE   CG  CD2  sing Y N 396 
PHE   CD1 CE1  sing Y N 397 
PHE   CD1 HD1  sing N N 398 
PHE   CD2 CE2  doub Y N 399 
PHE   CD2 HD2  sing N N 400 
PHE   CE1 CZ   doub Y N 401 
PHE   CE1 HE1  sing N N 402 
PHE   CE2 CZ   sing Y N 403 
PHE   CE2 HE2  sing N N 404 
PHE   CZ  HZ   sing N N 405 
PHE   OXT HXT  sing N N 406 
PRO   N   CA   sing N N 407 
PRO   N   CD   sing N N 408 
PRO   N   H    sing N N 409 
PRO   CA  C    sing N N 410 
PRO   CA  CB   sing N N 411 
PRO   CA  HA   sing N N 412 
PRO   C   O    doub N N 413 
PRO   C   OXT  sing N N 414 
PRO   CB  CG   sing N N 415 
PRO   CB  HB2  sing N N 416 
PRO   CB  HB3  sing N N 417 
PRO   CG  CD   sing N N 418 
PRO   CG  HG2  sing N N 419 
PRO   CG  HG3  sing N N 420 
PRO   CD  HD2  sing N N 421 
PRO   CD  HD3  sing N N 422 
PRO   OXT HXT  sing N N 423 
SER   N   CA   sing N N 424 
SER   N   H    sing N N 425 
SER   N   H2   sing N N 426 
SER   CA  C    sing N N 427 
SER   CA  CB   sing N N 428 
SER   CA  HA   sing N N 429 
SER   C   O    doub N N 430 
SER   C   OXT  sing N N 431 
SER   CB  OG   sing N N 432 
SER   CB  HB2  sing N N 433 
SER   CB  HB3  sing N N 434 
SER   OG  HG   sing N N 435 
SER   OXT HXT  sing N N 436 
THR   N   CA   sing N N 437 
THR   N   H    sing N N 438 
THR   N   H2   sing N N 439 
THR   CA  C    sing N N 440 
THR   CA  CB   sing N N 441 
THR   CA  HA   sing N N 442 
THR   C   O    doub N N 443 
THR   C   OXT  sing N N 444 
THR   CB  OG1  sing N N 445 
THR   CB  CG2  sing N N 446 
THR   CB  HB   sing N N 447 
THR   OG1 HG1  sing N N 448 
THR   CG2 HG21 sing N N 449 
THR   CG2 HG22 sing N N 450 
THR   CG2 HG23 sing N N 451 
THR   OXT HXT  sing N N 452 
TRP   N   CA   sing N N 453 
TRP   N   H    sing N N 454 
TRP   N   H2   sing N N 455 
TRP   CA  C    sing N N 456 
TRP   CA  CB   sing N N 457 
TRP   CA  HA   sing N N 458 
TRP   C   O    doub N N 459 
TRP   C   OXT  sing N N 460 
TRP   CB  CG   sing N N 461 
TRP   CB  HB2  sing N N 462 
TRP   CB  HB3  sing N N 463 
TRP   CG  CD1  doub Y N 464 
TRP   CG  CD2  sing Y N 465 
TRP   CD1 NE1  sing Y N 466 
TRP   CD1 HD1  sing N N 467 
TRP   CD2 CE2  doub Y N 468 
TRP   CD2 CE3  sing Y N 469 
TRP   NE1 CE2  sing Y N 470 
TRP   NE1 HE1  sing N N 471 
TRP   CE2 CZ2  sing Y N 472 
TRP   CE3 CZ3  doub Y N 473 
TRP   CE3 HE3  sing N N 474 
TRP   CZ2 CH2  doub Y N 475 
TRP   CZ2 HZ2  sing N N 476 
TRP   CZ3 CH2  sing Y N 477 
TRP   CZ3 HZ3  sing N N 478 
TRP   CH2 HH2  sing N N 479 
TRP   OXT HXT  sing N N 480 
TYR   N   CA   sing N N 481 
TYR   N   H    sing N N 482 
TYR   N   H2   sing N N 483 
TYR   CA  C    sing N N 484 
TYR   CA  CB   sing N N 485 
TYR   CA  HA   sing N N 486 
TYR   C   O    doub N N 487 
TYR   C   OXT  sing N N 488 
TYR   CB  CG   sing N N 489 
TYR   CB  HB2  sing N N 490 
TYR   CB  HB3  sing N N 491 
TYR   CG  CD1  doub Y N 492 
TYR   CG  CD2  sing Y N 493 
TYR   CD1 CE1  sing Y N 494 
TYR   CD1 HD1  sing N N 495 
TYR   CD2 CE2  doub Y N 496 
TYR   CD2 HD2  sing N N 497 
TYR   CE1 CZ   doub Y N 498 
TYR   CE1 HE1  sing N N 499 
TYR   CE2 CZ   sing Y N 500 
TYR   CE2 HE2  sing N N 501 
TYR   CZ  OH   sing N N 502 
TYR   OH  HH   sing N N 503 
TYR   OXT HXT  sing N N 504 
VAL   N   CA   sing N N 505 
VAL   N   H    sing N N 506 
VAL   N   H2   sing N N 507 
VAL   CA  C    sing N N 508 
VAL   CA  CB   sing N N 509 
VAL   CA  HA   sing N N 510 
VAL   C   O    doub N N 511 
VAL   C   OXT  sing N N 512 
VAL   CB  CG1  sing N N 513 
VAL   CB  CG2  sing N N 514 
VAL   CB  HB   sing N N 515 
VAL   CG1 HG11 sing N N 516 
VAL   CG1 HG12 sing N N 517 
VAL   CG1 HG13 sing N N 518 
VAL   CG2 HG21 sing N N 519 
VAL   CG2 HG22 sing N N 520 
VAL   CG2 HG23 sing N N 521 
VAL   OXT HXT  sing N N 522 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other government'    ?                451-03-47/2023-01/200125 1 
'Other government'    ?                142-451-3463/2023-01     2 
'European Union (EU)' 'European Union' LX22NPO5102              3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1ZQ5 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RRJ 
_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]   0.024290 
_atom_sites.fract_transf_matrix[1][2]   -0.006031 
_atom_sites.fract_transf_matrix[1][3]   -0.000664 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019252 
_atom_sites.fract_transf_matrix[2][3]   -0.003950 
_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]   0.013539 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLN   A 1 9   ? -6.175  20.509 38.798  1.00 36.12  ? 6   GLN   A N   1 
ATOM   2    C  CA  . GLN   A 1 9   ? -6.771  20.926 37.501  1.00 36.36  ? 6   GLN   A CA  1 
ATOM   3    C  C   . GLN   A 1 9   ? -6.228  19.959 36.439  1.00 31.99  ? 6   GLN   A C   1 
ATOM   4    O  O   . GLN   A 1 9   ? -5.072  20.051 36.061  1.00 29.33  ? 6   GLN   A O   1 
ATOM   5    C  CB  . GLN   A 1 9   ? -6.498  22.403 37.213  1.00 41.61  ? 6   GLN   A CB  1 
ATOM   6    C  CG  . GLN   A 1 9   ? -7.262  23.363 38.140  1.00 46.94  ? 6   GLN   A CG  1 
ATOM   7    C  CD  . GLN   A 1 9   ? -8.758  23.111 38.195  1.00 52.88  ? 6   GLN   A CD  1 
ATOM   8    O  OE1 . GLN   A 1 9   ? -9.461  23.197 37.183  1.00 58.54  ? 6   GLN   A OE1 1 
ATOM   9    N  NE2 . GLN   A 1 9   ? -9.272  22.815 39.385  1.00 54.22  ? 6   GLN   A NE2 1 
ATOM   10   N  N   . CYS   A 1 10  ? -7.049  18.988 36.084  1.00 31.25  ? 7   CYS   A N   1 
ATOM   11   C  CA  A CYS   A 1 10  ? -6.715  17.810 35.239  0.60 30.33  ? 7   CYS   A CA  1 
ATOM   12   C  CA  B CYS   A 1 10  ? -6.653  17.899 35.155  0.40 30.31  ? 7   CYS   A CA  1 
ATOM   13   C  C   . CYS   A 1 10  ? -7.733  17.720 34.093  1.00 30.39  ? 7   CYS   A C   1 
ATOM   14   O  O   . CYS   A 1 10  ? -8.794  18.305 34.240  1.00 31.33  ? 7   CYS   A O   1 
ATOM   15   C  CB  A CYS   A 1 10  ? -6.763  16.520 36.061  0.60 30.16  ? 7   CYS   A CB  1 
ATOM   16   C  CB  B CYS   A 1 10  ? -6.442  16.590 35.899  0.40 30.14  ? 7   CYS   A CB  1 
ATOM   17   S  SG  A CYS   A 1 10  ? -5.357  16.277 37.181  0.60 29.46  ? 7   CYS   A SG  1 
ATOM   18   S  SG  B CYS   A 1 10  ? -7.925  16.099 36.810  0.40 32.10  ? 7   CYS   A SG  1 
ATOM   19   N  N   . VAL   A 1 11  ? -7.423  16.941 33.055  1.00 28.30  ? 8   VAL   A N   1 
ATOM   20   C  CA  . VAL   A 1 11  ? -8.362  16.640 31.958  1.00 29.18  ? 8   VAL   A CA  1 
ATOM   21   C  C   . VAL   A 1 11  ? -8.455  15.124 31.940  1.00 28.33  ? 8   VAL   A C   1 
ATOM   22   O  O   . VAL   A 1 11  ? -7.465  14.456 32.293  1.00 27.15  ? 8   VAL   A O   1 
ATOM   23   C  CB  . VAL   A 1 11  ? -7.928  17.248 30.612  1.00 29.98  ? 8   VAL   A CB  1 
ATOM   24   C  CG1 . VAL   A 1 11  ? -7.888  18.756 30.724  1.00 32.54  ? 8   VAL   A CG1 1 
ATOM   25   C  CG2 . VAL   A 1 11  ? -6.584  16.744 30.142  1.00 29.28  ? 8   VAL   A CG2 1 
ATOM   26   N  N   . LYS   A 1 12  ? -9.639  14.645 31.636  1.00 28.69  ? 9   LYS   A N   1 
ATOM   27   C  CA  . LYS   A 1 12  ? -9.896  13.204 31.518  1.00 30.16  ? 9   LYS   A CA  1 
ATOM   28   C  C   . LYS   A 1 12  ? -9.456  12.781 30.126  1.00 28.01  ? 9   LYS   A C   1 
ATOM   29   O  O   . LYS   A 1 12  ? -9.964  13.351 29.131  1.00 28.85  ? 9   LYS   A O   1 
ATOM   30   C  CB  . LYS   A 1 12  ? -11.365 12.920 31.796  1.00 33.05  ? 9   LYS   A CB  1 
ATOM   31   C  CG  . LYS   A 1 12  ? -11.632 11.456 32.050  1.00 36.43  ? 9   LYS   A CG  1 
ATOM   32   C  CD  . LYS   A 1 12  ? -13.091 11.185 32.147  1.00 40.59  ? 9   LYS   A CD  1 
ATOM   33   C  CE  . LYS   A 1 12  ? -13.351 9.774  32.600  1.00 43.68  ? 9   LYS   A CE  1 
ATOM   34   N  NZ  . LYS   A 1 12  ? -14.772 9.455  32.322  1.00 47.90  ? 9   LYS   A NZ  1 
ATOM   35   N  N   . LEU   A 1 13  ? -8.520  11.837 30.064  1.00 26.13  ? 10  LEU   A N   1 
ATOM   36   C  CA  . LEU   A 1 13  ? -8.018  11.324 28.772  1.00 24.57  ? 10  LEU   A CA  1 
ATOM   37   C  C   . LEU   A 1 13  ? -9.019  10.292 28.273  1.00 25.48  ? 10  LEU   A C   1 
ATOM   38   O  O   . LEU   A 1 13  ? -9.896  9.830  29.087  1.00 26.63  ? 10  LEU   A O   1 
ATOM   39   C  CB  . LEU   A 1 13  ? -6.625  10.730 28.956  1.00 23.74  ? 10  LEU   A CB  1 
ATOM   40   C  CG  . LEU   A 1 13  ? -5.561  11.663 29.540  1.00 22.85  ? 10  LEU   A CG  1 
ATOM   41   C  CD1 . LEU   A 1 13  ? -4.275  10.921 29.755  1.00 22.52  ? 10  LEU   A CD1 1 
ATOM   42   C  CD2 . LEU   A 1 13  ? -5.275  12.866 28.655  1.00 23.11  ? 10  LEU   A CD2 1 
ATOM   43   N  N   . ASN   A 1 14  ? -8.903  9.921  27.002  1.00 24.85  ? 11  ASN   A N   1 
ATOM   44   C  CA  . ASN   A 1 14  ? -9.925  9.068  26.347  1.00 26.63  ? 11  ASN   A CA  1 
ATOM   45   C  C   . ASN   A 1 14  ? -9.767  7.604  26.816  1.00 27.62  ? 11  ASN   A C   1 
ATOM   46   O  O   . ASN   A 1 14  ? -10.608 6.827  26.410  1.00 28.16  ? 11  ASN   A O   1 
ATOM   47   C  CB  . ASN   A 1 14  ? -9.933  9.237  24.828  1.00 26.57  ? 11  ASN   A CB  1 
ATOM   48   C  CG  . ASN   A 1 14  ? -8.640  8.807  24.167  1.00 25.92  ? 11  ASN   A CG  1 
ATOM   49   O  OD1 . ASN   A 1 14  ? -8.024  7.861  24.622  1.00 27.76  ? 11  ASN   A OD1 1 
ATOM   50   N  ND2 . ASN   A 1 14  ? -8.243  9.482  23.095  1.00 24.37  ? 11  ASN   A ND2 1 
ATOM   51   N  N   . ASP   A 1 15  ? -8.760  7.256  27.641  1.00 26.71  ? 12  ASP   A N   1 
ATOM   52   C  CA  . ASP   A 1 15  ? -8.614  5.928  28.304  1.00 28.08  ? 12  ASP   A CA  1 
ATOM   53   C  C   . ASP   A 1 15  ? -9.019  5.972  29.786  1.00 29.22  ? 12  ASP   A C   1 
ATOM   54   O  O   . ASP   A 1 15  ? -8.794  4.960  30.480  1.00 29.40  ? 12  ASP   A O   1 
ATOM   55   C  CB  . ASP   A 1 15  ? -7.198  5.372  28.175  1.00 26.96  ? 12  ASP   A CB  1 
ATOM   56   C  CG  . ASP   A 1 15  ? -6.150  6.196  28.910  1.00 25.56  ? 12  ASP   A CG  1 
ATOM   57   O  OD1 . ASP   A 1 15  ? -6.521  7.251  29.498  1.00 24.19  ? 12  ASP   A OD1 1 
ATOM   58   O  OD2 . ASP   A 1 15  ? -4.963  5.789  28.887  1.00 24.88  ? 12  ASP   A OD2 1 
ATOM   59   N  N   . GLY   A 1 16  ? -9.581  7.081  30.277  1.00 30.08  ? 13  GLY   A N   1 
ATOM   60   C  CA  . GLY   A 1 16  ? -10.091 7.177  31.663  1.00 31.39  ? 13  GLY   A CA  1 
ATOM   61   C  C   . GLY   A 1 16  ? -9.040  7.635  32.667  1.00 30.60  ? 13  GLY   A C   1 
ATOM   62   O  O   . GLY   A 1 16  ? -9.419  7.919  33.826  1.00 29.98  ? 13  GLY   A O   1 
ATOM   63   N  N   . HIS   A 1 17  ? -7.764  7.730  32.288  1.00 29.70  ? 14  HIS   A N   1 
ATOM   64   C  CA  . HIS   A 1 17  ? -6.714  8.365  33.134  1.00 29.67  ? 14  HIS   A CA  1 
ATOM   65   C  C   . HIS   A 1 17  ? -6.836  9.906  33.072  1.00 29.08  ? 14  HIS   A C   1 
ATOM   66   O  O   . HIS   A 1 17  ? -7.564  10.431 32.205  1.00 28.76  ? 14  HIS   A O   1 
ATOM   67   C  CB  . HIS   A 1 17  ? -5.313  7.883  32.753  1.00 29.60  ? 14  HIS   A CB  1 
ATOM   68   C  CG  . HIS   A 1 17  ? -5.098  6.435  33.023  1.00 31.92  ? 14  HIS   A CG  1 
ATOM   69   N  ND1 . HIS   A 1 17  ? -5.208  5.906  34.296  1.00 34.47  ? 14  HIS   A ND1 1 
ATOM   70   C  CD2 . HIS   A 1 17  ? -4.784  5.408  32.203  1.00 32.64  ? 14  HIS   A CD2 1 
ATOM   71   C  CE1 . HIS   A 1 17  ? -5.006  4.600  34.240  1.00 35.40  ? 14  HIS   A CE1 1 
ATOM   72   N  NE2 . HIS   A 1 17  ? -4.731  4.274  32.967  1.00 34.86  ? 14  HIS   A NE2 1 
ATOM   73   N  N   . PHE   A 1 18  ? -6.158  10.592 34.004  1.00 27.13  ? 15  PHE   A N   1 
ATOM   74   C  CA  . PHE   A 1 18  ? -6.242  12.055 34.235  1.00 26.79  ? 15  PHE   A CA  1 
ATOM   75   C  C   . PHE   A 1 18  ? -4.860  12.678 34.073  1.00 24.73  ? 15  PHE   A C   1 
ATOM   76   O  O   . PHE   A 1 18  ? -3.856  12.213 34.648  1.00 24.00  ? 15  PHE   A O   1 
ATOM   77   C  CB  . PHE   A 1 18  ? -6.857  12.356 35.595  1.00 28.97  ? 15  PHE   A CB  1 
ATOM   78   C  CG  . PHE   A 1 18  ? -8.324  12.038 35.662  1.00 31.52  ? 15  PHE   A CG  1 
ATOM   79   C  CD1 . PHE   A 1 18  ? -9.271  12.948 35.219  1.00 33.22  ? 15  PHE   A CD1 1 
ATOM   80   C  CD2 . PHE   A 1 18  ? -8.756  10.802 36.118  1.00 33.62  ? 15  PHE   A CD2 1 
ATOM   81   C  CE1 . PHE   A 1 18  ? -10.628 12.638 35.272  1.00 35.19  ? 15  PHE   A CE1 1 
ATOM   82   C  CE2 . PHE   A 1 18  ? -10.105 10.485 36.147  1.00 35.07  ? 15  PHE   A CE2 1 
ATOM   83   C  CZ  . PHE   A 1 18  ? -11.041 11.410 35.745  1.00 35.74  ? 15  PHE   A CZ  1 
ATOM   84   N  N   . MET   A 1 19  ? -4.831  13.767 33.322  1.00 23.07  ? 16  MET   A N   1 
ATOM   85   C  CA  . MET   A 1 19  ? -3.585  14.492 33.011  1.00 22.52  ? 16  MET   A CA  1 
ATOM   86   C  C   . MET   A 1 19  ? -3.655  15.905 33.577  1.00 22.03  ? 16  MET   A C   1 
ATOM   87   O  O   . MET   A 1 19  ? -4.576  16.664 33.292  1.00 22.17  ? 16  MET   A O   1 
ATOM   88   C  CB  . MET   A 1 19  ? -3.386  14.569 31.502  1.00 22.09  ? 16  MET   A CB  1 
ATOM   89   C  CG  . MET   A 1 19  ? -2.153  15.353 31.085  1.00 22.68  ? 16  MET   A CG  1 
ATOM   90   S  SD  . MET   A 1 19  ? -2.084  15.660 29.273  1.00 24.04  ? 16  MET   A SD  1 
ATOM   91   C  CE  . MET   A 1 19  ? -1.390  14.090 28.767  1.00 22.71  ? 16  MET   A CE  1 
ATOM   92   N  N   . PRO   A 1 20  ? -2.702  16.335 34.424  1.00 21.63  ? 17  PRO   A N   1 
ATOM   93   C  CA  . PRO   A 1 20  ? -2.714  17.738 34.835  1.00 21.47  ? 17  PRO   A CA  1 
ATOM   94   C  C   . PRO   A 1 20  ? -2.494  18.685 33.649  1.00 20.40  ? 17  PRO   A C   1 
ATOM   95   O  O   . PRO   A 1 20  ? -1.724  18.368 32.778  1.00 19.39  ? 17  PRO   A O   1 
ATOM   96   C  CB  . PRO   A 1 20  ? -1.559  17.847 35.827  1.00 21.59  ? 17  PRO   A CB  1 
ATOM   97   C  CG  . PRO   A 1 20  ? -1.335  16.386 36.282  1.00 21.30  ? 17  PRO   A CG  1 
ATOM   98   C  CD  . PRO   A 1 20  ? -1.637  15.545 35.062  1.00 21.39  ? 17  PRO   A CD  1 
ATOM   99   N  N   . VAL   A 1 21  ? -3.188  19.815 33.660  1.00 20.81  ? 18  VAL   A N   1 
ATOM   100  C  CA  . VAL   A 1 21  ? -3.314  20.672 32.459  1.00 21.24  ? 18  VAL   A CA  1 
ATOM   101  C  C   . VAL   A 1 21  ? -2.088  21.562 32.383  1.00 20.75  ? 18  VAL   A C   1 
ATOM   102  O  O   . VAL   A 1 21  ? -1.906  22.216 31.302  1.00 20.33  ? 18  VAL   A O   1 
ATOM   103  C  CB  . VAL   A 1 21  ? -4.611  21.506 32.421  1.00 22.76  ? 18  VAL   A CB  1 
ATOM   104  C  CG1 . VAL   A 1 21  ? -5.857  20.614 32.371  1.00 23.70  ? 18  VAL   A CG1 1 
ATOM   105  C  CG2 . VAL   A 1 21  ? -4.690  22.545 33.544  1.00 23.17  ? 18  VAL   A CG2 1 
ATOM   106  N  N   . LEU   A 1 22  ? -1.325  21.694 33.485  1.00 20.41  ? 19  LEU   A N   1 
ATOM   107  C  CA  . LEU   A 1 22  ? -0.007  22.382 33.420  1.00 19.76  ? 19  LEU   A CA  1 
ATOM   108  C  C   . LEU   A 1 22  ? 1.116   21.366 33.563  1.00 19.49  ? 19  LEU   A C   1 
ATOM   109  O  O   . LEU   A 1 22  ? 1.128   20.611 34.553  1.00 19.45  ? 19  LEU   A O   1 
ATOM   110  C  CB  . LEU   A 1 22  ? 0.076   23.435 34.524  1.00 20.43  ? 19  LEU   A CB  1 
ATOM   111  C  CG  . LEU   A 1 22  ? 1.402   24.163 34.619  1.00 20.96  ? 19  LEU   A CG  1 
ATOM   112  C  CD1 . LEU   A 1 22  ? 1.635   24.969 33.340  1.00 21.06  ? 19  LEU   A CD1 1 
ATOM   113  C  CD2 . LEU   A 1 22  ? 1.405   25.037 35.869  1.00 21.83  ? 19  LEU   A CD2 1 
ATOM   114  N  N   . GLY   A 1 23  ? 2.090   21.391 32.659  1.00 18.73  ? 20  GLY   A N   1 
ATOM   115  C  CA  . GLY   A 1 23  ? 3.223   20.451 32.733  1.00 18.05  ? 20  GLY   A CA  1 
ATOM   116  C  C   . GLY   A 1 23  ? 4.555   21.154 32.774  1.00 18.78  ? 20  GLY   A C   1 
ATOM   117  O  O   . GLY   A 1 23  ? 4.691   22.286 32.202  1.00 18.61  ? 20  GLY   A O   1 
ATOM   118  N  N   . PHE   A 1 24  ? 5.534   20.518 33.412  1.00 19.10  ? 21  PHE   A N   1 
ATOM   119  C  CA  . PHE   A 1 24  ? 6.886   21.097 33.526  1.00 19.15  ? 21  PHE   A CA  1 
ATOM   120  C  C   . PHE   A 1 24  ? 7.753   20.564 32.392  1.00 18.31  ? 21  PHE   A C   1 
ATOM   121  O  O   . PHE   A 1 24  ? 7.936   19.318 32.253  1.00 17.78  ? 21  PHE   A O   1 
ATOM   122  C  CB  . PHE   A 1 24  ? 7.510   20.793 34.888  1.00 20.05  ? 21  PHE   A CB  1 
ATOM   123  C  CG  . PHE   A 1 24  ? 8.885   21.374 35.082  1.00 20.64  ? 21  PHE   A CG  1 
ATOM   124  C  CD1 . PHE   A 1 24  ? 9.071   22.749 35.112  1.00 21.66  ? 21  PHE   A CD1 1 
ATOM   125  C  CD2 . PHE   A 1 24  ? 10.010  20.575 35.207  1.00 20.76  ? 21  PHE   A CD2 1 
ATOM   126  C  CE1 . PHE   A 1 24  ? 10.338  23.293 35.286  1.00 21.99  ? 21  PHE   A CE1 1 
ATOM   127  C  CE2 . PHE   A 1 24  ? 11.280  21.114 35.340  1.00 21.63  ? 21  PHE   A CE2 1 
ATOM   128  C  CZ  . PHE   A 1 24  ? 11.440  22.479 35.378  1.00 21.96  ? 21  PHE   A CZ  1 
ATOM   129  N  N   . GLY   A 1 25  ? 8.313   21.481 31.608  1.00 19.02  ? 22  GLY   A N   1 
ATOM   130  C  CA  . GLY   A 1 25  ? 9.190   21.060 30.515  1.00 19.22  ? 22  GLY   A CA  1 
ATOM   131  C  C   . GLY   A 1 25  ? 10.611  20.881 30.995  1.00 19.41  ? 22  GLY   A C   1 
ATOM   132  O  O   . GLY   A 1 25  ? 11.144  21.795 31.613  1.00 21.49  ? 22  GLY   A O   1 
ATOM   133  N  N   . THR   A 1 26  ? 11.195  19.706 30.802  1.00 19.26  ? 23  THR   A N   1 
ATOM   134  C  CA  . THR   A 1 26  ? 12.522  19.387 31.396  1.00 19.50  ? 23  THR   A CA  1 
ATOM   135  C  C   . THR   A 1 26  ? 13.657  19.522 30.379  1.00 20.24  ? 23  THR   A C   1 
ATOM   136  O  O   . THR   A 1 26  ? 14.824  19.408 30.806  1.00 21.35  ? 23  THR   A O   1 
ATOM   137  C  CB  . THR   A 1 26  ? 12.613  17.978 32.003  1.00 19.21  ? 23  THR   A CB  1 
ATOM   138  O  OG1 . THR   A 1 26  ? 12.379  16.937 31.039  1.00 18.51  ? 23  THR   A OG1 1 
ATOM   139  C  CG2 . THR   A 1 26  ? 11.632  17.800 33.118  1.00 19.16  ? 23  THR   A CG2 1 
ATOM   140  N  N   . TYR   A 1 27  ? 13.383  19.721 29.089  1.00 20.90  ? 24  TYR   A N   1 
ATOM   141  C  CA  . TYR   A 1 27  ? 14.501  19.850 28.111  1.00 21.89  ? 24  TYR   A CA  1 
ATOM   142  C  C   . TYR   A 1 27  ? 15.334  21.092 28.435  1.00 22.83  ? 24  TYR   A C   1 
ATOM   143  O  O   . TYR   A 1 27  ? 14.815  22.211 28.502  1.00 22.60  ? 24  TYR   A O   1 
ATOM   144  C  CB  . TYR   A 1 27  ? 14.063  19.958 26.647  1.00 22.00  ? 24  TYR   A CB  1 
ATOM   145  C  CG  . TYR   A 1 27  ? 15.262  19.993 25.728  1.00 23.12  ? 24  TYR   A CG  1 
ATOM   146  C  CD1 . TYR   A 1 27  ? 15.949  18.830 25.378  1.00 24.10  ? 24  TYR   A CD1 1 
ATOM   147  C  CD2 . TYR   A 1 27  ? 15.768  21.203 25.279  1.00 23.79  ? 24  TYR   A CD2 1 
ATOM   148  C  CE1 . TYR   A 1 27  ? 17.071  18.869 24.555  1.00 25.57  ? 24  TYR   A CE1 1 
ATOM   149  C  CE2 . TYR   A 1 27  ? 16.895  21.269 24.481  1.00 24.95  ? 24  TYR   A CE2 1 
ATOM   150  C  CZ  . TYR   A 1 27  ? 17.540  20.097 24.098  1.00 26.59  ? 24  TYR   A CZ  1 
ATOM   151  O  OH  . TYR   A 1 27  ? 18.651  20.176 23.295  1.00 28.83  ? 24  TYR   A OH  1 
ATOM   152  N  N   . ALA   A 1 28  ? 16.639  20.899 28.500  1.00 24.23  ? 25  ALA   A N   1 
ATOM   153  C  CA  . ALA   A 1 28  ? 17.645  21.988 28.463  1.00 25.66  ? 25  ALA   A CA  1 
ATOM   154  C  C   . ALA   A 1 28  ? 18.711  21.600 27.450  1.00 27.00  ? 25  ALA   A C   1 
ATOM   155  O  O   . ALA   A 1 28  ? 18.963  20.405 27.244  1.00 27.78  ? 25  ALA   A O   1 
ATOM   156  C  CB  . ALA   A 1 28  ? 18.235  22.225 29.828  1.00 26.22  ? 25  ALA   A CB  1 
ATOM   157  N  N   . PRO   A 1 29  ? 19.315  22.597 26.775  1.00 29.12  ? 26  PRO   A N   1 
ATOM   158  C  CA  . PRO   A 1 29  ? 20.332  22.330 25.775  1.00 31.55  ? 26  PRO   A CA  1 
ATOM   159  C  C   . PRO   A 1 29  ? 21.476  21.540 26.409  1.00 33.37  ? 26  PRO   A C   1 
ATOM   160  O  O   . PRO   A 1 29  ? 21.735  21.657 27.605  1.00 32.03  ? 26  PRO   A O   1 
ATOM   161  C  CB  . PRO   A 1 29  ? 20.804  23.707 25.264  1.00 32.75  ? 26  PRO   A CB  1 
ATOM   162  C  CG  . PRO   A 1 29  ? 19.954  24.756 25.998  1.00 32.38  ? 26  PRO   A CG  1 
ATOM   163  C  CD  . PRO   A 1 29  ? 19.012  24.029 26.934  1.00 30.17  ? 26  PRO   A CD  1 
ATOM   164  N  N   . PRO   A 1 30  ? 22.281  20.830 25.593  1.00 37.02  ? 27  PRO   A N   1 
ATOM   165  C  CA  . PRO   A 1 30  ? 23.363  19.992 26.113  1.00 39.44  ? 27  PRO   A CA  1 
ATOM   166  C  C   . PRO   A 1 30  ? 24.406  20.770 26.933  1.00 41.31  ? 27  PRO   A C   1 
ATOM   167  O  O   . PRO   A 1 30  ? 25.115  20.159 27.687  1.00 44.11  ? 27  PRO   A O   1 
ATOM   168  C  CB  . PRO   A 1 30  ? 24.037  19.394 24.859  1.00 40.72  ? 27  PRO   A CB  1 
ATOM   169  C  CG  . PRO   A 1 30  ? 23.040  19.602 23.723  1.00 39.87  ? 27  PRO   A CG  1 
ATOM   170  C  CD  . PRO   A 1 30  ? 22.213  20.822 24.112  1.00 38.45  ? 27  PRO   A CD  1 
ATOM   171  N  N   . GLU   A 1 31  ? 24.529  22.085 26.746  1.00 41.63  ? 28  GLU   A N   1 
ATOM   172  C  CA  . GLU   A 1 31  ? 25.575  22.892 27.429  1.00 42.23  ? 28  GLU   A CA  1 
ATOM   173  C  C   . GLU   A 1 31  ? 25.217  23.044 28.918  1.00 41.55  ? 28  GLU   A C   1 
ATOM   174  O  O   . GLU   A 1 31  ? 26.105  23.407 29.705  1.00 42.50  ? 28  GLU   A O   1 
ATOM   175  C  CB  . GLU   A 1 31  ? 25.726  24.264 26.762  1.00 43.81  ? 28  GLU   A CB  1 
ATOM   176  C  CG  . GLU   A 1 31  ? 26.281  24.230 25.337  1.00 45.08  ? 28  GLU   A CG  1 
ATOM   177  C  CD  . GLU   A 1 31  ? 25.355  23.620 24.287  1.00 44.44  ? 28  GLU   A CD  1 
ATOM   178  O  OE1 . GLU   A 1 31  ? 24.099  23.750 24.419  1.00 40.58  ? 28  GLU   A OE1 1 
ATOM   179  O  OE2 . GLU   A 1 31  ? 25.896  23.040 23.326  1.00 44.62  ? 28  GLU   A OE2 1 
ATOM   180  N  N   . VAL   A 1 32  ? 23.958  22.791 29.296  1.00 38.78  ? 29  VAL   A N   1 
ATOM   181  C  CA  . VAL   A 1 32  ? 23.450  22.935 30.692  1.00 37.51  ? 29  VAL   A CA  1 
ATOM   182  C  C   . VAL   A 1 32  ? 23.788  21.653 31.448  1.00 36.98  ? 29  VAL   A C   1 
ATOM   183  O  O   . VAL   A 1 32  ? 23.465  20.550 31.015  1.00 36.17  ? 29  VAL   A O   1 
ATOM   184  C  CB  . VAL   A 1 32  ? 21.946  23.257 30.732  1.00 36.70  ? 29  VAL   A CB  1 
ATOM   185  C  CG1 . VAL   A 1 32  ? 21.388  23.291 32.167  1.00 36.44  ? 29  VAL   A CG1 1 
ATOM   186  C  CG2 . VAL   A 1 32  ? 21.624  24.563 29.978  1.00 37.58  ? 29  VAL   A CG2 1 
ATOM   187  N  N   . PRO   A 1 33  ? 24.489  21.747 32.593  1.00 37.76  ? 30  PRO   A N   1 
ATOM   188  C  CA  . PRO   A 1 33  ? 24.885  20.550 33.332  1.00 38.42  ? 30  PRO   A CA  1 
ATOM   189  C  C   . PRO   A 1 33  ? 23.675  19.685 33.698  1.00 35.89  ? 30  PRO   A C   1 
ATOM   190  O  O   . PRO   A 1 33  ? 22.662  20.224 34.016  1.00 33.34  ? 30  PRO   A O   1 
ATOM   191  C  CB  . PRO   A 1 33  ? 25.563  21.077 34.600  1.00 40.38  ? 30  PRO   A CB  1 
ATOM   192  C  CG  . PRO   A 1 33  ? 25.850  22.553 34.348  1.00 41.45  ? 30  PRO   A CG  1 
ATOM   193  C  CD  . PRO   A 1 33  ? 24.941  22.991 33.228  1.00 39.67  ? 30  PRO   A CD  1 
ATOM   194  N  N   . ARG   A 1 34  ? 23.844  18.362 33.644  1.00 35.41  ? 31  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 34  ? 22.776  17.392 33.992  1.00 34.20  ? 31  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 34  ? 22.320  17.576 35.446  1.00 33.62  ? 31  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 34  ? 21.136  17.253 35.713  1.00 32.66  ? 31  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 34  ? 23.251  15.959 33.748  1.00 34.98  ? 31  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 34  ? 23.616  15.637 32.308  1.00 36.06  ? 31  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 34  ? 22.529  15.931 31.315  1.00 34.03  ? 31  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 34  ? 22.604  17.281 30.780  1.00 34.13  ? 31  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 34  ? 21.732  17.781 29.906  1.00 32.50  ? 31  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 34  ? 21.844  19.021 29.456  1.00 32.47  ? 31  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 34  ? 20.731  17.022 29.507  1.00 32.10  ? 31  ARG   A NH2 1 
ATOM   205  N  N   . SER   A 1 35  ? 23.169  18.070 36.356  1.00 34.69  ? 32  SER   A N   1 
ATOM   206  C  CA  . SER   A 1 35  ? 22.753  18.340 37.761  1.00 34.78  ? 32  SER   A CA  1 
ATOM   207  C  C   . SER   A 1 35  ? 21.527  19.277 37.815  1.00 33.88  ? 32  SER   A C   1 
ATOM   208  O  O   . SER   A 1 35  ? 20.747  19.204 38.783  1.00 33.30  ? 32  SER   A O   1 
ATOM   209  C  CB  . SER   A 1 35  ? 23.867  18.920 38.572  1.00 36.60  ? 32  SER   A CB  1 
ATOM   210  O  OG  . SER   A 1 35  ? 24.255  20.180 38.047  1.00 36.87  ? 32  SER   A OG  1 
ATOM   211  N  N   . LYS   A 1 36  ? 21.392  20.183 36.848  1.00 33.11  ? 33  LYS   A N   1 
ATOM   212  C  CA  . LYS   A 1 36  ? 20.327  21.201 36.894  1.00 33.40  ? 33  LYS   A CA  1 
ATOM   213  C  C   . LYS   A 1 36  ? 18.967  20.507 36.798  1.00 30.43  ? 33  LYS   A C   1 
ATOM   214  O  O   . LYS   A 1 36  ? 18.057  20.945 37.497  1.00 29.30  ? 33  LYS   A O   1 
ATOM   215  C  CB  . LYS   A 1 36  ? 20.586  22.265 35.826  1.00 35.37  ? 33  LYS   A CB  1 
ATOM   216  C  CG  . LYS   A 1 36  ? 21.428  23.422 36.323  1.00 39.48  ? 33  LYS   A CG  1 
ATOM   217  C  CD  . LYS   A 1 36  ? 20.544  24.466 36.960  1.00 40.78  ? 33  LYS   A CD  1 
ATOM   218  C  CE  . LYS   A 1 36  ? 21.306  25.584 37.630  1.00 44.20  ? 33  LYS   A CE  1 
ATOM   219  N  NZ  . LYS   A 1 36  ? 20.384  26.416 38.437  1.00 46.17  ? 33  LYS   A NZ  1 
ATOM   220  N  N   . ALA   A 1 37  ? 18.832  19.460 35.980  1.00 29.35  ? 34  ALA   A N   1 
ATOM   221  C  CA  . ALA   A 1 37  ? 17.516  18.805 35.770  1.00 28.89  ? 34  ALA   A CA  1 
ATOM   222  C  C   . ALA   A 1 37  ? 17.021  18.222 37.102  1.00 28.20  ? 34  ALA   A C   1 
ATOM   223  O  O   . ALA   A 1 37  ? 15.803  18.234 37.335  1.00 25.56  ? 34  ALA   A O   1 
ATOM   224  C  CB  . ALA   A 1 37  ? 17.583  17.739 34.710  1.00 28.91  ? 34  ALA   A CB  1 
ATOM   225  N  N   . LEU   A 1 38  ? 17.942  17.694 37.920  1.00 29.75  ? 35  LEU   A N   1 
ATOM   226  C  CA  . LEU   A 1 38  ? 17.577  17.182 39.259  1.00 29.88  ? 35  LEU   A CA  1 
ATOM   227  C  C   . LEU   A 1 38  ? 17.125  18.383 40.094  1.00 29.42  ? 35  LEU   A C   1 
ATOM   228  O  O   . LEU   A 1 38  ? 16.030  18.341 40.617  1.00 27.96  ? 35  LEU   A O   1 
ATOM   229  C  CB  . LEU   A 1 38  ? 18.750  16.417 39.896  1.00 31.99  ? 35  LEU   A CB  1 
ATOM   230  C  CG  . LEU   A 1 38  ? 18.680  16.223 41.420  1.00 32.89  ? 35  LEU   A CG  1 
ATOM   231  C  CD1 . LEU   A 1 38  ? 17.460  15.432 41.854  1.00 32.66  ? 35  LEU   A CD1 1 
ATOM   232  C  CD2 . LEU   A 1 38  ? 19.936  15.555 41.951  1.00 35.25  ? 35  LEU   A CD2 1 
ATOM   233  N  N   . GLU   A 1 39  ? 17.914  19.451 40.147  1.00 30.18  ? 36  GLU   A N   1 
ATOM   234  C  CA  . GLU   A 1 39  ? 17.616  20.631 40.995  1.00 31.87  ? 36  GLU   A CA  1 
ATOM   235  C  C   . GLU   A 1 39  ? 16.248  21.216 40.608  1.00 28.72  ? 36  GLU   A C   1 
ATOM   236  O  O   . GLU   A 1 39  ? 15.405  21.449 41.485  1.00 27.43  ? 36  GLU   A O   1 
ATOM   237  C  CB  . GLU   A 1 39  ? 18.788  21.611 40.864  1.00 35.52  ? 36  GLU   A CB  1 
ATOM   238  C  CG  . GLU   A 1 39  ? 18.539  22.978 41.465  1.00 39.59  ? 36  GLU   A CG  1 
ATOM   239  C  CD  . GLU   A 1 39  ? 19.651  23.969 41.136  1.00 43.66  ? 36  GLU   A CD  1 
ATOM   240  O  OE1 . GLU   A 1 39  ? 19.423  24.863 40.316  1.00 46.79  ? 36  GLU   A OE1 1 
ATOM   241  O  OE2 . GLU   A 1 39  ? 20.762  23.807 41.655  1.00 49.78  ? 36  GLU   A OE2 1 
ATOM   242  N  N   . VAL   A 1 40  ? 16.017  21.490 39.323  1.00 28.21  ? 37  VAL   A N   1 
ATOM   243  C  CA  . VAL   A 1 40  ? 14.824  22.291 38.933  1.00 26.56  ? 37  VAL   A CA  1 
ATOM   244  C  C   . VAL   A 1 40  ? 13.585  21.405 38.932  1.00 25.05  ? 37  VAL   A C   1 
ATOM   245  O  O   . VAL   A 1 40  ? 12.510  21.958 39.206  1.00 24.76  ? 37  VAL   A O   1 
ATOM   246  C  CB  . VAL   A 1 40  ? 15.023  23.024 37.610  1.00 26.86  ? 37  VAL   A CB  1 
ATOM   247  C  CG1 . VAL   A 1 40  ? 16.245  23.906 37.730  1.00 28.37  ? 37  VAL   A CG1 1 
ATOM   248  C  CG2 . VAL   A 1 40  ? 15.092  22.042 36.450  1.00 26.05  ? 37  VAL   A CG2 1 
ATOM   249  N  N   . THR   A 1 41  ? 13.729  20.102 38.681  1.00 24.18  ? 38  THR   A N   1 
ATOM   250  C  CA  . THR   A 1 41  ? 12.564  19.175 38.707  1.00 23.85  ? 38  THR   A CA  1 
ATOM   251  C  C   . THR   A 1 41  ? 12.036  19.105 40.152  1.00 24.86  ? 38  THR   A C   1 
ATOM   252  O  O   . THR   A 1 41  ? 10.799  19.169 40.359  1.00 24.31  ? 38  THR   A O   1 
ATOM   253  C  CB  . THR   A 1 41  ? 12.873  17.816 38.066  1.00 23.45  ? 38  THR   A CB  1 
ATOM   254  O  OG1 . THR   A 1 41  ? 13.298  17.921 36.695  1.00 22.65  ? 38  THR   A OG1 1 
ATOM   255  C  CG2 . THR   A 1 41  ? 11.646  16.923 38.115  1.00 22.89  ? 38  THR   A CG2 1 
ATOM   256  N  N   . LYS   A 1 42  ? 12.924  19.050 41.156  1.00 26.04  ? 39  LYS   A N   1 
ATOM   257  C  CA  . LYS   A 1 42  ? 12.499  19.146 42.572  1.00 27.72  ? 39  LYS   A CA  1 
ATOM   258  C  C   . LYS   A 1 42  ? 11.860  20.506 42.849  1.00 27.17  ? 39  LYS   A C   1 
ATOM   259  O  O   . LYS   A 1 42  ? 10.822  20.530 43.505  1.00 27.15  ? 39  LYS   A O   1 
ATOM   260  C  CB  . LYS   A 1 42  ? 13.703  18.949 43.484  1.00 30.45  ? 39  LYS   A CB  1 
ATOM   261  C  CG  . LYS   A 1 42  ? 14.243  17.529 43.471  1.00 31.17  ? 39  LYS   A CG  1 
ATOM   262  C  CD  . LYS   A 1 42  ? 15.119  17.243 44.670  1.00 34.04  ? 39  LYS   A CD  1 
ATOM   263  C  CE  . LYS   A 1 42  ? 16.433  17.992 44.639  1.00 36.69  ? 39  LYS   A CE  1 
ATOM   264  N  NZ  . LYS   A 1 42  ? 17.234  17.731 45.870  1.00 39.84  ? 39  LYS   A NZ  1 
ATOM   265  N  N   . LEU   A 1 43  ? 12.445  21.602 42.361  1.00 26.87  ? 40  LEU   A N   1 
ATOM   266  C  CA  . LEU   A 1 43  ? 11.826  22.940 42.565  1.00 28.11  ? 40  LEU   A CA  1 
ATOM   267  C  C   . LEU   A 1 43  ? 10.434  22.959 41.905  1.00 26.28  ? 40  LEU   A C   1 
ATOM   268  O  O   . LEU   A 1 43  ? 9.531   23.513 42.503  1.00 26.31  ? 40  LEU   A O   1 
ATOM   269  C  CB  . LEU   A 1 43  ? 12.718  24.031 41.965  1.00 29.41  ? 40  LEU   A CB  1 
ATOM   270  C  CG  . LEU   A 1 43  ? 14.018  24.322 42.718  1.00 31.93  ? 40  LEU   A CG  1 
ATOM   271  C  CD1 . LEU   A 1 43  ? 14.883  25.269 41.900  1.00 32.75  ? 40  LEU   A CD1 1 
ATOM   272  C  CD2 . LEU   A 1 43  ? 13.730  24.887 44.114  1.00 33.79  ? 40  LEU   A CD2 1 
ATOM   273  N  N   . ALA   A 1 44  ? 10.285  22.418 40.696  1.00 23.97  ? 41  ALA   A N   1 
ATOM   274  C  CA  . ALA   A 1 44  ? 8.984   22.402 39.990  1.00 22.66  ? 41  ALA   A CA  1 
ATOM   275  C  C   . ALA   A 1 44  ? 7.945   21.699 40.869  1.00 22.87  ? 41  ALA   A C   1 
ATOM   276  O  O   . ALA   A 1 44  ? 6.819   22.226 41.054  1.00 22.37  ? 41  ALA   A O   1 
ATOM   277  C  CB  . ALA   A 1 44  ? 9.091   21.778 38.621  1.00 21.62  ? 41  ALA   A CB  1 
ATOM   278  N  N   . ILE   A 1 45  ? 8.323   20.551 41.426  1.00 23.61  ? 42  ILE   A N   1 
ATOM   279  C  CA  . ILE   A 1 45  ? 7.402   19.768 42.291  1.00 24.50  ? 42  ILE   A CA  1 
ATOM   280  C  C   . ILE   A 1 45  ? 7.075   20.586 43.549  1.00 26.06  ? 42  ILE   A C   1 
ATOM   281  O  O   . ILE   A 1 45  ? 5.931   20.630 43.947  1.00 26.45  ? 42  ILE   A O   1 
ATOM   282  C  CB  . ILE   A 1 45  ? 7.991   18.382 42.600  1.00 24.85  ? 42  ILE   A CB  1 
ATOM   283  C  CG1 . ILE   A 1 45  ? 8.013   17.575 41.307  1.00 24.35  ? 42  ILE   A CG1 1 
ATOM   284  C  CG2 . ILE   A 1 45  ? 7.185   17.679 43.677  1.00 26.21  ? 42  ILE   A CG2 1 
ATOM   285  C  CD1 . ILE   A 1 45  ? 8.780   16.283 41.373  1.00 25.11  ? 42  ILE   A CD1 1 
ATOM   286  N  N   . GLU   A 1 46  ? 8.064   21.216 44.150  1.00 27.64  ? 43  GLU   A N   1 
ATOM   287  C  CA  . GLU   A 1 46  ? 7.829   22.087 45.325  1.00 30.67  ? 43  GLU   A CA  1 
ATOM   288  C  C   . GLU   A 1 46  ? 6.837   23.188 44.979  1.00 29.73  ? 43  GLU   A C   1 
ATOM   289  O  O   . GLU   A 1 46  ? 5.990   23.429 45.820  1.00 31.78  ? 43  GLU   A O   1 
ATOM   290  C  CB  . GLU   A 1 46  ? 9.129   22.694 45.824  1.00 33.51  ? 43  GLU   A CB  1 
ATOM   291  C  CG  . GLU   A 1 46  ? 9.973   21.644 46.482  1.00 37.02  ? 43  GLU   A CG  1 
ATOM   292  C  CD  . GLU   A 1 46  ? 11.403  22.043 46.807  1.00 42.04  ? 43  GLU   A CD  1 
ATOM   293  O  OE1 . GLU   A 1 46  ? 11.684  23.298 46.918  1.00 46.03  ? 43  GLU   A OE1 1 
ATOM   294  O  OE2 . GLU   A 1 46  ? 12.226  21.089 47.013  1.00 46.81  ? 43  GLU   A OE2 1 
ATOM   295  N  N   . ALA   A 1 47  ? 6.961   23.809 43.807  1.00 27.76  ? 44  ALA   A N   1 
ATOM   296  C  CA  . ALA   A 1 47  ? 6.123   24.946 43.374  1.00 27.72  ? 44  ALA   A CA  1 
ATOM   297  C  C   . ALA   A 1 47  ? 4.698   24.469 43.086  1.00 27.22  ? 44  ALA   A C   1 
ATOM   298  O  O   . ALA   A 1 47  ? 3.804   25.330 43.053  1.00 28.88  ? 44  ALA   A O   1 
ATOM   299  C  CB  . ALA   A 1 47  ? 6.718   25.597 42.147  1.00 26.95  ? 44  ALA   A CB  1 
ATOM   300  N  N   . GLY   A 1 48  ? 4.512   23.177 42.802  1.00 26.35  ? 45  GLY   A N   1 
ATOM   301  C  CA  . GLY   A 1 48  ? 3.182   22.576 42.590  1.00 25.26  ? 45  GLY   A CA  1 
ATOM   302  C  C   . GLY   A 1 48  ? 2.992   21.938 41.218  1.00 23.22  ? 45  GLY   A C   1 
ATOM   303  O  O   . GLY   A 1 48  ? 1.860   21.469 40.935  1.00 22.58  ? 45  GLY   A O   1 
ATOM   304  N  N   . PHE   A 1 49  ? 4.037   21.822 40.412  1.00 22.01  ? 46  PHE   A N   1 
ATOM   305  C  CA  . PHE   A 1 49  ? 3.950   21.029 39.153  1.00 21.20  ? 46  PHE   A CA  1 
ATOM   306  C  C   . PHE   A 1 49  ? 3.792   19.540 39.529  1.00 21.44  ? 46  PHE   A C   1 
ATOM   307  O  O   . PHE   A 1 49  ? 4.431   19.080 40.508  1.00 21.16  ? 46  PHE   A O   1 
ATOM   308  C  CB  . PHE   A 1 49  ? 5.185   21.224 38.282  1.00 20.75  ? 46  PHE   A CB  1 
ATOM   309  C  CG  . PHE   A 1 49  ? 5.209   22.532 37.533  1.00 20.42  ? 46  PHE   A CG  1 
ATOM   310  C  CD1 . PHE   A 1 49  ? 5.799   23.649 38.128  1.00 21.21  ? 46  PHE   A CD1 1 
ATOM   311  C  CD2 . PHE   A 1 49  ? 4.703   22.641 36.243  1.00 19.57  ? 46  PHE   A CD2 1 
ATOM   312  C  CE1 . PHE   A 1 49  ? 5.867   24.843 37.437  1.00 21.40  ? 46  PHE   A CE1 1 
ATOM   313  C  CE2 . PHE   A 1 49  ? 4.767   23.851 35.567  1.00 19.62  ? 46  PHE   A CE2 1 
ATOM   314  C  CZ  . PHE   A 1 49  ? 5.314   24.951 36.187  1.00 20.72  ? 46  PHE   A CZ  1 
ATOM   315  N  N   . ARG   A 1 50  ? 2.935   18.824 38.812  1.00 21.91  ? 47  ARG   A N   1 
ATOM   316  C  CA  . ARG   A 1 50  ? 2.687   17.378 39.024  1.00 22.39  ? 47  ARG   A CA  1 
ATOM   317  C  C   . ARG   A 1 50  ? 2.854   16.611 37.703  1.00 22.19  ? 47  ARG   A C   1 
ATOM   318  O  O   . ARG   A 1 50  ? 3.245   15.443 37.727  1.00 24.28  ? 47  ARG   A O   1 
ATOM   319  C  CB  . ARG   A 1 50  ? 1.294   17.207 39.621  1.00 23.59  ? 47  ARG   A CB  1 
ATOM   320  C  CG  . ARG   A 1 50  ? 1.140   17.774 41.027  1.00 24.75  ? 47  ARG   A CG  1 
ATOM   321  C  CD  . ARG   A 1 50  ? 1.859   16.946 42.079  1.00 26.04  ? 47  ARG   A CD  1 
ATOM   322  N  NE  . ARG   A 1 50  ? 1.805   17.555 43.417  1.00 27.41  ? 47  ARG   A NE  1 
ATOM   323  C  CZ  . ARG   A 1 50  ? 2.629   18.483 43.892  1.00 28.06  ? 47  ARG   A CZ  1 
ATOM   324  N  NH1 . ARG   A 1 50  ? 3.561   19.036 43.132  1.00 27.32  ? 47  ARG   A NH1 1 
ATOM   325  N  NH2 . ARG   A 1 50  ? 2.474   18.926 45.130  1.00 29.02  ? 47  ARG   A NH2 1 
ATOM   326  N  N   . HIS   A 1 51  ? 2.717   17.293 36.577  1.00 21.43  ? 48  HIS   A N   1 
ATOM   327  C  CA  . HIS   A 1 51  ? 2.962   16.750 35.228  1.00 19.82  ? 48  HIS   A CA  1 
ATOM   328  C  C   . HIS   A 1 51  ? 4.383   17.146 34.848  1.00 18.94  ? 48  HIS   A C   1 
ATOM   329  O  O   . HIS   A 1 51  ? 4.715   18.372 34.870  1.00 19.01  ? 48  HIS   A O   1 
ATOM   330  C  CB  . HIS   A 1 51  ? 1.868   17.301 34.315  1.00 19.91  ? 48  HIS   A CB  1 
ATOM   331  C  CG  . HIS   A 1 51  ? 1.921   16.998 32.865  1.00 19.50  ? 48  HIS   A CG  1 
ATOM   332  N  ND1 . HIS   A 1 51  ? 0.819   17.329 32.078  1.00 18.50  ? 48  HIS   A ND1 1 
ATOM   333  C  CD2 . HIS   A 1 51  ? 2.898   16.550 32.020  1.00 19.75  ? 48  HIS   A CD2 1 
ATOM   334  C  CE1 . HIS   A 1 51  ? 1.097   17.017 30.831  1.00 19.10  ? 48  HIS   A CE1 1 
ATOM   335  N  NE2 . HIS   A 1 51  ? 2.355   16.522 30.751  1.00 18.82  ? 48  HIS   A NE2 1 
ATOM   336  N  N   A ILE   A 1 52  ? 5.215   16.153 34.551  0.47 18.91  ? 49  ILE   A N   1 
ATOM   337  N  N   B ILE   A 1 52  ? 5.204   16.146 34.541  0.53 18.68  ? 49  ILE   A N   1 
ATOM   338  C  CA  A ILE   A 1 52  ? 6.661   16.357 34.266  0.47 19.20  ? 49  ILE   A CA  1 
ATOM   339  C  CA  B ILE   A 1 52  ? 6.659   16.310 34.273  0.53 18.88  ? 49  ILE   A CA  1 
ATOM   340  C  C   A ILE   A 1 52  ? 6.951   15.732 32.901  0.47 18.68  ? 49  ILE   A C   1 
ATOM   341  C  C   B ILE   A 1 52  ? 6.934   15.727 32.886  0.53 18.52  ? 49  ILE   A C   1 
ATOM   342  O  O   A ILE   A 1 52  ? 6.667   14.528 32.727  0.47 18.95  ? 49  ILE   A O   1 
ATOM   343  O  O   B ILE   A 1 52  ? 6.650   14.526 32.696  0.53 18.85  ? 49  ILE   A O   1 
ATOM   344  C  CB  A ILE   A 1 52  ? 7.547   15.798 35.401  0.47 19.94  ? 49  ILE   A CB  1 
ATOM   345  C  CB  B ILE   A 1 52  ? 7.529   15.637 35.357  0.53 19.35  ? 49  ILE   A CB  1 
ATOM   346  C  CG1 A ILE   A 1 52  ? 7.333   16.552 36.713  0.47 20.20  ? 49  ILE   A CG1 1 
ATOM   347  C  CG1 B ILE   A 1 52  ? 7.077   15.981 36.779  0.53 19.48  ? 49  ILE   A CG1 1 
ATOM   348  C  CG2 A ILE   A 1 52  ? 9.031   15.792 35.036  0.47 20.30  ? 49  ILE   A CG2 1 
ATOM   349  C  CG2 B ILE   A 1 52  ? 9.016   15.944 35.169  0.53 19.76  ? 49  ILE   A CG2 1 
ATOM   350  C  CD1 A ILE   A 1 52  ? 7.975   15.865 37.882  0.47 21.17  ? 49  ILE   A CD1 1 
ATOM   351  C  CD1 B ILE   A 1 52  ? 7.224   17.420 37.152  0.53 19.25  ? 49  ILE   A CD1 1 
ATOM   352  N  N   . ASP   A 1 53  ? 7.438   16.546 31.963  1.00 17.89  ? 50  ASP   A N   1 
ATOM   353  C  CA  . ASP   A 1 53  ? 7.629   16.120 30.549  1.00 18.08  ? 50  ASP   A CA  1 
ATOM   354  C  C   . ASP   A 1 53  ? 9.108   15.867 30.264  1.00 18.81  ? 50  ASP   A C   1 
ATOM   355  O  O   . ASP   A 1 53  ? 9.920   16.840 30.256  1.00 20.02  ? 50  ASP   A O   1 
ATOM   356  C  CB  . ASP   A 1 53  ? 7.042   17.138 29.575  1.00 17.39  ? 50  ASP   A CB  1 
ATOM   357  C  CG  . ASP   A 1 53  ? 7.106   16.644 28.139  1.00 17.37  ? 50  ASP   A CG  1 
ATOM   358  O  OD1 . ASP   A 1 53  ? 6.194   15.866 27.754  1.00 19.66  ? 50  ASP   A OD1 1 
ATOM   359  O  OD2 . ASP   A 1 53  ? 8.092   16.971 27.450  1.00 16.32  ? 50  ASP   A OD2 1 
ATOM   360  N  N   . SER   A 1 54  ? 9.431   14.600 30.004  1.00 18.58  ? 51  SER   A N   1 
ATOM   361  C  CA  . SER   A 1 54  ? 10.785  14.158 29.629  1.00 18.91  ? 51  SER   A CA  1 
ATOM   362  C  C   . SER   A 1 54  ? 10.744  13.232 28.404  1.00 18.50  ? 51  SER   A C   1 
ATOM   363  O  O   . SER   A 1 54  ? 9.692   13.139 27.745  1.00 18.96  ? 51  SER   A O   1 
ATOM   364  C  CB  . SER   A 1 54  ? 11.428  13.530 30.825  1.00 19.28  ? 51  SER   A CB  1 
ATOM   365  O  OG  . SER   A 1 54  ? 12.790  13.210 30.594  1.00 20.72  ? 51  SER   A OG  1 
ATOM   366  N  N   . ALA   A 1 55  ? 11.893  12.649 28.068  1.00 19.21  ? 52  ALA   A N   1 
ATOM   367  C  CA  . ALA   A 1 55  ? 12.070  11.841 26.834  1.00 19.41  ? 52  ALA   A CA  1 
ATOM   368  C  C   . ALA   A 1 55  ? 13.449  11.225 26.840  1.00 20.88  ? 52  ALA   A C   1 
ATOM   369  O  O   . ALA   A 1 55  ? 14.376  11.851 27.414  1.00 20.98  ? 52  ALA   A O   1 
ATOM   370  C  CB  . ALA   A 1 55  ? 11.912  12.716 25.601  1.00 19.15  ? 52  ALA   A CB  1 
ATOM   371  N  N   . HIS   A 1 56  ? 13.602  10.081 26.141  1.00 22.34  ? 53  HIS   A N   1 
ATOM   372  C  CA  . HIS   A 1 56  ? 14.928  9.485  25.935  1.00 24.68  ? 53  HIS   A CA  1 
ATOM   373  C  C   . HIS   A 1 56  ? 15.847  10.567 25.369  1.00 24.40  ? 53  HIS   A C   1 
ATOM   374  O  O   . HIS   A 1 56  ? 16.978  10.718 25.829  1.00 25.10  ? 53  HIS   A O   1 
ATOM   375  C  CB  . HIS   A 1 56  ? 14.827  8.232  25.053  1.00 27.86  ? 53  HIS   A CB  1 
ATOM   376  C  CG  . HIS   A 1 56  ? 16.148  7.618  24.811  1.00 31.67  ? 53  HIS   A CG  1 
ATOM   377  N  ND1 . HIS   A 1 56  ? 16.869  7.067  25.848  1.00 36.09  ? 53  HIS   A ND1 1 
ATOM   378  C  CD2 . HIS   A 1 56  ? 16.937  7.560  23.729  1.00 35.12  ? 53  HIS   A CD2 1 
ATOM   379  C  CE1 . HIS   A 1 56  ? 18.010  6.607  25.382  1.00 37.75  ? 53  HIS   A CE1 1 
ATOM   380  N  NE2 . HIS   A 1 56  ? 18.088  6.929  24.102  1.00 37.05  ? 53  HIS   A NE2 1 
ATOM   381  N  N   . LEU   A 1 57  ? 15.357  11.331 24.415  1.00 23.81  ? 54  LEU   A N   1 
ATOM   382  C  CA  . LEU   A 1 57  ? 16.219  12.230 23.615  1.00 24.32  ? 54  LEU   A CA  1 
ATOM   383  C  C   . LEU   A 1 57  ? 16.853  13.293 24.512  1.00 24.26  ? 54  LEU   A C   1 
ATOM   384  O  O   . LEU   A 1 57  ? 17.893  13.814 24.132  1.00 24.75  ? 54  LEU   A O   1 
ATOM   385  C  CB  . LEU   A 1 57  ? 15.388  12.868 22.501  1.00 23.82  ? 54  LEU   A CB  1 
ATOM   386  C  CG  . LEU   A 1 57  ? 16.139  13.818 21.571  1.00 25.39  ? 54  LEU   A CG  1 
ATOM   387  C  CD1 . LEU   A 1 57  ? 17.166  13.059 20.734  1.00 27.42  ? 54  LEU   A CD1 1 
ATOM   388  C  CD2 . LEU   A 1 57  ? 15.141  14.598 20.690  1.00 24.99  ? 54  LEU   A CD2 1 
ATOM   389  N  N   . TYR   A 1 58  ? 16.232  13.651 25.625  1.00 23.87  ? 55  TYR   A N   1 
ATOM   390  C  CA  . TYR   A 1 58  ? 16.647  14.838 26.425  1.00 23.74  ? 55  TYR   A CA  1 
ATOM   391  C  C   . TYR   A 1 58  ? 17.907  14.552 27.251  1.00 25.14  ? 55  TYR   A C   1 
ATOM   392  O  O   . TYR   A 1 58  ? 18.420  15.491 27.839  1.00 25.69  ? 55  TYR   A O   1 
ATOM   393  C  CB  . TYR   A 1 58  ? 15.527  15.267 27.377  1.00 23.08  ? 55  TYR   A CB  1 
ATOM   394  C  CG  . TYR   A 1 58  ? 14.229  15.681 26.737  1.00 21.68  ? 55  TYR   A CG  1 
ATOM   395  C  CD1 . TYR   A 1 58  ? 14.094  15.852 25.366  1.00 21.83  ? 55  TYR   A CD1 1 
ATOM   396  C  CD2 . TYR   A 1 58  ? 13.116  15.951 27.535  1.00 21.90  ? 55  TYR   A CD2 1 
ATOM   397  C  CE1 . TYR   A 1 58  ? 12.916  16.323 24.813  1.00 20.59  ? 55  TYR   A CE1 1 
ATOM   398  C  CE2 . TYR   A 1 58  ? 11.915  16.371 26.988  1.00 20.48  ? 55  TYR   A CE2 1 
ATOM   399  C  CZ  . TYR   A 1 58  ? 11.809  16.526 25.614  1.00 20.52  ? 55  TYR   A CZ  1 
ATOM   400  O  OH  . TYR   A 1 58  ? 10.617  16.913 25.079  1.00 20.33  ? 55  TYR   A OH  1 
ATOM   401  N  N   . ASN   A 1 59  ? 18.334  13.290 27.364  1.00 25.83  ? 56  ASN   A N   1 
ATOM   402  C  CA  . ASN   A 1 59  ? 19.516  12.879 28.167  1.00 27.00  ? 56  ASN   A CA  1 
ATOM   403  C  C   . ASN   A 1 59  ? 19.327  13.398 29.595  1.00 26.65  ? 56  ASN   A C   1 
ATOM   404  O  O   . ASN   A 1 59  ? 20.252  14.047 30.174  1.00 28.19  ? 56  ASN   A O   1 
ATOM   405  C  CB  . ASN   A 1 59  ? 20.809  13.420 27.527  1.00 29.58  ? 56  ASN   A CB  1 
ATOM   406  C  CG  . ASN   A 1 59  ? 22.089  12.960 28.204  1.00 31.64  ? 56  ASN   A CG  1 
ATOM   407  O  OD1 . ASN   A 1 59  ? 22.156  11.839 28.691  1.00 35.41  ? 56  ASN   A OD1 1 
ATOM   408  N  ND2 . ASN   A 1 59  ? 23.105  13.804 28.251  1.00 32.49  ? 56  ASN   A ND2 1 
ATOM   409  N  N   . ASN   A 1 60  ? 18.140  13.239 30.160  1.00 24.91  ? 57  ASN   A N   1 
ATOM   410  C  CA  . ASN   A 1 60  ? 17.949  13.756 31.534  1.00 25.09  ? 57  ASN   A CA  1 
ATOM   411  C  C   . ASN   A 1 60  ? 17.085  12.798 32.353  1.00 24.90  ? 57  ASN   A C   1 
ATOM   412  O  O   . ASN   A 1 60  ? 16.754  13.178 33.502  1.00 23.65  ? 57  ASN   A O   1 
ATOM   413  C  CB  . ASN   A 1 60  ? 17.428  15.186 31.520  1.00 24.40  ? 57  ASN   A CB  1 
ATOM   414  C  CG  . ASN   A 1 60  ? 15.993  15.301 31.064  1.00 22.48  ? 57  ASN   A CG  1 
ATOM   415  O  OD1 . ASN   A 1 60  ? 15.313  14.303 30.838  1.00 21.94  ? 57  ASN   A OD1 1 
ATOM   416  N  ND2 . ASN   A 1 60  ? 15.533  16.535 30.904  1.00 23.20  ? 57  ASN   A ND2 1 
ATOM   417  N  N   . GLU   A 1 61  ? 16.725  11.607 31.837  1.00 25.10  ? 58  GLU   A N   1 
ATOM   418  C  CA  . GLU   A 1 61  ? 15.697  10.817 32.555  1.00 26.14  ? 58  GLU   A CA  1 
ATOM   419  C  C   . GLU   A 1 61  ? 16.261  10.359 33.911  1.00 27.19  ? 58  GLU   A C   1 
ATOM   420  O  O   . GLU   A 1 61  ? 15.469  10.263 34.862  1.00 25.25  ? 58  GLU   A O   1 
ATOM   421  C  CB  . GLU   A 1 61  ? 15.191  9.623  31.729  1.00 26.56  ? 58  GLU   A CB  1 
ATOM   422  C  CG  . GLU   A 1 61  ? 14.249  10.049 30.619  1.00 27.18  ? 58  GLU   A CG  1 
ATOM   423  C  CD  . GLU   A 1 61  ? 13.569  8.926  29.857  1.00 27.96  ? 58  GLU   A CD  1 
ATOM   424  O  OE1 . GLU   A 1 61  ? 14.217  8.248  29.059  1.00 28.38  ? 58  GLU   A OE1 1 
ATOM   425  O  OE2 . GLU   A 1 61  ? 12.378  8.733  30.088  1.00 30.02  ? 58  GLU   A OE2 1 
ATOM   426  N  N   . GLU   A 1 62  ? 17.568  10.091 33.985  1.00 29.25  ? 59  GLU   A N   1 
ATOM   427  C  CA  . GLU   A 1 62  ? 18.264  9.714  35.248  1.00 31.04  ? 59  GLU   A CA  1 
ATOM   428  C  C   . GLU   A 1 62  ? 17.999  10.800 36.295  1.00 29.47  ? 59  GLU   A C   1 
ATOM   429  O  O   . GLU   A 1 62  ? 17.551  10.469 37.431  1.00 28.90  ? 59  GLU   A O   1 
ATOM   430  C  CB  . GLU   A 1 62  ? 19.782  9.578  35.063  1.00 34.04  ? 59  GLU   A CB  1 
ATOM   431  C  CG  . GLU   A 1 62  ? 20.514  9.140  36.330  1.00 37.37  ? 59  GLU   A CG  1 
ATOM   432  C  CD  . GLU   A 1 62  ? 22.040  9.110  36.247  1.00 41.73  ? 59  GLU   A CD  1 
ATOM   433  O  OE1 . GLU   A 1 62  ? 22.608  9.359  35.147  1.00 44.49  ? 59  GLU   A OE1 1 
ATOM   434  O  OE2 . GLU   A 1 62  ? 22.677  8.856  37.289  1.00 44.22  ? 59  GLU   A OE2 1 
ATOM   435  N  N   . GLN   A 1 63  ? 18.219  12.051 35.915  1.00 28.26  ? 60  GLN   A N   1 
ATOM   436  C  CA  . GLN   A 1 63  ? 18.092  13.207 36.847  1.00 28.08  ? 60  GLN   A CA  1 
ATOM   437  C  C   . GLN   A 1 63  ? 16.627  13.522 37.144  1.00 26.29  ? 60  GLN   A C   1 
ATOM   438  O  O   . GLN   A 1 63  ? 16.335  13.808 38.302  1.00 25.03  ? 60  GLN   A O   1 
ATOM   439  C  CB  . GLN   A 1 63  ? 18.850  14.408 36.301  1.00 28.85  ? 60  GLN   A CB  1 
ATOM   440  C  CG  . GLN   A 1 63  ? 20.350  14.170 36.302  1.00 31.19  ? 60  GLN   A CG  1 
ATOM   441  C  CD  . GLN   A 1 63  ? 20.851  13.439 35.082  1.00 31.63  ? 60  GLN   A CD  1 
ATOM   442  O  OE1 . GLN   A 1 63  ? 20.149  13.242 34.093  1.00 31.05  ? 60  GLN   A OE1 1 
ATOM   443  N  NE2 . GLN   A 1 63  ? 22.108  13.035 35.156  1.00 35.40  ? 60  GLN   A NE2 1 
ATOM   444  N  N   . VAL   A 1 64  ? 15.743  13.520 36.142  1.00 24.90  ? 61  VAL   A N   1 
ATOM   445  C  CA  . VAL   A 1 64  ? 14.298  13.807 36.357  1.00 23.84  ? 61  VAL   A CA  1 
ATOM   446  C  C   . VAL   A 1 64  ? 13.710  12.707 37.257  1.00 24.01  ? 61  VAL   A C   1 
ATOM   447  O  O   . VAL   A 1 64  ? 13.004  13.025 38.233  1.00 23.54  ? 61  VAL   A O   1 
ATOM   448  C  CB  . VAL   A 1 64  ? 13.566  13.930 35.015  1.00 22.59  ? 61  VAL   A CB  1 
ATOM   449  C  CG1 . VAL   A 1 64  ? 12.090  14.121 35.202  1.00 21.94  ? 61  VAL   A CG1 1 
ATOM   450  C  CG2 . VAL   A 1 64  ? 14.165  15.042 34.155  1.00 23.12  ? 61  VAL   A CG2 1 
ATOM   451  N  N   . GLY   A 1 65  ? 14.060  11.457 36.967  1.00 24.20  ? 62  GLY   A N   1 
ATOM   452  C  CA  . GLY   A 1 65  ? 13.627  10.303 37.771  1.00 25.48  ? 62  GLY   A CA  1 
ATOM   453  C  C   . GLY   A 1 65  ? 14.034  10.479 39.201  1.00 26.46  ? 62  GLY   A C   1 
ATOM   454  O  O   . GLY   A 1 65  ? 13.204  10.229 40.097  1.00 26.86  ? 62  GLY   A O   1 
ATOM   455  N  N   . LEU   A 1 66  ? 15.283  10.871 39.400  1.00 27.17  ? 63  LEU   A N   1 
ATOM   456  C  CA  . LEU   A 1 66  ? 15.869  10.999 40.753  1.00 29.12  ? 63  LEU   A CA  1 
ATOM   457  C  C   . LEU   A 1 66  ? 15.186  12.156 41.494  1.00 27.89  ? 63  LEU   A C   1 
ATOM   458  O  O   . LEU   A 1 66  ? 14.850  11.948 42.660  1.00 27.84  ? 63  LEU   A O   1 
ATOM   459  C  CB  . LEU   A 1 66  ? 17.375  11.135 40.556  1.00 31.81  ? 63  LEU   A CB  1 
ATOM   460  C  CG  . LEU   A 1 66  ? 18.260  11.238 41.774  1.00 35.43  ? 63  LEU   A CG  1 
ATOM   461  C  CD1 . LEU   A 1 66  ? 17.969  10.104 42.756  1.00 37.25  ? 63  LEU   A CD1 1 
ATOM   462  C  CD2 . LEU   A 1 66  ? 19.717  11.205 41.320  1.00 37.13  ? 63  LEU   A CD2 1 
ATOM   463  N  N   . ALA   A 1 67  ? 14.801  13.243 40.816  1.00 25.51  ? 64  ALA   A N   1 
ATOM   464  C  CA  . ALA   A 1 67  ? 14.031  14.331 41.455  1.00 25.52  ? 64  ALA   A CA  1 
ATOM   465  C  C   . ALA   A 1 67  ? 12.660  13.781 41.898  1.00 24.52  ? 64  ALA   A C   1 
ATOM   466  O  O   . ALA   A 1 67  ? 12.246  14.055 43.036  1.00 25.05  ? 64  ALA   A O   1 
ATOM   467  C  CB  . ALA   A 1 67  ? 13.882  15.533 40.547  1.00 25.53  ? 64  ALA   A CB  1 
ATOM   468  N  N   . ILE   A 1 68  ? 12.008  12.962 41.069  1.00 23.87  ? 65  ILE   A N   1 
ATOM   469  C  CA  . ILE   A 1 68  ? 10.662  12.397 41.388  1.00 24.15  ? 65  ILE   A CA  1 
ATOM   470  C  C   . ILE   A 1 68  ? 10.811  11.424 42.572  1.00 26.28  ? 65  ILE   A C   1 
ATOM   471  O  O   . ILE   A 1 68  ? 10.021  11.534 43.562  1.00 26.91  ? 65  ILE   A O   1 
ATOM   472  C  CB  . ILE   A 1 68  ? 9.993   11.750 40.156  1.00 22.74  ? 65  ILE   A CB  1 
ATOM   473  C  CG1 . ILE   A 1 68  ? 9.636   12.830 39.127  1.00 21.74  ? 65  ILE   A CG1 1 
ATOM   474  C  CG2 . ILE   A 1 68  ? 8.803   10.877 40.574  1.00 22.89  ? 65  ILE   A CG2 1 
ATOM   475  C  CD1 . ILE   A 1 68  ? 9.255   12.309 37.749  1.00 21.03  ? 65  ILE   A CD1 1 
ATOM   476  N  N   . ARG   A 1 69  ? 11.787  10.520 42.491  1.00 27.52  ? 66  ARG   A N   1 
ATOM   477  C  CA  . ARG   A 1 69  ? 12.014  9.522  43.575  1.00 29.29  ? 66  ARG   A CA  1 
ATOM   478  C  C   . ARG   A 1 69  ? 12.292  10.244 44.897  1.00 29.70  ? 66  ARG   A C   1 
ATOM   479  O  O   . ARG   A 1 69  ? 11.785  9.810  45.937  1.00 28.84  ? 66  ARG   A O   1 
ATOM   480  C  CB  . ARG   A 1 69  ? 13.163  8.601  43.179  1.00 31.36  ? 66  ARG   A CB  1 
ATOM   481  C  CG  . ARG   A 1 69  ? 12.807  7.555  42.135  1.00 32.39  ? 66  ARG   A CG  1 
ATOM   482  C  CD  . ARG   A 1 69  ? 11.685  6.660  42.561  1.00 35.18  ? 66  ARG   A CD  1 
ATOM   483  N  NE  . ARG   A 1 69  ? 11.980  5.903  43.783  1.00 38.69  ? 66  ARG   A NE  1 
ATOM   484  C  CZ  . ARG   A 1 69  ? 12.732  4.799  43.833  1.00 41.62  ? 66  ARG   A CZ  1 
ATOM   485  N  NH1 . ARG   A 1 69  ? 13.322  4.347  42.734  1.00 42.42  ? 66  ARG   A NH1 1 
ATOM   486  N  NH2 . ARG   A 1 69  ? 12.940  4.180  44.987  1.00 43.80  ? 66  ARG   A NH2 1 
ATOM   487  N  N   . SER   A 1 70  ? 13.052  11.331 44.811  1.00 29.92  ? 67  SER   A N   1 
ATOM   488  C  CA  . SER   A 1 70  ? 13.459  12.156 45.962  1.00 31.81  ? 67  SER   A CA  1 
ATOM   489  C  C   . SER   A 1 70  ? 12.226  12.772 46.617  1.00 30.95  ? 67  SER   A C   1 
ATOM   490  O  O   . SER   A 1 70  ? 12.117  12.743 47.843  1.00 31.92  ? 67  SER   A O   1 
ATOM   491  C  CB  . SER   A 1 70  ? 14.475  13.182 45.508  1.00 32.11  ? 67  SER   A CB  1 
ATOM   492  O  OG  . SER   A 1 70  ? 15.129  13.685 46.623  1.00 36.71  ? 67  SER   A OG  1 
ATOM   493  N  N   . LYS   A 1 71  ? 11.313  13.328 45.825  1.00 29.88  ? 68  LYS   A N   1 
ATOM   494  C  CA  . LYS   A 1 71  ? 10.149  14.065 46.382  1.00 29.82  ? 68  LYS   A CA  1 
ATOM   495  C  C   . LYS   A 1 71  ? 9.106   13.053 46.849  1.00 29.33  ? 68  LYS   A C   1 
ATOM   496  O  O   . LYS   A 1 71  ? 8.281   13.430 47.691  1.00 29.99  ? 68  LYS   A O   1 
ATOM   497  C  CB  . LYS   A 1 71  ? 9.589   15.062 45.358  1.00 29.06  ? 68  LYS   A CB  1 
ATOM   498  C  CG  . LYS   A 1 71  ? 10.591  16.108 44.911  1.00 29.85  ? 68  LYS   A CG  1 
ATOM   499  C  CD  . LYS   A 1 71  ? 11.151  16.945 46.032  1.00 32.23  ? 68  LYS   A CD  1 
ATOM   500  C  CE  . LYS   A 1 71  ? 10.103  17.792 46.720  1.00 33.57  ? 68  LYS   A CE  1 
ATOM   501  N  NZ  . LYS   A 1 71  ? 10.720  18.661 47.752  1.00 36.01  ? 68  LYS   A NZ  1 
ATOM   502  N  N   . ILE   A 1 72  ? 9.155   11.809 46.369  1.00 28.57  ? 69  ILE   A N   1 
ATOM   503  C  CA  . ILE   A 1 72  ? 8.276   10.750 46.949  1.00 29.73  ? 69  ILE   A CA  1 
ATOM   504  C  C   . ILE   A 1 72  ? 8.862   10.295 48.305  1.00 31.44  ? 69  ILE   A C   1 
ATOM   505  O  O   . ILE   A 1 72  ? 8.102   10.109 49.284  1.00 31.88  ? 69  ILE   A O   1 
ATOM   506  C  CB  . ILE   A 1 72  ? 8.088   9.586  45.974  1.00 29.10  ? 69  ILE   A CB  1 
ATOM   507  C  CG1 . ILE   A 1 72  ? 7.404   10.049 44.686  1.00 27.99  ? 69  ILE   A CG1 1 
ATOM   508  C  CG2 . ILE   A 1 72  ? 7.351   8.426  46.648  1.00 30.35  ? 69  ILE   A CG2 1 
ATOM   509  C  CD1 . ILE   A 1 72  ? 7.611   9.059  43.538  1.00 27.64  ? 69  ILE   A CD1 1 
ATOM   510  N  N   . ALA   A 1 73  ? 10.171  10.050 48.345  1.00 32.20  ? 70  ALA   A N   1 
ATOM   511  C  CA  . ALA   A 1 73  ? 10.840  9.476  49.529  1.00 34.52  ? 70  ALA   A CA  1 
ATOM   512  C  C   . ALA   A 1 73  ? 10.859  10.549 50.629  1.00 36.20  ? 70  ALA   A C   1 
ATOM   513  O  O   . ALA   A 1 73  ? 10.785  10.178 51.811  1.00 37.25  ? 70  ALA   A O   1 
ATOM   514  C  CB  . ALA   A 1 73  ? 12.224  8.965  49.165  1.00 34.74  ? 70  ALA   A CB  1 
ATOM   515  N  N   . ASP   A 1 74  ? 10.874  11.835 50.269  1.00 36.29  ? 71  ASP   A N   1 
ATOM   516  C  CA  . ASP   A 1 74  ? 10.875  12.922 51.283  1.00 38.36  ? 71  ASP   A CA  1 
ATOM   517  C  C   . ASP   A 1 74  ? 9.456   13.138 51.843  1.00 38.07  ? 71  ASP   A C   1 
ATOM   518  O  O   . ASP   A 1 74  ? 9.344   13.911 52.810  1.00 38.78  ? 71  ASP   A O   1 
ATOM   519  C  CB  . ASP   A 1 74  ? 11.617  14.161 50.773  1.00 38.93  ? 71  ASP   A CB  1 
ATOM   520  C  CG  . ASP   A 1 74  ? 10.855  15.192 49.970  1.00 38.99  ? 71  ASP   A CG  1 
ATOM   521  O  OD1 . ASP   A 1 74  ? 9.622   15.151 49.964  1.00 39.88  ? 71  ASP   A OD1 1 
ATOM   522  O  OD2 . ASP   A 1 74  ? 11.529  16.086 49.397  1.00 41.38  ? 71  ASP   A OD2 1 
ATOM   523  N  N   . GLY   A 1 75  ? 8.434   12.461 51.305  1.00 37.71  ? 72  GLY   A N   1 
ATOM   524  C  CA  . GLY   A 1 75  ? 7.044   12.547 51.798  1.00 37.86  ? 72  GLY   A CA  1 
ATOM   525  C  C   . GLY   A 1 75  ? 6.268   13.683 51.156  1.00 36.87  ? 72  GLY   A C   1 
ATOM   526  O  O   . GLY   A 1 75  ? 5.112   13.854 51.524  1.00 37.10  ? 72  GLY   A O   1 
ATOM   527  N  N   . SER   A 1 76  ? 6.853   14.409 50.194  1.00 35.86  ? 73  SER   A N   1 
ATOM   528  C  CA  . SER   A 1 76  ? 6.236   15.591 49.531  1.00 35.90  ? 73  SER   A CA  1 
ATOM   529  C  C   . SER   A 1 76  ? 5.055   15.158 48.670  1.00 35.17  ? 73  SER   A C   1 
ATOM   530  O  O   . SER   A 1 76  ? 4.059   15.869 48.650  1.00 35.67  ? 73  SER   A O   1 
ATOM   531  C  CB  . SER   A 1 76  ? 7.219   16.329 48.671  1.00 35.41  ? 73  SER   A CB  1 
ATOM   532  O  OG  . SER   A 1 76  ? 8.104   17.085 49.460  1.00 36.67  ? 73  SER   A OG  1 
ATOM   533  N  N   . VAL   A 1 77  ? 5.216   14.061 47.936  1.00 34.23  ? 74  VAL   A N   1 
ATOM   534  C  CA  . VAL   A 1 77  ? 4.201   13.572 46.961  1.00 33.13  ? 74  VAL   A CA  1 
ATOM   535  C  C   . VAL   A 1 77  ? 4.225   12.063 47.033  1.00 33.42  ? 74  VAL   A C   1 
ATOM   536  O  O   . VAL   A 1 77  ? 5.239   11.492 47.490  1.00 33.87  ? 74  VAL   A O   1 
ATOM   537  C  CB  . VAL   A 1 77  ? 4.475   14.017 45.512  1.00 32.09  ? 74  VAL   A CB  1 
ATOM   538  C  CG1 . VAL   A 1 77  ? 4.246   15.507 45.342  1.00 32.50  ? 74  VAL   A CG1 1 
ATOM   539  C  CG2 . VAL   A 1 77  ? 5.871   13.607 45.025  1.00 30.85  ? 74  VAL   A CG2 1 
ATOM   540  N  N   . LYS   A 1 78  ? 3.168   11.469 46.537  1.00 32.81  ? 75  LYS   A N   1 
ATOM   541  C  CA  . LYS   A 1 78  ? 3.123   10.021 46.284  1.00 34.70  ? 75  LYS   A CA  1 
ATOM   542  C  C   . LYS   A 1 78  ? 3.258   9.828  44.780  1.00 32.77  ? 75  LYS   A C   1 
ATOM   543  O  O   . LYS   A 1 78  ? 3.041   10.809 44.004  1.00 29.95  ? 75  LYS   A O   1 
ATOM   544  C  CB  . LYS   A 1 78  ? 1.893   9.398  46.948  1.00 39.06  ? 75  LYS   A CB  1 
ATOM   545  C  CG  . LYS   A 1 78  ? 0.537   9.796  46.420  1.00 41.34  ? 75  LYS   A CG  1 
ATOM   546  C  CD  . LYS   A 1 78  ? -0.566  9.170  47.274  1.00 46.04  ? 75  LYS   A CD  1 
ATOM   547  C  CE  . LYS   A 1 78  ? -1.937  9.277  46.637  1.00 47.45  ? 75  LYS   A CE  1 
ATOM   548  N  NZ  . LYS   A 1 78  ? -2.517  7.932  46.445  1.00 49.44  ? 75  LYS   A NZ  1 
ATOM   549  N  N   . ARG   A 1 79  ? 3.671   8.618  44.424  1.00 31.44  ? 76  ARG   A N   1 
ATOM   550  C  CA  . ARG   A 1 79  ? 3.903   8.240  43.012  1.00 30.14  ? 76  ARG   A CA  1 
ATOM   551  C  C   . ARG   A 1 79  ? 2.668   8.613  42.198  1.00 28.83  ? 76  ARG   A C   1 
ATOM   552  O  O   . ARG   A 1 79  ? 2.856   9.157  41.105  1.00 28.16  ? 76  ARG   A O   1 
ATOM   553  C  CB  . ARG   A 1 79  ? 4.252   6.757  42.854  1.00 30.54  ? 76  ARG   A CB  1 
ATOM   554  C  CG  . ARG   A 1 79  ? 4.460   6.333  41.402  1.00 29.20  ? 76  ARG   A CG  1 
ATOM   555  C  CD  . ARG   A 1 79  ? 5.549   7.125  40.685  1.00 28.15  ? 76  ARG   A CD  1 
ATOM   556  N  NE  . ARG   A 1 79  ? 5.618   6.875  39.257  1.00 26.37  ? 76  ARG   A NE  1 
ATOM   557  C  CZ  . ARG   A 1 79  ? 4.932   7.520  38.335  1.00 25.74  ? 76  ARG   A CZ  1 
ATOM   558  N  NH1 . ARG   A 1 79  ? 4.101   8.519  38.627  1.00 25.20  ? 76  ARG   A NH1 1 
ATOM   559  N  NH2 . ARG   A 1 79  ? 5.113   7.185  37.068  1.00 25.47  ? 76  ARG   A NH2 1 
ATOM   560  N  N   . GLU   A 1 80  ? 1.476   8.344  42.716  1.00 30.13  ? 77  GLU   A N   1 
ATOM   561  C  CA  . GLU   A 1 80  ? 0.207   8.522  41.974  1.00 30.54  ? 77  GLU   A CA  1 
ATOM   562  C  C   . GLU   A 1 80  ? -0.123  10.001 41.785  1.00 28.96  ? 77  GLU   A C   1 
ATOM   563  O  O   . GLU   A 1 80  ? -0.969  10.266 40.886  1.00 27.75  ? 77  GLU   A O   1 
ATOM   564  C  CB  . GLU   A 1 80  ? -0.942  7.823  42.694  1.00 34.14  ? 77  GLU   A CB  1 
ATOM   565  C  CG  . GLU   A 1 80  ? -0.771  6.308  42.757  1.00 38.35  ? 77  GLU   A CG  1 
ATOM   566  C  CD  . GLU   A 1 80  ? 0.075   5.778  43.916  1.00 41.52  ? 77  GLU   A CD  1 
ATOM   567  O  OE1 . GLU   A 1 80  ? 0.140   4.532  44.051  1.00 46.72  ? 77  GLU   A OE1 1 
ATOM   568  O  OE2 . GLU   A 1 80  ? 0.695   6.591  44.668  1.00 42.13  ? 77  GLU   A OE2 1 
ATOM   569  N  N   . ASP   A 1 81  ? 0.492   10.917 42.564  1.00 28.08  ? 78  ASP   A N   1 
ATOM   570  C  CA  . ASP   A 1 81  ? 0.300   12.384 42.409  1.00 27.49  ? 78  ASP   A CA  1 
ATOM   571  C  C   . ASP   A 1 81  ? 1.112   12.901 41.215  1.00 25.93  ? 78  ASP   A C   1 
ATOM   572  O  O   . ASP   A 1 81  ? 0.876   14.019 40.816  1.00 25.97  ? 78  ASP   A O   1 
ATOM   573  C  CB  . ASP   A 1 81  ? 0.791   13.171 43.629  1.00 28.71  ? 78  ASP   A CB  1 
ATOM   574  C  CG  . ASP   A 1 81  ? 0.043   12.939 44.938  1.00 31.75  ? 78  ASP   A CG  1 
ATOM   575  O  OD1 . ASP   A 1 81  ? -1.149  12.601 44.858  1.00 34.47  ? 78  ASP   A OD1 1 
ATOM   576  O  OD2 . ASP   A 1 81  ? 0.667   13.144 46.049  1.00 32.72  ? 78  ASP   A OD2 1 
ATOM   577  N  N   . ILE   A 1 82  ? 2.116   12.165 40.749  1.00 24.09  ? 79  ILE   A N   1 
ATOM   578  C  CA  . ILE   A 1 82  ? 3.041   12.630 39.681  1.00 23.44  ? 79  ILE   A CA  1 
ATOM   579  C  C   . ILE   A 1 82  ? 2.545   12.020 38.374  1.00 22.23  ? 79  ILE   A C   1 
ATOM   580  O  O   . ILE   A 1 82  ? 2.124   10.854 38.367  1.00 23.09  ? 79  ILE   A O   1 
ATOM   581  C  CB  . ILE   A 1 82  ? 4.508   12.235 39.968  1.00 23.95  ? 79  ILE   A CB  1 
ATOM   582  C  CG1 . ILE   A 1 82  ? 5.028   12.939 41.215  1.00 24.73  ? 79  ILE   A CG1 1 
ATOM   583  C  CG2 . ILE   A 1 82  ? 5.410   12.478 38.768  1.00 23.11  ? 79  ILE   A CG2 1 
ATOM   584  C  CD1 . ILE   A 1 82  ? 5.171   14.434 41.039  1.00 25.33  ? 79  ILE   A CD1 1 
ATOM   585  N  N   . PHE   A 1 83  ? 2.564   12.818 37.328  1.00 20.82  ? 80  PHE   A N   1 
ATOM   586  C  CA  . PHE   A 1 83  ? 2.203   12.390 35.955  1.00 20.33  ? 80  PHE   A CA  1 
ATOM   587  C  C   . PHE   A 1 83  ? 3.485   12.552 35.142  1.00 19.38  ? 80  PHE   A C   1 
ATOM   588  O  O   . PHE   A 1 83  ? 3.865   13.694 34.818  1.00 18.21  ? 80  PHE   A O   1 
ATOM   589  C  CB  . PHE   A 1 83  ? 1.063   13.233 35.373  1.00 20.74  ? 80  PHE   A CB  1 
ATOM   590  C  CG  . PHE   A 1 83  ? 0.562   12.774 34.031  1.00 19.96  ? 80  PHE   A CG  1 
ATOM   591  C  CD1 . PHE   A 1 83  ? 1.274   13.033 32.875  1.00 19.38  ? 80  PHE   A CD1 1 
ATOM   592  C  CD2 . PHE   A 1 83  ? -0.648  12.103 33.924  1.00 20.75  ? 80  PHE   A CD2 1 
ATOM   593  C  CE1 . PHE   A 1 83  ? 0.798   12.595 31.644  1.00 19.77  ? 80  PHE   A CE1 1 
ATOM   594  C  CE2 . PHE   A 1 83  ? -1.106  11.644 32.699  1.00 20.31  ? 80  PHE   A CE2 1 
ATOM   595  C  CZ  . PHE   A 1 83  ? -0.393  11.919 31.553  1.00 19.82  ? 80  PHE   A CZ  1 
ATOM   596  N  N   . TYR   A 1 84  ? 4.197   11.445 34.965  1.00 19.70  ? 81  TYR   A N   1 
ATOM   597  C  CA  . TYR   A 1 84  ? 5.501   11.419 34.256  1.00 19.60  ? 81  TYR   A CA  1 
ATOM   598  C  C   . TYR   A 1 84  ? 5.307   10.965 32.805  1.00 18.66  ? 81  TYR   A C   1 
ATOM   599  O  O   . TYR   A 1 84  ? 4.792   9.872  32.588  1.00 18.21  ? 81  TYR   A O   1 
ATOM   600  C  CB  . TYR   A 1 84  ? 6.506   10.521 34.989  1.00 21.05  ? 81  TYR   A CB  1 
ATOM   601  C  CG  . TYR   A 1 84  ? 7.854   10.451 34.328  1.00 21.59  ? 81  TYR   A CG  1 
ATOM   602  C  CD1 . TYR   A 1 84  ? 8.751   11.498 34.398  1.00 22.69  ? 81  TYR   A CD1 1 
ATOM   603  C  CD2 . TYR   A 1 84  ? 8.230   9.360  33.566  1.00 23.22  ? 81  TYR   A CD2 1 
ATOM   604  C  CE1 . TYR   A 1 84  ? 9.990   11.441 33.774  1.00 23.20  ? 81  TYR   A CE1 1 
ATOM   605  C  CE2 . TYR   A 1 84  ? 9.437   9.308  32.891  1.00 23.26  ? 81  TYR   A CE2 1 
ATOM   606  C  CZ  . TYR   A 1 84  ? 10.335  10.349 33.006  1.00 23.61  ? 81  TYR   A CZ  1 
ATOM   607  O  OH  . TYR   A 1 84  ? 11.541  10.247 32.375  1.00 24.71  ? 81  TYR   A OH  1 
ATOM   608  N  N   . THR   A 1 85  ? 5.859   11.753 31.883  1.00 18.68  ? 82  THR   A N   1 
ATOM   609  C  CA  . THR   A 1 85  ? 5.836   11.501 30.440  1.00 17.70  ? 82  THR   A CA  1 
ATOM   610  C  C   . THR   A 1 85  ? 7.245   11.147 29.966  1.00 18.08  ? 82  THR   A C   1 
ATOM   611  O  O   . THR   A 1 85  ? 8.217   11.870 30.263  1.00 17.68  ? 82  THR   A O   1 
ATOM   612  C  CB  . THR   A 1 85  ? 5.303   12.706 29.657  1.00 17.63  ? 82  THR   A CB  1 
ATOM   613  O  OG1 . THR   A 1 85  ? 3.952   12.949 30.054  1.00 17.26  ? 82  THR   A OG1 1 
ATOM   614  C  CG2 . THR   A 1 85  ? 5.374   12.444 28.160  1.00 17.47  ? 82  THR   A CG2 1 
ATOM   615  N  N   . SER   A 1 86  ? 7.356   10.042 29.245  1.00 17.59  ? 83  SER   A N   1 
ATOM   616  C  CA  . SER   A 1 86  ? 8.574   9.763  28.444  1.00 18.35  ? 83  SER   A CA  1 
ATOM   617  C  C   . SER   A 1 86  ? 8.165   9.595  26.974  1.00 17.66  ? 83  SER   A C   1 
ATOM   618  O  O   . SER   A 1 86  ? 6.928   9.540  26.686  1.00 17.87  ? 83  SER   A O   1 
ATOM   619  C  CB  . SER   A 1 86  ? 9.406   8.607  28.919  1.00 19.23  ? 83  SER   A CB  1 
ATOM   620  O  OG  . SER   A 1 86  ? 10.660  8.626  28.225  1.00 19.80  ? 83  SER   A OG  1 
ATOM   621  N  N   . LYS   A 1 87  ? 9.167   9.538  26.100  1.00 18.15  ? 84  LYS   A N   1 
ATOM   622  C  CA  . LYS   A 1 87  ? 8.947   9.504  24.626  1.00 18.95  ? 84  LYS   A CA  1 
ATOM   623  C  C   . LYS   A 1 87  ? 9.903   8.498  23.983  1.00 19.88  ? 84  LYS   A C   1 
ATOM   624  O  O   . LYS   A 1 87  ? 11.119  8.452  24.320  1.00 20.19  ? 84  LYS   A O   1 
ATOM   625  C  CB  . LYS   A 1 87  ? 9.048   10.902 23.999  1.00 18.74  ? 84  LYS   A CB  1 
ATOM   626  C  CG  . LYS   A 1 87  ? 8.258   11.983 24.727  1.00 18.36  ? 84  LYS   A CG  1 
ATOM   627  C  CD  . LYS   A 1 87  ? 8.263   13.264 23.941  1.00 19.43  ? 84  LYS   A CD  1 
ATOM   628  C  CE  . LYS   A 1 87  ? 7.610   14.415 24.653  1.00 19.87  ? 84  LYS   A CE  1 
ATOM   629  N  NZ  . LYS   A 1 87  ? 8.553   14.986 25.650  1.00 20.73  ? 84  LYS   A NZ  1 
ATOM   630  N  N   . LEU   A 1 88  ? 9.335   7.712  23.076  1.00 20.24  ? 85  LEU   A N   1 
ATOM   631  C  CA  . LEU   A 1 88  ? 10.045  6.751  22.207  1.00 21.06  ? 85  LEU   A CA  1 
ATOM   632  C  C   . LEU   A 1 88  ? 10.784  7.505  21.092  1.00 20.66  ? 85  LEU   A C   1 
ATOM   633  O  O   . LEU   A 1 88  ? 10.127  8.143  20.261  1.00 20.09  ? 85  LEU   A O   1 
ATOM   634  C  CB  . LEU   A 1 88  ? 8.980   5.845  21.596  1.00 22.07  ? 85  LEU   A CB  1 
ATOM   635  C  CG  . LEU   A 1 88  ? 9.477   4.797  20.613  1.00 23.86  ? 85  LEU   A CG  1 
ATOM   636  C  CD1 . LEU   A 1 88  ? 10.165  3.646  21.353  1.00 24.87  ? 85  LEU   A CD1 1 
ATOM   637  C  CD2 . LEU   A 1 88  ? 8.310   4.288  19.776  1.00 23.56  ? 85  LEU   A CD2 1 
ATOM   638  N  N   . TRP   A 1 89  ? 12.089  7.393  21.036  1.00 21.07  ? 86  TRP   A N   1 
ATOM   639  C  CA  . TRP   A 1 89  ? 12.849  8.171  20.053  1.00 21.86  ? 86  TRP   A CA  1 
ATOM   640  C  C   . TRP   A 1 89  ? 12.778  7.449  18.684  1.00 23.38  ? 86  TRP   A C   1 
ATOM   641  O  O   . TRP   A 1 89  ? 12.448  6.234  18.616  1.00 23.64  ? 86  TRP   A O   1 
ATOM   642  C  CB  . TRP   A 1 89  ? 14.263  8.509  20.565  1.00 22.82  ? 86  TRP   A CB  1 
ATOM   643  C  CG  . TRP   A 1 89  ? 14.985  9.329  19.562  1.00 23.24  ? 86  TRP   A CG  1 
ATOM   644  C  CD1 . TRP   A 1 89  ? 16.141  8.987  18.939  1.00 25.20  ? 86  TRP   A CD1 1 
ATOM   645  C  CD2 . TRP   A 1 89  ? 14.530  10.556 18.957  1.00 23.13  ? 86  TRP   A CD2 1 
ATOM   646  N  NE1 . TRP   A 1 89  ? 16.461  9.927  18.009  1.00 25.95  ? 86  TRP   A NE1 1 
ATOM   647  C  CE2 . TRP   A 1 89  ? 15.476  10.883 17.971  1.00 24.39  ? 86  TRP   A CE2 1 
ATOM   648  C  CE3 . TRP   A 1 89  ? 13.426  11.389 19.152  1.00 21.70  ? 86  TRP   A CE3 1 
ATOM   649  C  CZ2 . TRP   A 1 89  ? 15.324  11.996 17.146  1.00 24.50  ? 86  TRP   A CZ2 1 
ATOM   650  C  CZ3 . TRP   A 1 89  ? 13.265  12.491 18.340  1.00 22.66  ? 86  TRP   A CZ3 1 
ATOM   651  C  CH2 . TRP   A 1 89  ? 14.222  12.797 17.362  1.00 23.60  ? 86  TRP   A CH2 1 
ATOM   652  N  N   . SER   A 1 90  ? 12.984  8.231  17.632  1.00 23.64  ? 87  SER   A N   1 
ATOM   653  C  CA  . SER   A 1 90  ? 12.735  7.908  16.204  1.00 24.96  ? 87  SER   A CA  1 
ATOM   654  C  C   . SER   A 1 90  ? 13.617  6.760  15.693  1.00 26.39  ? 87  SER   A C   1 
ATOM   655  O  O   . SER   A 1 90  ? 13.216  6.164  14.653  1.00 25.94  ? 87  SER   A O   1 
ATOM   656  C  CB  . SER   A 1 90  ? 12.873  9.164  15.415  1.00 25.40  ? 87  SER   A CB  1 
ATOM   657  O  OG  . SER   A 1 90  ? 11.940  10.085 15.941  1.00 25.40  ? 87  SER   A OG  1 
ATOM   658  N  N   . THR   A 1 91  ? 14.698  6.408  16.410  1.00 26.19  ? 88  THR   A N   1 
ATOM   659  C  CA  . THR   A 1 91  ? 15.555  5.219  16.111  1.00 27.64  ? 88  THR   A CA  1 
ATOM   660  C  C   . THR   A 1 91  ? 14.961  3.893  16.611  1.00 27.16  ? 88  THR   A C   1 
ATOM   661  O  O   . THR   A 1 91  ? 15.541  2.848  16.265  1.00 29.30  ? 88  THR   A O   1 
ATOM   662  C  CB  . THR   A 1 91  ? 16.981  5.436  16.615  1.00 28.19  ? 88  THR   A CB  1 
ATOM   663  O  OG1 . THR   A 1 91  ? 16.840  5.699  18.003  1.00 27.41  ? 88  THR   A OG1 1 
ATOM   664  C  CG2 . THR   A 1 91  ? 17.647  6.567  15.855  1.00 28.79  ? 88  THR   A CG2 1 
ATOM   665  N  N   . PHE   A 1 92  ? 13.828  3.936  17.313  1.00 26.25  ? 89  PHE   A N   1 
ATOM   666  C  CA  . PHE   A 1 92  ? 13.185  2.792  18.009  1.00 26.56  ? 89  PHE   A CA  1 
ATOM   667  C  C   . PHE   A 1 92  ? 11.744  2.604  17.541  1.00 26.59  ? 89  PHE   A C   1 
ATOM   668  O  O   . PHE   A 1 92  ? 10.964  1.941  18.247  1.00 26.81  ? 89  PHE   A O   1 
ATOM   669  C  CB  . PHE   A 1 92  ? 13.199  3.015  19.520  1.00 26.22  ? 89  PHE   A CB  1 
ATOM   670  C  CG  . PHE   A 1 92  ? 14.585  3.227  20.071  1.00 27.39  ? 89  PHE   A CG  1 
ATOM   671  C  CD1 . PHE   A 1 92  ? 15.503  2.178  20.118  1.00 30.05  ? 89  PHE   A CD1 1 
ATOM   672  C  CD2 . PHE   A 1 92  ? 14.989  4.470  20.511  1.00 27.06  ? 89  PHE   A CD2 1 
ATOM   673  C  CE1 . PHE   A 1 92  ? 16.800  2.366  20.597  1.00 31.26  ? 89  PHE   A CE1 1 
ATOM   674  C  CE2 . PHE   A 1 92  ? 16.281  4.659  20.994  1.00 28.95  ? 89  PHE   A CE2 1 
ATOM   675  C  CZ  . PHE   A 1 92  ? 17.189  3.609  21.043  1.00 30.56  ? 89  PHE   A CZ  1 
ATOM   676  N  N   . HIS   A 1 93  ? 11.395  3.096  16.347  1.00 26.81  ? 90  HIS   A N   1 
ATOM   677  C  CA  . HIS   A 1 93  ? 10.065  2.872  15.730  1.00 26.74  ? 90  HIS   A CA  1 
ATOM   678  C  C   . HIS   A 1 93  ? 9.870   1.387  15.353  1.00 28.49  ? 90  HIS   A C   1 
ATOM   679  O  O   . HIS   A 1 93  ? 8.695   0.944  15.297  1.00 28.80  ? 90  HIS   A O   1 
ATOM   680  C  CB  . HIS   A 1 93  ? 9.941   3.812  14.528  1.00 26.67  ? 90  HIS   A CB  1 
ATOM   681  C  CG  . HIS   A 1 93  ? 9.639   5.220  14.901  1.00 25.67  ? 90  HIS   A CG  1 
ATOM   682  N  ND1 . HIS   A 1 93  ? 9.285   6.167  13.947  1.00 25.91  ? 90  HIS   A ND1 1 
ATOM   683  C  CD2 . HIS   A 1 93  ? 9.522   5.828  16.111  1.00 25.32  ? 90  HIS   A CD2 1 
ATOM   684  C  CE1 . HIS   A 1 93  ? 9.058   7.314  14.555  1.00 25.70  ? 90  HIS   A CE1 1 
ATOM   685  N  NE2 . HIS   A 1 93  ? 9.180   7.143  15.881  1.00 24.71  ? 90  HIS   A NE2 1 
ATOM   686  N  N   . ARG   A 1 94  ? 10.913  0.659  14.971  1.00 29.90  ? 91  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 94  ? 10.665  -0.755 14.556  1.00 32.91  ? 91  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 94  ? 10.067  -1.472 15.757  1.00 33.03  ? 91  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 94  ? 10.515  -1.234 16.885  1.00 31.12  ? 91  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 94  ? 11.912  -1.459 14.043  1.00 35.90  ? 91  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 94  ? 12.454  -0.813 12.781  1.00 36.80  ? 91  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 94  ? 13.759  -1.446 12.364  1.00 39.72  ? 91  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 94  ? 14.127  -0.825 11.109  1.00 39.98  ? 91  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 94  ? 14.837  -1.400 10.161  1.00 43.47  ? 91  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 94  ? 15.284  -2.637 10.324  1.00 45.36  ? 91  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 94  ? 15.070  -0.753 9.027   1.00 44.37  ? 91  ARG   A NH2 1 
ATOM   697  N  N   . PRO   A 1 95  ? 8.932   -2.182 15.567  1.00 33.39  ? 92  PRO   A N   1 
ATOM   698  C  CA  . PRO   A 1 95  ? 8.076   -2.585 16.678  1.00 32.93  ? 92  PRO   A CA  1 
ATOM   699  C  C   . PRO   A 1 95  ? 8.804   -3.381 17.775  1.00 33.83  ? 92  PRO   A C   1 
ATOM   700  O  O   . PRO   A 1 95  ? 8.428   -3.259 18.924  1.00 32.11  ? 92  PRO   A O   1 
ATOM   701  C  CB  . PRO   A 1 95  ? 6.994   -3.493 16.047  1.00 34.75  ? 92  PRO   A CB  1 
ATOM   702  C  CG  . PRO   A 1 95  ? 7.310   -3.585 14.570  1.00 35.91  ? 92  PRO   A CG  1 
ATOM   703  C  CD  . PRO   A 1 95  ? 8.364   -2.532 14.257  1.00 34.82  ? 92  PRO   A CD  1 
ATOM   704  N  N   . GLU   A 1 96  ? 9.802   -4.185 17.398  1.00 36.11  ? 93  GLU   A N   1 
ATOM   705  C  CA  . GLU   A 1 96  ? 10.523  -5.068 18.355  1.00 37.99  ? 93  GLU   A CA  1 
ATOM   706  C  C   . GLU   A 1 96  ? 11.433  -4.190 19.227  1.00 36.11  ? 93  GLU   A C   1 
ATOM   707  O  O   . GLU   A 1 96  ? 11.933  -4.682 20.237  1.00 36.17  ? 93  GLU   A O   1 
ATOM   708  C  CB  . GLU   A 1 96  ? 11.297  -6.184 17.648  1.00 41.66  ? 93  GLU   A CB  1 
ATOM   709  C  CG  . GLU   A 1 96  ? 12.494  -5.710 16.835  1.00 43.67  ? 93  GLU   A CG  1 
ATOM   710  C  CD  . GLU   A 1 96  ? 12.259  -5.135 15.435  1.00 45.30  ? 93  GLU   A CD  1 
ATOM   711  O  OE1 . GLU   A 1 96  ? 11.061  -5.085 14.930  1.00 44.95  ? 93  GLU   A OE1 1 
ATOM   712  O  OE2 . GLU   A 1 96  ? 13.288  -4.723 14.815  1.00 47.44  ? 93  GLU   A OE2 1 
ATOM   713  N  N   . LEU   A 1 97  ? 11.638  -2.934 18.837  1.00 33.48  ? 94  LEU   A N   1 
ATOM   714  C  CA  . LEU   A 1 97  ? 12.544  -1.993 19.546  1.00 32.37  ? 94  LEU   A CA  1 
ATOM   715  C  C   . LEU   A 1 97  ? 11.776  -1.179 20.595  1.00 30.50  ? 94  LEU   A C   1 
ATOM   716  O  O   . LEU   A 1 97  ? 12.398  -0.602 21.488  1.00 29.19  ? 94  LEU   A O   1 
ATOM   717  C  CB  . LEU   A 1 97  ? 13.194  -1.071 18.504  1.00 31.56  ? 94  LEU   A CB  1 
ATOM   718  C  CG  . LEU   A 1 97  ? 14.148  -1.763 17.538  1.00 33.15  ? 94  LEU   A CG  1 
ATOM   719  C  CD1 . LEU   A 1 97  ? 14.917  -0.768 16.683  1.00 32.19  ? 94  LEU   A CD1 1 
ATOM   720  C  CD2 . LEU   A 1 97  ? 15.125  -2.672 18.287  1.00 34.76  ? 94  LEU   A CD2 1 
ATOM   721  N  N   . VAL   A 1 98  ? 10.452  -1.189 20.532  1.00 29.76  ? 95  VAL   A N   1 
ATOM   722  C  CA  . VAL   A 1 98  ? 9.633   -0.223 21.308  1.00 28.07  ? 95  VAL   A CA  1 
ATOM   723  C  C   . VAL   A 1 98  ? 9.661   -0.579 22.795  1.00 28.70  ? 95  VAL   A C   1 
ATOM   724  O  O   . VAL   A 1 98  ? 9.984   0.292  23.623  1.00 26.96  ? 95  VAL   A O   1 
ATOM   725  C  CB  . VAL   A 1 98  ? 8.204   -0.159 20.754  1.00 27.30  ? 95  VAL   A CB  1 
ATOM   726  C  CG1 . VAL   A 1 98  ? 7.280   0.573  21.699  1.00 26.00  ? 95  VAL   A CG1 1 
ATOM   727  C  CG2 . VAL   A 1 98  ? 8.182   0.507  19.388  1.00 26.69  ? 95  VAL   A CG2 1 
ATOM   728  N  N   . ARG   A 1 99  ? 9.342   -1.815 23.150  1.00 30.34  ? 96  ARG   A N   1 
ATOM   729  C  CA  . ARG   A 1 99  ? 9.224   -2.147 24.582  1.00 32.18  ? 96  ARG   A CA  1 
ATOM   730  C  C   . ARG   A 1 99  ? 10.596  -2.069 25.255  1.00 32.11  ? 96  ARG   A C   1 
ATOM   731  O  O   . ARG   A 1 99  ? 10.699  -1.500 26.349  1.00 31.35  ? 96  ARG   A O   1 
ATOM   732  C  CB  . ARG   A 1 99  ? 8.528   -3.482 24.786  1.00 35.44  ? 96  ARG   A CB  1 
ATOM   733  C  CG  . ARG   A 1 99  ? 8.520   -3.849 26.248  1.00 37.05  ? 96  ARG   A CG  1 
ATOM   734  C  CD  . ARG   A 1 99  ? 7.618   -5.009 26.505  1.00 40.62  ? 96  ARG   A CD  1 
ATOM   735  N  NE  . ARG   A 1 99  ? 7.897   -5.415 27.876  1.00 43.15  ? 96  ARG   A NE  1 
ATOM   736  C  CZ  . ARG   A 1 99  ? 7.151   -6.264 28.546  1.00 45.72  ? 96  ARG   A CZ  1 
ATOM   737  N  NH1 . ARG   A 1 99  ? 6.105   -6.808 27.937  1.00 45.87  ? 96  ARG   A NH1 1 
ATOM   738  N  NH2 . ARG   A 1 99  ? 7.455   -6.549 29.801  1.00 46.49  ? 96  ARG   A NH2 1 
ATOM   739  N  N   . PRO   A 1 100 ? 11.699  -2.574 24.649  1.00 33.87  ? 97  PRO   A N   1 
ATOM   740  C  CA  . PRO   A 1 100 ? 13.014  -2.422 25.274  1.00 33.49  ? 97  PRO   A CA  1 
ATOM   741  C  C   . PRO   A 1 100 ? 13.404  -0.944 25.440  1.00 31.02  ? 97  PRO   A C   1 
ATOM   742  O  O   . PRO   A 1 100 ? 14.051  -0.580 26.467  1.00 29.16  ? 97  PRO   A O   1 
ATOM   743  C  CB  . PRO   A 1 100 ? 13.966  -3.182 24.350  1.00 35.77  ? 97  PRO   A CB  1 
ATOM   744  C  CG  . PRO   A 1 100 ? 13.070  -4.161 23.606  1.00 37.20  ? 97  PRO   A CG  1 
ATOM   745  C  CD  . PRO   A 1 100 ? 11.757  -3.424 23.435  1.00 35.57  ? 97  PRO   A CD  1 
ATOM   746  N  N   . ALA   A 1 101 ? 12.919  -0.076 24.544  1.00 28.82  ? 98  ALA   A N   1 
ATOM   747  C  CA  . ALA   A 1 101 ? 13.179  1.382  24.654  1.00 27.37  ? 98  ALA   A CA  1 
ATOM   748  C  C   . ALA   A 1 101 ? 12.455  1.897  25.902  1.00 26.54  ? 98  ALA   A C   1 
ATOM   749  O  O   . ALA   A 1 101 ? 13.072  2.630  26.675  1.00 25.64  ? 98  ALA   A O   1 
ATOM   750  C  CB  . ALA   A 1 101 ? 12.810  2.129  23.398  1.00 26.30  ? 98  ALA   A CB  1 
ATOM   751  N  N   . LEU   A 1 102 ? 11.208  1.487  26.132  1.00 26.60  ? 99  LEU   A N   1 
ATOM   752  C  CA  . LEU   A 1 102 ? 10.469  1.942  27.336  1.00 26.35  ? 99  LEU   A CA  1 
ATOM   753  C  C   . LEU   A 1 102 ? 11.142  1.372  28.596  1.00 27.68  ? 99  LEU   A C   1 
ATOM   754  O  O   . LEU   A 1 102 ? 11.374  2.117  29.522  1.00 26.88  ? 99  LEU   A O   1 
ATOM   755  C  CB  . LEU   A 1 102 ? 9.004   1.516  27.217  1.00 26.23  ? 99  LEU   A CB  1 
ATOM   756  C  CG  . LEU   A 1 102 ? 8.100   1.786  28.428  1.00 25.34  ? 99  LEU   A CG  1 
ATOM   757  C  CD1 . LEU   A 1 102 ? 8.126   3.243  28.877  1.00 23.63  ? 99  LEU   A CD1 1 
ATOM   758  C  CD2 . LEU   A 1 102 ? 6.660   1.390  28.090  1.00 25.98  ? 99  LEU   A CD2 1 
ATOM   759  N  N   . GLU   A 1 103 ? 11.514  0.103  28.597  1.00 29.70  ? 100 GLU   A N   1 
ATOM   760  C  CA  . GLU   A 1 103 ? 12.146  -0.541 29.761  1.00 32.43  ? 100 GLU   A CA  1 
ATOM   761  C  C   . GLU   A 1 103 ? 13.459  0.191  30.081  1.00 31.90  ? 100 GLU   A C   1 
ATOM   762  O  O   . GLU   A 1 103 ? 13.750  0.353  31.285  1.00 31.39  ? 100 GLU   A O   1 
ATOM   763  C  CB  . GLU   A 1 103 ? 12.296  -2.053 29.525  1.00 35.59  ? 100 GLU   A CB  1 
ATOM   764  C  CG  . GLU   A 1 103 ? 10.975  -2.813 29.606  1.00 37.76  ? 100 GLU   A CG  1 
ATOM   765  C  CD  . GLU   A 1 103 ? 10.986  -4.296 29.256  1.00 41.60  ? 100 GLU   A CD  1 
ATOM   766  O  OE1 . GLU   A 1 103 ? 11.904  -4.741 28.530  1.00 44.82  ? 100 GLU   A OE1 1 
ATOM   767  O  OE2 . GLU   A 1 103 ? 10.046  -5.006 29.673  1.00 44.33  ? 100 GLU   A OE2 1 
ATOM   768  N  N   . ASN   A 1 104 ? 14.182  0.671  29.054  1.00 32.61  ? 101 ASN   A N   1 
ATOM   769  C  CA  . ASN   A 1 104 ? 15.468  1.410  29.200  1.00 33.37  ? 101 ASN   A CA  1 
ATOM   770  C  C   . ASN   A 1 104 ? 15.158  2.743  29.863  1.00 31.10  ? 101 ASN   A C   1 
ATOM   771  O  O   . ASN   A 1 104 ? 15.807  3.078  30.859  1.00 30.05  ? 101 ASN   A O   1 
ATOM   772  C  CB  . ASN   A 1 104 ? 16.227  1.562  27.884  1.00 36.34  ? 101 ASN   A CB  1 
ATOM   773  C  CG  . ASN   A 1 104 ? 17.523  2.328  28.043  1.00 40.16  ? 101 ASN   A CG  1 
ATOM   774  O  OD1 . ASN   A 1 104 ? 17.612  3.522  27.762  1.00 45.46  ? 101 ASN   A OD1 1 
ATOM   775  N  ND2 . ASN   A 1 104 ? 18.531  1.674  28.564  1.00 42.55  ? 101 ASN   A ND2 1 
ATOM   776  N  N   . SER   A 1 105 ? 14.108  3.434  29.438  1.00 29.24  ? 102 SER   A N   1 
ATOM   777  C  CA  . SER   A 1 105 ? 13.747  4.715  30.091  1.00 27.85  ? 102 SER   A CA  1 
ATOM   778  C  C   . SER   A 1 105 ? 13.354  4.453  31.557  1.00 27.32  ? 102 SER   A C   1 
ATOM   779  O  O   . SER   A 1 105 ? 13.727  5.265  32.412  1.00 26.36  ? 102 SER   A O   1 
ATOM   780  C  CB  . SER   A 1 105 ? 12.668  5.446  29.346  1.00 27.01  ? 102 SER   A CB  1 
ATOM   781  O  OG  . SER   A 1 105 ? 13.201  6.084  28.193  1.00 29.31  ? 102 SER   A OG  1 
ATOM   782  N  N   . LEU   A 1 106 ? 12.550  3.426  31.828  1.00 27.25  ? 103 LEU   A N   1 
ATOM   783  C  CA  . LEU   A 1 106 ? 12.098  3.131  33.210  1.00 27.81  ? 103 LEU   A CA  1 
ATOM   784  C  C   . LEU   A 1 106 ? 13.323  2.809  34.074  1.00 30.03  ? 103 LEU   A C   1 
ATOM   785  O  O   . LEU   A 1 106 ? 13.354  3.249  35.198  1.00 29.73  ? 103 LEU   A O   1 
ATOM   786  C  CB  . LEU   A 1 106 ? 11.080  1.986  33.189  1.00 27.94  ? 103 LEU   A CB  1 
ATOM   787  C  CG  . LEU   A 1 106 ? 9.745   2.335  32.548  1.00 26.75  ? 103 LEU   A CG  1 
ATOM   788  C  CD1 . LEU   A 1 106 ? 8.883   1.103  32.319  1.00 27.74  ? 103 LEU   A CD1 1 
ATOM   789  C  CD2 . LEU   A 1 106 ? 9.003   3.413  33.352  1.00 25.74  ? 103 LEU   A CD2 1 
ATOM   790  N  N   . LYS   A 1 107 ? 14.286  2.063  33.545  1.00 31.74  ? 104 LYS   A N   1 
ATOM   791  C  CA  . LYS   A 1 107 ? 15.526  1.743  34.280  1.00 34.75  ? 104 LYS   A CA  1 
ATOM   792  C  C   . LYS   A 1 107 ? 16.286  3.043  34.598  1.00 33.72  ? 104 LYS   A C   1 
ATOM   793  O  O   . LYS   A 1 107 ? 16.750  3.186  35.747  1.00 32.18  ? 104 LYS   A O   1 
ATOM   794  C  CB  . LYS   A 1 107 ? 16.402  0.790  33.466  1.00 37.36  ? 104 LYS   A CB  1 
ATOM   795  C  CG  . LYS   A 1 107 ? 17.553  0.214  34.292  1.00 40.85  ? 104 LYS   A CG  1 
ATOM   796  C  CD  . LYS   A 1 107 ? 18.652  -0.476 33.504  1.00 44.89  ? 104 LYS   A CD  1 
ATOM   797  C  CE  . LYS   A 1 107 ? 18.808  -1.963 33.755  1.00 49.86  ? 104 LYS   A CE  1 
ATOM   798  N  NZ  . LYS   A 1 107 ? 19.043  -2.299 35.187  1.00 53.22  ? 104 LYS   A NZ  1 
ATOM   799  N  N   . LYS   A 1 108 ? 16.436  3.962  33.629  1.00 33.06  ? 105 LYS   A N   1 
ATOM   800  C  CA  . LYS   A 1 108 ? 17.229  5.207  33.833  1.00 32.63  ? 105 LYS   A CA  1 
ATOM   801  C  C   . LYS   A 1 108 ? 16.516  6.078  34.858  1.00 30.06  ? 105 LYS   A C   1 
ATOM   802  O  O   . LYS   A 1 108 ? 17.181  6.586  35.745  1.00 28.74  ? 105 LYS   A O   1 
ATOM   803  C  CB  . LYS   A 1 108 ? 17.406  6.074  32.579  1.00 34.36  ? 105 LYS   A CB  1 
ATOM   804  C  CG  . LYS   A 1 108 ? 18.149  5.444  31.409  1.00 38.58  ? 105 LYS   A CG  1 
ATOM   805  C  CD  . LYS   A 1 108 ? 19.367  4.626  31.775  1.00 43.98  ? 105 LYS   A CD  1 
ATOM   806  C  CE  . LYS   A 1 108 ? 20.425  4.550  30.690  1.00 47.77  ? 105 LYS   A CE  1 
ATOM   807  N  NZ  . LYS   A 1 108 ? 21.557  5.456  30.997  1.00 50.29  ? 105 LYS   A NZ  1 
ATOM   808  N  N   . ALA   A 1 109 ? 15.197  6.199  34.753  1.00 27.86  ? 106 ALA   A N   1 
ATOM   809  C  CA  . ALA   A 1 109 ? 14.387  7.062  35.644  1.00 27.37  ? 106 ALA   A CA  1 
ATOM   810  C  C   . ALA   A 1 109 ? 14.135  6.359  36.986  1.00 28.37  ? 106 ALA   A C   1 
ATOM   811  O  O   . ALA   A 1 109 ? 13.652  7.022  37.905  1.00 27.79  ? 106 ALA   A O   1 
ATOM   812  C  CB  . ALA   A 1 109 ? 13.071  7.419  35.019  1.00 25.54  ? 106 ALA   A CB  1 
ATOM   813  N  N   . GLN   A 1 110 ? 14.386  5.051  37.066  1.00 29.34  ? 107 GLN   A N   1 
ATOM   814  C  CA  . GLN   A 1 110 ? 14.033  4.216  38.229  1.00 31.96  ? 107 GLN   A CA  1 
ATOM   815  C  C   . GLN   A 1 110 ? 12.570  4.463  38.638  1.00 30.15  ? 107 GLN   A C   1 
ATOM   816  O  O   . GLN   A 1 110 ? 12.288  4.593  39.859  1.00 29.12  ? 107 GLN   A O   1 
ATOM   817  C  CB  . GLN   A 1 110 ? 15.045  4.405  39.374  1.00 35.42  ? 107 GLN   A CB  1 
ATOM   818  C  CG  . GLN   A 1 110 ? 16.341  3.650  39.126  1.00 39.55  ? 107 GLN   A CG  1 
ATOM   819  C  CD  . GLN   A 1 110 ? 16.085  2.161  39.029  1.00 41.37  ? 107 GLN   A CD  1 
ATOM   820  O  OE1 . GLN   A 1 110 ? 15.613  1.553  39.991  1.00 45.16  ? 107 GLN   A OE1 1 
ATOM   821  N  NE2 . GLN   A 1 110 ? 16.415  1.537  37.904  1.00 40.58  ? 107 GLN   A NE2 1 
ATOM   822  N  N   . LEU   A 1 111 ? 11.652  4.355  37.681  1.00 28.26  ? 108 LEU   A N   1 
ATOM   823  C  CA  . LEU   A 1 111 ? 10.201  4.289  37.912  1.00 28.66  ? 108 LEU   A CA  1 
ATOM   824  C  C   . LEU   A 1 111 ? 9.722   2.928  37.423  1.00 29.52  ? 108 LEU   A C   1 
ATOM   825  O  O   . LEU   A 1 111 ? 10.396  2.370  36.551  1.00 29.96  ? 108 LEU   A O   1 
ATOM   826  C  CB  . LEU   A 1 111 ? 9.553   5.412  37.104  1.00 28.06  ? 108 LEU   A CB  1 
ATOM   827  C  CG  . LEU   A 1 111 ? 9.935   6.816  37.575  1.00 28.78  ? 108 LEU   A CG  1 
ATOM   828  C  CD1 . LEU   A 1 111 ? 9.490   7.846  36.569  1.00 27.74  ? 108 LEU   A CD1 1 
ATOM   829  C  CD2 . LEU   A 1 111 ? 9.361   7.077  38.964  1.00 30.01  ? 108 LEU   A CD2 1 
ATOM   830  N  N   . ASP   A 1 112 ? 8.594   2.452  37.936  1.00 29.90  ? 109 ASP   A N   1 
ATOM   831  C  CA  . ASP   A 1 112 ? 8.007   1.154  37.515  1.00 32.36  ? 109 ASP   A CA  1 
ATOM   832  C  C   . ASP   A 1 112 ? 7.161   1.345  36.245  1.00 31.20  ? 109 ASP   A C   1 
ATOM   833  O  O   . ASP   A 1 112 ? 6.965   0.368  35.497  1.00 32.15  ? 109 ASP   A O   1 
ATOM   834  C  CB  . ASP   A 1 112 ? 7.202   0.584  38.679  1.00 34.61  ? 109 ASP   A CB  1 
ATOM   835  C  CG  . ASP   A 1 112 ? 8.079   0.266  39.875  1.00 37.18  ? 109 ASP   A CG  1 
ATOM   836  O  OD1 . ASP   A 1 112 ? 9.153   -0.301 39.666  1.00 38.23  ? 109 ASP   A OD1 1 
ATOM   837  O  OD2 . ASP   A 1 112 ? 7.721   0.653  40.989  1.00 39.86  ? 109 ASP   A OD2 1 
ATOM   838  N  N   . TYR   A 1 113 ? 6.644   2.542  36.014  1.00 29.00  ? 110 TYR   A N   1 
ATOM   839  C  CA  . TYR   A 1 113 ? 5.724   2.805  34.883  1.00 28.74  ? 110 TYR   A CA  1 
ATOM   840  C  C   . TYR   A 1 113 ? 5.905   4.274  34.546  1.00 26.97  ? 110 TYR   A C   1 
ATOM   841  O  O   . TYR   A 1 113 ? 6.380   5.013  35.385  1.00 26.88  ? 110 TYR   A O   1 
ATOM   842  C  CB  . TYR   A 1 113 ? 4.280   2.413  35.225  1.00 29.87  ? 110 TYR   A CB  1 
ATOM   843  C  CG  . TYR   A 1 113 ? 3.646   3.260  36.304  1.00 30.09  ? 110 TYR   A CG  1 
ATOM   844  C  CD1 . TYR   A 1 113 ? 2.999   4.452  36.002  1.00 29.01  ? 110 TYR   A CD1 1 
ATOM   845  C  CD2 . TYR   A 1 113 ? 3.671   2.860  37.638  1.00 32.47  ? 110 TYR   A CD2 1 
ATOM   846  C  CE1 . TYR   A 1 113 ? 2.439   5.251  36.994  1.00 30.06  ? 110 TYR   A CE1 1 
ATOM   847  C  CE2 . TYR   A 1 113 ? 3.117   3.649  38.642  1.00 32.29  ? 110 TYR   A CE2 1 
ATOM   848  C  CZ  . TYR   A 1 113 ? 2.525   4.862  38.329  1.00 30.92  ? 110 TYR   A CZ  1 
ATOM   849  O  OH  . TYR   A 1 113 ? 2.005   5.647  39.325  1.00 32.05  ? 110 TYR   A OH  1 
ATOM   850  N  N   . VAL   A 1 114 ? 5.587   4.665  33.324  1.00 24.95  ? 111 VAL   A N   1 
ATOM   851  C  CA  . VAL   A 1 114 ? 5.385   6.103  33.012  1.00 23.17  ? 111 VAL   A CA  1 
ATOM   852  C  C   . VAL   A 1 114 ? 3.870   6.328  32.941  1.00 23.42  ? 111 VAL   A C   1 
ATOM   853  O  O   . VAL   A 1 114 ? 3.117   5.391  32.593  1.00 23.79  ? 111 VAL   A O   1 
ATOM   854  C  CB  . VAL   A 1 114 ? 6.074   6.492  31.696  1.00 22.19  ? 111 VAL   A CB  1 
ATOM   855  C  CG1 . VAL   A 1 114 ? 7.557   6.150  31.726  1.00 22.24  ? 111 VAL   A CG1 1 
ATOM   856  C  CG2 . VAL   A 1 114 ? 5.406   5.816  30.515  1.00 22.31  ? 111 VAL   A CG2 1 
ATOM   857  N  N   . ASP   A 1 115 ? 3.422   7.528  33.275  1.00 22.34  ? 112 ASP   A N   1 
ATOM   858  C  CA  . ASP   A 1 115 ? 1.985   7.846  33.131  1.00 22.11  ? 112 ASP   A CA  1 
ATOM   859  C  C   . ASP   A 1 115 ? 1.658   7.946  31.639  1.00 21.41  ? 112 ASP   A C   1 
ATOM   860  O  O   . ASP   A 1 115 ? 0.497   7.736  31.274  1.00 21.73  ? 112 ASP   A O   1 
ATOM   861  C  CB  . ASP   A 1 115 ? 1.676   9.093  33.928  1.00 21.99  ? 112 ASP   A CB  1 
ATOM   862  C  CG  . ASP   A 1 115 ? 1.922   8.833  35.403  1.00 22.96  ? 112 ASP   A CG  1 
ATOM   863  O  OD1 . ASP   A 1 115 ? 3.087   9.010  35.876  1.00 22.05  ? 112 ASP   A OD1 1 
ATOM   864  O  OD2 . ASP   A 1 115 ? 0.989   8.322  36.032  1.00 24.54  ? 112 ASP   A OD2 1 
ATOM   865  N  N   . LEU   A 1 116 ? 2.629   8.368  30.843  1.00 20.62  ? 113 LEU   A N   1 
ATOM   866  C  CA  . LEU   A 1 116 ? 2.376   8.650  29.409  1.00 20.13  ? 113 LEU   A CA  1 
ATOM   867  C  C   . LEU   A 1 116 ? 3.624   8.304  28.620  1.00 19.80  ? 113 LEU   A C   1 
ATOM   868  O  O   . LEU   A 1 116 ? 4.728   8.704  29.013  1.00 20.65  ? 113 LEU   A O   1 
ATOM   869  C  CB  . LEU   A 1 116 ? 1.987   10.115 29.236  1.00 19.31  ? 113 LEU   A CB  1 
ATOM   870  C  CG  . LEU   A 1 116 ? 1.637   10.540 27.804  1.00 18.54  ? 113 LEU   A CG  1 
ATOM   871  C  CD1 . LEU   A 1 116 ? 0.472   9.751  27.219  1.00 19.50  ? 113 LEU   A CD1 1 
ATOM   872  C  CD2 . LEU   A 1 116 ? 1.339   12.040 27.762  1.00 18.46  ? 113 LEU   A CD2 1 
ATOM   873  N  N   . TYR   A 1 117 ? 3.439   7.534  27.558  1.00 20.23  ? 114 TYR   A N   1 
ATOM   874  C  CA  . TYR   A 1 117 ? 4.519   7.245  26.598  1.00 20.08  ? 114 TYR   A CA  1 
ATOM   875  C  C   . TYR   A 1 117 ? 4.076   7.734  25.222  1.00 19.45  ? 114 TYR   A C   1 
ATOM   876  O  O   . TYR   A 1 117 ? 2.971   7.359  24.768  1.00 18.66  ? 114 TYR   A O   1 
ATOM   877  C  CB  . TYR   A 1 117 ? 4.865   5.756  26.531  1.00 21.26  ? 114 TYR   A CB  1 
ATOM   878  C  CG  . TYR   A 1 117 ? 6.262   5.451  26.037  1.00 21.33  ? 114 TYR   A CG  1 
ATOM   879  C  CD1 . TYR   A 1 117 ? 7.360   6.159  26.494  1.00 20.69  ? 114 TYR   A CD1 1 
ATOM   880  C  CD2 . TYR   A 1 117 ? 6.513   4.406  25.154  1.00 21.80  ? 114 TYR   A CD2 1 
ATOM   881  C  CE1 . TYR   A 1 117 ? 8.652   5.872  26.082  1.00 21.13  ? 114 TYR   A CE1 1 
ATOM   882  C  CE2 . TYR   A 1 117 ? 7.796   4.095  24.730  1.00 22.16  ? 114 TYR   A CE2 1 
ATOM   883  C  CZ  . TYR   A 1 117 ? 8.879   4.785  25.255  1.00 22.23  ? 114 TYR   A CZ  1 
ATOM   884  O  OH  . TYR   A 1 117 ? 10.135  4.498  24.831  1.00 23.72  ? 114 TYR   A OH  1 
ATOM   885  N  N   . LEU   A 1 118 ? 4.916   8.564  24.600  1.00 18.99  ? 115 LEU   A N   1 
ATOM   886  C  CA  . LEU   A 1 118 ? 4.644   9.098  23.251  1.00 18.79  ? 115 LEU   A CA  1 
ATOM   887  C  C   . LEU   A 1 118 ? 5.565   8.533  22.196  1.00 18.99  ? 115 LEU   A C   1 
ATOM   888  O  O   . LEU   A 1 118 ? 6.723   8.378  22.441  1.00 18.98  ? 115 LEU   A O   1 
ATOM   889  C  CB  . LEU   A 1 118 ? 4.839   10.609 23.280  1.00 18.45  ? 115 LEU   A CB  1 
ATOM   890  C  CG  . LEU   A 1 118 ? 4.048   11.358 24.338  1.00 17.88  ? 115 LEU   A CG  1 
ATOM   891  C  CD1 . LEU   A 1 118 ? 4.266   12.826 24.149  1.00 17.78  ? 115 LEU   A CD1 1 
ATOM   892  C  CD2 . LEU   A 1 118 ? 2.557   11.026 24.309  1.00 17.87  ? 115 LEU   A CD2 1 
ATOM   893  N  N   . ILE   A 1 119 ? 5.050   8.394  20.982  1.00 19.34  ? 116 ILE   A N   1 
ATOM   894  C  CA  . ILE   A 1 119 ? 5.907   8.419  19.775  1.00 19.63  ? 116 ILE   A CA  1 
ATOM   895  C  C   . ILE   A 1 119 ? 6.392   9.866  19.657  1.00 18.79  ? 116 ILE   A C   1 
ATOM   896  O  O   . ILE   A 1 119 ? 5.551   10.758 19.424  1.00 18.82  ? 116 ILE   A O   1 
ATOM   897  C  CB  . ILE   A 1 119 ? 5.105   7.931  18.540  1.00 21.07  ? 116 ILE   A CB  1 
ATOM   898  C  CG1 . ILE   A 1 119 ? 4.573   6.513  18.761  1.00 22.60  ? 116 ILE   A CG1 1 
ATOM   899  C  CG2 . ILE   A 1 119 ? 5.963   8.056  17.303  1.00 21.63  ? 116 ILE   A CG2 1 
ATOM   900  C  CD1 . ILE   A 1 119 ? 3.915   5.884  17.528  1.00 23.98  ? 116 ILE   A CD1 1 
ATOM   901  N  N   . HIS   A 1 120 ? 7.689   10.111 19.833  1.00 18.19  ? 117 HIS   A N   1 
ATOM   902  C  CA  . HIS   A 1 120 ? 8.286   11.460 19.906  1.00 18.34  ? 117 HIS   A CA  1 
ATOM   903  C  C   . HIS   A 1 120 ? 8.051   12.192 18.574  1.00 18.13  ? 117 HIS   A C   1 
ATOM   904  O  O   . HIS   A 1 120 ? 7.854   13.475 18.569  1.00 16.91  ? 117 HIS   A O   1 
ATOM   905  C  CB  . HIS   A 1 120 ? 9.783   11.366 20.277  1.00 19.03  ? 117 HIS   A CB  1 
ATOM   906  C  CG  . HIS   A 1 120 ? 10.302  12.612 20.934  1.00 18.88  ? 117 HIS   A CG  1 
ATOM   907  N  ND1 . HIS   A 1 120 ? 11.358  12.583 21.797  1.00 19.90  ? 117 HIS   A ND1 1 
ATOM   908  C  CD2 . HIS   A 1 120 ? 9.942   13.916 20.797  1.00 18.28  ? 117 HIS   A CD2 1 
ATOM   909  C  CE1 . HIS   A 1 120 ? 11.597  13.801 22.212  1.00 19.20  ? 117 HIS   A CE1 1 
ATOM   910  N  NE2 . HIS   A 1 120 ? 10.734  14.653 21.629  1.00 18.04  ? 117 HIS   A NE2 1 
ATOM   911  N  N   . SER   A 1 121 ? 8.088   11.456 17.463  1.00 18.71  ? 118 SER   A N   1 
ATOM   912  C  CA  . SER   A 1 121 ? 8.066   12.089 16.126  1.00 19.42  ? 118 SER   A CA  1 
ATOM   913  C  C   . SER   A 1 121 ? 7.674   11.045 15.100  1.00 20.48  ? 118 SER   A C   1 
ATOM   914  O  O   . SER   A 1 121 ? 8.080   9.905  15.247  1.00 21.14  ? 118 SER   A O   1 
ATOM   915  C  CB  . SER   A 1 121 ? 9.418   12.602 15.814  1.00 19.93  ? 118 SER   A CB  1 
ATOM   916  O  OG  . SER   A 1 121 ? 9.583   12.861 14.443  1.00 20.92  ? 118 SER   A OG  1 
ATOM   917  N  N   . PRO   A 1 122 ? 6.920   11.409 14.043  1.00 21.05  ? 119 PRO   A N   1 
ATOM   918  C  CA  . PRO   A 1 122 ? 6.596   10.432 13.012  1.00 21.74  ? 119 PRO   A CA  1 
ATOM   919  C  C   . PRO   A 1 122 ? 7.757   10.131 12.049  1.00 23.53  ? 119 PRO   A C   1 
ATOM   920  O  O   . PRO   A 1 122 ? 7.651   9.163  11.269  1.00 24.43  ? 119 PRO   A O   1 
ATOM   921  C  CB  . PRO   A 1 122 ? 5.406   11.098 12.309  1.00 21.62  ? 119 PRO   A CB  1 
ATOM   922  C  CG  . PRO   A 1 122 ? 5.647   12.564 12.429  1.00 20.91  ? 119 PRO   A CG  1 
ATOM   923  C  CD  . PRO   A 1 122 ? 6.335   12.746 13.764  1.00 20.42  ? 119 PRO   A CD  1 
ATOM   924  N  N   . MET   A 1 123 ? 8.851   10.884 12.163  1.00 23.54  ? 120 MET   A N   1 
ATOM   925  C  CA  . MET   A 1 123 ? 9.983   10.867 11.211  1.00 24.79  ? 120 MET   A CA  1 
ATOM   926  C  C   . MET   A 1 123 ? 10.983  9.796  11.630  1.00 25.00  ? 120 MET   A C   1 
ATOM   927  O  O   . MET   A 1 123 ? 11.988  10.169 12.235  1.00 25.31  ? 120 MET   A O   1 
ATOM   928  C  CB  . MET   A 1 123 ? 10.628  12.256 11.164  1.00 25.37  ? 120 MET   A CB  1 
ATOM   929  C  CG  . MET   A 1 123 ? 9.689   13.236 10.507  1.00 26.15  ? 120 MET   A CG  1 
ATOM   930  S  SD  . MET   A 1 123 ? 10.304  14.894 10.328  1.00 26.63  ? 120 MET   A SD  1 
ATOM   931  C  CE  . MET   A 1 123 ? 10.361  15.508 12.006  1.00 27.49  ? 120 MET   A CE  1 
ATOM   932  N  N   . SER   A 1 124 ? 10.672  8.524  11.350  1.00 24.95  ? 121 SER   A N   1 
ATOM   933  C  CA  . SER   A 1 124 ? 11.525  7.341  11.631  1.00 26.07  ? 121 SER   A CA  1 
ATOM   934  C  C   . SER   A 1 124 ? 12.976  7.561  11.169  1.00 27.66  ? 121 SER   A C   1 
ATOM   935  O  O   . SER   A 1 124 ? 13.182  7.997  10.012  1.00 29.14  ? 121 SER   A O   1 
ATOM   936  C  CB  . SER   A 1 124 ? 10.952  6.142  10.969  1.00 26.57  ? 121 SER   A CB  1 
ATOM   937  O  OG  . SER   A 1 124 ? 9.579   6.018  11.291  1.00 26.32  ? 121 SER   A OG  1 
ATOM   938  N  N   . LEU   A 1 125 ? 13.945  7.151  12.000  1.00 28.23  ? 122 LEU   A N   1 
ATOM   939  C  CA  . LEU   A 1 125 ? 15.389  7.166  11.663  1.00 29.68  ? 122 LEU   A CA  1 
ATOM   940  C  C   . LEU   A 1 125 ? 15.953  5.744  11.777  1.00 31.58  ? 122 LEU   A C   1 
ATOM   941  O  O   . LEU   A 1 125 ? 15.395  4.885  12.496  1.00 30.96  ? 122 LEU   A O   1 
ATOM   942  C  CB  . LEU   A 1 125 ? 16.137  8.121  12.601  1.00 28.75  ? 122 LEU   A CB  1 
ATOM   943  C  CG  . LEU   A 1 125 ? 15.587  9.537  12.706  1.00 28.37  ? 122 LEU   A CG  1 
ATOM   944  C  CD1 . LEU   A 1 125 ? 16.382  10.361 13.689  1.00 28.86  ? 122 LEU   A CD1 1 
ATOM   945  C  CD2 . LEU   A 1 125 ? 15.554  10.254 11.380  1.00 28.94  ? 122 LEU   A CD2 1 
ATOM   946  N  N   . LYS   A 1 126 ? 17.034  5.527  11.057  1.00 35.06  ? 123 LYS   A N   1 
ATOM   947  C  CA  . LYS   A 1 126 ? 17.738  4.224  10.983  1.00 39.20  ? 123 LYS   A CA  1 
ATOM   948  C  C   . LYS   A 1 126 ? 18.102  3.787  12.390  1.00 38.75  ? 123 LYS   A C   1 
ATOM   949  O  O   . LYS   A 1 126 ? 18.654  4.585  13.123  1.00 38.16  ? 123 LYS   A O   1 
ATOM   950  C  CB  . LYS   A 1 126 ? 18.988  4.393  10.109  1.00 42.91  ? 123 LYS   A CB  1 
ATOM   951  C  CG  . LYS   A 1 126 ? 19.878  3.161  9.983   1.00 46.72  ? 123 LYS   A CG  1 
ATOM   952  C  CD  . LYS   A 1 126 ? 20.956  3.318  8.930   1.00 49.95  ? 123 LYS   A CD  1 
ATOM   953  C  CE  . LYS   A 1 126 ? 21.900  2.142  8.842   1.00 53.53  ? 123 LYS   A CE  1 
ATOM   954  N  NZ  . LYS   A 1 126 ? 23.056  2.289  9.761   1.00 55.58  ? 123 LYS   A NZ  1 
ATOM   955  N  N   . PRO   A 1 127 ? 17.899  2.516  12.777  1.00 41.95  ? 124 PRO   A N   1 
ATOM   956  C  CA  . PRO   A 1 127 ? 18.322  2.050  14.089  1.00 44.15  ? 124 PRO   A CA  1 
ATOM   957  C  C   . PRO   A 1 127 ? 19.856  2.041  14.151  1.00 47.79  ? 124 PRO   A C   1 
ATOM   958  O  O   . PRO   A 1 127 ? 20.486  2.095  13.129  1.00 46.95  ? 124 PRO   A O   1 
ATOM   959  C  CB  . PRO   A 1 127 ? 17.782  0.616  14.195  1.00 44.73  ? 124 PRO   A CB  1 
ATOM   960  C  CG  . PRO   A 1 127 ? 16.786  0.478  13.064  1.00 44.29  ? 124 PRO   A CG  1 
ATOM   961  C  CD  . PRO   A 1 127 ? 17.208  1.484  12.013  1.00 44.17  ? 124 PRO   A CD  1 
ATOM   962  N  N   . GLY   A 1 128 ? 20.403  2.075  15.365  1.00 79.97  ? 125 GLY   A N   1 
ATOM   963  C  CA  . GLY   A 1 128 ? 21.857  2.035  15.619  1.00 85.70  ? 125 GLY   A CA  1 
ATOM   964  C  C   . GLY   A 1 128 ? 22.239  2.440  17.032  1.00 87.09  ? 125 GLY   A C   1 
ATOM   965  O  O   . GLY   A 1 128 ? 21.326  2.545  17.890  1.00 88.97  ? 125 GLY   A O   1 
ATOM   966  N  N   . GLU   A 1 129 ? 23.532  2.658  17.283  1.00 90.78  ? 126 GLU   A N   1 
ATOM   967  C  CA  . GLU   A 1 129 ? 23.998  3.273  18.554  1.00 89.83  ? 126 GLU   A CA  1 
ATOM   968  C  C   . GLU   A 1 129 ? 23.566  4.749  18.579  1.00 82.94  ? 126 GLU   A C   1 
ATOM   969  O  O   . GLU   A 1 129 ? 23.111  5.207  19.651  1.00 78.60  ? 126 GLU   A O   1 
ATOM   970  C  CB  . GLU   A 1 129 ? 25.510  3.124  18.714  1.00 97.24  ? 126 GLU   A CB  1 
ATOM   971  C  CG  . GLU   A 1 129 ? 25.982  3.297  20.148  1.00 100.49 ? 126 GLU   A CG  1 
ATOM   972  C  CD  . GLU   A 1 129 ? 27.427  2.874  20.364  1.00 110.49 ? 126 GLU   A CD  1 
ATOM   973  O  OE1 . GLU   A 1 129 ? 28.281  3.763  20.568  1.00 111.01 ? 126 GLU   A OE1 1 
ATOM   974  O  OE2 . GLU   A 1 129 ? 27.701  1.655  20.314  1.00 119.75 ? 126 GLU   A OE2 1 
ATOM   975  N  N   . GLU   A 1 130 ? 23.670  5.446  17.440  1.00 80.46  ? 127 GLU   A N   1 
ATOM   976  C  CA  . GLU   A 1 130 ? 23.530  6.927  17.351  1.00 75.36  ? 127 GLU   A CA  1 
ATOM   977  C  C   . GLU   A 1 130 ? 22.043  7.327  17.347  1.00 71.95  ? 127 GLU   A C   1 
ATOM   978  O  O   . GLU   A 1 130 ? 21.258  6.764  16.531  1.00 71.04  ? 127 GLU   A O   1 
ATOM   979  C  CB  . GLU   A 1 130 ? 24.288  7.466  16.133  1.00 76.81  ? 127 GLU   A CB  1 
ATOM   980  C  CG  . GLU   A 1 130 ? 25.808  7.456  16.296  1.00 83.00  ? 127 GLU   A CG  1 
ATOM   981  C  CD  . GLU   A 1 130 ? 26.386  8.454  17.297  1.00 85.66  ? 127 GLU   A CD  1 
ATOM   982  O  OE1 . GLU   A 1 130 ? 27.581  8.296  17.670  1.00 88.03  ? 127 GLU   A OE1 1 
ATOM   983  O  OE2 . GLU   A 1 130 ? 25.646  9.394  17.704  1.00 83.03  ? 127 GLU   A OE2 1 
ATOM   984  N  N   . LEU   A 1 131 ? 21.686  8.288  18.215  1.00 66.21  ? 128 LEU   A N   1 
ATOM   985  C  CA  . LEU   A 1 131 ? 20.333  8.917  18.301  1.00 61.23  ? 128 LEU   A CA  1 
ATOM   986  C  C   . LEU   A 1 131 ? 20.086  9.833  17.097  1.00 57.88  ? 128 LEU   A C   1 
ATOM   987  O  O   . LEU   A 1 131 ? 18.931  9.920  16.709  1.00 51.75  ? 128 LEU   A O   1 
ATOM   988  C  CB  . LEU   A 1 131 ? 20.200  9.721  19.598  1.00 60.77  ? 128 LEU   A CB  1 
ATOM   989  C  CG  . LEU   A 1 131 ? 20.128  8.917  20.894  1.00 60.07  ? 128 LEU   A CG  1 
ATOM   990  C  CD1 . LEU   A 1 131 ? 19.719  9.837  22.039  1.00 59.29  ? 128 LEU   A CD1 1 
ATOM   991  C  CD2 . LEU   A 1 131 ? 19.172  7.732  20.780  1.00 60.56  ? 128 LEU   A CD2 1 
ATOM   992  N  N   . SER   A 1 132 ? 21.127  10.495 16.571  1.00 59.27  ? 129 SER   A N   1 
ATOM   993  C  CA  . SER   A 1 132 ? 21.154  11.114 15.216  1.00 61.58  ? 129 SER   A CA  1 
ATOM   994  C  C   . SER   A 1 132 ? 22.131  10.328 14.342  1.00 65.11  ? 129 SER   A C   1 
ATOM   995  O  O   . SER   A 1 132 ? 23.324  10.640 14.293  1.00 62.10  ? 129 SER   A O   1 
ATOM   996  C  CB  . SER   A 1 132 ? 21.494  12.576 15.277  1.00 62.35  ? 129 SER   A CB  1 
ATOM   997  O  OG  . SER   A 1 132 ? 20.396  13.307 15.799  1.00 62.80  ? 129 SER   A OG  1 
ATOM   998  N  N   . PRO   A 1 133 ? 21.669  9.250  13.656  1.00 68.72  ? 130 PRO   A N   1 
ATOM   999  C  CA  . PRO   A 1 133 ? 22.529  8.514  12.736  1.00 71.74  ? 130 PRO   A CA  1 
ATOM   1000 C  C   . PRO   A 1 133 ? 22.718  9.410  11.505  1.00 70.36  ? 130 PRO   A C   1 
ATOM   1001 O  O   . PRO   A 1 133 ? 21.710  9.854  10.955  1.00 70.71  ? 130 PRO   A O   1 
ATOM   1002 C  CB  . PRO   A 1 133 ? 21.742  7.225  12.437  1.00 76.30  ? 130 PRO   A CB  1 
ATOM   1003 C  CG  . PRO   A 1 133 ? 20.293  7.646  12.581  1.00 75.16  ? 130 PRO   A CG  1 
ATOM   1004 C  CD  . PRO   A 1 133 ? 20.291  8.723  13.655  1.00 71.64  ? 130 PRO   A CD  1 
ATOM   1005 N  N   . THR   A 1 134 ? 23.972  9.671  11.123  1.00 68.74  ? 131 THR   A N   1 
ATOM   1006 C  CA  . THR   A 1 134 ? 24.333  10.602 10.018  1.00 67.34  ? 131 THR   A CA  1 
ATOM   1007 C  C   . THR   A 1 134 ? 25.328  9.935  9.059   1.00 70.55  ? 131 THR   A C   1 
ATOM   1008 O  O   . THR   A 1 134 ? 26.181  9.174  9.544   1.00 71.38  ? 131 THR   A O   1 
ATOM   1009 C  CB  . THR   A 1 134 ? 24.887  11.909 10.595  1.00 65.38  ? 131 THR   A CB  1 
ATOM   1010 O  OG1 . THR   A 1 134 ? 26.146  11.574 11.184  1.00 64.98  ? 131 THR   A OG1 1 
ATOM   1011 C  CG2 . THR   A 1 134 ? 23.935  12.564 11.580  1.00 63.26  ? 131 THR   A CG2 1 
ATOM   1012 N  N   . ASP   A 1 135 ? 25.204  10.215 7.757   1.00 70.53  ? 132 ASP   A N   1 
ATOM   1013 C  CA  . ASP   A 1 135 ? 26.184  9.844  6.699   1.00 74.83  ? 132 ASP   A CA  1 
ATOM   1014 C  C   . ASP   A 1 135 ? 27.452  10.719 6.813   1.00 75.09  ? 132 ASP   A C   1 
ATOM   1015 O  O   . ASP   A 1 135 ? 27.542  11.573 7.732   1.00 72.95  ? 132 ASP   A O   1 
ATOM   1016 C  CB  . ASP   A 1 135 ? 25.536  9.944  5.307   1.00 76.96  ? 132 ASP   A CB  1 
ATOM   1017 C  CG  . ASP   A 1 135 ? 25.324  11.356 4.759   1.00 74.17  ? 132 ASP   A CG  1 
ATOM   1018 O  OD1 . ASP   A 1 135 ? 25.781  12.334 5.387   1.00 71.37  ? 132 ASP   A OD1 1 
ATOM   1019 O  OD2 . ASP   A 1 135 ? 24.707  11.472 3.680   1.00 78.60  ? 132 ASP   A OD2 1 
ATOM   1020 N  N   . GLU   A 1 136 ? 28.367  10.549 5.858   1.00 77.99  ? 133 GLU   A N   1 
ATOM   1021 C  CA  . GLU   A 1 136 ? 29.686  11.229 5.766   1.00 81.15  ? 133 GLU   A CA  1 
ATOM   1022 C  C   . GLU   A 1 136 ? 29.563  12.767 5.688   1.00 78.39  ? 133 GLU   A C   1 
ATOM   1023 O  O   . GLU   A 1 136 ? 30.591  13.467 5.937   1.00 78.56  ? 133 GLU   A O   1 
ATOM   1024 C  CB  . GLU   A 1 136 ? 30.373  10.649 4.533   1.00 86.24  ? 133 GLU   A CB  1 
ATOM   1025 C  CG  . GLU   A 1 136 ? 31.800  11.096 4.373   1.00 92.16  ? 133 GLU   A CG  1 
ATOM   1026 C  CD  . GLU   A 1 136 ? 32.045  12.054 3.222   1.00 91.49  ? 133 GLU   A CD  1 
ATOM   1027 O  OE1 . GLU   A 1 136 ? 31.072  12.388 2.489   1.00 88.72  ? 133 GLU   A OE1 1 
ATOM   1028 O  OE2 . GLU   A 1 136 ? 33.222  12.408 3.016   1.00 95.86  ? 133 GLU   A OE2 1 
ATOM   1029 N  N   . ASN   A 1 137 ? 28.385  13.301 5.335   1.00 74.90  ? 134 ASN   A N   1 
ATOM   1030 C  CA  . ASN   A 1 137 ? 28.170  14.775 5.241   1.00 75.07  ? 134 ASN   A CA  1 
ATOM   1031 C  C   . ASN   A 1 137 ? 27.278  15.273 6.394   1.00 72.33  ? 134 ASN   A C   1 
ATOM   1032 O  O   . ASN   A 1 137 ? 26.779  16.427 6.318   1.00 70.53  ? 134 ASN   A O   1 
ATOM   1033 C  CB  . ASN   A 1 137 ? 27.655  15.137 3.847   1.00 75.14  ? 134 ASN   A CB  1 
ATOM   1034 C  CG  . ASN   A 1 137 ? 28.608  14.652 2.774   1.00 77.10  ? 134 ASN   A CG  1 
ATOM   1035 O  OD1 . ASN   A 1 137 ? 28.282  13.738 2.022   1.00 78.13  ? 134 ASN   A OD1 1 
ATOM   1036 N  ND2 . ASN   A 1 137 ? 29.809  15.212 2.733   1.00 77.07  ? 134 ASN   A ND2 1 
ATOM   1037 N  N   . GLY   A 1 138 ? 27.125  14.471 7.453   1.00 69.96  ? 135 GLY   A N   1 
ATOM   1038 C  CA  . GLY   A 1 138 ? 26.207  14.792 8.555   1.00 69.75  ? 135 GLY   A CA  1 
ATOM   1039 C  C   . GLY   A 1 138 ? 24.749  14.794 8.104   1.00 67.83  ? 135 GLY   A C   1 
ATOM   1040 O  O   . GLY   A 1 138 ? 23.928  15.404 8.816   1.00 64.93  ? 135 GLY   A O   1 
ATOM   1041 N  N   . LYS   A 1 139 ? 24.415  14.149 6.972   1.00 69.21  ? 136 LYS   A N   1 
ATOM   1042 C  CA  . LYS   A 1 139 ? 22.994  13.966 6.566   1.00 69.91  ? 136 LYS   A CA  1 
ATOM   1043 C  C   . LYS   A 1 139 ? 22.446  12.765 7.347   1.00 65.52  ? 136 LYS   A C   1 
ATOM   1044 O  O   . LYS   A 1 139 ? 23.031  11.672 7.266   1.00 61.16  ? 136 LYS   A O   1 
ATOM   1045 C  CB  . LYS   A 1 139 ? 22.816  13.835 5.050   1.00 76.29  ? 136 LYS   A CB  1 
ATOM   1046 C  CG  . LYS   A 1 139 ? 23.330  15.015 4.236   1.00 80.35  ? 136 LYS   A CG  1 
ATOM   1047 C  CD  . LYS   A 1 139 ? 22.929  16.395 4.747   1.00 82.88  ? 136 LYS   A CD  1 
ATOM   1048 C  CE  . LYS   A 1 139 ? 23.928  17.472 4.370   1.00 85.30  ? 136 LYS   A CE  1 
ATOM   1049 N  NZ  . LYS   A 1 139 ? 24.554  17.217 3.046   1.00 86.80  ? 136 LYS   A NZ  1 
ATOM   1050 N  N   . VAL   A 1 140 ? 21.410  13.026 8.144   1.00 63.15  ? 137 VAL   A N   1 
ATOM   1051 C  CA  . VAL   A 1 140 ? 20.627  12.025 8.935   1.00 61.67  ? 137 VAL   A CA  1 
ATOM   1052 C  C   . VAL   A 1 140 ? 20.117  10.938 7.980   1.00 63.36  ? 137 VAL   A C   1 
ATOM   1053 O  O   . VAL   A 1 140 ? 19.626  11.291 6.882   1.00 65.77  ? 137 VAL   A O   1 
ATOM   1054 C  CB  . VAL   A 1 140 ? 19.444  12.693 9.672   1.00 63.20  ? 137 VAL   A CB  1 
ATOM   1055 C  CG1 . VAL   A 1 140 ? 18.756  11.720 10.629  1.00 63.31  ? 137 VAL   A CG1 1 
ATOM   1056 C  CG2 . VAL   A 1 140 ? 19.851  13.972 10.408  1.00 61.64  ? 137 VAL   A CG2 1 
ATOM   1057 N  N   . ILE   A 1 141 ? 20.179  9.676  8.405   1.00 52.63  ? 138 ILE   A N   1 
ATOM   1058 C  CA  . ILE   A 1 141 ? 19.655  8.521  7.620   1.00 51.71  ? 138 ILE   A CA  1 
ATOM   1059 C  C   . ILE   A 1 141 ? 18.236  8.154  8.084   1.00 48.15  ? 138 ILE   A C   1 
ATOM   1060 O  O   . ILE   A 1 141 ? 18.074  7.827  9.276   1.00 50.00  ? 138 ILE   A O   1 
ATOM   1061 C  CB  . ILE   A 1 141 ? 20.610  7.334  7.733   1.00 53.72  ? 138 ILE   A CB  1 
ATOM   1062 C  CG1 . ILE   A 1 141 ? 22.024  7.744  7.304   1.00 55.83  ? 138 ILE   A CG1 1 
ATOM   1063 C  CG2 . ILE   A 1 141 ? 20.056  6.146  6.951   1.00 54.99  ? 138 ILE   A CG2 1 
ATOM   1064 C  CD1 . ILE   A 1 141 ? 22.980  6.588  7.162   1.00 58.21  ? 138 ILE   A CD1 1 
ATOM   1065 N  N   . PHE   A 1 142 ? 17.259  8.198  7.172   1.00 44.49  ? 139 PHE   A N   1 
ATOM   1066 C  CA  . PHE   A 1 142 ? 15.826  7.941  7.479   1.00 41.91  ? 139 PHE   A CA  1 
ATOM   1067 C  C   . PHE   A 1 142 ? 15.560  6.432  7.412   1.00 41.60  ? 139 PHE   A C   1 
ATOM   1068 O  O   . PHE   A 1 142 ? 16.313  5.692  6.756   1.00 43.22  ? 139 PHE   A O   1 
ATOM   1069 C  CB  . PHE   A 1 142 ? 14.889  8.672  6.515   1.00 41.44  ? 139 PHE   A CB  1 
ATOM   1070 C  CG  . PHE   A 1 142 ? 15.076  10.168 6.373   1.00 41.10  ? 139 PHE   A CG  1 
ATOM   1071 C  CD1 . PHE   A 1 142 ? 15.697  10.949 7.349   1.00 40.12  ? 139 PHE   A CD1 1 
ATOM   1072 C  CD2 . PHE   A 1 142 ? 14.562  10.818 5.257   1.00 41.01  ? 139 PHE   A CD2 1 
ATOM   1073 C  CE1 . PHE   A 1 142 ? 15.837  12.329 7.195   1.00 39.50  ? 139 PHE   A CE1 1 
ATOM   1074 C  CE2 . PHE   A 1 142 ? 14.718  12.188 5.095   1.00 41.34  ? 139 PHE   A CE2 1 
ATOM   1075 C  CZ  . PHE   A 1 142 ? 15.353  12.942 6.060   1.00 40.60  ? 139 PHE   A CZ  1 
ATOM   1076 N  N   . ASP   A 1 143 ? 14.453  6.019  8.022   1.00 39.18  ? 140 ASP   A N   1 
ATOM   1077 C  CA  . ASP   A 1 143 ? 13.921  4.635  8.009   1.00 38.62  ? 140 ASP   A CA  1 
ATOM   1078 C  C   . ASP   A 1 143 ? 12.473  4.668  7.504   1.00 37.67  ? 140 ASP   A C   1 
ATOM   1079 O  O   . ASP   A 1 143 ? 11.748  5.630  7.802   1.00 36.00  ? 140 ASP   A O   1 
ATOM   1080 C  CB  . ASP   A 1 143 ? 14.006  4.034  9.424   1.00 37.76  ? 140 ASP   A CB  1 
ATOM   1081 C  CG  . ASP   A 1 143 ? 13.956  2.516  9.454   1.00 38.72  ? 140 ASP   A CG  1 
ATOM   1082 O  OD1 . ASP   A 1 143 ? 14.313  1.890  8.407   1.00 39.89  ? 140 ASP   A OD1 1 
ATOM   1083 O  OD2 . ASP   A 1 143 ? 13.518  1.967  10.494  1.00 37.77  ? 140 ASP   A OD2 1 
ATOM   1084 N  N   . ILE   A 1 144 ? 12.044  3.677  6.734   1.00 39.27  ? 141 ILE   A N   1 
ATOM   1085 C  CA  . ILE   A 1 144 ? 10.619  3.587  6.319   1.00 39.71  ? 141 ILE   A CA  1 
ATOM   1086 C  C   . ILE   A 1 144 ? 9.967   2.550  7.231   1.00 39.60  ? 141 ILE   A C   1 
ATOM   1087 O  O   . ILE   A 1 144 ? 10.315  1.360  7.105   1.00 41.43  ? 141 ILE   A O   1 
ATOM   1088 C  CB  . ILE   A 1 144 ? 10.433  3.230  4.827   1.00 42.28  ? 141 ILE   A CB  1 
ATOM   1089 C  CG1 . ILE   A 1 144 ? 11.092  4.235  3.872   1.00 43.39  ? 141 ILE   A CG1 1 
ATOM   1090 C  CG2 . ILE   A 1 144 ? 8.948   3.063  4.510   1.00 41.53  ? 141 ILE   A CG2 1 
ATOM   1091 C  CD1 . ILE   A 1 144 ? 11.210  3.731  2.414   1.00 45.66  ? 141 ILE   A CD1 1 
ATOM   1092 N  N   . VAL   A 1 145 ? 9.094   3.006  8.127   1.00 37.22  ? 142 VAL   A N   1 
ATOM   1093 C  CA  . VAL   A 1 145 ? 8.376   2.172  9.130   1.00 36.37  ? 142 VAL   A CA  1 
ATOM   1094 C  C   . VAL   A 1 145 ? 6.899   2.544  9.046   1.00 35.27  ? 142 VAL   A C   1 
ATOM   1095 O  O   . VAL   A 1 145 ? 6.579   3.743  9.136   1.00 33.18  ? 142 VAL   A O   1 
ATOM   1096 C  CB  . VAL   A 1 145 ? 8.889   2.379  10.565  1.00 35.09  ? 142 VAL   A CB  1 
ATOM   1097 C  CG1 . VAL   A 1 145 ? 8.115   1.499  11.526  1.00 35.17  ? 142 VAL   A CG1 1 
ATOM   1098 C  CG2 . VAL   A 1 145 ? 10.380  2.115  10.702  1.00 36.36  ? 142 VAL   A CG2 1 
ATOM   1099 N  N   . ASP   A 1 146 ? 6.024   1.559  8.886   1.00 36.23  ? 143 ASP   A N   1 
ATOM   1100 C  CA  . ASP   A 1 146 ? 4.568   1.823  8.994   1.00 36.18  ? 143 ASP   A CA  1 
ATOM   1101 C  C   . ASP   A 1 146 ? 4.290   2.105  10.473  1.00 33.59  ? 143 ASP   A C   1 
ATOM   1102 O  O   . ASP   A 1 146 ? 4.446   1.184  11.277  1.00 32.41  ? 143 ASP   A O   1 
ATOM   1103 C  CB  . ASP   A 1 146 ? 3.726   0.651  8.477   1.00 38.62  ? 143 ASP   A CB  1 
ATOM   1104 C  CG  . ASP   A 1 146 ? 2.228   0.933  8.492   1.00 39.64  ? 143 ASP   A CG  1 
ATOM   1105 O  OD1 . ASP   A 1 146 ? 1.788   1.850  9.226   1.00 40.88  ? 143 ASP   A OD1 1 
ATOM   1106 O  OD2 . ASP   A 1 146 ? 1.495   0.240  7.764   1.00 42.53  ? 143 ASP   A OD2 1 
ATOM   1107 N  N   . LEU   A 1 147 ? 3.972   3.351  10.833  1.00 32.36  ? 144 LEU   A N   1 
ATOM   1108 C  CA  . LEU   A 1 147 ? 3.793   3.726  12.259  1.00 31.23  ? 144 LEU   A CA  1 
ATOM   1109 C  C   . LEU   A 1 147 ? 2.593   3.018  12.906  1.00 31.12  ? 144 LEU   A C   1 
ATOM   1110 O  O   . LEU   A 1 147 ? 2.512   3.048  14.078  1.00 28.35  ? 144 LEU   A O   1 
ATOM   1111 C  CB  . LEU   A 1 147 ? 3.627   5.238  12.388  1.00 31.28  ? 144 LEU   A CB  1 
ATOM   1112 C  CG  . LEU   A 1 147 ? 4.841   6.058  11.950  1.00 31.85  ? 144 LEU   A CG  1 
ATOM   1113 C  CD1 . LEU   A 1 147 ? 4.510   7.518  11.996  1.00 30.57  ? 144 LEU   A CD1 1 
ATOM   1114 C  CD2 . LEU   A 1 147 ? 6.081   5.744  12.764  1.00 32.61  ? 144 LEU   A CD2 1 
ATOM   1115 N  N   . CYS   A 1 148 ? 1.676   2.409  12.155  1.00 32.50  ? 145 CYS   A N   1 
ATOM   1116 C  CA  . CYS   A 1 148 ? 0.651   1.522  12.752  1.00 33.87  ? 145 CYS   A CA  1 
ATOM   1117 C  C   . CYS   A 1 148 ? 1.299   0.336  13.485  1.00 33.45  ? 145 CYS   A C   1 
ATOM   1118 O  O   . CYS   A 1 148 ? 0.706   -0.091 14.506  1.00 31.96  ? 145 CYS   A O   1 
ATOM   1119 C  CB  . CYS   A 1 148 ? -0.327  1.053  11.684  1.00 36.96  ? 145 CYS   A CB  1 
ATOM   1120 S  SG  . CYS   A 1 148 ? -1.384  2.440  11.204  1.00 42.25  ? 145 CYS   A SG  1 
ATOM   1121 N  N   . THR   A 1 149 ? 2.416   -0.204 12.960  1.00 33.96  ? 146 THR   A N   1 
ATOM   1122 C  CA  . THR   A 1 149 ? 3.152   -1.324 13.602  1.00 34.87  ? 146 THR   A CA  1 
ATOM   1123 C  C   . THR   A 1 149 ? 3.820   -0.765 14.862  1.00 32.93  ? 146 THR   A C   1 
ATOM   1124 O  O   . THR   A 1 149 ? 3.755   -1.425 15.886  1.00 32.88  ? 146 THR   A O   1 
ATOM   1125 C  CB  . THR   A 1 149 ? 4.195   -2.039 12.733  1.00 36.94  ? 146 THR   A CB  1 
ATOM   1126 O  OG1 . THR   A 1 149 ? 5.254   -1.172 12.325  1.00 35.42  ? 146 THR   A OG1 1 
ATOM   1127 C  CG2 . THR   A 1 149 ? 3.589   -2.706 11.518  1.00 38.97  ? 146 THR   A CG2 1 
ATOM   1128 N  N   . THR   A 1 150 ? 4.377   0.440  14.805  1.00 31.78  ? 147 THR   A N   1 
ATOM   1129 C  CA  . THR   A 1 150 ? 4.889   1.122  16.020  1.00 29.84  ? 147 THR   A CA  1 
ATOM   1130 C  C   . THR   A 1 150 ? 3.749   1.291  17.030  1.00 29.18  ? 147 THR   A C   1 
ATOM   1131 O  O   . THR   A 1 150 ? 3.940   1.003  18.240  1.00 29.14  ? 147 THR   A O   1 
ATOM   1132 C  CB  . THR   A 1 150 ? 5.505   2.466  15.660  1.00 28.41  ? 147 THR   A CB  1 
ATOM   1133 O  OG1 . THR   A 1 150 ? 6.377   2.232  14.558  1.00 28.33  ? 147 THR   A OG1 1 
ATOM   1134 C  CG2 . THR   A 1 150 ? 6.242   3.056  16.846  1.00 27.17  ? 147 THR   A CG2 1 
ATOM   1135 N  N   . TRP   A 1 151 ? 2.594   1.752  16.569  1.00 28.28  ? 148 TRP   A N   1 
ATOM   1136 C  CA  . TRP   A 1 151 ? 1.450   1.969  17.481  1.00 27.50  ? 148 TRP   A CA  1 
ATOM   1137 C  C   . TRP   A 1 151 ? 1.016   0.655  18.143  1.00 28.97  ? 148 TRP   A C   1 
ATOM   1138 O  O   . TRP   A 1 151 ? 0.755   0.683  19.381  1.00 28.95  ? 148 TRP   A O   1 
ATOM   1139 C  CB  . TRP   A 1 151 ? 0.299   2.659  16.771  1.00 26.91  ? 148 TRP   A CB  1 
ATOM   1140 C  CG  . TRP   A 1 151 ? -0.721  3.093  17.760  1.00 25.90  ? 148 TRP   A CG  1 
ATOM   1141 C  CD1 . TRP   A 1 151 ? -1.939  2.523  17.953  1.00 27.02  ? 148 TRP   A CD1 1 
ATOM   1142 C  CD2 . TRP   A 1 151 ? -0.575  4.104  18.775  1.00 24.44  ? 148 TRP   A CD2 1 
ATOM   1143 N  NE1 . TRP   A 1 151 ? -2.581  3.131  18.985  1.00 25.78  ? 148 TRP   A NE1 1 
ATOM   1144 C  CE2 . TRP   A 1 151 ? -1.775  4.111  19.512  1.00 24.74  ? 148 TRP   A CE2 1 
ATOM   1145 C  CE3 . TRP   A 1 151 ? 0.436   4.998  19.120  1.00 23.18  ? 148 TRP   A CE3 1 
ATOM   1146 C  CZ2 . TRP   A 1 151 ? -1.991  4.996  20.574  1.00 24.15  ? 148 TRP   A CZ2 1 
ATOM   1147 C  CZ3 . TRP   A 1 151 ? 0.221   5.873  20.170  1.00 22.39  ? 148 TRP   A CZ3 1 
ATOM   1148 C  CH2 . TRP   A 1 151 ? -0.980  5.873  20.876  1.00 22.61  ? 148 TRP   A CH2 1 
ATOM   1149 N  N   . GLU   A 1 152 ? 0.967   -0.463 17.408  1.00 30.45  ? 149 GLU   A N   1 
ATOM   1150 C  CA  . GLU   A 1 152 ? 0.570   -1.754 18.014  1.00 32.74  ? 149 GLU   A CA  1 
ATOM   1151 C  C   . GLU   A 1 152 ? 1.552   -2.108 19.132  1.00 31.24  ? 149 GLU   A C   1 
ATOM   1152 O  O   . GLU   A 1 152 ? 1.113   -2.621 20.130  1.00 30.66  ? 149 GLU   A O   1 
ATOM   1153 C  CB  . GLU   A 1 152 ? 0.537   -2.891 17.006  1.00 37.24  ? 149 GLU   A CB  1 
ATOM   1154 C  CG  . GLU   A 1 152 ? -0.389  -2.569 15.849  1.00 40.61  ? 149 GLU   A CG  1 
ATOM   1155 C  CD  . GLU   A 1 152 ? -0.543  -3.611 14.752  1.00 44.84  ? 149 GLU   A CD  1 
ATOM   1156 O  OE1 . GLU   A 1 152 ? -1.671  -3.693 14.220  1.00 45.07  ? 149 GLU   A OE1 1 
ATOM   1157 O  OE2 . GLU   A 1 152 ? 0.448   -4.322 14.430  1.00 50.37  ? 149 GLU   A OE2 1 
ATOM   1158 N  N   . ALA   A 1 153 ? 2.844   -1.854 18.971  1.00 30.61  ? 150 ALA   A N   1 
ATOM   1159 C  CA  . ALA   A 1 153 ? 3.853   -2.140 20.029  1.00 30.84  ? 150 ALA   A CA  1 
ATOM   1160 C  C   . ALA   A 1 153 ? 3.678   -1.197 21.233  1.00 29.78  ? 150 ALA   A C   1 
ATOM   1161 O  O   . ALA   A 1 153 ? 3.865   -1.664 22.387  1.00 30.09  ? 150 ALA   A O   1 
ATOM   1162 C  CB  . ALA   A 1 153 ? 5.263   -2.092 19.480  1.00 31.17  ? 150 ALA   A CB  1 
ATOM   1163 N  N   . MET   A 1 154 ? 3.302   0.069  21.009  1.00 27.85  ? 151 MET   A N   1 
ATOM   1164 C  CA  . MET   A 1 154 ? 2.895   1.003  22.097  1.00 26.59  ? 151 MET   A CA  1 
ATOM   1165 C  C   . MET   A 1 154 ? 1.691   0.407  22.853  1.00 26.91  ? 151 MET   A C   1 
ATOM   1166 O  O   . MET   A 1 154 ? 1.678   0.443  24.099  1.00 26.20  ? 151 MET   A O   1 
ATOM   1167 C  CB  . MET   A 1 154 ? 2.534   2.372  21.508  1.00 25.95  ? 151 MET   A CB  1 
ATOM   1168 C  CG  . MET   A 1 154 ? 3.692   3.058  20.811  1.00 25.85  ? 151 MET   A CG  1 
ATOM   1169 S  SD  . MET   A 1 154 ? 4.956   3.722  21.952  1.00 26.23  ? 151 MET   A SD  1 
ATOM   1170 C  CE  . MET   A 1 154 ? 4.108   5.196  22.518  1.00 24.66  ? 151 MET   A CE  1 
ATOM   1171 N  N   . GLU   A 1 155 ? 0.717   -0.150 22.140  1.00 27.02  ? 152 GLU   A N   1 
ATOM   1172 C  CA  . GLU   A 1 155 ? -0.527  -0.671 22.776  1.00 28.20  ? 152 GLU   A CA  1 
ATOM   1173 C  C   . GLU   A 1 155 ? -0.142  -1.826 23.704  1.00 29.54  ? 152 GLU   A C   1 
ATOM   1174 O  O   . GLU   A 1 155 ? -0.702  -1.935 24.850  1.00 29.48  ? 152 GLU   A O   1 
ATOM   1175 C  CB  . GLU   A 1 155 ? -1.511  -1.146 21.710  1.00 29.38  ? 152 GLU   A CB  1 
ATOM   1176 C  CG  . GLU   A 1 155 ? -2.195  -0.044 20.965  1.00 29.07  ? 152 GLU   A CG  1 
ATOM   1177 C  CD  . GLU   A 1 155 ? -3.130  -0.516 19.867  1.00 30.94  ? 152 GLU   A CD  1 
ATOM   1178 O  OE1 . GLU   A 1 155 ? -2.883  -1.603 19.306  1.00 31.55  ? 152 GLU   A OE1 1 
ATOM   1179 O  OE2 . GLU   A 1 155 ? -4.099  0.223  19.573  1.00 32.02  ? 152 GLU   A OE2 1 
ATOM   1180 N  N   . LYS   A 1 156 ? 0.812   -2.645 23.265  1.00 30.75  ? 153 LYS   A N   1 
ATOM   1181 C  CA  . LYS   A 1 156 ? 1.254   -3.777 24.109  1.00 33.02  ? 153 LYS   A CA  1 
ATOM   1182 C  C   . LYS   A 1 156 ? 1.914   -3.196 25.372  1.00 32.07  ? 153 LYS   A C   1 
ATOM   1183 O  O   . LYS   A 1 156 ? 1.775   -3.828 26.434  1.00 32.87  ? 153 LYS   A O   1 
ATOM   1184 C  CB  . LYS   A 1 156 ? 2.171   -4.728 23.344  1.00 35.51  ? 153 LYS   A CB  1 
ATOM   1185 C  CG  . LYS   A 1 156 ? 1.457   -5.516 22.253  1.00 38.05  ? 153 LYS   A CG  1 
ATOM   1186 C  CD  . LYS   A 1 156 ? 2.435   -6.265 21.370  1.00 40.72  ? 153 LYS   A CD  1 
ATOM   1187 C  CE  . LYS   A 1 156 ? 1.800   -7.214 20.367  1.00 43.57  ? 153 LYS   A CE  1 
ATOM   1188 N  NZ  . LYS   A 1 156 ? 1.012   -6.459 19.358  1.00 43.94  ? 153 LYS   A NZ  1 
ATOM   1189 N  N   . CYS   A 1 157 ? 2.619   -2.075 25.257  1.00 30.08  ? 154 CYS   A N   1 
ATOM   1190 C  CA  . CYS   A 1 157 ? 3.275   -1.429 26.436  1.00 29.90  ? 154 CYS   A CA  1 
ATOM   1191 C  C   . CYS   A 1 157 ? 2.233   -1.028 27.498  1.00 29.76  ? 154 CYS   A C   1 
ATOM   1192 O  O   . CYS   A 1 157 ? 2.452   -1.276 28.705  1.00 29.91  ? 154 CYS   A O   1 
ATOM   1193 C  CB  . CYS   A 1 157 ? 4.107   -0.235 26.012  1.00 28.73  ? 154 CYS   A CB  1 
ATOM   1194 S  SG  . CYS   A 1 157 ? 5.640   -0.732 25.207  1.00 31.02  ? 154 CYS   A SG  1 
ATOM   1195 N  N   . LYS   A 1 158 ? 1.122   -0.457 27.056  1.00 28.76  ? 155 LYS   A N   1 
ATOM   1196 C  CA  . LYS   A 1 158 ? -0.022  -0.169 27.925  1.00 29.73  ? 155 LYS   A CA  1 
ATOM   1197 C  C   . LYS   A 1 158 ? -0.573  -1.488 28.486  1.00 32.25  ? 155 LYS   A C   1 
ATOM   1198 O  O   . LYS   A 1 158 ? -0.781  -1.552 29.673  1.00 31.46  ? 155 LYS   A O   1 
ATOM   1199 C  CB  . LYS   A 1 158 ? -1.068  0.665  27.180  1.00 29.10  ? 155 LYS   A CB  1 
ATOM   1200 C  CG  . LYS   A 1 158 ? -2.350  0.909  27.973  1.00 29.64  ? 155 LYS   A CG  1 
ATOM   1201 C  CD  . LYS   A 1 158 ? -3.173  2.017  27.339  1.00 28.78  ? 155 LYS   A CD  1 
ATOM   1202 C  CE  . LYS   A 1 158 ? -4.596  2.105  27.824  1.00 30.31  ? 155 LYS   A CE  1 
ATOM   1203 N  NZ  . LYS   A 1 158 ? -4.673  2.678  29.189  1.00 30.70  ? 155 LYS   A NZ  1 
ATOM   1204 N  N   . ASP   A 1 159 ? -0.765  -2.529 27.673  1.00 34.17  ? 156 ASP   A N   1 
ATOM   1205 C  CA  . ASP   A 1 159 ? -1.344  -3.786 28.221  1.00 37.10  ? 156 ASP   A CA  1 
ATOM   1206 C  C   . ASP   A 1 159 ? -0.390  -4.372 29.277  1.00 36.54  ? 156 ASP   A C   1 
ATOM   1207 O  O   . ASP   A 1 159 ? -0.875  -4.993 30.211  1.00 36.94  ? 156 ASP   A O   1 
ATOM   1208 C  CB  . ASP   A 1 159 ? -1.783  -4.743 27.113  1.00 40.17  ? 156 ASP   A CB  1 
ATOM   1209 C  CG  . ASP   A 1 159 ? -3.069  -4.260 26.458  1.00 42.69  ? 156 ASP   A CG  1 
ATOM   1210 O  OD1 . ASP   A 1 159 ? -3.890  -3.662 27.166  1.00 45.11  ? 156 ASP   A OD1 1 
ATOM   1211 O  OD2 . ASP   A 1 159 ? -3.232  -4.438 25.250  1.00 44.94  ? 156 ASP   A OD2 1 
ATOM   1212 N  N   . ALA   A 1 160 ? 0.922   -4.160 29.150  1.00 34.53  ? 157 ALA   A N   1 
ATOM   1213 C  CA  . ALA   A 1 160 ? 1.926   -4.681 30.096  1.00 34.69  ? 157 ALA   A CA  1 
ATOM   1214 C  C   . ALA   A 1 160 ? 1.941   -3.830 31.377  1.00 34.40  ? 157 ALA   A C   1 
ATOM   1215 O  O   . ALA   A 1 160 ? 2.672   -4.216 32.305  1.00 35.21  ? 157 ALA   A O   1 
ATOM   1216 C  CB  . ALA   A 1 160 ? 3.294   -4.745 29.448  1.00 34.42  ? 157 ALA   A CB  1 
ATOM   1217 N  N   . GLY   A 1 161 ? 1.203   -2.716 31.432  1.00 32.86  ? 158 GLY   A N   1 
ATOM   1218 C  CA  . GLY   A 1 161 ? 1.221   -1.831 32.622  1.00 32.28  ? 158 GLY   A CA  1 
ATOM   1219 C  C   . GLY   A 1 161 ? 2.485   -0.965 32.701  1.00 31.40  ? 158 GLY   A C   1 
ATOM   1220 O  O   . GLY   A 1 161 ? 2.723   -0.351 33.750  1.00 31.43  ? 158 GLY   A O   1 
ATOM   1221 N  N   . LEU   A 1 162 ? 3.298   -0.897 31.655  1.00 30.37  ? 159 LEU   A N   1 
ATOM   1222 C  CA  . LEU   A 1 162 ? 4.565   -0.130 31.688  1.00 29.83  ? 159 LEU   A CA  1 
ATOM   1223 C  C   . LEU   A 1 162 ? 4.246   1.326  31.369  1.00 27.85  ? 159 LEU   A C   1 
ATOM   1224 O  O   . LEU   A 1 162 ? 5.073   2.206  31.690  1.00 25.90  ? 159 LEU   A O   1 
ATOM   1225 C  CB  . LEU   A 1 162 ? 5.548   -0.724 30.677  1.00 31.05  ? 159 LEU   A CB  1 
ATOM   1226 C  CG  . LEU   A 1 162 ? 6.022   -2.153 30.938  1.00 33.74  ? 159 LEU   A CG  1 
ATOM   1227 C  CD1 . LEU   A 1 162 ? 6.917   -2.571 29.787  1.00 34.70  ? 159 LEU   A CD1 1 
ATOM   1228 C  CD2 . LEU   A 1 162 ? 6.772   -2.258 32.266  1.00 34.58  ? 159 LEU   A CD2 1 
ATOM   1229 N  N   . ALA   A 1 163 ? 3.140   1.580  30.666  1.00 27.97  ? 160 ALA   A N   1 
ATOM   1230 C  CA  . ALA   A 1 163 ? 2.651   2.949  30.376  1.00 26.40  ? 160 ALA   A CA  1 
ATOM   1231 C  C   . ALA   A 1 163 ? 1.171   3.001  30.735  1.00 26.62  ? 160 ALA   A C   1 
ATOM   1232 O  O   . ALA   A 1 163 ? 0.451   2.112  30.272  1.00 26.78  ? 160 ALA   A O   1 
ATOM   1233 C  CB  . ALA   A 1 163 ? 2.873   3.273  28.919  1.00 26.02  ? 160 ALA   A CB  1 
ATOM   1234 N  N   . LYS   A 1 164 ? 0.729   3.977  31.535  1.00 25.50  ? 161 LYS   A N   1 
ATOM   1235 C  CA  . LYS   A 1 164 ? -0.718  4.067  31.892  1.00 26.58  ? 161 LYS   A CA  1 
ATOM   1236 C  C   . LYS   A 1 164 ? -1.488  4.491  30.627  1.00 25.26  ? 161 LYS   A C   1 
ATOM   1237 O  O   . LYS   A 1 164 ? -2.597  3.899  30.343  1.00 24.66  ? 161 LYS   A O   1 
ATOM   1238 C  CB  . LYS   A 1 164 ? -0.957  5.029  33.065  1.00 27.75  ? 161 LYS   A CB  1 
ATOM   1239 C  CG  . LYS   A 1 164 ? -0.355  4.610  34.402  1.00 31.03  ? 161 LYS   A CG  1 
ATOM   1240 C  CD  . LYS   A 1 164 ? -0.646  3.159  34.840  1.00 35.13  ? 161 LYS   A CD  1 
ATOM   1241 C  CE  . LYS   A 1 164 ? -0.267  2.957  36.295  1.00 39.15  ? 161 LYS   A CE  1 
ATOM   1242 N  NZ  . LYS   A 1 164 ? -0.868  1.739  36.873  1.00 42.78  ? 161 LYS   A NZ  1 
ATOM   1243 N  N   . SER   A 1 165 ? -0.909  5.455  29.896  1.00 22.93  ? 162 SER   A N   1 
ATOM   1244 C  CA  . SER   A 1 165 ? -1.483  6.028  28.665  1.00 22.04  ? 162 SER   A CA  1 
ATOM   1245 C  C   . SER   A 1 165 ? -0.412  6.097  27.588  1.00 20.72  ? 162 SER   A C   1 
ATOM   1246 O  O   . SER   A 1 165 ? 0.815   6.174  27.882  1.00 20.14  ? 162 SER   A O   1 
ATOM   1247 C  CB  . SER   A 1 165 ? -2.106  7.370  28.947  1.00 21.68  ? 162 SER   A CB  1 
ATOM   1248 O  OG  . SER   A 1 165 ? -3.137  7.263  29.919  1.00 23.07  ? 162 SER   A OG  1 
ATOM   1249 N  N   . ILE   A 1 166 ? -0.883  6.091  26.348  1.00 20.84  ? 163 ILE   A N   1 
ATOM   1250 C  CA  . ILE   A 1 166 ? -0.018  6.238  25.163  1.00 20.44  ? 163 ILE   A CA  1 
ATOM   1251 C  C   . ILE   A 1 166 ? -0.581  7.332  24.247  1.00 19.58  ? 163 ILE   A C   1 
ATOM   1252 O  O   . ILE   A 1 166 ? -1.804  7.524  24.141  1.00 20.35  ? 163 ILE   A O   1 
ATOM   1253 C  CB  . ILE   A 1 166 ? 0.107   4.867  24.475  1.00 21.54  ? 163 ILE   A CB  1 
ATOM   1254 C  CG1 . ILE   A 1 166 ? -1.247  4.235  24.171  1.00 22.81  ? 163 ILE   A CG1 1 
ATOM   1255 C  CG2 . ILE   A 1 166 ? 0.939   3.930  25.339  1.00 21.51  ? 163 ILE   A CG2 1 
ATOM   1256 C  CD1 . ILE   A 1 166 ? -1.111  2.894  23.423  1.00 24.36  ? 163 ILE   A CD1 1 
ATOM   1257 N  N   . GLY   A 1 167 ? 0.310   8.017  23.567  1.00 19.06  ? 164 GLY   A N   1 
ATOM   1258 C  CA  . GLY   A 1 167 ? -0.054  9.130  22.677  1.00 18.89  ? 164 GLY   A CA  1 
ATOM   1259 C  C   . GLY   A 1 167 ? 1.074   9.358  21.712  1.00 19.21  ? 164 GLY   A C   1 
ATOM   1260 O  O   . GLY   A 1 167 ? 1.948   8.475  21.562  1.00 19.40  ? 164 GLY   A O   1 
ATOM   1261 N  N   . VAL   A 1 168 ? 0.995   10.465 20.990  1.00 19.29  ? 165 VAL   A N   1 
ATOM   1262 C  CA  . VAL   A 1 168 ? 1.946   10.771 19.911  1.00 19.24  ? 165 VAL   A CA  1 
ATOM   1263 C  C   . VAL   A 1 168 ? 2.347   12.234 20.056  1.00 18.79  ? 165 VAL   A C   1 
ATOM   1264 O  O   . VAL   A 1 168 ? 1.768   12.977 20.870  1.00 17.86  ? 165 VAL   A O   1 
ATOM   1265 C  CB  . VAL   A 1 168 ? 1.319   10.504 18.531  1.00 20.37  ? 165 VAL   A CB  1 
ATOM   1266 C  CG1 . VAL   A 1 168 ? 0.880   9.045  18.354  1.00 21.65  ? 165 VAL   A CG1 1 
ATOM   1267 C  CG2 . VAL   A 1 168 ? 0.154   11.437 18.269  1.00 20.55  ? 165 VAL   A CG2 1 
ATOM   1268 N  N   . SER   A 1 169 ? 3.314   12.628 19.248  1.00 18.50  ? 166 SER   A N   1 
ATOM   1269 C  CA  . SER   A 1 169 ? 3.889   13.998 19.278  1.00 18.42  ? 166 SER   A CA  1 
ATOM   1270 C  C   . SER   A 1 169 ? 4.310   14.330 17.862  1.00 18.40  ? 166 SER   A C   1 
ATOM   1271 O  O   . SER   A 1 169 ? 4.808   13.429 17.149  1.00 19.66  ? 166 SER   A O   1 
ATOM   1272 C  CB  . SER   A 1 169 ? 5.073   14.078 20.203  1.00 18.49  ? 166 SER   A CB  1 
ATOM   1273 O  OG  . SER   A 1 169 ? 5.585   15.406 20.313  1.00 18.49  ? 166 SER   A OG  1 
ATOM   1274 N  N   . ASN   A 1 170 ? 4.199   15.603 17.487  1.00 18.23  ? 167 ASN   A N   1 
ATOM   1275 C  CA  . ASN   A 1 170 ? 4.631   16.110 16.153  1.00 18.31  ? 167 ASN   A CA  1 
ATOM   1276 C  C   . ASN   A 1 170 ? 3.871   15.479 14.973  1.00 19.17  ? 167 ASN   A C   1 
ATOM   1277 O  O   . ASN   A 1 170 ? 4.460   15.486 13.869  1.00 20.08  ? 167 ASN   A O   1 
ATOM   1278 C  CB  . ASN   A 1 170 ? 6.134   15.912 15.994  1.00 18.96  ? 167 ASN   A CB  1 
ATOM   1279 C  CG  . ASN   A 1 170 ? 6.878   16.799 16.968  1.00 18.60  ? 167 ASN   A CG  1 
ATOM   1280 O  OD1 . ASN   A 1 170 ? 6.662   18.014 16.964  1.00 19.91  ? 167 ASN   A OD1 1 
ATOM   1281 N  ND2 . ASN   A 1 170 ? 7.641   16.213 17.863  1.00 18.17  ? 167 ASN   A ND2 1 
ATOM   1282 N  N   . PHE   A 1 171 ? 2.690   14.913 15.207  1.00 18.94  ? 168 PHE   A N   1 
ATOM   1283 C  CA  . PHE   A 1 171 ? 1.833   14.316 14.151  1.00 20.25  ? 168 PHE   A CA  1 
ATOM   1284 C  C   . PHE   A 1 171 ? 0.925   15.410 13.609  1.00 21.33  ? 168 PHE   A C   1 
ATOM   1285 O  O   . PHE   A 1 171 ? 0.485   16.281 14.406  1.00 21.47  ? 168 PHE   A O   1 
ATOM   1286 C  CB  . PHE   A 1 171 ? 0.937   13.180 14.656  1.00 20.21  ? 168 PHE   A CB  1 
ATOM   1287 C  CG  . PHE   A 1 171 ? 1.581   11.842 14.854  1.00 20.21  ? 168 PHE   A CG  1 
ATOM   1288 C  CD1 . PHE   A 1 171 ? 2.864   11.736 15.340  1.00 19.97  ? 168 PHE   A CD1 1 
ATOM   1289 C  CD2 . PHE   A 1 171 ? 0.916   10.689 14.459  1.00 21.26  ? 168 PHE   A CD2 1 
ATOM   1290 C  CE1 . PHE   A 1 171 ? 3.449   10.493 15.551  1.00 20.68  ? 168 PHE   A CE1 1 
ATOM   1291 C  CE2 . PHE   A 1 171 ? 1.494   9.457  14.646  1.00 21.78  ? 168 PHE   A CE2 1 
ATOM   1292 C  CZ  . PHE   A 1 171 ? 2.773   9.356  15.139  1.00 21.84  ? 168 PHE   A CZ  1 
ATOM   1293 N  N   . ASN   A 1 172 ? 0.654   15.366 12.298  1.00 22.62  ? 169 ASN   A N   1 
ATOM   1294 C  CA  . ASN   A 1 172 ? -0.343  16.264 11.669  1.00 23.55  ? 169 ASN   A CA  1 
ATOM   1295 C  C   . ASN   A 1 172 ? -1.660  15.481 11.643  1.00 24.48  ? 169 ASN   A C   1 
ATOM   1296 O  O   . ASN   A 1 172 ? -1.707  14.298 12.102  1.00 23.23  ? 169 ASN   A O   1 
ATOM   1297 C  CB  . ASN   A 1 172 ? 0.151   16.807 10.322  1.00 24.56  ? 169 ASN   A CB  1 
ATOM   1298 C  CG  . ASN   A 1 172 ? 0.349   15.701 9.298   1.00 25.40  ? 169 ASN   A CG  1 
ATOM   1299 O  OD1 . ASN   A 1 172 ? -0.218  14.621 9.430   1.00 25.25  ? 169 ASN   A OD1 1 
ATOM   1300 N  ND2 . ASN   A 1 172 ? 1.202   15.930 8.312   1.00 26.74  ? 169 ASN   A ND2 1 
ATOM   1301 N  N   . ARG   A 1 173 ? -2.712  16.086 11.125  1.00 26.11  ? 170 ARG   A N   1 
ATOM   1302 C  CA  . ARG   A 1 173 ? -4.023  15.411 11.054  1.00 29.21  ? 170 ARG   A CA  1 
ATOM   1303 C  C   . ARG   A 1 173 ? -3.928  14.096 10.261  1.00 29.20  ? 170 ARG   A C   1 
ATOM   1304 O  O   . ARG   A 1 173 ? -4.519  13.116 10.699  1.00 28.87  ? 170 ARG   A O   1 
ATOM   1305 C  CB  . ARG   A 1 173 ? -5.052  16.334 10.411  1.00 33.42  ? 170 ARG   A CB  1 
ATOM   1306 C  CG  . ARG   A 1 173 ? -6.269  15.567 9.921   1.00 37.86  ? 170 ARG   A CG  1 
ATOM   1307 C  CD  . ARG   A 1 173 ? -7.311  16.533 9.473   1.00 41.45  ? 170 ARG   A CD  1 
ATOM   1308 N  NE  . ARG   A 1 173 ? -8.462  15.770 9.063   1.00 45.62  ? 170 ARG   A NE  1 
ATOM   1309 C  CZ  . ARG   A 1 173 ? -9.518  16.303 8.478   1.00 50.11  ? 170 ARG   A CZ  1 
ATOM   1310 N  NH1 . ARG   A 1 173 ? -10.552 15.546 8.138   1.00 53.25  ? 170 ARG   A NH1 1 
ATOM   1311 N  NH2 . ARG   A 1 173 ? -9.524  17.604 8.236   1.00 50.81  ? 170 ARG   A NH2 1 
ATOM   1312 N  N   . ARG   A 1 174 ? -3.301  14.092 9.086   1.00 29.88  ? 171 ARG   A N   1 
ATOM   1313 C  CA  . ARG   A 1 174 ? -3.259  12.881 8.228   1.00 32.50  ? 171 ARG   A CA  1 
ATOM   1314 C  C   . ARG   A 1 174 ? -2.609  11.756 9.049   1.00 30.11  ? 171 ARG   A C   1 
ATOM   1315 O  O   . ARG   A 1 174 ? -3.064  10.610 8.952   1.00 30.74  ? 171 ARG   A O   1 
ATOM   1316 C  CB  . ARG   A 1 174 ? -2.530  13.188 6.912   1.00 35.59  ? 171 ARG   A CB  1 
ATOM   1317 C  CG  . ARG   A 1 174 ? -2.391  11.987 5.977   1.00 40.15  ? 171 ARG   A CG  1 
ATOM   1318 C  CD  . ARG   A 1 174 ? -1.589  12.283 4.709   1.00 44.28  ? 171 ARG   A CD  1 
ATOM   1319 N  NE  . ARG   A 1 174 ? -0.483  13.206 4.987   1.00 45.95  ? 171 ARG   A NE  1 
ATOM   1320 C  CZ  . ARG   A 1 174 ? 0.707   12.879 5.530   1.00 45.06  ? 171 ARG   A CZ  1 
ATOM   1321 N  NH1 . ARG   A 1 174 ? 1.605   13.827 5.764   1.00 41.67  ? 171 ARG   A NH1 1 
ATOM   1322 N  NH2 . ARG   A 1 174 ? 1.003   11.620 5.811   1.00 45.37  ? 171 ARG   A NH2 1 
ATOM   1323 N  N   . GLN   A 1 175 ? -1.562  12.071 9.807   1.00 27.43  ? 172 GLN   A N   1 
ATOM   1324 C  CA  . GLN   A 1 175 ? -0.828  11.031 10.570  1.00 27.21  ? 172 GLN   A CA  1 
ATOM   1325 C  C   . GLN   A 1 175 ? -1.675  10.566 11.753  1.00 26.66  ? 172 GLN   A C   1 
ATOM   1326 O  O   . GLN   A 1 175 ? -1.615  9.375  12.064  1.00 27.78  ? 172 GLN   A O   1 
ATOM   1327 C  CB  . GLN   A 1 175 ? 0.536   11.541 11.008  1.00 26.13  ? 172 GLN   A CB  1 
ATOM   1328 C  CG  . GLN   A 1 175 ? 1.417   11.863 9.812   1.00 26.98  ? 172 GLN   A CG  1 
ATOM   1329 C  CD  . GLN   A 1 175 ? 2.580   12.755 10.185  1.00 26.49  ? 172 GLN   A CD  1 
ATOM   1330 O  OE1 . GLN   A 1 175 ? 2.498   13.610 11.099  1.00 25.89  ? 172 GLN   A OE1 1 
ATOM   1331 N  NE2 . GLN   A 1 175 ? 3.678   12.547 9.469   1.00 26.33  ? 172 GLN   A NE2 1 
ATOM   1332 N  N   . LEU   A 1 176 ? -2.391  11.459 12.416  1.00 26.15  ? 173 LEU   A N   1 
ATOM   1333 C  CA  . LEU   A 1 176 ? -3.364  11.016 13.446  1.00 26.77  ? 173 LEU   A CA  1 
ATOM   1334 C  C   . LEU   A 1 176 ? -4.378  10.064 12.811  1.00 28.48  ? 173 LEU   A C   1 
ATOM   1335 O  O   . LEU   A 1 176 ? -4.670  9.048  13.448  1.00 28.47  ? 173 LEU   A O   1 
ATOM   1336 C  CB  . LEU   A 1 176 ? -4.104  12.199 14.043  1.00 26.87  ? 173 LEU   A CB  1 
ATOM   1337 C  CG  . LEU   A 1 176 ? -3.283  13.065 14.985  1.00 26.09  ? 173 LEU   A CG  1 
ATOM   1338 C  CD1 . LEU   A 1 176 ? -4.091  14.255 15.493  1.00 26.50  ? 173 LEU   A CD1 1 
ATOM   1339 C  CD2 . LEU   A 1 176 ? -2.794  12.241 16.144  1.00 25.41  ? 173 LEU   A CD2 1 
ATOM   1340 N  N   . GLU   A 1 177 ? -4.955  10.443 11.660  1.00 30.55  ? 174 GLU   A N   1 
ATOM   1341 C  CA  . GLU   A 1 177 ? -5.999  9.645  10.983  1.00 33.96  ? 174 GLU   A CA  1 
ATOM   1342 C  C   . GLU   A 1 177 ? -5.413  8.274  10.640  1.00 35.24  ? 174 GLU   A C   1 
ATOM   1343 O  O   . GLU   A 1 177 ? -6.145  7.290  10.668  1.00 33.40  ? 174 GLU   A O   1 
ATOM   1344 C  CB  . GLU   A 1 177 ? -6.490  10.297 9.692   1.00 36.90  ? 174 GLU   A CB  1 
ATOM   1345 C  CG  . GLU   A 1 177 ? -7.483  11.426 9.910   1.00 39.58  ? 174 GLU   A CG  1 
ATOM   1346 C  CD  . GLU   A 1 177 ? -7.845  12.265 8.693   1.00 44.60  ? 174 GLU   A CD  1 
ATOM   1347 O  OE1 . GLU   A 1 177 ? -7.128  12.122 7.640   1.00 50.80  ? 174 GLU   A OE1 1 
ATOM   1348 O  OE2 . GLU   A 1 177 ? -8.843  13.072 8.779   1.00 48.07  ? 174 GLU   A OE2 1 
ATOM   1349 N  N   . MET   A 1 178 ? -4.137  8.203  10.290  1.00 36.56  ? 175 MET   A N   1 
ATOM   1350 C  CA  . MET   A 1 178 ? -3.528  6.885  10.003  1.00 39.57  ? 175 MET   A CA  1 
ATOM   1351 C  C   . MET   A 1 178 ? -3.674  5.977  11.236  1.00 35.58  ? 175 MET   A C   1 
ATOM   1352 O  O   . MET   A 1 178 ? -3.884  4.764  11.029  1.00 35.25  ? 175 MET   A O   1 
ATOM   1353 C  CB  . MET   A 1 178 ? -2.060  7.077  9.667   1.00 46.45  ? 175 MET   A CB  1 
ATOM   1354 C  CG  . MET   A 1 178 ? -1.309  5.809  9.407   1.00 54.30  ? 175 MET   A CG  1 
ATOM   1355 S  SD  . MET   A 1 178 ? 0.431   6.243  9.082   1.00 69.51  ? 175 MET   A SD  1 
ATOM   1356 C  CE  . MET   A 1 178 ? 0.840   7.245  10.516  1.00 64.80  ? 175 MET   A CE  1 
ATOM   1357 N  N   . ILE   A 1 179 ? -3.521  6.510  12.459  1.00 32.71  ? 176 ILE   A N   1 
ATOM   1358 C  CA  . ILE   A 1 179 ? -3.653  5.685  13.698  1.00 31.52  ? 176 ILE   A CA  1 
ATOM   1359 C  C   . ILE   A 1 179 ? -5.146  5.482  13.957  1.00 30.87  ? 176 ILE   A C   1 
ATOM   1360 O  O   . ILE   A 1 179 ? -5.536  4.349  14.230  1.00 31.93  ? 176 ILE   A O   1 
ATOM   1361 C  CB  . ILE   A 1 179 ? -2.943  6.288  14.932  1.00 30.63  ? 176 ILE   A CB  1 
ATOM   1362 C  CG1 . ILE   A 1 179 ? -1.452  6.584  14.717  1.00 30.76  ? 176 ILE   A CG1 1 
ATOM   1363 C  CG2 . ILE   A 1 179 ? -3.159  5.440  16.176  1.00 30.24  ? 176 ILE   A CG2 1 
ATOM   1364 C  CD1 . ILE   A 1 179 ? -0.644  5.431  14.232  1.00 32.97  ? 176 ILE   A CD1 1 
ATOM   1365 N  N   . LEU   A 1 180 ? -5.957  6.526  13.870  1.00 29.94  ? 177 LEU   A N   1 
ATOM   1366 C  CA  . LEU   A 1 180 ? -7.401  6.430  14.200  1.00 30.85  ? 177 LEU   A CA  1 
ATOM   1367 C  C   . LEU   A 1 180 ? -8.096  5.393  13.308  1.00 33.04  ? 177 LEU   A C   1 
ATOM   1368 O  O   . LEU   A 1 180 ? -9.055  4.764  13.796  1.00 34.77  ? 177 LEU   A O   1 
ATOM   1369 C  CB  . LEU   A 1 180 ? -8.086  7.787  14.069  1.00 30.18  ? 177 LEU   A CB  1 
ATOM   1370 C  CG  . LEU   A 1 180 ? -7.644  8.796  15.124  1.00 28.86  ? 177 LEU   A CG  1 
ATOM   1371 C  CD1 . LEU   A 1 180 ? -8.133  10.180 14.750  1.00 28.80  ? 177 LEU   A CD1 1 
ATOM   1372 C  CD2 . LEU   A 1 180 ? -8.104  8.408  16.541  1.00 28.55  ? 177 LEU   A CD2 1 
ATOM   1373 N  N   . ASN   A 1 181 ? -7.626  5.245  12.069  1.00 33.72  ? 178 ASN   A N   1 
ATOM   1374 C  CA  . ASN   A 1 181 ? -8.217  4.328  11.051  1.00 37.13  ? 178 ASN   A CA  1 
ATOM   1375 C  C   . ASN   A 1 181 ? -7.439  3.012  10.967  1.00 37.90  ? 178 ASN   A C   1 
ATOM   1376 O  O   . ASN   A 1 181 ? -7.723  2.244  10.045  1.00 39.20  ? 178 ASN   A O   1 
ATOM   1377 C  CB  . ASN   A 1 181 ? -8.245  4.997  9.678   1.00 39.15  ? 178 ASN   A CB  1 
ATOM   1378 C  CG  . ASN   A 1 181 ? -9.121  6.232  9.697   1.00 40.96  ? 178 ASN   A CG  1 
ATOM   1379 O  OD1 . ASN   A 1 181 ? -10.190 6.224  10.313  1.00 43.08  ? 178 ASN   A OD1 1 
ATOM   1380 N  ND2 . ASN   A 1 181 ? -8.645  7.311  9.087   1.00 42.31  ? 178 ASN   A ND2 1 
ATOM   1381 N  N   . LYS   A 1 182 ? -6.515  2.743  11.885  1.00 37.10  ? 179 LYS   A N   1 
ATOM   1382 C  CA  . LYS   A 1 182 ? -5.756  1.474  11.882  1.00 38.24  ? 179 LYS   A CA  1 
ATOM   1383 C  C   . LYS   A 1 182 ? -6.748  0.333  12.107  1.00 38.87  ? 179 LYS   A C   1 
ATOM   1384 O  O   . LYS   A 1 182 ? -7.575  0.349  13.033  1.00 37.97  ? 179 LYS   A O   1 
ATOM   1385 C  CB  . LYS   A 1 182 ? -4.666  1.412  12.948  1.00 38.83  ? 179 LYS   A CB  1 
ATOM   1386 C  CG  . LYS   A 1 182 ? -3.825  0.149  12.869  1.00 41.82  ? 179 LYS   A CG  1 
ATOM   1387 C  CD  . LYS   A 1 182 ? -2.784  0.024  13.940  1.00 42.43  ? 179 LYS   A CD  1 
ATOM   1388 C  CE  . LYS   A 1 182 ? -3.295  -0.732 15.135  1.00 44.37  ? 179 LYS   A CE  1 
ATOM   1389 N  NZ  . LYS   A 1 182 ? -3.727  -2.102 14.747  1.00 47.35  ? 179 LYS   A NZ  1 
ATOM   1390 N  N   . PRO   A 1 183 ? -6.738  -0.679 11.231  1.00 41.13  ? 180 PRO   A N   1 
ATOM   1391 C  CA  . PRO   A 1 183 ? -7.497  -1.904 11.481  1.00 41.67  ? 180 PRO   A CA  1 
ATOM   1392 C  C   . PRO   A 1 183 ? -7.161  -2.505 12.850  1.00 39.93  ? 180 PRO   A C   1 
ATOM   1393 O  O   . PRO   A 1 183 ? -6.008  -2.614 13.139  1.00 38.97  ? 180 PRO   A O   1 
ATOM   1394 C  CB  . PRO   A 1 183 ? -6.993  -2.856 10.394  1.00 44.00  ? 180 PRO   A CB  1 
ATOM   1395 C  CG  . PRO   A 1 183 ? -6.536  -1.946 9.277   1.00 43.58  ? 180 PRO   A CG  1 
ATOM   1396 C  CD  . PRO   A 1 183 ? -6.016  -0.694 9.948   1.00 41.68  ? 180 PRO   A CD  1 
ATOM   1397 N  N   . GLY   A 1 184 ? -8.162  -2.874 13.639  1.00 39.71  ? 181 GLY   A N   1 
ATOM   1398 C  CA  . GLY   A 1 184 ? -7.963  -3.528 14.946  1.00 39.09  ? 181 GLY   A CA  1 
ATOM   1399 C  C   . GLY   A 1 184 ? -7.467  -2.559 16.002  1.00 37.15  ? 181 GLY   A C   1 
ATOM   1400 O  O   . GLY   A 1 184 ? -6.928  -3.045 17.012  1.00 37.17  ? 181 GLY   A O   1 
ATOM   1401 N  N   . LEU   A 1 185 ? -7.592  -1.237 15.787  1.00 35.59  ? 182 LEU   A N   1 
ATOM   1402 C  CA  . LEU   A 1 185 ? -7.152  -0.233 16.797  1.00 33.35  ? 182 LEU   A CA  1 
ATOM   1403 C  C   . LEU   A 1 185 ? -7.685  -0.686 18.159  1.00 33.84  ? 182 LEU   A C   1 
ATOM   1404 O  O   . LEU   A 1 185 ? -8.899  -1.004 18.236  1.00 34.29  ? 182 LEU   A O   1 
ATOM   1405 C  CB  . LEU   A 1 185 ? -7.677  1.170  16.485  1.00 32.22  ? 182 LEU   A CB  1 
ATOM   1406 C  CG  . LEU   A 1 185 ? -7.183  2.264  17.435  1.00 30.76  ? 182 LEU   A CG  1 
ATOM   1407 C  CD1 . LEU   A 1 185 ? -5.698  2.499  17.263  1.00 29.21  ? 182 LEU   A CD1 1 
ATOM   1408 C  CD2 . LEU   A 1 185 ? -7.953  3.557  17.223  1.00 30.45  ? 182 LEU   A CD2 1 
ATOM   1409 N  N   . LYS   A 1 186 ? -6.832  -0.679 19.187  1.00 33.01  ? 183 LYS   A N   1 
ATOM   1410 C  CA  . LYS   A 1 186 ? -7.266  -0.974 20.575  1.00 33.85  ? 183 LYS   A CA  1 
ATOM   1411 C  C   . LYS   A 1 186 ? -7.306  0.325  21.391  1.00 32.59  ? 183 LYS   A C   1 
ATOM   1412 O  O   . LYS   A 1 186 ? -8.241  0.519  22.177  1.00 32.38  ? 183 LYS   A O   1 
ATOM   1413 C  CB  . LYS   A 1 186 ? -6.306  -1.953 21.240  1.00 35.34  ? 183 LYS   A CB  1 
ATOM   1414 C  CG  . LYS   A 1 186 ? -6.871  -2.535 22.532  1.00 36.94  ? 183 LYS   A CG  1 
ATOM   1415 C  CD  . LYS   A 1 186 ? -5.997  -3.594 23.172  1.00 38.58  ? 183 LYS   A CD  1 
ATOM   1416 C  CE  . LYS   A 1 186 ? -6.663  -4.238 24.376  1.00 41.06  ? 183 LYS   A CE  1 
ATOM   1417 N  NZ  . LYS   A 1 186 ? -5.908  -5.410 24.899  1.00 42.48  ? 183 LYS   A NZ  1 
ATOM   1418 N  N   . TYR   A 1 187 ? -6.270  1.147  21.257  1.00 30.48  ? 184 TYR   A N   1 
ATOM   1419 C  CA  . TYR   A 1 187 ? -6.150  2.385  22.055  1.00 29.39  ? 184 TYR   A CA  1 
ATOM   1420 C  C   . TYR   A 1 187 ? -5.905  3.566  21.124  1.00 28.41  ? 184 TYR   A C   1 
ATOM   1421 O  O   . TYR   A 1 187 ? -4.868  3.639  20.472  1.00 29.75  ? 184 TYR   A O   1 
ATOM   1422 C  CB  . TYR   A 1 187 ? -5.066  2.265  23.128  1.00 28.90  ? 184 TYR   A CB  1 
ATOM   1423 C  CG  . TYR   A 1 187 ? -5.249  1.129  24.097  1.00 30.55  ? 184 TYR   A CG  1 
ATOM   1424 C  CD1 . TYR   A 1 187 ? -6.436  0.967  24.812  1.00 32.65  ? 184 TYR   A CD1 1 
ATOM   1425 C  CD2 . TYR   A 1 187 ? -4.257  0.176  24.272  1.00 31.06  ? 184 TYR   A CD2 1 
ATOM   1426 C  CE1 . TYR   A 1 187 ? -6.610  -0.081 25.707  1.00 33.55  ? 184 TYR   A CE1 1 
ATOM   1427 C  CE2 . TYR   A 1 187 ? -4.432  -0.881 25.142  1.00 32.67  ? 184 TYR   A CE2 1 
ATOM   1428 C  CZ  . TYR   A 1 187 ? -5.602  -1.006 25.868  1.00 33.87  ? 184 TYR   A CZ  1 
ATOM   1429 O  OH  . TYR   A 1 187 ? -5.750  -2.064 26.723  1.00 36.00  ? 184 TYR   A OH  1 
ATOM   1430 N  N   . LYS   A 1 188 ? -6.828  4.517  21.121  1.00 28.80  ? 185 LYS   A N   1 
ATOM   1431 C  CA  . LYS   A 1 188 ? -6.612  5.854  20.488  1.00 28.67  ? 185 LYS   A CA  1 
ATOM   1432 C  C   . LYS   A 1 188 ? -5.405  6.514  21.148  1.00 26.87  ? 185 LYS   A C   1 
ATOM   1433 O  O   . LYS   A 1 188 ? -5.129  6.286  22.292  1.00 26.76  ? 185 LYS   A O   1 
ATOM   1434 C  CB  . LYS   A 1 188 ? -7.850  6.744  20.613  1.00 30.25  ? 185 LYS   A CB  1 
ATOM   1435 C  CG  . LYS   A 1 188 ? -9.098  6.143  19.984  1.00 34.42  ? 185 LYS   A CG  1 
ATOM   1436 C  CD  . LYS   A 1 188 ? -10.128 7.117  19.411  1.00 36.52  ? 185 LYS   A CD  1 
ATOM   1437 C  CE  . LYS   A 1 188 ? -10.446 8.344  20.226  1.00 37.65  ? 185 LYS   A CE  1 
ATOM   1438 N  NZ  . LYS   A 1 188 ? -11.867 8.742  20.046  1.00 39.85  ? 185 LYS   A NZ  1 
ATOM   1439 N  N   . PRO   A 1 189 ? -4.629  7.365  20.466  1.00 26.11  ? 186 PRO   A N   1 
ATOM   1440 C  CA  . PRO   A 1 189 ? -3.694  8.228  21.177  1.00 24.50  ? 186 PRO   A CA  1 
ATOM   1441 C  C   . PRO   A 1 189 ? -4.475  9.113  22.171  1.00 23.84  ? 186 PRO   A C   1 
ATOM   1442 O  O   . PRO   A 1 189 ? -5.500  9.707  21.782  1.00 23.46  ? 186 PRO   A O   1 
ATOM   1443 C  CB  . PRO   A 1 189 ? -3.051  9.117  20.116  1.00 24.29  ? 186 PRO   A CB  1 
ATOM   1444 C  CG  . PRO   A 1 189 ? -3.783  8.818  18.825  1.00 26.18  ? 186 PRO   A CG  1 
ATOM   1445 C  CD  . PRO   A 1 189 ? -4.704  7.628  19.027  1.00 26.63  ? 186 PRO   A CD  1 
ATOM   1446 N  N   . VAL   A 1 190 ? -4.017  9.220  23.423  1.00 21.87  ? 187 VAL   A N   1 
ATOM   1447 C  CA  . VAL   A 1 190 ? -4.678  10.153 24.375  1.00 22.00  ? 187 VAL   A CA  1 
ATOM   1448 C  C   . VAL   A 1 190 ? -4.361  11.595 24.012  1.00 20.74  ? 187 VAL   A C   1 
ATOM   1449 O  O   . VAL   A 1 190 ? -5.106  12.450 24.415  1.00 20.24  ? 187 VAL   A O   1 
ATOM   1450 C  CB  . VAL   A 1 190 ? -4.294  9.901  25.848  1.00 22.18  ? 187 VAL   A CB  1 
ATOM   1451 C  CG1 . VAL   A 1 190 ? -4.685  8.484  26.266  1.00 23.01  ? 187 VAL   A CG1 1 
ATOM   1452 C  CG2 . VAL   A 1 190 ? -2.821  10.176 26.101  1.00 21.00  ? 187 VAL   A CG2 1 
ATOM   1453 N  N   . CYS   A 1 191 ? -3.233  11.859 23.370  1.00 20.38  ? 188 CYS   A N   1 
ATOM   1454 C  CA  . CYS   A 1 191 ? -2.816  13.244 23.073  1.00 19.81  ? 188 CYS   A CA  1 
ATOM   1455 C  C   . CYS   A 1 191 ? -1.968  13.295 21.818  1.00 19.55  ? 188 CYS   A C   1 
ATOM   1456 O  O   . CYS   A 1 191 ? -1.472  12.239 21.334  1.00 19.28  ? 188 CYS   A O   1 
ATOM   1457 C  CB  . CYS   A 1 191 ? -2.026  13.861 24.212  1.00 19.81  ? 188 CYS   A CB  1 
ATOM   1458 S  SG  . CYS   A 1 191 ? -0.449  13.005 24.532  1.00 20.67  ? 188 CYS   A SG  1 
ATOM   1459 N  N   . ASN   A 1 192 ? -1.833  14.513 21.300  1.00 18.68  ? 189 ASN   A N   1 
ATOM   1460 C  CA  . ASN   A 1 192 ? -0.823  14.872 20.284  1.00 18.76  ? 189 ASN   A CA  1 
ATOM   1461 C  C   . ASN   A 1 192 ? -0.042  16.074 20.841  1.00 18.03  ? 189 ASN   A C   1 
ATOM   1462 O  O   . ASN   A 1 192 ? -0.675  17.129 21.027  1.00 16.95  ? 189 ASN   A O   1 
ATOM   1463 C  CB  . ASN   A 1 192 ? -1.516  15.176 18.948  1.00 20.06  ? 189 ASN   A CB  1 
ATOM   1464 C  CG  . ASN   A 1 192 ? -0.537  15.384 17.816  1.00 19.99  ? 189 ASN   A CG  1 
ATOM   1465 O  OD1 . ASN   A 1 192 ? 0.657   15.006 17.914  1.00 19.97  ? 189 ASN   A OD1 1 
ATOM   1466 N  ND2 . ASN   A 1 192 ? -1.035  16.040 16.777  1.00 20.46  ? 189 ASN   A ND2 1 
ATOM   1467 N  N   . GLN   A 1 193 ? 1.224   15.872 21.191  1.00 17.82  ? 190 GLN   A N   1 
ATOM   1468 C  CA  . GLN   A 1 193 ? 2.106   16.944 21.717  1.00 17.84  ? 190 GLN   A CA  1 
ATOM   1469 C  C   . GLN   A 1 193 ? 2.777   17.646 20.545  1.00 17.72  ? 190 GLN   A C   1 
ATOM   1470 O  O   . GLN   A 1 193 ? 3.594   17.047 19.844  1.00 19.66  ? 190 GLN   A O   1 
ATOM   1471 C  CB  . GLN   A 1 193 ? 3.135   16.416 22.729  1.00 17.26  ? 190 GLN   A CB  1 
ATOM   1472 C  CG  . GLN   A 1 193 ? 3.895   17.550 23.398  1.00 18.06  ? 190 GLN   A CG  1 
ATOM   1473 C  CD  . GLN   A 1 193 ? 4.996   17.097 24.329  1.00 17.29  ? 190 GLN   A CD  1 
ATOM   1474 O  OE1 . GLN   A 1 193 ? 6.170   17.378 24.079  1.00 18.08  ? 190 GLN   A OE1 1 
ATOM   1475 N  NE2 . GLN   A 1 193 ? 4.643   16.287 25.295  1.00 16.56  ? 190 GLN   A NE2 1 
ATOM   1476 N  N   . VAL   A 1 194 ? 2.440   18.906 20.357  1.00 18.07  ? 191 VAL   A N   1 
ATOM   1477 C  CA  . VAL   A 1 194 ? 2.841   19.676 19.150  1.00 18.93  ? 191 VAL   A CA  1 
ATOM   1478 C  C   . VAL   A 1 194 ? 3.302   21.061 19.588  1.00 18.90  ? 191 VAL   A C   1 
ATOM   1479 O  O   . VAL   A 1 194 ? 2.888   21.541 20.638  1.00 18.54  ? 191 VAL   A O   1 
ATOM   1480 C  CB  . VAL   A 1 194 ? 1.698   19.758 18.118  1.00 19.73  ? 191 VAL   A CB  1 
ATOM   1481 C  CG1 . VAL   A 1 194 ? 1.238   18.355 17.707  1.00 19.64  ? 191 VAL   A CG1 1 
ATOM   1482 C  CG2 . VAL   A 1 194 ? 0.523   20.622 18.560  1.00 20.08  ? 191 VAL   A CG2 1 
ATOM   1483 N  N   . GLU   A 1 195 ? 4.026   21.710 18.695  1.00 19.60  ? 192 GLU   A N   1 
ATOM   1484 C  CA  . GLU   A 1 195 ? 4.433   23.116 18.865  1.00 19.89  ? 192 GLU   A CA  1 
ATOM   1485 C  C   . GLU   A 1 195 ? 3.175   23.975 18.848  1.00 20.56  ? 192 GLU   A C   1 
ATOM   1486 O  O   . GLU   A 1 195 ? 2.441   23.929 17.832  1.00 20.24  ? 192 GLU   A O   1 
ATOM   1487 C  CB  . GLU   A 1 195 ? 5.376   23.587 17.762  1.00 21.19  ? 192 GLU   A CB  1 
ATOM   1488 C  CG  . GLU   A 1 195 ? 5.939   24.964 18.060  1.00 21.86  ? 192 GLU   A CG  1 
ATOM   1489 C  CD  . GLU   A 1 195 ? 6.864   25.550 17.016  1.00 23.41  ? 192 GLU   A CD  1 
ATOM   1490 O  OE1 . GLU   A 1 195 ? 7.449   24.742 16.242  1.00 24.55  ? 192 GLU   A OE1 1 
ATOM   1491 O  OE2 . GLU   A 1 195 ? 7.037   26.803 17.023  1.00 23.96  ? 192 GLU   A OE2 1 
ATOM   1492 N  N   . CYS   A 1 196 ? 2.917   24.718 19.922  1.00 19.49  ? 193 CYS   A N   1 
ATOM   1493 C  CA  . CYS   A 1 196 ? 1.677   25.512 19.986  1.00 20.38  ? 193 CYS   A CA  1 
ATOM   1494 C  C   . CYS   A 1 196 ? 1.890   26.763 20.838  1.00 20.14  ? 193 CYS   A C   1 
ATOM   1495 O  O   . CYS   A 1 196 ? 2.252   26.642 22.019  1.00 18.98  ? 193 CYS   A O   1 
ATOM   1496 C  CB  . CYS   A 1 196 ? 0.550   24.634 20.483  1.00 20.37  ? 193 CYS   A CB  1 
ATOM   1497 S  SG  . CYS   A 1 196 ? -1.037  25.472 20.546  1.00 22.49  ? 193 CYS   A SG  1 
ATOM   1498 N  N   . HIS   A 1 197 ? 1.671   27.947 20.252  1.00 20.42  ? 194 HIS   A N   1 
ATOM   1499 C  CA  . HIS   A 1 197 ? 1.868   29.221 20.978  1.00 20.21  ? 194 HIS   A CA  1 
ATOM   1500 C  C   . HIS   A 1 197 ? 1.126   30.258 20.169  1.00 21.39  ? 194 HIS   A C   1 
ATOM   1501 O  O   . HIS   A 1 197 ? 0.629   29.925 19.107  1.00 21.36  ? 194 HIS   A O   1 
ATOM   1502 C  CB  . HIS   A 1 197 ? 3.367   29.532 21.130  1.00 20.08  ? 194 HIS   A CB  1 
ATOM   1503 C  CG  . HIS   A 1 197 ? 4.121   29.390 19.850  1.00 20.32  ? 194 HIS   A CG  1 
ATOM   1504 N  ND1 . HIS   A 1 197 ? 3.926   30.238 18.747  1.00 21.12  ? 194 HIS   A ND1 1 
ATOM   1505 C  CD2 . HIS   A 1 197 ? 4.925   28.385 19.414  1.00 20.06  ? 194 HIS   A CD2 1 
ATOM   1506 C  CE1 . HIS   A 1 197 ? 4.711   29.828 17.777  1.00 21.89  ? 194 HIS   A CE1 1 
ATOM   1507 N  NE2 . HIS   A 1 197 ? 5.315   28.664 18.137  1.00 20.41  ? 194 HIS   A NE2 1 
ATOM   1508 N  N   . PRO   A 1 198 ? 0.987   31.501 20.655  1.00 22.10  ? 195 PRO   A N   1 
ATOM   1509 C  CA  . PRO   A 1 198 ? 0.198   32.470 19.922  1.00 23.50  ? 195 PRO   A CA  1 
ATOM   1510 C  C   . PRO   A 1 198 ? 0.638   32.803 18.495  1.00 24.86  ? 195 PRO   A C   1 
ATOM   1511 O  O   . PRO   A 1 198 ? -0.181  33.352 17.802  1.00 26.01  ? 195 PRO   A O   1 
ATOM   1512 C  CB  . PRO   A 1 198 ? 0.291   33.737 20.765  1.00 24.41  ? 195 PRO   A CB  1 
ATOM   1513 C  CG  . PRO   A 1 198 ? 0.444   33.168 22.165  1.00 23.38  ? 195 PRO   A CG  1 
ATOM   1514 C  CD  . PRO   A 1 198 ? 1.364   31.977 21.989  1.00 22.34  ? 195 PRO   A CD  1 
ATOM   1515 N  N   . TYR   A 1 199 ? 1.874   32.502 18.098  1.00 24.66  ? 196 TYR   A N   1 
ATOM   1516 C  CA  . TYR   A 1 199 ? 2.303   32.730 16.700  1.00 25.21  ? 196 TYR   A CA  1 
ATOM   1517 C  C   . TYR   A 1 199 ? 2.045   31.482 15.836  1.00 25.15  ? 196 TYR   A C   1 
ATOM   1518 O  O   . TYR   A 1 199 ? 2.202   31.572 14.590  1.00 25.48  ? 196 TYR   A O   1 
ATOM   1519 C  CB  . TYR   A 1 199 ? 3.760   33.153 16.657  1.00 25.63  ? 196 TYR   A CB  1 
ATOM   1520 C  CG  . TYR   A 1 199 ? 4.066   34.509 17.231  1.00 26.73  ? 196 TYR   A CG  1 
ATOM   1521 C  CD1 . TYR   A 1 199 ? 3.095   35.473 17.448  1.00 28.09  ? 196 TYR   A CD1 1 
ATOM   1522 C  CD2 . TYR   A 1 199 ? 5.379   34.849 17.453  1.00 27.43  ? 196 TYR   A CD2 1 
ATOM   1523 C  CE1 . TYR   A 1 199 ? 3.431   36.745 17.889  1.00 29.13  ? 196 TYR   A CE1 1 
ATOM   1524 C  CE2 . TYR   A 1 199 ? 5.732   36.110 17.912  1.00 28.89  ? 196 TYR   A CE2 1 
ATOM   1525 C  CZ  . TYR   A 1 199 ? 4.754   37.062 18.135  1.00 29.57  ? 196 TYR   A CZ  1 
ATOM   1526 O  OH  . TYR   A 1 199 ? 5.093   38.310 18.589  1.00 32.01  ? 196 TYR   A OH  1 
ATOM   1527 N  N   . PHE   A 1 200 ? 1.601   30.388 16.458  1.00 24.19  ? 197 PHE   A N   1 
ATOM   1528 C  CA  . PHE   A 1 200 ? 1.272   29.104 15.789  1.00 24.12  ? 197 PHE   A CA  1 
ATOM   1529 C  C   . PHE   A 1 200 ? 0.237   28.353 16.641  1.00 24.02  ? 197 PHE   A C   1 
ATOM   1530 O  O   . PHE   A 1 200 ? 0.600   27.428 17.379  1.00 23.30  ? 197 PHE   A O   1 
ATOM   1531 C  CB  . PHE   A 1 200 ? 2.584   28.352 15.557  1.00 24.65  ? 197 PHE   A CB  1 
ATOM   1532 C  CG  . PHE   A 1 200 ? 2.534   27.126 14.673  1.00 25.05  ? 197 PHE   A CG  1 
ATOM   1533 C  CD1 . PHE   A 1 200 ? 1.637   27.039 13.638  1.00 26.45  ? 197 PHE   A CD1 1 
ATOM   1534 C  CD2 . PHE   A 1 200 ? 3.410   26.064 14.884  1.00 25.93  ? 197 PHE   A CD2 1 
ATOM   1535 C  CE1 . PHE   A 1 200 ? 1.615   25.926 12.812  1.00 26.90  ? 197 PHE   A CE1 1 
ATOM   1536 C  CE2 . PHE   A 1 200 ? 3.427   24.974 14.027  1.00 26.55  ? 197 PHE   A CE2 1 
ATOM   1537 C  CZ  . PHE   A 1 200 ? 2.532   24.917 12.983  1.00 27.05  ? 197 PHE   A CZ  1 
ATOM   1538 N  N   . ASN   A 1 201 ? -1.022  28.781 16.596  1.00 23.84  ? 198 ASN   A N   1 
ATOM   1539 C  CA  . ASN   A 1 201 ? -2.003  28.457 17.656  1.00 23.16  ? 198 ASN   A CA  1 
ATOM   1540 C  C   . ASN   A 1 201 ? -2.687  27.128 17.325  1.00 23.10  ? 198 ASN   A C   1 
ATOM   1541 O  O   . ASN   A 1 201 ? -3.384  26.574 18.226  1.00 22.48  ? 198 ASN   A O   1 
ATOM   1542 C  CB  . ASN   A 1 201 ? -2.895  29.671 17.933  1.00 24.38  ? 198 ASN   A CB  1 
ATOM   1543 C  CG  . ASN   A 1 201 ? -4.000  29.900 16.933  1.00 26.04  ? 198 ASN   A CG  1 
ATOM   1544 O  OD1 . ASN   A 1 201 ? -4.403  28.984 16.204  1.00 26.65  ? 198 ASN   A OD1 1 
ATOM   1545 N  ND2 . ASN   A 1 201 ? -4.467  31.145 16.890  1.00 27.48  ? 198 ASN   A ND2 1 
ATOM   1546 N  N   . ARG   A 1 202 ? -2.437  26.608 16.118  1.00 23.07  ? 199 ARG   A N   1 
ATOM   1547 C  CA  . ARG   A 1 202 ? -2.920  25.264 15.700  1.00 23.80  ? 199 ARG   A CA  1 
ATOM   1548 C  C   . ARG   A 1 202 ? -4.428  25.155 15.929  1.00 23.98  ? 199 ARG   A C   1 
ATOM   1549 O  O   . ARG   A 1 202 ? -4.878  24.093 16.402  1.00 24.27  ? 199 ARG   A O   1 
ATOM   1550 C  CB  . ARG   A 1 202 ? -2.170  24.168 16.464  1.00 23.27  ? 199 ARG   A CB  1 
ATOM   1551 C  CG  . ARG   A 1 202 ? -0.714  24.499 16.756  1.00 22.87  ? 199 ARG   A CG  1 
ATOM   1552 C  CD  . ARG   A 1 202 ? 0.135   24.535 15.499  1.00 23.44  ? 199 ARG   A CD  1 
ATOM   1553 N  NE  . ARG   A 1 202 ? 0.071   23.287 14.751  1.00 23.61  ? 199 ARG   A NE  1 
ATOM   1554 C  CZ  . ARG   A 1 202 ? 1.006   22.345 14.778  1.00 23.55  ? 199 ARG   A CZ  1 
ATOM   1555 N  NH1 . ARG   A 1 202 ? 2.088   22.508 15.521  1.00 22.92  ? 199 ARG   A NH1 1 
ATOM   1556 N  NH2 . ARG   A 1 202 ? 0.858   21.245 14.063  1.00 23.02  ? 199 ARG   A NH2 1 
ATOM   1557 N  N   . SER   A 1 203 ? -5.170  26.214 15.606  1.00 24.61  ? 200 SER   A N   1 
ATOM   1558 C  CA  . SER   A 1 203 ? -6.647  26.197 15.807  1.00 26.46  ? 200 SER   A CA  1 
ATOM   1559 C  C   . SER   A 1 203 ? -7.306  25.038 15.029  1.00 26.25  ? 200 SER   A C   1 
ATOM   1560 O  O   . SER   A 1 203 ? -8.152  24.348 15.592  1.00 25.04  ? 200 SER   A O   1 
ATOM   1561 C  CB  . SER   A 1 203 ? -7.300  27.530 15.472  1.00 28.61  ? 200 SER   A CB  1 
ATOM   1562 O  OG  . SER   A 1 203 ? -7.072  27.850 14.104  1.00 31.86  ? 200 SER   A OG  1 
ATOM   1563 N  N   . LYS   A 1 204 ? -6.959  24.791 13.784  1.00 27.13  ? 201 LYS   A N   1 
ATOM   1564 C  CA  . LYS   A 1 204 ? -7.665  23.714 13.027  1.00 28.39  ? 201 LYS   A CA  1 
ATOM   1565 C  C   . LYS   A 1 204 ? -7.339  22.319 13.577  1.00 26.30  ? 201 LYS   A C   1 
ATOM   1566 O  O   . LYS   A 1 204 ? -8.262  21.454 13.693  1.00 25.66  ? 201 LYS   A O   1 
ATOM   1567 C  CB  . LYS   A 1 204 ? -7.302  23.773 11.546  1.00 31.49  ? 201 LYS   A CB  1 
ATOM   1568 C  CG  . LYS   A 1 204 ? -7.914  24.975 10.846  1.00 35.55  ? 201 LYS   A CG  1 
ATOM   1569 C  CD  . LYS   A 1 204 ? -7.685  24.933 9.366   1.00 38.73  ? 201 LYS   A CD  1 
ATOM   1570 C  CE  . LYS   A 1 204 ? -8.195  26.182 8.690   1.00 43.22  ? 201 LYS   A CE  1 
ATOM   1571 N  NZ  . LYS   A 1 204 ? -8.125  26.056 7.216   1.00 45.57  ? 201 LYS   A NZ  1 
ATOM   1572 N  N   . LEU   A 1 205 ? -6.069  22.077 13.855  1.00 24.46  ? 202 LEU   A N   1 
ATOM   1573 C  CA  . LEU   A 1 205 ? -5.624  20.769 14.408  1.00 23.91  ? 202 LEU   A CA  1 
ATOM   1574 C  C   . LEU   A 1 205 ? -6.255  20.582 15.794  1.00 23.66  ? 202 LEU   A C   1 
ATOM   1575 O  O   . LEU   A 1 205 ? -6.649  19.447 16.147  1.00 23.82  ? 202 LEU   A O   1 
ATOM   1576 C  CB  . LEU   A 1 205 ? -4.107  20.739 14.500  1.00 22.46  ? 202 LEU   A CB  1 
ATOM   1577 C  CG  . LEU   A 1 205 ? -3.524  19.474 15.119  1.00 21.57  ? 202 LEU   A CG  1 
ATOM   1578 C  CD1 . LEU   A 1 205 ? -3.873  18.281 14.281  1.00 22.53  ? 202 LEU   A CD1 1 
ATOM   1579 C  CD2 . LEU   A 1 205 ? -2.007  19.584 15.255  1.00 20.86  ? 202 LEU   A CD2 1 
ATOM   1580 N  N   . LEU   A 1 206 ? -6.340  21.674 16.569  1.00 23.62  ? 203 LEU   A N   1 
ATOM   1581 C  CA  . LEU   A 1 206 ? -6.988  21.634 17.907  1.00 23.59  ? 203 LEU   A CA  1 
ATOM   1582 C  C   . LEU   A 1 206 ? -8.433  21.151 17.771  1.00 24.61  ? 203 LEU   A C   1 
ATOM   1583 O  O   . LEU   A 1 206 ? -8.842  20.235 18.447  1.00 23.68  ? 203 LEU   A O   1 
ATOM   1584 C  CB  . LEU   A 1 206 ? -6.935  23.014 18.574  1.00 23.59  ? 203 LEU   A CB  1 
ATOM   1585 C  CG  . LEU   A 1 206 ? -7.670  23.104 19.911  1.00 23.43  ? 203 LEU   A CG  1 
ATOM   1586 C  CD1 . LEU   A 1 206 ? -7.129  22.048 20.866  1.00 22.62  ? 203 LEU   A CD1 1 
ATOM   1587 C  CD2 . LEU   A 1 206 ? -7.526  24.496 20.526  1.00 23.75  ? 203 LEU   A CD2 1 
ATOM   1588 N  N   . ASP   A 1 207 ? -9.208  21.776 16.910  1.00 26.56  ? 204 ASP   A N   1 
ATOM   1589 C  CA  . ASP   A 1 207 ? -10.612 21.375 16.660  1.00 29.17  ? 204 ASP   A CA  1 
ATOM   1590 C  C   . ASP   A 1 207 ? -10.692 19.906 16.245  1.00 28.54  ? 204 ASP   A C   1 
ATOM   1591 O  O   . ASP   A 1 207 ? -11.604 19.221 16.708  1.00 28.38  ? 204 ASP   A O   1 
ATOM   1592 C  CB  . ASP   A 1 207 ? -11.251 22.283 15.607  1.00 33.06  ? 204 ASP   A CB  1 
ATOM   1593 C  CG  . ASP   A 1 207 ? -11.562 23.653 16.186  1.00 36.86  ? 204 ASP   A CG  1 
ATOM   1594 O  OD1 . ASP   A 1 207 ? -11.571 23.769 17.441  1.00 39.14  ? 204 ASP   A OD1 1 
ATOM   1595 O  OD2 . ASP   A 1 207 ? -11.833 24.587 15.394  1.00 40.22  ? 204 ASP   A OD2 1 
ATOM   1596 N  N   . PHE   A 1 208 ? -9.819  19.476 15.340  1.00 27.69  ? 205 PHE   A N   1 
ATOM   1597 C  CA  . PHE   A 1 208 ? -9.744  18.082 14.883  1.00 27.47  ? 205 PHE   A CA  1 
ATOM   1598 C  C   . PHE   A 1 208 ? -9.479  17.172 16.093  1.00 26.71  ? 205 PHE   A C   1 
ATOM   1599 O  O   . PHE   A 1 208 ? -10.213 16.187 16.303  1.00 25.97  ? 205 PHE   A O   1 
ATOM   1600 C  CB  . PHE   A 1 208 ? -8.645  17.910 13.843  1.00 27.80  ? 205 PHE   A CB  1 
ATOM   1601 C  CG  . PHE   A 1 208 ? -8.499  16.467 13.431  1.00 28.67  ? 205 PHE   A CG  1 
ATOM   1602 C  CD1 . PHE   A 1 208 ? -9.427  15.900 12.568  1.00 30.45  ? 205 PHE   A CD1 1 
ATOM   1603 C  CD2 . PHE   A 1 208 ? -7.495  15.666 13.965  1.00 28.44  ? 205 PHE   A CD2 1 
ATOM   1604 C  CE1 . PHE   A 1 208 ? -9.346  14.559 12.246  1.00 31.11  ? 205 PHE   A CE1 1 
ATOM   1605 C  CE2 . PHE   A 1 208 ? -7.392  14.333 13.597  1.00 29.45  ? 205 PHE   A CE2 1 
ATOM   1606 C  CZ  . PHE   A 1 208 ? -8.313  13.790 12.724  1.00 30.79  ? 205 PHE   A CZ  1 
ATOM   1607 N  N   . CYS   A 1 209 ? -8.464  17.502 16.893  1.00 24.99  ? 206 CYS   A N   1 
ATOM   1608 C  CA  . CYS   A 1 209 ? -8.147  16.681 18.098  1.00 25.45  ? 206 CYS   A CA  1 
ATOM   1609 C  C   . CYS   A 1 209 ? -9.352  16.679 19.034  1.00 25.25  ? 206 CYS   A C   1 
ATOM   1610 O  O   . CYS   A 1 209 ? -9.721  15.633 19.473  1.00 25.76  ? 206 CYS   A O   1 
ATOM   1611 C  CB  . CYS   A 1 209 ? -6.911  17.185 18.822  1.00 24.53  ? 206 CYS   A CB  1 
ATOM   1612 S  SG  . CYS   A 1 209 ? -5.391  16.830 17.916  1.00 26.08  ? 206 CYS   A SG  1 
ATOM   1613 N  N   . LYS   A 1 210 ? -9.986  17.823 19.285  1.00 26.80  ? 207 LYS   A N   1 
ATOM   1614 C  CA  . LYS   A 1 210 ? -11.188 17.868 20.150  1.00 27.67  ? 207 LYS   A CA  1 
ATOM   1615 C  C   . LYS   A 1 210 ? -12.232 16.909 19.591  1.00 29.02  ? 207 LYS   A C   1 
ATOM   1616 O  O   . LYS   A 1 210 ? -12.760 16.150 20.385  1.00 28.69  ? 207 LYS   A O   1 
ATOM   1617 C  CB  . LYS   A 1 210 ? -11.728 19.286 20.244  1.00 29.89  ? 207 LYS   A CB  1 
ATOM   1618 C  CG  . LYS   A 1 210 ? -10.904 20.164 21.163  1.00 30.70  ? 207 LYS   A CG  1 
ATOM   1619 C  CD  . LYS   A 1 210 ? -11.388 21.586 21.245  1.00 32.90  ? 207 LYS   A CD  1 
ATOM   1620 C  CE  . LYS   A 1 210 ? -10.526 22.296 22.259  1.00 34.21  ? 207 LYS   A CE  1 
ATOM   1621 N  NZ  . LYS   A 1 210 ? -10.922 23.701 22.427  1.00 37.48  ? 207 LYS   A NZ  1 
ATOM   1622 N  N   . SER   A 1 211 ? -12.470 16.911 18.271  1.00 29.74  ? 208 SER   A N   1 
ATOM   1623 C  CA  . SER   A 1 211 ? -13.565 16.095 17.677  1.00 32.42  ? 208 SER   A CA  1 
ATOM   1624 C  C   . SER   A 1 211 ? -13.279 14.595 17.869  1.00 32.55  ? 208 SER   A C   1 
ATOM   1625 O  O   . SER   A 1 211 ? -14.233 13.835 17.762  1.00 33.85  ? 208 SER   A O   1 
ATOM   1626 C  CB  . SER   A 1 211 ? -13.806 16.405 16.207  1.00 33.50  ? 208 SER   A CB  1 
ATOM   1627 O  OG  . SER   A 1 211 ? -12.697 15.998 15.434  1.00 33.05  ? 208 SER   A OG  1 
ATOM   1628 N  N   . LYS   A 1 212 ? -12.021 14.203 18.064  1.00 31.32  ? 209 LYS   A N   1 
ATOM   1629 C  CA  . LYS   A 1 212 ? -11.555 12.788 18.197  1.00 32.73  ? 209 LYS   A CA  1 
ATOM   1630 C  C   . LYS   A 1 212 ? -11.250 12.445 19.659  1.00 31.50  ? 209 LYS   A C   1 
ATOM   1631 O  O   . LYS   A 1 212 ? -10.709 11.368 19.881  1.00 30.74  ? 209 LYS   A O   1 
ATOM   1632 C  CB  . LYS   A 1 212 ? -10.310 12.561 17.331  1.00 32.29  ? 209 LYS   A CB  1 
ATOM   1633 C  CG  . LYS   A 1 212 ? -10.510 12.873 15.851  1.00 34.77  ? 209 LYS   A CG  1 
ATOM   1634 C  CD  . LYS   A 1 212 ? -11.659 12.042 15.245  1.00 37.87  ? 209 LYS   A CD  1 
ATOM   1635 C  CE  . LYS   A 1 212 ? -11.765 12.269 13.751  1.00 39.83  ? 209 LYS   A CE  1 
ATOM   1636 N  NZ  . LYS   A 1 212 ? -12.877 11.499 13.160  1.00 43.27  ? 209 LYS   A NZ  1 
ATOM   1637 N  N   . ASP   A 1 213 ? -11.535 13.361 20.589  1.00 32.36  ? 210 ASP   A N   1 
ATOM   1638 C  CA  . ASP   A 1 213 ? -11.241 13.254 22.047  1.00 32.54  ? 210 ASP   A CA  1 
ATOM   1639 C  C   . ASP   A 1 213 ? -9.746  12.991 22.272  1.00 29.02  ? 210 ASP   A C   1 
ATOM   1640 O  O   . ASP   A 1 213 ? -9.368  12.207 23.152  1.00 28.27  ? 210 ASP   A O   1 
ATOM   1641 C  CB  . ASP   A 1 213 ? -12.129 12.194 22.701  1.00 36.98  ? 210 ASP   A CB  1 
ATOM   1642 C  CG  . ASP   A 1 213 ? -12.118 12.226 24.219  1.00 38.85  ? 210 ASP   A CG  1 
ATOM   1643 O  OD1 . ASP   A 1 213 ? -11.876 13.303 24.791  1.00 42.12  ? 210 ASP   A OD1 1 
ATOM   1644 O  OD2 . ASP   A 1 213 ? -12.405 11.174 24.817  1.00 44.87  ? 210 ASP   A OD2 1 
ATOM   1645 N  N   . ILE   A 1 214 ? -8.905  13.648 21.489  1.00 26.33  ? 211 ILE   A N   1 
ATOM   1646 C  CA  . ILE   A 1 214 ? -7.425  13.660 21.677  1.00 24.40  ? 211 ILE   A CA  1 
ATOM   1647 C  C   . ILE   A 1 214 ? -7.050  15.018 22.248  1.00 23.76  ? 211 ILE   A C   1 
ATOM   1648 O  O   . ILE   A 1 214 ? -7.518  16.031 21.678  1.00 23.25  ? 211 ILE   A O   1 
ATOM   1649 C  CB  . ILE   A 1 214 ? -6.722  13.472 20.329  1.00 24.38  ? 211 ILE   A CB  1 
ATOM   1650 C  CG1 . ILE   A 1 214 ? -7.075  12.116 19.726  1.00 25.48  ? 211 ILE   A CG1 1 
ATOM   1651 C  CG2 . ILE   A 1 214 ? -5.214  13.679 20.459  1.00 23.27  ? 211 ILE   A CG2 1 
ATOM   1652 C  CD1 . ILE   A 1 214 ? -6.642  12.002 18.296  1.00 26.04  ? 211 ILE   A CD1 1 
ATOM   1653 N  N   . VAL   A 1 215 ? -6.272  15.012 23.333  1.00 21.91  ? 212 VAL   A N   1 
ATOM   1654 C  CA  . VAL   A 1 215 ? -5.791  16.258 23.960  1.00 21.38  ? 212 VAL   A CA  1 
ATOM   1655 C  C   . VAL   A 1 215 ? -4.647  16.807 23.122  1.00 20.86  ? 212 VAL   A C   1 
ATOM   1656 O  O   . VAL   A 1 215 ? -3.717  16.070 22.880  1.00 20.32  ? 212 VAL   A O   1 
ATOM   1657 C  CB  . VAL   A 1 215 ? -5.318  15.992 25.401  1.00 20.80  ? 212 VAL   A CB  1 
ATOM   1658 C  CG1 . VAL   A 1 215 ? -4.660  17.236 25.971  1.00 19.76  ? 212 VAL   A CG1 1 
ATOM   1659 C  CG2 . VAL   A 1 215 ? -6.514  15.525 26.243  1.00 21.54  ? 212 VAL   A CG2 1 
ATOM   1660 N  N   . LEU   A 1 216 ? -4.670  18.109 22.840  1.00 20.60  ? 213 LEU   A N   1 
ATOM   1661 C  CA  . LEU   A 1 216 ? -3.509  18.794 22.238  1.00 21.03  ? 213 LEU   A CA  1 
ATOM   1662 C  C   . LEU   A 1 216 ? -2.625  19.244 23.400  1.00 20.66  ? 213 LEU   A C   1 
ATOM   1663 O  O   . LEU   A 1 216 ? -3.116  20.012 24.270  1.00 21.61  ? 213 LEU   A O   1 
ATOM   1664 C  CB  . LEU   A 1 216 ? -3.957  19.974 21.370  1.00 22.11  ? 213 LEU   A CB  1 
ATOM   1665 C  CG  . LEU   A 1 216 ? -2.880  20.430 20.392  1.00 23.07  ? 213 LEU   A CG  1 
ATOM   1666 C  CD1 . LEU   A 1 216 ? -3.442  21.003 19.103  1.00 25.13  ? 213 LEU   A CD1 1 
ATOM   1667 C  CD2 . LEU   A 1 216 ? -1.944  21.452 21.043  1.00 24.04  ? 213 LEU   A CD2 1 
ATOM   1668 N  N   . VAL   A 1 217 ? -1.352  18.853 23.409  1.00 18.80  ? 214 VAL   A N   1 
ATOM   1669 C  CA  . VAL   A 1 217 ? -0.405  19.330 24.438  1.00 17.52  ? 214 VAL   A CA  1 
ATOM   1670 C  C   . VAL   A 1 217 ? 0.579   20.262 23.777  1.00 17.61  ? 214 VAL   A C   1 
ATOM   1671 O  O   . VAL   A 1 217 ? 1.215   19.857 22.817  1.00 18.16  ? 214 VAL   A O   1 
ATOM   1672 C  CB  . VAL   A 1 217 ? 0.326   18.160 25.096  1.00 17.38  ? 214 VAL   A CB  1 
ATOM   1673 C  CG1 . VAL   A 1 217 ? 1.365   18.654 26.071  1.00 17.10  ? 214 VAL   A CG1 1 
ATOM   1674 C  CG2 . VAL   A 1 217 ? -0.636  17.204 25.763  1.00 17.73  ? 214 VAL   A CG2 1 
ATOM   1675 N  N   . ALA   A 1 218 ? 0.647   21.498 24.272  1.00 16.85  ? 215 ALA   A N   1 
ATOM   1676 C  CA  . ALA   A 1 218 ? 1.480   22.550 23.680  1.00 16.75  ? 215 ALA   A CA  1 
ATOM   1677 C  C   . ALA   A 1 218 ? 2.915   22.521 24.202  1.00 16.53  ? 215 ALA   A C   1 
ATOM   1678 O  O   . ALA   A 1 218 ? 3.130   22.685 25.462  1.00 17.22  ? 215 ALA   A O   1 
ATOM   1679 C  CB  . ALA   A 1 218 ? 0.842   23.895 23.976  1.00 17.32  ? 215 ALA   A CB  1 
ATOM   1680 N  N   . TYR   A 1 219 ? 3.860   22.418 23.260  1.00 16.25  ? 216 TYR   A N   1 
ATOM   1681 C  CA  . TYR   A 1 219 ? 5.279   22.677 23.554  1.00 17.08  ? 216 TYR   A CA  1 
ATOM   1682 C  C   . TYR   A 1 219 ? 5.688   24.006 22.928  1.00 17.89  ? 216 TYR   A C   1 
ATOM   1683 O  O   . TYR   A 1 219 ? 5.025   24.439 21.982  1.00 18.70  ? 216 TYR   A O   1 
ATOM   1684 C  CB  . TYR   A 1 219 ? 6.178   21.494 23.227  1.00 17.07  ? 216 TYR   A CB  1 
ATOM   1685 C  CG  . TYR   A 1 219 ? 6.533   21.228 21.794  1.00 16.77  ? 216 TYR   A CG  1 
ATOM   1686 C  CD1 . TYR   A 1 219 ? 7.359   22.059 21.084  1.00 17.69  ? 216 TYR   A CD1 1 
ATOM   1687 C  CD2 . TYR   A 1 219 ? 6.114   20.048 21.188  1.00 17.90  ? 216 TYR   A CD2 1 
ATOM   1688 C  CE1 . TYR   A 1 219 ? 7.704   21.765 19.769  1.00 18.32  ? 216 TYR   A CE1 1 
ATOM   1689 C  CE2 . TYR   A 1 219 ? 6.460   19.724 19.886  1.00 18.02  ? 216 TYR   A CE2 1 
ATOM   1690 C  CZ  . TYR   A 1 219 ? 7.292   20.574 19.192  1.00 18.77  ? 216 TYR   A CZ  1 
ATOM   1691 O  OH  . TYR   A 1 219 ? 7.612   20.276 17.915  1.00 19.05  ? 216 TYR   A OH  1 
ATOM   1692 N  N   . SER   A 1 220 ? 6.794   24.580 23.411  1.00 18.16  ? 217 SER   A N   1 
ATOM   1693 C  CA  . SER   A 1 220 ? 7.292   25.929 23.020  1.00 19.01  ? 217 SER   A CA  1 
ATOM   1694 C  C   . SER   A 1 220 ? 6.140   26.939 23.183  1.00 18.66  ? 217 SER   A C   1 
ATOM   1695 O  O   . SER   A 1 220 ? 6.079   27.957 22.418  1.00 18.84  ? 217 SER   A O   1 
ATOM   1696 C  CB  . SER   A 1 220 ? 7.903   25.905 21.620  1.00 19.97  ? 217 SER   A CB  1 
ATOM   1697 O  OG  . SER   A 1 220 ? 8.964   24.936 21.580  1.00 19.81  ? 217 SER   A OG  1 
ATOM   1698 N  N   . ALA   A 1 221 ? 5.325   26.748 24.235  1.00 18.03  ? 218 ALA   A N   1 
ATOM   1699 C  CA  . ALA   A 1 221 ? 4.158   27.602 24.533  1.00 18.21  ? 218 ALA   A CA  1 
ATOM   1700 C  C   . ALA   A 1 221 ? 4.612   28.991 24.964  1.00 19.08  ? 218 ALA   A C   1 
ATOM   1701 O  O   . ALA   A 1 221 ? 3.813   29.879 24.906  1.00 19.77  ? 218 ALA   A O   1 
ATOM   1702 C  CB  . ALA   A 1 221 ? 3.292   26.991 25.609  1.00 17.73  ? 218 ALA   A CB  1 
ATOM   1703 N  N   . LEU   A 1 222 ? 5.869   29.156 25.328  1.00 19.67  ? 219 LEU   A N   1 
ATOM   1704 C  CA  . LEU   A 1 222 ? 6.453   30.472 25.701  1.00 21.42  ? 219 LEU   A CA  1 
ATOM   1705 C  C   . LEU   A 1 222 ? 7.438   30.911 24.632  1.00 21.98  ? 219 LEU   A C   1 
ATOM   1706 O  O   . LEU   A 1 222 ? 8.121   31.920 24.862  1.00 22.85  ? 219 LEU   A O   1 
ATOM   1707 C  CB  . LEU   A 1 222 ? 7.172   30.383 27.048  1.00 21.87  ? 219 LEU   A CB  1 
ATOM   1708 C  CG  . LEU   A 1 222 ? 6.312   29.891 28.210  1.00 22.13  ? 219 LEU   A CG  1 
ATOM   1709 C  CD1 . LEU   A 1 222 ? 7.135   29.862 29.490  1.00 22.68  ? 219 LEU   A CD1 1 
ATOM   1710 C  CD2 . LEU   A 1 222 ? 5.102   30.765 28.408  1.00 22.90  ? 219 LEU   A CD2 1 
ATOM   1711 N  N   . GLY   A 1 223 ? 7.455   30.224 23.490  1.00 21.92  ? 220 GLY   A N   1 
ATOM   1712 C  CA  . GLY   A 1 223 ? 8.153   30.776 22.315  1.00 22.20  ? 220 GLY   A CA  1 
ATOM   1713 C  C   . GLY   A 1 223 ? 9.492   30.136 22.110  1.00 22.36  ? 220 GLY   A C   1 
ATOM   1714 O  O   . GLY   A 1 223 ? 10.263  30.603 21.255  1.00 23.26  ? 220 GLY   A O   1 
ATOM   1715 N  N   . SER   A 1 224 ? 9.742   29.043 22.837  1.00 21.84  ? 221 SER   A N   1 
ATOM   1716 C  CA  . SER   A 1 224 ? 10.978  28.248 22.710  1.00 22.08  ? 221 SER   A CA  1 
ATOM   1717 C  C   . SER   A 1 224 ? 12.142  28.976 23.367  1.00 22.98  ? 221 SER   A C   1 
ATOM   1718 O  O   . SER   A 1 224 ? 12.052  30.169 23.738  1.00 23.70  ? 221 SER   A O   1 
ATOM   1719 C  CB  . SER   A 1 224 ? 11.344  27.927 21.285  1.00 22.64  ? 221 SER   A CB  1 
ATOM   1720 O  OG  . SER   A 1 224 ? 12.103  28.984 20.710  1.00 24.04  ? 221 SER   A OG  1 
ATOM   1721 N  N   . GLN   A 1 225 ? 13.185  28.188 23.542  1.00 23.80  ? 222 GLN   A N   1 
ATOM   1722 C  CA  . GLN   A 1 225 ? 14.474  28.572 24.162  1.00 24.98  ? 222 GLN   A CA  1 
ATOM   1723 C  C   . GLN   A 1 225 ? 15.301  29.319 23.118  1.00 27.37  ? 222 GLN   A C   1 
ATOM   1724 O  O   . GLN   A 1 225 ? 16.368  29.815 23.461  1.00 27.27  ? 222 GLN   A O   1 
ATOM   1725 C  CB  . GLN   A 1 225 ? 15.164  27.306 24.666  1.00 24.39  ? 222 GLN   A CB  1 
ATOM   1726 C  CG  . GLN   A 1 225 ? 14.322  26.519 25.679  1.00 23.84  ? 222 GLN   A CG  1 
ATOM   1727 C  CD  . GLN   A 1 225 ? 15.044  25.486 26.522  1.00 24.14  ? 222 GLN   A CD  1 
ATOM   1728 O  OE1 . GLN   A 1 225 ? 16.153  25.752 26.990  1.00 25.89  ? 222 GLN   A OE1 1 
ATOM   1729 N  NE2 . GLN   A 1 225 ? 14.371  24.367 26.815  1.00 21.65  ? 222 GLN   A NE2 1 
ATOM   1730 N  N   . ARG   A 1 226 ? 14.849  29.344 21.864  1.00 28.91  ? 223 ARG   A N   1 
ATOM   1731 C  CA  . ARG   A 1 226 ? 15.529  30.098 20.772  1.00 32.01  ? 223 ARG   A CA  1 
ATOM   1732 C  C   . ARG   A 1 226 ? 16.980  29.656 20.650  1.00 34.29  ? 223 ARG   A C   1 
ATOM   1733 O  O   . ARG   A 1 226 ? 17.853  30.499 20.379  1.00 36.01  ? 223 ARG   A O   1 
ATOM   1734 C  CB  . ARG   A 1 226 ? 15.371  31.598 21.015  1.00 33.76  ? 223 ARG   A CB  1 
ATOM   1735 C  CG  . ARG   A 1 226 ? 13.910  32.024 21.128  1.00 32.67  ? 223 ARG   A CG  1 
ATOM   1736 C  CD  . ARG   A 1 226 ? 13.830  33.520 21.334  1.00 33.58  ? 223 ARG   A CD  1 
ATOM   1737 N  NE  . ARG   A 1 226 ? 14.410  34.195 20.191  1.00 34.58  ? 223 ARG   A NE  1 
ATOM   1738 C  CZ  . ARG   A 1 226 ? 13.794  34.383 19.027  1.00 33.96  ? 223 ARG   A CZ  1 
ATOM   1739 N  NH1 . ARG   A 1 226 ? 12.557  33.967 18.836  1.00 32.07  ? 223 ARG   A NH1 1 
ATOM   1740 N  NH2 . ARG   A 1 226 ? 14.435  34.980 18.044  1.00 35.61  ? 223 ARG   A NH2 1 
ATOM   1741 N  N   . ASP   A 1 227 ? 17.231  28.359 20.746  1.00 35.33  ? 224 ASP   A N   1 
ATOM   1742 C  CA  A ASP   A 1 227 ? 18.582  27.802 20.485  0.60 37.44  ? 224 ASP   A CA  1 
ATOM   1743 C  CA  B ASP   A 1 227 ? 18.588  27.809 20.488  0.40 37.71  ? 224 ASP   A CA  1 
ATOM   1744 C  C   . ASP   A 1 227 ? 18.924  27.993 19.000  1.00 38.74  ? 224 ASP   A C   1 
ATOM   1745 O  O   . ASP   A 1 227 ? 18.151  27.517 18.162  1.00 38.14  ? 224 ASP   A O   1 
ATOM   1746 C  CB  A ASP   A 1 227 ? 18.649  26.332 20.890  0.60 36.86  ? 224 ASP   A CB  1 
ATOM   1747 C  CB  B ASP   A 1 227 ? 18.710  26.341 20.903  0.40 37.57  ? 224 ASP   A CB  1 
ATOM   1748 C  CG  A ASP   A 1 227 ? 20.050  25.768 20.751  0.60 38.82  ? 224 ASP   A CG  1 
ATOM   1749 C  CG  B ASP   A 1 227 ? 20.074  25.776 20.540  0.40 39.79  ? 224 ASP   A CG  1 
ATOM   1750 O  OD1 A ASP   A 1 227 ? 20.581  25.744 19.605  0.60 38.90  ? 224 ASP   A OD1 1 
ATOM   1751 O  OD1 B ASP   A 1 227 ? 21.065  26.552 20.636  0.40 41.57  ? 224 ASP   A OD1 1 
ATOM   1752 O  OD2 A ASP   A 1 227 ? 20.610  25.394 21.788  0.60 38.34  ? 224 ASP   A OD2 1 
ATOM   1753 O  OD2 B ASP   A 1 227 ? 20.142  24.588 20.137  0.40 39.46  ? 224 ASP   A OD2 1 
ATOM   1754 N  N   . LYS   A 1 228 ? 20.051  28.644 18.719  1.00 43.06  ? 225 LYS   A N   1 
ATOM   1755 C  CA  . LYS   A 1 228 ? 20.630  28.929 17.372  1.00 47.99  ? 225 LYS   A CA  1 
ATOM   1756 C  C   . LYS   A 1 228 ? 20.567  27.754 16.391  1.00 45.83  ? 225 LYS   A C   1 
ATOM   1757 O  O   . LYS   A 1 228 ? 20.430  28.021 15.185  1.00 46.08  ? 225 LYS   A O   1 
ATOM   1758 C  CB  . LYS   A 1 228 ? 22.141  29.147 17.472  1.00 54.93  ? 225 LYS   A CB  1 
ATOM   1759 C  CG  . LYS   A 1 228 ? 22.592  30.364 18.261  1.00 59.58  ? 225 LYS   A CG  1 
ATOM   1760 C  CD  . LYS   A 1 228 ? 23.884  30.943 17.735  1.00 65.22  ? 225 LYS   A CD  1 
ATOM   1761 C  CE  . LYS   A 1 228 ? 24.970  29.900 17.535  1.00 69.15  ? 225 LYS   A CE  1 
ATOM   1762 N  NZ  . LYS   A 1 228 ? 26.229  30.509 17.032  1.00 74.17  ? 225 LYS   A NZ  1 
ATOM   1763 N  N   . ARG   A 1 229 ? 20.806  26.533 16.860  1.00 43.30  ? 226 ARG   A N   1 
ATOM   1764 C  CA  . ARG   A 1 229 ? 20.921  25.333 15.995  1.00 44.19  ? 226 ARG   A CA  1 
ATOM   1765 C  C   . ARG   A 1 229 ? 19.563  24.967 15.419  1.00 41.88  ? 226 ARG   A C   1 
ATOM   1766 O  O   . ARG   A 1 229 ? 19.536  24.247 14.408  1.00 40.48  ? 226 ARG   A O   1 
ATOM   1767 C  CB  . ARG   A 1 229 ? 21.492  24.150 16.783  1.00 45.58  ? 226 ARG   A CB  1 
ATOM   1768 C  CG  . ARG   A 1 229 ? 22.930  24.399 17.208  1.00 48.99  ? 226 ARG   A CG  1 
ATOM   1769 C  CD  . ARG   A 1 229 ? 23.370  23.523 18.356  1.00 51.08  ? 226 ARG   A CD  1 
ATOM   1770 N  NE  . ARG   A 1 229 ? 22.785  23.877 19.648  1.00 50.75  ? 226 ARG   A NE  1 
ATOM   1771 C  CZ  . ARG   A 1 229 ? 23.328  23.576 20.829  1.00 50.55  ? 226 ARG   A CZ  1 
ATOM   1772 N  NH1 . ARG   A 1 229 ? 24.475  22.917 20.883  1.00 53.29  ? 226 ARG   A NH1 1 
ATOM   1773 N  NH2 . ARG   A 1 229 ? 22.737  23.931 21.950  1.00 48.22  ? 226 ARG   A NH2 1 
ATOM   1774 N  N   . TRP   A 1 230 ? 18.484  25.378 16.083  1.00 39.87  ? 227 TRP   A N   1 
ATOM   1775 C  CA  . TRP   A 1 230 ? 17.121  24.962 15.683  1.00 39.63  ? 227 TRP   A CA  1 
ATOM   1776 C  C   . TRP   A 1 230 ? 16.261  26.145 15.268  1.00 38.93  ? 227 TRP   A C   1 
ATOM   1777 O  O   . TRP   A 1 230 ? 15.371  25.913 14.454  1.00 41.12  ? 227 TRP   A O   1 
ATOM   1778 C  CB  . TRP   A 1 230 ? 16.474  24.176 16.816  1.00 39.04  ? 227 TRP   A CB  1 
ATOM   1779 C  CG  . TRP   A 1 230 ? 17.208  22.902 17.051  1.00 40.15  ? 227 TRP   A CG  1 
ATOM   1780 C  CD1 . TRP   A 1 230 ? 18.071  22.635 18.060  1.00 41.68  ? 227 TRP   A CD1 1 
ATOM   1781 C  CD2 . TRP   A 1 230 ? 17.176  21.734 16.222  1.00 42.05  ? 227 TRP   A CD2 1 
ATOM   1782 N  NE1 . TRP   A 1 230 ? 18.583  21.377 17.915  1.00 44.12  ? 227 TRP   A NE1 1 
ATOM   1783 C  CE2 . TRP   A 1 230 ? 18.041  20.791 16.811  1.00 43.59  ? 227 TRP   A CE2 1 
ATOM   1784 C  CE3 . TRP   A 1 230 ? 16.471  21.371 15.074  1.00 43.29  ? 227 TRP   A CE3 1 
ATOM   1785 C  CZ2 . TRP   A 1 230 ? 18.243  19.523 16.276  1.00 44.11  ? 227 TRP   A CZ2 1 
ATOM   1786 C  CZ3 . TRP   A 1 230 ? 16.652  20.111 14.552  1.00 44.49  ? 227 TRP   A CZ3 1 
ATOM   1787 C  CH2 . TRP   A 1 230 ? 17.529  19.198 15.148  1.00 44.80  ? 227 TRP   A CH2 1 
ATOM   1788 N  N   . VAL   A 1 231 ? 16.524  27.328 15.814  1.00 38.63  ? 228 VAL   A N   1 
ATOM   1789 C  CA  . VAL   A 1 231 ? 15.600  28.498 15.771  1.00 38.05  ? 228 VAL   A CA  1 
ATOM   1790 C  C   . VAL   A 1 231 ? 16.345  29.681 15.149  1.00 39.28  ? 228 VAL   A C   1 
ATOM   1791 O  O   . VAL   A 1 231 ? 17.438  30.046 15.633  1.00 42.44  ? 228 VAL   A O   1 
ATOM   1792 C  CB  . VAL   A 1 231 ? 15.054  28.859 17.167  1.00 35.80  ? 228 VAL   A CB  1 
ATOM   1793 C  CG1 . VAL   A 1 231 ? 14.073  30.027 17.101  1.00 35.01  ? 228 VAL   A CG1 1 
ATOM   1794 C  CG2 . VAL   A 1 231 ? 14.402  27.666 17.855  1.00 34.21  ? 228 VAL   A CG2 1 
ATOM   1795 N  N   . ASP   A 1 232 ? 15.752  30.260 14.120  1.00 38.89  ? 229 ASP   A N   1 
ATOM   1796 C  CA  . ASP   A 1 232 ? 16.266  31.460 13.434  1.00 40.66  ? 229 ASP   A CA  1 
ATOM   1797 C  C   . ASP   A 1 232 ? 16.273  32.611 14.441  1.00 40.60  ? 229 ASP   A C   1 
ATOM   1798 O  O   . ASP   A 1 232 ? 15.226  32.994 14.936  1.00 37.82  ? 229 ASP   A O   1 
ATOM   1799 C  CB  . ASP   A 1 232 ? 15.425  31.688 12.181  1.00 41.04  ? 229 ASP   A CB  1 
ATOM   1800 C  CG  . ASP   A 1 232 ? 15.850  32.888 11.360  1.00 44.45  ? 229 ASP   A CG  1 
ATOM   1801 O  OD1 . ASP   A 1 232 ? 16.838  33.530 11.722  1.00 45.59  ? 229 ASP   A OD1 1 
ATOM   1802 O  OD2 . ASP   A 1 232 ? 15.127  33.195 10.399  1.00 47.00  ? 229 ASP   A OD2 1 
ATOM   1803 N  N   . PRO   A 1 233 ? 17.442  33.231 14.748  1.00 43.31  ? 230 PRO   A N   1 
ATOM   1804 C  CA  . PRO   A 1 233 ? 17.488  34.380 15.655  1.00 43.84  ? 230 PRO   A CA  1 
ATOM   1805 C  C   . PRO   A 1 233 ? 16.692  35.587 15.128  1.00 43.83  ? 230 PRO   A C   1 
ATOM   1806 O  O   . PRO   A 1 233 ? 16.376  36.450 15.905  1.00 44.38  ? 230 PRO   A O   1 
ATOM   1807 C  CB  . PRO   A 1 233 ? 18.979  34.790 15.729  1.00 45.97  ? 230 PRO   A CB  1 
ATOM   1808 C  CG  . PRO   A 1 233 ? 19.749  33.668 15.046  1.00 46.71  ? 230 PRO   A CG  1 
ATOM   1809 C  CD  . PRO   A 1 233 ? 18.764  32.926 14.166  1.00 45.26  ? 230 PRO   A CD  1 
ATOM   1810 N  N   . ASN   A 1 234 ? 16.398  35.627 13.827  1.00 43.52  ? 231 ASN   A N   1 
ATOM   1811 C  CA  . ASN   A 1 234 ? 15.572  36.713 13.225  1.00 44.27  ? 231 ASN   A CA  1 
ATOM   1812 C  C   . ASN   A 1 234 ? 14.077  36.499 13.517  1.00 41.81  ? 231 ASN   A C   1 
ATOM   1813 O  O   . ASN   A 1 234 ? 13.307  37.455 13.338  1.00 41.63  ? 231 ASN   A O   1 
ATOM   1814 C  CB  . ASN   A 1 234 ? 15.792  36.834 11.714  1.00 46.84  ? 231 ASN   A CB  1 
ATOM   1815 C  CG  . ASN   A 1 234 ? 17.230  37.170 11.346  1.00 49.32  ? 231 ASN   A CG  1 
ATOM   1816 O  OD1 . ASN   A 1 234 ? 17.883  37.954 12.029  1.00 49.68  ? 231 ASN   A OD1 1 
ATOM   1817 N  ND2 . ASN   A 1 234 ? 17.751  36.538 10.302  1.00 49.32  ? 231 ASN   A ND2 1 
ATOM   1818 N  N   . SER   A 1 235 ? 13.659  35.305 13.972  1.00 38.60  ? 232 SER   A N   1 
ATOM   1819 C  CA  . SER   A 1 235 ? 12.229  35.024 14.235  1.00 36.37  ? 232 SER   A CA  1 
ATOM   1820 C  C   . SER   A 1 235 ? 11.746  35.962 15.327  1.00 36.38  ? 232 SER   A C   1 
ATOM   1821 O  O   . SER   A 1 235 ? 12.506  36.330 16.221  1.00 36.85  ? 232 SER   A O   1 
ATOM   1822 C  CB  . SER   A 1 235 ? 12.005  33.595 14.604  1.00 35.08  ? 232 SER   A CB  1 
ATOM   1823 O  OG  . SER   A 1 235 ? 12.614  33.308 15.847  1.00 32.89  ? 232 SER   A OG  1 
ATOM   1824 N  N   . PRO   A 1 236 ? 10.483  36.420 15.266  1.00 36.86  ? 233 PRO   A N   1 
ATOM   1825 C  CA  . PRO   A 1 236 ? 9.938   37.305 16.293  1.00 35.78  ? 233 PRO   A CA  1 
ATOM   1826 C  C   . PRO   A 1 236 ? 9.945   36.634 17.671  1.00 33.21  ? 233 PRO   A C   1 
ATOM   1827 O  O   . PRO   A 1 236 ? 9.583   35.495 17.779  1.00 30.32  ? 233 PRO   A O   1 
ATOM   1828 C  CB  . PRO   A 1 236 ? 8.476   37.542 15.861  1.00 37.03  ? 233 PRO   A CB  1 
ATOM   1829 C  CG  . PRO   A 1 236 ? 8.189   36.438 14.840  1.00 36.75  ? 233 PRO   A CG  1 
ATOM   1830 C  CD  . PRO   A 1 236 ? 9.518   36.151 14.184  1.00 37.54  ? 233 PRO   A CD  1 
ATOM   1831 N  N   . VAL   A 1 237 ? 10.282  37.404 18.691  1.00 33.12  ? 234 VAL   A N   1 
ATOM   1832 C  CA  . VAL   A 1 237 ? 10.423  36.911 20.084  1.00 31.99  ? 234 VAL   A CA  1 
ATOM   1833 C  C   . VAL   A 1 237 ? 9.049   36.913 20.730  1.00 30.54  ? 234 VAL   A C   1 
ATOM   1834 O  O   . VAL   A 1 237 ? 8.571   38.001 21.039  1.00 31.84  ? 234 VAL   A O   1 
ATOM   1835 C  CB  . VAL   A 1 237 ? 11.399  37.789 20.879  1.00 34.02  ? 234 VAL   A CB  1 
ATOM   1836 C  CG1 . VAL   A 1 237 ? 11.483  37.298 22.319  1.00 33.70  ? 234 VAL   A CG1 1 
ATOM   1837 C  CG2 . VAL   A 1 237 ? 12.764  37.906 20.181  1.00 35.51  ? 234 VAL   A CG2 1 
ATOM   1838 N  N   . LEU   A 1 238 ? 8.479   35.740 20.990  1.00 27.71  ? 235 LEU   A N   1 
ATOM   1839 C  CA  . LEU   A 1 238 ? 7.096   35.689 21.510  1.00 27.15  ? 235 LEU   A CA  1 
ATOM   1840 C  C   . LEU   A 1 238 ? 6.932   36.594 22.737  1.00 27.75  ? 235 LEU   A C   1 
ATOM   1841 O  O   . LEU   A 1 238 ? 5.972   37.346 22.754  1.00 27.94  ? 235 LEU   A O   1 
ATOM   1842 C  CB  . LEU   A 1 238 ? 6.683   34.261 21.844  1.00 25.52  ? 235 LEU   A CB  1 
ATOM   1843 C  CG  . LEU   A 1 238 ? 5.230   34.108 22.311  1.00 25.36  ? 235 LEU   A CG  1 
ATOM   1844 C  CD1 . LEU   A 1 238 ? 4.242   34.393 21.185  1.00 26.04  ? 235 LEU   A CD1 1 
ATOM   1845 C  CD2 . LEU   A 1 238 ? 5.052   32.725 22.891  1.00 24.04  ? 235 LEU   A CD2 1 
ATOM   1846 N  N   . LEU   A 1 239 ? 7.791   36.490 23.751  1.00 28.48  ? 236 LEU   A N   1 
ATOM   1847 C  CA  . LEU   A 1 239 ? 7.535   37.137 25.069  1.00 29.75  ? 236 LEU   A CA  1 
ATOM   1848 C  C   . LEU   A 1 239 ? 7.756   38.652 24.988  1.00 31.47  ? 236 LEU   A C   1 
ATOM   1849 O  O   . LEU   A 1 239 ? 7.529   39.343 26.012  1.00 31.85  ? 236 LEU   A O   1 
ATOM   1850 C  CB  . LEU   A 1 239 ? 8.415   36.480 26.133  1.00 29.75  ? 236 LEU   A CB  1 
ATOM   1851 C  CG  . LEU   A 1 239 ? 8.116   34.999 26.383  1.00 28.55  ? 236 LEU   A CG  1 
ATOM   1852 C  CD1 . LEU   A 1 239 ? 9.003   34.457 27.511  1.00 28.95  ? 236 LEU   A CD1 1 
ATOM   1853 C  CD2 . LEU   A 1 239 ? 6.640   34.752 26.669  1.00 28.15  ? 236 LEU   A CD2 1 
ATOM   1854 N  N   . GLU   A 1 240 ? 8.166   39.172 23.835  1.00 32.25  ? 237 GLU   A N   1 
ATOM   1855 C  CA  . GLU   A 1 240 ? 8.254   40.636 23.599  1.00 34.67  ? 237 GLU   A CA  1 
ATOM   1856 C  C   . GLU   A 1 240 ? 7.071   41.095 22.758  1.00 33.94  ? 237 GLU   A C   1 
ATOM   1857 O  O   . GLU   A 1 240 ? 7.035   42.264 22.359  1.00 34.57  ? 237 GLU   A O   1 
ATOM   1858 C  CB  . GLU   A 1 240 ? 9.533   41.003 22.859  1.00 37.52  ? 237 GLU   A CB  1 
ATOM   1859 C  CG  . GLU   A 1 240 ? 10.776  40.707 23.661  1.00 39.96  ? 237 GLU   A CG  1 
ATOM   1860 C  CD  . GLU   A 1 240 ? 12.072  40.932 22.907  1.00 43.41  ? 237 GLU   A CD  1 
ATOM   1861 O  OE1 . GLU   A 1 240 ? 12.046  41.366 21.721  1.00 47.12  ? 237 GLU   A OE1 1 
ATOM   1862 O  OE2 . GLU   A 1 240 ? 13.107  40.643 23.500  1.00 46.73  ? 237 GLU   A OE2 1 
ATOM   1863 N  N   . ASP   A 1 241 ? 6.149   40.196 22.435  1.00 32.26  ? 238 ASP   A N   1 
ATOM   1864 C  CA  . ASP   A 1 241 ? 4.972   40.587 21.642  1.00 33.46  ? 238 ASP   A CA  1 
ATOM   1865 C  C   . ASP   A 1 241 ? 4.262   41.768 22.292  1.00 33.98  ? 238 ASP   A C   1 
ATOM   1866 O  O   . ASP   A 1 241 ? 3.903   41.710 23.445  1.00 32.45  ? 238 ASP   A O   1 
ATOM   1867 C  CB  . ASP   A 1 241 ? 4.043   39.401 21.459  1.00 32.76  ? 238 ASP   A CB  1 
ATOM   1868 C  CG  . ASP   A 1 241 ? 2.917   39.820 20.555  1.00 34.57  ? 238 ASP   A CG  1 
ATOM   1869 O  OD1 . ASP   A 1 241 ? 1.984   40.391 21.113  1.00 35.85  ? 238 ASP   A OD1 1 
ATOM   1870 O  OD2 . ASP   A 1 241 ? 3.032   39.615 19.302  1.00 35.92  ? 238 ASP   A OD2 1 
ATOM   1871 N  N   . PRO   A 1 242 ? 3.981   42.866 21.561  1.00 36.19  ? 239 PRO   A N   1 
ATOM   1872 C  CA  . PRO   A 1 242 ? 3.371   44.043 22.181  1.00 37.21  ? 239 PRO   A CA  1 
ATOM   1873 C  C   . PRO   A 1 242 ? 1.982   43.759 22.782  1.00 36.29  ? 239 PRO   A C   1 
ATOM   1874 O  O   . PRO   A 1 242 ? 1.729   44.239 23.886  1.00 36.70  ? 239 PRO   A O   1 
ATOM   1875 C  CB  . PRO   A 1 242 ? 3.370   45.085 21.047  1.00 39.53  ? 239 PRO   A CB  1 
ATOM   1876 C  CG  . PRO   A 1 242 ? 3.383   44.230 19.786  1.00 38.96  ? 239 PRO   A CG  1 
ATOM   1877 C  CD  . PRO   A 1 242 ? 4.286   43.058 20.130  1.00 37.03  ? 239 PRO   A CD  1 
ATOM   1878 N  N   . VAL   A 1 243 ? 1.165   42.926 22.133  1.00 34.76  ? 240 VAL   A N   1 
ATOM   1879 C  CA  . VAL   A 1 243 ? -0.193  42.558 22.633  1.00 34.28  ? 240 VAL   A CA  1 
ATOM   1880 C  C   . VAL   A 1 243 ? -0.036  41.741 23.929  1.00 33.10  ? 240 VAL   A C   1 
ATOM   1881 O  O   . VAL   A 1 243 ? -0.771  42.025 24.915  1.00 33.12  ? 240 VAL   A O   1 
ATOM   1882 C  CB  . VAL   A 1 243 ? -0.981  41.799 21.541  1.00 33.90  ? 240 VAL   A CB  1 
ATOM   1883 C  CG1 . VAL   A 1 243 ? -2.147  40.986 22.105  1.00 33.75  ? 240 VAL   A CG1 1 
ATOM   1884 C  CG2 . VAL   A 1 243 ? -1.481  42.726 20.441  1.00 35.54  ? 240 VAL   A CG2 1 
ATOM   1885 N  N   . LEU   A 1 244 ? 0.880   40.762 23.962  1.00 32.05  ? 241 LEU   A N   1 
ATOM   1886 C  CA  . LEU   A 1 244 ? 1.137   39.975 25.208  1.00 31.20  ? 241 LEU   A CA  1 
ATOM   1887 C  C   . LEU   A 1 244 ? 1.628   40.918 26.311  1.00 32.77  ? 241 LEU   A C   1 
ATOM   1888 O  O   . LEU   A 1 244 ? 1.149   40.828 27.440  1.00 33.29  ? 241 LEU   A O   1 
ATOM   1889 C  CB  . LEU   A 1 244 ? 2.144   38.845 24.944  1.00 30.22  ? 241 LEU   A CB  1 
ATOM   1890 C  CG  . LEU   A 1 244 ? 1.665   37.778 23.947  1.00 28.87  ? 241 LEU   A CG  1 
ATOM   1891 C  CD1 . LEU   A 1 244 ? 2.699   36.683 23.766  1.00 27.49  ? 241 LEU   A CD1 1 
ATOM   1892 C  CD2 . LEU   A 1 244 ? 0.335   37.169 24.364  1.00 28.59  ? 241 LEU   A CD2 1 
ATOM   1893 N  N   . CYS   A 1 245 ? 2.542   41.813 25.981  1.00 33.63  ? 242 CYS   A N   1 
ATOM   1894 C  CA  A CYS   A 1 245 ? 3.110   42.779 26.957  0.60 34.39  ? 242 CYS   A CA  1 
ATOM   1895 C  CA  B CYS   A 1 245 ? 3.123   42.808 26.929  0.40 35.38  ? 242 CYS   A CA  1 
ATOM   1896 C  C   . CYS   A 1 245 ? 2.005   43.710 27.467  1.00 35.62  ? 242 CYS   A C   1 
ATOM   1897 O  O   . CYS   A 1 245 ? 1.991   43.979 28.664  1.00 35.45  ? 242 CYS   A O   1 
ATOM   1898 C  CB  A CYS   A 1 245 ? 4.275   43.521 26.322  0.60 35.58  ? 242 CYS   A CB  1 
ATOM   1899 C  CB  B CYS   A 1 245 ? 4.208   43.638 26.244  0.40 37.71  ? 242 CYS   A CB  1 
ATOM   1900 S  SG  A CYS   A 1 245 ? 5.685   42.400 26.155  0.60 34.00  ? 242 CYS   A SG  1 
ATOM   1901 S  SG  B CYS   A 1 245 ? 4.678   45.136 27.149  0.40 42.55  ? 242 CYS   A SG  1 
ATOM   1902 N  N   . ALA   A 1 246 ? 1.093   44.152 26.602  1.00 35.07  ? 243 ALA   A N   1 
ATOM   1903 C  CA  . ALA   A 1 246 ? 0.017   45.080 27.034  1.00 35.85  ? 243 ALA   A CA  1 
ATOM   1904 C  C   . ALA   A 1 246 ? -0.963  44.282 27.911  1.00 34.71  ? 243 ALA   A C   1 
ATOM   1905 O  O   . ALA   A 1 246 ? -1.345  44.756 28.970  1.00 35.26  ? 243 ALA   A O   1 
ATOM   1906 C  CB  . ALA   A 1 246 ? -0.637  45.747 25.847  1.00 36.65  ? 243 ALA   A CB  1 
ATOM   1907 N  N   . LEU   A 1 247 ? -1.275  43.040 27.546  1.00 33.10  ? 244 LEU   A N   1 
ATOM   1908 C  CA  . LEU   A 1 247 ? -2.168  42.200 28.381  1.00 32.90  ? 244 LEU   A CA  1 
ATOM   1909 C  C   . LEU   A 1 247 ? -1.494  41.894 29.733  1.00 32.42  ? 244 LEU   A C   1 
ATOM   1910 O  O   . LEU   A 1 247 ? -2.209  41.897 30.748  1.00 32.06  ? 244 LEU   A O   1 
ATOM   1911 C  CB  . LEU   A 1 247 ? -2.506  40.897 27.645  1.00 31.95  ? 244 LEU   A CB  1 
ATOM   1912 C  CG  . LEU   A 1 247 ? -3.521  41.011 26.514  1.00 32.84  ? 244 LEU   A CG  1 
ATOM   1913 C  CD1 . LEU   A 1 247 ? -3.632  39.711 25.765  1.00 31.70  ? 244 LEU   A CD1 1 
ATOM   1914 C  CD2 . LEU   A 1 247 ? -4.898  41.397 27.032  1.00 34.87  ? 244 LEU   A CD2 1 
ATOM   1915 N  N   . ALA   A 1 248 ? -0.175  41.663 29.776  1.00 32.35  ? 245 ALA   A N   1 
ATOM   1916 C  CA  . ALA   A 1 248 ? 0.527   41.416 31.060  1.00 33.34  ? 245 ALA   A CA  1 
ATOM   1917 C  C   . ALA   A 1 248 ? 0.318   42.634 31.972  1.00 35.90  ? 245 ALA   A C   1 
ATOM   1918 O  O   . ALA   A 1 248 ? -0.058  42.456 33.155  1.00 35.84  ? 245 ALA   A O   1 
ATOM   1919 C  CB  . ALA   A 1 248 ? 1.990   41.153 30.871  1.00 33.37  ? 245 ALA   A CB  1 
ATOM   1920 N  N   . LYS   A 1 249 ? 0.536   43.837 31.454  1.00 39.09  ? 246 LYS   A N   1 
ATOM   1921 C  CA  . LYS   A 1 249 ? 0.380   45.068 32.282  1.00 42.99  ? 246 LYS   A CA  1 
ATOM   1922 C  C   . LYS   A 1 249 ? -1.070  45.251 32.737  1.00 42.58  ? 246 LYS   A C   1 
ATOM   1923 O  O   . LYS   A 1 249 ? -1.292  45.630 33.898  1.00 42.53  ? 246 LYS   A O   1 
ATOM   1924 C  CB  . LYS   A 1 249 ? 0.864   46.290 31.519  1.00 48.07  ? 246 LYS   A CB  1 
ATOM   1925 C  CG  . LYS   A 1 249 ? 2.378   46.406 31.532  1.00 52.91  ? 246 LYS   A CG  1 
ATOM   1926 C  CD  . LYS   A 1 249 ? 2.921   47.624 30.797  1.00 59.01  ? 246 LYS   A CD  1 
ATOM   1927 C  CE  . LYS   A 1 249 ? 1.920   48.757 30.691  1.00 63.27  ? 246 LYS   A CE  1 
ATOM   1928 N  NZ  . LYS   A 1 249 ? 2.598   50.071 30.632  1.00 68.43  ? 246 LYS   A NZ  1 
ATOM   1929 N  N   . LYS   A 1 250 ? -2.021  44.994 31.854  1.00 41.27  ? 247 LYS   A N   1 
ATOM   1930 C  CA  . LYS   A 1 250 ? -3.445  45.101 32.184  1.00 42.33  ? 247 LYS   A CA  1 
ATOM   1931 C  C   . LYS   A 1 250 ? -3.768  44.216 33.394  1.00 40.22  ? 247 LYS   A C   1 
ATOM   1932 O  O   . LYS   A 1 250 ? -4.445  44.737 34.297  1.00 39.87  ? 247 LYS   A O   1 
ATOM   1933 C  CB  . LYS   A 1 250 ? -4.259  44.698 30.967  1.00 43.42  ? 247 LYS   A CB  1 
ATOM   1934 C  CG  . LYS   A 1 250 ? -5.748  44.598 31.211  1.00 46.29  ? 247 LYS   A CG  1 
ATOM   1935 C  CD  . LYS   A 1 250 ? -6.461  44.164 29.960  1.00 46.96  ? 247 LYS   A CD  1 
ATOM   1936 C  CE  . LYS   A 1 250 ? -7.960  44.250 30.103  1.00 50.07  ? 247 LYS   A CE  1 
ATOM   1937 N  NZ  . LYS   A 1 250 ? -8.612  43.460 29.028  1.00 49.95  ? 247 LYS   A NZ  1 
ATOM   1938 N  N   . HIS   A 1 251 ? -3.378  42.925 33.363  1.00 37.95  ? 248 HIS   A N   1 
ATOM   1939 C  CA  . HIS   A 1 251 ? -3.671  41.902 34.412  1.00 37.15  ? 248 HIS   A CA  1 
ATOM   1940 C  C   . HIS   A 1 251 ? -2.643  41.941 35.570  1.00 37.03  ? 248 HIS   A C   1 
ATOM   1941 O  O   . HIS   A 1 251 ? -2.849  41.204 36.593  1.00 35.72  ? 248 HIS   A O   1 
ATOM   1942 C  CB  . HIS   A 1 251 ? -3.762  40.517 33.736  1.00 36.25  ? 248 HIS   A CB  1 
ATOM   1943 C  CG  . HIS   A 1 251 ? -5.014  40.293 32.941  1.00 36.57  ? 248 HIS   A CG  1 
ATOM   1944 N  ND1 . HIS   A 1 251 ? -6.199  39.939 33.533  1.00 38.30  ? 248 HIS   A ND1 1 
ATOM   1945 C  CD2 . HIS   A 1 251 ? -5.270  40.376 31.614  1.00 36.97  ? 248 HIS   A CD2 1 
ATOM   1946 C  CE1 . HIS   A 1 251 ? -7.141  39.824 32.621  1.00 38.94  ? 248 HIS   A CE1 1 
ATOM   1947 N  NE2 . HIS   A 1 251 ? -6.596  40.091 31.430  1.00 38.23  ? 248 HIS   A NE2 1 
ATOM   1948 N  N   . LYS   A 1 252 ? -1.591  42.767 35.462  1.00 37.49  ? 249 LYS   A N   1 
ATOM   1949 C  CA  . LYS   A 1 252 ? -0.425  42.776 36.390  1.00 38.66  ? 249 LYS   A CA  1 
ATOM   1950 C  C   . LYS   A 1 252 ? 0.113   41.358 36.530  1.00 36.94  ? 249 LYS   A C   1 
ATOM   1951 O  O   . LYS   A 1 252 ? 0.339   40.896 37.677  1.00 37.24  ? 249 LYS   A O   1 
ATOM   1952 C  CB  . LYS   A 1 252 ? -0.833  43.383 37.732  1.00 40.66  ? 249 LYS   A CB  1 
ATOM   1953 C  CG  . LYS   A 1 252 ? -1.374  44.801 37.592  1.00 43.88  ? 249 LYS   A CG  1 
ATOM   1954 C  CD  . LYS   A 1 252 ? -1.456  45.565 38.884  1.00 46.79  ? 249 LYS   A CD  1 
ATOM   1955 C  CE  . LYS   A 1 252 ? -2.061  46.939 38.713  1.00 49.58  ? 249 LYS   A CE  1 
ATOM   1956 N  NZ  . LYS   A 1 252 ? -2.411  47.556 40.016  1.00 52.63  ? 249 LYS   A NZ  1 
ATOM   1957 N  N   . ARG   A 1 253 ? 0.311   40.702 35.385  1.00 34.86  ? 250 ARG   A N   1 
ATOM   1958 C  CA  . ARG   A 1 253 ? 0.994   39.400 35.299  1.00 33.31  ? 250 ARG   A CA  1 
ATOM   1959 C  C   . ARG   A 1 253 ? 2.205   39.613 34.392  1.00 32.62  ? 250 ARG   A C   1 
ATOM   1960 O  O   . ARG   A 1 253 ? 2.724   40.690 34.382  1.00 35.80  ? 250 ARG   A O   1 
ATOM   1961 C  CB  . ARG   A 1 253 ? 0.008   38.335 34.816  1.00 32.08  ? 250 ARG   A CB  1 
ATOM   1962 C  CG  . ARG   A 1 253 ? -1.214  38.166 35.712  1.00 32.66  ? 250 ARG   A CG  1 
ATOM   1963 C  CD  . ARG   A 1 253 ? -0.911  37.458 37.008  1.00 32.45  ? 250 ARG   A CD  1 
ATOM   1964 N  NE  . ARG   A 1 253 ? -2.039  37.442 37.940  1.00 32.68  ? 250 ARG   A NE  1 
ATOM   1965 C  CZ  . ARG   A 1 253 ? -2.072  36.769 39.088  1.00 33.65  ? 250 ARG   A CZ  1 
ATOM   1966 N  NH1 . ARG   A 1 253 ? -1.051  36.014 39.467  1.00 32.87  ? 250 ARG   A NH1 1 
ATOM   1967 N  NH2 . ARG   A 1 253 ? -3.159  36.820 39.839  1.00 35.15  ? 250 ARG   A NH2 1 
ATOM   1968 N  N   . THR   A 1 254 ? 2.669   38.591 33.708  1.00 30.87  ? 251 THR   A N   1 
ATOM   1969 C  CA  . THR   A 1 254 ? 3.854   38.640 32.818  1.00 29.91  ? 251 THR   A CA  1 
ATOM   1970 C  C   . THR   A 1 254 ? 3.426   38.072 31.483  1.00 28.87  ? 251 THR   A C   1 
ATOM   1971 O  O   . THR   A 1 254 ? 2.458   37.321 31.440  1.00 28.26  ? 251 THR   A O   1 
ATOM   1972 C  CB  . THR   A 1 254 ? 4.994   37.781 33.368  1.00 29.19  ? 251 THR   A CB  1 
ATOM   1973 O  OG1 . THR   A 1 254 ? 4.472   36.455 33.368  1.00 26.97  ? 251 THR   A OG1 1 
ATOM   1974 C  CG2 . THR   A 1 254 ? 5.432   38.167 34.764  1.00 30.11  ? 251 THR   A CG2 1 
ATOM   1975 N  N   . PRO   A 1 255 ? 4.142   38.400 30.391  1.00 28.44  ? 252 PRO   A N   1 
ATOM   1976 C  CA  . PRO   A 1 255 ? 3.776   37.863 29.088  1.00 27.37  ? 252 PRO   A CA  1 
ATOM   1977 C  C   . PRO   A 1 255 ? 3.711   36.322 29.090  1.00 25.42  ? 252 PRO   A C   1 
ATOM   1978 O  O   . PRO   A 1 255 ? 2.829   35.768 28.435  1.00 24.43  ? 252 PRO   A O   1 
ATOM   1979 C  CB  . PRO   A 1 255 ? 4.836   38.428 28.150  1.00 28.36  ? 252 PRO   A CB  1 
ATOM   1980 C  CG  . PRO   A 1 255 ? 5.346   39.684 28.853  1.00 30.15  ? 252 PRO   A CG  1 
ATOM   1981 C  CD  . PRO   A 1 255 ? 5.220   39.407 30.338  1.00 30.03  ? 252 PRO   A CD  1 
ATOM   1982 N  N   . ALA   A 1 256 ? 4.621   35.667 29.806  1.00 25.28  ? 253 ALA   A N   1 
ATOM   1983 C  CA  . ALA   A 1 256 ? 4.680   34.191 29.932  1.00 23.95  ? 253 ALA   A CA  1 
ATOM   1984 C  C   . ALA   A 1 256 ? 3.338   33.720 30.495  1.00 24.04  ? 253 ALA   A C   1 
ATOM   1985 O  O   . ALA   A 1 256 ? 2.727   32.765 29.919  1.00 22.06  ? 253 ALA   A O   1 
ATOM   1986 C  CB  . ALA   A 1 256 ? 5.859   33.793 30.772  1.00 24.51  ? 253 ALA   A CB  1 
ATOM   1987 N  N   . LEU   A 1 257 ? 2.848   34.379 31.556  1.00 24.21  ? 254 LEU   A N   1 
ATOM   1988 C  CA  . LEU   A 1 257 ? 1.589   33.936 32.190  1.00 24.03  ? 254 LEU   A CA  1 
ATOM   1989 C  C   . LEU   A 1 257 ? 0.413   34.152 31.251  1.00 24.07  ? 254 LEU   A C   1 
ATOM   1990 O  O   . LEU   A 1 257 ? -0.454  33.287 31.218  1.00 22.79  ? 254 LEU   A O   1 
ATOM   1991 C  CB  . LEU   A 1 257 ? 1.388   34.642 33.521  1.00 25.13  ? 254 LEU   A CB  1 
ATOM   1992 C  CG  . LEU   A 1 257 ? 2.217   34.033 34.633  1.00 25.10  ? 254 LEU   A CG  1 
ATOM   1993 C  CD1 . LEU   A 1 257 ? 2.200   34.985 35.821  1.00 26.43  ? 254 LEU   A CD1 1 
ATOM   1994 C  CD2 . LEU   A 1 257 ? 1.690   32.653 34.987  1.00 24.27  ? 254 LEU   A CD2 1 
ATOM   1995 N  N   . ILE   A 1 258 ? 0.422   35.200 30.433  1.00 24.76  ? 255 ILE   A N   1 
ATOM   1996 C  CA  . ILE   A 1 258 ? -0.682  35.400 29.461  1.00 25.17  ? 255 ILE   A CA  1 
ATOM   1997 C  C   . ILE   A 1 258 ? -0.633  34.217 28.487  1.00 23.49  ? 255 ILE   A C   1 
ATOM   1998 O  O   . ILE   A 1 258 ? -1.703  33.663 28.132  1.00 22.72  ? 255 ILE   A O   1 
ATOM   1999 C  CB  . ILE   A 1 258 ? -0.583  36.763 28.735  1.00 27.45  ? 255 ILE   A CB  1 
ATOM   2000 C  CG1 . ILE   A 1 258 ? -0.530  37.953 29.709  1.00 28.97  ? 255 ILE   A CG1 1 
ATOM   2001 C  CG2 . ILE   A 1 258 ? -1.712  36.860 27.739  1.00 28.17  ? 255 ILE   A CG2 1 
ATOM   2002 C  CD1 . ILE   A 1 258 ? -1.732  38.053 30.627  1.00 30.17  ? 255 ILE   A CD1 1 
ATOM   2003 N  N   . ALA   A 1 259 ? 0.557   33.882 28.004  1.00 22.67  ? 256 ALA   A N   1 
ATOM   2004 C  CA  . ALA   A 1 259 ? 0.718   32.870 26.931  1.00 21.67  ? 256 ALA   A CA  1 
ATOM   2005 C  C   . ALA   A 1 259 ? 0.245   31.510 27.458  1.00 20.97  ? 256 ALA   A C   1 
ATOM   2006 O  O   . ALA   A 1 259 ? -0.339  30.692 26.640  1.00 20.03  ? 256 ALA   A O   1 
ATOM   2007 C  CB  . ALA   A 1 259 ? 2.146   32.852 26.404  1.00 21.61  ? 256 ALA   A CB  1 
ATOM   2008 N  N   . LEU   A 1 260 ? 0.515   31.231 28.743  1.00 21.07  ? 257 LEU   A N   1 
ATOM   2009 C  CA  . LEU   A 1 260 ? 0.123   29.945 29.363  1.00 20.75  ? 257 LEU   A CA  1 
ATOM   2010 C  C   . LEU   A 1 260 ? -1.383  29.966 29.564  1.00 21.19  ? 257 LEU   A C   1 
ATOM   2011 O  O   . LEU   A 1 260 ? -2.055  28.918 29.301  1.00 21.98  ? 257 LEU   A O   1 
ATOM   2012 C  CB  . LEU   A 1 260 ? 0.825   29.726 30.714  1.00 20.93  ? 257 LEU   A CB  1 
ATOM   2013 C  CG  . LEU   A 1 260 ? 2.355   29.558 30.680  1.00 20.77  ? 257 LEU   A CG  1 
ATOM   2014 C  CD1 . LEU   A 1 260 ? 2.897   29.352 32.101  1.00 21.90  ? 257 LEU   A CD1 1 
ATOM   2015 C  CD2 . LEU   A 1 260 ? 2.787   28.409 29.761  1.00 19.63  ? 257 LEU   A CD2 1 
ATOM   2016 N  N   . ARG   A 1 261 ? -1.917  31.076 30.077  1.00 21.54  ? 258 ARG   A N   1 
ATOM   2017 C  CA  . ARG   A 1 261 ? -3.364  31.124 30.392  1.00 21.66  ? 258 ARG   A CA  1 
ATOM   2018 C  C   . ARG   A 1 261 ? -4.203  31.016 29.114  1.00 21.45  ? 258 ARG   A C   1 
ATOM   2019 O  O   . ARG   A 1 261 ? -5.309  30.450 29.155  1.00 21.47  ? 258 ARG   A O   1 
ATOM   2020 C  CB  . ARG   A 1 261 ? -3.690  32.407 31.165  1.00 22.66  ? 258 ARG   A CB  1 
ATOM   2021 C  CG  . ARG   A 1 261 ? -5.140  32.477 31.613  1.00 23.33  ? 258 ARG   A CG  1 
ATOM   2022 C  CD  . ARG   A 1 261 ? -5.461  31.550 32.757  1.00 23.94  ? 258 ARG   A CD  1 
ATOM   2023 N  NE  . ARG   A 1 261 ? -6.895  31.373 32.874  1.00 24.49  ? 258 ARG   A NE  1 
ATOM   2024 C  CZ  . ARG   A 1 261 ? -7.460  30.544 33.750  1.00 25.07  ? 258 ARG   A CZ  1 
ATOM   2025 N  NH1 . ARG   A 1 261 ? -6.703  29.849 34.577  1.00 25.45  ? 258 ARG   A NH1 1 
ATOM   2026 N  NH2 . ARG   A 1 261 ? -8.765  30.412 33.820  1.00 26.04  ? 258 ARG   A NH2 1 
ATOM   2027 N  N   . TYR   A 1 262 ? -3.718  31.592 28.007  1.00 21.46  ? 259 TYR   A N   1 
ATOM   2028 C  CA  . TYR   A 1 262 ? -4.359  31.481 26.682  1.00 21.80  ? 259 TYR   A CA  1 
ATOM   2029 C  C   . TYR   A 1 262 ? -4.638  30.001 26.375  1.00 21.06  ? 259 TYR   A C   1 
ATOM   2030 O  O   . TYR   A 1 262 ? -5.772  29.665 25.974  1.00 21.35  ? 259 TYR   A O   1 
ATOM   2031 C  CB  . TYR   A 1 262 ? -3.438  32.144 25.649  1.00 22.26  ? 259 TYR   A CB  1 
ATOM   2032 C  CG  . TYR   A 1 262 ? -3.846  31.915 24.221  1.00 22.58  ? 259 TYR   A CG  1 
ATOM   2033 C  CD1 . TYR   A 1 262 ? -5.006  32.467 23.723  1.00 23.94  ? 259 TYR   A CD1 1 
ATOM   2034 C  CD2 . TYR   A 1 262 ? -3.084  31.132 23.366  1.00 22.30  ? 259 TYR   A CD2 1 
ATOM   2035 C  CE1 . TYR   A 1 262 ? -5.398  32.278 22.413  1.00 24.06  ? 259 TYR   A CE1 1 
ATOM   2036 C  CE2 . TYR   A 1 262 ? -3.454  30.923 22.051  1.00 22.28  ? 259 TYR   A CE2 1 
ATOM   2037 C  CZ  . TYR   A 1 262 ? -4.620  31.501 21.569  1.00 24.07  ? 259 TYR   A CZ  1 
ATOM   2038 O  OH  . TYR   A 1 262 ? -5.004  31.312 20.265  1.00 24.77  ? 259 TYR   A OH  1 
ATOM   2039 N  N   . GLN   A 1 263 ? -3.620  29.153 26.518  1.00 20.30  ? 260 GLN   A N   1 
ATOM   2040 C  CA  . GLN   A 1 263 ? -3.709  27.681 26.244  1.00 19.33  ? 260 GLN   A CA  1 
ATOM   2041 C  C   . GLN   A 1 263 ? -4.726  27.075 27.181  1.00 20.06  ? 260 GLN   A C   1 
ATOM   2042 O  O   . GLN   A 1 263 ? -5.636  26.382 26.680  1.00 19.63  ? 260 GLN   A O   1 
ATOM   2043 C  CB  . GLN   A 1 263 ? -2.364  26.981 26.322  1.00 18.33  ? 260 GLN   A CB  1 
ATOM   2044 C  CG  . GLN   A 1 263 ? -1.339  27.543 25.328  1.00 17.91  ? 260 GLN   A CG  1 
ATOM   2045 C  CD  . GLN   A 1 263 ? -1.679  27.414 23.869  1.00 18.14  ? 260 GLN   A CD  1 
ATOM   2046 O  OE1 . GLN   A 1 263 ? -2.744  26.916 23.502  1.00 18.53  ? 260 GLN   A OE1 1 
ATOM   2047 N  NE2 . GLN   A 1 263 ? -0.793  27.912 22.996  1.00 18.36  ? 260 GLN   A NE2 1 
ATOM   2048 N  N   . LEU   A 1 264 ? -4.679  27.404 28.475  1.00 21.00  ? 261 LEU   A N   1 
ATOM   2049 C  CA  . LEU   A 1 264 ? -5.664  26.766 29.380  1.00 22.59  ? 261 LEU   A CA  1 
ATOM   2050 C  C   . LEU   A 1 264 ? -7.092  27.077 28.939  1.00 23.93  ? 261 LEU   A C   1 
ATOM   2051 O  O   . LEU   A 1 264 ? -7.924  26.168 28.972  1.00 25.17  ? 261 LEU   A O   1 
ATOM   2052 C  CB  . LEU   A 1 264 ? -5.393  27.205 30.818  1.00 24.05  ? 261 LEU   A CB  1 
ATOM   2053 C  CG  . LEU   A 1 264 ? -4.090  26.642 31.389  1.00 24.02  ? 261 LEU   A CG  1 
ATOM   2054 C  CD1 . LEU   A 1 264 ? -4.093  26.855 32.896  1.00 25.33  ? 261 LEU   A CD1 1 
ATOM   2055 C  CD2 . LEU   A 1 264 ? -3.894  25.169 31.039  1.00 24.00  ? 261 LEU   A CD2 1 
ATOM   2056 N  N   . GLN   A 1 265 ? -7.378  28.307 28.510  1.00 25.25  ? 262 GLN   A N   1 
ATOM   2057 C  CA  . GLN   A 1 265 ? -8.785  28.738 28.333  1.00 26.35  ? 262 GLN   A CA  1 
ATOM   2058 C  C   . GLN   A 1 265 ? -9.249  28.163 26.995  1.00 26.64  ? 262 GLN   A C   1 
ATOM   2059 O  O   . GLN   A 1 265 ? -10.444 28.172 26.734  1.00 29.41  ? 262 GLN   A O   1 
ATOM   2060 C  CB  . GLN   A 1 265 ? -8.913  30.254 28.516  1.00 27.03  ? 262 GLN   A CB  1 
ATOM   2061 C  CG  . GLN   A 1 265 ? -8.691  30.748 29.948  1.00 27.56  ? 262 GLN   A CG  1 
ATOM   2062 C  CD  . GLN   A 1 265 ? -9.070  32.192 30.183  1.00 28.77  ? 262 GLN   A CD  1 
ATOM   2063 O  OE1 . GLN   A 1 265 ? -8.549  32.825 31.094  1.00 29.24  ? 262 GLN   A OE1 1 
ATOM   2064 N  NE2 . GLN   A 1 265 ? -10.003 32.725 29.411  1.00 29.19  ? 262 GLN   A NE2 1 
ATOM   2065 N  N   . ARG   A 1 266 ? -8.349  27.685 26.150  1.00 25.73  ? 263 ARG   A N   1 
ATOM   2066 C  CA  . ARG   A 1 266 ? -8.801  27.110 24.843  1.00 25.81  ? 263 ARG   A CA  1 
ATOM   2067 C  C   . ARG   A 1 266 ? -8.780  25.582 24.923  1.00 25.77  ? 263 ARG   A C   1 
ATOM   2068 O  O   . ARG   A 1 266 ? -9.020  24.977 23.875  1.00 25.84  ? 263 ARG   A O   1 
ATOM   2069 C  CB  . ARG   A 1 266 ? -8.015  27.645 23.641  1.00 25.24  ? 263 ARG   A CB  1 
ATOM   2070 C  CG  . ARG   A 1 266 ? -6.515  27.390 23.672  1.00 24.37  ? 263 ARG   A CG  1 
ATOM   2071 C  CD  . ARG   A 1 266 ? -5.738  28.446 22.894  1.00 23.65  ? 263 ARG   A CD  1 
ATOM   2072 N  NE  . ARG   A 1 266 ? -6.049  28.395 21.468  1.00 24.02  ? 263 ARG   A NE  1 
ATOM   2073 C  CZ  . ARG   A 1 266 ? -5.291  27.826 20.533  1.00 22.80  ? 263 ARG   A CZ  1 
ATOM   2074 N  NH1 . ARG   A 1 266 ? -4.143  27.229 20.822  1.00 22.28  ? 263 ARG   A NH1 1 
ATOM   2075 N  NH2 . ARG   A 1 266 ? -5.712  27.849 19.289  1.00 23.60  ? 263 ARG   A NH2 1 
ATOM   2076 N  N   . GLY   A 1 267 ? -8.653  24.995 26.122  1.00 24.97  ? 264 GLY   A N   1 
ATOM   2077 C  CA  . GLY   A 1 267 ? -8.716  23.526 26.291  1.00 24.30  ? 264 GLY   A CA  1 
ATOM   2078 C  C   . GLY   A 1 267 ? -7.437  22.816 25.854  1.00 23.38  ? 264 GLY   A C   1 
ATOM   2079 O  O   . GLY   A 1 267 ? -7.467  21.610 25.537  1.00 23.09  ? 264 GLY   A O   1 
ATOM   2080 N  N   . VAL   A 1 268 ? -6.335  23.530 25.779  1.00 22.07  ? 265 VAL   A N   1 
ATOM   2081 C  CA  . VAL   A 1 268 ? -5.006  22.942 25.491  1.00 20.68  ? 265 VAL   A CA  1 
ATOM   2082 C  C   . VAL   A 1 268 ? -4.282  22.660 26.815  1.00 20.27  ? 265 VAL   A C   1 
ATOM   2083 O  O   . VAL   A 1 268 ? -4.311  23.511 27.721  1.00 22.79  ? 265 VAL   A O   1 
ATOM   2084 C  CB  . VAL   A 1 268 ? -4.223  23.863 24.567  1.00 20.03  ? 265 VAL   A CB  1 
ATOM   2085 C  CG1 . VAL   A 1 268 ? -2.736  23.551 24.558  1.00 20.08  ? 265 VAL   A CG1 1 
ATOM   2086 C  CG2 . VAL   A 1 268 ? -4.847  23.790 23.183  1.00 20.99  ? 265 VAL   A CG2 1 
ATOM   2087 N  N   . VAL   A 1 269 ? -3.625  21.509 26.913  1.00 18.86  ? 266 VAL   A N   1 
ATOM   2088 C  CA  . VAL   A 1 269 ? -2.694  21.192 28.032  1.00 18.07  ? 266 VAL   A CA  1 
ATOM   2089 C  C   . VAL   A 1 269 ? -1.343  21.826 27.720  1.00 17.30  ? 266 VAL   A C   1 
ATOM   2090 O  O   . VAL   A 1 269 ? -0.853  21.667 26.586  1.00 16.01  ? 266 VAL   A O   1 
ATOM   2091 C  CB  . VAL   A 1 269 ? -2.616  19.681 28.336  1.00 18.73  ? 266 VAL   A CB  1 
ATOM   2092 C  CG1 . VAL   A 1 269 ? -1.505  19.306 29.292  1.00 18.55  ? 266 VAL   A CG1 1 
ATOM   2093 C  CG2 . VAL   A 1 269 ? -3.945  19.205 28.856  1.00 19.38  ? 266 VAL   A CG2 1 
ATOM   2094 N  N   . VAL   A 1 270 ? -0.808  22.632 28.663  1.00 16.50  ? 267 VAL   A N   1 
ATOM   2095 C  CA  . VAL   A 1 270 ? 0.390   23.435 28.335  1.00 16.69  ? 267 VAL   A CA  1 
ATOM   2096 C  C   . VAL   A 1 270 ? 1.619   23.023 29.170  1.00 16.39  ? 267 VAL   A C   1 
ATOM   2097 O  O   . VAL   A 1 270 ? 1.526   22.863 30.424  1.00 17.15  ? 267 VAL   A O   1 
ATOM   2098 C  CB  . VAL   A 1 270 ? 0.054   24.937 28.500  1.00 17.70  ? 267 VAL   A CB  1 
ATOM   2099 C  CG1 . VAL   A 1 270 ? -0.166  25.399 29.929  1.00 18.82  ? 267 VAL   A CG1 1 
ATOM   2100 C  CG2 . VAL   A 1 270 ? 1.087   25.795 27.808  1.00 18.29  ? 267 VAL   A CG2 1 
ATOM   2101 N  N   . LEU   A 1 271 ? 2.747   22.933 28.491  1.00 15.68  ? 268 LEU   A N   1 
ATOM   2102 C  CA  . LEU   A 1 271 ? 4.081   22.727 29.088  1.00 16.20  ? 268 LEU   A CA  1 
ATOM   2103 C  C   . LEU   A 1 271 ? 4.720   24.091 29.295  1.00 17.10  ? 268 LEU   A C   1 
ATOM   2104 O  O   . LEU   A 1 271 ? 4.359   25.030 28.533  1.00 17.94  ? 268 LEU   A O   1 
ATOM   2105 C  CB  . LEU   A 1 271 ? 4.911   21.901 28.128  1.00 16.07  ? 268 LEU   A CB  1 
ATOM   2106 C  CG  . LEU   A 1 271 ? 4.344   20.514 27.822  1.00 16.20  ? 268 LEU   A CG  1 
ATOM   2107 C  CD1 . LEU   A 1 271 ? 5.406   19.756 27.065  1.00 16.45  ? 268 LEU   A CD1 1 
ATOM   2108 C  CD2 . LEU   A 1 271 ? 3.960   19.740 29.098  1.00 16.52  ? 268 LEU   A CD2 1 
ATOM   2109 N  N   . ALA   A 1 272 ? 5.601   24.209 30.279  1.00 18.20  ? 269 ALA   A N   1 
ATOM   2110 C  CA  . ALA   A 1 272 ? 6.386   25.439 30.528  1.00 18.85  ? 269 ALA   A CA  1 
ATOM   2111 C  C   . ALA   A 1 272 ? 7.740   25.018 31.082  1.00 19.31  ? 269 ALA   A C   1 
ATOM   2112 O  O   . ALA   A 1 272 ? 7.779   24.408 32.171  1.00 19.53  ? 269 ALA   A O   1 
ATOM   2113 C  CB  . ALA   A 1 272 ? 5.680   26.347 31.505  1.00 19.24  ? 269 ALA   A CB  1 
ATOM   2114 N  N   . LYS   A 1 273 ? 8.801   25.219 30.309  1.00 19.32  ? 270 LYS   A N   1 
ATOM   2115 C  CA  . LYS   A 1 273 ? 10.168  24.867 30.727  1.00 20.64  ? 270 LYS   A CA  1 
ATOM   2116 C  C   . LYS   A 1 273 ? 10.665  26.108 31.422  1.00 21.77  ? 270 LYS   A C   1 
ATOM   2117 O  O   . LYS   A 1 273 ? 10.539  27.215 30.848  1.00 21.19  ? 270 LYS   A O   1 
ATOM   2118 C  CB  . LYS   A 1 273 ? 11.120  24.465 29.593  1.00 21.37  ? 270 LYS   A CB  1 
ATOM   2119 C  CG  . LYS   A 1 273 ? 12.611  24.378 29.912  1.00 22.25  ? 270 LYS   A CG  1 
ATOM   2120 C  CD  . LYS   A 1 273 ? 13.369  25.686 29.779  1.00 22.98  ? 270 LYS   A CD  1 
ATOM   2121 C  CE  . LYS   A 1 273 ? 14.843  25.551 30.091  1.00 23.80  ? 270 LYS   A CE  1 
ATOM   2122 N  NZ  . LYS   A 1 273 ? 15.546  26.848 29.911  1.00 25.20  ? 270 LYS   A NZ  1 
ATOM   2123 N  N   . SER   A 1 274 ? 11.210  25.945 32.614  1.00 22.59  ? 271 SER   A N   1 
ATOM   2124 C  CA  . SER   A 1 274 ? 12.057  26.993 33.230  1.00 23.66  ? 271 SER   A CA  1 
ATOM   2125 C  C   . SER   A 1 274 ? 13.093  26.298 34.102  1.00 24.64  ? 271 SER   A C   1 
ATOM   2126 O  O   . SER   A 1 274 ? 12.696  25.371 34.799  1.00 24.99  ? 271 SER   A O   1 
ATOM   2127 C  CB  . SER   A 1 274 ? 11.264  27.982 34.044  1.00 24.32  ? 271 SER   A CB  1 
ATOM   2128 O  OG  . SER   A 1 274 ? 12.150  28.946 34.613  1.00 26.15  ? 271 SER   A OG  1 
ATOM   2129 N  N   . TYR   A 1 275 ? 14.354  26.732 34.022  1.00 25.57  ? 272 TYR   A N   1 
ATOM   2130 C  CA  . TYR   A 1 275 ? 15.458  26.266 34.886  1.00 27.33  ? 272 TYR   A CA  1 
ATOM   2131 C  C   . TYR   A 1 275 ? 15.725  27.363 35.922  1.00 28.97  ? 272 TYR   A C   1 
ATOM   2132 O  O   . TYR   A 1 275 ? 16.767  27.330 36.505  1.00 30.29  ? 272 TYR   A O   1 
ATOM   2133 C  CB  . TYR   A 1 275 ? 16.676  25.852 34.056  1.00 27.77  ? 272 TYR   A CB  1 
ATOM   2134 C  CG  . TYR   A 1 275 ? 16.611  24.409 33.606  1.00 27.08  ? 272 TYR   A CG  1 
ATOM   2135 C  CD1 . TYR   A 1 275 ? 15.425  23.844 33.139  1.00 25.50  ? 272 TYR   A CD1 1 
ATOM   2136 C  CD2 . TYR   A 1 275 ? 17.712  23.581 33.722  1.00 27.76  ? 272 TYR   A CD2 1 
ATOM   2137 C  CE1 . TYR   A 1 275 ? 15.334  22.501 32.816  1.00 24.67  ? 272 TYR   A CE1 1 
ATOM   2138 C  CE2 . TYR   A 1 275 ? 17.644  22.250 33.343  1.00 27.54  ? 272 TYR   A CE2 1 
ATOM   2139 C  CZ  . TYR   A 1 275 ? 16.458  21.712 32.888  1.00 25.30  ? 272 TYR   A CZ  1 
ATOM   2140 O  OH  . TYR   A 1 275 ? 16.420  20.413 32.476  1.00 25.76  ? 272 TYR   A OH  1 
ATOM   2141 N  N   . ASN   A 1 276 ? 14.808  28.320 36.095  1.00 28.98  ? 273 ASN   A N   1 
ATOM   2142 C  CA  . ASN   A 1 276 ? 15.037  29.504 36.972  1.00 30.68  ? 273 ASN   A CA  1 
ATOM   2143 C  C   . ASN   A 1 276 ? 14.070  29.443 38.143  1.00 30.99  ? 273 ASN   A C   1 
ATOM   2144 O  O   . ASN   A 1 276 ? 12.844  29.318 37.906  1.00 29.59  ? 273 ASN   A O   1 
ATOM   2145 C  CB  . ASN   A 1 276 ? 14.827  30.823 36.237  1.00 30.83  ? 273 ASN   A CB  1 
ATOM   2146 C  CG  . ASN   A 1 276 ? 14.960  32.025 37.154  1.00 32.97  ? 273 ASN   A CG  1 
ATOM   2147 O  OD1 . ASN   A 1 276 ? 13.966  32.441 37.756  1.00 32.48  ? 273 ASN   A OD1 1 
ATOM   2148 N  ND2 . ASN   A 1 276 ? 16.158  32.603 37.221  1.00 33.85  ? 273 ASN   A ND2 1 
ATOM   2149 N  N   . GLU   A 1 277 ? 14.593  29.524 39.364  1.00 33.27  ? 274 GLU   A N   1 
ATOM   2150 C  CA  . GLU   A 1 277 ? 13.733  29.251 40.538  1.00 34.61  ? 274 GLU   A CA  1 
ATOM   2151 C  C   . GLU   A 1 277 ? 12.554  30.218 40.548  1.00 33.06  ? 274 GLU   A C   1 
ATOM   2152 O  O   . GLU   A 1 277 ? 11.424  29.739 40.813  1.00 31.46  ? 274 GLU   A O   1 
ATOM   2153 C  CB  . GLU   A 1 277 ? 14.426  29.292 41.895  1.00 37.69  ? 274 GLU   A CB  1 
ATOM   2154 C  CG  . GLU   A 1 277 ? 13.374  29.294 43.000  1.00 39.88  ? 274 GLU   A CG  1 
ATOM   2155 C  CD  . GLU   A 1 277 ? 13.837  28.914 44.396  1.00 42.95  ? 274 GLU   A CD  1 
ATOM   2156 O  OE1 . GLU   A 1 277 ? 15.047  28.854 44.569  1.00 43.52  ? 274 GLU   A OE1 1 
ATOM   2157 O  OE2 . GLU   A 1 277 ? 12.963  28.662 45.292  1.00 44.23  ? 274 GLU   A OE2 1 
ATOM   2158 N  N   . GLN   A 1 278 ? 12.789  31.505 40.284  1.00 33.55  ? 275 GLN   A N   1 
ATOM   2159 C  CA  . GLN   A 1 278 ? 11.695  32.491 40.377  1.00 34.50  ? 275 GLN   A CA  1 
ATOM   2160 C  C   . GLN   A 1 278 ? 10.629  32.206 39.318  1.00 31.26  ? 275 GLN   A C   1 
ATOM   2161 O  O   . GLN   A 1 278 ? 9.436   32.324 39.644  1.00 30.39  ? 275 GLN   A O   1 
ATOM   2162 C  CB  . GLN   A 1 278 ? 12.216  33.927 40.268  1.00 39.07  ? 275 GLN   A CB  1 
ATOM   2163 C  CG  . GLN   A 1 278 ? 11.075  34.904 40.104  1.00 42.36  ? 275 GLN   A CG  1 
ATOM   2164 C  CD  . GLN   A 1 278 ? 11.481  36.293 39.677  1.00 48.51  ? 275 GLN   A CD  1 
ATOM   2165 O  OE1 . GLN   A 1 278 ? 10.978  37.265 40.229  1.00 53.82  ? 275 GLN   A OE1 1 
ATOM   2166 N  NE2 . GLN   A 1 278 ? 12.348  36.400 38.666  1.00 50.71  ? 275 GLN   A NE2 1 
ATOM   2167 N  N   . ARG   A 1 279 ? 11.028  31.874 38.094  1.00 29.24  ? 276 ARG   A N   1 
ATOM   2168 C  CA  . ARG   A 1 279 ? 10.081  31.693 36.957  1.00 28.11  ? 276 ARG   A CA  1 
ATOM   2169 C  C   . ARG   A 1 279 ? 9.328   30.380 37.122  1.00 26.13  ? 276 ARG   A C   1 
ATOM   2170 O  O   . ARG   A 1 279 ? 8.138   30.368 36.853  1.00 23.71  ? 276 ARG   A O   1 
ATOM   2171 C  CB  . ARG   A 1 279 ? 10.811  31.862 35.624  1.00 28.49  ? 276 ARG   A CB  1 
ATOM   2172 C  CG  . ARG   A 1 279 ? 11.178  33.324 35.393  1.00 29.81  ? 276 ARG   A CG  1 
ATOM   2173 C  CD  . ARG   A 1 279 ? 11.699  33.526 33.992  1.00 30.28  ? 276 ARG   A CD  1 
ATOM   2174 N  NE  . ARG   A 1 279 ? 13.060  33.023 33.819  1.00 31.66  ? 276 ARG   A NE  1 
ATOM   2175 C  CZ  . ARG   A 1 279 ? 14.184  33.677 34.152  1.00 34.03  ? 276 ARG   A CZ  1 
ATOM   2176 N  NH1 . ARG   A 1 279 ? 14.142  34.869 34.749  1.00 34.73  ? 276 ARG   A NH1 1 
ATOM   2177 N  NH2 . ARG   A 1 279 ? 15.362  33.118 33.897  1.00 34.19  ? 276 ARG   A NH2 1 
ATOM   2178 N  N   . ILE   A 1 280 ? 9.978   29.368 37.679  1.00 26.98  ? 277 ILE   A N   1 
ATOM   2179 C  CA  . ILE   A 1 280 ? 9.299   28.080 37.957  1.00 26.46  ? 277 ILE   A CA  1 
ATOM   2180 C  C   . ILE   A 1 280 ? 8.126   28.356 38.899  1.00 26.98  ? 277 ILE   A C   1 
ATOM   2181 O  O   . ILE   A 1 280 ? 7.017   27.877 38.636  1.00 26.12  ? 277 ILE   A O   1 
ATOM   2182 C  CB  . ILE   A 1 280 ? 10.287  27.083 38.542  1.00 26.69  ? 277 ILE   A CB  1 
ATOM   2183 C  CG1 . ILE   A 1 280 ? 11.278  26.631 37.475  1.00 26.12  ? 277 ILE   A CG1 1 
ATOM   2184 C  CG2 . ILE   A 1 280 ? 9.542   25.933 39.224  1.00 27.47  ? 277 ILE   A CG2 1 
ATOM   2185 C  CD1 . ILE   A 1 280 ? 12.458  25.862 38.038  1.00 26.95  ? 277 ILE   A CD1 1 
ATOM   2186 N  N   . ARG   A 1 281 ? 8.371   29.083 39.981  1.00 28.07  ? 278 ARG   A N   1 
ATOM   2187 C  CA  . ARG   A 1 281 ? 7.286   29.394 40.958  1.00 30.20  ? 278 ARG   A CA  1 
ATOM   2188 C  C   . ARG   A 1 281 ? 6.281   30.371 40.351  1.00 29.46  ? 278 ARG   A C   1 
ATOM   2189 O  O   . ARG   A 1 281 ? 5.106   30.247 40.698  1.00 30.63  ? 278 ARG   A O   1 
ATOM   2190 C  CB  . ARG   A 1 281 ? 7.847   29.996 42.243  1.00 33.32  ? 278 ARG   A CB  1 
ATOM   2191 C  CG  . ARG   A 1 281 ? 8.699   28.975 42.964  1.00 35.37  ? 278 ARG   A CG  1 
ATOM   2192 C  CD  . ARG   A 1 281 ? 9.178   29.627 44.224  1.00 39.97  ? 278 ARG   A CD  1 
ATOM   2193 N  NE  . ARG   A 1 281 ? 9.997   28.717 44.979  1.00 43.14  ? 278 ARG   A NE  1 
ATOM   2194 C  CZ  . ARG   A 1 281 ? 9.531   27.726 45.743  1.00 45.94  ? 278 ARG   A CZ  1 
ATOM   2195 N  NH1 . ARG   A 1 281 ? 8.230   27.479 45.832  1.00 46.57  ? 278 ARG   A NH1 1 
ATOM   2196 N  NH2 . ARG   A 1 281 ? 10.395  26.959 46.390  1.00 47.14  ? 278 ARG   A NH2 1 
ATOM   2197 N  N   . GLN   A 1 282 ? 6.726   31.290 39.499  1.00 27.90  ? 279 GLN   A N   1 
ATOM   2198 C  CA  . GLN   A 1 282 ? 5.792   32.223 38.816  1.00 28.46  ? 279 GLN   A CA  1 
ATOM   2199 C  C   . GLN   A 1 282 ? 4.792   31.441 37.961  1.00 27.04  ? 279 GLN   A C   1 
ATOM   2200 O  O   . GLN   A 1 282 ? 3.598   31.813 37.964  1.00 26.66  ? 279 GLN   A O   1 
ATOM   2201 C  CB  . GLN   A 1 282 ? 6.548   33.257 37.996  1.00 29.16  ? 279 GLN   A CB  1 
ATOM   2202 C  CG  . GLN   A 1 282 ? 5.645   34.294 37.352  1.00 29.84  ? 279 GLN   A CG  1 
ATOM   2203 C  CD  . GLN   A 1 282 ? 6.423   35.012 36.284  1.00 30.73  ? 279 GLN   A CD  1 
ATOM   2204 O  OE1 . GLN   A 1 282 ? 6.091   34.926 35.111  1.00 30.12  ? 279 GLN   A OE1 1 
ATOM   2205 N  NE2 . GLN   A 1 282 ? 7.511   35.668 36.667  1.00 32.08  ? 279 GLN   A NE2 1 
ATOM   2206 N  N   . ASN   A 1 283 ? 5.219   30.369 37.297  1.00 25.25  ? 280 ASN   A N   1 
ATOM   2207 C  CA  . ASN   A 1 283 ? 4.377   29.821 36.206  1.00 24.34  ? 280 ASN   A CA  1 
ATOM   2208 C  C   . ASN   A 1 283 ? 3.126   29.182 36.775  1.00 24.53  ? 280 ASN   A C   1 
ATOM   2209 O  O   . ASN   A 1 283 ? 2.144   29.108 36.027  1.00 24.63  ? 280 ASN   A O   1 
ATOM   2210 C  CB  . ASN   A 1 283 ? 5.157   28.926 35.240  1.00 23.40  ? 280 ASN   A CB  1 
ATOM   2211 C  CG  . ASN   A 1 283 ? 6.122   29.710 34.386  1.00 23.21  ? 280 ASN   A CG  1 
ATOM   2212 O  OD1 . ASN   A 1 283 ? 5.976   30.916 34.254  1.00 23.37  ? 280 ASN   A OD1 1 
ATOM   2213 N  ND2 . ASN   A 1 283 ? 7.136   29.051 33.858  1.00 22.59  ? 280 ASN   A ND2 1 
ATOM   2214 N  N   . VAL   A 1 284 ? 3.135   28.720 38.034  1.00 25.45  ? 281 VAL   A N   1 
ATOM   2215 C  CA  . VAL   A 1 284 ? 1.929   28.074 38.627  1.00 25.88  ? 281 VAL   A CA  1 
ATOM   2216 C  C   . VAL   A 1 284 ? 0.873   29.160 38.877  1.00 26.43  ? 281 VAL   A C   1 
ATOM   2217 O  O   . VAL   A 1 284 ? -0.268  28.785 39.184  1.00 25.84  ? 281 VAL   A O   1 
ATOM   2218 C  CB  . VAL   A 1 284 ? 2.246   27.228 39.882  1.00 27.78  ? 281 VAL   A CB  1 
ATOM   2219 C  CG1 . VAL   A 1 284 ? 3.274   26.179 39.555  1.00 27.52  ? 281 VAL   A CG1 1 
ATOM   2220 C  CG2 . VAL   A 1 284 ? 2.738   28.057 41.052  1.00 29.83  ? 281 VAL   A CG2 1 
ATOM   2221 N  N   . GLN   A 1 285 ? 1.232   30.451 38.721  1.00 26.51  ? 282 GLN   A N   1 
ATOM   2222 C  CA  . GLN   A 1 285 ? 0.268   31.579 38.843  1.00 28.51  ? 282 GLN   A CA  1 
ATOM   2223 C  C   . GLN   A 1 285 ? -0.755  31.560 37.710  1.00 27.33  ? 282 GLN   A C   1 
ATOM   2224 O  O   . GLN   A 1 285 ? -1.735  32.330 37.789  1.00 28.41  ? 282 GLN   A O   1 
ATOM   2225 C  CB  . GLN   A 1 285 ? 0.949   32.948 38.858  1.00 29.71  ? 282 GLN   A CB  1 
ATOM   2226 C  CG  . GLN   A 1 285 ? 1.544   33.291 40.209  1.00 32.79  ? 282 GLN   A CG  1 
ATOM   2227 C  CD  . GLN   A 1 285 ? 2.228   34.632 40.118  1.00 34.59  ? 282 GLN   A CD  1 
ATOM   2228 O  OE1 . GLN   A 1 285 ? 1.788   35.566 39.392  1.00 37.00  ? 282 GLN   A OE1 1 
ATOM   2229 N  NE2 . GLN   A 1 285 ? 3.401   34.662 40.726  1.00 35.26  ? 282 GLN   A NE2 1 
ATOM   2230 N  N   . VAL   A 1 286 ? -0.577  30.696 36.712  1.00 26.11  ? 283 VAL   A N   1 
ATOM   2231 C  CA  . VAL   A 1 286 ? -1.544  30.590 35.594  1.00 26.07  ? 283 VAL   A CA  1 
ATOM   2232 C  C   . VAL   A 1 286 ? -2.948  30.262 36.129  1.00 26.67  ? 283 VAL   A C   1 
ATOM   2233 O  O   . VAL   A 1 286 ? -3.898  30.641 35.443  1.00 25.91  ? 283 VAL   A O   1 
ATOM   2234 C  CB  . VAL   A 1 286 ? -1.093  29.553 34.533  1.00 25.35  ? 283 VAL   A CB  1 
ATOM   2235 C  CG1 . VAL   A 1 286 ? -1.159  28.122 35.056  1.00 25.41  ? 283 VAL   A CG1 1 
ATOM   2236 C  CG2 . VAL   A 1 286 ? -1.913  29.687 33.243  1.00 25.38  ? 283 VAL   A CG2 1 
ATOM   2237 N  N   . PHE   A 1 287 ? -3.107  29.538 37.251  1.00 26.90  ? 284 PHE   A N   1 
ATOM   2238 C  CA  . PHE   A 1 287 ? -4.453  29.170 37.767  1.00 27.72  ? 284 PHE   A CA  1 
ATOM   2239 C  C   . PHE   A 1 287 ? -5.080  30.342 38.500  1.00 28.87  ? 284 PHE   A C   1 
ATOM   2240 O  O   . PHE   A 1 287 ? -6.198  30.154 38.948  1.00 29.10  ? 284 PHE   A O   1 
ATOM   2241 C  CB  . PHE   A 1 287 ? -4.413  27.922 38.658  1.00 28.91  ? 284 PHE   A CB  1 
ATOM   2242 C  CG  . PHE   A 1 287 ? -3.946  26.700 37.898  1.00 28.39  ? 284 PHE   A CG  1 
ATOM   2243 C  CD1 . PHE   A 1 287 ? -4.766  26.134 36.947  1.00 28.38  ? 284 PHE   A CD1 1 
ATOM   2244 C  CD2 . PHE   A 1 287 ? -2.675  26.173 38.075  1.00 28.23  ? 284 PHE   A CD2 1 
ATOM   2245 C  CE1 . PHE   A 1 287 ? -4.359  25.010 36.230  1.00 27.02  ? 284 PHE   A CE1 1 
ATOM   2246 C  CE2 . PHE   A 1 287 ? -2.251  25.078 37.324  1.00 27.24  ? 284 PHE   A CE2 1 
ATOM   2247 C  CZ  . PHE   A 1 287 ? -3.090  24.509 36.407  1.00 26.47  ? 284 PHE   A CZ  1 
ATOM   2248 N  N   . GLU   A 1 288 ? -4.388  31.478 38.645  1.00 29.41  ? 285 GLU   A N   1 
ATOM   2249 C  CA  . GLU   A 1 288 ? -4.783  32.536 39.622  1.00 31.50  ? 285 GLU   A CA  1 
ATOM   2250 C  C   . GLU   A 1 288 ? -5.578  33.655 38.954  1.00 31.56  ? 285 GLU   A C   1 
ATOM   2251 O  O   . GLU   A 1 288 ? -6.118  34.495 39.658  1.00 32.19  ? 285 GLU   A O   1 
ATOM   2252 C  CB  . GLU   A 1 288 ? -3.574  33.181 40.283  1.00 32.77  ? 285 GLU   A CB  1 
ATOM   2253 C  CG  . GLU   A 1 288 ? -2.857  32.265 41.220  1.00 33.30  ? 285 GLU   A CG  1 
ATOM   2254 C  CD  . GLU   A 1 288 ? -1.637  32.892 41.861  1.00 35.38  ? 285 GLU   A CD  1 
ATOM   2255 O  OE1 . GLU   A 1 288 ? -1.469  34.151 41.777  1.00 36.12  ? 285 GLU   A OE1 1 
ATOM   2256 O  OE2 . GLU   A 1 288 ? -0.861  32.096 42.448  1.00 37.56  ? 285 GLU   A OE2 1 
ATOM   2257 N  N   . PHE   A 1 289 ? -5.670  33.677 37.633  1.00 30.14  ? 286 PHE   A N   1 
ATOM   2258 C  CA  . PHE   A 1 289 ? -6.333  34.800 36.932  1.00 31.44  ? 286 PHE   A CA  1 
ATOM   2259 C  C   . PHE   A 1 289 ? -6.999  34.285 35.661  1.00 31.49  ? 286 PHE   A C   1 
ATOM   2260 O  O   . PHE   A 1 289 ? -6.744  33.136 35.302  1.00 30.40  ? 286 PHE   A O   1 
ATOM   2261 C  CB  . PHE   A 1 289 ? -5.313  35.908 36.668  1.00 31.73  ? 286 PHE   A CB  1 
ATOM   2262 C  CG  . PHE   A 1 289 ? -4.345  35.623 35.548  1.00 30.09  ? 286 PHE   A CG  1 
ATOM   2263 C  CD1 . PHE   A 1 289 ? -3.186  34.880 35.754  1.00 28.71  ? 286 PHE   A CD1 1 
ATOM   2264 C  CD2 . PHE   A 1 289 ? -4.580  36.139 34.280  1.00 29.85  ? 286 PHE   A CD2 1 
ATOM   2265 C  CE1 . PHE   A 1 289 ? -2.352  34.591 34.687  1.00 27.51  ? 286 PHE   A CE1 1 
ATOM   2266 C  CE2 . PHE   A 1 289 ? -3.731  35.867 33.221  1.00 28.40  ? 286 PHE   A CE2 1 
ATOM   2267 C  CZ  . PHE   A 1 289 ? -2.602  35.121 33.433  1.00 27.34  ? 286 PHE   A CZ  1 
ATOM   2268 N  N   . GLN   A 1 290 ? -7.831  35.115 35.042  1.00 33.13  ? 287 GLN   A N   1 
ATOM   2269 C  CA  . GLN   A 1 290 ? -8.561  34.762 33.796  1.00 34.79  ? 287 GLN   A CA  1 
ATOM   2270 C  C   . GLN   A 1 290 ? -8.380  35.856 32.738  1.00 34.72  ? 287 GLN   A C   1 
ATOM   2271 O  O   . GLN   A 1 290 ? -8.426  37.019 33.131  1.00 34.61  ? 287 GLN   A O   1 
ATOM   2272 C  CB  . GLN   A 1 290 ? -10.050 34.738 34.086  1.00 38.44  ? 287 GLN   A CB  1 
ATOM   2273 C  CG  . GLN   A 1 290 ? -10.548 33.411 34.610  1.00 41.78  ? 287 GLN   A CG  1 
ATOM   2274 C  CD  . GLN   A 1 290 ? -12.047 33.550 34.718  1.00 45.86  ? 287 GLN   A CD  1 
ATOM   2275 O  OE1 . GLN   A 1 290 ? -12.761 33.592 33.710  1.00 49.31  ? 287 GLN   A OE1 1 
ATOM   2276 N  NE2 . GLN   A 1 290 ? -12.512 33.737 35.940  1.00 47.93  ? 287 GLN   A NE2 1 
ATOM   2277 N  N   . LEU   A 1 291 ? -8.257  35.472 31.468  1.00 32.85  ? 288 LEU   A N   1 
ATOM   2278 C  CA  . LEU   A 1 291 ? -8.364  36.406 30.314  1.00 33.37  ? 288 LEU   A CA  1 
ATOM   2279 C  C   . LEU   A 1 291 ? -9.833  36.590 29.955  1.00 33.72  ? 288 LEU   A C   1 
ATOM   2280 O  O   . LEU   A 1 291 ? -10.557 35.624 30.042  1.00 32.49  ? 288 LEU   A O   1 
ATOM   2281 C  CB  . LEU   A 1 291 ? -7.559  35.833 29.146  1.00 32.14  ? 288 LEU   A CB  1 
ATOM   2282 C  CG  . LEU   A 1 291 ? -6.084  35.607 29.463  1.00 30.84  ? 288 LEU   A CG  1 
ATOM   2283 C  CD1 . LEU   A 1 291 ? -5.436  34.704 28.436  1.00 29.89  ? 288 LEU   A CD1 1 
ATOM   2284 C  CD2 . LEU   A 1 291 ? -5.328  36.922 29.601  1.00 31.66  ? 288 LEU   A CD2 1 
ATOM   2285 N  N   . THR   A 1 292 ? -10.225 37.782 29.521  1.00 35.24  ? 289 THR   A N   1 
ATOM   2286 C  CA  . THR   A 1 292 ? -11.573 38.021 28.939  1.00 37.65  ? 289 THR   A CA  1 
ATOM   2287 C  C   . THR   A 1 292 ? -11.698 37.343 27.565  1.00 37.14  ? 289 THR   A C   1 
ATOM   2288 O  O   . THR   A 1 292 ? -10.667 36.983 26.976  1.00 35.24  ? 289 THR   A O   1 
ATOM   2289 C  CB  . THR   A 1 292 ? -11.863 39.519 28.822  1.00 39.81  ? 289 THR   A CB  1 
ATOM   2290 O  OG1 . THR   A 1 292 ? -10.996 40.059 27.806  1.00 39.97  ? 289 THR   A OG1 1 
ATOM   2291 C  CG2 . THR   A 1 292 ? -11.704 40.191 30.167  1.00 40.64  ? 289 THR   A CG2 1 
ATOM   2292 N  N   . ALA   A 1 293 ? -12.921 37.180 27.073  1.00 39.35  ? 290 ALA   A N   1 
ATOM   2293 C  CA  . ALA   A 1 293 ? -13.204 36.732 25.684  1.00 39.70  ? 290 ALA   A CA  1 
ATOM   2294 C  C   . ALA   A 1 293 ? -12.496 37.652 24.680  1.00 39.51  ? 290 ALA   A C   1 
ATOM   2295 O  O   . ALA   A 1 293 ? -12.019 37.175 23.649  1.00 39.21  ? 290 ALA   A O   1 
ATOM   2296 C  CB  . ALA   A 1 293 ? -14.694 36.716 25.441  1.00 41.68  ? 290 ALA   A CB  1 
ATOM   2297 N  N   . GLU   A 1 294 ? -12.520 38.958 24.926  1.00 41.33  ? 291 GLU   A N   1 
ATOM   2298 C  CA  . GLU   A 1 294 ? -11.853 39.964 24.055  1.00 41.91  ? 291 GLU   A CA  1 
ATOM   2299 C  C   . GLU   A 1 294 ? -10.331 39.770 24.116  1.00 38.73  ? 291 GLU   A C   1 
ATOM   2300 O  O   . GLU   A 1 294 ? -9.664  39.932 23.093  1.00 37.63  ? 291 GLU   A O   1 
ATOM   2301 C  CB  . GLU   A 1 294 ? -12.163 41.397 24.516  1.00 45.43  ? 291 GLU   A CB  1 
ATOM   2302 C  CG  . GLU   A 1 294 ? -13.638 41.781 24.535  1.00 49.70  ? 291 GLU   A CG  1 
ATOM   2303 C  CD  . GLU   A 1 294 ? -14.594 41.128 25.549  1.00 52.70  ? 291 GLU   A CD  1 
ATOM   2304 O  OE1 . GLU   A 1 294 ? -14.144 40.483 26.545  1.00 50.74  ? 291 GLU   A OE1 1 
ATOM   2305 O  OE2 . GLU   A 1 294 ? -15.827 41.244 25.323  1.00 57.66  ? 291 GLU   A OE2 1 
ATOM   2306 N  N   . ASP   A 1 295 ? -9.780  39.496 25.302  1.00 36.10  ? 292 ASP   A N   1 
ATOM   2307 C  CA  . ASP   A 1 295 ? -8.339  39.166 25.440  1.00 34.32  ? 292 ASP   A CA  1 
ATOM   2308 C  C   . ASP   A 1 295 ? -8.044  37.908 24.593  1.00 31.96  ? 292 ASP   A C   1 
ATOM   2309 O  O   . ASP   A 1 295 ? -7.056  37.881 23.844  1.00 29.58  ? 292 ASP   A O   1 
ATOM   2310 C  CB  . ASP   A 1 295 ? -7.960  38.938 26.902  1.00 34.09  ? 292 ASP   A CB  1 
ATOM   2311 C  CG  . ASP   A 1 295 ? -8.058  40.143 27.828  1.00 36.08  ? 292 ASP   A CG  1 
ATOM   2312 O  OD1 . ASP   A 1 295 ? -8.246  41.270 27.323  1.00 37.28  ? 292 ASP   A OD1 1 
ATOM   2313 O  OD2 . ASP   A 1 295 ? -8.016  39.919 29.081  1.00 37.62  ? 292 ASP   A OD2 1 
ATOM   2314 N  N   . MET   A 1 296 ? -8.896  36.895 24.681  1.00 32.56  ? 293 MET   A N   1 
ATOM   2315 C  CA  . MET   A 1 296 ? -8.673  35.620 23.948  1.00 32.03  ? 293 MET   A CA  1 
ATOM   2316 C  C   . MET   A 1 296 ? -8.670  35.898 22.441  1.00 32.53  ? 293 MET   A C   1 
ATOM   2317 O  O   . MET   A 1 296 ? -7.774  35.384 21.758  1.00 32.13  ? 293 MET   A O   1 
ATOM   2318 C  CB  . MET   A 1 296 ? -9.702  34.544 24.310  1.00 31.77  ? 293 MET   A CB  1 
ATOM   2319 C  CG  . MET   A 1 296 ? -9.525  34.048 25.746  1.00 31.40  ? 293 MET   A CG  1 
ATOM   2320 S  SD  . MET   A 1 296 ? -7.938  33.164 26.016  1.00 28.95  ? 293 MET   A SD  1 
ATOM   2321 C  CE  . MET   A 1 296 ? -8.145  31.681 25.023  1.00 27.96  ? 293 MET   A CE  1 
ATOM   2322 N  N   . LYS   A 1 297 ? -9.598  36.728 21.967  1.00 34.92  ? 294 LYS   A N   1 
ATOM   2323 C  CA  . LYS   A 1 297 ? -9.744  37.093 20.527  1.00 36.51  ? 294 LYS   A CA  1 
ATOM   2324 C  C   . LYS   A 1 297 ? -8.485  37.845 20.086  1.00 34.95  ? 294 LYS   A C   1 
ATOM   2325 O  O   . LYS   A 1 297 ? -7.928  37.501 19.072  1.00 33.58  ? 294 LYS   A O   1 
ATOM   2326 C  CB  . LYS   A 1 297 ? -11.054 37.865 20.371  1.00 41.15  ? 294 LYS   A CB  1 
ATOM   2327 C  CG  . LYS   A 1 297 ? -11.496 38.230 18.965  1.00 44.17  ? 294 LYS   A CG  1 
ATOM   2328 C  CD  . LYS   A 1 297 ? -12.952 38.741 18.947  1.00 48.94  ? 294 LYS   A CD  1 
ATOM   2329 C  CE  . LYS   A 1 297 ? -13.590 38.874 17.568  1.00 52.05  ? 294 LYS   A CE  1 
ATOM   2330 N  NZ  . LYS   A 1 297 ? -12.577 39.079 16.501  1.00 52.51  ? 294 LYS   A NZ  1 
ATOM   2331 N  N   . ALA   A 1 298 ? -7.982  38.778 20.890  1.00 35.17  ? 295 ALA   A N   1 
ATOM   2332 C  CA  . ALA   A 1 298 ? -6.757  39.530 20.545  1.00 35.24  ? 295 ALA   A CA  1 
ATOM   2333 C  C   . ALA   A 1 298 ? -5.576  38.563 20.448  1.00 33.16  ? 295 ALA   A C   1 
ATOM   2334 O  O   . ALA   A 1 298 ? -4.729  38.783 19.578  1.00 32.49  ? 295 ALA   A O   1 
ATOM   2335 C  CB  . ALA   A 1 298 ? -6.467  40.602 21.544  1.00 36.10  ? 295 ALA   A CB  1 
ATOM   2336 N  N   . ILE   A 1 299 ? -5.488  37.545 21.314  1.00 30.75  ? 296 ILE   A N   1 
ATOM   2337 C  CA  . ILE   A 1 299 ? -4.309  36.646 21.246  1.00 29.15  ? 296 ILE   A CA  1 
ATOM   2338 C  C   . ILE   A 1 299 ? -4.491  35.770 20.001  1.00 29.10  ? 296 ILE   A C   1 
ATOM   2339 O  O   . ILE   A 1 299 ? -3.498  35.528 19.282  1.00 28.90  ? 296 ILE   A O   1 
ATOM   2340 C  CB  . ILE   A 1 299 ? -4.091  35.832 22.544  1.00 27.33  ? 296 ILE   A CB  1 
ATOM   2341 C  CG1 . ILE   A 1 299 ? -3.831  36.758 23.738  1.00 27.68  ? 296 ILE   A CG1 1 
ATOM   2342 C  CG2 . ILE   A 1 299 ? -2.976  34.823 22.369  1.00 25.21  ? 296 ILE   A CG2 1 
ATOM   2343 C  CD1 . ILE   A 1 299 ? -4.120  36.090 25.057  1.00 27.00  ? 296 ILE   A CD1 1 
ATOM   2344 N  N   . ASP   A 1 300 ? -5.723  35.346 19.732  1.00 29.71  ? 297 ASP   A N   1 
ATOM   2345 C  CA  . ASP   A 1 300 ? -6.004  34.549 18.507  1.00 30.48  ? 297 ASP   A CA  1 
ATOM   2346 C  C   . ASP   A 1 300 ? -5.482  35.275 17.261  1.00 30.79  ? 297 ASP   A C   1 
ATOM   2347 O  O   . ASP   A 1 300 ? -4.994  34.615 16.326  1.00 29.84  ? 297 ASP   A O   1 
ATOM   2348 C  CB  . ASP   A 1 300 ? -7.490  34.310 18.274  1.00 31.90  ? 297 ASP   A CB  1 
ATOM   2349 C  CG  . ASP   A 1 300 ? -8.110  33.295 19.187  1.00 31.43  ? 297 ASP   A CG  1 
ATOM   2350 O  OD1 . ASP   A 1 300 ? -7.357  32.465 19.770  1.00 31.33  ? 297 ASP   A OD1 1 
ATOM   2351 O  OD2 . ASP   A 1 300 ? -9.343  33.366 19.326  1.00 33.67  ? 297 ASP   A OD2 1 
ATOM   2352 N  N   . GLY   A 1 301 ? -5.614  36.597 17.240  1.00 32.31  ? 298 GLY   A N   1 
ATOM   2353 C  CA  . GLY   A 1 301 ? -5.215  37.444 16.095  1.00 32.81  ? 298 GLY   A CA  1 
ATOM   2354 C  C   . GLY   A 1 301 ? -3.711  37.452 15.884  1.00 32.28  ? 298 GLY   A C   1 
ATOM   2355 O  O   . GLY   A 1 301 ? -3.299  37.928 14.832  1.00 33.39  ? 298 GLY   A O   1 
ATOM   2356 N  N   . LEU   A 1 302 ? -2.891  37.020 16.853  1.00 30.72  ? 299 LEU   A N   1 
ATOM   2357 C  CA  . LEU   A 1 302 ? -1.415  37.024 16.712  1.00 29.53  ? 299 LEU   A CA  1 
ATOM   2358 C  C   . LEU   A 1 302 ? -0.997  35.870 15.807  1.00 28.91  ? 299 LEU   A C   1 
ATOM   2359 O  O   . LEU   A 1 302 ? 0.182   35.831 15.483  1.00 28.24  ? 299 LEU   A O   1 
ATOM   2360 C  CB  . LEU   A 1 302 ? -0.751  36.900 18.085  1.00 28.27  ? 299 LEU   A CB  1 
ATOM   2361 C  CG  . LEU   A 1 302 ? -1.038  38.065 19.029  1.00 29.54  ? 299 LEU   A CG  1 
ATOM   2362 C  CD1 . LEU   A 1 302 ? -0.485  37.819 20.419  1.00 28.54  ? 299 LEU   A CD1 1 
ATOM   2363 C  CD2 . LEU   A 1 302 ? -0.513  39.381 18.442  1.00 31.03  ? 299 LEU   A CD2 1 
ATOM   2364 N  N   . ASP   A 1 303 ? -1.898  34.948 15.443  1.00 30.12  ? 300 ASP   A N   1 
ATOM   2365 C  CA  . ASP   A 1 303 ? -1.481  33.689 14.765  1.00 30.66  ? 300 ASP   A CA  1 
ATOM   2366 C  C   . ASP   A 1 303 ? -0.750  34.035 13.476  1.00 32.14  ? 300 ASP   A C   1 
ATOM   2367 O  O   . ASP   A 1 303 ? -1.231  34.932 12.728  1.00 33.03  ? 300 ASP   A O   1 
ATOM   2368 C  CB  . ASP   A 1 303 ? -2.630  32.710 14.528  1.00 32.10  ? 300 ASP   A CB  1 
ATOM   2369 C  CG  . ASP   A 1 303 ? -2.237  31.336 13.980  1.00 33.23  ? 300 ASP   A CG  1 
ATOM   2370 O  OD1 . ASP   A 1 303 ? -1.133  30.835 14.262  1.00 31.41  ? 300 ASP   A OD1 1 
ATOM   2371 O  OD2 . ASP   A 1 303 ? -3.079  30.752 13.259  1.00 38.42  ? 300 ASP   A OD2 1 
ATOM   2372 N  N   . ARG   A 1 304 ? 0.387   33.384 13.241  1.00 32.23  ? 301 ARG   A N   1 
ATOM   2373 C  CA  . ARG   A 1 304 ? 1.077   33.537 11.945  1.00 33.96  ? 301 ARG   A CA  1 
ATOM   2374 C  C   . ARG   A 1 304 ? 1.670   32.233 11.424  1.00 33.25  ? 301 ARG   A C   1 
ATOM   2375 O  O   . ARG   A 1 304 ? 2.504   32.353 10.492  1.00 32.20  ? 301 ARG   A O   1 
ATOM   2376 C  CB  . ARG   A 1 304 ? 2.126   34.643 11.992  1.00 36.07  ? 301 ARG   A CB  1 
ATOM   2377 C  CG  . ARG   A 1 304 ? 3.221   34.463 13.019  1.00 36.34  ? 301 ARG   A CG  1 
ATOM   2378 C  CD  . ARG   A 1 304 ? 3.705   35.857 13.332  1.00 39.84  ? 301 ARG   A CD  1 
ATOM   2379 N  NE  . ARG   A 1 304 ? 2.719   36.604 14.111  1.00 42.20  ? 301 ARG   A NE  1 
ATOM   2380 C  CZ  . ARG   A 1 304 ? 2.901   37.843 14.577  1.00 42.01  ? 301 ARG   A CZ  1 
ATOM   2381 N  NH1 . ARG   A 1 304 ? 4.014   38.496 14.283  1.00 42.78  ? 301 ARG   A NH1 1 
ATOM   2382 N  NH2 . ARG   A 1 304 ? 1.963   38.405 15.326  1.00 40.45  ? 301 ARG   A NH2 1 
ATOM   2383 N  N   . ASN   A 1 305 ? 1.226   31.065 11.904  1.00 32.88  ? 302 ASN   A N   1 
ATOM   2384 C  CA  . ASN   A 1 305 ? 1.694   29.778 11.324  1.00 34.99  ? 302 ASN   A CA  1 
ATOM   2385 C  C   . ASN   A 1 305 ? 3.227   29.716 11.399  1.00 34.14  ? 302 ASN   A C   1 
ATOM   2386 O  O   . ASN   A 1 305 ? 3.857   29.188 10.471  1.00 32.90  ? 302 ASN   A O   1 
ATOM   2387 C  CB  . ASN   A 1 305 ? 1.244   29.675 9.861   1.00 40.02  ? 302 ASN   A CB  1 
ATOM   2388 C  CG  . ASN   A 1 305 ? 1.509   28.335 9.196   1.00 43.41  ? 302 ASN   A CG  1 
ATOM   2389 O  OD1 . ASN   A 1 305 ? 2.248   28.254 8.209   1.00 46.30  ? 302 ASN   A OD1 1 
ATOM   2390 N  ND2 . ASN   A 1 305 ? 0.876   27.285 9.700   1.00 47.00  ? 302 ASN   A ND2 1 
ATOM   2391 N  N   . LEU   A 1 306 ? 3.821   30.267 12.455  1.00 32.76  ? 303 LEU   A N   1 
ATOM   2392 C  CA  . LEU   A 1 306 ? 5.289   30.347 12.592  1.00 33.65  ? 303 LEU   A CA  1 
ATOM   2393 C  C   . LEU   A 1 306 ? 5.713   29.158 13.434  1.00 31.38  ? 303 LEU   A C   1 
ATOM   2394 O  O   . LEU   A 1 306 ? 5.438   29.214 14.617  1.00 27.81  ? 303 LEU   A O   1 
ATOM   2395 C  CB  . LEU   A 1 306 ? 5.676   31.657 13.286  1.00 35.89  ? 303 LEU   A CB  1 
ATOM   2396 C  CG  . LEU   A 1 306 ? 7.125   31.739 13.767  1.00 38.04  ? 303 LEU   A CG  1 
ATOM   2397 C  CD1 . LEU   A 1 306 ? 8.075   31.914 12.611  1.00 40.41  ? 303 LEU   A CD1 1 
ATOM   2398 C  CD2 . LEU   A 1 306 ? 7.296   32.869 14.776  1.00 38.68  ? 303 LEU   A CD2 1 
ATOM   2399 N  N   . HIS   A 1 307 ? 6.278   28.098 12.849  1.00 31.27  ? 304 HIS   A N   1 
ATOM   2400 C  CA  . HIS   A 1 307 ? 7.042   27.134 13.685  1.00 32.33  ? 304 HIS   A CA  1 
ATOM   2401 C  C   . HIS   A 1 307 ? 8.467   27.646 13.910  1.00 31.62  ? 304 HIS   A C   1 
ATOM   2402 O  O   . HIS   A 1 307 ? 9.153   28.009 12.956  1.00 35.79  ? 304 HIS   A O   1 
ATOM   2403 C  CB  . HIS   A 1 307 ? 6.994   25.675 13.222  1.00 34.68  ? 304 HIS   A CB  1 
ATOM   2404 C  CG  . HIS   A 1 307 ? 7.164   25.443 11.774  1.00 36.67  ? 304 HIS   A CG  1 
ATOM   2405 N  ND1 . HIS   A 1 307 ? 8.407   25.184 11.222  1.00 39.88  ? 304 HIS   A ND1 1 
ATOM   2406 C  CD2 . HIS   A 1 307 ? 6.254   25.286 10.800  1.00 38.55  ? 304 HIS   A CD2 1 
ATOM   2407 C  CE1 . HIS   A 1 307 ? 8.266   24.940 9.939   1.00 41.60  ? 304 HIS   A CE1 1 
ATOM   2408 N  NE2 . HIS   A 1 307 ? 6.959   24.995 9.661   1.00 41.58  ? 304 HIS   A NE2 1 
ATOM   2409 N  N   . TYR   A 1 308 ? 8.883   27.658 15.173  1.00 29.19  ? 305 TYR   A N   1 
ATOM   2410 C  CA  . TYR   A 1 308 ? 10.220  28.137 15.600  1.00 28.36  ? 305 TYR   A CA  1 
ATOM   2411 C  C   . TYR   A 1 308 ? 11.299  27.156 15.116  1.00 29.02  ? 305 TYR   A C   1 
ATOM   2412 O  O   . TYR   A 1 308 ? 12.381  27.599 14.707  1.00 29.97  ? 305 TYR   A O   1 
ATOM   2413 C  CB  . TYR   A 1 308 ? 10.217  28.344 17.113  1.00 26.45  ? 305 TYR   A CB  1 
ATOM   2414 C  CG  . TYR   A 1 308 ? 9.657   29.676 17.525  1.00 25.68  ? 305 TYR   A CG  1 
ATOM   2415 C  CD1 . TYR   A 1 308 ? 10.345  30.838 17.221  1.00 25.90  ? 305 TYR   A CD1 1 
ATOM   2416 C  CD2 . TYR   A 1 308 ? 8.438   29.783 18.171  1.00 24.14  ? 305 TYR   A CD2 1 
ATOM   2417 C  CE1 . TYR   A 1 308 ? 9.850   32.068 17.583  1.00 26.18  ? 305 TYR   A CE1 1 
ATOM   2418 C  CE2 . TYR   A 1 308 ? 7.939   31.015 18.545  1.00 24.04  ? 305 TYR   A CE2 1 
ATOM   2419 C  CZ  . TYR   A 1 308 ? 8.653   32.151 18.265  1.00 25.33  ? 305 TYR   A CZ  1 
ATOM   2420 O  OH  . TYR   A 1 308 ? 8.183   33.385 18.607  1.00 25.96  ? 305 TYR   A OH  1 
ATOM   2421 N  N   . PHE   A 1 309 ? 11.031  25.863 15.197  1.00 28.47  ? 306 PHE   A N   1 
ATOM   2422 C  CA  . PHE   A 1 309 ? 12.001  24.798 14.841  1.00 30.29  ? 306 PHE   A CA  1 
ATOM   2423 C  C   . PHE   A 1 309 ? 11.935  24.520 13.349  1.00 33.23  ? 306 PHE   A C   1 
ATOM   2424 O  O   . PHE   A 1 309 ? 10.847  24.313 12.760  1.00 35.96  ? 306 PHE   A O   1 
ATOM   2425 C  CB  . PHE   A 1 309 ? 11.695  23.521 15.607  1.00 29.46  ? 306 PHE   A CB  1 
ATOM   2426 C  CG  . PHE   A 1 309 ? 11.772  23.736 17.087  1.00 28.42  ? 306 PHE   A CG  1 
ATOM   2427 C  CD1 . PHE   A 1 309 ? 12.925  24.204 17.689  1.00 30.09  ? 306 PHE   A CD1 1 
ATOM   2428 C  CD2 . PHE   A 1 309 ? 10.640  23.594 17.867  1.00 28.79  ? 306 PHE   A CD2 1 
ATOM   2429 C  CE1 . PHE   A 1 309 ? 12.961  24.433 19.061  1.00 29.55  ? 306 PHE   A CE1 1 
ATOM   2430 C  CE2 . PHE   A 1 309 ? 10.701  23.775 19.243  1.00 28.95  ? 306 PHE   A CE2 1 
ATOM   2431 C  CZ  . PHE   A 1 309 ? 11.852  24.226 19.828  1.00 28.06  ? 306 PHE   A CZ  1 
ATOM   2432 N  N   . ASN   A 1 310 ? 13.086  24.545 12.730  1.00 53.88  ? 307 ASN   A N   1 
ATOM   2433 C  CA  A ASN   A 1 310 ? 13.193  24.241 11.285  0.60 55.47  ? 307 ASN   A CA  1 
ATOM   2434 C  CA  B ASN   A 1 310 ? 13.212  24.263 11.279  0.40 54.38  ? 307 ASN   A CA  1 
ATOM   2435 C  C   . ASN   A 1 310 ? 14.374  23.290 11.109  1.00 56.35  ? 307 ASN   A C   1 
ATOM   2436 O  O   . ASN   A 1 310 ? 15.318  23.374 11.890  1.00 58.90  ? 307 ASN   A O   1 
ATOM   2437 C  CB  A ASN   A 1 310 ? 13.346  25.545 10.519  0.60 60.93  ? 307 ASN   A CB  1 
ATOM   2438 C  CB  B ASN   A 1 310 ? 13.351  25.546 10.458  0.40 58.42  ? 307 ASN   A CB  1 
ATOM   2439 C  CG  A ASN   A 1 310 ? 14.376  26.381 11.234  0.60 66.66  ? 307 ASN   A CG  1 
ATOM   2440 C  CG  B ASN   A 1 310 ? 12.004  26.077 10.013  0.40 55.89  ? 307 ASN   A CG  1 
ATOM   2441 O  OD1 A ASN   A 1 310 ? 15.531  25.965 11.322  0.60 69.46  ? 307 ASN   A OD1 1 
ATOM   2442 O  OD1 B ASN   A 1 310 ? 11.336  25.458 9.187   0.40 52.55  ? 307 ASN   A OD1 1 
ATOM   2443 N  ND2 A ASN   A 1 310 ? 13.959  27.495 11.820  0.60 69.46  ? 307 ASN   A ND2 1 
ATOM   2444 N  ND2 B ASN   A 1 310 ? 11.594  27.207 10.564  0.40 56.79  ? 307 ASN   A ND2 1 
ATOM   2445 N  N   . SER   A 1 311 ? 14.280  22.407 10.139  1.00 56.77  ? 308 SER   A N   1 
ATOM   2446 C  CA  . SER   A 1 311 ? 15.393  21.502 9.787   1.00 60.57  ? 308 SER   A CA  1 
ATOM   2447 C  C   . SER   A 1 311 ? 15.241  21.146 8.320   1.00 62.49  ? 308 SER   A C   1 
ATOM   2448 O  O   . SER   A 1 311 ? 14.272  20.438 8.021   1.00 59.27  ? 308 SER   A O   1 
ATOM   2449 C  CB  . SER   A 1 311 ? 15.348  20.262 10.623  1.00 57.44  ? 308 SER   A CB  1 
ATOM   2450 O  OG  . SER   A 1 311 ? 16.176  19.254 10.056  1.00 58.80  ? 308 SER   A OG  1 
ATOM   2451 N  N   . ASP   A 1 312 ? 16.138  21.613 7.454   1.00 69.84  ? 309 ASP   A N   1 
ATOM   2452 C  CA  . ASP   A 1 312 ? 16.029  21.289 6.010   1.00 73.11  ? 309 ASP   A CA  1 
ATOM   2453 C  C   . ASP   A 1 312 ? 16.299  19.782 5.875   1.00 70.74  ? 309 ASP   A C   1 
ATOM   2454 O  O   . ASP   A 1 312 ? 15.635  19.137 5.032   1.00 70.36  ? 309 ASP   A O   1 
ATOM   2455 C  CB  . ASP   A 1 312 ? 16.861  22.238 5.131   1.00 81.51  ? 309 ASP   A CB  1 
ATOM   2456 C  CG  . ASP   A 1 312 ? 18.333  22.312 5.503   1.00 86.79  ? 309 ASP   A CG  1 
ATOM   2457 O  OD1 . ASP   A 1 312 ? 18.686  21.758 6.559   1.00 83.73  ? 309 ASP   A OD1 1 
ATOM   2458 O  OD2 . ASP   A 1 312 ? 19.124  22.925 4.732   1.00 94.60  ? 309 ASP   A OD2 1 
ATOM   2459 N  N   . SER   A 1 313 ? 17.185  19.244 6.720   1.00 71.37  ? 310 SER   A N   1 
ATOM   2460 C  CA  . SER   A 1 313 ? 17.402  17.792 6.939   1.00 68.77  ? 310 SER   A CA  1 
ATOM   2461 C  C   . SER   A 1 313 ? 16.061  17.052 7.057   1.00 61.93  ? 310 SER   A C   1 
ATOM   2462 O  O   . SER   A 1 313 ? 15.860  16.100 6.274   1.00 64.13  ? 310 SER   A O   1 
ATOM   2463 C  CB  . SER   A 1 313 ? 18.238  17.563 8.148   1.00 71.39  ? 310 SER   A CB  1 
ATOM   2464 O  OG  . SER   A 1 313 ? 18.084  16.223 8.598   1.00 72.15  ? 310 SER   A OG  1 
ATOM   2465 N  N   . PHE   A 1 314 ? 15.158  17.471 7.951   1.00 54.82  ? 311 PHE   A N   1 
ATOM   2466 C  CA  . PHE   A 1 314 ? 13.885  16.738 8.210   1.00 50.03  ? 311 PHE   A CA  1 
ATOM   2467 C  C   . PHE   A 1 314 ? 12.782  17.169 7.250   1.00 48.34  ? 311 PHE   A C   1 
ATOM   2468 O  O   . PHE   A 1 314 ? 11.856  16.385 7.003   1.00 44.54  ? 311 PHE   A O   1 
ATOM   2469 C  CB  . PHE   A 1 314 ? 13.448  16.858 9.670   1.00 48.08  ? 311 PHE   A CB  1 
ATOM   2470 C  CG  . PHE   A 1 314 ? 14.312  15.949 10.487  1.00 47.87  ? 311 PHE   A CG  1 
ATOM   2471 C  CD1 . PHE   A 1 314 ? 14.203  14.585 10.304  1.00 48.18  ? 311 PHE   A CD1 1 
ATOM   2472 C  CD2 . PHE   A 1 314 ? 15.343  16.444 11.261  1.00 50.30  ? 311 PHE   A CD2 1 
ATOM   2473 C  CE1 . PHE   A 1 314 ? 15.051  13.721 10.966  1.00 50.21  ? 311 PHE   A CE1 1 
ATOM   2474 C  CE2 . PHE   A 1 314 ? 16.196  15.580 11.923  1.00 52.84  ? 311 PHE   A CE2 1 
ATOM   2475 C  CZ  . PHE   A 1 314 ? 16.044  14.219 11.779  1.00 52.06  ? 311 PHE   A CZ  1 
ATOM   2476 N  N   . ALA   A 1 315 ? 12.905  18.362 6.684   1.00 49.83  ? 312 ALA   A N   1 
ATOM   2477 C  CA  . ALA   A 1 315 ? 11.922  18.887 5.717   1.00 50.73  ? 312 ALA   A CA  1 
ATOM   2478 C  C   . ALA   A 1 315 ? 11.651  17.851 4.618   1.00 50.16  ? 312 ALA   A C   1 
ATOM   2479 O  O   . ALA   A 1 315 ? 10.528  17.872 4.058   1.00 48.72  ? 312 ALA   A O   1 
ATOM   2480 C  CB  . ALA   A 1 315 ? 12.432  20.177 5.121   1.00 54.93  ? 312 ALA   A CB  1 
ATOM   2481 N  N   . SER   A 1 316 ? 12.663  17.046 4.263   1.00 52.05  ? 313 SER   A N   1 
ATOM   2482 C  CA  . SER   A 1 316 ? 12.595  16.110 3.111   1.00 52.91  ? 313 SER   A CA  1 
ATOM   2483 C  C   . SER   A 1 316 ? 12.053  14.752 3.564   1.00 47.98  ? 313 SER   A C   1 
ATOM   2484 O  O   . SER   A 1 316 ? 11.748  13.926 2.687   1.00 49.01  ? 313 SER   A O   1 
ATOM   2485 C  CB  . SER   A 1 316 ? 13.931  15.971 2.439   1.00 58.67  ? 313 SER   A CB  1 
ATOM   2486 O  OG  . SER   A 1 316 ? 14.878  15.471 3.366   1.00 59.20  ? 313 SER   A OG  1 
ATOM   2487 N  N   . HIS   A 1 317 ? 11.898  14.518 4.872   1.00 42.67  ? 314 HIS   A N   1 
ATOM   2488 C  CA  . HIS   A 1 317 ? 11.423  13.197 5.354   1.00 39.92  ? 314 HIS   A CA  1 
ATOM   2489 C  C   . HIS   A 1 317 ? 10.019  12.945 4.820   1.00 39.31  ? 314 HIS   A C   1 
ATOM   2490 O  O   . HIS   A 1 317 ? 9.166   13.815 4.918   1.00 37.35  ? 314 HIS   A O   1 
ATOM   2491 C  CB  . HIS   A 1 317 ? 11.447  13.148 6.866   1.00 36.13  ? 314 HIS   A CB  1 
ATOM   2492 C  CG  . HIS   A 1 317 ? 11.381  11.770 7.417   1.00 35.55  ? 314 HIS   A CG  1 
ATOM   2493 N  ND1 . HIS   A 1 317 ? 10.254  10.967 7.283   1.00 35.44  ? 314 HIS   A ND1 1 
ATOM   2494 C  CD2 . HIS   A 1 317 ? 12.280  11.068 8.133   1.00 35.56  ? 314 HIS   A CD2 1 
ATOM   2495 C  CE1 . HIS   A 1 317 ? 10.462  9.837  7.928   1.00 36.24  ? 314 HIS   A CE1 1 
ATOM   2496 N  NE2 . HIS   A 1 317 ? 11.716  9.872  8.431   1.00 36.04  ? 314 HIS   A NE2 1 
ATOM   2497 N  N   . PRO   A 1 318 ? 9.684   11.738 4.322   1.00 41.22  ? 315 PRO   A N   1 
ATOM   2498 C  CA  . PRO   A 1 318 ? 8.297   11.461 3.941   1.00 42.26  ? 315 PRO   A CA  1 
ATOM   2499 C  C   . PRO   A 1 318 ? 7.241   11.783 5.016   1.00 39.47  ? 315 PRO   A C   1 
ATOM   2500 O  O   . PRO   A 1 318 ? 6.099   12.164 4.680   1.00 38.87  ? 315 PRO   A O   1 
ATOM   2501 C  CB  . PRO   A 1 318 ? 8.274   9.943  3.677   1.00 45.51  ? 315 PRO   A CB  1 
ATOM   2502 C  CG  . PRO   A 1 318 ? 9.729   9.553  3.437   1.00 46.90  ? 315 PRO   A CG  1 
ATOM   2503 C  CD  . PRO   A 1 318 ? 10.592  10.584 4.151   1.00 43.63  ? 315 PRO   A CD  1 
ATOM   2504 N  N   . ASN   A 1 319 ? 7.604   11.645 6.292   1.00 37.56  ? 316 ASN   A N   1 
ATOM   2505 C  CA  . ASN   A 1 319 ? 6.657   11.864 7.414   1.00 36.69  ? 316 ASN   A CA  1 
ATOM   2506 C  C   . ASN   A 1 319 ? 6.850   13.262 8.007   1.00 34.62  ? 316 ASN   A C   1 
ATOM   2507 O  O   . ASN   A 1 319 ? 6.349   13.509 9.139   1.00 33.40  ? 316 ASN   A O   1 
ATOM   2508 C  CB  . ASN   A 1 319 ? 6.800   10.778 8.479   1.00 38.58  ? 316 ASN   A CB  1 
ATOM   2509 C  CG  . ASN   A 1 319 ? 5.924   9.580  8.187   1.00 43.49  ? 316 ASN   A CG  1 
ATOM   2510 O  OD1 . ASN   A 1 319 ? 4.965   9.679  7.422   1.00 48.29  ? 316 ASN   A OD1 1 
ATOM   2511 N  ND2 . ASN   A 1 319 ? 6.248   8.451  8.792   1.00 45.95  ? 316 ASN   A ND2 1 
ATOM   2512 N  N   . TYR   A 1 320 ? 7.578   14.152 7.317   1.00 34.27  ? 317 TYR   A N   1 
ATOM   2513 C  CA  . TYR   A 1 320 ? 7.664   15.562 7.745   1.00 32.39  ? 317 TYR   A CA  1 
ATOM   2514 C  C   . TYR   A 1 320 ? 6.230   16.026 7.963   1.00 31.18  ? 317 TYR   A C   1 
ATOM   2515 O  O   . TYR   A 1 320 ? 5.379   15.900 7.069   1.00 31.46  ? 317 TYR   A O   1 
ATOM   2516 C  CB  . TYR   A 1 320 ? 8.374   16.424 6.696   1.00 34.44  ? 317 TYR   A CB  1 
ATOM   2517 C  CG  . TYR   A 1 320 ? 8.646   17.831 7.169   1.00 34.05  ? 317 TYR   A CG  1 
ATOM   2518 C  CD1 . TYR   A 1 320 ? 9.348   18.047 8.333   1.00 33.57  ? 317 TYR   A CD1 1 
ATOM   2519 C  CD2 . TYR   A 1 320 ? 8.272   18.942 6.427   1.00 36.29  ? 317 TYR   A CD2 1 
ATOM   2520 C  CE1 . TYR   A 1 320 ? 9.572   19.321 8.833   1.00 34.47  ? 317 TYR   A CE1 1 
ATOM   2521 C  CE2 . TYR   A 1 320 ? 8.517   20.228 6.881   1.00 36.80  ? 317 TYR   A CE2 1 
ATOM   2522 C  CZ  . TYR   A 1 320 ? 9.174   20.426 8.083   1.00 37.08  ? 317 TYR   A CZ  1 
ATOM   2523 O  OH  . TYR   A 1 320 ? 9.437   21.701 8.520   1.00 39.66  ? 317 TYR   A OH  1 
ATOM   2524 N  N   . PRO   A 1 321 ? 5.876   16.467 9.178   1.00 29.76  ? 318 PRO   A N   1 
ATOM   2525 C  CA  . PRO   A 1 321 ? 4.490   16.800 9.470   1.00 30.09  ? 318 PRO   A CA  1 
ATOM   2526 C  C   . PRO   A 1 321 ? 4.047   18.138 8.882   1.00 31.89  ? 318 PRO   A C   1 
ATOM   2527 O  O   . PRO   A 1 321 ? 2.867   18.390 8.880   1.00 31.66  ? 318 PRO   A O   1 
ATOM   2528 C  CB  . PRO   A 1 321 ? 4.444   16.905 10.988  1.00 28.66  ? 318 PRO   A CB  1 
ATOM   2529 C  CG  . PRO   A 1 321 ? 5.856   17.231 11.394  1.00 27.76  ? 318 PRO   A CG  1 
ATOM   2530 C  CD  . PRO   A 1 321 ? 6.762   16.643 10.331  1.00 29.08  ? 318 PRO   A CD  1 
ATOM   2531 N  N   . TYR   A 1 322 ? 4.989   19.014 8.509   1.00 34.10  ? 319 TYR   A N   1 
ATOM   2532 C  CA  . TYR   A 1 322 ? 4.593   20.337 7.961   1.00 37.74  ? 319 TYR   A CA  1 
ATOM   2533 C  C   . TYR   A 1 322 ? 4.580   20.231 6.427   1.00 43.41  ? 319 TYR   A C   1 
ATOM   2534 O  O   . TYR   A 1 322 ? 4.093   21.172 5.839   1.00 48.52  ? 319 TYR   A O   1 
ATOM   2535 C  CB  . TYR   A 1 322 ? 5.439   21.451 8.571   1.00 37.32  ? 319 TYR   A CB  1 
ATOM   2536 C  CG  . TYR   A 1 322 ? 5.442   21.507 10.088  1.00 35.66  ? 319 TYR   A CG  1 
ATOM   2537 C  CD1 . TYR   A 1 322 ? 4.276   21.563 10.851  1.00 34.70  ? 319 TYR   A CD1 1 
ATOM   2538 C  CD2 . TYR   A 1 322 ? 6.647   21.548 10.776  1.00 35.55  ? 319 TYR   A CD2 1 
ATOM   2539 C  CE1 . TYR   A 1 322 ? 4.322   21.617 12.250  1.00 33.87  ? 319 TYR   A CE1 1 
ATOM   2540 C  CE2 . TYR   A 1 322 ? 6.707   21.637 12.160  1.00 34.81  ? 319 TYR   A CE2 1 
ATOM   2541 C  CZ  . TYR   A 1 322 ? 5.545   21.663 12.912  1.00 34.13  ? 319 TYR   A CZ  1 
ATOM   2542 O  OH  . TYR   A 1 322 ? 5.677   21.770 14.286  1.00 34.20  ? 319 TYR   A OH  1 
ATOM   2543 N  N   . SER   A 1 323 ? 4.797   19.015 5.904   1.00 49.06  ? 320 SER   A N   1 
ATOM   2544 C  CA  . SER   A 1 323 ? 5.345   18.621 4.565   1.00 57.32  ? 320 SER   A CA  1 
ATOM   2545 C  C   . SER   A 1 323 ? 4.601   19.211 3.372   1.00 65.23  ? 320 SER   A C   1 
ATOM   2546 O  O   . SER   A 1 323 ? 5.245   19.293 2.305   1.00 74.81  ? 320 SER   A O   1 
ATOM   2547 C  CB  . SER   A 1 323 ? 5.387   17.112 4.433   1.00 57.32  ? 320 SER   A CB  1 
ATOM   2548 O  OG  . SER   A 1 323 ? 5.675   16.703 3.112   1.00 59.03  ? 320 SER   A OG  1 
ATOM   2549 N  N   . ASP   A 1 324 ? 3.315   19.559 3.495   1.00 69.47  ? 321 ASP   A N   1 
ATOM   2550 C  CA  . ASP   A 1 324 ? 2.508   20.021 2.327   1.00 74.47  ? 321 ASP   A CA  1 
ATOM   2551 C  C   . ASP   A 1 324 ? 1.925   21.420 2.618   1.00 75.79  ? 321 ASP   A C   1 
ATOM   2552 O  O   . ASP   A 1 324 ? 0.793   21.736 2.140   1.00 75.40  ? 321 ASP   A O   1 
ATOM   2553 C  CB  . ASP   A 1 324 ? 1.477   18.945 1.962   1.00 78.17  ? 321 ASP   A CB  1 
ATOM   2554 C  CG  . ASP   A 1 324 ? 2.074   17.588 1.582   1.00 80.00  ? 321 ASP   A CG  1 
ATOM   2555 O  OD1 . ASP   A 1 324 ? 2.256   17.342 0.362   1.00 82.60  ? 321 ASP   A OD1 1 
ATOM   2556 O  OD2 . ASP   A 1 324 ? 2.344   16.773 2.514   1.00 78.81  ? 321 ASP   A OD2 1 
ATOM   2557 N  N   . GLU   A 1 325 ? 2.700   22.242 3.349   1.00 75.28  ? 322 GLU   A N   1 
ATOM   2558 C  CA  . GLU   A 1 325 ? 2.392   23.655 3.736   1.00 73.40  ? 322 GLU   A CA  1 
ATOM   2559 C  C   . GLU   A 1 325 ? 2.290   24.545 2.477   1.00 76.14  ? 322 GLU   A C   1 
ATOM   2560 O  O   . GLU   A 1 325 ? 1.398   25.430 2.419   1.00 81.38  ? 322 GLU   A O   1 
ATOM   2561 C  CB  . GLU   A 1 325 ? 3.496   24.168 4.675   1.00 74.13  ? 322 GLU   A CB  1 
ATOM   2562 C  CG  . GLU   A 1 325 ? 3.403   25.660 5.021   1.00 77.89  ? 322 GLU   A CG  1 
ATOM   2563 C  CD  . GLU   A 1 325 ? 4.644   26.555 4.850   1.00 82.48  ? 322 GLU   A CD  1 
ATOM   2564 O  OE1 . GLU   A 1 325 ? 5.388   26.786 5.850   1.00 81.40  ? 322 GLU   A OE1 1 
ATOM   2565 O  OE2 . GLU   A 1 325 ? 4.831   27.105 3.721   1.00 86.65  ? 322 GLU   A OE2 1 
ATOM   2566 N  N   . TYR   A 1 326 ? 3.205   24.365 1.518   1.00 73.73  ? 323 TYR   A N   1 
ATOM   2567 C  CA  . TYR   A 1 326 ? 3.244   25.124 0.229   1.00 75.48  ? 323 TYR   A CA  1 
ATOM   2568 C  C   . TYR   A 1 326 ? 3.574   24.179 -0.941  1.00 75.91  ? 323 TYR   A C   1 
ATOM   2569 O  O   . TYR   A 1 326 ? 3.965   23.020 -0.602  1.00 69.14  ? 323 TYR   A O   1 
ATOM   2570 C  CB  . TYR   A 1 326 ? 4.256   26.273 0.319   1.00 77.55  ? 323 TYR   A CB  1 
ATOM   2571 C  CG  . TYR   A 1 326 ? 5.667   25.860 -0.015  1.00 79.59  ? 323 TYR   A CG  1 
ATOM   2572 C  CD1 . TYR   A 1 326 ? 6.155   25.999 -1.308  1.00 84.55  ? 323 TYR   A CD1 1 
ATOM   2573 C  CD2 . TYR   A 1 326 ? 6.478   25.249 0.937   1.00 75.78  ? 323 TYR   A CD2 1 
ATOM   2574 C  CE1 . TYR   A 1 326 ? 7.436   25.597 -1.640  1.00 88.17  ? 323 TYR   A CE1 1 
ATOM   2575 C  CE2 . TYR   A 1 326 ? 7.763   24.836 0.618   1.00 79.04  ? 323 TYR   A CE2 1 
ATOM   2576 C  CZ  . TYR   A 1 326 ? 8.236   25.013 -0.671  1.00 86.09  ? 323 TYR   A CZ  1 
ATOM   2577 O  OH  . TYR   A 1 326 ? 9.499   24.626 -0.984  1.00 92.08  ? 323 TYR   A OH  1 
ATOM   2578 O  OXT . TYR   A 1 326 ? 3.470   24.550 -2.176  1.00 74.55  ? 323 TYR   A OXT 1 
ATOM   2579 N  N   . GLN   B 1 9   ? 6.866   48.434 -18.021 1.00 53.97  ? 6   GLN   B N   1 
ATOM   2580 C  CA  . GLN   B 1 9   ? 7.658   47.493 -17.180 1.00 53.33  ? 6   GLN   B CA  1 
ATOM   2581 C  C   . GLN   B 1 9   ? 7.044   46.082 -17.293 1.00 47.54  ? 6   GLN   B C   1 
ATOM   2582 O  O   . GLN   B 1 9   ? 5.887   45.818 -16.880 1.00 41.96  ? 6   GLN   B O   1 
ATOM   2583 C  CB  . GLN   B 1 9   ? 7.810   47.945 -15.717 1.00 57.21  ? 6   GLN   B CB  1 
ATOM   2584 C  CG  . GLN   B 1 9   ? 8.969   47.231 -15.004 1.00 60.95  ? 6   GLN   B CG  1 
ATOM   2585 C  CD  . GLN   B 1 9   ? 8.842   47.015 -13.507 1.00 63.82  ? 6   GLN   B CD  1 
ATOM   2586 O  OE1 . GLN   B 1 9   ? 8.382   47.890 -12.770 1.00 67.50  ? 6   GLN   B OE1 1 
ATOM   2587 N  NE2 . GLN   B 1 9   ? 9.308   45.864 -13.024 1.00 62.88  ? 6   GLN   B NE2 1 
ATOM   2588 N  N   . CYS   B 1 10  ? 7.852   45.191 -17.827 1.00 47.08  ? 7   CYS   B N   1 
ATOM   2589 C  CA  . CYS   B 1 10  ? 7.469   43.830 -18.263 1.00 45.61  ? 7   CYS   B CA  1 
ATOM   2590 C  C   . CYS   B 1 10  ? 8.479   42.879 -17.627 1.00 43.59  ? 7   CYS   B C   1 
ATOM   2591 O  O   . CYS   B 1 10  ? 9.538   43.367 -17.223 1.00 45.26  ? 7   CYS   B O   1 
ATOM   2592 C  CB  . CYS   B 1 10  ? 7.504   43.747 -19.788 1.00 48.64  ? 7   CYS   B CB  1 
ATOM   2593 S  SG  . CYS   B 1 10  ? 6.027   44.412 -20.609 1.00 51.71  ? 7   CYS   B SG  1 
ATOM   2594 N  N   . VAL   B 1 11  ? 8.162   41.590 -17.550 1.00 40.77  ? 8   VAL   B N   1 
ATOM   2595 C  CA  . VAL   B 1 11  ? 9.139   40.524 -17.207 1.00 40.76  ? 8   VAL   B CA  1 
ATOM   2596 C  C   . VAL   B 1 11  ? 9.199   39.584 -18.402 1.00 39.91  ? 8   VAL   B C   1 
ATOM   2597 O  O   . VAL   B 1 11  ? 8.151   39.426 -19.085 1.00 39.46  ? 8   VAL   B O   1 
ATOM   2598 C  CB  . VAL   B 1 11  ? 8.773   39.791 -15.906 1.00 40.27  ? 8   VAL   B CB  1 
ATOM   2599 C  CG1 . VAL   B 1 11  ? 8.799   40.777 -14.753 1.00 41.79  ? 8   VAL   B CG1 1 
ATOM   2600 C  CG2 . VAL   B 1 11  ? 7.429   39.089 -15.983 1.00 37.99  ? 8   VAL   B CG2 1 
ATOM   2601 N  N   . LYS   B 1 12  ? 10.365  38.986 -18.621 1.00 40.46  ? 9   LYS   B N   1 
ATOM   2602 C  CA  . LYS   B 1 12  ? 10.586  38.064 -19.749 1.00 41.71  ? 9   LYS   B CA  1 
ATOM   2603 C  C   . LYS   B 1 12  ? 10.149  36.677 -19.277 1.00 39.17  ? 9   LYS   B C   1 
ATOM   2604 O  O   . LYS   B 1 12  ? 10.677  36.191 -18.273 1.00 40.21  ? 9   LYS   B O   1 
ATOM   2605 C  CB  . LYS   B 1 12  ? 12.035  38.104 -20.226 1.00 44.94  ? 9   LYS   B CB  1 
ATOM   2606 C  CG  . LYS   B 1 12  ? 12.244  37.379 -21.543 1.00 47.33  ? 9   LYS   B CG  1 
ATOM   2607 C  CD  . LYS   B 1 12  ? 13.673  37.074 -21.819 1.00 50.75  ? 9   LYS   B CD  1 
ATOM   2608 C  CE  . LYS   B 1 12  ? 13.857  36.637 -23.252 1.00 54.15  ? 9   LYS   B CE  1 
ATOM   2609 N  NZ  . LYS   B 1 12  ? 15.262  36.834 -23.675 1.00 58.54  ? 9   LYS   B NZ  1 
ATOM   2610 N  N   . LEU   B 1 13  ? 9.150   36.086 -19.929 1.00 37.12  ? 10  LEU   B N   1 
ATOM   2611 C  CA  . LEU   B 1 13  ? 8.684   34.730 -19.547 1.00 34.29  ? 10  LEU   B CA  1 
ATOM   2612 C  C   . LEU   B 1 13  ? 9.677   33.682 -20.063 1.00 34.95  ? 10  LEU   B C   1 
ATOM   2613 O  O   . LEU   B 1 13  ? 10.505  33.985 -20.951 1.00 35.85  ? 10  LEU   B O   1 
ATOM   2614 C  CB  . LEU   B 1 13  ? 7.285   34.516 -20.122 1.00 32.95  ? 10  LEU   B CB  1 
ATOM   2615 C  CG  . LEU   B 1 13  ? 6.245   35.567 -19.740 1.00 31.75  ? 10  LEU   B CG  1 
ATOM   2616 C  CD1 . LEU   B 1 13  ? 4.947   35.339 -20.497 1.00 30.80  ? 10  LEU   B CD1 1 
ATOM   2617 C  CD2 . LEU   B 1 13  ? 5.962   35.592 -18.248 1.00 31.20  ? 10  LEU   B CD2 1 
ATOM   2618 N  N   . ASN   B 1 14  ? 9.559   32.458 -19.564 1.00 34.19  ? 11  ASN   B N   1 
ATOM   2619 C  CA  . ASN   B 1 14  ? 10.506  31.372 -19.911 1.00 35.98  ? 11  ASN   B CA  1 
ATOM   2620 C  C   . ASN   B 1 14  ? 10.293  30.877 -21.358 1.00 36.79  ? 11  ASN   B C   1 
ATOM   2621 O  O   . ASN   B 1 14  ? 11.100  30.046 -21.747 1.00 38.45  ? 11  ASN   B O   1 
ATOM   2622 C  CB  . ASN   B 1 14  ? 10.440  30.247 -18.881 1.00 35.38  ? 11  ASN   B CB  1 
ATOM   2623 C  CG  . ASN   B 1 14  ? 9.094   29.559 -18.803 1.00 33.97  ? 11  ASN   B CG  1 
ATOM   2624 O  OD1 . ASN   B 1 14  ? 8.431   29.373 -19.821 1.00 34.13  ? 11  ASN   B OD1 1 
ATOM   2625 N  ND2 . ASN   B 1 14  ? 8.708   29.115 -17.617 1.00 32.90  ? 11  ASN   B ND2 1 
ATOM   2626 N  N   . ASP   B 1 15  ? 9.281   31.364 -22.113 1.00 35.99  ? 12  ASP   B N   1 
ATOM   2627 C  CA  . ASP   B 1 15  ? 9.089   31.072 -23.563 1.00 36.92  ? 12  ASP   B CA  1 
ATOM   2628 C  C   . ASP   B 1 15  ? 9.466   32.272 -24.450 1.00 38.23  ? 12  ASP   B C   1 
ATOM   2629 O  O   . ASP   B 1 15  ? 9.169   32.222 -25.660 1.00 38.20  ? 12  ASP   B O   1 
ATOM   2630 C  CB  . ASP   B 1 15  ? 7.653   30.646 -23.861 1.00 35.94  ? 12  ASP   B CB  1 
ATOM   2631 C  CG  . ASP   B 1 15  ? 6.624   31.754 -23.727 1.00 35.35  ? 12  ASP   B CG  1 
ATOM   2632 O  OD1 . ASP   B 1 15  ? 7.014   32.875 -23.300 1.00 35.59  ? 12  ASP   B OD1 1 
ATOM   2633 O  OD2 . ASP   B 1 15  ? 5.422   31.493 -24.041 1.00 34.93  ? 12  ASP   B OD2 1 
ATOM   2634 N  N   . GLY   B 1 16  ? 10.047  33.340 -23.892 1.00 38.30  ? 13  GLY   B N   1 
ATOM   2635 C  CA  . GLY   B 1 16  ? 10.586  34.454 -24.694 1.00 39.90  ? 13  GLY   B CA  1 
ATOM   2636 C  C   . GLY   B 1 16  ? 9.607   35.606 -24.819 1.00 39.23  ? 13  GLY   B C   1 
ATOM   2637 O  O   . GLY   B 1 16  ? 10.031  36.669 -25.235 1.00 41.41  ? 13  GLY   B O   1 
ATOM   2638 N  N   . HIS   B 1 17  ? 8.325   35.400 -24.527 1.00 37.88  ? 14  HIS   B N   1 
ATOM   2639 C  CA  . HIS   B 1 17  ? 7.301   36.476 -24.508 1.00 37.78  ? 14  HIS   B CA  1 
ATOM   2640 C  C   . HIS   B 1 17  ? 7.434   37.334 -23.236 1.00 37.05  ? 14  HIS   B C   1 
ATOM   2641 O  O   . HIS   B 1 17  ? 8.116   36.915 -22.268 1.00 36.47  ? 14  HIS   B O   1 
ATOM   2642 C  CB  . HIS   B 1 17  ? 5.889   35.886 -24.637 1.00 37.30  ? 14  HIS   B CB  1 
ATOM   2643 C  CG  . HIS   B 1 17  ? 5.646   35.247 -25.962 1.00 38.88  ? 14  HIS   B CG  1 
ATOM   2644 N  ND1 . HIS   B 1 17  ? 5.422   33.871 -26.118 1.00 39.23  ? 14  HIS   B ND1 1 
ATOM   2645 C  CD2 . HIS   B 1 17  ? 5.621   35.787 -27.199 1.00 40.13  ? 14  HIS   B CD2 1 
ATOM   2646 C  CE1 . HIS   B 1 17  ? 5.250   33.610 -27.413 1.00 39.55  ? 14  HIS   B CE1 1 
ATOM   2647 N  NE2 . HIS   B 1 17  ? 5.399   34.760 -28.089 1.00 40.76  ? 14  HIS   B NE2 1 
ATOM   2648 N  N   . PHE   B 1 18  ? 6.751   38.480 -23.245 1.00 37.40  ? 15  PHE   B N   1 
ATOM   2649 C  CA  . PHE   B 1 18  ? 6.843   39.563 -22.233 1.00 37.09  ? 15  PHE   B CA  1 
ATOM   2650 C  C   . PHE   B 1 18  ? 5.476   39.777 -21.615 1.00 35.20  ? 15  PHE   B C   1 
ATOM   2651 O  O   . PHE   B 1 18  ? 4.464   39.851 -22.336 1.00 33.99  ? 15  PHE   B O   1 
ATOM   2652 C  CB  . PHE   B 1 18  ? 7.399   40.855 -22.833 1.00 40.06  ? 15  PHE   B CB  1 
ATOM   2653 C  CG  . PHE   B 1 18  ? 8.844   40.714 -23.214 1.00 43.32  ? 15  PHE   B CG  1 
ATOM   2654 C  CD1 . PHE   B 1 18  ? 9.834   40.833 -22.258 1.00 44.54  ? 15  PHE   B CD1 1 
ATOM   2655 C  CD2 . PHE   B 1 18  ? 9.204   40.409 -24.521 1.00 46.42  ? 15  PHE   B CD2 1 
ATOM   2656 C  CE1 . PHE   B 1 18  ? 11.173  40.696 -22.608 1.00 47.67  ? 15  PHE   B CE1 1 
ATOM   2657 C  CE2 . PHE   B 1 18  ? 10.540  40.262 -24.869 1.00 48.89  ? 15  PHE   B CE2 1 
ATOM   2658 C  CZ  . PHE   B 1 18  ? 11.520  40.383 -23.906 1.00 49.00  ? 15  PHE   B CZ  1 
ATOM   2659 N  N   . MET   B 1 19  ? 5.474   39.852 -20.287 1.00 33.19  ? 16  MET   B N   1 
ATOM   2660 C  CA  . MET   B 1 19  ? 4.243   40.060 -19.507 1.00 31.38  ? 16  MET   B CA  1 
ATOM   2661 C  C   . MET   B 1 19  ? 4.387   41.358 -18.734 1.00 30.38  ? 16  MET   B C   1 
ATOM   2662 O  O   . MET   B 1 19  ? 5.345   41.501 -17.966 1.00 31.14  ? 16  MET   B O   1 
ATOM   2663 C  CB  . MET   B 1 19  ? 4.037   38.873 -18.563 1.00 30.89  ? 16  MET   B CB  1 
ATOM   2664 C  CG  . MET   B 1 19  ? 2.872   39.049 -17.637 1.00 30.96  ? 16  MET   B CG  1 
ATOM   2665 S  SD  . MET   B 1 19  ? 2.870   37.832 -16.275 1.00 32.00  ? 16  MET   B SD  1 
ATOM   2666 C  CE  . MET   B 1 19  ? 2.087   36.504 -17.184 1.00 30.11  ? 16  MET   B CE  1 
ATOM   2667 N  N   . PRO   B 1 20  ? 3.481   42.351 -18.899 1.00 29.98  ? 17  PRO   B N   1 
ATOM   2668 C  CA  . PRO   B 1 20  ? 3.516   43.533 -18.028 1.00 30.34  ? 17  PRO   B CA  1 
ATOM   2669 C  C   . PRO   B 1 20  ? 3.345   43.158 -16.548 1.00 29.13  ? 17  PRO   B C   1 
ATOM   2670 O  O   . PRO   B 1 20  ? 2.538   42.294 -16.240 1.00 27.16  ? 17  PRO   B O   1 
ATOM   2671 C  CB  . PRO   B 1 20  ? 2.318   44.351 -18.498 1.00 30.42  ? 17  PRO   B CB  1 
ATOM   2672 C  CG  . PRO   B 1 20  ? 2.091   43.885 -19.916 1.00 30.27  ? 17  PRO   B CG  1 
ATOM   2673 C  CD  . PRO   B 1 20  ? 2.395   42.409 -19.894 1.00 29.27  ? 17  PRO   B CD  1 
ATOM   2674 N  N   . VAL   B 1 21  ? 4.111   43.782 -15.653 1.00 29.92  ? 18  VAL   B N   1 
ATOM   2675 C  CA  . VAL   B 1 21  ? 4.170   43.351 -14.227 1.00 29.76  ? 18  VAL   B CA  1 
ATOM   2676 C  C   . VAL   B 1 21  ? 2.963   43.852 -13.432 1.00 28.99  ? 18  VAL   B C   1 
ATOM   2677 O  O   . VAL   B 1 21  ? 2.712   43.279 -12.340 1.00 28.93  ? 18  VAL   B O   1 
ATOM   2678 C  CB  . VAL   B 1 21  ? 5.483   43.775 -13.566 1.00 32.22  ? 18  VAL   B CB  1 
ATOM   2679 C  CG1 . VAL   B 1 21  ? 6.667   43.140 -14.279 1.00 33.65  ? 18  VAL   B CG1 1 
ATOM   2680 C  CG2 . VAL   B 1 21  ? 5.628   45.288 -13.451 1.00 33.94  ? 18  VAL   B CG2 1 
ATOM   2681 N  N   . LEU   B 1 22  ? 2.247   44.869 -13.912 1.00 29.54  ? 19  LEU   B N   1 
ATOM   2682 C  CA  . LEU   B 1 22  ? 0.930   45.255 -13.344 1.00 29.54  ? 19  LEU   B CA  1 
ATOM   2683 C  C   . LEU   B 1 22  ? -0.211  44.814 -14.246 1.00 29.57  ? 19  LEU   B C   1 
ATOM   2684 O  O   . LEU   B 1 22  ? -0.252  45.206 -15.438 1.00 31.64  ? 19  LEU   B O   1 
ATOM   2685 C  CB  . LEU   B 1 22  ? 0.863   46.763 -13.158 1.00 31.05  ? 19  LEU   B CB  1 
ATOM   2686 C  CG  . LEU   B 1 22  ? -0.483  47.299 -12.680 1.00 30.71  ? 19  LEU   B CG  1 
ATOM   2687 C  CD1 . LEU   B 1 22  ? -0.788  46.871 -11.260 1.00 30.66  ? 19  LEU   B CD1 1 
ATOM   2688 C  CD2 . LEU   B 1 22  ? -0.503  48.812 -12.809 1.00 33.06  ? 19  LEU   B CD2 1 
ATOM   2689 N  N   . GLY   B 1 23  ? -1.150  44.064 -13.694 1.00 28.22  ? 20  GLY   B N   1 
ATOM   2690 C  CA  . GLY   B 1 23  ? -2.296  43.586 -14.490 1.00 27.05  ? 20  GLY   B CA  1 
ATOM   2691 C  C   . GLY   B 1 23  ? -3.629  44.091 -13.964 1.00 26.60  ? 20  GLY   B C   1 
ATOM   2692 O  O   . GLY   B 1 23  ? -3.791  44.294 -12.710 1.00 24.90  ? 20  GLY   B O   1 
ATOM   2693 N  N   . PHE   B 1 24  ? -4.614  44.207 -14.850 1.00 25.63  ? 21  PHE   B N   1 
ATOM   2694 C  CA  . PHE   B 1 24  ? -5.970  44.659 -14.467 1.00 25.60  ? 21  PHE   B CA  1 
ATOM   2695 C  C   . PHE   B 1 24  ? -6.837  43.439 -14.151 1.00 24.65  ? 21  PHE   B C   1 
ATOM   2696 O  O   . PHE   B 1 24  ? -7.018  42.537 -15.030 1.00 23.61  ? 21  PHE   B O   1 
ATOM   2697 C  CB  . PHE   B 1 24  ? -6.602  45.522 -15.556 1.00 26.23  ? 21  PHE   B CB  1 
ATOM   2698 C  CG  . PHE   B 1 24  ? -7.935  46.099 -15.152 1.00 26.58  ? 21  PHE   B CG  1 
ATOM   2699 C  CD1 . PHE   B 1 24  ? -8.054  46.957 -14.076 1.00 27.31  ? 21  PHE   B CD1 1 
ATOM   2700 C  CD2 . PHE   B 1 24  ? -9.094  45.769 -15.819 1.00 25.68  ? 21  PHE   B CD2 1 
ATOM   2701 C  CE1 . PHE   B 1 24  ? -9.288  47.480 -13.709 1.00 27.50  ? 21  PHE   B CE1 1 
ATOM   2702 C  CE2 . PHE   B 1 24  ? -10.331 46.247 -15.413 1.00 26.18  ? 21  PHE   B CE2 1 
ATOM   2703 C  CZ  . PHE   B 1 24  ? -10.418 47.156 -14.391 1.00 27.01  ? 21  PHE   B CZ  1 
ATOM   2704 N  N   . GLY   B 1 25  ? -7.403  43.393 -12.951 1.00 24.43  ? 22  GLY   B N   1 
ATOM   2705 C  CA  . GLY   B 1 25  ? -8.308  42.298 -12.568 1.00 24.52  ? 22  GLY   B CA  1 
ATOM   2706 C  C   . GLY   B 1 25  ? -9.744  42.595 -12.981 1.00 24.64  ? 22  GLY   B C   1 
ATOM   2707 O  O   . GLY   B 1 25  ? -10.243 43.645 -12.591 1.00 26.03  ? 22  GLY   B O   1 
ATOM   2708 N  N   . THR   B 1 26  ? -10.392 41.719 -13.757 1.00 23.58  ? 23  THR   B N   1 
ATOM   2709 C  CA  . THR   B 1 26  ? -11.701 42.046 -14.361 1.00 23.82  ? 23  THR   B CA  1 
ATOM   2710 C  C   . THR   B 1 26  ? -12.854 41.377 -13.634 1.00 24.37  ? 23  THR   B C   1 
ATOM   2711 O  O   . THR   B 1 26  ? -14.011 41.703 -13.971 1.00 25.51  ? 23  THR   B O   1 
ATOM   2712 C  CB  . THR   B 1 26  ? -11.813 41.739 -15.868 1.00 22.83  ? 23  THR   B CB  1 
ATOM   2713 O  OG1 . THR   B 1 26  ? -11.601 40.363 -16.173 1.00 22.31  ? 23  THR   B OG1 1 
ATOM   2714 C  CG2 . THR   B 1 26  ? -10.825 42.534 -16.678 1.00 22.81  ? 23  THR   B CG2 1 
ATOM   2715 N  N   . TYR   B 1 27  ? -12.607 40.491 -12.680 1.00 24.63  ? 24  TYR   B N   1 
ATOM   2716 C  CA  . TYR   B 1 27  ? -13.745 39.790 -12.053 1.00 25.34  ? 24  TYR   B CA  1 
ATOM   2717 C  C   . TYR   B 1 27  ? -14.561 40.797 -11.269 1.00 27.00  ? 24  TYR   B C   1 
ATOM   2718 O  O   . TYR   B 1 27  ? -13.990 41.497 -10.404 1.00 27.97  ? 24  TYR   B O   1 
ATOM   2719 C  CB  . TYR   B 1 27  ? -13.344 38.712 -11.042 1.00 25.36  ? 24  TYR   B CB  1 
ATOM   2720 C  CG  . TYR   B 1 27  ? -14.554 38.037 -10.452 1.00 26.02  ? 24  TYR   B CG  1 
ATOM   2721 C  CD1 . TYR   B 1 27  ? -15.263 37.085 -11.179 1.00 26.61  ? 24  TYR   B CD1 1 
ATOM   2722 C  CD2 . TYR   B 1 27  ? -15.026 38.389 -9.198  1.00 26.70  ? 24  TYR   B CD2 1 
ATOM   2723 C  CE1 . TYR   B 1 27  ? -16.397 36.482 -10.657 1.00 28.00  ? 24  TYR   B CE1 1 
ATOM   2724 C  CE2 . TYR   B 1 27  ? -16.173 37.824 -8.679  1.00 28.39  ? 24  TYR   B CE2 1 
ATOM   2725 C  CZ  . TYR   B 1 27  ? -16.843 36.840 -9.397  1.00 29.46  ? 24  TYR   B CZ  1 
ATOM   2726 O  OH  . TYR   B 1 27  ? -17.977 36.257 -8.902  1.00 33.10  ? 24  TYR   B OH  1 
ATOM   2727 N  N   . ALA   B 1 28  ? -15.868 40.764 -11.459 1.00 28.04  ? 25  ALA   B N   1 
ATOM   2728 C  CA  . ALA   B 1 28  ? -16.812 41.440 -10.545 1.00 29.51  ? 25  ALA   B CA  1 
ATOM   2729 C  C   . ALA   B 1 28  ? -17.946 40.480 -10.256 1.00 30.69  ? 25  ALA   B C   1 
ATOM   2730 O  O   . ALA   B 1 28  ? -18.219 39.602 -11.075 1.00 29.56  ? 25  ALA   B O   1 
ATOM   2731 C  CB  . ALA   B 1 28  ? -17.317 42.725 -11.134 1.00 30.30  ? 25  ALA   B CB  1 
ATOM   2732 N  N   . PRO   B 1 29  ? -18.551 40.580 -9.058  1.00 32.62  ? 26  PRO   B N   1 
ATOM   2733 C  CA  . PRO   B 1 29  ? -19.601 39.661 -8.650  1.00 35.94  ? 26  PRO   B CA  1 
ATOM   2734 C  C   . PRO   B 1 29  ? -20.765 39.703 -9.640  1.00 38.61  ? 26  PRO   B C   1 
ATOM   2735 O  O   . PRO   B 1 29  ? -21.003 40.711 -10.317 1.00 38.07  ? 26  PRO   B O   1 
ATOM   2736 C  CB  . PRO   B 1 29  ? -20.051 40.119 -7.251  1.00 36.82  ? 26  PRO   B CB  1 
ATOM   2737 C  CG  . PRO   B 1 29  ? -18.965 41.071 -6.768  1.00 36.62  ? 26  PRO   B CG  1 
ATOM   2738 C  CD  . PRO   B 1 29  ? -18.208 41.544 -7.996  1.00 34.69  ? 26  PRO   B CD  1 
ATOM   2739 N  N   . PRO   B 1 30  ? -21.561 38.618 -9.716  1.00 42.61  ? 27  PRO   B N   1 
ATOM   2740 C  CA  . PRO   B 1 30  ? -22.707 38.578 -10.628 1.00 45.01  ? 27  PRO   B CA  1 
ATOM   2741 C  C   . PRO   B 1 30  ? -23.682 39.759 -10.465 1.00 46.20  ? 27  PRO   B C   1 
ATOM   2742 O  O   . PRO   B 1 30  ? -24.338 40.080 -11.415 1.00 47.13  ? 27  PRO   B O   1 
ATOM   2743 C  CB  . PRO   B 1 30  ? -23.423 37.259 -10.277 1.00 47.03  ? 27  PRO   B CB  1 
ATOM   2744 C  CG  . PRO   B 1 30  ? -22.341 36.410 -9.611  1.00 47.05  ? 27  PRO   B CG  1 
ATOM   2745 C  CD  . PRO   B 1 30  ? -21.439 37.401 -8.895  1.00 44.47  ? 27  PRO   B CD  1 
ATOM   2746 N  N   . GLU   B 1 31  ? -23.755 40.378 -9.284  1.00 47.38  ? 28  GLU   B N   1 
ATOM   2747 C  CA  . GLU   B 1 31  ? -24.709 41.487 -9.015  1.00 48.77  ? 28  GLU   B CA  1 
ATOM   2748 C  C   . GLU   B 1 31  ? -24.348 42.690 -9.899  1.00 46.27  ? 28  GLU   B C   1 
ATOM   2749 O  O   . GLU   B 1 31  ? -25.255 43.466 -10.207 1.00 48.98  ? 28  GLU   B O   1 
ATOM   2750 C  CB  . GLU   B 1 31  ? -24.713 41.866 -7.526  1.00 50.93  ? 28  GLU   B CB  1 
ATOM   2751 C  CG  . GLU   B 1 31  ? -25.284 40.791 -6.588  1.00 52.99  ? 28  GLU   B CG  1 
ATOM   2752 C  CD  . GLU   B 1 31  ? -24.531 39.461 -6.490  1.00 52.88  ? 28  GLU   B CD  1 
ATOM   2753 O  OE1 . GLU   B 1 31  ? -23.288 39.482 -6.575  1.00 49.54  ? 28  GLU   B OE1 1 
ATOM   2754 O  OE2 . GLU   B 1 31  ? -25.189 38.397 -6.336  1.00 54.11  ? 28  GLU   B OE2 1 
ATOM   2755 N  N   . VAL   B 1 32  ? -23.076 42.825 -10.306 1.00 41.46  ? 29  VAL   B N   1 
ATOM   2756 C  CA  . VAL   B 1 32  ? -22.551 43.998 -11.070 1.00 38.64  ? 29  VAL   B CA  1 
ATOM   2757 C  C   . VAL   B 1 32  ? -22.949 43.842 -12.539 1.00 37.47  ? 29  VAL   B C   1 
ATOM   2758 O  O   . VAL   B 1 32  ? -22.660 42.834 -13.141 1.00 36.44  ? 29  VAL   B O   1 
ATOM   2759 C  CB  . VAL   B 1 32  ? -21.029 44.128 -10.893 1.00 36.84  ? 29  VAL   B CB  1 
ATOM   2760 C  CG1 . VAL   B 1 32  ? -20.396 45.183 -11.787 1.00 36.23  ? 29  VAL   B CG1 1 
ATOM   2761 C  CG2 . VAL   B 1 32  ? -20.667 44.386 -9.432  1.00 36.72  ? 29  VAL   B CG2 1 
ATOM   2762 N  N   . PRO   B 1 33  ? -23.664 44.809 -13.149 1.00 38.44  ? 30  PRO   B N   1 
ATOM   2763 C  CA  . PRO   B 1 33  ? -24.068 44.692 -14.552 1.00 38.08  ? 30  PRO   B CA  1 
ATOM   2764 C  C   . PRO   B 1 33  ? -22.883 44.430 -15.480 1.00 35.82  ? 30  PRO   B C   1 
ATOM   2765 O  O   . PRO   B 1 33  ? -21.861 45.000 -15.298 1.00 33.64  ? 30  PRO   B O   1 
ATOM   2766 C  CB  . PRO   B 1 33  ? -24.652 46.072 -14.876 1.00 40.17  ? 30  PRO   B CB  1 
ATOM   2767 C  CG  . PRO   B 1 33  ? -25.153 46.551 -13.521 1.00 42.00  ? 30  PRO   B CG  1 
ATOM   2768 C  CD  . PRO   B 1 33  ? -24.093 46.090 -12.549 1.00 39.78  ? 30  PRO   B CD  1 
ATOM   2769 N  N   . ARG   B 1 34  ? -23.079 43.594 -16.485 1.00 35.76  ? 31  ARG   B N   1 
ATOM   2770 C  CA  . ARG   B 1 34  ? -21.999 43.206 -17.433 1.00 34.75  ? 31  ARG   B CA  1 
ATOM   2771 C  C   . ARG   B 1 34  ? -21.478 44.434 -18.189 1.00 34.26  ? 31  ARG   B C   1 
ATOM   2772 O  O   . ARG   B 1 34  ? -20.287 44.427 -18.572 1.00 33.15  ? 31  ARG   B O   1 
ATOM   2773 C  CB  . ARG   B 1 34  ? -22.525 42.111 -18.362 1.00 36.10  ? 31  ARG   B CB  1 
ATOM   2774 C  CG  . ARG   B 1 34  ? -23.046 40.863 -17.652 1.00 36.95  ? 31  ARG   B CG  1 
ATOM   2775 C  CD  . ARG   B 1 34  ? -21.994 40.149 -16.849 1.00 35.42  ? 31  ARG   B CD  1 
ATOM   2776 N  NE  . ARG   B 1 34  ? -21.833 40.626 -15.482 1.00 35.76  ? 31  ARG   B NE  1 
ATOM   2777 C  CZ  . ARG   B 1 34  ? -20.899 40.155 -14.664 1.00 34.65  ? 31  ARG   B CZ  1 
ATOM   2778 N  NH1 . ARG   B 1 34  ? -20.045 39.258 -15.131 1.00 33.39  ? 31  ARG   B NH1 1 
ATOM   2779 N  NH2 . ARG   B 1 34  ? -20.760 40.615 -13.421 1.00 34.39  ? 31  ARG   B NH2 1 
ATOM   2780 N  N   . SER   B 1 35  ? -22.294 45.479 -18.359 1.00 35.28  ? 32  SER   B N   1 
ATOM   2781 C  CA  . SER   B 1 35  ? -21.883 46.752 -19.009 1.00 36.13  ? 32  SER   B CA  1 
ATOM   2782 C  C   . SER   B 1 35  ? -20.651 47.356 -18.310 1.00 35.39  ? 32  SER   B C   1 
ATOM   2783 O  O   . SER   B 1 35  ? -19.841 48.037 -18.997 1.00 35.12  ? 32  SER   B O   1 
ATOM   2784 C  CB  . SER   B 1 35  ? -23.017 47.731 -19.012 1.00 38.21  ? 32  SER   B CB  1 
ATOM   2785 O  OG  . SER   B 1 35  ? -23.524 47.899 -17.701 1.00 39.58  ? 32  SER   B OG  1 
ATOM   2786 N  N   . LYS   B 1 36  ? -20.509 47.129 -17.009 1.00 35.32  ? 33  LYS   B N   1 
ATOM   2787 C  CA  . LYS   B 1 36  ? -19.425 47.761 -16.213 1.00 36.33  ? 33  LYS   B CA  1 
ATOM   2788 C  C   . LYS   B 1 36  ? -18.059 47.219 -16.655 1.00 33.59  ? 33  LYS   B C   1 
ATOM   2789 O  O   . LYS   B 1 36  ? -17.175 48.014 -16.843 1.00 33.24  ? 33  LYS   B O   1 
ATOM   2790 C  CB  . LYS   B 1 36  ? -19.719 47.586 -14.725 1.00 39.49  ? 33  LYS   B CB  1 
ATOM   2791 C  CG  . LYS   B 1 36  ? -20.571 48.703 -14.167 1.00 43.44  ? 33  LYS   B CG  1 
ATOM   2792 C  CD  . LYS   B 1 36  ? -19.733 49.944 -13.994 1.00 46.17  ? 33  LYS   B CD  1 
ATOM   2793 C  CE  . LYS   B 1 36  ? -20.512 51.123 -13.441 1.00 49.91  ? 33  LYS   B CE  1 
ATOM   2794 N  NZ  . LYS   B 1 36  ? -19.590 52.252 -13.213 1.00 51.26  ? 33  LYS   B NZ  1 
ATOM   2795 N  N   . ALA   B 1 37  ? -17.917 45.920 -16.910 1.00 31.50  ? 34  ALA   B N   1 
ATOM   2796 C  CA  . ALA   B 1 37  ? -16.642 45.355 -17.413 1.00 30.44  ? 34  ALA   B CA  1 
ATOM   2797 C  C   . ALA   B 1 37  ? -16.182 46.089 -18.692 1.00 30.29  ? 34  ALA   B C   1 
ATOM   2798 O  O   . ALA   B 1 37  ? -14.966 46.312 -18.849 1.00 29.67  ? 34  ALA   B O   1 
ATOM   2799 C  CB  . ALA   B 1 37  ? -16.772 43.868 -17.647 1.00 29.11  ? 34  ALA   B CB  1 
ATOM   2800 N  N   . LEU   B 1 38  ? -17.108 46.411 -19.596 1.00 30.88  ? 35  LEU   B N   1 
ATOM   2801 C  CA  . LEU   B 1 38  ? -16.755 47.160 -20.829 1.00 31.89  ? 35  LEU   B CA  1 
ATOM   2802 C  C   . LEU   B 1 38  ? -16.242 48.547 -20.421 1.00 32.54  ? 35  LEU   B C   1 
ATOM   2803 O  O   . LEU   B 1 38  ? -15.142 48.930 -20.844 1.00 33.93  ? 35  LEU   B O   1 
ATOM   2804 C  CB  . LEU   B 1 38  ? -17.968 47.223 -21.768 1.00 32.51  ? 35  LEU   B CB  1 
ATOM   2805 C  CG  . LEU   B 1 38  ? -17.835 48.195 -22.934 1.00 33.45  ? 35  LEU   B CG  1 
ATOM   2806 C  CD1 . LEU   B 1 38  ? -16.589 47.929 -23.749 1.00 32.64  ? 35  LEU   B CD1 1 
ATOM   2807 C  CD2 . LEU   B 1 38  ? -19.077 48.160 -23.813 1.00 34.72  ? 35  LEU   B CD2 1 
ATOM   2808 N  N   . GLU   B 1 39  ? -16.976 49.253 -19.580 1.00 33.58  ? 36  GLU   B N   1 
ATOM   2809 C  CA  . GLU   B 1 39  ? -16.612 50.633 -19.194 1.00 35.51  ? 36  GLU   B CA  1 
ATOM   2810 C  C   . GLU   B 1 39  ? -15.226 50.665 -18.528 1.00 33.50  ? 36  GLU   B C   1 
ATOM   2811 O  O   . GLU   B 1 39  ? -14.352 51.498 -18.951 1.00 33.68  ? 36  GLU   B O   1 
ATOM   2812 C  CB  . GLU   B 1 39  ? -17.694 51.193 -18.279 1.00 38.66  ? 36  GLU   B CB  1 
ATOM   2813 C  CG  . GLU   B 1 39  ? -17.336 52.556 -17.754 1.00 41.98  ? 36  GLU   B CG  1 
ATOM   2814 C  CD  . GLU   B 1 39  ? -18.233 52.941 -16.598 1.00 46.29  ? 36  GLU   B CD  1 
ATOM   2815 O  OE1 . GLU   B 1 39  ? -17.693 53.208 -15.471 1.00 50.57  ? 36  GLU   B OE1 1 
ATOM   2816 O  OE2 . GLU   B 1 39  ? -19.467 52.927 -16.806 1.00 49.86  ? 36  GLU   B OE2 1 
ATOM   2817 N  N   . VAL   B 1 40  ? -15.031 49.836 -17.502 1.00 30.99  ? 37  VAL   B N   1 
ATOM   2818 C  CA  . VAL   B 1 40  ? -13.820 49.898 -16.639 1.00 31.05  ? 37  VAL   B CA  1 
ATOM   2819 C  C   . VAL   B 1 40  ? -12.591 49.327 -17.348 1.00 30.01  ? 37  VAL   B C   1 
ATOM   2820 O  O   . VAL   B 1 40  ? -11.466 49.814 -17.078 1.00 30.02  ? 37  VAL   B O   1 
ATOM   2821 C  CB  . VAL   B 1 40  ? -14.043 49.221 -15.281 1.00 30.55  ? 37  VAL   B CB  1 
ATOM   2822 C  CG1 . VAL   B 1 40  ? -15.249 49.819 -14.573 1.00 32.27  ? 37  VAL   B CG1 1 
ATOM   2823 C  CG2 . VAL   B 1 40  ? -14.120 47.700 -15.401 1.00 29.19  ? 37  VAL   B CG2 1 
ATOM   2824 N  N   . THR   B 1 41  ? -12.771 48.380 -18.268 1.00 28.56  ? 38  THR   B N   1 
ATOM   2825 C  CA  . THR   B 1 41  ? -11.630 47.816 -19.008 1.00 28.35  ? 38  THR   B CA  1 
ATOM   2826 C  C   . THR   B 1 41  ? -11.075 48.922 -19.921 1.00 29.63  ? 38  THR   B C   1 
ATOM   2827 O  O   . THR   B 1 41  ? -9.862  49.036 -20.032 1.00 30.14  ? 38  THR   B O   1 
ATOM   2828 C  CB  . THR   B 1 41  ? -12.034 46.508 -19.709 1.00 27.75  ? 38  THR   B CB  1 
ATOM   2829 O  OG1 . THR   B 1 41  ? -12.458 45.540 -18.739 1.00 26.39  ? 38  THR   B OG1 1 
ATOM   2830 C  CG2 . THR   B 1 41  ? -10.866 45.941 -20.482 1.00 27.71  ? 38  THR   B CG2 1 
ATOM   2831 N  N   . LYS   B 1 42  ? -11.935 49.689 -20.588 1.00 30.75  ? 39  LYS   B N   1 
ATOM   2832 C  CA  . LYS   B 1 42  ? -11.490 50.853 -21.385 1.00 32.54  ? 39  LYS   B CA  1 
ATOM   2833 C  C   . LYS   B 1 42  ? -10.816 51.878 -20.469 1.00 33.43  ? 39  LYS   B C   1 
ATOM   2834 O  O   . LYS   B 1 42  ? -9.755  52.376 -20.854 1.00 34.07  ? 39  LYS   B O   1 
ATOM   2835 C  CB  . LYS   B 1 42  ? -12.693 51.471 -22.079 1.00 33.81  ? 39  LYS   B CB  1 
ATOM   2836 C  CG  . LYS   B 1 42  ? -13.221 50.677 -23.250 1.00 34.04  ? 39  LYS   B CG  1 
ATOM   2837 C  CD  . LYS   B 1 42  ? -14.057 51.578 -24.118 1.00 36.41  ? 39  LYS   B CD  1 
ATOM   2838 C  CE  . LYS   B 1 42  ? -15.492 51.652 -23.639 1.00 37.96  ? 39  LYS   B CE  1 
ATOM   2839 N  NZ  . LYS   B 1 42  ? -16.305 52.579 -24.479 1.00 40.86  ? 39  LYS   B NZ  1 
ATOM   2840 N  N   . LEU   B 1 43  ? -11.407 52.189 -19.313 1.00 33.83  ? 40  LEU   B N   1 
ATOM   2841 C  CA  . LEU   B 1 43  ? -10.770 53.100 -18.322 1.00 35.05  ? 40  LEU   B CA  1 
ATOM   2842 C  C   . LEU   B 1 43  ? -9.383  52.576 -17.915 1.00 34.15  ? 40  LEU   B C   1 
ATOM   2843 O  O   . LEU   B 1 43  ? -8.478  53.418 -17.732 1.00 35.72  ? 40  LEU   B O   1 
ATOM   2844 C  CB  . LEU   B 1 43  ? -11.650 53.252 -17.082 1.00 35.49  ? 40  LEU   B CB  1 
ATOM   2845 C  CG  . LEU   B 1 43  ? -12.974 54.017 -17.255 1.00 37.20  ? 40  LEU   B CG  1 
ATOM   2846 C  CD1 . LEU   B 1 43  ? -13.695 54.075 -15.911 1.00 37.37  ? 40  LEU   B CD1 1 
ATOM   2847 C  CD2 . LEU   B 1 43  ? -12.802 55.466 -17.795 1.00 39.44  ? 40  LEU   B CD2 1 
ATOM   2848 N  N   . ALA   B 1 44  ? -9.253  51.266 -17.664 1.00 31.69  ? 41  ALA   B N   1 
ATOM   2849 C  CA  . ALA   B 1 44  ? -7.966  50.648 -17.280 1.00 30.59  ? 41  ALA   B CA  1 
ATOM   2850 C  C   . ALA   B 1 44  ? -6.940  50.931 -18.395 1.00 31.48  ? 41  ALA   B C   1 
ATOM   2851 O  O   . ALA   B 1 44  ? -5.826  51.443 -18.117 1.00 31.83  ? 41  ALA   B O   1 
ATOM   2852 C  CB  . ALA   B 1 44  ? -8.142  49.186 -16.970 1.00 28.73  ? 41  ALA   B CB  1 
ATOM   2853 N  N   . ILE   B 1 45  ? -7.322  50.676 -19.645 1.00 31.27  ? 42  ILE   B N   1 
ATOM   2854 C  CA  . ILE   B 1 45  ? -6.391  50.859 -20.795 1.00 32.48  ? 42  ILE   B CA  1 
ATOM   2855 C  C   . ILE   B 1 45  ? -6.030  52.337 -20.876 1.00 35.54  ? 42  ILE   B C   1 
ATOM   2856 O  O   . ILE   B 1 45  ? -4.856  52.649 -21.065 1.00 36.37  ? 42  ILE   B O   1 
ATOM   2857 C  CB  . ILE   B 1 45  ? -6.999  50.271 -22.078 1.00 31.82  ? 42  ILE   B CB  1 
ATOM   2858 C  CG1 . ILE   B 1 45  ? -7.120  48.762 -21.875 1.00 30.38  ? 42  ILE   B CG1 1 
ATOM   2859 C  CG2 . ILE   B 1 45  ? -6.184  50.635 -23.317 1.00 33.05  ? 42  ILE   B CG2 1 
ATOM   2860 C  CD1 . ILE   B 1 45  ? -7.978  48.068 -22.889 1.00 29.76  ? 42  ILE   B CD1 1 
ATOM   2861 N  N   . GLU   B 1 46  ? -6.996  53.224 -20.696 1.00 37.93  ? 43  GLU   B N   1 
ATOM   2862 C  CA  . GLU   B 1 46  ? -6.729  54.673 -20.803 1.00 40.91  ? 43  GLU   B CA  1 
ATOM   2863 C  C   . GLU   B 1 46  ? -5.762  55.097 -19.702 1.00 41.57  ? 43  GLU   B C   1 
ATOM   2864 O  O   . GLU   B 1 46  ? -4.955  55.979 -20.012 1.00 43.22  ? 43  GLU   B O   1 
ATOM   2865 C  CB  . GLU   B 1 46  ? -8.036  55.450 -20.730 1.00 43.99  ? 43  GLU   B CB  1 
ATOM   2866 C  CG  . GLU   B 1 46  ? -8.768  55.351 -22.056 1.00 44.99  ? 43  GLU   B CG  1 
ATOM   2867 C  CD  . GLU   B 1 46  ? -10.267 55.599 -22.053 1.00 47.40  ? 43  GLU   B CD  1 
ATOM   2868 O  OE1 . GLU   B 1 46  ? -10.783 56.075 -21.014 1.00 49.30  ? 43  GLU   B OE1 1 
ATOM   2869 O  OE2 . GLU   B 1 46  ? -10.926 55.315 -23.125 1.00 47.73  ? 43  GLU   B OE2 1 
ATOM   2870 N  N   . ALA   B 1 47  ? -5.859  54.517 -18.493 1.00 39.02  ? 44  ALA   B N   1 
ATOM   2871 C  CA  . ALA   B 1 47  ? -4.955  54.852 -17.359 1.00 39.76  ? 44  ALA   B CA  1 
ATOM   2872 C  C   . ALA   B 1 47  ? -3.552  54.289 -17.613 1.00 39.60  ? 44  ALA   B C   1 
ATOM   2873 O  O   . ALA   B 1 47  ? -2.609  54.825 -17.043 1.00 41.00  ? 44  ALA   B O   1 
ATOM   2874 C  CB  . ALA   B 1 47  ? -5.523  54.358 -16.065 1.00 38.22  ? 44  ALA   B CB  1 
ATOM   2875 N  N   . GLY   B 1 48  ? -3.418  53.236 -18.432 1.00 38.15  ? 45  GLY   B N   1 
ATOM   2876 C  CA  . GLY   B 1 48  ? -2.089  52.701 -18.801 1.00 38.17  ? 45  GLY   B CA  1 
ATOM   2877 C  C   . GLY   B 1 48  ? -1.932  51.227 -18.466 1.00 35.43  ? 45  GLY   B C   1 
ATOM   2878 O  O   . GLY   B 1 48  ? -0.812  50.696 -18.667 1.00 35.37  ? 45  GLY   B O   1 
ATOM   2879 N  N   . PHE   B 1 49  ? -3.006  50.550 -18.063 1.00 33.36  ? 46  PHE   B N   1 
ATOM   2880 C  CA  . PHE   B 1 49  ? -2.959  49.070 -17.912 1.00 31.14  ? 46  PHE   B CA  1 
ATOM   2881 C  C   . PHE   B 1 49  ? -2.856  48.452 -19.305 1.00 31.03  ? 46  PHE   B C   1 
ATOM   2882 O  O   . PHE   B 1 49  ? -3.601  48.900 -20.196 1.00 30.82  ? 46  PHE   B O   1 
ATOM   2883 C  CB  . PHE   B 1 49  ? -4.191  48.517 -17.204 1.00 29.67  ? 46  PHE   B CB  1 
ATOM   2884 C  CG  . PHE   B 1 49  ? -4.228  48.722 -15.715 1.00 29.84  ? 46  PHE   B CG  1 
ATOM   2885 C  CD1 . PHE   B 1 49  ? -4.784  49.868 -15.184 1.00 31.06  ? 46  PHE   B CD1 1 
ATOM   2886 C  CD2 . PHE   B 1 49  ? -3.799  47.720 -14.846 1.00 28.79  ? 46  PHE   B CD2 1 
ATOM   2887 C  CE1 . PHE   B 1 49  ? -4.837  50.049 -13.810 1.00 31.13  ? 46  PHE   B CE1 1 
ATOM   2888 C  CE2 . PHE   B 1 49  ? -3.854  47.897 -13.474 1.00 29.15  ? 46  PHE   B CE2 1 
ATOM   2889 C  CZ  . PHE   B 1 49  ? -4.364  49.072 -12.963 1.00 30.90  ? 46  PHE   B CZ  1 
ATOM   2890 N  N   . ARG   B 1 50  ? -1.995  47.447 -19.453 1.00 30.67  ? 47  ARG   B N   1 
ATOM   2891 C  CA  . ARG   B 1 50  ? -1.767  46.711 -20.720 1.00 31.43  ? 47  ARG   B CA  1 
ATOM   2892 C  C   . ARG   B 1 50  ? -2.021  45.218 -20.550 1.00 29.65  ? 47  ARG   B C   1 
ATOM   2893 O  O   . ARG   B 1 50  ? -2.418  44.593 -21.527 1.00 30.15  ? 47  ARG   B O   1 
ATOM   2894 C  CB  . ARG   B 1 50  ? -0.370  47.032 -21.250 1.00 33.34  ? 47  ARG   B CB  1 
ATOM   2895 C  CG  . ARG   B 1 50  ? -0.279  48.478 -21.710 1.00 35.52  ? 47  ARG   B CG  1 
ATOM   2896 C  CD  . ARG   B 1 50  ? -1.063  48.781 -22.989 1.00 36.41  ? 47  ARG   B CD  1 
ATOM   2897 N  NE  . ARG   B 1 50  ? -0.951  50.202 -23.361 1.00 38.28  ? 47  ARG   B NE  1 
ATOM   2898 C  CZ  . ARG   B 1 50  ? -1.709  51.203 -22.887 1.00 39.03  ? 47  ARG   B CZ  1 
ATOM   2899 N  NH1 . ARG   B 1 50  ? -2.655  50.992 -21.974 1.00 37.29  ? 47  ARG   B NH1 1 
ATOM   2900 N  NH2 . ARG   B 1 50  ? -1.500  52.438 -23.325 1.00 41.45  ? 47  ARG   B NH2 1 
ATOM   2901 N  N   . HIS   B 1 51  ? -1.857  44.727 -19.323 1.00 28.56  ? 48  HIS   B N   1 
ATOM   2902 C  CA  . HIS   B 1 51  ? -2.093  43.317 -18.928 1.00 26.65  ? 48  HIS   B CA  1 
ATOM   2903 C  C   . HIS   B 1 51  ? -3.528  43.271 -18.391 1.00 25.29  ? 48  HIS   B C   1 
ATOM   2904 O  O   . HIS   B 1 51  ? -3.834  44.014 -17.458 1.00 25.28  ? 48  HIS   B O   1 
ATOM   2905 C  CB  . HIS   B 1 51  ? -0.994  42.941 -17.930 1.00 27.53  ? 48  HIS   B CB  1 
ATOM   2906 C  CG  . HIS   B 1 51  ? -1.122  41.609 -17.290 1.00 26.13  ? 48  HIS   B CG  1 
ATOM   2907 N  ND1 . HIS   B 1 51  ? -0.107  41.078 -16.539 1.00 26.03  ? 48  HIS   B ND1 1 
ATOM   2908 C  CD2 . HIS   B 1 51  ? -2.128  40.713 -17.273 1.00 24.79  ? 48  HIS   B CD2 1 
ATOM   2909 C  CE1 . HIS   B 1 51  ? -0.471  39.906 -16.091 1.00 25.00  ? 48  HIS   B CE1 1 
ATOM   2910 N  NE2 . HIS   B 1 51  ? -1.707  39.660 -16.524 1.00 24.61  ? 48  HIS   B NE2 1 
ATOM   2911 N  N   A ILE   B 1 52  ? -4.397  42.487 -19.038 0.36 24.02  ? 49  ILE   B N   1 
ATOM   2912 N  N   B ILE   B 1 52  ? -4.380  42.473 -19.044 0.64 24.07  ? 49  ILE   B N   1 
ATOM   2913 C  CA  A ILE   B 1 52  ? -5.831  42.379 -18.648 0.36 23.32  ? 49  ILE   B CA  1 
ATOM   2914 C  CA  B ILE   B 1 52  ? -5.817  42.357 -18.684 0.64 23.66  ? 49  ILE   B CA  1 
ATOM   2915 C  C   A ILE   B 1 52  ? -6.135  40.924 -18.311 0.36 22.14  ? 49  ILE   B C   1 
ATOM   2916 C  C   B ILE   B 1 52  ? -6.121  40.906 -18.312 0.64 22.27  ? 49  ILE   B C   1 
ATOM   2917 O  O   A ILE   B 1 52  ? -5.911  40.050 -19.178 0.36 21.94  ? 49  ILE   B O   1 
ATOM   2918 O  O   B ILE   B 1 52  ? -5.916  40.003 -19.176 0.64 22.18  ? 49  ILE   B O   1 
ATOM   2919 C  CB  A ILE   B 1 52  ? -6.748  42.937 -19.749 0.36 23.68  ? 49  ILE   B CB  1 
ATOM   2920 C  CB  B ILE   B 1 52  ? -6.691  42.871 -19.839 0.64 24.27  ? 49  ILE   B CB  1 
ATOM   2921 C  CG1 A ILE   B 1 52  ? -6.578  44.453 -19.850 0.36 24.71  ? 49  ILE   B CG1 1 
ATOM   2922 C  CG1 B ILE   B 1 52  ? -6.187  44.212 -20.379 0.64 25.58  ? 49  ILE   B CG1 1 
ATOM   2923 C  CG2 A ILE   B 1 52  ? -8.200  42.526 -19.509 0.36 23.27  ? 49  ILE   B CG2 1 
ATOM   2924 C  CG2 B ILE   B 1 52  ? -8.161  42.907 -19.441 0.64 24.25  ? 49  ILE   B CG2 1 
ATOM   2925 C  CD1 A ILE   B 1 52  ? -7.273  45.076 -21.030 0.36 25.32  ? 49  ILE   B CD1 1 
ATOM   2926 C  CD1 B ILE   B 1 52  ? -6.327  45.405 -19.459 0.64 25.94  ? 49  ILE   B CD1 1 
ATOM   2927 N  N   . ASP   B 1 53  ? -6.636  40.695 -17.097 1.00 21.47  ? 50  ASP   B N   1 
ATOM   2928 C  CA  . ASP   B 1 53  ? -6.880  39.327 -16.575 1.00 21.12  ? 50  ASP   B CA  1 
ATOM   2929 C  C   . ASP   B 1 53  ? -8.381  39.026 -16.602 1.00 21.22  ? 50  ASP   B C   1 
ATOM   2930 O  O   . ASP   B 1 53  ? -9.125  39.616 -15.807 1.00 21.33  ? 50  ASP   B O   1 
ATOM   2931 C  CB  . ASP   B 1 53  ? -6.248  39.132 -15.199 1.00 21.12  ? 50  ASP   B CB  1 
ATOM   2932 C  CG  . ASP   B 1 53  ? -6.369  37.682 -14.722 1.00 20.81  ? 50  ASP   B CG  1 
ATOM   2933 O  OD1 . ASP   B 1 53  ? -5.480  36.864 -15.093 1.00 21.23  ? 50  ASP   B OD1 1 
ATOM   2934 O  OD2 . ASP   B 1 53  ? -7.361  37.384 -14.006 1.00 20.15  ? 50  ASP   B OD2 1 
ATOM   2935 N  N   . SER   B 1 54  ? -8.779  38.031 -17.418 1.00 21.94  ? 51  SER   B N   1 
ATOM   2936 C  CA  . SER   B 1 54  ? -10.143 37.447 -17.452 1.00 22.20  ? 51  SER   B CA  1 
ATOM   2937 C  C   . SER   B 1 54  ? -10.075 35.906 -17.464 1.00 22.01  ? 51  SER   B C   1 
ATOM   2938 O  O   . SER   B 1 54  ? -9.007  35.327 -17.170 1.00 21.07  ? 51  SER   B O   1 
ATOM   2939 C  CB  . SER   B 1 54  ? -10.851 37.985 -18.662 1.00 23.26  ? 51  SER   B CB  1 
ATOM   2940 O  OG  . SER   B 1 54  ? -12.230 37.616 -18.720 1.00 23.57  ? 51  SER   B OG  1 
ATOM   2941 N  N   . ALA   B 1 55  ? -11.229 35.296 -17.711 1.00 21.79  ? 52  ALA   B N   1 
ATOM   2942 C  CA  . ALA   B 1 55  ? -11.482 33.845 -17.638 1.00 22.17  ? 52  ALA   B CA  1 
ATOM   2943 C  C   . ALA   B 1 55  ? -12.897 33.552 -18.133 1.00 22.54  ? 52  ALA   B C   1 
ATOM   2944 O  O   . ALA   B 1 55  ? -13.776 34.401 -17.987 1.00 23.18  ? 52  ALA   B O   1 
ATOM   2945 C  CB  . ALA   B 1 55  ? -11.320 33.375 -16.220 1.00 22.18  ? 52  ALA   B CB  1 
ATOM   2946 N  N   . HIS   B 1 56  ? -13.121 32.347 -18.645 1.00 23.08  ? 53  HIS   B N   1 
ATOM   2947 C  CA  . HIS   B 1 56  ? -14.469 31.868 -18.975 1.00 23.89  ? 53  HIS   B CA  1 
ATOM   2948 C  C   . HIS   B 1 56  ? -15.373 32.020 -17.756 1.00 24.87  ? 53  HIS   B C   1 
ATOM   2949 O  O   . HIS   B 1 56  ? -16.516 32.503 -17.891 1.00 25.83  ? 53  HIS   B O   1 
ATOM   2950 C  CB  . HIS   B 1 56  ? -14.413 30.422 -19.477 1.00 24.75  ? 53  HIS   B CB  1 
ATOM   2951 C  CG  . HIS   B 1 56  ? -15.748 29.873 -19.788 1.00 26.03  ? 53  HIS   B CG  1 
ATOM   2952 N  ND1 . HIS   B 1 56  ? -16.455 30.334 -20.858 1.00 27.04  ? 53  HIS   B ND1 1 
ATOM   2953 C  CD2 . HIS   B 1 56  ? -16.508 28.950 -19.189 1.00 27.56  ? 53  HIS   B CD2 1 
ATOM   2954 C  CE1 . HIS   B 1 56  ? -17.610 29.728 -20.917 1.00 28.52  ? 53  HIS   B CE1 1 
ATOM   2955 N  NE2 . HIS   B 1 56  ? -17.668 28.843 -19.925 1.00 29.21  ? 53  HIS   B NE2 1 
ATOM   2956 N  N   . LEU   B 1 57  ? -14.866 31.677 -16.577 1.00 25.18  ? 54  LEU   B N   1 
ATOM   2957 C  CA  . LEU   B 1 57  ? -15.671 31.663 -15.344 1.00 25.80  ? 54  LEU   B CA  1 
ATOM   2958 C  C   . LEU   B 1 57  ? -16.261 33.039 -15.036 1.00 25.11  ? 54  LEU   B C   1 
ATOM   2959 O  O   . LEU   B 1 57  ? -17.285 33.064 -14.389 1.00 25.34  ? 54  LEU   B O   1 
ATOM   2960 C  CB  . LEU   B 1 57  ? -14.795 31.206 -14.179 1.00 26.47  ? 54  LEU   B CB  1 
ATOM   2961 C  CG  . LEU   B 1 57  ? -15.561 30.968 -12.885 1.00 28.29  ? 54  LEU   B CG  1 
ATOM   2962 C  CD1 . LEU   B 1 57  ? -16.502 29.786 -13.051 1.00 29.67  ? 54  LEU   B CD1 1 
ATOM   2963 C  CD2 . LEU   B 1 57  ? -14.597 30.744 -11.714 1.00 28.49  ? 54  LEU   B CD2 1 
ATOM   2964 N  N   . TYR   B 1 58  ? -15.643 34.141 -15.468 1.00 24.37  ? 55  TYR   B N   1 
ATOM   2965 C  CA  . TYR   B 1 58  ? -16.006 35.498 -14.987 1.00 24.63  ? 55  TYR   B CA  1 
ATOM   2966 C  C   . TYR   B 1 58  ? -17.265 35.999 -15.687 1.00 25.67  ? 55  TYR   B C   1 
ATOM   2967 O  O   . TYR   B 1 58  ? -17.786 37.044 -15.273 1.00 25.64  ? 55  TYR   B O   1 
ATOM   2968 C  CB  . TYR   B 1 58  ? -14.872 36.492 -15.236 1.00 23.94  ? 55  TYR   B CB  1 
ATOM   2969 C  CG  . TYR   B 1 58  ? -13.590 36.186 -14.514 1.00 22.70  ? 55  TYR   B CG  1 
ATOM   2970 C  CD1 . TYR   B 1 58  ? -13.488 35.154 -13.601 1.00 23.25  ? 55  TYR   B CD1 1 
ATOM   2971 C  CD2 . TYR   B 1 58  ? -12.456 36.930 -14.773 1.00 22.86  ? 55  TYR   B CD2 1 
ATOM   2972 C  CE1 . TYR   B 1 58  ? -12.306 34.923 -12.911 1.00 22.66  ? 55  TYR   B CE1 1 
ATOM   2973 C  CE2 . TYR   B 1 58  ? -11.247 36.661 -14.148 1.00 22.04  ? 55  TYR   B CE2 1 
ATOM   2974 C  CZ  . TYR   B 1 58  ? -11.182 35.674 -13.192 1.00 22.38  ? 55  TYR   B CZ  1 
ATOM   2975 O  OH  . TYR   B 1 58  ? -9.981  35.377 -12.599 1.00 23.40  ? 55  TYR   B OH  1 
ATOM   2976 N  N   . ASN   B 1 59  ? -17.728 35.294 -16.733 1.00 25.66  ? 56  ASN   B N   1 
ATOM   2977 C  CA  . ASN   B 1 59  ? -18.912 35.730 -17.506 1.00 27.13  ? 56  ASN   B CA  1 
ATOM   2978 C  C   . ASN   B 1 59  ? -18.693 37.187 -17.907 1.00 26.70  ? 56  ASN   B C   1 
ATOM   2979 O  O   . ASN   B 1 59  ? -19.609 37.993 -17.695 1.00 27.97  ? 56  ASN   B O   1 
ATOM   2980 C  CB  . ASN   B 1 59  ? -20.210 35.552 -16.705 1.00 28.72  ? 56  ASN   B CB  1 
ATOM   2981 C  CG  . ASN   B 1 59  ? -21.438 35.869 -17.541 1.00 30.35  ? 56  ASN   B CG  1 
ATOM   2982 O  OD1 . ASN   B 1 59  ? -21.428 35.655 -18.749 1.00 30.01  ? 56  ASN   B OD1 1 
ATOM   2983 N  ND2 . ASN   B 1 59  ? -22.485 36.375 -16.919 1.00 31.52  ? 56  ASN   B ND2 1 
ATOM   2984 N  N   . ASN   B 1 60  ? -17.509 37.535 -18.438 1.00 25.45  ? 57  ASN   B N   1 
ATOM   2985 C  CA  . ASN   B 1 60  ? -17.300 38.921 -18.923 1.00 25.78  ? 57  ASN   B CA  1 
ATOM   2986 C  C   . ASN   B 1 60  ? -16.424 38.955 -20.178 1.00 25.28  ? 57  ASN   B C   1 
ATOM   2987 O  O   . ASN   B 1 60  ? -16.032 40.055 -20.559 1.00 24.53  ? 57  ASN   B O   1 
ATOM   2988 C  CB  . ASN   B 1 60  ? -16.738 39.807 -17.809 1.00 25.59  ? 57  ASN   B CB  1 
ATOM   2989 C  CG  . ASN   B 1 60  ? -15.311 39.478 -17.453 1.00 24.32  ? 57  ASN   B CG  1 
ATOM   2990 O  OD1 . ASN   B 1 60  ? -14.711 38.659 -18.113 1.00 24.18  ? 57  ASN   B OD1 1 
ATOM   2991 N  ND2 . ASN   B 1 60  ? -14.788 40.030 -16.361 1.00 23.84  ? 57  ASN   B ND2 1 
ATOM   2992 N  N   . GLU   B 1 61  ? -16.081 37.816 -20.790 1.00 25.05  ? 58  GLU   B N   1 
ATOM   2993 C  CA  . GLU   B 1 61  ? -15.066 37.889 -21.878 1.00 25.51  ? 58  GLU   B CA  1 
ATOM   2994 C  C   . GLU   B 1 61  ? -15.657 38.675 -23.054 1.00 25.86  ? 58  GLU   B C   1 
ATOM   2995 O  O   . GLU   B 1 61  ? -14.869 39.265 -23.811 1.00 25.32  ? 58  GLU   B O   1 
ATOM   2996 C  CB  . GLU   B 1 61  ? -14.572 36.514 -22.341 1.00 25.38  ? 58  GLU   B CB  1 
ATOM   2997 C  CG  . GLU   B 1 61  ? -13.630 35.898 -21.326 1.00 25.13  ? 58  GLU   B CG  1 
ATOM   2998 C  CD  . GLU   B 1 61  ? -12.952 34.617 -21.762 1.00 25.41  ? 58  GLU   B CD  1 
ATOM   2999 O  OE1 . GLU   B 1 61  ? -13.623 33.597 -21.784 1.00 26.08  ? 58  GLU   B OE1 1 
ATOM   3000 O  OE2 . GLU   B 1 61  ? -11.743 34.674 -22.079 1.00 25.31  ? 58  GLU   B OE2 1 
ATOM   3001 N  N   . GLU   B 1 62  ? -16.981 38.649 -23.243 1.00 27.78  ? 59  GLU   B N   1 
ATOM   3002 C  CA  . GLU   B 1 62  ? -17.634 39.436 -24.328 1.00 29.21  ? 59  GLU   B CA  1 
ATOM   3003 C  C   . GLU   B 1 62  ? -17.355 40.932 -24.146 1.00 28.74  ? 59  GLU   B C   1 
ATOM   3004 O  O   . GLU   B 1 62  ? -16.891 41.626 -25.063 1.00 28.48  ? 59  GLU   B O   1 
ATOM   3005 C  CB  . GLU   B 1 62  ? -19.146 39.221 -24.339 1.00 31.89  ? 59  GLU   B CB  1 
ATOM   3006 C  CG  . GLU   B 1 62  ? -19.821 40.020 -25.433 1.00 33.90  ? 59  GLU   B CG  1 
ATOM   3007 C  CD  . GLU   B 1 62  ? -21.337 39.943 -25.508 1.00 37.32  ? 59  GLU   B CD  1 
ATOM   3008 O  OE1 . GLU   B 1 62  ? -21.949 39.127 -24.804 1.00 38.36  ? 59  GLU   B OE1 1 
ATOM   3009 O  OE2 . GLU   B 1 62  ? -21.907 40.695 -26.313 1.00 40.18  ? 59  GLU   B OE2 1 
ATOM   3010 N  N   . GLN   B 1 63  ? -17.548 41.400 -22.938 1.00 27.86  ? 60  GLN   B N   1 
ATOM   3011 C  CA  . GLN   B 1 63  ? -17.404 42.823 -22.584 1.00 28.76  ? 60  GLN   B CA  1 
ATOM   3012 C  C   . GLN   B 1 63  ? -15.931 43.226 -22.515 1.00 27.76  ? 60  GLN   B C   1 
ATOM   3013 O  O   . GLN   B 1 63  ? -15.659 44.361 -22.937 1.00 28.05  ? 60  GLN   B O   1 
ATOM   3014 C  CB  . GLN   B 1 63  ? -18.140 43.085 -21.284 1.00 29.32  ? 60  GLN   B CB  1 
ATOM   3015 C  CG  . GLN   B 1 63  ? -19.643 42.940 -21.456 1.00 30.58  ? 60  GLN   B CG  1 
ATOM   3016 C  CD  . GLN   B 1 63  ? -20.155 41.535 -21.270 1.00 29.80  ? 60  GLN   B CD  1 
ATOM   3017 O  OE1 . GLN   B 1 63  ? -19.453 40.623 -20.849 1.00 29.05  ? 60  GLN   B OE1 1 
ATOM   3018 N  NE2 . GLN   B 1 63  ? -21.426 41.384 -21.552 1.00 31.36  ? 60  GLN   B NE2 1 
ATOM   3019 N  N   . VAL   B 1 64  ? -15.056 42.404 -21.916 1.00 25.84  ? 61  VAL   B N   1 
ATOM   3020 C  CA  . VAL   B 1 64  ? -13.610 42.739 -21.812 1.00 24.74  ? 61  VAL   B CA  1 
ATOM   3021 C  C   . VAL   B 1 64  ? -13.037 42.807 -23.236 1.00 25.08  ? 61  VAL   B C   1 
ATOM   3022 O  O   . VAL   B 1 64  ? -12.279 43.720 -23.559 1.00 24.72  ? 61  VAL   B O   1 
ATOM   3023 C  CB  . VAL   B 1 64  ? -12.866 41.755 -20.895 1.00 23.71  ? 61  VAL   B CB  1 
ATOM   3024 C  CG1 . VAL   B 1 64  ? -11.374 42.004 -20.860 1.00 22.79  ? 61  VAL   B CG1 1 
ATOM   3025 C  CG2 . VAL   B 1 64  ? -13.439 41.778 -19.477 1.00 23.94  ? 61  VAL   B CG2 1 
ATOM   3026 N  N   . GLY   B 1 65  ? -13.408 41.848 -24.074 1.00 25.12  ? 62  GLY   B N   1 
ATOM   3027 C  CA  . GLY   B 1 65  ? -12.882 41.771 -25.445 1.00 25.54  ? 62  GLY   B CA  1 
ATOM   3028 C  C   . GLY   B 1 65  ? -13.286 42.993 -26.246 1.00 26.45  ? 62  GLY   B C   1 
ATOM   3029 O  O   . GLY   B 1 65  ? -12.456 43.572 -26.949 1.00 26.50  ? 62  GLY   B O   1 
ATOM   3030 N  N   . LEU   B 1 66  ? -14.540 43.390 -26.101 1.00 26.98  ? 63  LEU   B N   1 
ATOM   3031 C  CA  . LEU   B 1 66  ? -15.117 44.567 -26.785 1.00 28.80  ? 63  LEU   B CA  1 
ATOM   3032 C  C   . LEU   B 1 66  ? -14.372 45.815 -26.329 1.00 28.76  ? 63  LEU   B C   1 
ATOM   3033 O  O   . LEU   B 1 66  ? -14.081 46.673 -27.209 1.00 28.83  ? 63  LEU   B O   1 
ATOM   3034 C  CB  . LEU   B 1 66  ? -16.574 44.560 -26.352 1.00 30.57  ? 63  LEU   B CB  1 
ATOM   3035 C  CG  . LEU   B 1 66  ? -17.623 45.284 -27.146 1.00 32.94  ? 63  LEU   B CG  1 
ATOM   3036 C  CD1 . LEU   B 1 66  ? -17.392 45.217 -28.669 1.00 34.42  ? 63  LEU   B CD1 1 
ATOM   3037 C  CD2 . LEU   B 1 66  ? -18.971 44.618 -26.786 1.00 33.36  ? 63  LEU   B CD2 1 
ATOM   3038 N  N   . ALA   B 1 67  ? -14.028 45.916 -25.034 1.00 28.19  ? 64  ALA   B N   1 
ATOM   3039 C  CA  . ALA   B 1 67  ? -13.257 47.090 -24.544 1.00 28.87  ? 64  ALA   B CA  1 
ATOM   3040 C  C   . ALA   B 1 67  ? -11.898 47.112 -25.259 1.00 29.20  ? 64  ALA   B C   1 
ATOM   3041 O  O   . ALA   B 1 67  ? -11.502 48.163 -25.742 1.00 29.67  ? 64  ALA   B O   1 
ATOM   3042 C  CB  . ALA   B 1 67  ? -13.044 47.036 -23.056 1.00 28.55  ? 64  ALA   B CB  1 
ATOM   3043 N  N   . ILE   B 1 68  ? -11.248 45.943 -25.391 1.00 28.58  ? 65  ILE   B N   1 
ATOM   3044 C  CA  . ILE   B 1 68  ? -9.927  45.810 -26.071 1.00 29.51  ? 65  ILE   B CA  1 
ATOM   3045 C  C   . ILE   B 1 68  ? -10.068 46.184 -27.547 1.00 31.19  ? 65  ILE   B C   1 
ATOM   3046 O  O   . ILE   B 1 68  ? -9.255  47.018 -28.017 1.00 32.18  ? 65  ILE   B O   1 
ATOM   3047 C  CB  . ILE   B 1 68  ? -9.292  44.426 -25.836 1.00 28.15  ? 65  ILE   B CB  1 
ATOM   3048 C  CG1 . ILE   B 1 68  ? -8.994  44.275 -24.340 1.00 27.03  ? 65  ILE   B CG1 1 
ATOM   3049 C  CG2 . ILE   B 1 68  ? -8.055  44.235 -26.712 1.00 28.65  ? 65  ILE   B CG2 1 
ATOM   3050 C  CD1 . ILE   B 1 68  ? -8.601  42.883 -23.911 1.00 25.95  ? 65  ILE   B CD1 1 
ATOM   3051 N  N   . ARG   B 1 69  ? -11.044 45.602 -28.227 1.00 32.72  ? 66  ARG   B N   1 
ATOM   3052 C  CA  . ARG   B 1 69  ? -11.263 45.862 -29.667 1.00 35.30  ? 66  ARG   B CA  1 
ATOM   3053 C  C   . ARG   B 1 69  ? -11.516 47.355 -29.859 1.00 35.04  ? 66  ARG   B C   1 
ATOM   3054 O  O   . ARG   B 1 69  ? -11.015 47.890 -30.805 1.00 36.63  ? 66  ARG   B O   1 
ATOM   3055 C  CB  . ARG   B 1 69  ? -12.433 45.026 -30.183 1.00 37.25  ? 66  ARG   B CB  1 
ATOM   3056 C  CG  . ARG   B 1 69  ? -12.042 43.649 -30.674 1.00 39.80  ? 66  ARG   B CG  1 
ATOM   3057 C  CD  . ARG   B 1 69  ? -12.994 43.195 -31.775 1.00 44.16  ? 66  ARG   B CD  1 
ATOM   3058 N  NE  . ARG   B 1 69  ? -14.368 42.984 -31.317 1.00 46.63  ? 66  ARG   B NE  1 
ATOM   3059 C  CZ  . ARG   B 1 69  ? -15.476 43.197 -32.043 1.00 49.09  ? 66  ARG   B CZ  1 
ATOM   3060 N  NH1 . ARG   B 1 69  ? -16.676 42.922 -31.534 1.00 47.56  ? 66  ARG   B NH1 1 
ATOM   3061 N  NH2 . ARG   B 1 69  ? -15.375 43.686 -33.268 1.00 51.65  ? 66  ARG   B NH2 1 
ATOM   3062 N  N   . SER   B 1 70  ? -12.256 47.954 -28.943 1.00 34.27  ? 67  SER   B N   1 
ATOM   3063 C  CA  . SER   B 1 70  ? -12.638 49.384 -28.972 1.00 36.21  ? 67  SER   B CA  1 
ATOM   3064 C  C   . SER   B 1 70  ? -11.395 50.267 -28.841 1.00 36.37  ? 67  SER   B C   1 
ATOM   3065 O  O   . SER   B 1 70  ? -11.250 51.197 -29.655 1.00 37.20  ? 67  SER   B O   1 
ATOM   3066 C  CB  . SER   B 1 70  ? -13.701 49.656 -27.954 1.00 36.57  ? 67  SER   B CB  1 
ATOM   3067 O  OG  . SER   B 1 70  ? -14.311 50.890 -28.226 1.00 40.52  ? 67  SER   B OG  1 
ATOM   3068 N  N   . LYS   B 1 71  ? -10.462 49.915 -27.947 1.00 35.12  ? 68  LYS   B N   1 
ATOM   3069 C  CA  . LYS   B 1 71  ? -9.237  50.731 -27.711 1.00 36.41  ? 68  LYS   B CA  1 
ATOM   3070 C  C   . LYS   B 1 71  ? -8.235  50.531 -28.853 1.00 36.62  ? 68  LYS   B C   1 
ATOM   3071 O  O   . LYS   B 1 71  ? -7.413  51.419 -29.061 1.00 39.33  ? 68  LYS   B O   1 
ATOM   3072 C  CB  . LYS   B 1 71  ? -8.656  50.437 -26.322 1.00 35.60  ? 68  LYS   B CB  1 
ATOM   3073 C  CG  . LYS   B 1 71  ? -9.530  50.922 -25.189 1.00 36.21  ? 68  LYS   B CG  1 
ATOM   3074 C  CD  . LYS   B 1 71  ? -9.940  52.379 -25.269 1.00 38.60  ? 68  LYS   B CD  1 
ATOM   3075 C  CE  . LYS   B 1 71  ? -8.767  53.319 -25.301 1.00 41.06  ? 68  LYS   B CE  1 
ATOM   3076 N  NZ  . LYS   B 1 71  ? -9.222  54.734 -25.419 1.00 43.75  ? 68  LYS   B NZ  1 
ATOM   3077 N  N   . ILE   B 1 72  ? -8.273  49.400 -29.541 1.00 35.25  ? 69  ILE   B N   1 
ATOM   3078 C  CA  . ILE   B 1 72  ? -7.427  49.188 -30.739 1.00 36.09  ? 69  ILE   B CA  1 
ATOM   3079 C  C   . ILE   B 1 72  ? -8.055  49.974 -31.900 1.00 37.63  ? 69  ILE   B C   1 
ATOM   3080 O  O   . ILE   B 1 72  ? -7.321  50.775 -32.575 1.00 39.92  ? 69  ILE   B O   1 
ATOM   3081 C  CB  . ILE   B 1 72  ? -7.269  47.689 -31.056 1.00 34.88  ? 69  ILE   B CB  1 
ATOM   3082 C  CG1 . ILE   B 1 72  ? -6.564  46.946 -29.919 1.00 33.90  ? 69  ILE   B CG1 1 
ATOM   3083 C  CG2 . ILE   B 1 72  ? -6.555  47.529 -32.394 1.00 36.42  ? 69  ILE   B CG2 1 
ATOM   3084 C  CD1 . ILE   B 1 72  ? -6.764  45.435 -29.899 1.00 32.92  ? 69  ILE   B CD1 1 
ATOM   3085 N  N   . ALA   B 1 73  ? -9.374  49.844 -32.110 1.00 37.46  ? 70  ALA   B N   1 
ATOM   3086 C  CA  . ALA   B 1 73  ? -10.035 50.501 -33.265 1.00 39.95  ? 70  ALA   B CA  1 
ATOM   3087 C  C   . ALA   B 1 73  ? -10.001 52.028 -33.092 1.00 42.44  ? 70  ALA   B C   1 
ATOM   3088 O  O   . ALA   B 1 73  ? -9.966  52.748 -34.137 1.00 44.66  ? 70  ALA   B O   1 
ATOM   3089 C  CB  . ALA   B 1 73  ? -11.428 49.962 -33.476 1.00 39.37  ? 70  ALA   B CB  1 
ATOM   3090 N  N   . ASP   B 1 74  ? -9.994  52.550 -31.861 1.00 43.02  ? 71  ASP   B N   1 
ATOM   3091 C  CA  . ASP   B 1 74  ? -9.992  54.022 -31.622 1.00 46.02  ? 71  ASP   B CA  1 
ATOM   3092 C  C   . ASP   B 1 74  ? -8.574  54.597 -31.784 1.00 46.42  ? 71  ASP   B C   1 
ATOM   3093 O  O   . ASP   B 1 74  ? -8.463  55.818 -31.742 1.00 48.14  ? 71  ASP   B O   1 
ATOM   3094 C  CB  . ASP   B 1 74  ? -10.703 54.400 -30.312 1.00 47.00  ? 71  ASP   B CB  1 
ATOM   3095 C  CG  . ASP   B 1 74  ? -9.924  54.318 -29.011 1.00 47.92  ? 71  ASP   B CG  1 
ATOM   3096 O  OD1 . ASP   B 1 74  ? -8.683  54.250 -29.036 1.00 48.63  ? 71  ASP   B OD1 1 
ATOM   3097 O  OD2 . ASP   B 1 74  ? -10.576 54.413 -27.965 1.00 50.62  ? 71  ASP   B OD2 1 
ATOM   3098 N  N   . GLY   B 1 75  ? -7.570  53.766 -32.088 1.00 45.89  ? 72  GLY   B N   1 
ATOM   3099 C  CA  . GLY   B 1 75  ? -6.169  54.189 -32.302 1.00 47.47  ? 72  GLY   B CA  1 
ATOM   3100 C  C   . GLY   B 1 75  ? -5.408  54.310 -30.985 1.00 47.57  ? 72  GLY   B C   1 
ATOM   3101 O  O   . GLY   B 1 75  ? -4.251  54.738 -30.991 1.00 48.38  ? 72  GLY   B O   1 
ATOM   3102 N  N   . SER   B 1 76  ? -6.015  53.954 -29.856 1.00 46.39  ? 73  SER   B N   1 
ATOM   3103 C  CA  . SER   B 1 76  ? -5.359  54.125 -28.526 1.00 47.19  ? 73  SER   B CA  1 
ATOM   3104 C  C   . SER   B 1 76  ? -4.175  53.158 -28.382 1.00 46.21  ? 73  SER   B C   1 
ATOM   3105 O  O   . SER   B 1 76  ? -3.134  53.587 -27.904 1.00 48.26  ? 73  SER   B O   1 
ATOM   3106 C  CB  . SER   B 1 76  ? -6.328  53.958 -27.386 1.00 45.32  ? 73  SER   B CB  1 
ATOM   3107 O  OG  . SER   B 1 76  ? -7.201  55.068 -27.329 1.00 47.02  ? 73  SER   B OG  1 
ATOM   3108 N  N   . VAL   B 1 77  ? -4.339  51.906 -28.787 1.00 44.59  ? 74  VAL   B N   1 
ATOM   3109 C  CA  . VAL   B 1 77  ? -3.303  50.846 -28.597 1.00 43.95  ? 74  VAL   B CA  1 
ATOM   3110 C  C   . VAL   B 1 77  ? -3.322  49.932 -29.815 1.00 43.10  ? 74  VAL   B C   1 
ATOM   3111 O  O   . VAL   B 1 77  ? -4.358  49.896 -30.505 1.00 41.98  ? 74  VAL   B O   1 
ATOM   3112 C  CB  . VAL   B 1 77  ? -3.560  50.012 -27.334 1.00 41.98  ? 74  VAL   B CB  1 
ATOM   3113 C  CG1 . VAL   B 1 77  ? -3.324  50.814 -26.078 1.00 42.78  ? 74  VAL   B CG1 1 
ATOM   3114 C  CG2 . VAL   B 1 77  ? -4.951  49.374 -27.338 1.00 40.80  ? 74  VAL   B CG2 1 
ATOM   3115 N  N   . LYS   B 1 78  ? -2.236  49.200 -30.017 1.00 43.62  ? 75  LYS   B N   1 
ATOM   3116 C  CA  . LYS   B 1 78  ? -2.205  48.127 -31.032 1.00 44.73  ? 75  LYS   B CA  1 
ATOM   3117 C  C   . LYS   B 1 78  ? -2.422  46.822 -30.270 1.00 41.08  ? 75  LYS   B C   1 
ATOM   3118 O  O   . LYS   B 1 78  ? -2.254  46.801 -28.999 1.00 38.20  ? 75  LYS   B O   1 
ATOM   3119 C  CB  . LYS   B 1 78  ? -0.966  48.228 -31.933 1.00 49.56  ? 75  LYS   B CB  1 
ATOM   3120 C  CG  . LYS   B 1 78  ? 0.404   47.987 -31.304 1.00 52.70  ? 75  LYS   B CG  1 
ATOM   3121 C  CD  . LYS   B 1 78  ? 1.558   48.492 -32.216 1.00 56.34  ? 75  LYS   B CD  1 
ATOM   3122 C  CE  . LYS   B 1 78  ? 2.939   47.920 -31.923 1.00 58.55  ? 75  LYS   B CE  1 
ATOM   3123 N  NZ  . LYS   B 1 78  ? 3.578   48.459 -30.682 1.00 59.70  ? 75  LYS   B NZ  1 
ATOM   3124 N  N   . ARG   B 1 79  ? -2.894  45.817 -30.996 1.00 38.87  ? 76  ARG   B N   1 
ATOM   3125 C  CA  . ARG   B 1 79  ? -3.156  44.481 -30.409 1.00 37.08  ? 76  ARG   B CA  1 
ATOM   3126 C  C   . ARG   B 1 79  ? -1.908  44.034 -29.652 1.00 37.13  ? 76  ARG   B C   1 
ATOM   3127 O  O   . ARG   B 1 79  ? -2.065  43.458 -28.585 1.00 35.65  ? 76  ARG   B O   1 
ATOM   3128 C  CB  . ARG   B 1 79  ? -3.577  43.445 -31.456 1.00 36.24  ? 76  ARG   B CB  1 
ATOM   3129 C  CG  . ARG   B 1 79  ? -3.733  42.044 -30.894 1.00 34.26  ? 76  ARG   B CG  1 
ATOM   3130 C  CD  . ARG   B 1 79  ? -4.860  41.964 -29.868 1.00 32.83  ? 76  ARG   B CD  1 
ATOM   3131 N  NE  . ARG   B 1 79  ? -4.956  40.668 -29.193 1.00 30.90  ? 76  ARG   B NE  1 
ATOM   3132 C  CZ  . ARG   B 1 79  ? -4.255  40.302 -28.117 1.00 29.72  ? 76  ARG   B CZ  1 
ATOM   3133 N  NH1 . ARG   B 1 79  ? -3.397  41.123 -27.531 1.00 29.55  ? 76  ARG   B NH1 1 
ATOM   3134 N  NH2 . ARG   B 1 79  ? -4.440  39.108 -27.583 1.00 28.40  ? 76  ARG   B NH2 1 
ATOM   3135 N  N   . GLU   B 1 80  ? -0.713  44.267 -30.185 1.00 39.94  ? 77  GLU   B N   1 
ATOM   3136 C  CA  . GLU   B 1 80  ? 0.519   43.674 -29.612 1.00 41.57  ? 77  GLU   B CA  1 
ATOM   3137 C  C   . GLU   B 1 80  ? 0.913   44.426 -28.340 1.00 40.88  ? 77  GLU   B C   1 
ATOM   3138 O  O   . GLU   B 1 80  ? 1.756   43.901 -27.605 1.00 39.92  ? 77  GLU   B O   1 
ATOM   3139 C  CB  . GLU   B 1 80  ? 1.680   43.653 -30.603 1.00 46.59  ? 77  GLU   B CB  1 
ATOM   3140 C  CG  . GLU   B 1 80  ? 1.366   42.865 -31.851 1.00 49.82  ? 77  GLU   B CG  1 
ATOM   3141 C  CD  . GLU   B 1 80  ? 0.987   43.796 -32.992 1.00 54.82  ? 77  GLU   B CD  1 
ATOM   3142 O  OE1 . GLU   B 1 80  ? 1.727   43.812 -33.985 1.00 61.37  ? 77  GLU   B OE1 1 
ATOM   3143 O  OE2 . GLU   B 1 80  ? -0.037  44.514 -32.880 1.00 56.33  ? 77  GLU   B OE2 1 
ATOM   3144 N  N   . ASP   B 1 81  ? 0.322   45.590 -28.081 1.00 39.84  ? 78  ASP   B N   1 
ATOM   3145 C  CA  . ASP   B 1 81  ? 0.540   46.328 -26.822 1.00 39.06  ? 78  ASP   B CA  1 
ATOM   3146 C  C   . ASP   B 1 81  ? -0.297  45.716 -25.696 1.00 36.04  ? 78  ASP   B C   1 
ATOM   3147 O  O   . ASP   B 1 81  ? 0.001   46.031 -24.564 1.00 36.27  ? 78  ASP   B O   1 
ATOM   3148 C  CB  . ASP   B 1 81  ? 0.126   47.791 -26.901 1.00 40.85  ? 78  ASP   B CB  1 
ATOM   3149 C  CG  . ASP   B 1 81  ? 0.959   48.655 -27.825 1.00 44.83  ? 78  ASP   B CG  1 
ATOM   3150 O  OD1 . ASP   B 1 81  ? 2.173   48.369 -27.926 1.00 45.87  ? 78  ASP   B OD1 1 
ATOM   3151 O  OD2 . ASP   B 1 81  ? 0.364   49.625 -28.434 1.00 47.17  ? 78  ASP   B OD2 1 
ATOM   3152 N  N   . ILE   B 1 82  ? -1.374  44.993 -25.994 1.00 33.32  ? 79  ILE   B N   1 
ATOM   3153 C  CA  . ILE   B 1 82  ? -2.293  44.426 -24.964 1.00 31.43  ? 79  ILE   B CA  1 
ATOM   3154 C  C   . ILE   B 1 82  ? -1.870  42.990 -24.637 1.00 30.04  ? 79  ILE   B C   1 
ATOM   3155 O  O   . ILE   B 1 82  ? -1.615  42.180 -25.560 1.00 31.29  ? 79  ILE   B O   1 
ATOM   3156 C  CB  . ILE   B 1 82  ? -3.766  44.476 -25.405 1.00 30.12  ? 79  ILE   B CB  1 
ATOM   3157 C  CG1 . ILE   B 1 82  ? -4.228  45.915 -25.577 1.00 31.45  ? 79  ILE   B CG1 1 
ATOM   3158 C  CG2 . ILE   B 1 82  ? -4.674  43.753 -24.420 1.00 28.92  ? 79  ILE   B CG2 1 
ATOM   3159 C  CD1 . ILE   B 1 82  ? -4.412  46.632 -24.297 1.00 31.45  ? 79  ILE   B CD1 1 
ATOM   3160 N  N   . PHE   B 1 83  ? -1.855  42.663 -23.360 1.00 28.45  ? 80  PHE   B N   1 
ATOM   3161 C  CA  . PHE   B 1 83  ? -1.515  41.299 -22.888 1.00 26.93  ? 80  PHE   B CA  1 
ATOM   3162 C  C   . PHE   B 1 83  ? -2.782  40.756 -22.254 1.00 25.96  ? 80  PHE   B C   1 
ATOM   3163 O  O   . PHE   B 1 83  ? -3.115  41.235 -21.156 1.00 25.87  ? 80  PHE   B O   1 
ATOM   3164 C  CB  . PHE   B 1 83  ? -0.380  41.323 -21.868 1.00 27.34  ? 80  PHE   B CB  1 
ATOM   3165 C  CG  . PHE   B 1 83  ? 0.089   39.953 -21.444 1.00 25.91  ? 80  PHE   B CG  1 
ATOM   3166 C  CD1 . PHE   B 1 83  ? -0.633  39.207 -20.522 1.00 24.06  ? 80  PHE   B CD1 1 
ATOM   3167 C  CD2 . PHE   B 1 83  ? 1.253   39.413 -21.995 1.00 26.36  ? 80  PHE   B CD2 1 
ATOM   3168 C  CE1 . PHE   B 1 83  ? -0.163  37.953 -20.125 1.00 23.73  ? 80  PHE   B CE1 1 
ATOM   3169 C  CE2 . PHE   B 1 83  ? 1.698   38.155 -21.606 1.00 25.61  ? 80  PHE   B CE2 1 
ATOM   3170 C  CZ  . PHE   B 1 83  ? 1.002   37.440 -20.666 1.00 24.20  ? 80  PHE   B CZ  1 
ATOM   3171 N  N   . TYR   B 1 84  ? -3.528  39.919 -22.970 1.00 25.23  ? 81  TYR   B N   1 
ATOM   3172 C  CA  . TYR   B 1 84  ? -4.842  39.391 -22.533 1.00 24.18  ? 81  TYR   B CA  1 
ATOM   3173 C  C   . TYR   B 1 84  ? -4.680  37.944 -22.057 1.00 22.95  ? 81  TYR   B C   1 
ATOM   3174 O  O   . TYR   B 1 84  ? -4.128  37.094 -22.785 1.00 22.39  ? 81  TYR   B O   1 
ATOM   3175 C  CB  . TYR   B 1 84  ? -5.867  39.436 -23.678 1.00 24.93  ? 81  TYR   B CB  1 
ATOM   3176 C  CG  . TYR   B 1 84  ? -7.227  38.899 -23.290 1.00 24.83  ? 81  TYR   B CG  1 
ATOM   3177 C  CD1 . TYR   B 1 84  ? -8.074  39.586 -22.438 1.00 25.52  ? 81  TYR   B CD1 1 
ATOM   3178 C  CD2 . TYR   B 1 84  ? -7.664  37.670 -23.740 1.00 25.85  ? 81  TYR   B CD2 1 
ATOM   3179 C  CE1 . TYR   B 1 84  ? -9.315  39.083 -22.067 1.00 25.56  ? 81  TYR   B CE1 1 
ATOM   3180 C  CE2 . TYR   B 1 84  ? -8.879  37.128 -23.349 1.00 25.33  ? 81  TYR   B CE2 1 
ATOM   3181 C  CZ  . TYR   B 1 84  ? -9.711  37.838 -22.515 1.00 24.97  ? 81  TYR   B CZ  1 
ATOM   3182 O  OH  . TYR   B 1 84  ? -10.931 37.325 -22.187 1.00 26.20  ? 81  TYR   B OH  1 
ATOM   3183 N  N   . THR   B 1 85  ? -5.219  37.680 -20.881 1.00 22.48  ? 82  THR   B N   1 
ATOM   3184 C  CA  . THR   B 1 85  ? -5.201  36.362 -20.204 1.00 22.03  ? 82  THR   B CA  1 
ATOM   3185 C  C   . THR   B 1 85  ? -6.631  35.821 -20.168 1.00 21.83  ? 82  THR   B C   1 
ATOM   3186 O  O   . THR   B 1 85  ? -7.574  36.540 -19.737 1.00 22.29  ? 82  THR   B O   1 
ATOM   3187 C  CB  . THR   B 1 85  ? -4.641  36.448 -18.790 1.00 22.01  ? 82  THR   B CB  1 
ATOM   3188 O  OG1 . THR   B 1 85  ? -3.292  36.910 -18.835 1.00 21.66  ? 82  THR   B OG1 1 
ATOM   3189 C  CG2 . THR   B 1 85  ? -4.709  35.098 -18.119 1.00 21.98  ? 82  THR   B CG2 1 
ATOM   3190 N  N   . SER   B 1 86  ? -6.784  34.591 -20.607 1.00 22.15  ? 83  SER   B N   1 
ATOM   3191 C  CA  . SER   B 1 86  ? -8.008  33.800 -20.331 1.00 22.81  ? 83  SER   B CA  1 
ATOM   3192 C  C   . SER   B 1 86  ? -7.601  32.530 -19.585 1.00 22.00  ? 83  SER   B C   1 
ATOM   3193 O  O   . SER   B 1 86  ? -6.381  32.257 -19.508 1.00 23.86  ? 83  SER   B O   1 
ATOM   3194 C  CB  . SER   B 1 86  ? -8.839  33.505 -21.546 1.00 23.95  ? 83  SER   B CB  1 
ATOM   3195 O  OG  . SER   B 1 86  ? -10.064 32.914 -21.105 1.00 25.75  ? 83  SER   B OG  1 
ATOM   3196 N  N   . LYS   B 1 87  ? -8.580  31.809 -19.043 1.00 21.40  ? 84  LYS   B N   1 
ATOM   3197 C  CA  . LYS   B 1 87  ? -8.343  30.617 -18.196 1.00 21.96  ? 84  LYS   B CA  1 
ATOM   3198 C  C   . LYS   B 1 87  ? -9.334  29.512 -18.587 1.00 22.27  ? 84  LYS   B C   1 
ATOM   3199 O  O   . LYS   B 1 87  ? -10.553 29.817 -18.811 1.00 22.99  ? 84  LYS   B O   1 
ATOM   3200 C  CB  . LYS   B 1 87  ? -8.441  30.970 -16.708 1.00 21.64  ? 84  LYS   B CB  1 
ATOM   3201 C  CG  . LYS   B 1 87  ? -7.682  32.222 -16.307 1.00 21.50  ? 84  LYS   B CG  1 
ATOM   3202 C  CD  . LYS   B 1 87  ? -7.639  32.371 -14.803 1.00 21.95  ? 84  LYS   B CD  1 
ATOM   3203 C  CE  . LYS   B 1 87  ? -6.921  33.616 -14.334 1.00 22.83  ? 84  LYS   B CE  1 
ATOM   3204 N  NZ  . LYS   B 1 87  ? -7.843  34.766 -14.405 1.00 23.60  ? 84  LYS   B NZ  1 
ATOM   3205 N  N   . LEU   B 1 88  ? -8.797  28.306 -18.701 1.00 22.08  ? 85  LEU   B N   1 
ATOM   3206 C  CA  . LEU   B 1 88  ? -9.550  27.044 -18.918 1.00 22.97  ? 85  LEU   B CA  1 
ATOM   3207 C  C   . LEU   B 1 88  ? -10.279 26.665 -17.637 1.00 23.06  ? 85  LEU   B C   1 
ATOM   3208 O  O   . LEU   B 1 88  ? -9.580  26.383 -16.604 1.00 22.82  ? 85  LEU   B O   1 
ATOM   3209 C  CB  . LEU   B 1 88  ? -8.548  25.960 -19.290 1.00 23.23  ? 85  LEU   B CB  1 
ATOM   3210 C  CG  . LEU   B 1 88  ? -9.133  24.578 -19.516 1.00 24.47  ? 85  LEU   B CG  1 
ATOM   3211 C  CD1 . LEU   B 1 88  ? -9.817  24.557 -20.878 1.00 25.46  ? 85  LEU   B CD1 1 
ATOM   3212 C  CD2 . LEU   B 1 88  ? -8.043  23.512 -19.401 1.00 24.62  ? 85  LEU   B CD2 1 
ATOM   3213 N  N   . TRP   B 1 89  ? -11.598 26.615 -17.674 1.00 24.22  ? 86  TRP   B N   1 
ATOM   3214 C  CA  . TRP   B 1 89  ? -12.362 26.211 -16.461 1.00 25.04  ? 86  TRP   B CA  1 
ATOM   3215 C  C   . TRP   B 1 89  ? -12.238 24.693 -16.203 1.00 26.96  ? 86  TRP   B C   1 
ATOM   3216 O  O   . TRP   B 1 89  ? -11.923 23.914 -17.133 1.00 27.80  ? 86  TRP   B O   1 
ATOM   3217 C  CB  . TRP   B 1 89  ? -13.819 26.723 -16.524 1.00 25.87  ? 86  TRP   B CB  1 
ATOM   3218 C  CG  . TRP   B 1 89  ? -14.538 26.514 -15.237 1.00 26.45  ? 86  TRP   B CG  1 
ATOM   3219 C  CD1 . TRP   B 1 89  ? -15.690 25.806 -15.070 1.00 28.07  ? 86  TRP   B CD1 1 
ATOM   3220 C  CD2 . TRP   B 1 89  ? -14.028 26.771 -13.915 1.00 26.03  ? 86  TRP   B CD2 1 
ATOM   3221 N  NE1 . TRP   B 1 89  ? -15.975 25.687 -13.743 1.00 28.48  ? 86  TRP   B NE1 1 
ATOM   3222 C  CE2 . TRP   B 1 89  ? -14.985 26.272 -13.012 1.00 27.32  ? 86  TRP   B CE2 1 
ATOM   3223 C  CE3 . TRP   B 1 89  ? -12.916 27.456 -13.414 1.00 24.48  ? 86  TRP   B CE3 1 
ATOM   3224 C  CZ2 . TRP   B 1 89  ? -14.841 26.382 -11.629 1.00 27.68  ? 86  TRP   B CZ2 1 
ATOM   3225 C  CZ3 . TRP   B 1 89  ? -12.790 27.606 -12.059 1.00 25.34  ? 86  TRP   B CZ3 1 
ATOM   3226 C  CH2 . TRP   B 1 89  ? -13.726 27.056 -11.181 1.00 26.81  ? 86  TRP   B CH2 1 
ATOM   3227 N  N   . SER   B 1 90  ? -12.515 24.289 -14.962 1.00 26.99  ? 87  SER   B N   1 
ATOM   3228 C  CA  . SER   B 1 90  ? -12.240 22.953 -14.369 1.00 28.09  ? 87  SER   B CA  1 
ATOM   3229 C  C   . SER   B 1 90  ? -13.161 21.858 -14.942 1.00 29.68  ? 87  SER   B C   1 
ATOM   3230 O  O   . SER   B 1 90  ? -12.891 20.653 -14.704 1.00 30.05  ? 87  SER   B O   1 
ATOM   3231 C  CB  . SER   B 1 90  ? -12.354 23.058 -12.859 1.00 28.33  ? 87  SER   B CB  1 
ATOM   3232 O  OG  . SER   B 1 90  ? -11.477 24.074 -12.373 1.00 27.80  ? 87  SER   B OG  1 
ATOM   3233 N  N   . THR   B 1 91  ? -14.224 22.242 -15.639 1.00 30.08  ? 88  THR   B N   1 
ATOM   3234 C  CA  . THR   B 1 91  ? -15.122 21.313 -16.380 1.00 31.78  ? 88  THR   B CA  1 
ATOM   3235 C  C   . THR   B 1 91  ? -14.579 20.947 -17.773 1.00 31.71  ? 88  THR   B C   1 
ATOM   3236 O  O   . THR   B 1 91  ? -15.199 20.065 -18.418 1.00 33.87  ? 88  THR   B O   1 
ATOM   3237 C  CB  . THR   B 1 91  ? -16.531 21.904 -16.465 1.00 32.39  ? 88  THR   B CB  1 
ATOM   3238 O  OG1 . THR   B 1 91  ? -16.403 23.181 -17.094 1.00 30.33  ? 88  THR   B OG1 1 
ATOM   3239 C  CG2 . THR   B 1 91  ? -17.162 22.038 -15.092 1.00 33.09  ? 88  THR   B CG2 1 
ATOM   3240 N  N   . PHE   B 1 92  ? -13.458 21.523 -18.194 1.00 30.21  ? 89  PHE   B N   1 
ATOM   3241 C  CA  . PHE   B 1 92  ? -12.850 21.367 -19.544 1.00 30.53  ? 89  PHE   B CA  1 
ATOM   3242 C  C   . PHE   B 1 92  ? -11.409 20.857 -19.440 1.00 30.63  ? 89  PHE   B C   1 
ATOM   3243 O  O   . PHE   B 1 92  ? -10.625 21.036 -20.378 1.00 31.73  ? 89  PHE   B O   1 
ATOM   3244 C  CB  . PHE   B 1 92  ? -12.869 22.708 -20.282 1.00 29.34  ? 89  PHE   B CB  1 
ATOM   3245 C  CG  . PHE   B 1 92  ? -14.227 23.345 -20.414 1.00 29.88  ? 89  PHE   B CG  1 
ATOM   3246 C  CD1 . PHE   B 1 92  ? -15.229 22.778 -21.199 1.00 32.12  ? 89  PHE   B CD1 1 
ATOM   3247 C  CD2 . PHE   B 1 92  ? -14.521 24.509 -19.730 1.00 29.40  ? 89  PHE   B CD2 1 
ATOM   3248 C  CE1 . PHE   B 1 92  ? -16.474 23.384 -21.321 1.00 32.50  ? 89  PHE   B CE1 1 
ATOM   3249 C  CE2 . PHE   B 1 92  ? -15.777 25.097 -19.828 1.00 30.02  ? 89  PHE   B CE2 1 
ATOM   3250 C  CZ  . PHE   B 1 92  ? -16.747 24.542 -20.628 1.00 31.15  ? 89  PHE   B CZ  1 
ATOM   3251 N  N   . HIS   B 1 93  ? -11.052 20.223 -18.337 1.00 30.08  ? 90  HIS   B N   1 
ATOM   3252 C  CA  . HIS   B 1 93  ? -9.725  19.584 -18.138 1.00 30.42  ? 90  HIS   B CA  1 
ATOM   3253 C  C   . HIS   B 1 93  ? -9.556  18.362 -19.071 1.00 32.00  ? 90  HIS   B C   1 
ATOM   3254 O  O   . HIS   B 1 93  ? -8.397  18.060 -19.469 1.00 31.99  ? 90  HIS   B O   1 
ATOM   3255 C  CB  . HIS   B 1 93  ? -9.575  19.180 -16.667 1.00 30.44  ? 90  HIS   B CB  1 
ATOM   3256 C  CG  . HIS   B 1 93  ? -9.281  20.300 -15.731 1.00 29.46  ? 90  HIS   B CG  1 
ATOM   3257 N  ND1 . HIS   B 1 93  ? -8.958  20.077 -14.401 1.00 30.08  ? 90  HIS   B ND1 1 
ATOM   3258 C  CD2 . HIS   B 1 93  ? -9.151  21.633 -15.947 1.00 28.34  ? 90  HIS   B CD2 1 
ATOM   3259 C  CE1 . HIS   B 1 93  ? -8.653  21.227 -13.838 1.00 28.60  ? 90  HIS   B CE1 1 
ATOM   3260 N  NE2 . HIS   B 1 93  ? -8.776  22.197 -14.749 1.00 27.55  ? 90  HIS   B NE2 1 
ATOM   3261 N  N   . ARG   B 1 94  ? -10.608 17.640 -19.413 1.00 33.80  ? 91  ARG   B N   1 
ATOM   3262 C  CA  . ARG   B 1 94  ? -10.369 16.449 -20.289 1.00 36.84  ? 91  ARG   B CA  1 
ATOM   3263 C  C   . ARG   B 1 94  ? -9.790  16.975 -21.595 1.00 36.60  ? 91  ARG   B C   1 
ATOM   3264 O  O   . ARG   B 1 94  ? -10.267 18.015 -22.048 1.00 35.62  ? 91  ARG   B O   1 
ATOM   3265 C  CB  . ARG   B 1 94  ? -11.621 15.616 -20.521 1.00 39.58  ? 91  ARG   B CB  1 
ATOM   3266 C  CG  . ARG   B 1 94  ? -12.086 14.929 -19.254 1.00 41.20  ? 91  ARG   B CG  1 
ATOM   3267 C  CD  . ARG   B 1 94  ? -13.360 14.162 -19.416 1.00 44.24  ? 91  ARG   B CD  1 
ATOM   3268 N  NE  . ARG   B 1 94  ? -13.577 13.504 -18.135 1.00 45.90  ? 91  ARG   B NE  1 
ATOM   3269 C  CZ  . ARG   B 1 94  ? -13.380 12.202 -17.910 1.00 49.38  ? 91  ARG   B CZ  1 
ATOM   3270 N  NH1 . ARG   B 1 94  ? -13.007 11.404 -18.902 1.00 50.89  ? 91  ARG   B NH1 1 
ATOM   3271 N  NH2 . ARG   B 1 94  ? -13.586 11.686 -16.708 1.00 49.99  ? 91  ARG   B NH2 1 
ATOM   3272 N  N   . PRO   B 1 95  ? -8.677  16.376 -22.101 1.00 37.16  ? 92  PRO   B N   1 
ATOM   3273 C  CA  . PRO   B 1 95  ? -7.835  16.992 -23.135 1.00 36.91  ? 92  PRO   B CA  1 
ATOM   3274 C  C   . PRO   B 1 95  ? -8.584  17.402 -24.409 1.00 37.18  ? 92  PRO   B C   1 
ATOM   3275 O  O   . PRO   B 1 95  ? -8.264  18.427 -24.953 1.00 35.69  ? 92  PRO   B O   1 
ATOM   3276 C  CB  . PRO   B 1 95  ? -6.712  15.971 -23.435 1.00 38.90  ? 92  PRO   B CB  1 
ATOM   3277 C  CG  . PRO   B 1 95  ? -7.021  14.743 -22.580 1.00 40.10  ? 92  PRO   B CG  1 
ATOM   3278 C  CD  . PRO   B 1 95  ? -8.071  15.150 -21.569 1.00 38.72  ? 92  PRO   B CD  1 
ATOM   3279 N  N   . GLU   B 1 96  ? -9.599  16.629 -24.800 1.00 39.07  ? 93  GLU   B N   1 
ATOM   3280 C  CA  . GLU   B 1 96  ? -10.391 16.851 -26.033 1.00 40.13  ? 93  GLU   B CA  1 
ATOM   3281 C  C   . GLU   B 1 96  ? -11.279 18.079 -25.835 1.00 38.01  ? 93  GLU   B C   1 
ATOM   3282 O  O   . GLU   B 1 96  ? -11.811 18.573 -26.838 1.00 37.74  ? 93  GLU   B O   1 
ATOM   3283 C  CB  . GLU   B 1 96  ? -11.219 15.616 -26.409 1.00 43.11  ? 93  GLU   B CB  1 
ATOM   3284 C  CG  . GLU   B 1 96  ? -12.364 15.350 -25.446 1.00 44.37  ? 93  GLU   B CG  1 
ATOM   3285 C  CD  . GLU   B 1 96  ? -12.095 14.485 -24.218 1.00 46.06  ? 93  GLU   B CD  1 
ATOM   3286 O  OE1 . GLU   B 1 96  ? -10.907 14.175 -23.929 1.00 46.83  ? 93  GLU   B OE1 1 
ATOM   3287 O  OE2 . GLU   B 1 96  ? -13.090 14.093 -23.552 1.00 48.37  ? 93  GLU   B OE2 1 
ATOM   3288 N  N   . LEU   B 1 97  ? -11.391 18.596 -24.604 1.00 35.90  ? 94  LEU   B N   1 
ATOM   3289 C  CA  . LEU   B 1 97  ? -12.277 19.753 -24.332 1.00 34.49  ? 94  LEU   B CA  1 
ATOM   3290 C  C   . LEU   B 1 97  ? -11.454 21.059 -24.296 1.00 32.47  ? 94  LEU   B C   1 
ATOM   3291 O  O   . LEU   B 1 97  ? -12.033 22.155 -24.275 1.00 31.34  ? 94  LEU   B O   1 
ATOM   3292 C  CB  . LEU   B 1 97  ? -12.996 19.499 -23.005 1.00 34.69  ? 94  LEU   B CB  1 
ATOM   3293 C  CG  . LEU   B 1 97  ? -13.909 18.267 -22.952 1.00 36.84  ? 94  LEU   B CG  1 
ATOM   3294 C  CD1 . LEU   B 1 97  ? -14.646 18.182 -21.625 1.00 37.02  ? 94  LEU   B CD1 1 
ATOM   3295 C  CD2 . LEU   B 1 97  ? -14.946 18.256 -24.060 1.00 38.23  ? 94  LEU   B CD2 1 
ATOM   3296 N  N   . VAL   B 1 98  ? -10.138 20.975 -24.305 1.00 31.69  ? 95  VAL   B N   1 
ATOM   3297 C  CA  . VAL   B 1 98  ? -9.293  22.164 -24.000 1.00 29.68  ? 95  VAL   B CA  1 
ATOM   3298 C  C   . VAL   B 1 98  ? -9.331  23.158 -25.176 1.00 29.82  ? 95  VAL   B C   1 
ATOM   3299 O  O   . VAL   B 1 98  ? -9.649  24.345 -24.959 1.00 28.29  ? 95  VAL   B O   1 
ATOM   3300 C  CB  . VAL   B 1 98  ? -7.867  21.723 -23.646 1.00 29.50  ? 95  VAL   B CB  1 
ATOM   3301 C  CG1 . VAL   B 1 98  ? -6.902  22.893 -23.606 1.00 28.27  ? 95  VAL   B CG1 1 
ATOM   3302 C  CG2 . VAL   B 1 98  ? -7.839  20.976 -22.316 1.00 29.60  ? 95  VAL   B CG2 1 
ATOM   3303 N  N   . ARG   B 1 99  ? -8.957  22.708 -26.357 1.00 30.57  ? 96  ARG   B N   1 
ATOM   3304 C  CA  . ARG   B 1 99  ? -8.911  23.601 -27.526 1.00 31.00  ? 96  ARG   B CA  1 
ATOM   3305 C  C   . ARG   B 1 99  ? -10.292 24.195 -27.776 1.00 30.96  ? 96  ARG   B C   1 
ATOM   3306 O  O   . ARG   B 1 99  ? -10.398 25.410 -28.002 1.00 30.37  ? 96  ARG   B O   1 
ATOM   3307 C  CB  . ARG   B 1 99  ? -8.326  22.952 -28.772 1.00 32.86  ? 96  ARG   B CB  1 
ATOM   3308 C  CG  . ARG   B 1 99  ? -8.344  23.928 -29.924 1.00 33.14  ? 96  ARG   B CG  1 
ATOM   3309 C  CD  . ARG   B 1 99  ? -7.586  23.477 -31.124 1.00 34.78  ? 96  ARG   B CD  1 
ATOM   3310 N  NE  . ARG   B 1 99  ? -7.935  24.356 -32.215 1.00 35.29  ? 96  ARG   B NE  1 
ATOM   3311 C  CZ  . ARG   B 1 99  ? -7.169  24.554 -33.284 1.00 36.68  ? 96  ARG   B CZ  1 
ATOM   3312 N  NH1 . ARG   B 1 99  ? -5.986  23.971 -33.366 1.00 37.90  ? 96  ARG   B NH1 1 
ATOM   3313 N  NH2 . ARG   B 1 99  ? -7.581  25.332 -34.263 1.00 36.64  ? 96  ARG   B NH2 1 
ATOM   3314 N  N   . PRO   B 1 100 ? -11.391 23.422 -27.754 1.00 31.86  ? 97  PRO   B N   1 
ATOM   3315 C  CA  . PRO   B 1 100 ? -12.696 24.044 -27.985 1.00 32.15  ? 97  PRO   B CA  1 
ATOM   3316 C  C   . PRO   B 1 100 ? -13.058 25.089 -26.917 1.00 30.31  ? 97  PRO   B C   1 
ATOM   3317 O  O   . PRO   B 1 100 ? -13.726 26.069 -27.277 1.00 29.31  ? 97  PRO   B O   1 
ATOM   3318 C  CB  . PRO   B 1 100 ? -13.642 22.852 -27.998 1.00 33.80  ? 97  PRO   B CB  1 
ATOM   3319 C  CG  . PRO   B 1 100 ? -12.764 21.723 -28.515 1.00 35.19  ? 97  PRO   B CG  1 
ATOM   3320 C  CD  . PRO   B 1 100 ? -11.469 21.946 -27.760 1.00 33.89  ? 97  PRO   B CD  1 
ATOM   3321 N  N   . ALA   B 1 101 ? -12.579 24.900 -25.674 1.00 29.78  ? 98  ALA   B N   1 
ATOM   3322 C  CA  . ALA   B 1 101 ? -12.813 25.867 -24.582 1.00 28.38  ? 98  ALA   B CA  1 
ATOM   3323 C  C   . ALA   B 1 101 ? -12.034 27.137 -24.923 1.00 27.26  ? 98  ALA   B C   1 
ATOM   3324 O  O   . ALA   B 1 101 ? -12.599 28.227 -24.825 1.00 27.59  ? 98  ALA   B O   1 
ATOM   3325 C  CB  . ALA   B 1 101 ? -12.431 25.325 -23.210 1.00 27.75  ? 98  ALA   B CB  1 
ATOM   3326 N  N   . LEU   B 1 102 ? -10.798 27.015 -25.377 1.00 27.29  ? 99  LEU   B N   1 
ATOM   3327 C  CA  . LEU   B 1 102 ? -10.039 28.218 -25.787 1.00 26.56  ? 99  LEU   B CA  1 
ATOM   3328 C  C   . LEU   B 1 102 ? -10.739 28.879 -26.982 1.00 27.64  ? 99  LEU   B C   1 
ATOM   3329 O  O   . LEU   B 1 102 ? -10.876 30.100 -26.983 1.00 25.90  ? 99  LEU   B O   1 
ATOM   3330 C  CB  . LEU   B 1 102 ? -8.592  27.825 -26.078 1.00 26.70  ? 99  LEU   B CB  1 
ATOM   3331 C  CG  . LEU   B 1 102 ? -7.663  28.914 -26.600 1.00 26.53  ? 99  LEU   B CG  1 
ATOM   3332 C  CD1 . LEU   B 1 102 ? -7.716  30.180 -25.737 1.00 24.83  ? 99  LEU   B CD1 1 
ATOM   3333 C  CD2 . LEU   B 1 102 ? -6.241  28.360 -26.723 1.00 26.80  ? 99  LEU   B CD2 1 
ATOM   3334 N  N   . GLU   B 1 103 ? -11.184 28.112 -27.987 1.00 29.35  ? 100 GLU   B N   1 
ATOM   3335 C  CA  . GLU   B 1 103 ? -11.797 28.733 -29.189 1.00 31.83  ? 100 GLU   B CA  1 
ATOM   3336 C  C   . GLU   B 1 103 ? -13.101 29.434 -28.807 1.00 30.91  ? 100 GLU   B C   1 
ATOM   3337 O  O   . GLU   B 1 103 ? -13.433 30.455 -29.418 1.00 31.01  ? 100 GLU   B O   1 
ATOM   3338 C  CB  . GLU   B 1 103 ? -12.074 27.684 -30.279 1.00 34.40  ? 100 GLU   B CB  1 
ATOM   3339 C  CG  . GLU   B 1 103 ? -10.809 27.099 -30.850 1.00 36.67  ? 100 GLU   B CG  1 
ATOM   3340 C  CD  . GLU   B 1 103 ? -11.034 25.894 -31.741 1.00 39.31  ? 100 GLU   B CD  1 
ATOM   3341 O  OE1 . GLU   B 1 103 ? -11.986 25.093 -31.490 1.00 44.62  ? 100 GLU   B OE1 1 
ATOM   3342 O  OE2 . GLU   B 1 103 ? -10.230 25.722 -32.638 1.00 40.55  ? 100 GLU   B OE2 1 
ATOM   3343 N  N   . ASN   B 1 104 ? -13.820 28.906 -27.836 1.00 31.96  ? 101 ASN   B N   1 
ATOM   3344 C  CA  . ASN   B 1 104 ? -15.059 29.535 -27.333 1.00 32.17  ? 101 ASN   B CA  1 
ATOM   3345 C  C   . ASN   B 1 104 ? -14.688 30.896 -26.715 1.00 30.14  ? 101 ASN   B C   1 
ATOM   3346 O  O   . ASN   B 1 104 ? -15.319 31.899 -27.061 1.00 29.85  ? 101 ASN   B O   1 
ATOM   3347 C  CB  . ASN   B 1 104 ? -15.785 28.639 -26.331 1.00 34.91  ? 101 ASN   B CB  1 
ATOM   3348 C  CG  . ASN   B 1 104 ? -17.054 29.308 -25.865 1.00 37.37  ? 101 ASN   B CG  1 
ATOM   3349 O  OD1 . ASN   B 1 104 ? -17.113 29.903 -24.787 1.00 42.84  ? 101 ASN   B OD1 1 
ATOM   3350 N  ND2 . ASN   B 1 104 ? -18.031 29.325 -26.736 1.00 38.47  ? 101 ASN   B ND2 1 
ATOM   3351 N  N   . SER   B 1 105 ? -13.651 30.951 -25.889 1.00 27.98  ? 102 SER   B N   1 
ATOM   3352 C  CA  . SER   B 1 105 ? -13.196 32.232 -25.278 1.00 26.54  ? 102 SER   B CA  1 
ATOM   3353 C  C   . SER   B 1 105 ? -12.818 33.222 -26.386 1.00 26.60  ? 102 SER   B C   1 
ATOM   3354 O  O   . SER   B 1 105 ? -13.200 34.374 -26.247 1.00 25.48  ? 102 SER   B O   1 
ATOM   3355 C  CB  . SER   B 1 105 ? -12.095 32.039 -24.277 1.00 25.49  ? 102 SER   B CB  1 
ATOM   3356 O  OG  . SER   B 1 105 ? -12.625 31.523 -23.060 1.00 26.09  ? 102 SER   B OG  1 
ATOM   3357 N  N   . LEU   B 1 106 ? -12.008 32.816 -27.358 1.00 27.44  ? 103 LEU   B N   1 
ATOM   3358 C  CA  . LEU   B 1 106 ? -11.601 33.691 -28.490 1.00 29.00  ? 103 LEU   B CA  1 
ATOM   3359 C  C   . LEU   B 1 106 ? -12.837 34.209 -29.221 1.00 30.72  ? 103 LEU   B C   1 
ATOM   3360 O  O   . LEU   B 1 106 ? -12.867 35.380 -29.537 1.00 30.24  ? 103 LEU   B O   1 
ATOM   3361 C  CB  . LEU   B 1 106 ? -10.668 32.914 -29.418 1.00 30.61  ? 103 LEU   B CB  1 
ATOM   3362 C  CG  . LEU   B 1 106 ? -9.300  32.584 -28.849 1.00 31.07  ? 103 LEU   B CG  1 
ATOM   3363 C  CD1 . LEU   B 1 106 ? -8.500  31.746 -29.825 1.00 33.03  ? 103 LEU   B CD1 1 
ATOM   3364 C  CD2 . LEU   B 1 106 ? -8.541  33.863 -28.477 1.00 30.61  ? 103 LEU   B CD2 1 
ATOM   3365 N  N   . LYS   B 1 107 ? -13.807 33.345 -29.514 1.00 32.14  ? 104 LYS   B N   1 
ATOM   3366 C  CA  . LYS   B 1 107 ? -15.081 33.760 -30.149 1.00 34.13  ? 104 LYS   B CA  1 
ATOM   3367 C  C   . LYS   B 1 107 ? -15.795 34.826 -29.299 1.00 32.66  ? 104 LYS   B C   1 
ATOM   3368 O  O   . LYS   B 1 107 ? -16.191 35.855 -29.879 1.00 31.23  ? 104 LYS   B O   1 
ATOM   3369 C  CB  . LYS   B 1 107 ? -15.953 32.535 -30.425 1.00 37.17  ? 104 LYS   B CB  1 
ATOM   3370 C  CG  . LYS   B 1 107 ? -17.166 32.855 -31.267 1.00 40.73  ? 104 LYS   B CG  1 
ATOM   3371 C  CD  . LYS   B 1 107 ? -18.172 31.739 -31.476 1.00 44.94  ? 104 LYS   B CD  1 
ATOM   3372 C  CE  . LYS   B 1 107 ? -19.540 32.388 -31.611 1.00 48.94  ? 104 LYS   B CE  1 
ATOM   3373 N  NZ  . LYS   B 1 107 ? -20.602 31.497 -32.132 1.00 54.12  ? 104 LYS   B NZ  1 
ATOM   3374 N  N   . LYS   B 1 108 ? -15.967 34.606 -27.985 1.00 31.52  ? 105 LYS   B N   1 
ATOM   3375 C  CA  . LYS   B 1 108 ? -16.693 35.557 -27.097 1.00 32.32  ? 105 LYS   B CA  1 
ATOM   3376 C  C   . LYS   B 1 108 ? -15.986 36.914 -27.070 1.00 29.54  ? 105 LYS   B C   1 
ATOM   3377 O  O   . LYS   B 1 108 ? -16.673 37.955 -27.212 1.00 29.09  ? 105 LYS   B O   1 
ATOM   3378 C  CB  . LYS   B 1 108 ? -16.694 35.148 -25.625 1.00 34.02  ? 105 LYS   B CB  1 
ATOM   3379 C  CG  . LYS   B 1 108 ? -17.339 33.827 -25.294 1.00 38.89  ? 105 LYS   B CG  1 
ATOM   3380 C  CD  . LYS   B 1 108 ? -18.709 33.697 -25.847 1.00 43.59  ? 105 LYS   B CD  1 
ATOM   3381 C  CE  . LYS   B 1 108 ? -19.654 34.666 -25.185 1.00 46.46  ? 105 LYS   B CE  1 
ATOM   3382 N  NZ  . LYS   B 1 108 ? -20.875 33.934 -24.788 1.00 47.91  ? 105 LYS   B NZ  1 
ATOM   3383 N  N   . ALA   B 1 109 ? -14.664 36.886 -26.911 1.00 27.41  ? 106 ALA   B N   1 
ATOM   3384 C  CA  . ALA   B 1 109 ? -13.834 38.090 -26.744 1.00 27.73  ? 106 ALA   B CA  1 
ATOM   3385 C  C   . ALA   B 1 109 ? -13.534 38.734 -28.105 1.00 28.86  ? 106 ALA   B C   1 
ATOM   3386 O  O   . ALA   B 1 109 ? -12.959 39.832 -28.107 1.00 28.80  ? 106 ALA   B O   1 
ATOM   3387 C  CB  . ALA   B 1 109 ? -12.555 37.754 -26.048 1.00 26.05  ? 106 ALA   B CB  1 
ATOM   3388 N  N   . GLN   B 1 110 ? -13.850 38.024 -29.189 1.00 30.54  ? 107 GLN   B N   1 
ATOM   3389 C  CA  . GLN   B 1 110 ? -13.496 38.395 -30.588 1.00 33.69  ? 107 GLN   B CA  1 
ATOM   3390 C  C   . GLN   B 1 110 ? -12.024 38.814 -30.662 1.00 32.90  ? 107 GLN   B C   1 
ATOM   3391 O  O   . GLN   B 1 110 ? -11.718 39.854 -31.271 1.00 33.69  ? 107 GLN   B O   1 
ATOM   3392 C  CB  . GLN   B 1 110 ? -14.479 39.431 -31.155 1.00 36.46  ? 107 GLN   B CB  1 
ATOM   3393 C  CG  . GLN   B 1 110 ? -15.745 38.761 -31.661 1.00 38.84  ? 107 GLN   B CG  1 
ATOM   3394 C  CD  . GLN   B 1 110 ? -15.467 37.754 -32.761 1.00 40.35  ? 107 GLN   B CD  1 
ATOM   3395 O  OE1 . GLN   B 1 110 ? -14.856 38.103 -33.783 1.00 42.92  ? 107 GLN   B OE1 1 
ATOM   3396 N  NE2 . GLN   B 1 110 ? -15.894 36.508 -32.559 1.00 37.30  ? 107 GLN   B NE2 1 
ATOM   3397 N  N   . LEU   B 1 111 ? -11.137 37.945 -30.174 1.00 31.78  ? 108 LEU   B N   1 
ATOM   3398 C  CA  . LEU   B 1 111 ? -9.673  38.061 -30.356 1.00 32.39  ? 108 LEU   B CA  1 
ATOM   3399 C  C   . LEU   B 1 111 ? -9.203  36.873 -31.186 1.00 33.54  ? 108 LEU   B C   1 
ATOM   3400 O  O   . LEU   B 1 111 ? -9.925  35.853 -31.199 1.00 33.46  ? 108 LEU   B O   1 
ATOM   3401 C  CB  . LEU   B 1 111 ? -9.042  38.101 -28.969 1.00 32.93  ? 108 LEU   B CB  1 
ATOM   3402 C  CG  . LEU   B 1 111 ? -9.490  39.280 -28.108 1.00 32.71  ? 108 LEU   B CG  1 
ATOM   3403 C  CD1 . LEU   B 1 111 ? -9.002  39.116 -26.680 1.00 32.65  ? 108 LEU   B CD1 1 
ATOM   3404 C  CD2 . LEU   B 1 111 ? -9.017  40.613 -28.674 1.00 34.15  ? 108 LEU   B CD2 1 
ATOM   3405 N  N   . ASP   B 1 112 ? -8.089  37.023 -31.901 1.00 34.65  ? 109 ASP   B N   1 
ATOM   3406 C  CA  . ASP   B 1 112 ? -7.497  35.932 -32.721 1.00 35.96  ? 109 ASP   B CA  1 
ATOM   3407 C  C   . ASP   B 1 112 ? -6.638  35.017 -31.851 1.00 33.41  ? 109 ASP   B C   1 
ATOM   3408 O  O   . ASP   B 1 112 ? -6.476  33.822 -32.197 1.00 34.46  ? 109 ASP   B O   1 
ATOM   3409 C  CB  . ASP   B 1 112 ? -6.672  36.526 -33.851 1.00 39.60  ? 109 ASP   B CB  1 
ATOM   3410 C  CG  . ASP   B 1 112 ? -7.543  37.350 -34.782 1.00 42.59  ? 109 ASP   B CG  1 
ATOM   3411 O  OD1 . ASP   B 1 112 ? -8.694  36.934 -35.019 1.00 44.20  ? 109 ASP   B OD1 1 
ATOM   3412 O  OD2 . ASP   B 1 112 ? -7.104  38.447 -35.181 1.00 44.86  ? 109 ASP   B OD2 1 
ATOM   3413 N  N   . TYR   B 1 113 ? -6.089  35.534 -30.758 1.00 31.21  ? 110 TYR   B N   1 
ATOM   3414 C  CA  . TYR   B 1 113 ? -5.259  34.732 -29.843 1.00 30.06  ? 110 TYR   B CA  1 
ATOM   3415 C  C   . TYR   B 1 113 ? -5.393  35.320 -28.441 1.00 28.52  ? 110 TYR   B C   1 
ATOM   3416 O  O   . TYR   B 1 113 ? -5.809  36.476 -28.336 1.00 28.21  ? 110 TYR   B O   1 
ATOM   3417 C  CB  . TYR   B 1 113 ? -3.811  34.732 -30.325 1.00 30.86  ? 110 TYR   B CB  1 
ATOM   3418 C  CG  . TYR   B 1 113 ? -3.166  36.091 -30.318 1.00 31.94  ? 110 TYR   B CG  1 
ATOM   3419 C  CD1 . TYR   B 1 113 ? -2.527  36.565 -29.179 1.00 30.93  ? 110 TYR   B CD1 1 
ATOM   3420 C  CD2 . TYR   B 1 113 ? -3.133  36.887 -31.463 1.00 33.86  ? 110 TYR   B CD2 1 
ATOM   3421 C  CE1 . TYR   B 1 113 ? -1.866  37.783 -29.174 1.00 32.27  ? 110 TYR   B CE1 1 
ATOM   3422 C  CE2 . TYR   B 1 113 ? -2.490  38.122 -31.459 1.00 34.52  ? 110 TYR   B CE2 1 
ATOM   3423 C  CZ  . TYR   B 1 113 ? -1.888  38.591 -30.296 1.00 33.70  ? 110 TYR   B CZ  1 
ATOM   3424 O  OH  . TYR   B 1 113 ? -1.286  39.821 -30.287 1.00 35.13  ? 110 TYR   B OH  1 
ATOM   3425 N  N   . VAL   B 1 114 ? -5.110  34.520 -27.416 1.00 27.21  ? 111 VAL   B N   1 
ATOM   3426 C  CA  . VAL   B 1 114 ? -4.835  35.106 -26.083 1.00 26.06  ? 111 VAL   B CA  1 
ATOM   3427 C  C   . VAL   B 1 114 ? -3.322  35.203 -25.908 1.00 26.72  ? 111 VAL   B C   1 
ATOM   3428 O  O   . VAL   B 1 114 ? -2.587  34.348 -26.383 1.00 27.47  ? 111 VAL   B O   1 
ATOM   3429 C  CB  . VAL   B 1 114 ? -5.505  34.318 -24.940 1.00 24.87  ? 111 VAL   B CB  1 
ATOM   3430 C  CG1 . VAL   B 1 114 ? -7.009  34.222 -25.109 1.00 24.46  ? 111 VAL   B CG1 1 
ATOM   3431 C  CG2 . VAL   B 1 114 ? -4.913  32.942 -24.762 1.00 24.83  ? 111 VAL   B CG2 1 
ATOM   3432 N  N   . ASP   B 1 115 ? -2.870  36.184 -25.139 1.00 26.25  ? 112 ASP   B N   1 
ATOM   3433 C  CA  . ASP   B 1 115 ? -1.431  36.258 -24.766 1.00 26.56  ? 112 ASP   B CA  1 
ATOM   3434 C  C   . ASP   B 1 115 ? -1.097  35.128 -23.792 1.00 25.53  ? 112 ASP   B C   1 
ATOM   3435 O  O   . ASP   B 1 115 ? 0.025   34.606 -23.808 1.00 25.90  ? 112 ASP   B O   1 
ATOM   3436 C  CB  . ASP   B 1 115 ? -1.123  37.658 -24.269 1.00 26.48  ? 112 ASP   B CB  1 
ATOM   3437 C  CG  . ASP   B 1 115 ? -1.369  38.670 -25.369 1.00 27.44  ? 112 ASP   B CG  1 
ATOM   3438 O  OD1 . ASP   B 1 115 ? -2.492  39.133 -25.493 1.00 26.63  ? 112 ASP   B OD1 1 
ATOM   3439 O  OD2 . ASP   B 1 115 ? -0.443  38.948 -26.117 1.00 29.18  ? 112 ASP   B OD2 1 
ATOM   3440 N  N   . LEU   B 1 116 ? -2.060  34.729 -22.979 1.00 24.29  ? 113 LEU   B N   1 
ATOM   3441 C  CA  . LEU   B 1 116 ? -1.803  33.749 -21.909 1.00 23.30  ? 113 LEU   B CA  1 
ATOM   3442 C  C   . LEU   B 1 116 ? -3.049  32.936 -21.677 1.00 22.73  ? 113 LEU   B C   1 
ATOM   3443 O  O   . LEU   B 1 116 ? -4.145  33.529 -21.556 1.00 22.38  ? 113 LEU   B O   1 
ATOM   3444 C  CB  . LEU   B 1 116 ? -1.448  34.495 -20.625 1.00 22.53  ? 113 LEU   B CB  1 
ATOM   3445 C  CG  . LEU   B 1 116 ? -1.049  33.610 -19.441 1.00 22.38  ? 113 LEU   B CG  1 
ATOM   3446 C  CD1 . LEU   B 1 116 ? 0.090   32.656 -19.787 1.00 23.15  ? 113 LEU   B CD1 1 
ATOM   3447 C  CD2 . LEU   B 1 116 ? -0.706  34.471 -18.242 1.00 21.87  ? 113 LEU   B CD2 1 
ATOM   3448 N  N   . TYR   B 1 117 ? -2.889  31.617 -21.650 1.00 23.30  ? 114 TYR   B N   1 
ATOM   3449 C  CA  . TYR   B 1 117 ? -4.000  30.719 -21.278 1.00 23.02  ? 114 TYR   B CA  1 
ATOM   3450 C  C   . TYR   B 1 117 ? -3.557  29.921 -20.057 1.00 23.46  ? 114 TYR   B C   1 
ATOM   3451 O  O   . TYR   B 1 117 ? -2.485  29.268 -20.154 1.00 24.27  ? 114 TYR   B O   1 
ATOM   3452 C  CB  . TYR   B 1 117 ? -4.419  29.817 -22.451 1.00 23.44  ? 114 TYR   B CB  1 
ATOM   3453 C  CG  . TYR   B 1 117 ? -5.834  29.288 -22.369 1.00 22.91  ? 114 TYR   B CG  1 
ATOM   3454 C  CD1 . TYR   B 1 117 ? -6.914  30.105 -22.088 1.00 22.41  ? 114 TYR   B CD1 1 
ATOM   3455 C  CD2 . TYR   B 1 117 ? -6.111  27.952 -22.642 1.00 23.59  ? 114 TYR   B CD2 1 
ATOM   3456 C  CE1 . TYR   B 1 117 ? -8.214  29.615 -22.034 1.00 22.32  ? 114 TYR   B CE1 1 
ATOM   3457 C  CE2 . TYR   B 1 117 ? -7.406  27.441 -22.609 1.00 23.45  ? 114 TYR   B CE2 1 
ATOM   3458 C  CZ  . TYR   B 1 117 ? -8.474  28.279 -22.346 1.00 23.43  ? 114 TYR   B CZ  1 
ATOM   3459 O  OH  . TYR   B 1 117 ? -9.768  27.792 -22.335 1.00 23.80  ? 114 TYR   B OH  1 
ATOM   3460 N  N   . LEU   B 1 118 ? -4.375  29.931 -18.988 1.00 22.56  ? 115 LEU   B N   1 
ATOM   3461 C  CA  . LEU   B 1 118 ? -4.087  29.177 -17.747 1.00 22.32  ? 115 LEU   B CA  1 
ATOM   3462 C  C   . LEU   B 1 118 ? -5.040  28.011 -17.547 1.00 22.48  ? 115 LEU   B C   1 
ATOM   3463 O  O   . LEU   B 1 118 ? -6.217  28.182 -17.867 1.00 22.20  ? 115 LEU   B O   1 
ATOM   3464 C  CB  . LEU   B 1 118 ? -4.242  30.139 -16.578 1.00 21.48  ? 115 LEU   B CB  1 
ATOM   3465 C  CG  . LEU   B 1 118 ? -3.443  31.431 -16.689 1.00 21.10  ? 115 LEU   B CG  1 
ATOM   3466 C  CD1 . LEU   B 1 118 ? -3.542  32.217 -15.390 1.00 21.00  ? 115 LEU   B CD1 1 
ATOM   3467 C  CD2 . LEU   B 1 118 ? -1.975  31.189 -17.022 1.00 21.69  ? 115 LEU   B CD2 1 
ATOM   3468 N  N   . ILE   B 1 119 ? -4.548  26.900 -16.988 1.00 23.00  ? 116 ILE   B N   1 
ATOM   3469 C  CA  . ILE   B 1 119 ? -5.407  25.986 -16.201 1.00 23.48  ? 116 ILE   B CA  1 
ATOM   3470 C  C   . ILE   B 1 119 ? -5.883  26.821 -15.012 1.00 22.64  ? 116 ILE   B C   1 
ATOM   3471 O  O   . ILE   B 1 119 ? -5.045  27.183 -14.165 1.00 22.59  ? 116 ILE   B O   1 
ATOM   3472 C  CB  . ILE   B 1 119 ? -4.687  24.684 -15.801 1.00 24.37  ? 116 ILE   B CB  1 
ATOM   3473 C  CG1 . ILE   B 1 119 ? -4.134  23.943 -17.026 1.00 26.10  ? 116 ILE   B CG1 1 
ATOM   3474 C  CG2 . ILE   B 1 119 ? -5.644  23.845 -14.993 1.00 24.72  ? 116 ILE   B CG2 1 
ATOM   3475 C  CD1 . ILE   B 1 119 ? -3.451  22.585 -16.739 1.00 27.06  ? 116 ILE   B CD1 1 
ATOM   3476 N  N   . HIS   B 1 120 ? -7.183  27.086 -14.916 1.00 22.24  ? 117 HIS   B N   1 
ATOM   3477 C  CA  . HIS   B 1 120 ? -7.762  27.974 -13.871 1.00 21.61  ? 117 HIS   B CA  1 
ATOM   3478 C  C   . HIS   B 1 120 ? -7.502  27.396 -12.478 1.00 22.25  ? 117 HIS   B C   1 
ATOM   3479 O  O   . HIS   B 1 120 ? -7.254  28.145 -11.522 1.00 21.25  ? 117 HIS   B O   1 
ATOM   3480 C  CB  . HIS   B 1 120 ? -9.269  28.202 -14.071 1.00 21.94  ? 117 HIS   B CB  1 
ATOM   3481 C  CG  . HIS   B 1 120 ? -9.759  29.490 -13.484 1.00 21.52  ? 117 HIS   B CG  1 
ATOM   3482 N  ND1 . HIS   B 1 120 ? -10.815 30.201 -14.015 1.00 21.33  ? 117 HIS   B ND1 1 
ATOM   3483 C  CD2 . HIS   B 1 120 ? -9.338  30.187 -12.407 1.00 21.19  ? 117 HIS   B CD2 1 
ATOM   3484 C  CE1 . HIS   B 1 120 ? -11.030 31.286 -13.292 1.00 21.21  ? 117 HIS   B CE1 1 
ATOM   3485 N  NE2 . HIS   B 1 120 ? -10.114 31.324 -12.321 1.00 21.64  ? 117 HIS   B NE2 1 
ATOM   3486 N  N   . SER   B 1 121 ? -7.602  26.077 -12.353 1.00 23.02  ? 118 SER   B N   1 
ATOM   3487 C  CA  . SER   B 1 121 ? -7.539  25.400 -11.043 1.00 23.94  ? 118 SER   B CA  1 
ATOM   3488 C  C   . SER   B 1 121 ? -7.191  23.942 -11.276 1.00 24.95  ? 118 SER   B C   1 
ATOM   3489 O  O   . SER   B 1 121 ? -7.568  23.399 -12.298 1.00 25.04  ? 118 SER   B O   1 
ATOM   3490 C  CB  . SER   B 1 121 ? -8.851  25.544 -10.341 1.00 24.63  ? 118 SER   B CB  1 
ATOM   3491 O  OG  . SER   B 1 121 ? -8.998  24.534 -9.377  1.00 25.52  ? 118 SER   B OG  1 
ATOM   3492 N  N   . PRO   B 1 122 ? -6.423  23.296 -10.383 1.00 25.54  ? 119 PRO   B N   1 
ATOM   3493 C  CA  . PRO   B 1 122 ? -6.153  21.876 -10.557 1.00 26.95  ? 119 PRO   B CA  1 
ATOM   3494 C  C   . PRO   B 1 122 ? -7.330  20.970 -10.170 1.00 28.53  ? 119 PRO   B C   1 
ATOM   3495 O  O   . PRO   B 1 122 ? -7.228  19.747 -10.411 1.00 30.40  ? 119 PRO   B O   1 
ATOM   3496 C  CB  . PRO   B 1 122 ? -4.936  21.683 -9.631  1.00 27.15  ? 119 PRO   B CB  1 
ATOM   3497 C  CG  . PRO   B 1 122 ? -5.116  22.697 -8.513  1.00 26.25  ? 119 PRO   B CG  1 
ATOM   3498 C  CD  . PRO   B 1 122 ? -5.757  23.885 -9.192  1.00 25.44  ? 119 PRO   B CD  1 
ATOM   3499 N  N   . MET   B 1 123 ? -8.414  21.544 -9.630  1.00 27.96  ? 120 MET   B N   1 
ATOM   3500 C  CA  . MET   B 1 123 ? -9.529  20.740 -9.030  1.00 29.79  ? 120 MET   B CA  1 
ATOM   3501 C  C   . MET   B 1 123 ? -10.562 20.414 -10.105 1.00 29.97  ? 120 MET   B C   1 
ATOM   3502 O  O   . MET   B 1 123 ? -11.505 21.173 -10.265 1.00 29.27  ? 120 MET   B O   1 
ATOM   3503 C  CB  . MET   B 1 123 ? -10.133 21.521 -7.870  1.00 30.63  ? 120 MET   B CB  1 
ATOM   3504 C  CG  . MET   B 1 123 ? -9.164  21.591 -6.742  1.00 31.21  ? 120 MET   B CG  1 
ATOM   3505 S  SD  . MET   B 1 123 ? -9.782  22.503 -5.301  1.00 32.89  ? 120 MET   B SD  1 
ATOM   3506 C  CE  . MET   B 1 123 ? -9.857  24.173 -5.946  1.00 31.51  ? 120 MET   B CE  1 
ATOM   3507 N  N   . SER   B 1 124 ? -10.309 19.375 -10.899 1.00 30.63  ? 121 SER   B N   1 
ATOM   3508 C  CA  . SER   B 1 124 ? -11.153 18.945 -12.043 1.00 32.12  ? 121 SER   B CA  1 
ATOM   3509 C  C   . SER   B 1 124 ? -12.616 18.778 -11.598 1.00 33.79  ? 121 SER   B C   1 
ATOM   3510 O  O   . SER   B 1 124 ? -12.841 18.221 -10.486 1.00 34.89  ? 121 SER   B O   1 
ATOM   3511 C  CB  . SER   B 1 124 ? -10.611 17.668 -12.599 1.00 33.17  ? 121 SER   B CB  1 
ATOM   3512 O  OG  . SER   B 1 124 ? -9.240  17.840 -12.900 1.00 32.67  ? 121 SER   B OG  1 
ATOM   3513 N  N   . LEU   B 1 125 ? -13.564 19.215 -12.425 1.00 33.63  ? 122 LEU   B N   1 
ATOM   3514 C  CA  . LEU   B 1 125 ? -15.009 19.071 -12.140 1.00 35.76  ? 122 LEU   B CA  1 
ATOM   3515 C  C   . LEU   B 1 125 ? -15.651 18.319 -13.305 1.00 38.53  ? 122 LEU   B C   1 
ATOM   3516 O  O   . LEU   B 1 125 ? -15.061 18.260 -14.414 1.00 38.89  ? 122 LEU   B O   1 
ATOM   3517 C  CB  . LEU   B 1 125 ? -15.681 20.434 -11.936 1.00 34.61  ? 122 LEU   B CB  1 
ATOM   3518 C  CG  . LEU   B 1 125 ? -15.063 21.324 -10.864 1.00 33.66  ? 122 LEU   B CG  1 
ATOM   3519 C  CD1 . LEU   B 1 125 ? -15.820 22.629 -10.741 1.00 32.92  ? 122 LEU   B CD1 1 
ATOM   3520 C  CD2 . LEU   B 1 125 ? -15.006 20.610 -9.520  1.00 35.14  ? 122 LEU   B CD2 1 
ATOM   3521 N  N   . LYS   B 1 126 ? -16.772 17.691 -12.994 1.00 41.15  ? 123 LYS   B N   1 
ATOM   3522 C  CA  . LYS   B 1 126 ? -17.533 16.857 -13.932 1.00 44.14  ? 123 LYS   B CA  1 
ATOM   3523 C  C   . LYS   B 1 126 ? -17.716 17.639 -15.220 1.00 43.43  ? 123 LYS   B C   1 
ATOM   3524 O  O   . LYS   B 1 126 ? -18.168 18.773 -15.171 1.00 40.21  ? 123 LYS   B O   1 
ATOM   3525 C  CB  . LYS   B 1 126 ? -18.873 16.514 -13.288 1.00 47.44  ? 123 LYS   B CB  1 
ATOM   3526 C  CG  . LYS   B 1 126 ? -19.789 15.686 -14.173 1.00 51.30  ? 123 LYS   B CG  1 
ATOM   3527 C  CD  . LYS   B 1 126 ? -21.227 16.105 -14.020 1.00 53.82  ? 123 LYS   B CD  1 
ATOM   3528 C  CE  . LYS   B 1 126 ? -22.055 15.748 -15.238 1.00 56.78  ? 123 LYS   B CE  1 
ATOM   3529 N  NZ  . LYS   B 1 126 ? -22.722 14.451 -15.009 1.00 59.76  ? 123 LYS   B NZ  1 
ATOM   3530 N  N   . PRO   B 1 127 ? -17.411 17.019 -16.380 1.00 45.32  ? 124 PRO   B N   1 
ATOM   3531 C  CA  . PRO   B 1 127 ? -17.620 17.652 -17.675 1.00 47.03  ? 124 PRO   B CA  1 
ATOM   3532 C  C   . PRO   B 1 127 ? -19.121 17.672 -17.954 1.00 51.33  ? 124 PRO   B C   1 
ATOM   3533 O  O   . PRO   B 1 127 ? -19.800 16.770 -17.508 1.00 52.56  ? 124 PRO   B O   1 
ATOM   3534 C  CB  . PRO   B 1 127 ? -16.891 16.784 -18.702 1.00 47.41  ? 124 PRO   B CB  1 
ATOM   3535 C  CG  . PRO   B 1 127 ? -16.191 15.697 -17.894 1.00 48.39  ? 124 PRO   B CG  1 
ATOM   3536 C  CD  . PRO   B 1 127 ? -16.794 15.691 -16.498 1.00 47.46  ? 124 PRO   B CD  1 
ATOM   3537 N  N   . GLY   B 1 128 ? -19.593 18.699 -18.654 1.00 47.25  ? 125 GLY   B N   1 
ATOM   3538 C  CA  . GLY   B 1 128 ? -21.038 18.941 -18.827 1.00 54.25  ? 125 GLY   B CA  1 
ATOM   3539 C  C   . GLY   B 1 128 ? -21.362 20.411 -18.963 1.00 57.64  ? 125 GLY   B C   1 
ATOM   3540 O  O   . GLY   B 1 128 ? -20.411 21.232 -19.122 1.00 58.42  ? 125 GLY   B O   1 
ATOM   3541 N  N   . GLU   B 1 129 ? -22.652 20.740 -18.895 1.00 63.44  ? 126 GLU   B N   1 
ATOM   3542 C  CA  . GLU   B 1 129 ? -23.128 22.103 -19.235 1.00 67.79  ? 126 GLU   B CA  1 
ATOM   3543 C  C   . GLU   B 1 129 ? -22.799 23.045 -18.065 1.00 63.80  ? 126 GLU   B C   1 
ATOM   3544 O  O   . GLU   B 1 129 ? -22.241 24.128 -18.343 1.00 65.19  ? 126 GLU   B O   1 
ATOM   3545 C  CB  . GLU   B 1 129 ? -24.603 22.084 -19.655 1.00 75.43  ? 126 GLU   B CB  1 
ATOM   3546 C  CG  . GLU   B 1 129 ? -25.056 23.349 -20.383 1.00 80.41  ? 126 GLU   B CG  1 
ATOM   3547 C  CD  . GLU   B 1 129 ? -24.059 24.029 -21.323 1.00 82.67  ? 126 GLU   B CD  1 
ATOM   3548 O  OE1 . GLU   B 1 129 ? -24.157 23.817 -22.558 1.00 83.62  ? 126 GLU   B OE1 1 
ATOM   3549 O  OE2 . GLU   B 1 129 ? -23.205 24.808 -20.827 1.00 82.92  ? 126 GLU   B OE2 1 
ATOM   3550 N  N   . GLU   B 1 130 ? -23.075 22.642 -16.815 1.00 59.76  ? 127 GLU   B N   1 
ATOM   3551 C  CA  . GLU   B 1 130 ? -22.923 23.523 -15.620 1.00 57.21  ? 127 GLU   B CA  1 
ATOM   3552 C  C   . GLU   B 1 130 ? -21.424 23.710 -15.293 1.00 52.77  ? 127 GLU   B C   1 
ATOM   3553 O  O   . GLU   B 1 130 ? -20.668 22.686 -15.206 1.00 48.36  ? 127 GLU   B O   1 
ATOM   3554 C  CB  . GLU   B 1 130 ? -23.692 22.984 -14.404 1.00 59.76  ? 127 GLU   B CB  1 
ATOM   3555 C  CG  . GLU   B 1 130 ? -25.208 22.901 -14.568 1.00 64.48  ? 127 GLU   B CG  1 
ATOM   3556 C  CD  . GLU   B 1 130 ? -25.955 24.210 -14.835 1.00 69.41  ? 127 GLU   B CD  1 
ATOM   3557 O  OE1 . GLU   B 1 130 ? -27.049 24.157 -15.449 1.00 69.01  ? 127 GLU   B OE1 1 
ATOM   3558 O  OE2 . GLU   B 1 130 ? -25.452 25.289 -14.431 1.00 70.71  ? 127 GLU   B OE2 1 
ATOM   3559 N  N   . LEU   B 1 131 ? -21.001 24.969 -15.094 1.00 48.41  ? 128 LEU   B N   1 
ATOM   3560 C  CA  . LEU   B 1 131 ? -19.636 25.320 -14.601 1.00 45.05  ? 128 LEU   B CA  1 
ATOM   3561 C  C   . LEU   B 1 131 ? -19.495 24.871 -13.144 1.00 42.77  ? 128 LEU   B C   1 
ATOM   3562 O  O   . LEU   B 1 131 ? -18.373 24.542 -12.774 1.00 37.73  ? 128 LEU   B O   1 
ATOM   3563 C  CB  . LEU   B 1 131 ? -19.336 26.821 -14.740 1.00 44.90  ? 128 LEU   B CB  1 
ATOM   3564 C  CG  . LEU   B 1 131 ? -19.390 27.371 -16.167 1.00 45.40  ? 128 LEU   B CG  1 
ATOM   3565 C  CD1 . LEU   B 1 131 ? -19.033 28.843 -16.210 1.00 46.54  ? 128 LEU   B CD1 1 
ATOM   3566 C  CD2 . LEU   B 1 131 ? -18.496 26.593 -17.125 1.00 44.16  ? 128 LEU   B CD2 1 
ATOM   3567 N  N   . SER   B 1 132 ? -20.570 24.881 -12.358 1.00 46.62  ? 129 SER   B N   1 
ATOM   3568 C  CA  . SER   B 1 132 ? -20.599 24.299 -10.982 1.00 49.42  ? 129 SER   B CA  1 
ATOM   3569 C  C   . SER   B 1 132 ? -21.589 23.143 -10.986 1.00 50.48  ? 129 SER   B C   1 
ATOM   3570 O  O   . SER   B 1 132 ? -22.745 23.331 -10.621 1.00 53.56  ? 129 SER   B O   1 
ATOM   3571 C  CB  . SER   B 1 132 ? -20.961 25.303 -9.903  1.00 53.42  ? 129 SER   B CB  1 
ATOM   3572 O  OG  . SER   B 1 132 ? -20.133 26.459 -9.964  1.00 55.40  ? 129 SER   B OG  1 
ATOM   3573 N  N   . PRO   B 1 133 ? -21.177 21.931 -11.424 1.00 48.06  ? 130 PRO   B N   1 
ATOM   3574 C  CA  . PRO   B 1 133 ? -22.093 20.795 -11.498 1.00 48.74  ? 130 PRO   B CA  1 
ATOM   3575 C  C   . PRO   B 1 133 ? -22.338 20.338 -10.057 1.00 49.18  ? 130 PRO   B C   1 
ATOM   3576 O  O   . PRO   B 1 133 ? -21.369 20.139 -9.343  1.00 47.38  ? 130 PRO   B O   1 
ATOM   3577 C  CB  . PRO   B 1 133 ? -21.334 19.745 -12.322 1.00 48.09  ? 130 PRO   B CB  1 
ATOM   3578 C  CG  . PRO   B 1 133 ? -19.864 20.069 -12.060 1.00 46.11  ? 130 PRO   B CG  1 
ATOM   3579 C  CD  . PRO   B 1 133 ? -19.807 21.567 -11.817 1.00 45.65  ? 130 PRO   B CD  1 
ATOM   3580 N  N   . THR   B 1 134 ? -23.604 20.240 -9.663  1.00 50.34  ? 131 THR   B N   1 
ATOM   3581 C  CA  . THR   B 1 134 ? -24.018 19.928 -8.274  1.00 52.09  ? 131 THR   B CA  1 
ATOM   3582 C  C   . THR   B 1 134 ? -25.013 18.766 -8.292  1.00 54.74  ? 131 THR   B C   1 
ATOM   3583 O  O   . THR   B 1 134 ? -25.842 18.712 -9.186  1.00 55.44  ? 131 THR   B O   1 
ATOM   3584 C  CB  . THR   B 1 134 ? -24.538 21.185 -7.569  1.00 53.82  ? 131 THR   B CB  1 
ATOM   3585 O  OG1 . THR   B 1 134 ? -25.745 21.602 -8.213  1.00 55.77  ? 131 THR   B OG1 1 
ATOM   3586 C  CG2 . THR   B 1 134 ? -23.501 22.290 -7.577  1.00 52.74  ? 131 THR   B CG2 1 
ATOM   3587 N  N   . ASP   B 1 135 ? -24.880 17.851 -7.335  1.00 56.99  ? 132 ASP   B N   1 
ATOM   3588 C  CA  . ASP   B 1 135 ? -25.809 16.714 -7.096  1.00 61.53  ? 132 ASP   B CA  1 
ATOM   3589 C  C   . ASP   B 1 135 ? -27.097 17.246 -6.439  1.00 63.66  ? 132 ASP   B C   1 
ATOM   3590 O  O   . ASP   B 1 135 ? -27.233 18.466 -6.257  1.00 60.83  ? 132 ASP   B O   1 
ATOM   3591 C  CB  . ASP   B 1 135 ? -25.108 15.617 -6.281  1.00 62.54  ? 132 ASP   B CB  1 
ATOM   3592 C  CG  . ASP   B 1 135 ? -24.809 15.967 -4.829  1.00 63.71  ? 132 ASP   B CG  1 
ATOM   3593 O  OD1 . ASP   B 1 135 ? -25.384 16.953 -4.300  1.00 64.19  ? 132 ASP   B OD1 1 
ATOM   3594 O  OD2 . ASP   B 1 135 ? -24.010 15.239 -4.219  1.00 66.75  ? 132 ASP   B OD2 1 
ATOM   3595 N  N   . GLU   B 1 136 ? -27.982 16.335 -6.039  1.00 70.20  ? 133 GLU   B N   1 
ATOM   3596 C  CA  . GLU   B 1 136 ? -29.242 16.592 -5.280  1.00 75.28  ? 133 GLU   B CA  1 
ATOM   3597 C  C   . GLU   B 1 136 ? -29.008 17.460 -4.027  1.00 74.02  ? 133 GLU   B C   1 
ATOM   3598 O  O   . GLU   B 1 136 ? -29.959 18.174 -3.619  1.00 75.34  ? 133 GLU   B O   1 
ATOM   3599 C  CB  . GLU   B 1 136 ? -29.864 15.253 -4.862  1.00 83.08  ? 133 GLU   B CB  1 
ATOM   3600 C  CG  . GLU   B 1 136 ? -29.796 14.168 -5.935  1.00 88.10  ? 133 GLU   B CG  1 
ATOM   3601 C  CD  . GLU   B 1 136 ? -28.544 13.298 -5.951  1.00 90.33  ? 133 GLU   B CD  1 
ATOM   3602 O  OE1 . GLU   B 1 136 ? -28.508 12.277 -5.210  1.00 95.13  ? 133 GLU   B OE1 1 
ATOM   3603 O  OE2 . GLU   B 1 136 ? -27.608 13.644 -6.712  1.00 89.36  ? 133 GLU   B OE2 1 
ATOM   3604 N  N   . ASN   B 1 137 ? -27.821 17.398 -3.412  1.00 71.28  ? 134 ASN   B N   1 
ATOM   3605 C  CA  . ASN   B 1 137 ? -27.563 18.056 -2.098  1.00 71.54  ? 134 ASN   B CA  1 
ATOM   3606 C  C   . ASN   B 1 137 ? -26.753 19.338 -2.298  1.00 67.22  ? 134 ASN   B C   1 
ATOM   3607 O  O   . ASN   B 1 137 ? -26.248 19.870 -1.313  1.00 68.56  ? 134 ASN   B O   1 
ATOM   3608 C  CB  . ASN   B 1 137 ? -26.919 17.075 -1.127  1.00 73.36  ? 134 ASN   B CB  1 
ATOM   3609 C  CG  . ASN   B 1 137 ? -27.801 15.858 -0.961  1.00 77.75  ? 134 ASN   B CG  1 
ATOM   3610 O  OD1 . ASN   B 1 137 ? -27.428 14.767 -1.386  1.00 80.30  ? 134 ASN   B OD1 1 
ATOM   3611 N  ND2 . ASN   B 1 137 ? -28.986 16.050 -0.398  1.00 78.97  ? 134 ASN   B ND2 1 
ATOM   3612 N  N   . GLY   B 1 138 ? -26.677 19.818 -3.533  1.00 63.48  ? 135 GLY   B N   1 
ATOM   3613 C  CA  . GLY   B 1 138 ? -25.864 20.984 -3.912  1.00 60.81  ? 135 GLY   B CA  1 
ATOM   3614 C  C   . GLY   B 1 138 ? -24.383 20.722 -3.684  1.00 57.59  ? 135 GLY   B C   1 
ATOM   3615 O  O   . GLY   B 1 138 ? -23.611 21.719 -3.626  1.00 53.96  ? 135 GLY   B O   1 
ATOM   3616 N  N   . LYS   B 1 139 ? -23.992 19.447 -3.563  1.00 57.86  ? 136 LYS   B N   1 
ATOM   3617 C  CA  . LYS   B 1 139 ? -22.563 19.056 -3.528  1.00 56.64  ? 136 LYS   B CA  1 
ATOM   3618 C  C   . LYS   B 1 139 ? -22.035 19.104 -4.967  1.00 52.12  ? 136 LYS   B C   1 
ATOM   3619 O  O   . LYS   B 1 139 ? -22.602 18.448 -5.846  1.00 49.48  ? 136 LYS   B O   1 
ATOM   3620 C  CB  . LYS   B 1 139 ? -22.377 17.712 -2.821  1.00 61.36  ? 136 LYS   B CB  1 
ATOM   3621 C  CG  . LYS   B 1 139 ? -22.769 17.743 -1.347  1.00 67.13  ? 136 LYS   B CG  1 
ATOM   3622 C  CD  . LYS   B 1 139 ? -22.182 18.958 -0.614  1.00 68.23  ? 136 LYS   B CD  1 
ATOM   3623 C  CE  . LYS   B 1 139 ? -22.462 19.015 0.874   1.00 73.25  ? 136 LYS   B CE  1 
ATOM   3624 N  NZ  . LYS   B 1 139 ? -23.668 19.827 1.167   1.00 74.58  ? 136 LYS   B NZ  1 
ATOM   3625 N  N   . VAL   B 1 140 ? -20.983 19.901 -5.144  1.00 49.44  ? 137 VAL   B N   1 
ATOM   3626 C  CA  . VAL   B 1 140 ? -20.169 20.045 -6.388  1.00 46.93  ? 137 VAL   B CA  1 
ATOM   3627 C  C   . VAL   B 1 140 ? -19.585 18.678 -6.758  1.00 45.05  ? 137 VAL   B C   1 
ATOM   3628 O  O   . VAL   B 1 140 ? -19.021 18.029 -5.880  1.00 44.41  ? 137 VAL   B O   1 
ATOM   3629 C  CB  . VAL   B 1 140 ? -19.053 21.084 -6.189  1.00 47.50  ? 137 VAL   B CB  1 
ATOM   3630 C  CG1 . VAL   B 1 140 ? -18.163 21.191 -7.426  1.00 46.72  ? 137 VAL   B CG1 1 
ATOM   3631 C  CG2 . VAL   B 1 140 ? -19.635 22.442 -5.807  1.00 49.38  ? 137 VAL   B CG2 1 
ATOM   3632 N  N   . ILE   B 1 141 ? -19.706 18.285 -8.030  1.00 42.60  ? 138 ILE   B N   1 
ATOM   3633 C  CA  . ILE   B 1 141 ? -19.268 16.958 -8.529  1.00 43.30  ? 138 ILE   B CA  1 
ATOM   3634 C  C   . ILE   B 1 141 ? -17.882 17.108 -9.149  1.00 40.27  ? 138 ILE   B C   1 
ATOM   3635 O  O   . ILE   B 1 141 ? -17.688 17.922 -10.126 1.00 39.21  ? 138 ILE   B O   1 
ATOM   3636 C  CB  . ILE   B 1 141 ? -20.285 16.370 -9.517  1.00 45.92  ? 138 ILE   B CB  1 
ATOM   3637 C  CG1 . ILE   B 1 141 ? -21.676 16.267 -8.890  1.00 49.14  ? 138 ILE   B CG1 1 
ATOM   3638 C  CG2 . ILE   B 1 141 ? -19.815 15.012 -10.017 1.00 48.17  ? 138 ILE   B CG2 1 
ATOM   3639 C  CD1 . ILE   B 1 141 ? -22.766 16.160 -9.942  1.00 51.13  ? 138 ILE   B CD1 1 
ATOM   3640 N  N   . PHE   B 1 142 ? -16.946 16.370 -8.585  1.00 39.83  ? 139 PHE   B N   1 
ATOM   3641 C  CA  . PHE   B 1 142 ? -15.531 16.383 -8.995  1.00 38.19  ? 139 PHE   B CA  1 
ATOM   3642 C  C   . PHE   B 1 142 ? -15.382 15.471 -10.206 1.00 39.00  ? 139 PHE   B C   1 
ATOM   3643 O  O   . PHE   B 1 142 ? -16.313 14.684 -10.491 1.00 40.96  ? 139 PHE   B O   1 
ATOM   3644 C  CB  . PHE   B 1 142 ? -14.656 15.877 -7.853  1.00 39.99  ? 139 PHE   B CB  1 
ATOM   3645 C  CG  . PHE   B 1 142 ? -14.764 16.637 -6.558  1.00 40.08  ? 139 PHE   B CG  1 
ATOM   3646 C  CD1 . PHE   B 1 142 ? -15.370 17.882 -6.488  1.00 38.96  ? 139 PHE   B CD1 1 
ATOM   3647 C  CD2 . PHE   B 1 142 ? -14.178 16.130 -5.415  1.00 42.27  ? 139 PHE   B CD2 1 
ATOM   3648 C  CE1 . PHE   B 1 142 ? -15.437 18.572 -5.287  1.00 39.99  ? 139 PHE   B CE1 1 
ATOM   3649 C  CE2 . PHE   B 1 142 ? -14.233 16.829 -4.223  1.00 43.53  ? 139 PHE   B CE2 1 
ATOM   3650 C  CZ  . PHE   B 1 142 ? -14.856 18.051 -4.162  1.00 42.16  ? 139 PHE   B CZ  1 
ATOM   3651 N  N   . ASP   B 1 143 ? -14.220 15.554 -10.831 1.00 37.54  ? 140 ASP   B N   1 
ATOM   3652 C  CA  . ASP   B 1 143 ? -13.769 14.640 -11.908 1.00 38.60  ? 140 ASP   B CA  1 
ATOM   3653 C  C   . ASP   B 1 143 ? -12.333 14.239 -11.599 1.00 38.36  ? 140 ASP   B C   1 
ATOM   3654 O  O   . ASP   B 1 143 ? -11.602 15.007 -10.913 1.00 37.07  ? 140 ASP   B O   1 
ATOM   3655 C  CB  . ASP   B 1 143 ? -13.910 15.320 -13.276 1.00 37.75  ? 140 ASP   B CB  1 
ATOM   3656 C  CG  . ASP   B 1 143 ? -13.778 14.409 -14.490 1.00 39.97  ? 140 ASP   B CG  1 
ATOM   3657 O  OD1 . ASP   B 1 143 ? -13.945 13.171 -14.320 1.00 44.10  ? 140 ASP   B OD1 1 
ATOM   3658 O  OD2 . ASP   B 1 143 ? -13.510 14.951 -15.604 1.00 37.20  ? 140 ASP   B OD2 1 
ATOM   3659 N  N   . ILE   B 1 144 ? -11.903 13.103 -12.114 1.00 40.89  ? 141 ILE   B N   1 
ATOM   3660 C  CA  . ILE   B 1 144 ? -10.512 12.625 -11.908 1.00 42.32  ? 141 ILE   B CA  1 
ATOM   3661 C  C   . ILE   B 1 144 ? -9.846  12.734 -13.275 1.00 40.95  ? 141 ILE   B C   1 
ATOM   3662 O  O   . ILE   B 1 144 ? -10.262 12.026 -14.212 1.00 40.53  ? 141 ILE   B O   1 
ATOM   3663 C  CB  . ILE   B 1 144 ? -10.479 11.193 -11.327 1.00 48.01  ? 141 ILE   B CB  1 
ATOM   3664 C  CG1 . ILE   B 1 144 ? -11.163 11.086 -9.955  1.00 50.04  ? 141 ILE   B CG1 1 
ATOM   3665 C  CG2 . ILE   B 1 144 ? -9.038  10.714 -11.277 1.00 50.06  ? 141 ILE   B CG2 1 
ATOM   3666 C  CD1 . ILE   B 1 144 ? -12.083 9.887  -9.796  1.00 54.94  ? 141 ILE   B CD1 1 
ATOM   3667 N  N   . VAL   B 1 145 ? -8.889  13.634 -13.412 1.00 38.98  ? 142 VAL   B N   1 
ATOM   3668 C  CA  . VAL   B 1 145 ? -8.179  13.841 -14.703 1.00 38.95  ? 142 VAL   B CA  1 
ATOM   3669 C  C   . VAL   B 1 145 ? -6.691  13.961 -14.393 1.00 38.76  ? 142 VAL   B C   1 
ATOM   3670 O  O   . VAL   B 1 145 ? -6.326  14.762 -13.528 1.00 36.39  ? 142 VAL   B O   1 
ATOM   3671 C  CB  . VAL   B 1 145 ? -8.684  15.075 -15.472 1.00 36.39  ? 142 VAL   B CB  1 
ATOM   3672 C  CG1 . VAL   B 1 145 ? -7.941  15.236 -16.803 1.00 36.77  ? 142 VAL   B CG1 1 
ATOM   3673 C  CG2 . VAL   B 1 145 ? -10.200 15.018 -15.685 1.00 37.07  ? 142 VAL   B CG2 1 
ATOM   3674 N  N   . ASP   B 1 146 ? -5.880  13.181 -15.079 1.00 40.70  ? 143 ASP   B N   1 
ATOM   3675 C  CA  . ASP   B 1 146 ? -4.414  13.390 -15.102 1.00 41.28  ? 143 ASP   B CA  1 
ATOM   3676 C  C   . ASP   B 1 146 ? -4.131  14.779 -15.696 1.00 36.81  ? 143 ASP   B C   1 
ATOM   3677 O  O   . ASP   B 1 146 ? -4.387  15.010 -16.903 1.00 34.56  ? 143 ASP   B O   1 
ATOM   3678 C  CB  . ASP   B 1 146 ? -3.750  12.286 -15.903 1.00 46.29  ? 143 ASP   B CB  1 
ATOM   3679 C  CG  . ASP   B 1 146 ? -2.247  12.457 -16.014 1.00 48.54  ? 143 ASP   B CG  1 
ATOM   3680 O  OD1 . ASP   B 1 146 ? -1.700  13.354 -15.332 1.00 46.24  ? 143 ASP   B OD1 1 
ATOM   3681 O  OD2 . ASP   B 1 146 ? -1.638  11.662 -16.764 1.00 54.25  ? 143 ASP   B OD2 1 
ATOM   3682 N  N   . LEU   B 1 147 ? -3.635  15.702 -14.897 1.00 35.40  ? 144 LEU   B N   1 
ATOM   3683 C  CA  . LEU   B 1 147 ? -3.489  17.112 -15.383 1.00 32.69  ? 144 LEU   B CA  1 
ATOM   3684 C  C   . LEU   B 1 147 ? -2.320  17.223 -16.364 1.00 32.65  ? 144 LEU   B C   1 
ATOM   3685 O  O   . LEU   B 1 147 ? -2.230  18.245 -17.027 1.00 28.60  ? 144 LEU   B O   1 
ATOM   3686 C  CB  . LEU   B 1 147 ? -3.301  18.089 -14.220 1.00 31.88  ? 144 LEU   B CB  1 
ATOM   3687 C  CG  . LEU   B 1 147 ? -4.490  18.268 -13.289 1.00 31.78  ? 144 LEU   B CG  1 
ATOM   3688 C  CD1 . LEU   B 1 147 ? -4.122  19.247 -12.199 1.00 31.62  ? 144 LEU   B CD1 1 
ATOM   3689 C  CD2 . LEU   B 1 147 ? -5.743  18.723 -13.992 1.00 31.00  ? 144 LEU   B CD2 1 
ATOM   3690 N  N   . CYS   B 1 148 ? -1.445  16.219 -16.442 1.00 35.86  ? 145 CYS   B N   1 
ATOM   3691 C  CA  . CYS   B 1 148 ? -0.373  16.180 -17.482 1.00 38.24  ? 145 CYS   B CA  1 
ATOM   3692 C  C   . CYS   B 1 148 ? -0.989  16.079 -18.877 1.00 36.95  ? 145 CYS   B C   1 
ATOM   3693 O  O   . CYS   B 1 148 ? -0.344  16.521 -19.857 1.00 37.20  ? 145 CYS   B O   1 
ATOM   3694 C  CB  . CYS   B 1 148 ? 0.569   15.014 -17.268 1.00 42.14  ? 145 CYS   B CB  1 
ATOM   3695 S  SG  . CYS   B 1 148 ? 1.642   15.327 -15.847 1.00 45.55  ? 145 CYS   B SG  1 
ATOM   3696 N  N   . THR   B 1 149 ? -2.137  15.412 -18.971 1.00 36.85  ? 146 THR   B N   1 
ATOM   3697 C  CA  . THR   B 1 149 ? -2.851  15.263 -20.268 1.00 36.62  ? 146 THR   B CA  1 
ATOM   3698 C  C   . THR   B 1 149 ? -3.466  16.626 -20.579 1.00 32.94  ? 146 THR   B C   1 
ATOM   3699 O  O   . THR   B 1 149 ? -3.365  17.045 -21.709 1.00 33.11  ? 146 THR   B O   1 
ATOM   3700 C  CB  . THR   B 1 149 ? -3.862  14.103 -20.291 1.00 38.17  ? 146 THR   B CB  1 
ATOM   3701 O  OG1 . THR   B 1 149 ? -4.979  14.368 -19.445 1.00 35.68  ? 146 THR   B OG1 1 
ATOM   3702 C  CG2 . THR   B 1 149 ? -3.199  12.783 -19.960 1.00 42.25  ? 146 THR   B CG2 1 
ATOM   3703 N  N   . THR   B 1 150 ? -4.032  17.303 -19.576 1.00 30.37  ? 147 THR   B N   1 
ATOM   3704 C  CA  . THR   B 1 150 ? -4.611  18.650 -19.756 1.00 28.36  ? 147 THR   B CA  1 
ATOM   3705 C  C   . THR   B 1 150 ? -3.491  19.548 -20.252 1.00 27.72  ? 147 THR   B C   1 
ATOM   3706 O  O   . THR   B 1 150 ? -3.687  20.243 -21.274 1.00 27.51  ? 147 THR   B O   1 
ATOM   3707 C  CB  . THR   B 1 150 ? -5.235  19.156 -18.455 1.00 27.11  ? 147 THR   B CB  1 
ATOM   3708 O  OG1 . THR   B 1 150 ? -6.110  18.171 -17.936 1.00 27.92  ? 147 THR   B OG1 1 
ATOM   3709 C  CG2 . THR   B 1 150 ? -6.023  20.419 -18.674 1.00 25.67  ? 147 THR   B CG2 1 
ATOM   3710 N  N   . TRP   B 1 151 ? -2.353  19.492 -19.563 1.00 28.72  ? 148 TRP   B N   1 
ATOM   3711 C  CA  . TRP   B 1 151 ? -1.152  20.273 -19.953 1.00 29.45  ? 148 TRP   B CA  1 
ATOM   3712 C  C   . TRP   B 1 151 ? -0.723  19.983 -21.402 1.00 30.80  ? 148 TRP   B C   1 
ATOM   3713 O  O   . TRP   B 1 151 ? -0.462  20.961 -22.121 1.00 31.26  ? 148 TRP   B O   1 
ATOM   3714 C  CB  . TRP   B 1 151 ? -0.008  20.082 -18.959 1.00 30.51  ? 148 TRP   B CB  1 
ATOM   3715 C  CG  . TRP   B 1 151 ? 1.041   21.091 -19.279 1.00 30.30  ? 148 TRP   B CG  1 
ATOM   3716 C  CD1 . TRP   B 1 151 ? 2.217   20.873 -19.924 1.00 32.22  ? 148 TRP   B CD1 1 
ATOM   3717 C  CD2 . TRP   B 1 151 ? 0.918   22.515 -19.131 1.00 29.00  ? 148 TRP   B CD2 1 
ATOM   3718 N  NE1 . TRP   B 1 151 ? 2.864   22.055 -20.143 1.00 32.42  ? 148 TRP   B NE1 1 
ATOM   3719 C  CE2 . TRP   B 1 151 ? 2.105   23.084 -19.649 1.00 30.52  ? 148 TRP   B CE2 1 
ATOM   3720 C  CE3 . TRP   B 1 151 ? -0.055  23.359 -18.590 1.00 26.87  ? 148 TRP   B CE3 1 
ATOM   3721 C  CZ2 . TRP   B 1 151 ? 2.355   24.461 -19.613 1.00 30.60  ? 148 TRP   B CZ2 1 
ATOM   3722 C  CZ3 . TRP   B 1 151 ? 0.183   24.716 -18.580 1.00 27.41  ? 148 TRP   B CZ3 1 
ATOM   3723 C  CH2 . TRP   B 1 151 ? 1.359   25.259 -19.096 1.00 28.95  ? 148 TRP   B CH2 1 
ATOM   3724 N  N   . GLU   B 1 152 ? -0.709  18.727 -21.852 1.00 32.97  ? 149 GLU   B N   1 
ATOM   3725 C  CA  . GLU   B 1 152 ? -0.330  18.405 -23.260 1.00 35.14  ? 149 GLU   B CA  1 
ATOM   3726 C  C   . GLU   B 1 152 ? -1.292  19.106 -24.232 1.00 32.95  ? 149 GLU   B C   1 
ATOM   3727 O  O   . GLU   B 1 152 ? -0.816  19.595 -25.252 1.00 32.47  ? 149 GLU   B O   1 
ATOM   3728 C  CB  . GLU   B 1 152 ? -0.296  16.896 -23.549 1.00 39.71  ? 149 GLU   B CB  1 
ATOM   3729 C  CG  . GLU   B 1 152 ? 0.889   16.211 -22.924 1.00 43.83  ? 149 GLU   B CG  1 
ATOM   3730 C  CD  . GLU   B 1 152 ? 0.901   14.688 -22.915 1.00 50.04  ? 149 GLU   B CD  1 
ATOM   3731 O  OE1 . GLU   B 1 152 ? 1.915   14.148 -22.449 1.00 54.34  ? 149 GLU   B OE1 1 
ATOM   3732 O  OE2 . GLU   B 1 152 ? -0.092  14.049 -23.372 1.00 53.55  ? 149 GLU   B OE2 1 
ATOM   3733 N  N   . ALA   B 1 153 ? -2.595  19.150 -23.943 1.00 31.31  ? 150 ALA   B N   1 
ATOM   3734 C  CA  . ALA   B 1 153 ? -3.602  19.813 -24.809 1.00 31.06  ? 150 ALA   B CA  1 
ATOM   3735 C  C   . ALA   B 1 153 ? -3.428  21.345 -24.791 1.00 29.40  ? 150 ALA   B C   1 
ATOM   3736 O  O   . ALA   B 1 153 ? -3.596  21.943 -25.835 1.00 28.99  ? 150 ALA   B O   1 
ATOM   3737 C  CB  . ALA   B 1 153 ? -5.005  19.423 -24.441 1.00 30.90  ? 150 ALA   B CB  1 
ATOM   3738 N  N   . MET   B 1 154 ? -3.057  21.940 -23.656 1.00 28.17  ? 151 MET   B N   1 
ATOM   3739 C  CA  . MET   B 1 154 ? -2.619  23.363 -23.562 1.00 28.04  ? 151 MET   B CA  1 
ATOM   3740 C  C   . MET   B 1 154 ? -1.420  23.591 -24.488 1.00 29.78  ? 151 MET   B C   1 
ATOM   3741 O  O   . MET   B 1 154 ? -1.407  24.587 -25.195 1.00 29.65  ? 151 MET   B O   1 
ATOM   3742 C  CB  . MET   B 1 154 ? -2.206  23.714 -22.125 1.00 27.21  ? 151 MET   B CB  1 
ATOM   3743 C  CG  . MET   B 1 154 ? -3.361  23.615 -21.122 1.00 26.16  ? 151 MET   B CG  1 
ATOM   3744 S  SD  . MET   B 1 154 ? -4.627  24.901 -21.297 1.00 26.30  ? 151 MET   B SD  1 
ATOM   3745 C  CE  . MET   B 1 154 ? -3.666  26.231 -20.570 1.00 26.26  ? 151 MET   B CE  1 
ATOM   3746 N  N   . GLU   B 1 155 ? -0.436  22.689 -24.489 1.00 31.29  ? 152 GLU   B N   1 
ATOM   3747 C  CA  . GLU   B 1 155 ? 0.786   22.842 -25.335 1.00 33.22  ? 152 GLU   B CA  1 
ATOM   3748 C  C   . GLU   B 1 155 ? 0.355   22.892 -26.812 1.00 35.10  ? 152 GLU   B C   1 
ATOM   3749 O  O   . GLU   B 1 155 ? 0.941   23.714 -27.580 1.00 36.01  ? 152 GLU   B O   1 
ATOM   3750 C  CB  . GLU   B 1 155 ? 1.764   21.691 -25.122 1.00 34.66  ? 152 GLU   B CB  1 
ATOM   3751 C  CG  . GLU   B 1 155 ? 2.399   21.697 -23.751 1.00 34.68  ? 152 GLU   B CG  1 
ATOM   3752 C  CD  . GLU   B 1 155 ? 3.353   20.553 -23.478 1.00 37.14  ? 152 GLU   B CD  1 
ATOM   3753 O  OE1 . GLU   B 1 155 ? 3.153   19.466 -24.077 1.00 38.57  ? 152 GLU   B OE1 1 
ATOM   3754 O  OE2 . GLU   B 1 155 ? 4.324   20.757 -22.713 1.00 38.32  ? 152 GLU   B OE2 1 
ATOM   3755 N  N   . LYS   B 1 156 ? -0.633  22.071 -27.191 1.00 35.71  ? 153 LYS   B N   1 
ATOM   3756 C  CA  . LYS   B 1 156 ? -1.102  22.052 -28.601 1.00 39.10  ? 153 LYS   B CA  1 
ATOM   3757 C  C   . LYS   B 1 156 ? -1.736  23.408 -28.929 1.00 37.26  ? 153 LYS   B C   1 
ATOM   3758 O  O   . LYS   B 1 156 ? -1.577  23.857 -30.075 1.00 38.36  ? 153 LYS   B O   1 
ATOM   3759 C  CB  . LYS   B 1 156 ? -1.913  20.784 -28.874 1.00 42.81  ? 153 LYS   B CB  1 
ATOM   3760 C  CG  . LYS   B 1 156 ? -0.963  19.604 -29.051 1.00 48.23  ? 153 LYS   B CG  1 
ATOM   3761 C  CD  . LYS   B 1 156 ? -1.320  18.280 -28.419 1.00 52.83  ? 153 LYS   B CD  1 
ATOM   3762 C  CE  . LYS   B 1 156 ? -0.182  17.265 -28.522 1.00 57.81  ? 153 LYS   B CE  1 
ATOM   3763 N  NZ  . LYS   B 1 156 ? 0.505   17.084 -27.216 1.00 58.37  ? 153 LYS   B NZ  1 
ATOM   3764 N  N   . CYS   B 1 157 ? -2.350  24.070 -27.951 1.00 38.65  ? 154 CYS   B N   1 
ATOM   3765 C  CA  . CYS   B 1 157 ? -2.987  25.402 -28.144 1.00 37.02  ? 154 CYS   B CA  1 
ATOM   3766 C  C   . CYS   B 1 157 ? -1.893  26.435 -28.443 1.00 36.56  ? 154 CYS   B C   1 
ATOM   3767 O  O   . CYS   B 1 157 ? -2.087  27.303 -29.358 1.00 35.99  ? 154 CYS   B O   1 
ATOM   3768 C  CB  . CYS   B 1 157 ? -3.850  25.773 -26.954 1.00 35.81  ? 154 CYS   B CB  1 
ATOM   3769 S  SG  . CYS   B 1 157 ? -5.359  24.763 -26.901 1.00 37.26  ? 154 CYS   B SG  1 
ATOM   3770 N  N   . LYS   B 1 158 ? -0.731  26.266 -27.826 1.00 36.19  ? 155 LYS   B N   1 
ATOM   3771 C  CA  . LYS   B 1 158 ? 0.383   27.224 -28.038 1.00 36.67  ? 155 LYS   B CA  1 
ATOM   3772 C  C   . LYS   B 1 158 ? 0.994   26.942 -29.402 1.00 39.31  ? 155 LYS   B C   1 
ATOM   3773 O  O   . LYS   B 1 158 ? 1.219   27.929 -30.089 1.00 39.23  ? 155 LYS   B O   1 
ATOM   3774 C  CB  . LYS   B 1 158 ? 1.417   27.171 -26.916 1.00 35.59  ? 155 LYS   B CB  1 
ATOM   3775 C  CG  . LYS   B 1 158 ? 2.743   27.828 -27.231 1.00 36.74  ? 155 LYS   B CG  1 
ATOM   3776 C  CD  . LYS   B 1 158 ? 3.558   28.009 -25.974 1.00 36.24  ? 155 LYS   B CD  1 
ATOM   3777 C  CE  . LYS   B 1 158 ? 4.972   28.445 -26.224 1.00 38.40  ? 155 LYS   B CE  1 
ATOM   3778 N  NZ  . LYS   B 1 158 ? 5.038   29.866 -26.627 1.00 38.79  ? 155 LYS   B NZ  1 
ATOM   3779 N  N   . ASP   B 1 159 ? 1.160   25.664 -29.778 1.00 41.25  ? 156 ASP   B N   1 
ATOM   3780 C  CA  . ASP   B 1 159 ? 1.680   25.271 -31.108 1.00 45.49  ? 156 ASP   B CA  1 
ATOM   3781 C  C   . ASP   B 1 159 ? 0.766   25.869 -32.191 1.00 45.29  ? 156 ASP   B C   1 
ATOM   3782 O  O   . ASP   B 1 159 ? 1.307   26.325 -33.211 1.00 46.88  ? 156 ASP   B O   1 
ATOM   3783 C  CB  . ASP   B 1 159 ? 1.771   23.752 -31.299 1.00 48.54  ? 156 ASP   B CB  1 
ATOM   3784 C  CG  . ASP   B 1 159 ? 2.846   23.057 -30.474 1.00 50.83  ? 156 ASP   B CG  1 
ATOM   3785 O  OD1 . ASP   B 1 159 ? 3.938   23.656 -30.280 1.00 52.00  ? 156 ASP   B OD1 1 
ATOM   3786 O  OD2 . ASP   B 1 159 ? 2.582   21.917 -30.017 1.00 53.41  ? 156 ASP   B OD2 1 
ATOM   3787 N  N   . ALA   B 1 160 ? -0.564  25.861 -31.990 1.00 43.84  ? 157 ALA   B N   1 
ATOM   3788 C  CA  . ALA   B 1 160 ? -1.554  26.348 -32.991 1.00 43.85  ? 157 ALA   B CA  1 
ATOM   3789 C  C   . ALA   B 1 160 ? -1.548  27.881 -33.032 1.00 42.56  ? 157 ALA   B C   1 
ATOM   3790 O  O   . ALA   B 1 160 ? -2.209  28.411 -33.899 1.00 42.75  ? 157 ALA   B O   1 
ATOM   3791 C  CB  . ALA   B 1 160 ? -2.941  25.836 -32.709 1.00 43.06  ? 157 ALA   B CB  1 
ATOM   3792 N  N   . GLY   B 1 161 ? -0.835  28.559 -32.126 1.00 40.42  ? 158 GLY   B N   1 
ATOM   3793 C  CA  . GLY   B 1 161 ? -0.830  30.029 -32.056 1.00 39.96  ? 158 GLY   B CA  1 
ATOM   3794 C  C   . GLY   B 1 161 ? -2.127  30.591 -31.494 1.00 38.01  ? 158 GLY   B C   1 
ATOM   3795 O  O   . GLY   B 1 161 ? -2.296  31.829 -31.551 1.00 38.27  ? 158 GLY   B O   1 
ATOM   3796 N  N   . LEU   B 1 162 ? -2.973  29.765 -30.866 1.00 36.16  ? 159 LEU   B N   1 
ATOM   3797 C  CA  . LEU   B 1 162 ? -4.216  30.287 -30.227 1.00 33.72  ? 159 LEU   B CA  1 
ATOM   3798 C  C   . LEU   B 1 162 ? -3.869  30.957 -28.886 1.00 31.31  ? 159 LEU   B C   1 
ATOM   3799 O  O   . LEU   B 1 162 ? -4.637  31.836 -28.435 1.00 29.13  ? 159 LEU   B O   1 
ATOM   3800 C  CB  . LEU   B 1 162 ? -5.205  29.146 -30.011 1.00 34.23  ? 159 LEU   B CB  1 
ATOM   3801 C  CG  . LEU   B 1 162 ? -5.681  28.412 -31.268 1.00 37.18  ? 159 LEU   B CG  1 
ATOM   3802 C  CD1 . LEU   B 1 162 ? -6.668  27.333 -30.902 1.00 37.78  ? 159 LEU   B CD1 1 
ATOM   3803 C  CD2 . LEU   B 1 162 ? -6.349  29.324 -32.249 1.00 38.46  ? 159 LEU   B CD2 1 
ATOM   3804 N  N   . ALA   B 1 163 ? -2.809  30.481 -28.239 1.00 30.57  ? 160 ALA   B N   1 
ATOM   3805 C  CA  . ALA   B 1 163 ? -2.241  31.090 -27.018 1.00 29.52  ? 160 ALA   B CA  1 
ATOM   3806 C  C   . ALA   B 1 163 ? -0.748  31.398 -27.224 1.00 30.84  ? 160 ALA   B C   1 
ATOM   3807 O  O   . ALA   B 1 163 ? -0.045  30.470 -27.624 1.00 32.33  ? 160 ALA   B O   1 
ATOM   3808 C  CB  . ALA   B 1 163 ? -2.454  30.136 -25.888 1.00 28.37  ? 160 ALA   B CB  1 
ATOM   3809 N  N   . LYS   B 1 164 ? -0.287  32.643 -26.979 1.00 30.64  ? 161 LYS   B N   1 
ATOM   3810 C  CA  . LYS   B 1 164 ? 1.158   32.982 -27.093 1.00 32.65  ? 161 LYS   B CA  1 
ATOM   3811 C  C   . LYS   B 1 164 ? 1.919   32.227 -25.996 1.00 31.06  ? 161 LYS   B C   1 
ATOM   3812 O  O   . LYS   B 1 164 ? 2.997   31.667 -26.277 1.00 32.36  ? 161 LYS   B O   1 
ATOM   3813 C  CB  . LYS   B 1 164 ? 1.445   34.488 -27.003 1.00 34.35  ? 161 LYS   B CB  1 
ATOM   3814 C  CG  . LYS   B 1 164 ? 0.909   35.357 -28.133 1.00 37.14  ? 161 LYS   B CG  1 
ATOM   3815 C  CD  . LYS   B 1 164 ? 1.197   34.824 -29.528 1.00 41.14  ? 161 LYS   B CD  1 
ATOM   3816 C  CE  . LYS   B 1 164 ? 0.814   35.782 -30.635 1.00 43.17  ? 161 LYS   B CE  1 
ATOM   3817 N  NZ  . LYS   B 1 164 ? 1.514   35.409 -31.886 1.00 47.10  ? 161 LYS   B NZ  1 
ATOM   3818 N  N   . SER   B 1 165 ? 1.357   32.209 -24.785 1.00 28.46  ? 162 SER   B N   1 
ATOM   3819 C  CA  . SER   B 1 165 ? 1.956   31.546 -23.617 1.00 27.50  ? 162 SER   B CA  1 
ATOM   3820 C  C   . SER   B 1 165 ? 0.903   30.727 -22.894 1.00 25.70  ? 162 SER   B C   1 
ATOM   3821 O  O   . SER   B 1 165 ? -0.294  31.047 -23.002 1.00 24.66  ? 162 SER   B O   1 
ATOM   3822 C  CB  . SER   B 1 165 ? 2.591   32.579 -22.693 1.00 27.14  ? 162 SER   B CB  1 
ATOM   3823 O  OG  . SER   B 1 165 ? 3.646   33.239 -23.356 1.00 28.58  ? 162 SER   B OG  1 
ATOM   3824 N  N   . ILE   B 1 166 ? 1.366   29.726 -22.146 1.00 25.99  ? 163 ILE   B N   1 
ATOM   3825 C  CA  . ILE   B 1 166 ? 0.493   28.883 -21.292 1.00 24.86  ? 163 ILE   B CA  1 
ATOM   3826 C  C   . ILE   B 1 166 ? 1.078   28.807 -19.877 1.00 24.08  ? 163 ILE   B C   1 
ATOM   3827 O  O   . ILE   B 1 166 ? 2.321   28.784 -19.698 1.00 23.82  ? 163 ILE   B O   1 
ATOM   3828 C  CB  . ILE   B 1 166 ? 0.279   27.502 -21.936 1.00 26.36  ? 163 ILE   B CB  1 
ATOM   3829 C  CG1 . ILE   B 1 166 ? 1.588   26.799 -22.255 1.00 28.11  ? 163 ILE   B CG1 1 
ATOM   3830 C  CG2 . ILE   B 1 166 ? -0.558  27.665 -23.184 1.00 26.59  ? 163 ILE   B CG2 1 
ATOM   3831 C  CD1 . ILE   B 1 166 ? 1.405   25.479 -22.881 1.00 30.33  ? 163 ILE   B CD1 1 
ATOM   3832 N  N   . GLY   B 1 167 ? 0.184   28.723 -18.903 1.00 23.24  ? 164 GLY   B N   1 
ATOM   3833 C  CA  . GLY   B 1 167 ? 0.572   28.629 -17.503 1.00 22.83  ? 164 GLY   B CA  1 
ATOM   3834 C  C   . GLY   B 1 167 ? -0.547  28.032 -16.715 1.00 22.40  ? 164 GLY   B C   1 
ATOM   3835 O  O   . GLY   B 1 167 ? -1.478  27.453 -17.305 1.00 21.88  ? 164 GLY   B O   1 
ATOM   3836 N  N   . VAL   B 1 168 ? -0.407  28.114 -15.398 1.00 22.41  ? 165 VAL   B N   1 
ATOM   3837 C  CA  . VAL   B 1 168 ? -1.385  27.490 -14.485 1.00 22.69  ? 165 VAL   B CA  1 
ATOM   3838 C  C   . VAL   B 1 168 ? -1.772  28.509 -13.429 1.00 22.11  ? 165 VAL   B C   1 
ATOM   3839 O  O   . VAL   B 1 168 ? -1.163  29.589 -13.398 1.00 21.48  ? 165 VAL   B O   1 
ATOM   3840 C  CB  . VAL   B 1 168 ? -0.836  26.190 -13.871 1.00 23.82  ? 165 VAL   B CB  1 
ATOM   3841 C  CG1 . VAL   B 1 168 ? -0.487  25.156 -14.948 1.00 25.22  ? 165 VAL   B CG1 1 
ATOM   3842 C  CG2 . VAL   B 1 168 ? 0.352   26.463 -12.965 1.00 23.86  ? 165 VAL   B CG2 1 
ATOM   3843 N  N   . SER   B 1 169 ? -2.803  28.157 -12.653 1.00 22.87  ? 166 SER   B N   1 
ATOM   3844 C  CA  . SER   B 1 169 ? -3.333  28.988 -11.544 1.00 21.97  ? 166 SER   B CA  1 
ATOM   3845 C  C   . SER   B 1 169 ? -3.758  28.082 -10.394 1.00 22.06  ? 166 SER   B C   1 
ATOM   3846 O  O   . SER   B 1 169 ? -4.305  26.992 -10.633 1.00 22.27  ? 166 SER   B O   1 
ATOM   3847 C  CB  . SER   B 1 169 ? -4.484  29.848 -11.991 1.00 21.68  ? 166 SER   B CB  1 
ATOM   3848 O  OG  . SER   B 1 169 ? -4.886  30.775 -10.988 1.00 21.65  ? 166 SER   B OG  1 
ATOM   3849 N  N   . ASN   B 1 170 ? -3.499  28.537 -9.171  1.00 21.83  ? 167 ASN   B N   1 
ATOM   3850 C  CA  . ASN   B 1 170 ? -3.939  27.805 -7.960  1.00 22.00  ? 167 ASN   B CA  1 
ATOM   3851 C  C   . ASN   B 1 170 ? -3.251  26.435 -7.829  1.00 23.19  ? 167 ASN   B C   1 
ATOM   3852 O  O   . ASN   B 1 170 ? -3.849  25.553 -7.174  1.00 25.07  ? 167 ASN   B O   1 
ATOM   3853 C  CB  . ASN   B 1 170 ? -5.445  27.606 -7.975  1.00 21.87  ? 167 ASN   B CB  1 
ATOM   3854 C  CG  . ASN   B 1 170 ? -6.202  28.902 -7.837  1.00 21.61  ? 167 ASN   B CG  1 
ATOM   3855 O  OD1 . ASN   B 1 170 ? -5.958  29.647 -6.882  1.00 21.71  ? 167 ASN   B OD1 1 
ATOM   3856 N  ND2 . ASN   B 1 170 ? -7.008  29.231 -8.831  1.00 20.26  ? 167 ASN   B ND2 1 
ATOM   3857 N  N   . PHE   B 1 171 ? -2.073  26.253 -8.430  1.00 23.12  ? 168 PHE   B N   1 
ATOM   3858 C  CA  . PHE   B 1 171 ? -1.214  25.049 -8.262  1.00 24.28  ? 168 PHE   B CA  1 
ATOM   3859 C  C   . PHE   B 1 171 ? -0.305  25.280 -7.043  1.00 25.05  ? 168 PHE   B C   1 
ATOM   3860 O  O   . PHE   B 1 171 ? 0.151   26.444 -6.812  1.00 24.16  ? 168 PHE   B O   1 
ATOM   3861 C  CB  . PHE   B 1 171 ? -0.372  24.740 -9.505  1.00 24.54  ? 168 PHE   B CB  1 
ATOM   3862 C  CG  . PHE   B 1 171 ? -1.070  24.017 -10.627 1.00 25.49  ? 168 PHE   B CG  1 
ATOM   3863 C  CD1 . PHE   B 1 171 ? -2.358  24.359 -10.993 1.00 25.38  ? 168 PHE   B CD1 1 
ATOM   3864 C  CD2 . PHE   B 1 171 ? -0.451  22.985 -11.305 1.00 26.97  ? 168 PHE   B CD2 1 
ATOM   3865 C  CE1 . PHE   B 1 171 ? -2.998  23.728 -12.047 1.00 26.04  ? 168 PHE   B CE1 1 
ATOM   3866 C  CE2 . PHE   B 1 171 ? -1.101  22.323 -12.337 1.00 27.69  ? 168 PHE   B CE2 1 
ATOM   3867 C  CZ  . PHE   B 1 171 ? -2.365  22.718 -12.731 1.00 27.17  ? 168 PHE   B CZ  1 
ATOM   3868 N  N   . ASN   B 1 172 ? -0.033  24.214 -6.316  1.00 26.47  ? 169 ASN   B N   1 
ATOM   3869 C  CA  . ASN   B 1 172 ? 1.010   24.179 -5.265  1.00 27.95  ? 169 ASN   B CA  1 
ATOM   3870 C  C   . ASN   B 1 172 ? 2.287   23.650 -5.926  1.00 29.61  ? 169 ASN   B C   1 
ATOM   3871 O  O   . ASN   B 1 172 ? 2.269   23.301 -7.118  1.00 28.80  ? 169 ASN   B O   1 
ATOM   3872 C  CB  . ASN   B 1 172 ? 0.533   23.420 -4.031  1.00 28.78  ? 169 ASN   B CB  1 
ATOM   3873 C  CG  . ASN   B 1 172 ? 0.234   21.957 -4.317  1.00 29.85  ? 169 ASN   B CG  1 
ATOM   3874 O  OD1 . ASN   B 1 172 ? 0.756   21.379 -5.275  1.00 30.94  ? 169 ASN   B OD1 1 
ATOM   3875 N  ND2 . ASN   B 1 172 ? -0.614  21.345 -3.508  1.00 30.17  ? 169 ASN   B ND2 1 
ATOM   3876 N  N   . ARG   B 1 173 ? 3.356   23.573 -5.145  1.00 31.47  ? 170 ARG   B N   1 
ATOM   3877 C  CA  . ARG   B 1 173 ? 4.673   23.076 -5.572  1.00 33.47  ? 170 ARG   B CA  1 
ATOM   3878 C  C   . ARG   B 1 173 ? 4.580   21.678 -6.175  1.00 34.35  ? 170 ARG   B C   1 
ATOM   3879 O  O   . ARG   B 1 173 ? 5.224   21.412 -7.216  1.00 33.31  ? 170 ARG   B O   1 
ATOM   3880 C  CB  . ARG   B 1 173 ? 5.605   22.981 -4.367  1.00 36.52  ? 170 ARG   B CB  1 
ATOM   3881 C  CG  . ARG   B 1 173 ? 6.983   22.476 -4.751  1.00 39.10  ? 170 ARG   B CG  1 
ATOM   3882 C  CD  . ARG   B 1 173 ? 8.034   22.841 -3.744  1.00 43.39  ? 170 ARG   B CD  1 
ATOM   3883 N  NE  . ARG   B 1 173 ? 9.192   22.011 -3.998  1.00 48.17  ? 170 ARG   B NE  1 
ATOM   3884 C  CZ  . ARG   B 1 173 ? 10.390  22.199 -3.458  1.00 53.02  ? 170 ARG   B CZ  1 
ATOM   3885 N  NH1 . ARG   B 1 173 ? 11.371  21.352 -3.719  1.00 54.75  ? 170 ARG   B NH1 1 
ATOM   3886 N  NH2 . ARG   B 1 173 ? 10.602  23.232 -2.662  1.00 53.49  ? 170 ARG   B NH2 1 
ATOM   3887 N  N   A ARG   B 1 174 ? 3.867   20.782 -5.492  0.50 34.65  ? 171 ARG   B N   1 
ATOM   3888 N  N   B ARG   B 1 174 ? 3.865   20.785 -5.493  0.50 34.90  ? 171 ARG   B N   1 
ATOM   3889 C  CA  A ARG   B 1 174 ? 3.773   19.364 -5.893  0.50 36.65  ? 171 ARG   B CA  1 
ATOM   3890 C  CA  B ARG   B 1 174 ? 3.771   19.366 -5.884  0.50 37.06  ? 171 ARG   B CA  1 
ATOM   3891 C  C   A ARG   B 1 174 ? 3.170   19.318 -7.302  0.50 35.73  ? 171 ARG   B C   1 
ATOM   3892 C  C   B ARG   B 1 174 ? 3.168   19.315 -7.295  0.50 35.96  ? 171 ARG   B C   1 
ATOM   3893 O  O   A ARG   B 1 174 ? 3.690   18.566 -8.161  0.50 36.02  ? 171 ARG   B O   1 
ATOM   3894 O  O   B ARG   B 1 174 ? 3.691   18.564 -8.153  0.50 36.22  ? 171 ARG   B O   1 
ATOM   3895 C  CB  A ARG   B 1 174 ? 2.941   18.584 -4.868  0.50 38.67  ? 171 ARG   B CB  1 
ATOM   3896 C  CB  B ARG   B 1 174 ? 2.948   18.613 -4.831  0.50 39.38  ? 171 ARG   B CB  1 
ATOM   3897 C  CG  A ARG   B 1 174 ? 3.086   17.072 -4.976  0.50 41.76  ? 171 ARG   B CG  1 
ATOM   3898 C  CG  B ARG   B 1 174 ? 3.521   17.266 -4.414  0.50 42.92  ? 171 ARG   B CG  1 
ATOM   3899 C  CD  A ARG   B 1 174 ? 1.767   16.328 -4.894  0.50 43.50  ? 171 ARG   B CD  1 
ATOM   3900 C  CD  B ARG   B 1 174 ? 4.744   17.370 -3.521  0.50 44.55  ? 171 ARG   B CD  1 
ATOM   3901 N  NE  A ARG   B 1 174 ? 0.743   17.127 -4.224  0.50 43.28  ? 171 ARG   B NE  1 
ATOM   3902 N  NE  B ARG   B 1 174 ? 5.997   17.201 -4.254  0.50 46.26  ? 171 ARG   B NE  1 
ATOM   3903 C  CZ  A ARG   B 1 174 ? -0.503  17.256 -4.666  0.50 42.63  ? 171 ARG   B CZ  1 
ATOM   3904 C  CZ  B ARG   B 1 174 ? 6.963   18.110 -4.311  0.50 46.40  ? 171 ARG   B CZ  1 
ATOM   3905 N  NH1 A ARG   B 1 174 ? -1.365  18.008 -3.997  0.50 41.74  ? 171 ARG   B NH1 1 
ATOM   3906 N  NH1 B ARG   B 1 174 ? 8.063   17.874 -5.008  0.50 48.84  ? 171 ARG   B NH1 1 
ATOM   3907 N  NH2 A ARG   B 1 174 ? -0.862  16.650 -5.788  0.50 42.93  ? 171 ARG   B NH2 1 
ATOM   3908 N  NH2 B ARG   B 1 174 ? 6.826   19.250 -3.671  0.50 45.17  ? 171 ARG   B NH2 1 
ATOM   3909 N  N   . GLN   B 1 175 ? 2.123   20.118 -7.530  1.00 34.07  ? 172 GLN   B N   1 
ATOM   3910 C  CA  . GLN   B 1 175 ? 1.349   20.061 -8.800  1.00 33.20  ? 172 GLN   B CA  1 
ATOM   3911 C  C   . GLN   B 1 175 ? 2.228   20.652 -9.905  1.00 32.54  ? 172 GLN   B C   1 
ATOM   3912 O  O   . GLN   B 1 175 ? 2.288   20.062 -11.009 1.00 33.95  ? 172 GLN   B O   1 
ATOM   3913 C  CB  . GLN   B 1 175 ? 0.010   20.767 -8.650  1.00 31.18  ? 172 GLN   B CB  1 
ATOM   3914 C  CG  . GLN   B 1 175 ? -0.930  20.053 -7.691  1.00 32.32  ? 172 GLN   B CG  1 
ATOM   3915 C  CD  . GLN   B 1 175 ? -1.999  20.944 -7.091  1.00 30.95  ? 172 GLN   B CD  1 
ATOM   3916 O  OE1 . GLN   B 1 175 ? -1.841  22.159 -6.996  1.00 29.81  ? 172 GLN   B OE1 1 
ATOM   3917 N  NE2 . GLN   B 1 175 ? -3.105  20.350 -6.669  1.00 32.04  ? 172 GLN   B NE2 1 
ATOM   3918 N  N   . LEU   B 1 176 ? 2.929   21.747 -9.620  1.00 31.61  ? 173 LEU   B N   1 
ATOM   3919 C  CA  . LEU   B 1 176 ? 3.929   22.280 -10.585 1.00 32.31  ? 173 LEU   B CA  1 
ATOM   3920 C  C   . LEU   B 1 176 ? 4.965   21.218 -10.936 1.00 35.16  ? 173 LEU   B C   1 
ATOM   3921 O  O   . LEU   B 1 176 ? 5.200   21.033 -12.143 1.00 34.93  ? 173 LEU   B O   1 
ATOM   3922 C  CB  . LEU   B 1 176 ? 4.627   23.506 -10.015 1.00 31.62  ? 173 LEU   B CB  1 
ATOM   3923 C  CG  . LEU   B 1 176 ? 3.767   24.743 -9.874  1.00 30.33  ? 173 LEU   B CG  1 
ATOM   3924 C  CD1 . LEU   B 1 176 ? 4.540   25.880 -9.226  1.00 29.80  ? 173 LEU   B CD1 1 
ATOM   3925 C  CD2 . LEU   B 1 176 ? 3.252   25.152 -11.236 1.00 29.80  ? 173 LEU   B CD2 1 
ATOM   3926 N  N   . GLU   B 1 177 ? 5.573   20.575 -9.926  1.00 37.65  ? 174 GLU   B N   1 
ATOM   3927 C  CA  . GLU   B 1 177 ? 6.603   19.531 -10.125 1.00 41.36  ? 174 GLU   B CA  1 
ATOM   3928 C  C   . GLU   B 1 177 ? 6.055   18.467 -11.076 1.00 42.88  ? 174 GLU   B C   1 
ATOM   3929 O  O   . GLU   B 1 177 ? 6.818   17.954 -11.901 1.00 42.17  ? 174 GLU   B O   1 
ATOM   3930 C  CB  . GLU   B 1 177 ? 6.990   18.818 -8.830  1.00 44.49  ? 174 GLU   B CB  1 
ATOM   3931 C  CG  . GLU   B 1 177 ? 7.641   19.699 -7.788  1.00 45.80  ? 174 GLU   B CG  1 
ATOM   3932 C  CD  . GLU   B 1 177 ? 9.143   19.866 -7.910  1.00 50.47  ? 174 GLU   B CD  1 
ATOM   3933 O  OE1 . GLU   B 1 177 ? 9.802   20.030 -6.826  1.00 52.52  ? 174 GLU   B OE1 1 
ATOM   3934 O  OE2 . GLU   B 1 177 ? 9.644   19.882 -9.079  1.00 53.77  ? 174 GLU   B OE2 1 
ATOM   3935 N  N   . MET   B 1 178 ? 4.809   18.077 -10.860 1.00 43.38  ? 175 MET   B N   1 
ATOM   3936 C  CA  . MET   B 1 178 ? 4.144   17.077 -11.696 1.00 46.92  ? 175 MET   B CA  1 
ATOM   3937 C  C   . MET   B 1 178 ? 4.255   17.508 -13.165 1.00 44.23  ? 175 MET   B C   1 
ATOM   3938 O  O   . MET   B 1 178 ? 4.509   16.631 -14.007 1.00 45.30  ? 175 MET   B O   1 
ATOM   3939 C  CB  . MET   B 1 178 ? 2.678   16.952 -11.289 1.00 51.24  ? 175 MET   B CB  1 
ATOM   3940 C  CG  . MET   B 1 178 ? 1.921   15.906 -12.085 1.00 58.51  ? 175 MET   B CG  1 
ATOM   3941 S  SD  . MET   B 1 178 ? 0.187   15.831 -11.567 1.00 67.78  ? 175 MET   B SD  1 
ATOM   3942 C  CE  . MET   B 1 178 ? -0.292  17.559 -11.702 1.00 64.84  ? 175 MET   B CE  1 
ATOM   3943 N  N   . ILE   B 1 179 ? 4.054   18.793 -13.486 1.00 40.88  ? 176 ILE   B N   1 
ATOM   3944 C  CA  . ILE   B 1 179 ? 4.132   19.257 -14.903 1.00 40.25  ? 176 ILE   B CA  1 
ATOM   3945 C  C   . ILE   B 1 179 ? 5.618   19.297 -15.274 1.00 40.89  ? 176 ILE   B C   1 
ATOM   3946 O  O   . ILE   B 1 179 ? 5.951   18.892 -16.400 1.00 42.25  ? 176 ILE   B O   1 
ATOM   3947 C  CB  . ILE   B 1 179 ? 3.464   20.626 -15.163 1.00 38.38  ? 176 ILE   B CB  1 
ATOM   3948 C  CG1 . ILE   B 1 179 ? 1.999   20.720 -14.726 1.00 37.63  ? 176 ILE   B CG1 1 
ATOM   3949 C  CG2 . ILE   B 1 179 ? 3.623   21.046 -16.616 1.00 38.94  ? 176 ILE   B CG2 1 
ATOM   3950 C  CD1 . ILE   B 1 179 ? 1.107   19.646 -15.250 1.00 39.07  ? 176 ILE   B CD1 1 
ATOM   3951 N  N   . LEU   B 1 180 ? 6.473   19.817 -14.387 1.00 40.02  ? 177 LEU   B N   1 
ATOM   3952 C  CA  . LEU   B 1 180 ? 7.891   20.097 -14.746 1.00 41.32  ? 177 LEU   B CA  1 
ATOM   3953 C  C   . LEU   B 1 180 ? 8.615   18.779 -15.016 1.00 44.49  ? 177 LEU   B C   1 
ATOM   3954 O  O   . LEU   B 1 180 ? 9.550   18.765 -15.844 1.00 45.74  ? 177 LEU   B O   1 
ATOM   3955 C  CB  . LEU   B 1 180 ? 8.597   20.872 -13.631 1.00 40.13  ? 177 LEU   B CB  1 
ATOM   3956 C  CG  . LEU   B 1 180 ? 8.116   22.307 -13.461 1.00 37.75  ? 177 LEU   B CG  1 
ATOM   3957 C  CD1 . LEU   B 1 180 ? 8.664   22.895 -12.163 1.00 37.01  ? 177 LEU   B CD1 1 
ATOM   3958 C  CD2 . LEU   B 1 180 ? 8.495   23.164 -14.661 1.00 37.13  ? 177 LEU   B CD2 1 
ATOM   3959 N  N   . ASN   B 1 181 ? 8.180   17.715 -14.354 1.00 45.96  ? 178 ASN   B N   1 
ATOM   3960 C  CA  . ASN   B 1 181 ? 8.850   16.393 -14.438 1.00 50.16  ? 178 ASN   B CA  1 
ATOM   3961 C  C   . ASN   B 1 181 ? 8.137   15.481 -15.430 1.00 51.38  ? 178 ASN   B C   1 
ATOM   3962 O  O   . ASN   B 1 181 ? 8.557   14.335 -15.520 1.00 53.38  ? 178 ASN   B O   1 
ATOM   3963 C  CB  . ASN   B 1 181 ? 8.917   15.726 -13.073 1.00 52.31  ? 178 ASN   B CB  1 
ATOM   3964 C  CG  . ASN   B 1 181 ? 9.769   16.520 -12.108 1.00 52.90  ? 178 ASN   B CG  1 
ATOM   3965 O  OD1 . ASN   B 1 181 ? 10.797  17.079 -12.487 1.00 55.22  ? 178 ASN   B OD1 1 
ATOM   3966 N  ND2 . ASN   B 1 181 ? 9.339   16.575 -10.858 1.00 52.11  ? 178 ASN   B ND2 1 
ATOM   3967 N  N   . LYS   B 1 182 ? 7.114   15.975 -16.129 1.00 49.89  ? 179 LYS   B N   1 
ATOM   3968 C  CA  . LYS   B 1 182 ? 6.355   15.180 -17.121 1.00 52.28  ? 179 LYS   B CA  1 
ATOM   3969 C  C   . LYS   B 1 182 ? 7.326   14.729 -18.209 1.00 54.28  ? 179 LYS   B C   1 
ATOM   3970 O  O   . LYS   B 1 182 ? 8.033   15.554 -18.798 1.00 53.38  ? 179 LYS   B O   1 
ATOM   3971 C  CB  . LYS   B 1 182 ? 5.197   16.012 -17.682 1.00 51.02  ? 179 LYS   B CB  1 
ATOM   3972 C  CG  . LYS   B 1 182 ? 4.216   15.251 -18.564 1.00 53.65  ? 179 LYS   B CG  1 
ATOM   3973 C  CD  . LYS   B 1 182 ? 3.182   16.131 -19.241 1.00 52.46  ? 179 LYS   B CD  1 
ATOM   3974 C  CE  . LYS   B 1 182 ? 3.635   16.562 -20.611 1.00 54.31  ? 179 LYS   B CE  1 
ATOM   3975 N  NZ  . LYS   B 1 182 ? 3.983   15.377 -21.434 1.00 57.96  ? 179 LYS   B NZ  1 
ATOM   3976 N  N   . PRO   B 1 183 ? 7.381   13.408 -18.506 1.00 56.98  ? 180 PRO   B N   1 
ATOM   3977 C  CA  . PRO   B 1 183 ? 8.013   12.905 -19.726 1.00 59.09  ? 180 PRO   B CA  1 
ATOM   3978 C  C   . PRO   B 1 183 ? 7.563   13.639 -20.997 1.00 57.00  ? 180 PRO   B C   1 
ATOM   3979 O  O   . PRO   B 1 183 ? 6.381   13.833 -21.181 1.00 55.43  ? 180 PRO   B O   1 
ATOM   3980 C  CB  . PRO   B 1 183 ? 7.535   11.439 -19.771 1.00 62.48  ? 180 PRO   B CB  1 
ATOM   3981 C  CG  . PRO   B 1 183 ? 7.430   11.081 -18.296 1.00 62.25  ? 180 PRO   B CG  1 
ATOM   3982 C  CD  . PRO   B 1 183 ? 6.815   12.319 -17.690 1.00 58.14  ? 180 PRO   B CD  1 
ATOM   3983 N  N   . GLY   B 1 184 ? 8.531   14.051 -21.814 1.00 56.91  ? 181 GLY   B N   1 
ATOM   3984 C  CA  . GLY   B 1 184 ? 8.285   14.727 -23.095 1.00 55.78  ? 181 GLY   B CA  1 
ATOM   3985 C  C   . GLY   B 1 184 ? 7.633   16.078 -22.921 1.00 51.90  ? 181 GLY   B C   1 
ATOM   3986 O  O   . GLY   B 1 184 ? 6.962   16.547 -23.864 1.00 51.20  ? 181 GLY   B O   1 
ATOM   3987 N  N   . LEU   B 1 185 ? 7.811   16.719 -21.763 1.00 49.28  ? 182 LEU   B N   1 
ATOM   3988 C  CA  . LEU   B 1 185 ? 7.360   18.113 -21.597 1.00 46.65  ? 182 LEU   B CA  1 
ATOM   3989 C  C   . LEU   B 1 185 ? 7.824   18.894 -22.830 1.00 47.50  ? 182 LEU   B C   1 
ATOM   3990 O  O   . LEU   B 1 185 ? 8.995   18.725 -23.193 1.00 49.61  ? 182 LEU   B O   1 
ATOM   3991 C  CB  . LEU   B 1 185 ? 7.972   18.703 -20.325 1.00 44.80  ? 182 LEU   B CB  1 
ATOM   3992 C  CG  . LEU   B 1 185 ? 7.560   20.141 -20.016 1.00 42.35  ? 182 LEU   B CG  1 
ATOM   3993 C  CD1 . LEU   B 1 185 ? 6.082   20.212 -19.653 1.00 39.97  ? 182 LEU   B CD1 1 
ATOM   3994 C  CD2 . LEU   B 1 185 ? 8.445   20.720 -18.927 1.00 42.01  ? 182 LEU   B CD2 1 
ATOM   3995 N  N   . LYS   B 1 186 ? 6.988   19.772 -23.386 1.00 46.24  ? 183 LYS   B N   1 
ATOM   3996 C  CA  . LYS   B 1 186 ? 7.405   20.682 -24.483 1.00 48.64  ? 183 LYS   B CA  1 
ATOM   3997 C  C   . LYS   B 1 186 ? 7.561   22.104 -23.927 1.00 46.53  ? 183 LYS   B C   1 
ATOM   3998 O  O   . LYS   B 1 186 ? 8.567   22.779 -24.243 1.00 48.15  ? 183 LYS   B O   1 
ATOM   3999 C  CB  . LYS   B 1 186 ? 6.394   20.641 -25.641 1.00 50.26  ? 183 LYS   B CB  1 
ATOM   4000 C  CG  . LYS   B 1 186 ? 6.892   21.309 -26.919 1.00 53.94  ? 183 LYS   B CG  1 
ATOM   4001 C  CD  . LYS   B 1 186 ? 5.979   21.268 -28.160 1.00 56.15  ? 183 LYS   B CD  1 
ATOM   4002 C  CE  . LYS   B 1 186 ? 6.655   21.895 -29.365 1.00 59.28  ? 183 LYS   B CE  1 
ATOM   4003 N  NZ  . LYS   B 1 186 ? 5.924   21.623 -30.623 1.00 62.58  ? 183 LYS   B NZ  1 
ATOM   4004 N  N   . TYR   B 1 187 ? 6.570   22.566 -23.175 1.00 43.14  ? 184 TYR   B N   1 
ATOM   4005 C  CA  . TYR   B 1 187 ? 6.501   23.961 -22.662 1.00 40.99  ? 184 TYR   B CA  1 
ATOM   4006 C  C   . TYR   B 1 187 ? 6.262   23.935 -21.149 1.00 38.93  ? 184 TYR   B C   1 
ATOM   4007 O  O   . TYR   B 1 187 ? 5.240   23.400 -20.710 1.00 36.83  ? 184 TYR   B O   1 
ATOM   4008 C  CB  . TYR   B 1 187 ? 5.366   24.730 -23.349 1.00 40.29  ? 184 TYR   B CB  1 
ATOM   4009 C  CG  . TYR   B 1 187 ? 5.492   24.830 -24.849 1.00 42.62  ? 184 TYR   B CG  1 
ATOM   4010 C  CD1 . TYR   B 1 187 ? 6.647   25.318 -25.453 1.00 44.95  ? 184 TYR   B CD1 1 
ATOM   4011 C  CD2 . TYR   B 1 187 ? 4.459   24.403 -25.668 1.00 43.40  ? 184 TYR   B CD2 1 
ATOM   4012 C  CE1 . TYR   B 1 187 ? 6.765   25.392 -26.835 1.00 47.01  ? 184 TYR   B CE1 1 
ATOM   4013 C  CE2 . TYR   B 1 187 ? 4.567   24.455 -27.050 1.00 45.84  ? 184 TYR   B CE2 1 
ATOM   4014 C  CZ  . TYR   B 1 187 ? 5.717   24.964 -27.635 1.00 47.46  ? 184 TYR   B CZ  1 
ATOM   4015 O  OH  . TYR   B 1 187 ? 5.786   25.000 -29.002 1.00 49.83  ? 184 TYR   B OH  1 
ATOM   4016 N  N   . LYS   B 1 188 ? 7.161   24.569 -20.396 1.00 38.71  ? 185 LYS   B N   1 
ATOM   4017 C  CA  . LYS   B 1 188 ? 6.985   24.812 -18.950 1.00 37.57  ? 185 LYS   B CA  1 
ATOM   4018 C  C   . LYS   B 1 188 ? 5.834   25.784 -18.786 1.00 34.79  ? 185 LYS   B C   1 
ATOM   4019 O  O   . LYS   B 1 188 ? 5.586   26.598 -19.662 1.00 33.57  ? 185 LYS   B O   1 
ATOM   4020 C  CB  . LYS   B 1 188 ? 8.255   25.409 -18.338 1.00 39.09  ? 185 LYS   B CB  1 
ATOM   4021 C  CG  . LYS   B 1 188 ? 9.475   24.510 -18.410 1.00 42.36  ? 185 LYS   B CG  1 
ATOM   4022 C  CD  . LYS   B 1 188 ? 10.505  24.782 -17.336 1.00 44.10  ? 185 LYS   B CD  1 
ATOM   4023 C  CE  . LYS   B 1 188 ? 11.103  26.168 -17.400 1.00 44.86  ? 185 LYS   B CE  1 
ATOM   4024 N  NZ  . LYS   B 1 188 ? 12.246  26.290 -16.464 1.00 45.71  ? 185 LYS   B NZ  1 
ATOM   4025 N  N   . PRO   B 1 189 ? 5.084   25.759 -17.669 1.00 33.06  ? 186 PRO   B N   1 
ATOM   4026 C  CA  . PRO   B 1 189 ? 4.158   26.848 -17.404 1.00 31.02  ? 186 PRO   B CA  1 
ATOM   4027 C  C   . PRO   B 1 189 ? 4.971   28.145 -17.304 1.00 29.93  ? 186 PRO   B C   1 
ATOM   4028 O  O   . PRO   B 1 189 ? 6.000   28.117 -16.674 1.00 30.20  ? 186 PRO   B O   1 
ATOM   4029 C  CB  . PRO   B 1 189 ? 3.529   26.487 -16.049 1.00 30.61  ? 186 PRO   B CB  1 
ATOM   4030 C  CG  . PRO   B 1 189 ? 3.780   24.992 -15.918 1.00 32.71  ? 186 PRO   B CG  1 
ATOM   4031 C  CD  . PRO   B 1 189 ? 5.105   24.740 -16.606 1.00 34.06  ? 186 PRO   B CD  1 
ATOM   4032 N  N   . VAL   B 1 190 ? 4.522   29.236 -17.915 1.00 28.53  ? 187 VAL   B N   1 
ATOM   4033 C  CA  . VAL   B 1 190 ? 5.244   30.536 -17.793 1.00 28.48  ? 187 VAL   B CA  1 
ATOM   4034 C  C   . VAL   B 1 190 ? 4.952   31.141 -16.419 1.00 26.15  ? 187 VAL   B C   1 
ATOM   4035 O  O   . VAL   B 1 190 ? 5.700   32.027 -15.975 1.00 25.36  ? 187 VAL   B O   1 
ATOM   4036 C  CB  . VAL   B 1 190 ? 4.874   31.531 -18.910 1.00 29.20  ? 187 VAL   B CB  1 
ATOM   4037 C  CG1 . VAL   B 1 190 ? 5.315   31.027 -20.269 1.00 30.83  ? 187 VAL   B CG1 1 
ATOM   4038 C  CG2 . VAL   B 1 190 ? 3.390   31.895 -18.884 1.00 27.84  ? 187 VAL   B CG2 1 
ATOM   4039 N  N   . CYS   B 1 191 ? 3.834   30.790 -15.793 1.00 24.50  ? 188 CYS   B N   1 
ATOM   4040 C  CA  . CYS   B 1 191 ? 3.448   31.438 -14.518 1.00 23.83  ? 188 CYS   B CA  1 
ATOM   4041 C  C   . CYS   B 1 191 ? 2.610   30.473 -13.696 1.00 22.51  ? 188 CYS   B C   1 
ATOM   4042 O  O   . CYS   B 1 191 ? 2.059   29.490 -14.258 1.00 22.56  ? 188 CYS   B O   1 
ATOM   4043 C  CB  . CYS   B 1 191 ? 2.642   32.718 -14.719 1.00 23.75  ? 188 CYS   B CB  1 
ATOM   4044 S  SG  . CYS   B 1 191 ? 1.042   32.462 -15.575 1.00 25.12  ? 188 CYS   B SG  1 
ATOM   4045 N  N   . ASN   B 1 192 ? 2.435   30.835 -12.434 1.00 22.08  ? 189 ASN   B N   1 
ATOM   4046 C  CA  . ASN   B 1 192 ? 1.450   30.232 -11.505 1.00 21.66  ? 189 ASN   B CA  1 
ATOM   4047 C  C   . ASN   B 1 192 ? 0.711   31.400 -10.854 1.00 21.32  ? 189 ASN   B C   1 
ATOM   4048 O  O   . ASN   B 1 192 ? 1.349   32.171 -10.093 1.00 20.66  ? 189 ASN   B O   1 
ATOM   4049 C  CB  . ASN   B 1 192 ? 2.120   29.342 -10.472 1.00 22.43  ? 189 ASN   B CB  1 
ATOM   4050 C  CG  . ASN   B 1 192 ? 1.147   28.542 -9.624  1.00 22.43  ? 189 ASN   B CG  1 
ATOM   4051 O  OD1 . ASN   B 1 192 ? -0.026  28.405 -9.965  1.00 22.32  ? 189 ASN   B OD1 1 
ATOM   4052 N  ND2 . ASN   B 1 192 ? 1.633   28.035 -8.492  1.00 22.22  ? 189 ASN   B ND2 1 
ATOM   4053 N  N   . GLN   B 1 193 ? -0.540  31.604 -11.245 1.00 20.69  ? 190 GLN   B N   1 
ATOM   4054 C  CA  . GLN   B 1 193 ? -1.383  32.683 -10.689 1.00 20.24  ? 190 GLN   B CA  1 
ATOM   4055 C  C   . GLN   B 1 193 ? -2.051  32.184 -9.402  1.00 20.03  ? 190 GLN   B C   1 
ATOM   4056 O  O   . GLN   B 1 193 ? -2.874  31.290 -9.441  1.00 20.55  ? 190 GLN   B O   1 
ATOM   4057 C  CB  . GLN   B 1 193 ? -2.399  33.153 -11.731 1.00 20.07  ? 190 GLN   B CB  1 
ATOM   4058 C  CG  . GLN   B 1 193 ? -3.215  34.309 -11.183 1.00 20.82  ? 190 GLN   B CG  1 
ATOM   4059 C  CD  . GLN   B 1 193 ? -4.292  34.875 -12.060 1.00 20.56  ? 190 GLN   B CD  1 
ATOM   4060 O  OE1 . GLN   B 1 193 ? -5.442  34.901 -11.624 1.00 20.81  ? 190 GLN   B OE1 1 
ATOM   4061 N  NE2 . GLN   B 1 193 ? -3.909  35.316 -13.262 1.00 21.11  ? 190 GLN   B NE2 1 
ATOM   4062 N  N   . VAL   B 1 194 ? -1.731  32.810 -8.271  1.00 20.52  ? 191 VAL   B N   1 
ATOM   4063 C  CA  . VAL   B 1 194 ? -2.126  32.266 -6.934  1.00 21.05  ? 191 VAL   B CA  1 
ATOM   4064 C  C   . VAL   B 1 194 ? -2.535  33.423 -6.039  1.00 20.67  ? 191 VAL   B C   1 
ATOM   4065 O  O   . VAL   B 1 194 ? -2.145  34.593 -6.288  1.00 20.26  ? 191 VAL   B O   1 
ATOM   4066 C  CB  . VAL   B 1 194 ? -1.011  31.419 -6.292  1.00 21.68  ? 191 VAL   B CB  1 
ATOM   4067 C  CG1 . VAL   B 1 194 ? -0.609  30.258 -7.194  1.00 22.35  ? 191 VAL   B CG1 1 
ATOM   4068 C  CG2 . VAL   B 1 194 ? 0.209   32.245 -5.958  1.00 22.05  ? 191 VAL   B CG2 1 
ATOM   4069 N  N   . GLU   B 1 195 ? -3.296  33.088 -5.011  1.00 22.04  ? 192 GLU   B N   1 
ATOM   4070 C  CA  . GLU   B 1 195 ? -3.651  34.109 -3.994  1.00 22.90  ? 192 GLU   B CA  1 
ATOM   4071 C  C   . GLU   B 1 195 ? -2.355  34.560 -3.333  1.00 22.68  ? 192 GLU   B C   1 
ATOM   4072 O  O   . GLU   B 1 195 ? -1.579  33.708 -2.841  1.00 22.51  ? 192 GLU   B O   1 
ATOM   4073 C  CB  . GLU   B 1 195 ? -4.680  33.601 -3.003  1.00 24.57  ? 192 GLU   B CB  1 
ATOM   4074 C  CG  . GLU   B 1 195 ? -4.983  34.627 -1.923  1.00 26.28  ? 192 GLU   B CG  1 
ATOM   4075 C  CD  . GLU   B 1 195 ? -5.935  34.118 -0.865  1.00 27.35  ? 192 GLU   B CD  1 
ATOM   4076 O  OE1 . GLU   B 1 195 ? -6.348  32.971 -0.978  1.00 29.08  ? 192 GLU   B OE1 1 
ATOM   4077 O  OE2 . GLU   B 1 195 ? -6.277  34.881 0.034   1.00 28.15  ? 192 GLU   B OE2 1 
ATOM   4078 N  N   . CYS   B 1 196 ? -2.114  35.862 -3.330  1.00 22.49  ? 193 CYS   B N   1 
ATOM   4079 C  CA  . CYS   B 1 196 ? -0.812  36.368 -2.822  1.00 23.25  ? 193 CYS   B CA  1 
ATOM   4080 C  C   . CYS   B 1 196 ? -0.993  37.805 -2.351  1.00 23.85  ? 193 CYS   B C   1 
ATOM   4081 O  O   . CYS   B 1 196 ? -1.322  38.671 -3.170  1.00 23.80  ? 193 CYS   B O   1 
ATOM   4082 C  CB  . CYS   B 1 196 ? 0.280   36.205 -3.871  1.00 23.48  ? 193 CYS   B CB  1 
ATOM   4083 S  SG  . CYS   B 1 196 ? 1.896   36.775 -3.298  1.00 25.52  ? 193 CYS   B SG  1 
ATOM   4084 N  N   . HIS   B 1 197 ? -0.813  38.030 -1.053  1.00 24.04  ? 194 HIS   B N   1 
ATOM   4085 C  CA  . HIS   B 1 197 ? -0.928  39.368 -0.423  1.00 24.56  ? 194 HIS   B CA  1 
ATOM   4086 C  C   . HIS   B 1 197 ? -0.190  39.298 0.903   1.00 25.24  ? 194 HIS   B C   1 
ATOM   4087 O  O   . HIS   B 1 197 ? 0.231   38.208 1.293   1.00 24.94  ? 194 HIS   B O   1 
ATOM   4088 C  CB  . HIS   B 1 197 ? -2.418  39.717 -0.260  1.00 24.77  ? 194 HIS   B CB  1 
ATOM   4089 C  CG  . HIS   B 1 197 ? -3.204  38.613 0.363   1.00 24.53  ? 194 HIS   B CG  1 
ATOM   4090 N  ND1 . HIS   B 1 197 ? -3.066  38.259 1.691   1.00 25.84  ? 194 HIS   B ND1 1 
ATOM   4091 C  CD2 . HIS   B 1 197 ? -4.085  37.739 -0.169  1.00 23.96  ? 194 HIS   B CD2 1 
ATOM   4092 C  CE1 . HIS   B 1 197 ? -3.872  37.247 1.956   1.00 26.11  ? 194 HIS   B CE1 1 
ATOM   4093 N  NE2 . HIS   B 1 197 ? -4.479  36.875 0.811   1.00 24.47  ? 194 HIS   B NE2 1 
ATOM   4094 N  N   . PRO   B 1 198 ? -0.005  40.419 1.629   1.00 26.44  ? 195 PRO   B N   1 
ATOM   4095 C  CA  . PRO   B 1 198 ? 0.794   40.402 2.846   1.00 27.63  ? 195 PRO   B CA  1 
ATOM   4096 C  C   . PRO   B 1 198 ? 0.303   39.466 3.954   1.00 28.38  ? 195 PRO   B C   1 
ATOM   4097 O  O   . PRO   B 1 198 ? 1.104   39.228 4.802   1.00 29.56  ? 195 PRO   B O   1 
ATOM   4098 C  CB  . PRO   B 1 198 ? 0.698   41.858 3.349   1.00 28.68  ? 195 PRO   B CB  1 
ATOM   4099 C  CG  . PRO   B 1 198 ? 0.562   42.635 2.071   1.00 28.81  ? 195 PRO   B CG  1 
ATOM   4100 C  CD  . PRO   B 1 198 ? -0.366  41.788 1.230   1.00 26.89  ? 195 PRO   B CD  1 
ATOM   4101 N  N   . TYR   B 1 199 ? -0.954  38.988 3.950   1.00 28.09  ? 196 TYR   B N   1 
ATOM   4102 C  CA  . TYR   B 1 199 ? -1.446  38.010 4.953   1.00 29.26  ? 196 TYR   B CA  1 
ATOM   4103 C  C   . TYR   B 1 199 ? -1.184  36.563 4.501   1.00 28.29  ? 196 TYR   B C   1 
ATOM   4104 O  O   . TYR   B 1 199 ? -1.344  35.610 5.296   1.00 28.84  ? 196 TYR   B O   1 
ATOM   4105 C  CB  . TYR   B 1 199 ? -2.901  38.284 5.290   1.00 30.92  ? 196 TYR   B CB  1 
ATOM   4106 C  CG  . TYR   B 1 199 ? -3.165  39.597 5.973   1.00 33.27  ? 196 TYR   B CG  1 
ATOM   4107 C  CD1 . TYR   B 1 199 ? -2.177  40.289 6.666   1.00 34.83  ? 196 TYR   B CD1 1 
ATOM   4108 C  CD2 . TYR   B 1 199 ? -4.454  40.081 6.014   1.00 34.89  ? 196 TYR   B CD2 1 
ATOM   4109 C  CE1 . TYR   B 1 199 ? -2.453  41.461 7.347   1.00 36.80  ? 196 TYR   B CE1 1 
ATOM   4110 C  CE2 . TYR   B 1 199 ? -4.761  41.231 6.712   1.00 37.15  ? 196 TYR   B CE2 1 
ATOM   4111 C  CZ  . TYR   B 1 199 ? -3.753  41.935 7.354   1.00 38.11  ? 196 TYR   B CZ  1 
ATOM   4112 O  OH  . TYR   B 1 199 ? -4.073  43.083 8.001   1.00 40.29  ? 196 TYR   B OH  1 
ATOM   4113 N  N   . PHE   B 1 200 ? -0.722  36.397 3.271   1.00 26.58  ? 197 PHE   B N   1 
ATOM   4114 C  CA  . PHE   B 1 200 ? -0.407  35.093 2.655   1.00 26.31  ? 197 PHE   B CA  1 
ATOM   4115 C  C   . PHE   B 1 200 ? 0.586   35.342 1.517   1.00 25.47  ? 197 PHE   B C   1 
ATOM   4116 O  O   . PHE   B 1 200 ? 0.196   35.357 0.325   1.00 24.06  ? 197 PHE   B O   1 
ATOM   4117 C  CB  . PHE   B 1 200 ? -1.728  34.483 2.181   1.00 26.95  ? 197 PHE   B CB  1 
ATOM   4118 C  CG  . PHE   B 1 200 ? -1.671  33.047 1.732   1.00 27.57  ? 197 PHE   B CG  1 
ATOM   4119 C  CD1 . PHE   B 1 200 ? -0.727  32.170 2.236   1.00 28.43  ? 197 PHE   B CD1 1 
ATOM   4120 C  CD2 . PHE   B 1 200 ? -2.608  32.587 0.813   1.00 28.57  ? 197 PHE   B CD2 1 
ATOM   4121 C  CE1 . PHE   B 1 200 ? -0.722  30.845 1.826   1.00 29.81  ? 197 PHE   B CE1 1 
ATOM   4122 C  CE2 . PHE   B 1 200 ? -2.598  31.262 0.406   1.00 29.48  ? 197 PHE   B CE2 1 
ATOM   4123 C  CZ  . PHE   B 1 200 ? -1.677  30.393 0.952   1.00 29.00  ? 197 PHE   B CZ  1 
ATOM   4124 N  N   . ASN   B 1 201 ? 1.848   35.537 1.847   1.00 25.55  ? 198 ASN   B N   1 
ATOM   4125 C  CA  . ASN   B 1 201 ? 2.810   36.175 0.912   1.00 25.35  ? 198 ASN   B CA  1 
ATOM   4126 C  C   . ASN   B 1 201 ? 3.464   35.116 0.019   1.00 25.25  ? 198 ASN   B C   1 
ATOM   4127 O  O   . ASN   B 1 201 ? 4.128   35.509 -0.988  1.00 25.97  ? 198 ASN   B O   1 
ATOM   4128 C  CB  . ASN   B 1 201 ? 3.757   37.120 1.653   1.00 26.18  ? 198 ASN   B CB  1 
ATOM   4129 C  CG  . ASN   B 1 201 ? 4.846   36.431 2.433   1.00 27.14  ? 198 ASN   B CG  1 
ATOM   4130 O  OD1 . ASN   B 1 201 ? 5.235   35.300 2.113   1.00 26.48  ? 198 ASN   B OD1 1 
ATOM   4131 N  ND2 . ASN   B 1 201 ? 5.355   37.132 3.451   1.00 27.21  ? 198 ASN   B ND2 1 
ATOM   4132 N  N   . ARG   B 1 202 ? 3.239   33.837 0.351   1.00 25.27  ? 199 ARG   B N   1 
ATOM   4133 C  CA  . ARG   B 1 202 ? 3.717   32.680 -0.456  1.00 25.53  ? 199 ARG   B CA  1 
ATOM   4134 C  C   . ARG   B 1 202 ? 5.218   32.809 -0.719  1.00 26.55  ? 199 ARG   B C   1 
ATOM   4135 O  O   . ARG   B 1 202 ? 5.630   32.609 -1.879  1.00 25.69  ? 199 ARG   B O   1 
ATOM   4136 C  CB  . ARG   B 1 202 ? 2.936   32.590 -1.771  1.00 25.07  ? 199 ARG   B CB  1 
ATOM   4137 C  CG  . ARG   B 1 202 ? 1.511   33.117 -1.686  1.00 24.94  ? 199 ARG   B CG  1 
ATOM   4138 C  CD  . ARG   B 1 202 ? 0.585   32.169 -0.947  1.00 25.34  ? 199 ARG   B CD  1 
ATOM   4139 N  NE  . ARG   B 1 202 ? 0.652   30.811 -1.467  1.00 26.17  ? 199 ARG   B NE  1 
ATOM   4140 C  CZ  . ARG   B 1 202 ? -0.257  30.266 -2.267  1.00 25.79  ? 199 ARG   B CZ  1 
ATOM   4141 N  NH1 . ARG   B 1 202 ? -1.312  30.967 -2.644  1.00 25.35  ? 199 ARG   B NH1 1 
ATOM   4142 N  NH2 . ARG   B 1 202 ? -0.108  29.022 -2.687  1.00 26.05  ? 199 ARG   B NH2 1 
ATOM   4143 N  N   . SER   B 1 203 ? 6.001   33.132 0.313   1.00 27.00  ? 200 SER   B N   1 
ATOM   4144 C  CA  . SER   B 1 203 ? 7.463   33.325 0.094   1.00 28.19  ? 200 SER   B CA  1 
ATOM   4145 C  C   . SER   B 1 203 ? 8.125   32.021 -0.371  1.00 29.43  ? 200 SER   B C   1 
ATOM   4146 O  O   . SER   B 1 203 ? 8.981   32.095 -1.245  1.00 30.08  ? 200 SER   B O   1 
ATOM   4147 C  CB  . SER   B 1 203 ? 8.178   33.869 1.274   1.00 29.49  ? 200 SER   B CB  1 
ATOM   4148 O  OG  . SER   B 1 203 ? 7.914   33.031 2.377   1.00 31.44  ? 200 SER   B OG  1 
ATOM   4149 N  N   . LYS   B 1 204 ? 7.808   30.865 0.203   1.00 30.39  ? 201 LYS   B N   1 
ATOM   4150 C  CA  . LYS   B 1 204 ? 8.487   29.605 -0.219  1.00 32.00  ? 201 LYS   B CA  1 
ATOM   4151 C  C   . LYS   B 1 204 ? 8.081   29.211 -1.646  1.00 30.73  ? 201 LYS   B C   1 
ATOM   4152 O  O   . LYS   B 1 204 ? 8.951   28.797 -2.421  1.00 30.75  ? 201 LYS   B O   1 
ATOM   4153 C  CB  . LYS   B 1 204 ? 8.176   28.473 0.761   1.00 34.61  ? 201 LYS   B CB  1 
ATOM   4154 C  CG  . LYS   B 1 204 ? 8.821   28.700 2.118   1.00 36.49  ? 201 LYS   B CG  1 
ATOM   4155 C  CD  . LYS   B 1 204 ? 8.294   27.714 3.102   1.00 39.14  ? 201 LYS   B CD  1 
ATOM   4156 C  CE  . LYS   B 1 204 ? 8.968   27.821 4.454   1.00 42.64  ? 201 LYS   B CE  1 
ATOM   4157 N  NZ  . LYS   B 1 204 ? 8.745   26.571 5.211   1.00 44.70  ? 201 LYS   B NZ  1 
ATOM   4158 N  N   . LEU   B 1 205 ? 6.804   29.309 -1.983  1.00 29.08  ? 202 LEU   B N   1 
ATOM   4159 C  CA  . LEU   B 1 205 ? 6.339   28.960 -3.356  1.00 28.37  ? 202 LEU   B CA  1 
ATOM   4160 C  C   . LEU   B 1 205 ? 6.959   29.937 -4.365  1.00 27.96  ? 202 LEU   B C   1 
ATOM   4161 O  O   . LEU   B 1 205 ? 7.343   29.520 -5.462  1.00 28.22  ? 202 LEU   B O   1 
ATOM   4162 C  CB  . LEU   B 1 205 ? 4.823   29.084 -3.434  1.00 27.09  ? 202 LEU   B CB  1 
ATOM   4163 C  CG  . LEU   B 1 205 ? 4.248   28.788 -4.812  1.00 26.61  ? 202 LEU   B CG  1 
ATOM   4164 C  CD1 . LEU   B 1 205 ? 4.572   27.358 -5.208  1.00 27.27  ? 202 LEU   B CD1 1 
ATOM   4165 C  CD2 . LEU   B 1 205 ? 2.756   29.002 -4.792  1.00 26.06  ? 202 LEU   B CD2 1 
ATOM   4166 N  N   . LEU   B 1 206 ? 7.097   31.200 -3.964  1.00 27.35  ? 203 LEU   B N   1 
ATOM   4167 C  CA  . LEU   B 1 206 ? 7.735   32.221 -4.818  1.00 28.04  ? 203 LEU   B CA  1 
ATOM   4168 C  C   . LEU   B 1 206 ? 9.174   31.820 -5.114  1.00 29.87  ? 203 LEU   B C   1 
ATOM   4169 O  O   . LEU   B 1 206 ? 9.586   31.912 -6.277  1.00 30.22  ? 203 LEU   B O   1 
ATOM   4170 C  CB  . LEU   B 1 206 ? 7.674   33.596 -4.137  1.00 26.99  ? 203 LEU   B CB  1 
ATOM   4171 C  CG  . LEU   B 1 206 ? 8.412   34.708 -4.881  1.00 26.95  ? 203 LEU   B CG  1 
ATOM   4172 C  CD1 . LEU   B 1 206 ? 7.765   34.904 -6.239  1.00 25.87  ? 203 LEU   B CD1 1 
ATOM   4173 C  CD2 . LEU   B 1 206 ? 8.410   35.978 -4.047  1.00 26.53  ? 203 LEU   B CD2 1 
ATOM   4174 N  N   . ASP   B 1 207 ? 9.925   31.426 -4.089  1.00 31.95  ? 204 ASP   B N   1 
ATOM   4175 C  CA  . ASP   B 1 207 ? 11.355  31.043 -4.273  1.00 35.03  ? 204 ASP   B CA  1 
ATOM   4176 C  C   . ASP   B 1 207 ? 11.452  29.810 -5.178  1.00 34.16  ? 204 ASP   B C   1 
ATOM   4177 O  O   . ASP   B 1 207 ? 12.373  29.732 -6.036  1.00 34.79  ? 204 ASP   B O   1 
ATOM   4178 C  CB  . ASP   B 1 207 ? 11.998  30.729 -2.925  1.00 38.02  ? 204 ASP   B CB  1 
ATOM   4179 C  CG  . ASP   B 1 207 ? 12.377  31.978 -2.156  1.00 40.98  ? 204 ASP   B CG  1 
ATOM   4180 O  OD1 . ASP   B 1 207 ? 12.551  33.029 -2.799  1.00 43.13  ? 204 ASP   B OD1 1 
ATOM   4181 O  OD2 . ASP   B 1 207 ? 12.569  31.868 -0.931  1.00 44.63  ? 204 ASP   B OD2 1 
ATOM   4182 N  N   . PHE   B 1 208 ? 10.563  28.843 -4.945  1.00 33.46  ? 205 PHE   B N   1 
ATOM   4183 C  CA  . PHE   B 1 208 ? 10.457  27.633 -5.799  1.00 33.61  ? 205 PHE   B CA  1 
ATOM   4184 C  C   . PHE   B 1 208 ? 10.211  28.083 -7.246  1.00 32.51  ? 205 PHE   B C   1 
ATOM   4185 O  O   . PHE   B 1 208 ? 10.929  27.681 -8.147  1.00 32.69  ? 205 PHE   B O   1 
ATOM   4186 C  CB  . PHE   B 1 208 ? 9.344   26.714 -5.323  1.00 33.42  ? 205 PHE   B CB  1 
ATOM   4187 C  CG  . PHE   B 1 208 ? 9.149   25.567 -6.274  1.00 34.85  ? 205 PHE   B CG  1 
ATOM   4188 C  CD1 . PHE   B 1 208 ? 10.085  24.531 -6.293  1.00 37.00  ? 205 PHE   B CD1 1 
ATOM   4189 C  CD2 . PHE   B 1 208 ? 8.125   25.584 -7.210  1.00 34.15  ? 205 PHE   B CD2 1 
ATOM   4190 C  CE1 . PHE   B 1 208 ? 9.933   23.483 -7.185  1.00 38.53  ? 205 PHE   B CE1 1 
ATOM   4191 C  CE2 . PHE   B 1 208 ? 7.986   24.534 -8.102  1.00 35.42  ? 205 PHE   B CE2 1 
ATOM   4192 C  CZ  . PHE   B 1 208 ? 8.890   23.496 -8.092  1.00 37.25  ? 205 PHE   B CZ  1 
ATOM   4193 N  N   . CYS   B 1 209 ? 9.212   28.931 -7.452  1.00 31.20  ? 206 CYS   B N   1 
ATOM   4194 C  CA  . CYS   B 1 209 ? 8.852   29.415 -8.816  1.00 30.70  ? 206 CYS   B CA  1 
ATOM   4195 C  C   . CYS   B 1 209 ? 10.046  30.119 -9.457  1.00 32.05  ? 206 CYS   B C   1 
ATOM   4196 O  O   . CYS   B 1 209 ? 10.353  29.795 -10.615 1.00 31.67  ? 206 CYS   B O   1 
ATOM   4197 C  CB  . CYS   B 1 209 ? 7.642   30.323 -8.796  1.00 29.65  ? 206 CYS   B CB  1 
ATOM   4198 S  SG  . CYS   B 1 209 ? 6.115   29.374 -8.600  1.00 30.23  ? 206 CYS   B SG  1 
ATOM   4199 N  N   . LYS   B 1 210 ? 10.675  31.057 -8.752  1.00 33.13  ? 207 LYS   B N   1 
ATOM   4200 C  CA  . LYS   B 1 210 ? 11.896  31.720 -9.264  1.00 35.95  ? 207 LYS   B CA  1 
ATOM   4201 C  C   . LYS   B 1 210 ? 12.917  30.664 -9.707  1.00 38.27  ? 207 LYS   B C   1 
ATOM   4202 O  O   . LYS   B 1 210 ? 13.489  30.854 -10.782 1.00 39.82  ? 207 LYS   B O   1 
ATOM   4203 C  CB  . LYS   B 1 210 ? 12.504  32.660 -8.232  1.00 38.46  ? 207 LYS   B CB  1 
ATOM   4204 C  CG  . LYS   B 1 210 ? 11.728  33.952 -8.072  1.00 38.84  ? 207 LYS   B CG  1 
ATOM   4205 C  CD  . LYS   B 1 210 ? 12.240  34.795 -6.937  1.00 41.62  ? 207 LYS   B CD  1 
ATOM   4206 C  CE  . LYS   B 1 210 ? 11.881  36.242 -7.186  1.00 42.44  ? 207 LYS   B CE  1 
ATOM   4207 N  NZ  . LYS   B 1 210 ? 11.791  36.993 -5.924  1.00 44.09  ? 207 LYS   B NZ  1 
ATOM   4208 N  N   . SER   B 1 211 ? 13.112  29.586 -8.942  1.00 37.58  ? 208 SER   B N   1 
ATOM   4209 C  CA  . SER   B 1 211 ? 14.185  28.603 -9.209  1.00 39.89  ? 208 SER   B CA  1 
ATOM   4210 C  C   . SER   B 1 211 ? 13.884  27.881 -10.525 1.00 40.49  ? 208 SER   B C   1 
ATOM   4211 O  O   . SER   B 1 211 ? 14.809  27.334 -11.083 1.00 42.27  ? 208 SER   B O   1 
ATOM   4212 C  CB  . SER   B 1 211 ? 14.394  27.627 -8.066  1.00 40.24  ? 208 SER   B CB  1 
ATOM   4213 O  OG  . SER   B 1 211 ? 13.294  26.746 -7.911  1.00 38.12  ? 208 SER   B OG  1 
ATOM   4214 N  N   . LYS   B 1 212 ? 12.613  27.840 -10.944 1.00 39.46  ? 209 LYS   B N   1 
ATOM   4215 C  CA  . LYS   B 1 212 ? 12.176  27.154 -12.190 1.00 39.88  ? 209 LYS   B CA  1 
ATOM   4216 C  C   . LYS   B 1 212 ? 11.843  28.165 -13.290 1.00 39.40  ? 209 LYS   B C   1 
ATOM   4217 O  O   . LYS   B 1 212 ? 11.322  27.741 -14.308 1.00 39.83  ? 209 LYS   B O   1 
ATOM   4218 C  CB  . LYS   B 1 212 ? 10.973  26.274 -11.870 1.00 38.90  ? 209 LYS   B CB  1 
ATOM   4219 C  CG  . LYS   B 1 212 ? 11.199  25.283 -10.748 1.00 40.23  ? 209 LYS   B CG  1 
ATOM   4220 C  CD  . LYS   B 1 212 ? 12.280  24.270 -11.012 1.00 42.92  ? 209 LYS   B CD  1 
ATOM   4221 C  CE  . LYS   B 1 212 ? 12.266  23.192 -9.951  1.00 43.85  ? 209 LYS   B CE  1 
ATOM   4222 N  NZ  . LYS   B 1 212 ? 13.469  22.332 -10.034 1.00 47.23  ? 209 LYS   B NZ  1 
ATOM   4223 N  N   . ASP   B 1 213 ? 12.158  29.447 -13.101 1.00 39.45  ? 210 ASP   B N   1 
ATOM   4224 C  CA  . ASP   B 1 213 ? 11.829  30.570 -14.033 1.00 40.39  ? 210 ASP   B CA  1 
ATOM   4225 C  C   . ASP   B 1 213 ? 10.327  30.586 -14.338 1.00 36.78  ? 210 ASP   B C   1 
ATOM   4226 O  O   . ASP   B 1 213 ? 9.917   30.831 -15.497 1.00 36.22  ? 210 ASP   B O   1 
ATOM   4227 C  CB  . ASP   B 1 213 ? 12.639  30.569 -15.341 1.00 43.85  ? 210 ASP   B CB  1 
ATOM   4228 C  CG  . ASP   B 1 213 ? 12.610  31.925 -16.055 1.00 46.49  ? 210 ASP   B CG  1 
ATOM   4229 O  OD1 . ASP   B 1 213 ? 12.401  32.974 -15.366 1.00 48.15  ? 210 ASP   B OD1 1 
ATOM   4230 O  OD2 . ASP   B 1 213 ? 12.809  31.959 -17.302 1.00 50.36  ? 210 ASP   B OD2 1 
ATOM   4231 N  N   . ILE   B 1 214 ? 9.518   30.311 -13.329 1.00 33.88  ? 211 ILE   B N   1 
ATOM   4232 C  CA  . ILE   B 1 214 ? 8.043   30.477 -13.399 1.00 31.23  ? 211 ILE   B CA  1 
ATOM   4233 C  C   . ILE   B 1 214 ? 7.718   31.765 -12.652 1.00 30.29  ? 211 ILE   B C   1 
ATOM   4234 O  O   . ILE   B 1 214 ? 8.204   31.954 -11.508 1.00 30.53  ? 211 ILE   B O   1 
ATOM   4235 C  CB  . ILE   B 1 214 ? 7.293   29.291 -12.799 1.00 30.37  ? 211 ILE   B CB  1 
ATOM   4236 C  CG1 . ILE   B 1 214 ? 7.618   27.985 -13.521 1.00 31.29  ? 211 ILE   B CG1 1 
ATOM   4237 C  CG2 . ILE   B 1 214 ? 5.810   29.586 -12.821 1.00 28.92  ? 211 ILE   B CG2 1 
ATOM   4238 C  CD1 . ILE   B 1 214 ? 7.298   26.782 -12.692 1.00 31.28  ? 211 ILE   B CD1 1 
ATOM   4239 N  N   . VAL   B 1 215 ? 6.947   32.627 -13.299 1.00 28.84  ? 212 VAL   B N   1 
ATOM   4240 C  CA  . VAL   B 1 215 ? 6.472   33.892 -12.694 1.00 27.33  ? 212 VAL   B CA  1 
ATOM   4241 C  C   . VAL   B 1 215 ? 5.359   33.570 -11.713 1.00 25.68  ? 212 VAL   B C   1 
ATOM   4242 O  O   . VAL   B 1 215 ? 4.381   32.908 -12.122 1.00 24.43  ? 212 VAL   B O   1 
ATOM   4243 C  CB  . VAL   B 1 215 ? 5.977   34.880 -13.764 1.00 27.80  ? 212 VAL   B CB  1 
ATOM   4244 C  CG1 . VAL   B 1 215 ? 5.301   36.075 -13.110 1.00 26.98  ? 212 VAL   B CG1 1 
ATOM   4245 C  CG2 . VAL   B 1 215 ? 7.132   35.316 -14.663 1.00 29.29  ? 212 VAL   B CG2 1 
ATOM   4246 N  N   . LEU   B 1 216 ? 5.449   34.093 -10.488 1.00 24.51  ? 213 LEU   B N   1 
ATOM   4247 C  CA  . LEU   B 1 216 ? 4.259   34.070 -9.603  1.00 23.80  ? 213 LEU   B CA  1 
ATOM   4248 C  C   . LEU   B 1 216 ? 3.388   35.291 -9.937  1.00 23.15  ? 213 LEU   B C   1 
ATOM   4249 O  O   . LEU   B 1 216 ? 3.901   36.386 -9.911  1.00 22.48  ? 213 LEU   B O   1 
ATOM   4250 C  CB  . LEU   B 1 216 ? 4.704   34.028 -8.133  1.00 24.31  ? 213 LEU   B CB  1 
ATOM   4251 C  CG  . LEU   B 1 216 ? 3.627   33.534 -7.178  1.00 24.75  ? 213 LEU   B CG  1 
ATOM   4252 C  CD1 . LEU   B 1 216 ? 4.249   32.933 -5.929  1.00 27.10  ? 213 LEU   B CD1 1 
ATOM   4253 C  CD2 . LEU   B 1 216 ? 2.669   34.646 -6.776  1.00 24.89  ? 213 LEU   B CD2 1 
ATOM   4254 N  N   . VAL   B 1 217 ? 2.097   35.103 -10.176 1.00 21.91  ? 214 VAL   B N   1 
ATOM   4255 C  CA  . VAL   B 1 217 ? 1.145   36.224 -10.430 1.00 22.17  ? 214 VAL   B CA  1 
ATOM   4256 C  C   . VAL   B 1 217 ? 0.165   36.274 -9.266  1.00 21.53  ? 214 VAL   B C   1 
ATOM   4257 O  O   . VAL   B 1 217 ? -0.439  35.228 -8.940  1.00 22.22  ? 214 VAL   B O   1 
ATOM   4258 C  CB  . VAL   B 1 217 ? 0.411   36.014 -11.763 1.00 22.57  ? 214 VAL   B CB  1 
ATOM   4259 C  CG1 . VAL   B 1 217 ? -0.605  37.115 -12.017 1.00 22.43  ? 214 VAL   B CG1 1 
ATOM   4260 C  CG2 . VAL   B 1 217 ? 1.399   35.929 -12.917 1.00 23.92  ? 214 VAL   B CG2 1 
ATOM   4261 N  N   . ALA   B 1 218 ? 0.114   37.416 -8.581  1.00 21.14  ? 215 ALA   B N   1 
ATOM   4262 C  CA  . ALA   B 1 218 ? -0.687  37.602 -7.360  1.00 20.54  ? 215 ALA   B CA  1 
ATOM   4263 C  C   . ALA   B 1 218 ? -2.118  38.001 -7.709  1.00 20.61  ? 215 ALA   B C   1 
ATOM   4264 O  O   . ALA   B 1 218 ? -2.331  39.037 -8.376  1.00 20.79  ? 215 ALA   B O   1 
ATOM   4265 C  CB  . ALA   B 1 218 ? 0.002   38.631 -6.508  1.00 20.99  ? 215 ALA   B CB  1 
ATOM   4266 N  N   . TYR   B 1 219 ? -3.087  37.205 -7.264  1.00 20.11  ? 216 TYR   B N   1 
ATOM   4267 C  CA  . TYR   B 1 219 ? -4.487  37.679 -7.172  1.00 20.37  ? 216 TYR   B CA  1 
ATOM   4268 C  C   . TYR   B 1 219 ? -4.871  37.940 -5.705  1.00 20.88  ? 216 TYR   B C   1 
ATOM   4269 O  O   . TYR   B 1 219 ? -4.232  37.422 -4.797  1.00 21.04  ? 216 TYR   B O   1 
ATOM   4270 C  CB  . TYR   B 1 219 ? -5.470  36.743 -7.867  1.00 20.47  ? 216 TYR   B CB  1 
ATOM   4271 C  CG  . TYR   B 1 219 ? -5.802  35.427 -7.218  1.00 20.95  ? 216 TYR   B CG  1 
ATOM   4272 C  CD1 . TYR   B 1 219 ? -6.646  35.370 -6.129  1.00 21.84  ? 216 TYR   B CD1 1 
ATOM   4273 C  CD2 . TYR   B 1 219 ? -5.415  34.233 -7.817  1.00 21.43  ? 216 TYR   B CD2 1 
ATOM   4274 C  CE1 . TYR   B 1 219 ? -7.018  34.155 -5.585  1.00 22.59  ? 216 TYR   B CE1 1 
ATOM   4275 C  CE2 . TYR   B 1 219 ? -5.748  33.000 -7.264  1.00 21.97  ? 216 TYR   B CE2 1 
ATOM   4276 C  CZ  . TYR   B 1 219 ? -6.553  32.961 -6.145  1.00 22.55  ? 216 TYR   B CZ  1 
ATOM   4277 O  OH  . TYR   B 1 219 ? -6.950  31.761 -5.641  1.00 23.41  ? 216 TYR   B OH  1 
ATOM   4278 N  N   . SER   B 1 220 ? -5.928  38.720 -5.527  1.00 21.68  ? 217 SER   B N   1 
ATOM   4279 C  CA  . SER   B 1 220 ? -6.407  39.254 -4.230  1.00 23.60  ? 217 SER   B CA  1 
ATOM   4280 C  C   . SER   B 1 220 ? -5.241  39.967 -3.559  1.00 24.16  ? 217 SER   B C   1 
ATOM   4281 O  O   . SER   B 1 220 ? -5.137  39.896 -2.308  1.00 24.30  ? 217 SER   B O   1 
ATOM   4282 C  CB  . SER   B 1 220 ? -6.968  38.139 -3.378  1.00 24.44  ? 217 SER   B CB  1 
ATOM   4283 O  OG  . SER   B 1 220 ? -8.096  37.561 -4.050  1.00 22.97  ? 217 SER   B OG  1 
ATOM   4284 N  N   . ALA   B 1 221 ? -4.388  40.618 -4.361  1.00 23.83  ? 218 ALA   B N   1 
ATOM   4285 C  CA  . ALA   B 1 221 ? -3.192  41.318 -3.836  1.00 24.49  ? 218 ALA   B CA  1 
ATOM   4286 C  C   . ALA   B 1 221 ? -3.653  42.460 -2.940  1.00 25.74  ? 218 ALA   B C   1 
ATOM   4287 O  O   . ALA   B 1 221 ? -2.850  42.982 -2.200  1.00 26.29  ? 218 ALA   B O   1 
ATOM   4288 C  CB  . ALA   B 1 221 ? -2.340  41.835 -4.973  1.00 24.72  ? 218 ALA   B CB  1 
ATOM   4289 N  N   . LEU   B 1 222 ? -4.900  42.900 -3.062  1.00 25.98  ? 219 LEU   B N   1 
ATOM   4290 C  CA  . LEU   B 1 222 ? -5.402  44.029 -2.237  1.00 27.53  ? 219 LEU   B CA  1 
ATOM   4291 C  C   . LEU   B 1 222 ? -6.373  43.506 -1.188  1.00 28.00  ? 219 LEU   B C   1 
ATOM   4292 O  O   . LEU   B 1 222 ? -7.082  44.333 -0.623  1.00 29.68  ? 219 LEU   B O   1 
ATOM   4293 C  CB  . LEU   B 1 222 ? -6.100  45.057 -3.125  1.00 27.88  ? 219 LEU   B CB  1 
ATOM   4294 C  CG  . LEU   B 1 222 ? -5.253  45.633 -4.265  1.00 27.55  ? 219 LEU   B CG  1 
ATOM   4295 C  CD1 . LEU   B 1 222 ? -6.060  46.673 -5.058  1.00 28.51  ? 219 LEU   B CD1 1 
ATOM   4296 C  CD2 . LEU   B 1 222 ? -3.981  46.260 -3.744  1.00 28.55  ? 219 LEU   B CD2 1 
ATOM   4297 N  N   . GLY   B 1 223 ? -6.385  42.190 -0.992  1.00 27.02  ? 220 GLY   B N   1 
ATOM   4298 C  CA  . GLY   B 1 223 ? -7.096  41.516 0.097   1.00 27.62  ? 220 GLY   B CA  1 
ATOM   4299 C  C   . GLY   B 1 223 ? -8.501  41.116 -0.245  1.00 27.77  ? 220 GLY   B C   1 
ATOM   4300 O  O   . GLY   B 1 223 ? -9.270  40.807 0.684   1.00 29.24  ? 220 GLY   B O   1 
ATOM   4301 N  N   . SER   B 1 224 ? -8.792  40.976 -1.530  1.00 27.65  ? 221 SER   B N   1 
ATOM   4302 C  CA  . SER   B 1 224 ? -10.093 40.491 -2.065  1.00 27.61  ? 221 SER   B CA  1 
ATOM   4303 C  C   . SER   B 1 224 ? -11.211 41.531 -1.982  1.00 28.92  ? 221 SER   B C   1 
ATOM   4304 O  O   . SER   B 1 224 ? -11.101 42.547 -1.295  1.00 29.52  ? 221 SER   B O   1 
ATOM   4305 C  CB  . SER   B 1 224 ? -10.521 39.245 -1.355  1.00 27.92  ? 221 SER   B CB  1 
ATOM   4306 O  OG  . SER   B 1 224 ? -11.255 39.543 -0.194  1.00 29.51  ? 221 SER   B OG  1 
ATOM   4307 N  N   . GLN   B 1 225 ? -12.305 41.198 -2.659  1.00 29.30  ? 222 GLN   B N   1 
ATOM   4308 C  CA  . GLN   B 1 225 ? -13.552 41.988 -2.774  1.00 31.37  ? 222 GLN   B CA  1 
ATOM   4309 C  C   . GLN   B 1 225 ? -14.367 41.738 -1.498  1.00 34.32  ? 222 GLN   B C   1 
ATOM   4310 O  O   . GLN   B 1 225 ? -15.435 42.347 -1.340  1.00 36.21  ? 222 GLN   B O   1 
ATOM   4311 C  CB  . GLN   B 1 225 ? -14.254 41.585 -4.083  1.00 30.30  ? 222 GLN   B CB  1 
ATOM   4312 C  CG  . GLN   B 1 225 ? -13.372 41.813 -5.309  1.00 28.38  ? 222 GLN   B CG  1 
ATOM   4313 C  CD  . GLN   B 1 225 ? -14.085 42.005 -6.624  1.00 28.22  ? 222 GLN   B CD  1 
ATOM   4314 O  OE1 . GLN   B 1 225 ? -15.171 42.587 -6.691  1.00 30.99  ? 222 GLN   B OE1 1 
ATOM   4315 N  NE2 . GLN   B 1 225 ? -13.479 41.485 -7.685  1.00 27.53  ? 222 GLN   B NE2 1 
ATOM   4316 N  N   . ARG   B 1 226 ? -13.926 40.793 -0.675  1.00 34.87  ? 223 ARG   B N   1 
ATOM   4317 C  CA  . ARG   B 1 226 ? -14.615 40.423 0.589   1.00 38.04  ? 223 ARG   B CA  1 
ATOM   4318 C  C   . ARG   B 1 226 ? -16.086 40.082 0.303   1.00 40.32  ? 223 ARG   B C   1 
ATOM   4319 O  O   . ARG   B 1 226 ? -16.936 40.384 1.093   1.00 41.61  ? 223 ARG   B O   1 
ATOM   4320 C  CB  . ARG   B 1 226 ? -14.425 41.567 1.594   1.00 39.49  ? 223 ARG   B CB  1 
ATOM   4321 C  CG  . ARG   B 1 226 ? -12.966 41.911 1.873   1.00 38.09  ? 223 ARG   B CG  1 
ATOM   4322 C  CD  . ARG   B 1 226 ? -12.871 42.925 3.004   1.00 40.25  ? 223 ARG   B CD  1 
ATOM   4323 N  NE  . ARG   B 1 226 ? -13.403 42.401 4.257   1.00 42.30  ? 223 ARG   B NE  1 
ATOM   4324 C  CZ  . ARG   B 1 226 ? -12.762 41.560 5.083   1.00 41.84  ? 223 ARG   B CZ  1 
ATOM   4325 N  NH1 . ARG   B 1 226 ? -11.542 41.133 4.804   1.00 39.68  ? 223 ARG   B NH1 1 
ATOM   4326 N  NH2 . ARG   B 1 226 ? -13.346 41.143 6.193   1.00 43.83  ? 223 ARG   B NH2 1 
ATOM   4327 N  N   . ASP   B 1 227 ? -16.381 39.440 -0.815  1.00 42.68  ? 224 ASP   B N   1 
ATOM   4328 C  CA  . ASP   B 1 227 ? -17.757 38.970 -1.092  1.00 46.45  ? 224 ASP   B CA  1 
ATOM   4329 C  C   . ASP   B 1 227 ? -18.156 37.931 -0.032  1.00 48.05  ? 224 ASP   B C   1 
ATOM   4330 O  O   . ASP   B 1 227 ? -17.419 36.939 0.116   1.00 45.29  ? 224 ASP   B O   1 
ATOM   4331 C  CB  . ASP   B 1 227 ? -17.853 38.395 -2.507  1.00 47.84  ? 224 ASP   B CB  1 
ATOM   4332 C  CG  . ASP   B 1 227 ? -19.291 38.039 -2.819  1.00 52.74  ? 224 ASP   B CG  1 
ATOM   4333 O  OD1 . ASP   B 1 227 ? -19.861 37.256 -2.032  1.00 56.35  ? 224 ASP   B OD1 1 
ATOM   4334 O  OD2 . ASP   B 1 227 ? -19.851 38.607 -3.792  1.00 56.63  ? 224 ASP   B OD2 1 
ATOM   4335 N  N   . LYS   B 1 228 ? -19.343 38.099 0.548   1.00 51.99  ? 225 LYS   B N   1 
ATOM   4336 C  CA  . LYS   B 1 228 ? -19.869 37.300 1.685   1.00 56.86  ? 225 LYS   B CA  1 
ATOM   4337 C  C   . LYS   B 1 228 ? -19.872 35.810 1.356   1.00 54.78  ? 225 LYS   B C   1 
ATOM   4338 O  O   . LYS   B 1 228 ? -19.653 35.008 2.261   1.00 55.47  ? 225 LYS   B O   1 
ATOM   4339 C  CB  . LYS   B 1 228 ? -21.364 37.600 1.846   1.00 63.06  ? 225 LYS   B CB  1 
ATOM   4340 C  CG  . LYS   B 1 228 ? -21.757 38.761 2.745   1.00 68.42  ? 225 LYS   B CG  1 
ATOM   4341 C  CD  . LYS   B 1 228 ? -23.257 38.956 2.810   1.00 74.21  ? 225 LYS   B CD  1 
ATOM   4342 C  CE  . LYS   B 1 228 ? -23.722 39.669 4.060   1.00 79.97  ? 225 LYS   B CE  1 
ATOM   4343 N  NZ  . LYS   B 1 228 ? -22.763 39.493 5.174   1.00 82.42  ? 225 LYS   B NZ  1 
ATOM   4344 N  N   . ARG   B 1 229 ? -20.139 35.467 0.103   1.00 52.70  ? 226 ARG   B N   1 
ATOM   4345 C  CA  . ARG   B 1 229 ? -20.315 34.057 -0.303  1.00 52.32  ? 226 ARG   B CA  1 
ATOM   4346 C  C   . ARG   B 1 229 ? -18.992 33.323 -0.165  1.00 48.38  ? 226 ARG   B C   1 
ATOM   4347 O  O   . ARG   B 1 229 ? -19.035 32.101 -0.051  1.00 47.76  ? 226 ARG   B O   1 
ATOM   4348 C  CB  . ARG   B 1 229 ? -20.798 33.962 -1.752  1.00 54.73  ? 226 ARG   B CB  1 
ATOM   4349 C  CG  . ARG   B 1 229 ? -22.187 34.531 -1.981  1.00 60.75  ? 226 ARG   B CG  1 
ATOM   4350 C  CD  . ARG   B 1 229 ? -22.520 34.528 -3.464  1.00 63.96  ? 226 ARG   B CD  1 
ATOM   4351 N  NE  . ARG   B 1 229 ? -21.953 35.682 -4.156  1.00 65.17  ? 226 ARG   B NE  1 
ATOM   4352 C  CZ  . ARG   B 1 229 ? -22.610 36.815 -4.428  1.00 68.62  ? 226 ARG   B CZ  1 
ATOM   4353 N  NH1 . ARG   B 1 229 ? -23.878 36.968 -4.070  1.00 72.92  ? 226 ARG   B NH1 1 
ATOM   4354 N  NH2 . ARG   B 1 229 ? -21.987 37.803 -5.046  1.00 64.85  ? 226 ARG   B NH2 1 
ATOM   4355 N  N   . TRP   B 1 230 ? -17.863 34.033 -0.256  1.00 45.28  ? 227 TRP   B N   1 
ATOM   4356 C  CA  . TRP   B 1 230 ? -16.529 33.391 -0.353  1.00 43.54  ? 227 TRP   B CA  1 
ATOM   4357 C  C   . TRP   B 1 230 ? -15.633 33.745 0.825   1.00 42.65  ? 227 TRP   B C   1 
ATOM   4358 O  O   . TRP   B 1 230 ? -14.745 32.961 1.117   1.00 43.10  ? 227 TRP   B O   1 
ATOM   4359 C  CB  . TRP   B 1 230 ? -15.835 33.785 -1.653  1.00 42.79  ? 227 TRP   B CB  1 
ATOM   4360 C  CG  . TRP   B 1 230 ? -16.581 33.297 -2.846  1.00 42.91  ? 227 TRP   B CG  1 
ATOM   4361 C  CD1 . TRP   B 1 230 ? -17.370 34.042 -3.668  1.00 43.82  ? 227 TRP   B CD1 1 
ATOM   4362 C  CD2 . TRP   B 1 230 ? -16.659 31.946 -3.315  1.00 44.14  ? 227 TRP   B CD2 1 
ATOM   4363 N  NE1 . TRP   B 1 230 ? -17.897 33.257 -4.648  1.00 44.13  ? 227 TRP   B NE1 1 
ATOM   4364 C  CE2 . TRP   B 1 230 ? -17.493 31.964 -4.450  1.00 44.90  ? 227 TRP   B CE2 1 
ATOM   4365 C  CE3 . TRP   B 1 230 ? -16.077 30.738 -2.921  1.00 45.64  ? 227 TRP   B CE3 1 
ATOM   4366 C  CZ2 . TRP   B 1 230 ? -17.785 30.811 -5.177  1.00 45.47  ? 227 TRP   B CZ2 1 
ATOM   4367 C  CZ3 . TRP   B 1 230 ? -16.356 29.597 -3.645  1.00 46.53  ? 227 TRP   B CZ3 1 
ATOM   4368 C  CH2 . TRP   B 1 230 ? -17.193 29.639 -4.764  1.00 46.04  ? 227 TRP   B CH2 1 
ATOM   4369 N  N   . VAL   B 1 231 ? -15.855 34.900 1.430   1.00 42.82  ? 228 VAL   B N   1 
ATOM   4370 C  CA  . VAL   B 1 231 ? -14.882 35.532 2.358   1.00 41.93  ? 228 VAL   B CA  1 
ATOM   4371 C  C   . VAL   B 1 231 ? -15.603 35.783 3.678   1.00 44.16  ? 228 VAL   B C   1 
ATOM   4372 O  O   . VAL   B 1 231 ? -16.601 36.504 3.696   1.00 44.65  ? 228 VAL   B O   1 
ATOM   4373 C  CB  . VAL   B 1 231 ? -14.292 36.826 1.766   1.00 40.38  ? 228 VAL   B CB  1 
ATOM   4374 C  CG1 . VAL   B 1 231 ? -13.311 37.461 2.759   1.00 40.18  ? 228 VAL   B CG1 1 
ATOM   4375 C  CG2 . VAL   B 1 231 ? -13.612 36.604 0.417   1.00 37.79  ? 228 VAL   B CG2 1 
ATOM   4376 N  N   . ASP   B 1 232 ? -15.078 35.185 4.734   1.00 45.74  ? 229 ASP   B N   1 
ATOM   4377 C  CA  . ASP   B 1 232 ? -15.483 35.451 6.138   1.00 49.42  ? 229 ASP   B CA  1 
ATOM   4378 C  C   . ASP   B 1 232 ? -15.393 36.954 6.431   1.00 49.97  ? 229 ASP   B C   1 
ATOM   4379 O  O   . ASP   B 1 232 ? -14.306 37.530 6.374   1.00 47.61  ? 229 ASP   B O   1 
ATOM   4380 C  CB  . ASP   B 1 232 ? -14.621 34.609 7.079   1.00 49.55  ? 229 ASP   B CB  1 
ATOM   4381 C  CG  . ASP   B 1 232 ? -15.104 34.586 8.514   1.00 52.99  ? 229 ASP   B CG  1 
ATOM   4382 O  OD1 . ASP   B 1 232 ? -15.958 35.393 8.867   1.00 54.89  ? 229 ASP   B OD1 1 
ATOM   4383 O  OD2 . ASP   B 1 232 ? -14.598 33.756 9.265   1.00 54.76  ? 229 ASP   B OD2 1 
ATOM   4384 N  N   . PRO   B 1 233 ? -16.508 37.629 6.810   1.00 52.70  ? 230 PRO   B N   1 
ATOM   4385 C  CA  . PRO   B 1 233 ? -16.457 39.051 7.139   1.00 53.41  ? 230 PRO   B CA  1 
ATOM   4386 C  C   . PRO   B 1 233 ? -15.607 39.292 8.397   1.00 53.87  ? 230 PRO   B C   1 
ATOM   4387 O  O   . PRO   B 1 233 ? -15.237 40.418 8.611   1.00 54.10  ? 230 PRO   B O   1 
ATOM   4388 C  CB  . PRO   B 1 233 ? -17.925 39.494 7.361   1.00 56.44  ? 230 PRO   B CB  1 
ATOM   4389 C  CG  . PRO   B 1 233 ? -18.786 38.275 7.015   1.00 57.44  ? 230 PRO   B CG  1 
ATOM   4390 C  CD  . PRO   B 1 233 ? -17.865 37.070 6.974   1.00 55.47  ? 230 PRO   B CD  1 
ATOM   4391 N  N   . ASN   B 1 234 ? -15.339 38.258 9.202   1.00 54.15  ? 231 ASN   B N   1 
ATOM   4392 C  CA  . ASN   B 1 234 ? -14.501 38.395 10.433  1.00 55.45  ? 231 ASN   B CA  1 
ATOM   4393 C  C   . ASN   B 1 234 ? -13.008 38.394 10.059  1.00 51.61  ? 231 ASN   B C   1 
ATOM   4394 O  O   . ASN   B 1 234 ? -12.196 38.797 10.915  1.00 51.97  ? 231 ASN   B O   1 
ATOM   4395 C  CB  . ASN   B 1 234 ? -14.798 37.305 11.471  1.00 58.48  ? 231 ASN   B CB  1 
ATOM   4396 C  CG  . ASN   B 1 234 ? -16.239 37.302 11.957  1.00 62.20  ? 231 ASN   B CG  1 
ATOM   4397 O  OD1 . ASN   B 1 234 ? -16.861 38.356 12.094  1.00 63.99  ? 231 ASN   B OD1 1 
ATOM   4398 N  ND2 . ASN   B 1 234 ? -16.782 36.116 12.211  1.00 63.85  ? 231 ASN   B ND2 1 
ATOM   4399 N  N   . SER   B 1 235 ? -12.657 37.986 8.826   1.00 48.35  ? 232 SER   B N   1 
ATOM   4400 C  CA  . SER   B 1 235 ? -11.252 37.982 8.339   1.00 45.03  ? 232 SER   B CA  1 
ATOM   4401 C  C   . SER   B 1 235 ? -10.685 39.397 8.403   1.00 44.98  ? 232 SER   B C   1 
ATOM   4402 O  O   . SER   B 1 235 ? -11.370 40.378 8.140   1.00 45.45  ? 232 SER   B O   1 
ATOM   4403 C  CB  . SER   B 1 235 ? -11.104 37.373 6.959   1.00 43.01  ? 232 SER   B CB  1 
ATOM   4404 O  OG  . SER   B 1 235 ? -11.558 38.261 5.966   1.00 41.39  ? 232 SER   B OG  1 
ATOM   4405 N  N   . PRO   B 1 236 ? -9.396  39.541 8.769   1.00 44.39  ? 233 PRO   B N   1 
ATOM   4406 C  CA  . PRO   B 1 236 ? -8.761  40.855 8.858   1.00 44.15  ? 233 PRO   B CA  1 
ATOM   4407 C  C   . PRO   B 1 236 ? -8.859  41.593 7.521   1.00 41.83  ? 233 PRO   B C   1 
ATOM   4408 O  O   . PRO   B 1 236 ? -8.723  40.971 6.469   1.00 39.44  ? 233 PRO   B O   1 
ATOM   4409 C  CB  . PRO   B 1 236 ? -7.294  40.547 9.232   1.00 43.40  ? 233 PRO   B CB  1 
ATOM   4410 C  CG  . PRO   B 1 236 ? -7.124  39.083 8.880   1.00 42.26  ? 233 PRO   B CG  1 
ATOM   4411 C  CD  . PRO   B 1 236 ? -8.474  38.440 9.109   1.00 43.50  ? 233 PRO   B CD  1 
ATOM   4412 N  N   . VAL   B 1 237 ? -9.106  42.890 7.595   1.00 42.20  ? 234 VAL   B N   1 
ATOM   4413 C  CA  . VAL   B 1 237 ? -9.275  43.747 6.392   1.00 41.68  ? 234 VAL   B CA  1 
ATOM   4414 C  C   . VAL   B 1 237 ? -7.896  44.238 5.963   1.00 39.25  ? 234 VAL   B C   1 
ATOM   4415 O  O   . VAL   B 1 237 ? -7.338  45.119 6.648   1.00 39.79  ? 234 VAL   B O   1 
ATOM   4416 C  CB  . VAL   B 1 237 ? -10.227 44.925 6.671   1.00 44.65  ? 234 VAL   B CB  1 
ATOM   4417 C  CG1 . VAL   B 1 237 ? -10.322 45.823 5.456   1.00 44.01  ? 234 VAL   B CG1 1 
ATOM   4418 C  CG2 . VAL   B 1 237 ? -11.606 44.470 7.133   1.00 46.03  ? 234 VAL   B CG2 1 
ATOM   4419 N  N   . LEU   B 1 238 ? -7.395  43.742 4.829   1.00 35.83  ? 235 LEU   B N   1 
ATOM   4420 C  CA  . LEU   B 1 238 ? -5.998  44.040 4.437   1.00 34.22  ? 235 LEU   B CA  1 
ATOM   4421 C  C   . LEU   B 1 238 ? -5.784  45.549 4.374   1.00 35.58  ? 235 LEU   B C   1 
ATOM   4422 O  O   . LEU   B 1 238 ? -4.742  45.996 4.875   1.00 35.62  ? 235 LEU   B O   1 
ATOM   4423 C  CB  . LEU   B 1 238 ? -5.618  43.384 3.111   1.00 31.87  ? 235 LEU   B CB  1 
ATOM   4424 C  CG  . LEU   B 1 238 ? -4.155  43.614 2.719   1.00 30.77  ? 235 LEU   B CG  1 
ATOM   4425 C  CD1 . LEU   B 1 238 ? -3.208  42.864 3.646   1.00 30.69  ? 235 LEU   B CD1 1 
ATOM   4426 C  CD2 . LEU   B 1 238 ? -3.915  43.226 1.284   1.00 29.33  ? 235 LEU   B CD2 1 
ATOM   4427 N  N   . LEU   B 1 239 ? -6.688  46.304 3.756   1.00 36.50  ? 236 LEU   B N   1 
ATOM   4428 C  CA  . LEU   B 1 239 ? -6.436  47.722 3.396   1.00 38.17  ? 236 LEU   B CA  1 
ATOM   4429 C  C   . LEU   B 1 239 ? -6.567  48.620 4.625   1.00 41.64  ? 236 LEU   B C   1 
ATOM   4430 O  O   . LEU   B 1 239 ? -6.328  49.814 4.468   1.00 42.78  ? 236 LEU   B O   1 
ATOM   4431 C  CB  . LEU   B 1 239 ? -7.386  48.126 2.264   1.00 38.03  ? 236 LEU   B CB  1 
ATOM   4432 C  CG  . LEU   B 1 239 ? -7.082  47.399 0.959   1.00 35.74  ? 236 LEU   B CG  1 
ATOM   4433 C  CD1 . LEU   B 1 239 ? -7.892  48.003 -0.192  1.00 35.79  ? 236 LEU   B CD1 1 
ATOM   4434 C  CD2 . LEU   B 1 239 ? -5.581  47.408 0.650   1.00 34.62  ? 236 LEU   B CD2 1 
ATOM   4435 N  N   . GLU   B 1 240 ? -6.949  48.064 5.776   1.00 43.09  ? 237 GLU   B N   1 
ATOM   4436 C  CA  . GLU   B 1 240 ? -6.943  48.784 7.088   1.00 46.89  ? 237 GLU   B CA  1 
ATOM   4437 C  C   . GLU   B 1 240 ? -5.784  48.322 7.965   1.00 47.32  ? 237 GLU   B C   1 
ATOM   4438 O  O   . GLU   B 1 240 ? -5.657  48.860 9.076   1.00 50.95  ? 237 GLU   B O   1 
ATOM   4439 C  CB  . GLU   B 1 240 ? -8.254  48.562 7.829   1.00 49.06  ? 237 GLU   B CB  1 
ATOM   4440 C  CG  . GLU   B 1 240 ? -9.423  49.178 7.098   1.00 50.76  ? 237 GLU   B CG  1 
ATOM   4441 C  CD  . GLU   B 1 240 ? -10.761 48.934 7.763   1.00 53.40  ? 237 GLU   B CD  1 
ATOM   4442 O  OE1 . GLU   B 1 240 ? -10.773 48.277 8.830   1.00 54.77  ? 237 GLU   B OE1 1 
ATOM   4443 O  OE2 . GLU   B 1 240 ? -11.782 49.399 7.220   1.00 54.75  ? 237 GLU   B OE2 1 
ATOM   4444 N  N   . ASP   B 1 241 ? -4.960  47.398 7.493   1.00 44.65  ? 238 ASP   B N   1 
ATOM   4445 C  CA  . ASP   B 1 241 ? -3.794  46.932 8.278   1.00 45.43  ? 238 ASP   B CA  1 
ATOM   4446 C  C   . ASP   B 1 241 ? -2.996  48.135 8.786   1.00 46.58  ? 238 ASP   B C   1 
ATOM   4447 O  O   . ASP   B 1 241 ? -2.602  49.000 8.013   1.00 44.97  ? 238 ASP   B O   1 
ATOM   4448 C  CB  . ASP   B 1 241 ? -2.927  46.005 7.437   1.00 43.62  ? 238 ASP   B CB  1 
ATOM   4449 C  CG  . ASP   B 1 241 ? -1.888  45.315 8.280   1.00 44.92  ? 238 ASP   B CG  1 
ATOM   4450 O  OD1 . ASP   B 1 241 ? -2.233  44.281 8.900   1.00 46.09  ? 238 ASP   B OD1 1 
ATOM   4451 O  OD2 . ASP   B 1 241 ? -0.773  45.881 8.393   1.00 47.95  ? 238 ASP   B OD2 1 
ATOM   4452 N  N   . PRO   B 1 242 ? -2.711  48.230 10.104  1.00 49.57  ? 239 PRO   B N   1 
ATOM   4453 C  CA  . PRO   B 1 242 ? -1.997  49.402 10.637  1.00 51.33  ? 239 PRO   B CA  1 
ATOM   4454 C  C   . PRO   B 1 242 ? -0.600  49.619 10.024  1.00 49.46  ? 239 PRO   B C   1 
ATOM   4455 O  O   . PRO   B 1 242 ? -0.222  50.757 9.799   1.00 51.12  ? 239 PRO   B O   1 
ATOM   4456 C  CB  . PRO   B 1 242 ? -1.973  49.163 12.157  1.00 54.11  ? 239 PRO   B CB  1 
ATOM   4457 C  CG  . PRO   B 1 242 ? -2.230  47.686 12.312  1.00 52.91  ? 239 PRO   B CG  1 
ATOM   4458 C  CD  . PRO   B 1 242 ? -3.116  47.282 11.152  1.00 50.20  ? 239 PRO   B CD  1 
ATOM   4459 N  N   . VAL   B 1 243 ? 0.079   48.544 9.624   1.00 46.69  ? 240 VAL   B N   1 
ATOM   4460 C  CA  . VAL   B 1 243 ? 1.424   48.608 8.968   1.00 45.52  ? 240 VAL   B CA  1 
ATOM   4461 C  C   . VAL   B 1 243 ? 1.273   49.219 7.569   1.00 44.27  ? 240 VAL   B C   1 
ATOM   4462 O  O   . VAL   B 1 243 ? 2.006   50.157 7.210   1.00 43.91  ? 240 VAL   B O   1 
ATOM   4463 C  CB  . VAL   B 1 243 ? 2.054   47.200 8.934   1.00 44.20  ? 240 VAL   B CB  1 
ATOM   4464 C  CG1 . VAL   B 1 243 ? 3.251   47.113 7.990   1.00 42.66  ? 240 VAL   B CG1 1 
ATOM   4465 C  CG2 . VAL   B 1 243 ? 2.412   46.752 10.348  1.00 45.92  ? 240 VAL   B CG2 1 
ATOM   4466 N  N   . LEU   B 1 244 ? 0.337   48.702 6.775   1.00 42.03  ? 241 LEU   B N   1 
ATOM   4467 C  CA  . LEU   B 1 244 ? 0.055   49.290 5.450   1.00 42.24  ? 241 LEU   B CA  1 
ATOM   4468 C  C   . LEU   B 1 244 ? -0.385  50.757 5.592   1.00 44.86  ? 241 LEU   B C   1 
ATOM   4469 O  O   . LEU   B 1 244 ? 0.073   51.567 4.797   1.00 45.32  ? 241 LEU   B O   1 
ATOM   4470 C  CB  . LEU   B 1 244 ? -1.023  48.457 4.760   1.00 40.25  ? 241 LEU   B CB  1 
ATOM   4471 C  CG  . LEU   B 1 244 ? -0.671  46.993 4.491   1.00 38.14  ? 241 LEU   B CG  1 
ATOM   4472 C  CD1 . LEU   B 1 244 ? -1.665  46.382 3.511   1.00 36.40  ? 241 LEU   B CD1 1 
ATOM   4473 C  CD2 . LEU   B 1 244 ? 0.742   46.811 3.959   1.00 37.44  ? 241 LEU   B CD2 1 
ATOM   4474 N  N   . CYS   B 1 245 ? -1.233  51.079 6.570   1.00 48.02  ? 242 CYS   B N   1 
ATOM   4475 C  CA  . CYS   B 1 245 ? -1.716  52.469 6.833   1.00 51.43  ? 242 CYS   B CA  1 
ATOM   4476 C  C   . CYS   B 1 245 ? -0.575  53.414 7.245   1.00 52.75  ? 242 CYS   B C   1 
ATOM   4477 O  O   . CYS   B 1 245 ? -0.531  54.528 6.714   1.00 53.57  ? 242 CYS   B O   1 
ATOM   4478 C  CB  . CYS   B 1 245 ? -2.836  52.445 7.856   1.00 54.47  ? 242 CYS   B CB  1 
ATOM   4479 S  SG  . CYS   B 1 245 ? -4.306  51.678 7.124   1.00 55.66  ? 242 CYS   B SG  1 
ATOM   4480 N  N   . ALA   B 1 246 ? 0.331   52.976 8.126   1.00 53.03  ? 243 ALA   B N   1 
ATOM   4481 C  CA  . ALA   B 1 246 ? 1.533   53.750 8.508   1.00 54.72  ? 243 ALA   B CA  1 
ATOM   4482 C  C   . ALA   B 1 246 ? 2.440   53.955 7.277   1.00 53.19  ? 243 ALA   B C   1 
ATOM   4483 O  O   . ALA   B 1 246 ? 2.902   55.084 7.018   1.00 54.96  ? 243 ALA   B O   1 
ATOM   4484 C  CB  . ALA   B 1 246 ? 2.248   53.053 9.640   1.00 55.19  ? 243 ALA   B CB  1 
ATOM   4485 N  N   . LEU   B 1 247 ? 2.718   52.903 6.520   1.00 50.26  ? 244 LEU   B N   1 
ATOM   4486 C  CA  . LEU   B 1 247 ? 3.582   53.027 5.320   1.00 49.40  ? 244 LEU   B CA  1 
ATOM   4487 C  C   . LEU   B 1 247 ? 2.939   53.967 4.288   1.00 50.00  ? 244 LEU   B C   1 
ATOM   4488 O  O   . LEU   B 1 247 ? 3.681   54.724 3.626   1.00 51.02  ? 244 LEU   B O   1 
ATOM   4489 C  CB  . LEU   B 1 247 ? 3.839   51.629 4.749   1.00 46.52  ? 244 LEU   B CB  1 
ATOM   4490 C  CG  . LEU   B 1 247 ? 4.784   50.766 5.587   1.00 45.94  ? 244 LEU   B CG  1 
ATOM   4491 C  CD1 . LEU   B 1 247 ? 4.955   49.375 4.980   1.00 43.00  ? 244 LEU   B CD1 1 
ATOM   4492 C  CD2 . LEU   B 1 247 ? 6.141   51.419 5.723   1.00 47.49  ? 244 LEU   B CD2 1 
ATOM   4493 N  N   . ALA   B 1 248 ? 1.620   53.920 4.131   1.00 49.91  ? 245 ALA   B N   1 
ATOM   4494 C  CA  . ALA   B 1 248 ? 0.899   54.817 3.211   1.00 51.77  ? 245 ALA   B CA  1 
ATOM   4495 C  C   . ALA   B 1 248 ? 1.172   56.270 3.643   1.00 56.52  ? 245 ALA   B C   1 
ATOM   4496 O  O   . ALA   B 1 248 ? 1.555   57.084 2.790   1.00 57.97  ? 245 ALA   B O   1 
ATOM   4497 C  CB  . ALA   B 1 248 ? -0.576  54.488 3.162   1.00 50.48  ? 245 ALA   B CB  1 
ATOM   4498 N  N   . LYS   B 1 249 ? 1.072   56.573 4.934   1.00 59.92  ? 246 LYS   B N   1 
ATOM   4499 C  CA  . LYS   B 1 249 ? 1.319   57.959 5.423   1.00 65.66  ? 246 LYS   B CA  1 
ATOM   4500 C  C   . LYS   B 1 249 ? 2.774   58.341 5.141   1.00 66.60  ? 246 LYS   B C   1 
ATOM   4501 O  O   . LYS   B 1 249 ? 3.003   59.391 4.524   1.00 70.27  ? 246 LYS   B O   1 
ATOM   4502 C  CB  . LYS   B 1 249 ? 1.041   58.058 6.913   1.00 68.37  ? 246 LYS   B CB  1 
ATOM   4503 C  CG  . LYS   B 1 249 ? -0.414  58.197 7.307   1.00 69.93  ? 246 LYS   B CG  1 
ATOM   4504 C  CD  . LYS   B 1 249 ? -0.493  58.744 8.706   1.00 74.63  ? 246 LYS   B CD  1 
ATOM   4505 C  CE  . LYS   B 1 249 ? 0.438   59.931 8.887   1.00 78.99  ? 246 LYS   B CE  1 
ATOM   4506 N  NZ  . LYS   B 1 249 ? 0.166   60.731 10.103  1.00 83.71  ? 246 LYS   B NZ  1 
ATOM   4507 N  N   . LYS   B 1 250 ? 3.711   57.485 5.537   1.00 65.91  ? 247 LYS   B N   1 
ATOM   4508 C  CA  . LYS   B 1 250 ? 5.164   57.702 5.320   1.00 67.34  ? 247 LYS   B CA  1 
ATOM   4509 C  C   . LYS   B 1 250 ? 5.411   58.127 3.867   1.00 66.08  ? 247 LYS   B C   1 
ATOM   4510 O  O   . LYS   B 1 250 ? 6.068   59.153 3.672   1.00 69.64  ? 247 LYS   B O   1 
ATOM   4511 C  CB  . LYS   B 1 250 ? 5.961   56.440 5.676   1.00 66.87  ? 247 LYS   B CB  1 
ATOM   4512 C  CG  . LYS   B 1 250 ? 7.281   56.299 4.932   1.00 66.98  ? 247 LYS   B CG  1 
ATOM   4513 C  CD  . LYS   B 1 250 ? 8.297   55.493 5.673   1.00 67.79  ? 247 LYS   B CD  1 
ATOM   4514 C  CE  . LYS   B 1 250 ? 9.533   55.236 4.836   1.00 67.56  ? 247 LYS   B CE  1 
ATOM   4515 N  NZ  . LYS   B 1 250 ? 10.416  54.253 5.500   1.00 66.72  ? 247 LYS   B NZ  1 
ATOM   4516 N  N   . HIS   B 1 251 ? 4.901   57.373 2.884   1.00 61.83  ? 248 HIS   B N   1 
ATOM   4517 C  CA  . HIS   B 1 251 ? 5.205   57.568 1.443   1.00 60.60  ? 248 HIS   B CA  1 
ATOM   4518 C  C   . HIS   B 1 251 ? 4.177   58.487 0.776   1.00 60.85  ? 248 HIS   B C   1 
ATOM   4519 O  O   . HIS   B 1 251 ? 4.279   58.651 -0.460  1.00 60.43  ? 248 HIS   B O   1 
ATOM   4520 C  CB  . HIS   B 1 251 ? 5.244   56.205 0.725   1.00 57.83  ? 248 HIS   B CB  1 
ATOM   4521 C  CG  . HIS   B 1 251 ? 6.439   55.372 1.062   1.00 57.64  ? 248 HIS   B CG  1 
ATOM   4522 N  ND1 . HIS   B 1 251 ? 7.613   55.442 0.332   1.00 59.07  ? 248 HIS   B ND1 1 
ATOM   4523 C  CD2 . HIS   B 1 251 ? 6.655   54.465 2.043   1.00 55.52  ? 248 HIS   B CD2 1 
ATOM   4524 C  CE1 . HIS   B 1 251 ? 8.499   54.620 0.861   1.00 58.39  ? 248 HIS   B CE1 1 
ATOM   4525 N  NE2 . HIS   B 1 251 ? 7.933   54.010 1.909   1.00 55.88  ? 248 HIS   B NE2 1 
ATOM   4526 N  N   . LYS   B 1 252 ? 3.198   59.000 1.537   1.00 61.44  ? 249 LYS   B N   1 
ATOM   4527 C  CA  . LYS   B 1 252 ? 2.041   59.800 1.037   1.00 62.70  ? 249 LYS   B CA  1 
ATOM   4528 C  C   . LYS   B 1 252 ? 1.357   59.034 -0.101  1.00 58.57  ? 249 LYS   B C   1 
ATOM   4529 O  O   . LYS   B 1 252 ? 1.125   59.603 -1.176  1.00 58.17  ? 249 LYS   B O   1 
ATOM   4530 C  CB  . LYS   B 1 252 ? 2.442   61.178 0.495   1.00 67.90  ? 249 LYS   B CB  1 
ATOM   4531 C  CG  . LYS   B 1 252 ? 3.640   61.852 1.135   1.00 72.43  ? 249 LYS   B CG  1 
ATOM   4532 C  CD  . LYS   B 1 252 ? 4.411   62.764 0.155   1.00 76.40  ? 249 LYS   B CD  1 
ATOM   4533 C  CE  . LYS   B 1 252 ? 5.302   61.951 -0.780  1.00 75.79  ? 249 LYS   B CE  1 
ATOM   4534 N  NZ  . LYS   B 1 252 ? 6.477   61.374 -0.056  1.00 76.96  ? 249 LYS   B NZ  1 
ATOM   4535 N  N   . ARG   B 1 253 ? 1.094   57.761 0.117   1.00 55.73  ? 250 ARG   B N   1 
ATOM   4536 C  CA  . ARG   B 1 253 ? 0.414   56.883 -0.870  1.00 52.69  ? 250 ARG   B CA  1 
ATOM   4537 C  C   . ARG   B 1 253 ? -0.808  56.343 -0.152  1.00 51.09  ? 250 ARG   B C   1 
ATOM   4538 O  O   . ARG   B 1 253 ? -1.252  57.015 0.770   1.00 53.02  ? 250 ARG   B O   1 
ATOM   4539 C  CB  . ARG   B 1 253 ? 1.381   55.821 -1.390  1.00 51.35  ? 250 ARG   B CB  1 
ATOM   4540 C  CG  . ARG   B 1 253 ? 2.540   56.396 -2.188  1.00 53.41  ? 250 ARG   B CG  1 
ATOM   4541 C  CD  . ARG   B 1 253 ? 2.148   57.135 -3.458  1.00 54.48  ? 250 ARG   B CD  1 
ATOM   4542 N  NE  . ARG   B 1 253 ? 3.294   57.808 -4.068  1.00 57.21  ? 250 ARG   B NE  1 
ATOM   4543 C  CZ  . ARG   B 1 253 ? 3.330   58.331 -5.299  1.00 59.05  ? 250 ARG   B CZ  1 
ATOM   4544 N  NH1 . ARG   B 1 253 ? 2.276   58.265 -6.109  1.00 57.30  ? 250 ARG   B NH1 1 
ATOM   4545 N  NH2 . ARG   B 1 253 ? 4.443   58.907 -5.724  1.00 61.90  ? 250 ARG   B NH2 1 
ATOM   4546 N  N   . THR   B 1 254 ? -1.341  55.210 -0.585  1.00 48.70  ? 251 THR   B N   1 
ATOM   4547 C  CA  . THR   B 1 254 ? -2.531  54.542 0.003   1.00 46.78  ? 251 THR   B CA  1 
ATOM   4548 C  C   . THR   B 1 254 ? -2.103  53.128 0.383   1.00 44.00  ? 251 THR   B C   1 
ATOM   4549 O  O   . THR   B 1 254 ? -1.139  52.606 -0.155  1.00 41.95  ? 251 THR   B O   1 
ATOM   4550 C  CB  . THR   B 1 254 ? -3.712  54.572 -0.983  1.00 46.07  ? 251 THR   B CB  1 
ATOM   4551 O  OG1 . THR   B 1 254 ? -3.347  53.747 -2.090  1.00 44.35  ? 251 THR   B OG1 1 
ATOM   4552 C  CG2 . THR   B 1 254 ? -4.065  55.968 -1.443  1.00 48.37  ? 251 THR   B CG2 1 
ATOM   4553 N  N   . PRO   B 1 255 ? -2.816  52.466 1.314   1.00 43.40  ? 252 PRO   B N   1 
ATOM   4554 C  CA  . PRO   B 1 255 ? -2.517  51.079 1.650   1.00 41.64  ? 252 PRO   B CA  1 
ATOM   4555 C  C   . PRO   B 1 255 ? -2.500  50.202 0.388   1.00 38.58  ? 252 PRO   B C   1 
ATOM   4556 O  O   . PRO   B 1 255 ? -1.624  49.372 0.299   1.00 36.69  ? 252 PRO   B O   1 
ATOM   4557 C  CB  . PRO   B 1 255 ? -3.650  50.688 2.611   1.00 42.19  ? 252 PRO   B CB  1 
ATOM   4558 C  CG  . PRO   B 1 255 ? -4.111  52.002 3.211   1.00 45.01  ? 252 PRO   B CG  1 
ATOM   4559 C  CD  . PRO   B 1 255 ? -3.910  53.028 2.121   1.00 45.63  ? 252 PRO   B CD  1 
ATOM   4560 N  N   . ALA   B 1 256 ? -3.444  50.414 -0.540  1.00 37.90  ? 253 ALA   B N   1 
ATOM   4561 C  CA  . ALA   B 1 256 ? -3.512  49.642 -1.800  1.00 35.58  ? 253 ALA   B CA  1 
ATOM   4562 C  C   . ALA   B 1 256 ? -2.175  49.770 -2.539  1.00 35.20  ? 253 ALA   B C   1 
ATOM   4563 O  O   . ALA   B 1 256 ? -1.617  48.740 -2.912  1.00 33.89  ? 253 ALA   B O   1 
ATOM   4564 C  CB  . ALA   B 1 256 ? -4.682  50.054 -2.637  1.00 35.81  ? 253 ALA   B CB  1 
ATOM   4565 N  N   . LEU   B 1 257 ? -1.651  50.982 -2.694  1.00 37.55  ? 254 LEU   B N   1 
ATOM   4566 C  CA  . LEU   B 1 257 ? -0.389  51.201 -3.436  1.00 38.02  ? 254 LEU   B CA  1 
ATOM   4567 C  C   . LEU   B 1 257 ? 0.762   50.519 -2.692  1.00 37.96  ? 254 LEU   B C   1 
ATOM   4568 O  O   . LEU   B 1 257 ? 1.634   49.939 -3.348  1.00 37.38  ? 254 LEU   B O   1 
ATOM   4569 C  CB  . LEU   B 1 257 ? -0.143  52.695 -3.640  1.00 40.49  ? 254 LEU   B CB  1 
ATOM   4570 C  CG  . LEU   B 1 257 ? -0.962  53.312 -4.773  1.00 41.85  ? 254 LEU   B CG  1 
ATOM   4571 C  CD1 . LEU   B 1 257 ? -0.850  54.829 -4.729  1.00 45.19  ? 254 LEU   B CD1 1 
ATOM   4572 C  CD2 . LEU   B 1 257 ? -0.516  52.787 -6.135  1.00 40.87  ? 254 LEU   B CD2 1 
ATOM   4573 N  N   . ILE   B 1 258 ? 0.743   50.550 -1.370  1.00 38.20  ? 255 ILE   B N   1 
ATOM   4574 C  CA  . ILE   B 1 258 ? 1.807   49.862 -0.591  1.00 37.91  ? 255 ILE   B CA  1 
ATOM   4575 C  C   . ILE   B 1 258 ? 1.743   48.371 -0.936  1.00 34.83  ? 255 ILE   B C   1 
ATOM   4576 O  O   . ILE   B 1 258 ? 2.794   47.805 -1.285  1.00 33.04  ? 255 ILE   B O   1 
ATOM   4577 C  CB  . ILE   B 1 258 ? 1.665   50.140 0.912   1.00 39.86  ? 255 ILE   B CB  1 
ATOM   4578 C  CG1 . ILE   B 1 258 ? 1.730   51.647 1.221   1.00 43.22  ? 255 ILE   B CG1 1 
ATOM   4579 C  CG2 . ILE   B 1 258 ? 2.719   49.365 1.682   1.00 40.01  ? 255 ILE   B CG2 1 
ATOM   4580 C  CD1 . ILE   B 1 258 ? 3.006   52.320 0.767   1.00 44.65  ? 255 ILE   B CD1 1 
ATOM   4581 N  N   . ALA   B 1 259 ? 0.539   47.794 -0.908  1.00 33.36  ? 256 ALA   B N   1 
ATOM   4582 C  CA  . ALA   B 1 259 ? 0.351   46.337 -1.086  1.00 31.74  ? 256 ALA   B CA  1 
ATOM   4583 C  C   . ALA   B 1 259 ? 0.808   45.952 -2.500  1.00 30.66  ? 256 ALA   B C   1 
ATOM   4584 O  O   . ALA   B 1 259 ? 1.284   44.813 -2.699  1.00 30.61  ? 256 ALA   B O   1 
ATOM   4585 C  CB  . ALA   B 1 259 ? -1.101  45.954 -0.833  1.00 31.33  ? 256 ALA   B CB  1 
ATOM   4586 N  N   . LEU   B 1 260 ? 0.574   46.815 -3.484  1.00 30.74  ? 257 LEU   B N   1 
ATOM   4587 C  CA  . LEU   B 1 260 ? 0.944   46.542 -4.898  1.00 30.70  ? 257 LEU   B CA  1 
ATOM   4588 C  C   . LEU   B 1 260 ? 2.462   46.639 -5.034  1.00 31.94  ? 257 LEU   B C   1 
ATOM   4589 O  O   . LEU   B 1 260 ? 3.074   45.747 -5.684  1.00 31.44  ? 257 LEU   B O   1 
ATOM   4590 C  CB  . LEU   B 1 260 ? 0.283   47.548 -5.843  1.00 30.90  ? 257 LEU   B CB  1 
ATOM   4591 C  CG  . LEU   B 1 260 ? -1.234  47.483 -6.019  1.00 30.61  ? 257 LEU   B CG  1 
ATOM   4592 C  CD1 . LEU   B 1 260 ? -1.662  48.517 -7.058  1.00 31.77  ? 257 LEU   B CD1 1 
ATOM   4593 C  CD2 . LEU   B 1 260 ? -1.719  46.100 -6.442  1.00 28.24  ? 257 LEU   B CD2 1 
ATOM   4594 N  N   . ARG   B 1 261 ? 3.020   47.720 -4.484  1.00 33.75  ? 258 ARG   B N   1 
ATOM   4595 C  CA  . ARG   B 1 261 ? 4.472   48.000 -4.556  1.00 35.51  ? 258 ARG   B CA  1 
ATOM   4596 C  C   . ARG   B 1 261 ? 5.242   46.852 -3.915  1.00 33.83  ? 258 ARG   B C   1 
ATOM   4597 O  O   . ARG   B 1 261 ? 6.281   46.446 -4.479  1.00 34.30  ? 258 ARG   B O   1 
ATOM   4598 C  CB  . ARG   B 1 261 ? 4.789   49.357 -3.931  1.00 38.43  ? 258 ARG   B CB  1 
ATOM   4599 C  CG  . ARG   B 1 261 ? 6.217   49.808 -4.181  1.00 41.03  ? 258 ARG   B CG  1 
ATOM   4600 C  CD  . ARG   B 1 261 ? 6.517   50.052 -5.638  1.00 42.00  ? 258 ARG   B CD  1 
ATOM   4601 N  NE  . ARG   B 1 261 ? 7.950   49.939 -5.862  1.00 44.32  ? 258 ARG   B NE  1 
ATOM   4602 C  CZ  . ARG   B 1 261 ? 8.513   50.131 -7.040  1.00 45.58  ? 258 ARG   B CZ  1 
ATOM   4603 N  NH1 . ARG   B 1 261 ? 7.755   50.461 -8.068  1.00 46.06  ? 258 ARG   B NH1 1 
ATOM   4604 N  NH2 . ARG   B 1 261 ? 9.815   50.007 -7.195  1.00 47.33  ? 258 ARG   B NH2 1 
ATOM   4605 N  N   . TYR   B 1 262 ? 4.769   46.368 -2.773  1.00 32.66  ? 259 TYR   B N   1 
ATOM   4606 C  CA  . TYR   B 1 262 ? 5.344   45.180 -2.094  1.00 31.62  ? 259 TYR   B CA  1 
ATOM   4607 C  C   . TYR   B 1 262 ? 5.564   44.050 -3.111  1.00 29.44  ? 259 TYR   B C   1 
ATOM   4608 O  O   . TYR   B 1 262 ? 6.693   43.473 -3.158  1.00 29.53  ? 259 TYR   B O   1 
ATOM   4609 C  CB  . TYR   B 1 262 ? 4.413   44.736 -0.975  1.00 31.06  ? 259 TYR   B CB  1 
ATOM   4610 C  CG  . TYR   B 1 262 ? 4.808   43.448 -0.313  1.00 30.16  ? 259 TYR   B CG  1 
ATOM   4611 C  CD1 . TYR   B 1 262 ? 5.964   43.356 0.435   1.00 31.23  ? 259 TYR   B CD1 1 
ATOM   4612 C  CD2 . TYR   B 1 262 ? 4.009   42.321 -0.404  1.00 29.12  ? 259 TYR   B CD2 1 
ATOM   4613 C  CE1 . TYR   B 1 262 ? 6.308   42.191 1.091   1.00 30.82  ? 259 TYR   B CE1 1 
ATOM   4614 C  CE2 . TYR   B 1 262 ? 4.349   41.137 0.238   1.00 28.48  ? 259 TYR   B CE2 1 
ATOM   4615 C  CZ  . TYR   B 1 262 ? 5.505   41.069 0.993   1.00 30.24  ? 259 TYR   B CZ  1 
ATOM   4616 O  OH  . TYR   B 1 262 ? 5.862   39.914 1.665   1.00 30.53  ? 259 TYR   B OH  1 
ATOM   4617 N  N   . GLN   B 1 263 ? 4.533   43.722 -3.901  1.00 28.20  ? 260 GLN   B N   1 
ATOM   4618 C  CA  . GLN   B 1 263 ? 4.638   42.581 -4.852  1.00 27.21  ? 260 GLN   B CA  1 
ATOM   4619 C  C   . GLN   B 1 263 ? 5.666   42.906 -5.932  1.00 28.66  ? 260 GLN   B C   1 
ATOM   4620 O  O   . GLN   B 1 263 ? 6.495   42.044 -6.220  1.00 27.90  ? 260 GLN   B O   1 
ATOM   4621 C  CB  . GLN   B 1 263 ? 3.280   42.182 -5.402  1.00 25.76  ? 260 GLN   B CB  1 
ATOM   4622 C  CG  . GLN   B 1 263 ? 2.291   41.823 -4.312  1.00 25.17  ? 260 GLN   B CG  1 
ATOM   4623 C  CD  . GLN   B 1 263 ? 2.615   40.544 -3.594  1.00 24.71  ? 260 GLN   B CD  1 
ATOM   4624 O  OE1 . GLN   B 1 263 ? 3.642   39.915 -3.836  1.00 25.33  ? 260 GLN   B OE1 1 
ATOM   4625 N  NE2 . GLN   B 1 263 ? 1.740   40.164 -2.675  1.00 25.39  ? 260 GLN   B NE2 1 
ATOM   4626 N  N   . LEU   B 1 264 ? 5.714   44.135 -6.431  1.00 31.16  ? 261 LEU   B N   1 
ATOM   4627 C  CA  . LEU   B 1 264 ? 6.666   44.404 -7.530  1.00 33.92  ? 261 LEU   B CA  1 
ATOM   4628 C  C   . LEU   B 1 264 ? 8.100   44.294 -7.019  1.00 35.28  ? 261 LEU   B C   1 
ATOM   4629 O  O   . LEU   B 1 264 ? 8.943   43.839 -7.766  1.00 35.33  ? 261 LEU   B O   1 
ATOM   4630 C  CB  . LEU   B 1 264 ? 6.405   45.797 -8.092  1.00 36.08  ? 261 LEU   B CB  1 
ATOM   4631 C  CG  . LEU   B 1 264 ? 5.107   45.941 -8.883  1.00 35.38  ? 261 LEU   B CG  1 
ATOM   4632 C  CD1 . LEU   B 1 264 ? 5.112   47.284 -9.586  1.00 38.36  ? 261 LEU   B CD1 1 
ATOM   4633 C  CD2 . LEU   B 1 264 ? 4.932   44.800 -9.896  1.00 34.61  ? 261 LEU   B CD2 1 
ATOM   4634 N  N   . GLN   B 1 265 ? 8.371   44.715 -5.783  1.00 37.21  ? 262 GLN   B N   1 
ATOM   4635 C  CA  . GLN   B 1 265 ? 9.758   44.765 -5.279  1.00 37.63  ? 262 GLN   B CA  1 
ATOM   4636 C  C   . GLN   B 1 265 ? 10.194  43.339 -4.922  1.00 37.25  ? 262 GLN   B C   1 
ATOM   4637 O  O   . GLN   B 1 265 ? 11.382  43.129 -4.773  1.00 39.88  ? 262 GLN   B O   1 
ATOM   4638 C  CB  . GLN   B 1 265 ? 9.853   45.817 -4.183  1.00 39.77  ? 262 GLN   B CB  1 
ATOM   4639 C  CG  . GLN   B 1 265 ? 9.901   47.236 -4.723  1.00 41.29  ? 262 GLN   B CG  1 
ATOM   4640 C  CD  . GLN   B 1 265 ? 10.239  48.269 -3.675  1.00 43.16  ? 262 GLN   B CD  1 
ATOM   4641 O  OE1 . GLN   B 1 265 ? 9.642   49.344 -3.667  1.00 43.67  ? 262 GLN   B OE1 1 
ATOM   4642 N  NE2 . GLN   B 1 265 ? 11.189  47.960 -2.789  1.00 43.12  ? 262 GLN   B NE2 1 
ATOM   4643 N  N   . ARG   B 1 266 ? 9.281   42.378 -4.833  1.00 34.49  ? 263 ARG   B N   1 
ATOM   4644 C  CA  . ARG   B 1 266 ? 9.697   40.971 -4.555  1.00 34.53  ? 263 ARG   B CA  1 
ATOM   4645 C  C   . ARG   B 1 266 ? 9.662   40.131 -5.846  1.00 33.08  ? 263 ARG   B C   1 
ATOM   4646 O  O   . ARG   B 1 266 ? 9.922   38.940 -5.715  1.00 31.75  ? 263 ARG   B O   1 
ATOM   4647 C  CB  . ARG   B 1 266 ? 8.890   40.360 -3.403  1.00 33.39  ? 263 ARG   B CB  1 
ATOM   4648 C  CG  . ARG   B 1 266 ? 7.392   40.223 -3.648  1.00 31.87  ? 263 ARG   B CG  1 
ATOM   4649 C  CD  . ARG   B 1 266 ? 6.694   40.259 -2.287  1.00 31.48  ? 263 ARG   B CD  1 
ATOM   4650 N  NE  . ARG   B 1 266 ? 6.973   39.058 -1.487  1.00 30.53  ? 263 ARG   B NE  1 
ATOM   4651 C  CZ  . ARG   B 1 266 ? 6.167   37.992 -1.377  1.00 28.81  ? 263 ARG   B CZ  1 
ATOM   4652 N  NH1 . ARG   B 1 266 ? 4.995   37.971 -1.989  1.00 28.31  ? 263 ARG   B NH1 1 
ATOM   4653 N  NH2 . ARG   B 1 266 ? 6.523   36.962 -0.615  1.00 28.77  ? 263 ARG   B NH2 1 
ATOM   4654 N  N   . GLY   B 1 267 ? 9.467   40.739 -7.033  1.00 32.83  ? 264 GLY   B N   1 
ATOM   4655 C  CA  . GLY   B 1 267 ? 9.553   40.057 -8.338  1.00 32.31  ? 264 GLY   B CA  1 
ATOM   4656 C  C   . GLY   B 1 267 ? 8.257   39.331 -8.647  1.00 30.40  ? 264 GLY   B C   1 
ATOM   4657 O  O   . GLY   B 1 267 ? 8.269   38.313 -9.352  1.00 30.59  ? 264 GLY   B O   1 
ATOM   4658 N  N   . VAL   B 1 268 ? 7.181   39.733 -7.990  1.00 28.71  ? 265 VAL   B N   1 
ATOM   4659 C  CA  . VAL   B 1 268 ? 5.839   39.153 -8.233  1.00 26.64  ? 265 VAL   B CA  1 
ATOM   4660 C  C   . VAL   B 1 268 ? 5.129   40.050 -9.250  1.00 26.47  ? 265 VAL   B C   1 
ATOM   4661 O  O   . VAL   B 1 268 ? 5.183   41.272 -9.124  1.00 27.87  ? 265 VAL   B O   1 
ATOM   4662 C  CB  . VAL   B 1 268 ? 5.064   38.956 -6.922  1.00 25.88  ? 265 VAL   B CB  1 
ATOM   4663 C  CG1 . VAL   B 1 268 ? 3.583   38.686 -7.125  1.00 25.38  ? 265 VAL   B CG1 1 
ATOM   4664 C  CG2 . VAL   B 1 268 ? 5.690   37.838 -6.108  1.00 25.30  ? 265 VAL   B CG2 1 
ATOM   4665 N  N   . VAL   B 1 269 ? 4.476   39.446 -10.244 1.00 25.26  ? 266 VAL   B N   1 
ATOM   4666 C  CA  . VAL   B 1 269 ? 3.523   40.172 -11.128 1.00 25.45  ? 266 VAL   B CA  1 
ATOM   4667 C  C   . VAL   B 1 269 ? 2.193   40.310 -10.364 1.00 24.67  ? 266 VAL   B C   1 
ATOM   4668 O  O   . VAL   B 1 269 ? 1.761   39.352 -9.709  1.00 24.64  ? 266 VAL   B O   1 
ATOM   4669 C  CB  . VAL   B 1 269 ? 3.409   39.447 -12.486 1.00 25.10  ? 266 VAL   B CB  1 
ATOM   4670 C  CG1 . VAL   B 1 269 ? 2.272   39.980 -13.325 1.00 24.33  ? 266 VAL   B CG1 1 
ATOM   4671 C  CG2 . VAL   B 1 269 ? 4.735   39.560 -13.224 1.00 26.31  ? 266 VAL   B CG2 1 
ATOM   4672 N  N   . VAL   B 1 270 ? 1.620   41.509 -10.342 1.00 25.15  ? 267 VAL   B N   1 
ATOM   4673 C  CA  . VAL   B 1 270 ? 0.478   41.782 -9.427  1.00 24.58  ? 267 VAL   B CA  1 
ATOM   4674 C  C   . VAL   B 1 270 ? -0.756  42.224 -10.221 1.00 24.11  ? 267 VAL   B C   1 
ATOM   4675 O  O   . VAL   B 1 270 ? -0.616  43.038 -11.160 1.00 27.50  ? 267 VAL   B O   1 
ATOM   4676 C  CB  . VAL   B 1 270 ? 0.889   42.778 -8.323  1.00 25.88  ? 267 VAL   B CB  1 
ATOM   4677 C  CG1 . VAL   B 1 270 ? 1.132   44.191 -8.823  1.00 27.64  ? 267 VAL   B CG1 1 
ATOM   4678 C  CG2 . VAL   B 1 270 ? -0.158  42.812 -7.241  1.00 26.37  ? 267 VAL   B CG2 1 
ATOM   4679 N  N   . LEU   B 1 271 ? -1.908  41.649 -9.888  1.00 22.42  ? 268 LEU   B N   1 
ATOM   4680 C  CA  . LEU   B 1 271 ? -3.212  42.059 -10.435 1.00 22.83  ? 268 LEU   B CA  1 
ATOM   4681 C  C   . LEU   B 1 271 ? -3.810  43.068 -9.466  1.00 23.69  ? 268 LEU   B C   1 
ATOM   4682 O  O   . LEU   B 1 271 ? -3.533  42.947 -8.233  1.00 23.08  ? 268 LEU   B O   1 
ATOM   4683 C  CB  . LEU   B 1 271 ? -4.131  40.853 -10.600 1.00 22.37  ? 268 LEU   B CB  1 
ATOM   4684 C  CG  . LEU   B 1 271 ? -3.553  39.720 -11.445 1.00 22.08  ? 268 LEU   B CG  1 
ATOM   4685 C  CD1 . LEU   B 1 271 ? -4.593  38.618 -11.556 1.00 22.03  ? 268 LEU   B CD1 1 
ATOM   4686 C  CD2 . LEU   B 1 271 ? -3.115  40.199 -12.858 1.00 22.34  ? 268 LEU   B CD2 1 
ATOM   4687 N  N   . ALA   B 1 272 ? -4.606  43.991 -9.971  1.00 23.91  ? 269 ALA   B N   1 
ATOM   4688 C  CA  . ALA   B 1 272 ? -5.400  44.938 -9.153  1.00 25.63  ? 269 ALA   B CA  1 
ATOM   4689 C  C   . ALA   B 1 272 ? -6.755  45.085 -9.832  1.00 25.98  ? 269 ALA   B C   1 
ATOM   4690 O  O   . ALA   B 1 272 ? -6.786  45.526 -10.967 1.00 27.12  ? 269 ALA   B O   1 
ATOM   4691 C  CB  . ALA   B 1 272 ? -4.689  46.262 -8.964  1.00 26.56  ? 269 ALA   B CB  1 
ATOM   4692 N  N   . LYS   B 1 273 ? -7.805  44.615 -9.182  1.00 25.83  ? 270 LYS   B N   1 
ATOM   4693 C  CA  . LYS   B 1 273 ? -9.182  44.845 -9.655  1.00 26.90  ? 270 LYS   B CA  1 
ATOM   4694 C  C   . LYS   B 1 273 ? -9.633  46.169 -9.057  1.00 28.93  ? 270 LYS   B C   1 
ATOM   4695 O  O   . LYS   B 1 273 ? -9.449  46.381 -7.830  1.00 30.22  ? 270 LYS   B O   1 
ATOM   4696 C  CB  . LYS   B 1 273 ? -10.128 43.711 -9.239  1.00 26.93  ? 270 LYS   B CB  1 
ATOM   4697 C  CG  . LYS   B 1 273 ? -11.598 43.934 -9.562  1.00 27.68  ? 270 LYS   B CG  1 
ATOM   4698 C  CD  . LYS   B 1 273 ? -12.351 44.634 -8.446  1.00 28.99  ? 270 LYS   B CD  1 
ATOM   4699 C  CE  . LYS   B 1 273 ? -13.826 44.817 -8.718  1.00 30.01  ? 270 LYS   B CE  1 
ATOM   4700 N  NZ  . LYS   B 1 273 ? -14.469 45.446 -7.539  1.00 31.19  ? 270 LYS   B NZ  1 
ATOM   4701 N  N   . SER   B 1 274 ? -10.184 47.022 -9.898  1.00 29.29  ? 271 SER   B N   1 
ATOM   4702 C  CA  . SER   B 1 274 ? -10.981 48.200 -9.488  1.00 31.43  ? 271 SER   B CA  1 
ATOM   4703 C  C   . SER   B 1 274 ? -11.993 48.482 -10.589 1.00 31.94  ? 271 SER   B C   1 
ATOM   4704 O  O   . SER   B 1 274 ? -11.588 48.541 -11.757 1.00 31.68  ? 271 SER   B O   1 
ATOM   4705 C  CB  . SER   B 1 274 ? -10.131 49.418 -9.243  1.00 32.67  ? 271 SER   B CB  1 
ATOM   4706 O  OG  . SER   B 1 274 ? -10.922 50.560 -8.871  1.00 34.60  ? 271 SER   B OG  1 
ATOM   4707 N  N   . TYR   B 1 275 ? -13.252 48.655 -10.201 1.00 33.43  ? 272 TYR   B N   1 
ATOM   4708 C  CA  . TYR   B 1 275 ? -14.359 49.110 -11.076 1.00 35.05  ? 272 TYR   B CA  1 
ATOM   4709 C  C   . TYR   B 1 275 ? -14.580 50.600 -10.811 1.00 37.76  ? 272 TYR   B C   1 
ATOM   4710 O  O   . TYR   B 1 275 ? -15.613 51.111 -11.193 1.00 38.35  ? 272 TYR   B O   1 
ATOM   4711 C  CB  . TYR   B 1 275 ? -15.605 48.252 -10.866 1.00 34.30  ? 272 TYR   B CB  1 
ATOM   4712 C  CG  . TYR   B 1 275 ? -15.610 47.018 -11.733 1.00 32.49  ? 272 TYR   B CG  1 
ATOM   4713 C  CD1 . TYR   B 1 275 ? -14.455 46.260 -11.910 1.00 30.37  ? 272 TYR   B CD1 1 
ATOM   4714 C  CD2 . TYR   B 1 275 ? -16.754 46.634 -12.412 1.00 32.57  ? 272 TYR   B CD2 1 
ATOM   4715 C  CE1 . TYR   B 1 275 ? -14.430 45.161 -12.755 1.00 28.73  ? 272 TYR   B CE1 1 
ATOM   4716 C  CE2 . TYR   B 1 275 ? -16.752 45.524 -13.234 1.00 31.29  ? 272 TYR   B CE2 1 
ATOM   4717 C  CZ  . TYR   B 1 275 ? -15.587 44.786 -13.396 1.00 29.11  ? 272 TYR   B CZ  1 
ATOM   4718 O  OH  . TYR   B 1 275 ? -15.555 43.682 -14.176 1.00 27.43  ? 272 TYR   B OH  1 
ATOM   4719 N  N   . ASN   B 1 276 ? -13.627 51.269 -10.153 1.00 38.80  ? 273 ASN   B N   1 
ATOM   4720 C  CA  . ASN   B 1 276 ? -13.793 52.689 -9.758  1.00 41.77  ? 273 ASN   B CA  1 
ATOM   4721 C  C   . ASN   B 1 276 ? -12.794 53.530 -10.548 1.00 43.49  ? 273 ASN   B C   1 
ATOM   4722 O  O   . ASN   B 1 276 ? -11.587 53.199 -10.537 1.00 42.29  ? 273 ASN   B O   1 
ATOM   4723 C  CB  . ASN   B 1 276 ? -13.630 52.865 -8.254  1.00 43.30  ? 273 ASN   B CB  1 
ATOM   4724 C  CG  . ASN   B 1 276 ? -13.703 54.323 -7.833  1.00 45.61  ? 273 ASN   B CG  1 
ATOM   4725 O  OD1 . ASN   B 1 276 ? -12.696 55.017 -7.867  1.00 46.09  ? 273 ASN   B OD1 1 
ATOM   4726 N  ND2 . ASN   B 1 276 ? -14.887 54.783 -7.471  1.00 47.49  ? 273 ASN   B ND2 1 
ATOM   4727 N  N   . GLU   B 1 277 ? -13.265 54.600 -11.195 1.00 46.58  ? 274 GLU   B N   1 
ATOM   4728 C  CA  . GLU   B 1 277 ? -12.403 55.366 -12.122 1.00 48.70  ? 274 GLU   B CA  1 
ATOM   4729 C  C   . GLU   B 1 277 ? -11.227 56.009 -11.390 1.00 48.67  ? 274 GLU   B C   1 
ATOM   4730 O  O   . GLU   B 1 277 ? -10.126 56.020 -11.985 1.00 46.91  ? 274 GLU   B O   1 
ATOM   4731 C  CB  . GLU   B 1 277 ? -13.157 56.446 -12.877 1.00 53.31  ? 274 GLU   B CB  1 
ATOM   4732 C  CG  . GLU   B 1 277 ? -12.238 57.232 -13.792 1.00 57.16  ? 274 GLU   B CG  1 
ATOM   4733 C  CD  . GLU   B 1 277 ? -13.009 58.112 -14.770 1.00 60.53  ? 274 GLU   B CD  1 
ATOM   4734 O  OE1 . GLU   B 1 277 ? -14.229 58.262 -14.575 1.00 62.31  ? 274 GLU   B OE1 1 
ATOM   4735 O  OE2 . GLU   B 1 277 ? -12.408 58.591 -15.755 1.00 63.05  ? 274 GLU   B OE2 1 
ATOM   4736 N  N   . GLN   B 1 278 ? -11.425 56.540 -10.177 1.00 50.02  ? 275 GLN   B N   1 
ATOM   4737 C  CA  . GLN   B 1 278 ? -10.312 57.200 -9.440  1.00 51.52  ? 275 GLN   B CA  1 
ATOM   4738 C  C   . GLN   B 1 278 ? -9.291  56.136 -9.015  1.00 46.97  ? 275 GLN   B C   1 
ATOM   4739 O  O   . GLN   B 1 278 ? -8.100  56.413 -9.132  1.00 46.41  ? 275 GLN   B O   1 
ATOM   4740 C  CB  . GLN   B 1 278 ? -10.823 58.027 -8.257  1.00 56.87  ? 275 GLN   B CB  1 
ATOM   4741 C  CG  . GLN   B 1 278 ? -12.067 58.855 -8.613  1.00 63.77  ? 275 GLN   B CG  1 
ATOM   4742 C  CD  . GLN   B 1 278 ? -12.786 59.447 -7.417  1.00 69.94  ? 275 GLN   B CD  1 
ATOM   4743 O  OE1 . GLN   B 1 278 ? -12.821 58.855 -6.333  1.00 73.94  ? 275 GLN   B OE1 1 
ATOM   4744 N  NE2 . GLN   B 1 278 ? -13.371 60.629 -7.600  1.00 75.83  ? 275 GLN   B NE2 1 
ATOM   4745 N  N   . ARG   B 1 279 ? -9.737  54.971 -8.540  1.00 43.35  ? 276 ARG   B N   1 
ATOM   4746 C  CA  . ARG   B 1 279 ? -8.838  53.900 -8.035  1.00 41.46  ? 276 ARG   B CA  1 
ATOM   4747 C  C   . ARG   B 1 279 ? -8.082  53.273 -9.199  1.00 39.15  ? 276 ARG   B C   1 
ATOM   4748 O  O   . ARG   B 1 279 ? -6.890  53.004 -9.025  1.00 38.36  ? 276 ARG   B O   1 
ATOM   4749 C  CB  . ARG   B 1 279 ? -9.628  52.930 -7.153  1.00 40.20  ? 276 ARG   B CB  1 
ATOM   4750 C  CG  . ARG   B 1 279 ? -10.036 53.615 -5.859  1.00 42.79  ? 276 ARG   B CG  1 
ATOM   4751 C  CD  . ARG   B 1 279 ? -10.463 52.660 -4.789  1.00 42.30  ? 276 ARG   B CD  1 
ATOM   4752 N  NE  . ARG   B 1 279 ? -11.827 52.230 -5.007  1.00 42.30  ? 276 ARG   B NE  1 
ATOM   4753 C  CZ  . ARG   B 1 279 ? -12.914 52.947 -4.742  1.00 45.02  ? 276 ARG   B CZ  1 
ATOM   4754 N  NH1 . ARG   B 1 279 ? -12.830 54.179 -4.258  1.00 46.85  ? 276 ARG   B NH1 1 
ATOM   4755 N  NH2 . ARG   B 1 279 ? -14.101 52.419 -4.973  1.00 45.66  ? 276 ARG   B NH2 1 
ATOM   4756 N  N   . ILE   B 1 280 ? -8.712  53.132 -10.367 1.00 38.93  ? 277 ILE   B N   1 
ATOM   4757 C  CA  . ILE   B 1 280 ? -8.015  52.573 -11.555 1.00 37.31  ? 277 ILE   B CA  1 
ATOM   4758 C  C   . ILE   B 1 280 ? -6.820  53.470 -11.913 1.00 38.79  ? 277 ILE   B C   1 
ATOM   4759 O  O   . ILE   B 1 280 ? -5.706  52.949 -12.134 1.00 37.73  ? 277 ILE   B O   1 
ATOM   4760 C  CB  . ILE   B 1 280 ? -9.029  52.402 -12.699 1.00 36.57  ? 277 ILE   B CB  1 
ATOM   4761 C  CG1 . ILE   B 1 280 ? -10.010 51.277 -12.367 1.00 35.10  ? 277 ILE   B CG1 1 
ATOM   4762 C  CG2 . ILE   B 1 280 ? -8.312  52.175 -14.006 1.00 36.38  ? 277 ILE   B CG2 1 
ATOM   4763 C  CD1 . ILE   B 1 280 ? -11.209 51.219 -13.288 1.00 35.27  ? 277 ILE   B CD1 1 
ATOM   4764 N  N   . ARG   B 1 281 ? -7.038  54.775 -11.974 1.00 42.46  ? 278 ARG   B N   1 
ATOM   4765 C  CA  . ARG   B 1 281 ? -5.975  55.799 -12.230 1.00 46.36  ? 278 ARG   B CA  1 
ATOM   4766 C  C   . ARG   B 1 281 ? -4.964  55.808 -11.074 1.00 45.61  ? 278 ARG   B C   1 
ATOM   4767 O  O   . ARG   B 1 281 ? -3.769  55.871 -11.355 1.00 45.94  ? 278 ARG   B O   1 
ATOM   4768 C  CB  . ARG   B 1 281 ? -6.599  57.185 -12.449 1.00 51.01  ? 278 ARG   B CB  1 
ATOM   4769 C  CG  . ARG   B 1 281 ? -7.428  57.305 -13.726 1.00 53.79  ? 278 ARG   B CG  1 
ATOM   4770 C  CD  . ARG   B 1 281 ? -6.802  58.298 -14.699 1.00 58.83  ? 278 ARG   B CD  1 
ATOM   4771 N  NE  . ARG   B 1 281 ? -7.043  58.054 -16.126 1.00 61.62  ? 278 ARG   B NE  1 
ATOM   4772 C  CZ  . ARG   B 1 281 ? -6.165  58.312 -17.106 1.00 64.25  ? 278 ARG   B CZ  1 
ATOM   4773 N  NH1 . ARG   B 1 281 ? -4.966  58.799 -16.824 1.00 67.16  ? 278 ARG   B NH1 1 
ATOM   4774 N  NH2 . ARG   B 1 281 ? -6.490  58.096 -18.370 1.00 66.09  ? 278 ARG   B NH2 1 
ATOM   4775 N  N   . GLN   B 1 282 ? -5.407  55.674 -9.828  1.00 45.23  ? 279 GLN   B N   1 
ATOM   4776 C  CA  . GLN   B 1 282 ? -4.452  55.616 -8.670  1.00 45.67  ? 279 GLN   B CA  1 
ATOM   4777 C  C   . GLN   B 1 282 ? -3.514  54.395 -8.776  1.00 42.75  ? 279 GLN   B C   1 
ATOM   4778 O  O   . GLN   B 1 282 ? -2.325  54.509 -8.458  1.00 43.12  ? 279 GLN   B O   1 
ATOM   4779 C  CB  . GLN   B 1 282 ? -5.190  55.536 -7.340  1.00 46.05  ? 279 GLN   B CB  1 
ATOM   4780 C  CG  . GLN   B 1 282 ? -4.266  55.662 -6.121  1.00 47.88  ? 279 GLN   B CG  1 
ATOM   4781 C  CD  . GLN   B 1 282 ? -5.048  55.333 -4.877  1.00 47.88  ? 279 GLN   B CD  1 
ATOM   4782 O  OE1 . GLN   B 1 282 ? -4.868  54.293 -4.262  1.00 46.29  ? 279 GLN   B OE1 1 
ATOM   4783 N  NE2 . GLN   B 1 282 ? -6.034  56.157 -4.593  1.00 50.45  ? 279 GLN   B NE2 1 
ATOM   4784 N  N   . ASN   B 1 283 ? -4.000  53.227 -9.173  1.00 40.03  ? 280 ASN   B N   1 
ATOM   4785 C  CA  . ASN   B 1 283 ? -3.166  52.004 -9.020  1.00 37.87  ? 280 ASN   B CA  1 
ATOM   4786 C  C   . ASN   B 1 283 ? -1.962  52.009 -9.971  1.00 37.76  ? 280 ASN   B C   1 
ATOM   4787 O  O   . ASN   B 1 283 ? -0.982  51.294 -9.661  1.00 35.47  ? 280 ASN   B O   1 
ATOM   4788 C  CB  . ASN   B 1 283 ? -3.980  50.727 -9.202  1.00 36.25  ? 280 ASN   B CB  1 
ATOM   4789 C  CG  . ASN   B 1 283 ? -4.978  50.524 -8.082  1.00 36.51  ? 280 ASN   B CG  1 
ATOM   4790 O  OD1 . ASN   B 1 283 ? -4.848  51.146 -7.029  1.00 38.48  ? 280 ASN   B OD1 1 
ATOM   4791 N  ND2 . ASN   B 1 283 ? -5.967  49.664 -8.307  1.00 34.06  ? 280 ASN   B ND2 1 
ATOM   4792 N  N   . VAL   B 1 284 ? -1.976  52.805 -11.053 1.00 38.91  ? 281 VAL   B N   1 
ATOM   4793 C  CA  . VAL   B 1 284 ? -0.799  52.878 -11.968 1.00 39.88  ? 281 VAL   B CA  1 
ATOM   4794 C  C   . VAL   B 1 284 ? 0.280   53.720 -11.277 1.00 42.11  ? 281 VAL   B C   1 
ATOM   4795 O  O   . VAL   B 1 284 ? 1.420   53.596 -11.697 1.00 42.25  ? 281 VAL   B O   1 
ATOM   4796 C  CB  . VAL   B 1 284 ? -1.144  53.337 -13.399 1.00 41.16  ? 281 VAL   B CB  1 
ATOM   4797 C  CG1 . VAL   B 1 284 ? -2.262  52.477 -13.999 1.00 39.27  ? 281 VAL   B CG1 1 
ATOM   4798 C  CG2 . VAL   B 1 284 ? -1.527  54.804 -13.503 1.00 44.70  ? 281 VAL   B CG2 1 
ATOM   4799 N  N   . GLN   B 1 285 ? -0.049  54.464 -10.210 1.00 43.90  ? 282 GLN   B N   1 
ATOM   4800 C  CA  . GLN   B 1 285 ? 0.949   55.207 -9.365  1.00 47.33  ? 282 GLN   B CA  1 
ATOM   4801 C  C   . GLN   B 1 285 ? 1.914   54.224 -8.660  1.00 45.94  ? 282 GLN   B C   1 
ATOM   4802 O  O   . GLN   B 1 285 ? 2.843   54.705 -7.990  1.00 47.95  ? 282 GLN   B O   1 
ATOM   4803 C  CB  . GLN   B 1 285 ? 0.237   56.211 -8.433  1.00 50.96  ? 282 GLN   B CB  1 
ATOM   4804 C  CG  . GLN   B 1 285 ? -0.482  57.332 -9.221  1.00 54.49  ? 282 GLN   B CG  1 
ATOM   4805 C  CD  . GLN   B 1 285 ? -1.652  58.085 -8.599  1.00 58.17  ? 282 GLN   B CD  1 
ATOM   4806 O  OE1 . GLN   B 1 285 ? -1.718  58.336 -7.393  1.00 60.37  ? 282 GLN   B OE1 1 
ATOM   4807 N  NE2 . GLN   B 1 285 ? -2.577  58.547 -9.449  1.00 61.80  ? 282 GLN   B NE2 1 
ATOM   4808 N  N   . VAL   B 1 286 ? 1.803   52.908 -8.861  1.00 42.16  ? 283 VAL   B N   1 
ATOM   4809 C  CA  . VAL   B 1 286 ? 2.722   51.904 -8.238  1.00 42.03  ? 283 VAL   B CA  1 
ATOM   4810 C  C   . VAL   B 1 286 ? 4.131   52.076 -8.825  1.00 43.41  ? 283 VAL   B C   1 
ATOM   4811 O  O   . VAL   B 1 286 ? 5.089   51.648 -8.164  1.00 44.63  ? 283 VAL   B O   1 
ATOM   4812 C  CB  . VAL   B 1 286 ? 2.233   50.438 -8.410  1.00 38.36  ? 283 VAL   B CB  1 
ATOM   4813 C  CG1 . VAL   B 1 286 ? 2.344   49.950 -9.862  1.00 37.43  ? 283 VAL   B CG1 1 
ATOM   4814 C  CG2 . VAL   B 1 286 ? 2.963   49.478 -7.490  1.00 37.05  ? 283 VAL   B CG2 1 
ATOM   4815 N  N   . PHE   B 1 287 ? 4.290   52.618 -10.037 1.00 44.93  ? 284 PHE   B N   1 
ATOM   4816 C  CA  . PHE   B 1 287 ? 5.648   52.722 -10.641 1.00 46.42  ? 284 PHE   B CA  1 
ATOM   4817 C  C   . PHE   B 1 287 ? 6.317   53.998 -10.149 1.00 49.56  ? 284 PHE   B C   1 
ATOM   4818 O  O   . PHE   B 1 287 ? 7.448   54.204 -10.539 1.00 51.63  ? 284 PHE   B O   1 
ATOM   4819 C  CB  . PHE   B 1 287 ? 5.612   52.675 -12.168 1.00 46.90  ? 284 PHE   B CB  1 
ATOM   4820 C  CG  . PHE   B 1 287 ? 5.054   51.381 -12.704 1.00 44.51  ? 284 PHE   B CG  1 
ATOM   4821 C  CD1 . PHE   B 1 287 ? 5.824   50.227 -12.670 1.00 43.79  ? 284 PHE   B CD1 1 
ATOM   4822 C  CD2 . PHE   B 1 287 ? 3.760   51.298 -13.214 1.00 43.56  ? 284 PHE   B CD2 1 
ATOM   4823 C  CE1 . PHE   B 1 287 ? 5.326   49.019 -13.126 1.00 41.04  ? 284 PHE   B CE1 1 
ATOM   4824 C  CE2 . PHE   B 1 287 ? 3.255   50.079 -13.657 1.00 41.41  ? 284 PHE   B CE2 1 
ATOM   4825 C  CZ  . PHE   B 1 287 ? 4.043   48.944 -13.625 1.00 40.92  ? 284 PHE   B CZ  1 
ATOM   4826 N  N   . GLU   B 1 288 ? 5.635   54.813 -9.342  1.00 51.26  ? 285 GLU   B N   1 
ATOM   4827 C  CA  . GLU   B 1 288 ? 6.057   56.211 -9.033  1.00 55.40  ? 285 GLU   B CA  1 
ATOM   4828 C  C   . GLU   B 1 288 ? 6.824   56.289 -7.705  1.00 55.98  ? 285 GLU   B C   1 
ATOM   4829 O  O   . GLU   B 1 288 ? 7.169   57.410 -7.312  1.00 56.43  ? 285 GLU   B O   1 
ATOM   4830 C  CB  . GLU   B 1 288 ? 4.856   57.159 -8.898  1.00 57.96  ? 285 GLU   B CB  1 
ATOM   4831 C  CG  . GLU   B 1 288 ? 4.019   57.336 -10.161 1.00 58.65  ? 285 GLU   B CG  1 
ATOM   4832 C  CD  . GLU   B 1 288 ? 2.814   58.268 -10.000 1.00 61.39  ? 285 GLU   B CD  1 
ATOM   4833 O  OE1 . GLU   B 1 288 ? 2.615   58.790 -8.889  1.00 62.83  ? 285 GLU   B OE1 1 
ATOM   4834 O  OE2 . GLU   B 1 288 ? 2.048   58.463 -10.992 1.00 63.46  ? 285 GLU   B OE2 1 
ATOM   4835 N  N   . PHE   B 1 289 ? 7.056   55.174 -7.005  1.00 53.04  ? 286 PHE   B N   1 
ATOM   4836 C  CA  . PHE   B 1 289 ? 7.702   55.233 -5.667  1.00 54.27  ? 286 PHE   B CA  1 
ATOM   4837 C  C   . PHE   B 1 289 ? 8.281   53.875 -5.274  1.00 52.71  ? 286 PHE   B C   1 
ATOM   4838 O  O   . PHE   B 1 289 ? 7.897   52.853 -5.875  1.00 49.70  ? 286 PHE   B O   1 
ATOM   4839 C  CB  . PHE   B 1 289 ? 6.710   55.701 -4.606  1.00 54.35  ? 286 PHE   B CB  1 
ATOM   4840 C  CG  . PHE   B 1 289 ? 5.700   54.673 -4.150  1.00 51.10  ? 286 PHE   B CG  1 
ATOM   4841 C  CD1 . PHE   B 1 289 ? 4.523   54.461 -4.848  1.00 49.39  ? 286 PHE   B CD1 1 
ATOM   4842 C  CD2 . PHE   B 1 289 ? 5.906   53.970 -2.963  1.00 50.09  ? 286 PHE   B CD2 1 
ATOM   4843 C  CE1 . PHE   B 1 289 ? 3.611   53.515 -4.408  1.00 46.82  ? 286 PHE   B CE1 1 
ATOM   4844 C  CE2 . PHE   B 1 289 ? 4.960   53.077 -2.492  1.00 47.11  ? 286 PHE   B CE2 1 
ATOM   4845 C  CZ  . PHE   B 1 289 ? 3.805   52.876 -3.207  1.00 45.69  ? 286 PHE   B CZ  1 
ATOM   4846 N  N   . GLN   B 1 290 ? 9.173   53.894 -4.278  1.00 54.42  ? 287 GLN   B N   1 
ATOM   4847 C  CA  . GLN   B 1 290 ? 9.863   52.687 -3.759  1.00 54.20  ? 287 GLN   B CA  1 
ATOM   4848 C  C   . GLN   B 1 290 ? 9.683   52.533 -2.251  1.00 52.41  ? 287 GLN   B C   1 
ATOM   4849 O  O   . GLN   B 1 290 ? 9.741   53.561 -1.532  1.00 53.87  ? 287 GLN   B O   1 
ATOM   4850 C  CB  . GLN   B 1 290 ? 11.351  52.806 -4.029  1.00 59.47  ? 287 GLN   B CB  1 
ATOM   4851 C  CG  . GLN   B 1 290 ? 11.725  52.406 -5.436  1.00 61.83  ? 287 GLN   B CG  1 
ATOM   4852 C  CD  . GLN   B 1 290 ? 13.190  52.667 -5.639  1.00 65.87  ? 287 GLN   B CD  1 
ATOM   4853 O  OE1 . GLN   B 1 290 ? 14.029  52.086 -4.958  1.00 67.81  ? 287 GLN   B OE1 1 
ATOM   4854 N  NE2 . GLN   B 1 290 ? 13.493  53.571 -6.558  1.00 70.31  ? 287 GLN   B NE2 1 
ATOM   4855 N  N   . LEU   B 1 291 ? 9.553   51.281 -1.798  1.00 48.18  ? 288 LEU   B N   1 
ATOM   4856 C  CA  . LEU   B 1 291 ? 9.601   50.887 -0.368  1.00 47.21  ? 288 LEU   B CA  1 
ATOM   4857 C  C   . LEU   B 1 291 ? 11.054  50.613 0.016   1.00 47.69  ? 288 LEU   B C   1 
ATOM   4858 O  O   . LEU   B 1 291 ? 11.800  50.149 -0.840  1.00 46.38  ? 288 LEU   B O   1 
ATOM   4859 C  CB  . LEU   B 1 291 ? 8.745   49.627 -0.183  1.00 44.15  ? 288 LEU   B CB  1 
ATOM   4860 C  CG  . LEU   B 1 291 ? 7.275   49.781 -0.573  1.00 42.28  ? 288 LEU   B CG  1 
ATOM   4861 C  CD1 . LEU   B 1 291 ? 6.587   48.431 -0.557  1.00 39.29  ? 288 LEU   B CD1 1 
ATOM   4862 C  CD2 . LEU   B 1 291 ? 6.556   50.758 0.352   1.00 43.69  ? 288 LEU   B CD2 1 
ATOM   4863 N  N   . THR   B 1 292 ? 11.423  50.896 1.265   1.00 49.91  ? 289 THR   B N   1 
ATOM   4864 C  CA  . THR   B 1 292 ? 12.780  50.645 1.827   1.00 51.36  ? 289 THR   B CA  1 
ATOM   4865 C  C   . THR   B 1 292 ? 12.856  49.188 2.284   1.00 49.34  ? 289 THR   B C   1 
ATOM   4866 O  O   . THR   B 1 292 ? 11.812  48.529 2.259   1.00 47.36  ? 289 THR   B O   1 
ATOM   4867 C  CB  . THR   B 1 292 ? 13.078  51.581 2.996   1.00 54.29  ? 289 THR   B CB  1 
ATOM   4868 O  OG1 . THR   B 1 292 ? 12.233  51.208 4.090   1.00 52.44  ? 289 THR   B OG1 1 
ATOM   4869 C  CG2 . THR   B 1 292 ? 12.893  53.032 2.593   1.00 56.92  ? 289 THR   B CG2 1 
ATOM   4870 N  N   . ALA   B 1 293 ? 14.054  48.721 2.627   1.00 50.28  ? 290 ALA   B N   1 
ATOM   4871 C  CA  . ALA   B 1 293 ? 14.343  47.339 3.067   1.00 49.18  ? 290 ALA   B CA  1 
ATOM   4872 C  C   . ALA   B 1 293 ? 13.513  47.080 4.322   1.00 48.61  ? 290 ALA   B C   1 
ATOM   4873 O  O   . ALA   B 1 293 ? 12.924  45.972 4.457   1.00 46.10  ? 290 ALA   B O   1 
ATOM   4874 C  CB  . ALA   B 1 293 ? 15.826  47.196 3.333   1.00 51.03  ? 290 ALA   B CB  1 
ATOM   4875 N  N   . GLU   B 1 294 ? 13.481  48.073 5.211   1.00 50.60  ? 291 GLU   B N   1 
ATOM   4876 C  CA  . GLU   B 1 294 ? 12.754  47.980 6.497   1.00 51.24  ? 291 GLU   B CA  1 
ATOM   4877 C  C   . GLU   B 1 294 ? 11.248  47.972 6.229   1.00 47.98  ? 291 GLU   B C   1 
ATOM   4878 O  O   . GLU   B 1 294 ? 10.530  47.234 6.896   1.00 46.08  ? 291 GLU   B O   1 
ATOM   4879 C  CB  . GLU   B 1 294 ? 13.155  49.109 7.454   1.00 55.61  ? 291 GLU   B CB  1 
ATOM   4880 C  CG  . GLU   B 1 294 ? 14.427  48.799 8.242   1.00 58.83  ? 291 GLU   B CG  1 
ATOM   4881 C  CD  . GLU   B 1 294 ? 14.448  47.510 9.072   1.00 58.17  ? 291 GLU   B CD  1 
ATOM   4882 O  OE1 . GLU   B 1 294 ? 13.455  47.225 9.791   1.00 57.20  ? 291 GLU   B OE1 1 
ATOM   4883 O  OE2 . GLU   B 1 294 ? 15.474  46.800 9.015   1.00 59.96  ? 291 GLU   B OE2 1 
ATOM   4884 N  N   . ASP   B 1 295 ? 10.782  48.793 5.295   1.00 47.80  ? 292 ASP   B N   1 
ATOM   4885 C  CA  . ASP   B 1 295 ? 9.367   48.772 4.849   1.00 45.48  ? 292 ASP   B CA  1 
ATOM   4886 C  C   . ASP   B 1 295 ? 9.015   47.339 4.413   1.00 42.37  ? 292 ASP   B C   1 
ATOM   4887 O  O   . ASP   B 1 295 ? 7.986   46.834 4.859   1.00 40.49  ? 292 ASP   B O   1 
ATOM   4888 C  CB  . ASP   B 1 295 ? 9.130   49.762 3.706   1.00 46.18  ? 292 ASP   B CB  1 
ATOM   4889 C  CG  . ASP   B 1 295 ? 9.230   51.257 4.012   1.00 49.92  ? 292 ASP   B CG  1 
ATOM   4890 O  OD1 . ASP   B 1 295 ? 9.272   51.660 5.198   1.00 50.76  ? 292 ASP   B OD1 1 
ATOM   4891 O  OD2 . ASP   B 1 295 ? 9.250   52.034 3.010   1.00 52.11  ? 292 ASP   B OD2 1 
ATOM   4892 N  N   . MET   B 1 296 ? 9.828   46.743 3.532   1.00 42.19  ? 293 MET   B N   1 
ATOM   4893 C  CA  . MET   B 1 296 ? 9.596   45.389 2.949   1.00 40.36  ? 293 MET   B CA  1 
ATOM   4894 C  C   . MET   B 1 296 ? 9.641   44.310 4.052   1.00 40.38  ? 293 MET   B C   1 
ATOM   4895 O  O   . MET   B 1 296 ? 8.811   43.391 4.012   1.00 38.60  ? 293 MET   B O   1 
ATOM   4896 C  CB  . MET   B 1 296 ? 10.637  45.039 1.882   1.00 40.49  ? 293 MET   B CB  1 
ATOM   4897 C  CG  . MET   B 1 296 ? 10.491  45.854 0.602   1.00 41.31  ? 293 MET   B CG  1 
ATOM   4898 S  SD  . MET   B 1 296 ? 8.971   45.554 -0.370  1.00 39.63  ? 293 MET   B SD  1 
ATOM   4899 C  CE  . MET   B 1 296 ? 9.294   43.882 -0.911  1.00 37.37  ? 293 MET   B CE  1 
ATOM   4900 N  N   . LYS   B 1 297 ? 10.541  44.438 5.025   1.00 41.68  ? 294 LYS   B N   1 
ATOM   4901 C  CA  . LYS   B 1 297 ? 10.641  43.502 6.180   1.00 41.68  ? 294 LYS   B CA  1 
ATOM   4902 C  C   . LYS   B 1 297 ? 9.360   43.618 7.027   1.00 40.15  ? 294 LYS   B C   1 
ATOM   4903 O  O   . LYS   B 1 297 ? 8.812   42.580 7.463   1.00 38.18  ? 294 LYS   B O   1 
ATOM   4904 C  CB  . LYS   B 1 297 ? 11.929  43.815 6.955   1.00 46.07  ? 294 LYS   B CB  1 
ATOM   4905 C  CG  . LYS   B 1 297 ? 12.294  42.853 8.073   1.00 48.46  ? 294 LYS   B CG  1 
ATOM   4906 C  CD  . LYS   B 1 297 ? 13.730  43.036 8.554   1.00 52.44  ? 294 LYS   B CD  1 
ATOM   4907 C  CE  . LYS   B 1 297 ? 13.875  43.064 10.061  1.00 55.32  ? 294 LYS   B CE  1 
ATOM   4908 N  NZ  . LYS   B 1 297 ? 15.021  43.920 10.473  1.00 59.11  ? 294 LYS   B NZ  1 
ATOM   4909 N  N   . ALA   B 1 298 ? 8.844   44.827 7.245   1.00 40.14  ? 295 ALA   B N   1 
ATOM   4910 C  CA  . ALA   B 1 298 ? 7.619   45.016 8.054   1.00 40.09  ? 295 ALA   B CA  1 
ATOM   4911 C  C   . ALA   B 1 298 ? 6.449   44.344 7.342   1.00 37.89  ? 295 ALA   B C   1 
ATOM   4912 O  O   . ALA   B 1 298 ? 5.589   43.805 8.050   1.00 37.65  ? 295 ALA   B O   1 
ATOM   4913 C  CB  . ALA   B 1 298 ? 7.319   46.465 8.308   1.00 41.78  ? 295 ALA   B CB  1 
ATOM   4914 N  N   . ILE   B 1 299 ? 6.370   44.440 6.011   1.00 36.60  ? 296 ILE   B N   1 
ATOM   4915 C  CA  . ILE   B 1 299 ? 5.213   43.845 5.272   1.00 34.74  ? 296 ILE   B CA  1 
ATOM   4916 C  C   . ILE   B 1 299 ? 5.379   42.322 5.325   1.00 33.54  ? 296 ILE   B C   1 
ATOM   4917 O  O   . ILE   B 1 299 ? 4.378   41.634 5.564   1.00 31.81  ? 296 ILE   B O   1 
ATOM   4918 C  CB  . ILE   B 1 299 ? 5.061   44.415 3.842   1.00 33.92  ? 296 ILE   B CB  1 
ATOM   4919 C  CG1 . ILE   B 1 299 ? 4.868   45.928 3.885   1.00 35.62  ? 296 ILE   B CG1 1 
ATOM   4920 C  CG2 . ILE   B 1 299 ? 3.922   43.763 3.083   1.00 32.18  ? 296 ILE   B CG2 1 
ATOM   4921 C  CD1 . ILE   B 1 299 ? 5.190   46.597 2.585   1.00 35.38  ? 296 ILE   B CD1 1 
ATOM   4922 N  N   . ASP   B 1 300 ? 6.607   41.831 5.141   1.00 33.86  ? 297 ASP   B N   1 
ATOM   4923 C  CA  . ASP   B 1 300 ? 6.928   40.379 5.256   1.00 33.48  ? 297 ASP   B CA  1 
ATOM   4924 C  C   . ASP   B 1 300 ? 6.403   39.839 6.596   1.00 33.42  ? 297 ASP   B C   1 
ATOM   4925 O  O   . ASP   B 1 300 ? 5.871   38.719 6.656   1.00 31.59  ? 297 ASP   B O   1 
ATOM   4926 C  CB  . ASP   B 1 300 ? 8.433   40.140 5.180   1.00 35.00  ? 297 ASP   B CB  1 
ATOM   4927 C  CG  . ASP   B 1 300 ? 9.053   40.246 3.798   1.00 35.88  ? 297 ASP   B CG  1 
ATOM   4928 O  OD1 . ASP   B 1 300 ? 8.315   40.118 2.751   1.00 35.45  ? 297 ASP   B OD1 1 
ATOM   4929 O  OD2 . ASP   B 1 300 ? 10.273  40.478 3.746   1.00 37.73  ? 297 ASP   B OD2 1 
ATOM   4930 N  N   . GLY   B 1 301 ? 6.537   40.633 7.650   1.00 35.04  ? 298 GLY   B N   1 
ATOM   4931 C  CA  . GLY   B 1 301 ? 6.127   40.270 9.020   1.00 36.56  ? 298 GLY   B CA  1 
ATOM   4932 C  C   . GLY   B 1 301 ? 4.625   40.111 9.197   1.00 37.04  ? 298 GLY   B C   1 
ATOM   4933 O  O   . GLY   B 1 301 ? 4.254   39.505 10.213  1.00 38.04  ? 298 GLY   B O   1 
ATOM   4934 N  N   . LEU   B 1 302 ? 3.792   40.553 8.250   1.00 36.16  ? 299 LEU   B N   1 
ATOM   4935 C  CA  . LEU   B 1 302 ? 2.310   40.451 8.347   1.00 36.02  ? 299 LEU   B CA  1 
ATOM   4936 C  C   . LEU   B 1 302 ? 1.824   39.068 7.927   1.00 34.91  ? 299 LEU   B C   1 
ATOM   4937 O  O   . LEU   B 1 302 ? 0.580   38.794 8.090   1.00 34.19  ? 299 LEU   B O   1 
ATOM   4938 C  CB  . LEU   B 1 302 ? 1.693   41.482 7.409   1.00 36.16  ? 299 LEU   B CB  1 
ATOM   4939 C  CG  . LEU   B 1 302 ? 1.936   42.933 7.779   1.00 38.64  ? 299 LEU   B CG  1 
ATOM   4940 C  CD1 . LEU   B 1 302 ? 1.368   43.860 6.733   1.00 38.74  ? 299 LEU   B CD1 1 
ATOM   4941 C  CD2 . LEU   B 1 302 ? 1.331   43.214 9.149   1.00 40.85  ? 299 LEU   B CD2 1 
ATOM   4942 N  N   . ASP   B 1 303 ? 2.710   38.248 7.340   1.00 34.33  ? 300 ASP   B N   1 
ATOM   4943 C  CA  . ASP   B 1 303 ? 2.319   36.923 6.789   1.00 34.31  ? 300 ASP   B CA  1 
ATOM   4944 C  C   . ASP   B 1 303 ? 1.638   36.069 7.866   1.00 36.34  ? 300 ASP   B C   1 
ATOM   4945 O  O   . ASP   B 1 303 ? 2.177   35.920 8.988   1.00 36.88  ? 300 ASP   B O   1 
ATOM   4946 C  CB  . ASP   B 1 303 ? 3.513   36.209 6.164   1.00 34.44  ? 300 ASP   B CB  1 
ATOM   4947 C  CG  . ASP   B 1 303 ? 3.128   35.041 5.296   1.00 33.78  ? 300 ASP   B CG  1 
ATOM   4948 O  OD1 . ASP   B 1 303 ? 2.094   35.081 4.685   1.00 31.63  ? 300 ASP   B OD1 1 
ATOM   4949 O  OD2 . ASP   B 1 303 ? 3.908   34.115 5.253   1.00 36.62  ? 300 ASP   B OD2 1 
ATOM   4950 N  N   . ARG   B 1 304 ? 0.484   35.509 7.534   1.00 37.25  ? 301 ARG   B N   1 
ATOM   4951 C  CA  . ARG   B 1 304 ? -0.265  34.675 8.493   1.00 39.68  ? 301 ARG   B CA  1 
ATOM   4952 C  C   . ARG   B 1 304 ? -0.975  33.521 7.811   1.00 40.42  ? 301 ARG   B C   1 
ATOM   4953 O  O   . ARG   B 1 304 ? -1.898  32.986 8.450   1.00 42.95  ? 301 ARG   B O   1 
ATOM   4954 C  CB  . ARG   B 1 304 ? -1.215  35.530 9.337   1.00 41.76  ? 301 ARG   B CB  1 
ATOM   4955 C  CG  . ARG   B 1 304 ? -2.357  36.213 8.606   1.00 41.51  ? 301 ARG   B CG  1 
ATOM   4956 C  CD  . ARG   B 1 304 ? -2.878  37.285 9.557   1.00 44.13  ? 301 ARG   B CD  1 
ATOM   4957 N  NE  . ARG   B 1 304 ? -1.879  38.347 9.690   1.00 45.26  ? 301 ARG   B NE  1 
ATOM   4958 C  CZ  . ARG   B 1 304 ? -2.043  39.531 10.281  1.00 46.57  ? 301 ARG   B CZ  1 
ATOM   4959 N  NH1 . ARG   B 1 304 ? -3.184  39.855 10.880  1.00 48.07  ? 301 ARG   B NH1 1 
ATOM   4960 N  NH2 . ARG   B 1 304 ? -1.042  40.396 10.252  1.00 46.13  ? 301 ARG   B NH2 1 
ATOM   4961 N  N   . ASN   B 1 305 ? -0.553  33.103 6.612   1.00 39.16  ? 302 ASN   B N   1 
ATOM   4962 C  CA  . ASN   B 1 305 ? -1.222  31.953 5.961   1.00 39.16  ? 302 ASN   B CA  1 
ATOM   4963 C  C   . ASN   B 1 305 ? -2.746  32.186 5.883   1.00 38.89  ? 302 ASN   B C   1 
ATOM   4964 O  O   . ASN   B 1 305 ? -3.533  31.227 6.094   1.00 39.71  ? 302 ASN   B O   1 
ATOM   4965 C  CB  . ASN   B 1 305 ? -0.954  30.677 6.763   1.00 41.75  ? 302 ASN   B CB  1 
ATOM   4966 C  CG  . ASN   B 1 305 ? -1.262  29.426 5.977   1.00 43.21  ? 302 ASN   B CG  1 
ATOM   4967 O  OD1 . ASN   B 1 305 ? -0.971  29.385 4.787   1.00 44.74  ? 302 ASN   B OD1 1 
ATOM   4968 N  ND2 . ASN   B 1 305 ? -1.861  28.419 6.613   1.00 45.17  ? 302 ASN   B ND2 1 
ATOM   4969 N  N   . LEU   B 1 306 ? -3.191  33.411 5.638   1.00 36.85  ? 303 LEU   B N   1 
ATOM   4970 C  CA  . LEU   B 1 306 ? -4.637  33.673 5.496   1.00 37.37  ? 303 LEU   B CA  1 
ATOM   4971 C  C   . LEU   B 1 306 ? -5.060  33.522 4.038   1.00 35.55  ? 303 LEU   B C   1 
ATOM   4972 O  O   . LEU   B 1 306 ? -4.670  34.360 3.232   1.00 34.95  ? 303 LEU   B O   1 
ATOM   4973 C  CB  . LEU   B 1 306 ? -4.953  35.083 5.966   1.00 39.75  ? 303 LEU   B CB  1 
ATOM   4974 C  CG  . LEU   B 1 306 ? -6.436  35.450 5.905   1.00 41.81  ? 303 LEU   B CG  1 
ATOM   4975 C  CD1 . LEU   B 1 306 ? -7.235  34.600 6.886   1.00 44.94  ? 303 LEU   B CD1 1 
ATOM   4976 C  CD2 . LEU   B 1 306 ? -6.620  36.927 6.208   1.00 42.90  ? 303 LEU   B CD2 1 
ATOM   4977 N  N   . HIS   B 1 307 ? -5.793  32.541 3.678   1.00 38.10  ? 304 HIS   B N   1 
ATOM   4978 C  CA  . HIS   B 1 307 ? -6.439  32.573 2.345   1.00 37.40  ? 304 HIS   B CA  1 
ATOM   4979 C  C   . HIS   B 1 307 ? -7.876  33.047 2.531   1.00 36.95  ? 304 HIS   B C   1 
ATOM   4980 O  O   . HIS   B 1 307 ? -8.547  32.578 3.422   1.00 39.91  ? 304 HIS   B O   1 
ATOM   4981 C  CB  . HIS   B 1 307 ? -6.223  31.308 1.498   1.00 39.75  ? 304 HIS   B CB  1 
ATOM   4982 C  CG  . HIS   B 1 307 ? -6.346  30.006 2.196   1.00 41.75  ? 304 HIS   B CG  1 
ATOM   4983 N  ND1 . HIS   B 1 307 ? -7.574  29.353 2.302   1.00 44.66  ? 304 HIS   B ND1 1 
ATOM   4984 C  CD2 . HIS   B 1 307 ? -5.397  29.185 2.691   1.00 43.10  ? 304 HIS   B CD2 1 
ATOM   4985 C  CE1 . HIS   B 1 307 ? -7.394  28.195 2.900   1.00 47.67  ? 304 HIS   B CE1 1 
ATOM   4986 N  NE2 . HIS   B 1 307 ? -6.060  28.081 3.172   1.00 48.03  ? 304 HIS   B NE2 1 
ATOM   4987 N  N   . TYR   B 1 308 ? -8.228  34.055 1.732   1.00 33.08  ? 305 TYR   B N   1 
ATOM   4988 C  CA  . TYR   B 1 308 ? -9.524  34.748 1.886   1.00 33.23  ? 305 TYR   B CA  1 
ATOM   4989 C  C   . TYR   B 1 308 ? -10.686 33.845 1.445   1.00 35.27  ? 305 TYR   B C   1 
ATOM   4990 O  O   . TYR   B 1 308 ? -11.782 33.922 2.029   1.00 37.40  ? 305 TYR   B O   1 
ATOM   4991 C  CB  . TYR   B 1 308 ? -9.444  36.070 1.140   1.00 31.70  ? 305 TYR   B CB  1 
ATOM   4992 C  CG  . TYR   B 1 308 ? -8.826  37.178 1.952   1.00 30.79  ? 305 TYR   B CG  1 
ATOM   4993 C  CD1 . TYR   B 1 308 ? -9.484  37.662 3.076   1.00 32.18  ? 305 TYR   B CD1 1 
ATOM   4994 C  CD2 . TYR   B 1 308 ? -7.580  37.699 1.648   1.00 29.07  ? 305 TYR   B CD2 1 
ATOM   4995 C  CE1 . TYR   B 1 308 ? -8.948  38.681 3.841   1.00 32.58  ? 305 TYR   B CE1 1 
ATOM   4996 C  CE2 . TYR   B 1 308 ? -7.043  38.752 2.388   1.00 29.43  ? 305 TYR   B CE2 1 
ATOM   4997 C  CZ  . TYR   B 1 308 ? -7.726  39.227 3.491   1.00 31.32  ? 305 TYR   B CZ  1 
ATOM   4998 O  OH  . TYR   B 1 308 ? -7.250  40.241 4.279   1.00 32.83  ? 305 TYR   B OH  1 
ATOM   4999 N  N   . PHE   B 1 309 ? -10.458 32.997 0.446   1.00 53.17  ? 306 PHE   B N   1 
ATOM   5000 C  CA  . PHE   B 1 309 ? -11.499 32.123 -0.146  1.00 52.74  ? 306 PHE   B CA  1 
ATOM   5001 C  C   . PHE   B 1 309 ? -11.479 30.820 0.619   1.00 54.12  ? 306 PHE   B C   1 
ATOM   5002 O  O   . PHE   B 1 309 ? -10.465 30.152 0.648   1.00 51.25  ? 306 PHE   B O   1 
ATOM   5003 C  CB  . PHE   B 1 309 ? -11.206 31.896 -1.628  1.00 47.96  ? 306 PHE   B CB  1 
ATOM   5004 C  CG  . PHE   B 1 309 ? -11.013 33.213 -2.310  1.00 48.52  ? 306 PHE   B CG  1 
ATOM   5005 C  CD1 . PHE   B 1 309 ? -12.101 34.032 -2.541  1.00 51.10  ? 306 PHE   B CD1 1 
ATOM   5006 C  CD2 . PHE   B 1 309 ? -9.750  33.728 -2.508  1.00 48.80  ? 306 PHE   B CD2 1 
ATOM   5007 C  CE1 . PHE   B 1 309 ? -11.950 35.299 -3.076  1.00 51.99  ? 306 PHE   B CE1 1 
ATOM   5008 C  CE2 . PHE   B 1 309 ? -9.597  34.996 -3.058  1.00 50.81  ? 306 PHE   B CE2 1 
ATOM   5009 C  CZ  . PHE   B 1 309 ? -10.700 35.765 -3.368  1.00 51.36  ? 306 PHE   B CZ  1 
ATOM   5010 N  N   A ASN   B 1 310 ? -12.595 30.520 1.278   0.53 59.80  ? 307 ASN   B N   1 
ATOM   5011 N  N   B ASN   B 1 310 ? -12.591 30.433 1.211   0.47 59.31  ? 307 ASN   B N   1 
ATOM   5012 C  CA  A ASN   B 1 310 ? -12.878 29.195 1.882   0.53 62.89  ? 307 ASN   B CA  1 
ATOM   5013 C  CA  B ASN   B 1 310 ? -12.657 29.097 1.838   0.47 61.89  ? 307 ASN   B CA  1 
ATOM   5014 C  C   A ASN   B 1 310 ? -13.626 28.367 0.847   0.53 62.10  ? 307 ASN   B C   1 
ATOM   5015 C  C   B ASN   B 1 310 ? -13.795 28.346 1.185   0.47 63.89  ? 307 ASN   B C   1 
ATOM   5016 O  O   A ASN   B 1 310 ? -14.183 28.953 -0.087  0.53 59.56  ? 307 ASN   B O   1 
ATOM   5017 O  O   B ASN   B 1 310 ? -14.821 28.984 0.842   0.47 64.97  ? 307 ASN   B O   1 
ATOM   5018 C  CB  A ASN   B 1 310 ? -13.677 29.299 3.181   0.53 70.03  ? 307 ASN   B CB  1 
ATOM   5019 C  CB  B ASN   B 1 310 ? -12.694 29.188 3.356   0.47 67.49  ? 307 ASN   B CB  1 
ATOM   5020 C  CG  A ASN   B 1 310 ? -15.146 29.619 2.983   0.53 73.57  ? 307 ASN   B CG  1 
ATOM   5021 C  CG  B ASN   B 1 310 ? -11.287 29.262 3.904   0.47 65.81  ? 307 ASN   B CG  1 
ATOM   5022 O  OD1 A ASN   B 1 310 ? -15.561 30.011 1.896   0.53 70.33  ? 307 ASN   B OD1 1 
ATOM   5023 O  OD1 B ASN   B 1 310 ? -10.527 28.310 3.766   0.47 61.98  ? 307 ASN   B OD1 1 
ATOM   5024 N  ND2 A ASN   B 1 310 ? -15.936 29.472 4.040   0.53 80.96  ? 307 ASN   B ND2 1 
ATOM   5025 N  ND2 B ASN   B 1 310 ? -10.923 30.398 4.471   0.47 68.42  ? 307 ASN   B ND2 1 
ATOM   5026 N  N   . SER   B 1 311 ? -13.574 27.042 0.985   1.00 64.97  ? 308 SER   B N   1 
ATOM   5027 C  CA  . SER   B 1 311 ? -14.636 26.179 0.449   1.00 71.28  ? 308 SER   B CA  1 
ATOM   5028 C  C   . SER   B 1 311 ? -14.475 24.792 1.022   1.00 76.44  ? 308 SER   B C   1 
ATOM   5029 O  O   . SER   B 1 311 ? -13.486 24.114 0.662   1.00 74.53  ? 308 SER   B O   1 
ATOM   5030 C  CB  . SER   B 1 311 ? -14.651 26.171 -1.041  1.00 69.87  ? 308 SER   B CB  1 
ATOM   5031 O  OG  . SER   B 1 311 ? -15.975 25.918 -1.490  1.00 76.16  ? 308 SER   B OG  1 
ATOM   5032 N  N   . ASP   B 1 312 ? -15.414 24.449 1.904   1.00 85.59  ? 309 ASP   B N   1 
ATOM   5033 C  CA  . ASP   B 1 312 ? -15.642 23.072 2.398   1.00 89.30  ? 309 ASP   B CA  1 
ATOM   5034 C  C   . ASP   B 1 312 ? -15.818 22.197 1.156   1.00 84.10  ? 309 ASP   B C   1 
ATOM   5035 O  O   . ASP   B 1 312 ? -15.120 21.169 1.053   1.00 84.12  ? 309 ASP   B O   1 
ATOM   5036 C  CB  . ASP   B 1 312 ? -16.857 23.036 3.327   1.00 98.98  ? 309 ASP   B CB  1 
ATOM   5037 C  CG  . ASP   B 1 312 ? -16.683 23.908 4.556   1.00 104.40 ? 309 ASP   B CG  1 
ATOM   5038 O  OD1 . ASP   B 1 312 ? -15.733 24.735 4.554   1.00 98.98  ? 309 ASP   B OD1 1 
ATOM   5039 O  OD2 . ASP   B 1 312 ? -17.482 23.738 5.513   1.00 112.66 ? 309 ASP   B OD2 1 
ATOM   5040 N  N   . SER   B 1 313 ? -16.692 22.648 0.247   1.00 81.65  ? 310 SER   B N   1 
ATOM   5041 C  CA  . SER   B 1 313 ? -16.825 22.192 -1.166  1.00 77.87  ? 310 SER   B CA  1 
ATOM   5042 C  C   . SER   B 1 313 ? -15.553 21.606 -1.791  1.00 71.67  ? 310 SER   B C   1 
ATOM   5043 O  O   . SER   B 1 313 ? -15.572 20.429 -2.228  1.00 72.32  ? 310 SER   B O   1 
ATOM   5044 C  CB  . SER   B 1 313 ? -17.241 23.320 -2.091  1.00 75.14  ? 310 SER   B CB  1 
ATOM   5045 O  OG  . SER   B 1 313 ? -18.510 23.843 -1.744  1.00 81.99  ? 310 SER   B OG  1 
ATOM   5046 N  N   . PHE   B 1 314 ? -14.466 22.376 -1.758  1.00 65.37  ? 311 PHE   B N   1 
ATOM   5047 C  CA  . PHE   B 1 314 ? -13.239 22.116 -2.554  1.00 59.24  ? 311 PHE   B CA  1 
ATOM   5048 C  C   . PHE   B 1 314 ? -12.190 21.517 -1.631  1.00 57.22  ? 311 PHE   B C   1 
ATOM   5049 O  O   . PHE   B 1 314 ? -11.323 20.808 -2.157  1.00 53.30  ? 311 PHE   B O   1 
ATOM   5050 C  CB  . PHE   B 1 314 ? -12.766 23.356 -3.306  1.00 56.27  ? 311 PHE   B CB  1 
ATOM   5051 C  CG  . PHE   B 1 314 ? -13.804 23.733 -4.324  1.00 56.75  ? 311 PHE   B CG  1 
ATOM   5052 C  CD1 . PHE   B 1 314 ? -14.158 22.830 -5.311  1.00 57.78  ? 311 PHE   B CD1 1 
ATOM   5053 C  CD2 . PHE   B 1 314 ? -14.532 24.900 -4.198  1.00 59.64  ? 311 PHE   B CD2 1 
ATOM   5054 C  CE1 . PHE   B 1 314 ? -15.186 23.110 -6.191  1.00 59.05  ? 311 PHE   B CE1 1 
ATOM   5055 C  CE2 . PHE   B 1 314 ? -15.548 25.195 -5.092  1.00 61.16  ? 311 PHE   B CE2 1 
ATOM   5056 C  CZ  . PHE   B 1 314 ? -15.875 24.295 -6.086  1.00 61.19  ? 311 PHE   B CZ  1 
ATOM   5057 N  N   . ALA   B 1 315 ? -12.315 21.730 -0.318  1.00 59.54  ? 312 ALA   B N   1 
ATOM   5058 C  CA  . ALA   B 1 315 ? -11.344 21.245 0.689   1.00 60.32  ? 312 ALA   B CA  1 
ATOM   5059 C  C   . ALA   B 1 315 ? -11.088 19.747 0.519   1.00 60.13  ? 312 ALA   B C   1 
ATOM   5060 O  O   . ALA   B 1 315 ? -9.968  19.300 0.821   1.00 60.18  ? 312 ALA   B O   1 
ATOM   5061 C  CB  . ALA   B 1 315 ? -11.850 21.521 2.084   1.00 66.13  ? 312 ALA   B CB  1 
ATOM   5062 N  N   . SER   B 1 316 ? -12.120 18.987 0.148   1.00 62.19  ? 313 SER   B N   1 
ATOM   5063 C  CA  . SER   B 1 316 ? -12.090 17.502 0.083   1.00 63.26  ? 313 SER   B CA  1 
ATOM   5064 C  C   . SER   B 1 316 ? -11.622 17.027 -1.295  1.00 58.41  ? 313 SER   B C   1 
ATOM   5065 O  O   . SER   B 1 316 ? -11.472 15.817 -1.469  1.00 60.05  ? 313 SER   B O   1 
ATOM   5066 C  CB  . SER   B 1 316 ? -13.443 16.934 0.409   1.00 69.88  ? 313 SER   B CB  1 
ATOM   5067 O  OG  . SER   B 1 316 ? -14.418 17.460 -0.478  1.00 69.31  ? 313 SER   B OG  1 
ATOM   5068 N  N   . HIS   B 1 317 ? -11.400 17.929 -2.247  1.00 51.82  ? 314 HIS   B N   1 
ATOM   5069 C  CA  . HIS   B 1 317 ? -10.960 17.521 -3.607  1.00 48.75  ? 314 HIS   B CA  1 
ATOM   5070 C  C   . HIS   B 1 317 ? -9.559  16.930 -3.523  1.00 47.35  ? 314 HIS   B C   1 
ATOM   5071 O  O   . HIS   B 1 317 ? -8.666  17.541 -2.957  1.00 44.69  ? 314 HIS   B O   1 
ATOM   5072 C  CB  . HIS   B 1 317 ? -10.986 18.722 -4.564  1.00 44.22  ? 314 HIS   B CB  1 
ATOM   5073 C  CG  . HIS   B 1 317 ? -10.952 18.325 -5.997  1.00 42.84  ? 314 HIS   B CG  1 
ATOM   5074 N  ND1 . HIS   B 1 317 ? -9.828  17.792 -6.573  1.00 41.82  ? 314 HIS   B ND1 1 
ATOM   5075 C  CD2 . HIS   B 1 317 ? -11.870 18.452 -6.976  1.00 43.16  ? 314 HIS   B CD2 1 
ATOM   5076 C  CE1 . HIS   B 1 317 ? -10.057 17.573 -7.853  1.00 42.32  ? 314 HIS   B CE1 1 
ATOM   5077 N  NE2 . HIS   B 1 317 ? -11.309 17.970 -8.122  1.00 42.95  ? 314 HIS   B NE2 1 
ATOM   5078 N  N   . PRO   B 1 318 ? -9.259  15.793 -4.171  1.00 49.77  ? 315 PRO   B N   1 
ATOM   5079 C  CA  . PRO   B 1 318 ? -7.891  15.281 -4.139  1.00 49.82  ? 315 PRO   B CA  1 
ATOM   5080 C  C   . PRO   B 1 318 ? -6.836  16.325 -4.541  1.00 46.46  ? 315 PRO   B C   1 
ATOM   5081 O  O   . PRO   B 1 318 ? -5.725  16.202 -4.066  1.00 46.77  ? 315 PRO   B O   1 
ATOM   5082 C  CB  . PRO   B 1 318 ? -7.889  14.120 -5.153  1.00 52.95  ? 315 PRO   B CB  1 
ATOM   5083 C  CG  . PRO   B 1 318 ? -9.372  13.729 -5.316  1.00 55.64  ? 315 PRO   B CG  1 
ATOM   5084 C  CD  . PRO   B 1 318 ? -10.172 14.981 -4.998  1.00 53.38  ? 315 PRO   B CD  1 
ATOM   5085 N  N   . ASN   B 1 319 ? -7.170  17.271 -5.433  1.00 43.29  ? 316 ASN   B N   1 
ATOM   5086 C  CA  . ASN   B 1 319 ? -6.204  18.264 -5.985  1.00 40.30  ? 316 ASN   B CA  1 
ATOM   5087 C  C   . ASN   B 1 319 ? -6.346  19.618 -5.293  1.00 38.62  ? 316 ASN   B C   1 
ATOM   5088 O  O   . ASN   B 1 319 ? -5.801  20.600 -5.817  1.00 36.13  ? 316 ASN   B O   1 
ATOM   5089 C  CB  . ASN   B 1 319 ? -6.355  18.413 -7.497  1.00 40.97  ? 316 ASN   B CB  1 
ATOM   5090 C  CG  . ASN   B 1 319 ? -5.724  17.259 -8.241  1.00 43.98  ? 316 ASN   B CG  1 
ATOM   5091 O  OD1 . ASN   B 1 319 ? -5.135  16.393 -7.615  1.00 46.51  ? 316 ASN   B OD1 1 
ATOM   5092 N  ND2 . ASN   B 1 319 ? -5.893  17.192 -9.553  1.00 45.19  ? 316 ASN   B ND2 1 
ATOM   5093 N  N   . TYR   B 1 320 ? -7.053  19.679 -4.154  1.00 40.20  ? 317 TYR   B N   1 
ATOM   5094 C  CA  . TYR   B 1 320 ? -7.101  20.871 -3.279  1.00 39.84  ? 317 TYR   B CA  1 
ATOM   5095 C  C   . TYR   B 1 320 ? -5.656  21.289 -3.040  1.00 39.32  ? 317 TYR   B C   1 
ATOM   5096 O  O   . TYR   B 1 320 ? -4.845  20.505 -2.538  1.00 40.50  ? 317 TYR   B O   1 
ATOM   5097 C  CB  . TYR   B 1 320 ? -7.799  20.562 -1.949  1.00 44.02  ? 317 TYR   B CB  1 
ATOM   5098 C  CG  . TYR   B 1 320 ? -8.038  21.780 -1.092  1.00 45.25  ? 317 TYR   B CG  1 
ATOM   5099 C  CD1 . TYR   B 1 320 ? -8.721  22.872 -1.602  1.00 44.58  ? 317 TYR   B CD1 1 
ATOM   5100 C  CD2 . TYR   B 1 320 ? -7.598  21.847 0.224   1.00 48.75  ? 317 TYR   B CD2 1 
ATOM   5101 C  CE1 . TYR   B 1 320 ? -8.954  24.007 -0.843  1.00 46.36  ? 317 TYR   B CE1 1 
ATOM   5102 C  CE2 . TYR   B 1 320 ? -7.826  22.974 1.001   1.00 50.40  ? 317 TYR   B CE2 1 
ATOM   5103 C  CZ  . TYR   B 1 320 ? -8.501  24.062 0.467   1.00 50.03  ? 317 TYR   B CZ  1 
ATOM   5104 O  OH  . TYR   B 1 320 ? -8.753  25.177 1.219   1.00 51.73  ? 317 TYR   B OH  1 
ATOM   5105 N  N   . PRO   B 1 321 ? -5.250  22.494 -3.479  1.00 37.87  ? 318 PRO   B N   1 
ATOM   5106 C  CA  . PRO   B 1 321 ? -3.847  22.867 -3.395  1.00 37.81  ? 318 PRO   B CA  1 
ATOM   5107 C  C   . PRO   B 1 321 ? -3.374  23.093 -1.959  1.00 39.10  ? 318 PRO   B C   1 
ATOM   5108 O  O   . PRO   B 1 321 ? -2.203  23.103 -1.749  1.00 39.43  ? 318 PRO   B O   1 
ATOM   5109 C  CB  . PRO   B 1 321 ? -3.760  24.168 -4.212  1.00 36.71  ? 318 PRO   B CB  1 
ATOM   5110 C  CG  . PRO   B 1 321 ? -5.163  24.725 -4.226  1.00 36.08  ? 318 PRO   B CG  1 
ATOM   5111 C  CD  . PRO   B 1 321 ? -6.073  23.513 -4.157  1.00 37.00  ? 318 PRO   B CD  1 
ATOM   5112 N  N   . TYR   B 1 322 ? -4.277  23.288 -1.005  1.00 41.33  ? 319 TYR   B N   1 
ATOM   5113 C  CA  . TYR   B 1 322 ? -3.884  23.655 0.383   1.00 45.16  ? 319 TYR   B CA  1 
ATOM   5114 C  C   . TYR   B 1 322 ? -4.011  22.420 1.293   1.00 49.71  ? 319 TYR   B C   1 
ATOM   5115 O  O   . TYR   B 1 322 ? -4.166  22.595 2.456   1.00 53.42  ? 319 TYR   B O   1 
ATOM   5116 C  CB  . TYR   B 1 322 ? -4.712  24.863 0.831   1.00 45.33  ? 319 TYR   B CB  1 
ATOM   5117 C  CG  . TYR   B 1 322 ? -4.687  26.100 -0.046  1.00 43.11  ? 319 TYR   B CG  1 
ATOM   5118 C  CD1 . TYR   B 1 322 ? -3.503  26.694 -0.478  1.00 41.91  ? 319 TYR   B CD1 1 
ATOM   5119 C  CD2 . TYR   B 1 322 ? -5.873  26.743 -0.379  1.00 42.39  ? 319 TYR   B CD2 1 
ATOM   5120 C  CE1 . TYR   B 1 322 ? -3.512  27.858 -1.245  1.00 40.92  ? 319 TYR   B CE1 1 
ATOM   5121 C  CE2 . TYR   B 1 322 ? -5.898  27.896 -1.153  1.00 41.11  ? 319 TYR   B CE2 1 
ATOM   5122 C  CZ  . TYR   B 1 322 ? -4.713  28.476 -1.571  1.00 40.23  ? 319 TYR   B CZ  1 
ATOM   5123 O  OH  . TYR   B 1 322 ? -4.796  29.636 -2.301  1.00 40.56  ? 319 TYR   B OH  1 
ATOM   5124 N  N   . SER   B 1 323 ? -3.898  21.203 0.760   1.00 54.47  ? 320 SER   B N   1 
ATOM   5125 C  CA  . SER   B 1 323 ? -4.467  19.946 1.337   1.00 60.99  ? 320 SER   B CA  1 
ATOM   5126 C  C   . SER   B 1 323 ? -3.750  19.404 2.580   1.00 66.10  ? 320 SER   B C   1 
ATOM   5127 O  O   . SER   B 1 323 ? -4.356  18.508 3.220   1.00 74.09  ? 320 SER   B O   1 
ATOM   5128 C  CB  . SER   B 1 323 ? -4.555  18.855 0.305   1.00 61.50  ? 320 SER   B CB  1 
ATOM   5129 O  OG  . SER   B 1 323 ? -5.456  17.857 0.752   1.00 67.09  ? 320 SER   B OG  1 
ATOM   5130 N  N   . ASP   B 1 324 ? -2.532  19.822 2.948   1.00 66.36  ? 321 ASP   B N   1 
ATOM   5131 C  CA  . ASP   B 1 324 ? -1.949  19.317 4.237   1.00 70.45  ? 321 ASP   B CA  1 
ATOM   5132 C  C   . ASP   B 1 324 ? -1.499  20.534 5.075   1.00 68.92  ? 321 ASP   B C   1 
ATOM   5133 O  O   . ASP   B 1 324 ? -0.361  20.578 5.621   1.00 67.70  ? 321 ASP   B O   1 
ATOM   5134 C  CB  . ASP   B 1 324 ? -0.915  18.205 3.979   1.00 73.73  ? 321 ASP   B CB  1 
ATOM   5135 C  CG  . ASP   B 1 324 ? -1.034  16.915 4.797   1.00 78.79  ? 321 ASP   B CG  1 
ATOM   5136 O  OD1 . ASP   B 1 324 ? -2.168  16.499 5.128   1.00 81.78  ? 321 ASP   B OD1 1 
ATOM   5137 O  OD2 . ASP   B 1 324 ? 0.029   16.314 5.092   1.00 80.71  ? 321 ASP   B OD2 1 
ATOM   5138 N  N   . GLU   B 1 325 ? -2.403  21.504 5.195   1.00 65.94  ? 322 GLU   B N   1 
ATOM   5139 C  CA  . GLU   B 1 325 ? -2.120  22.799 5.859   1.00 65.09  ? 322 GLU   B CA  1 
ATOM   5140 C  C   . GLU   B 1 325 ? -2.277  22.633 7.374   1.00 68.02  ? 322 GLU   B C   1 
ATOM   5141 O  O   . GLU   B 1 325 ? -1.884  23.562 8.103   1.00 71.04  ? 322 GLU   B O   1 
ATOM   5142 C  CB  . GLU   B 1 325 ? -2.999  23.895 5.259   1.00 64.51  ? 322 GLU   B CB  1 
ATOM   5143 C  CG  . GLU   B 1 325 ? -4.467  23.546 5.141   1.00 65.94  ? 322 GLU   B CG  1 
ATOM   5144 C  CD  . GLU   B 1 325 ? -5.338  24.780 5.282   1.00 70.23  ? 322 GLU   B CD  1 
ATOM   5145 O  OE1 . GLU   B 1 325 ? -5.998  24.897 6.352   1.00 78.19  ? 322 GLU   B OE1 1 
ATOM   5146 O  OE2 . GLU   B 1 325 ? -5.303  25.670 4.375   1.00 67.16  ? 322 GLU   B OE2 1 
ATOM   5147 N  N   . TYR   B 1 326 ? -2.801  21.486 7.825   1.00 67.89  ? 323 TYR   B N   1 
ATOM   5148 C  CA  . TYR   B 1 326 ? -2.687  21.000 9.228   1.00 72.48  ? 323 TYR   B CA  1 
ATOM   5149 C  C   . TYR   B 1 326 ? -2.859  19.472 9.264   1.00 73.18  ? 323 TYR   B C   1 
ATOM   5150 O  O   . TYR   B 1 326 ? -2.624  18.826 10.308  1.00 75.67  ? 323 TYR   B O   1 
ATOM   5151 C  CB  . TYR   B 1 326 ? -3.707  21.671 10.149  1.00 77.42  ? 323 TYR   B CB  1 
ATOM   5152 C  CG  . TYR   B 1 326 ? -5.137  21.292 9.872   1.00 78.52  ? 323 TYR   B CG  1 
ATOM   5153 C  CD1 . TYR   B 1 326 ? -5.789  21.807 8.758   1.00 74.21  ? 323 TYR   B CD1 1 
ATOM   5154 C  CD2 . TYR   B 1 326 ? -5.821  20.403 10.683  1.00 84.79  ? 323 TYR   B CD2 1 
ATOM   5155 C  CE1 . TYR   B 1 326 ? -7.103  21.479 8.486   1.00 75.99  ? 323 TYR   B CE1 1 
ATOM   5156 C  CE2 . TYR   B 1 326 ? -7.134  20.055 10.421  1.00 87.14  ? 323 TYR   B CE2 1 
ATOM   5157 C  CZ  . TYR   B 1 326 ? -7.776  20.621 9.336   1.00 82.86  ? 323 TYR   B CZ  1 
ATOM   5158 O  OH  . TYR   B 1 326 ? -9.062  20.293 9.055   1.00 86.99  ? 323 TYR   B OH  1 
ATOM   5159 O  OXT . TYR   B 1 326 ? -3.250  18.935 8.181   1.00 69.26  ? 323 TYR   B OXT 1 
HETATM 5160 P  PA  . NAP   C 2 .   ? 9.191   27.031 26.497  1.00 15.27  ? 401 NAP   A PA  1 
HETATM 5161 O  O1A . NAP   C 2 .   ? 8.231   26.405 27.436  1.00 13.78  ? 401 NAP   A O1A 1 
HETATM 5162 O  O2A . NAP   C 2 .   ? 8.649   27.679 25.278  1.00 13.82  ? 401 NAP   A O2A 1 
HETATM 5163 O  O5B . NAP   C 2 .   ? 9.974   28.149 27.325  1.00 14.07  ? 401 NAP   A O5B 1 
HETATM 5164 C  C5B . NAP   C 2 .   ? 10.930  28.937 26.651  1.00 14.17  ? 401 NAP   A C5B 1 
HETATM 5165 C  C4B . NAP   C 2 .   ? 11.700  29.783 27.644  1.00 14.09  ? 401 NAP   A C4B 1 
HETATM 5166 O  O4B . NAP   C 2 .   ? 10.799  30.544 28.410  1.00 16.64  ? 401 NAP   A O4B 1 
HETATM 5167 C  C3B . NAP   C 2 .   ? 12.532  29.006 28.664  1.00 15.42  ? 401 NAP   A C3B 1 
HETATM 5168 O  O3B . NAP   C 2 .   ? 13.855  28.820 28.189  1.00 15.81  ? 401 NAP   A O3B 1 
HETATM 5169 C  C2B . NAP   C 2 .   ? 12.459  29.843 29.939  1.00 14.78  ? 401 NAP   A C2B 1 
HETATM 5170 O  O2B . NAP   C 2 .   ? 13.727  30.355 30.326  1.00 16.69  ? 401 NAP   A O2B 1 
HETATM 5171 C  C1B . NAP   C 2 .   ? 11.468  30.938 29.603  1.00 15.09  ? 401 NAP   A C1B 1 
HETATM 5172 N  N9A . NAP   C 2 .   ? 10.462  31.140 30.648  1.00 15.28  ? 401 NAP   A N9A 1 
HETATM 5173 C  C8A . NAP   C 2 .   ? 9.805   30.186 31.306  1.00 14.58  ? 401 NAP   A C8A 1 
HETATM 5174 N  N7A . NAP   C 2 .   ? 8.949   30.715 32.186  1.00 15.69  ? 401 NAP   A N7A 1 
HETATM 5175 C  C5A . NAP   C 2 .   ? 9.056   32.042 32.099  1.00 15.21  ? 401 NAP   A C5A 1 
HETATM 5176 C  C6A . NAP   C 2 .   ? 8.439   33.205 32.755  1.00 16.08  ? 401 NAP   A C6A 1 
HETATM 5177 N  N6A . NAP   C 2 .   ? 7.512   33.061 33.705  1.00 17.26  ? 401 NAP   A N6A 1 
HETATM 5178 N  N1A . NAP   C 2 .   ? 8.831   34.417 32.356  1.00 16.28  ? 401 NAP   A N1A 1 
HETATM 5179 C  C2A . NAP   C 2 .   ? 9.758   34.594 31.412  1.00 15.20  ? 401 NAP   A C2A 1 
HETATM 5180 N  N3A . NAP   C 2 .   ? 10.366  33.591 30.779  1.00 15.29  ? 401 NAP   A N3A 1 
HETATM 5181 C  C4A . NAP   C 2 .   ? 10.058  32.316 31.075  1.00 15.28  ? 401 NAP   A C4A 1 
HETATM 5182 O  O3  . NAP   C 2 .   ? 10.409  26.053 26.146  1.00 13.40  ? 401 NAP   A O3  1 
HETATM 5183 P  PN  . NAP   C 2 .   ? 10.510  24.744 25.223  1.00 13.48  ? 401 NAP   A PN  1 
HETATM 5184 O  O1N . NAP   C 2 .   ? 11.635  23.935 25.702  1.00 12.99  ? 401 NAP   A O1N 1 
HETATM 5185 O  O2N . NAP   C 2 .   ? 10.566  25.206 23.805  1.00 16.11  ? 401 NAP   A O2N 1 
HETATM 5186 O  O5D . NAP   C 2 .   ? 9.145   23.971 25.454  1.00 12.51  ? 401 NAP   A O5D 1 
HETATM 5187 C  C5D . NAP   C 2 .   ? 8.855   23.440 26.730  1.00 13.01  ? 401 NAP   A C5D 1 
HETATM 5188 C  C4D . NAP   C 2 .   ? 8.977   21.928 26.796  1.00 13.98  ? 401 NAP   A C4D 1 
HETATM 5189 O  O4D . NAP   C 2 .   ? 8.241   21.226 25.794  1.00 14.83  ? 401 NAP   A O4D 1 
HETATM 5190 C  C3D . NAP   C 2 .   ? 10.386  21.372 26.695  1.00 15.75  ? 401 NAP   A C3D 1 
HETATM 5191 O  O3D . NAP   C 2 .   ? 11.120  21.530 27.895  1.00 16.08  ? 401 NAP   A O3D 1 
HETATM 5192 C  C2D . NAP   C 2 .   ? 10.088  19.910 26.437  1.00 15.16  ? 401 NAP   A C2D 1 
HETATM 5193 O  O2D . NAP   C 2 .   ? 9.740   19.256 27.661  1.00 13.95  ? 401 NAP   A O2D 1 
HETATM 5194 C  C1D . NAP   C 2 .   ? 8.864   19.977 25.530  1.00 14.10  ? 401 NAP   A C1D 1 
HETATM 5195 N  N1N . NAP   C 2 .   ? 9.228   19.913 24.117  1.00 15.44  ? 401 NAP   A N1N 1 
HETATM 5196 C  C2N . NAP   C 2 .   ? 8.768   18.928 23.342  1.00 14.90  ? 401 NAP   A C2N 1 
HETATM 5197 C  C3N . NAP   C 2 .   ? 9.090   18.860 21.992  1.00 14.20  ? 401 NAP   A C3N 1 
HETATM 5198 C  C7N . NAP   C 2 .   ? 8.570   17.743 21.134  1.00 14.25  ? 401 NAP   A C7N 1 
HETATM 5199 O  O7N . NAP   C 2 .   ? 9.031   17.564 20.036  1.00 15.25  ? 401 NAP   A O7N 1 
HETATM 5200 N  N7N . NAP   C 2 .   ? 7.599   16.992 21.624  1.00 15.84  ? 401 NAP   A N7N 1 
HETATM 5201 C  C4N . NAP   C 2 .   ? 9.898   19.837 21.451  1.00 13.58  ? 401 NAP   A C4N 1 
HETATM 5202 C  C5N . NAP   C 2 .   ? 10.347  20.850 22.275  1.00 15.14  ? 401 NAP   A C5N 1 
HETATM 5203 C  C6N . NAP   C 2 .   ? 9.991   20.862 23.604  1.00 14.56  ? 401 NAP   A C6N 1 
HETATM 5204 P  P2B . NAP   C 2 .   ? 14.339  30.072 31.789  1.00 16.82  ? 401 NAP   A P2B 1 
HETATM 5205 O  O1X . NAP   C 2 .   ? 14.698  28.628 31.841  1.00 16.29  ? 401 NAP   A O1X 1 
HETATM 5206 O  O2X . NAP   C 2 .   ? 15.559  30.922 31.832  1.00 17.53  ? 401 NAP   A O2X 1 
HETATM 5207 O  O3X . NAP   C 2 .   ? 13.272  30.503 32.706  1.00 14.59  ? 401 NAP   A O3X 1 
HETATM 5208 N  N1  . A1H2U D 3 .   ? 11.533  18.686 13.239  1.00 25.62  ? 402 A1H2U A N1  1 
HETATM 5209 C  C4  . A1H2U D 3 .   ? 16.071  19.328 19.908  1.00 23.48  ? 402 A1H2U A C4  1 
HETATM 5210 C  C5  . A1H2U D 3 .   ? 14.731  21.461 19.892  1.00 24.09  ? 402 A1H2U A C5  1 
HETATM 5211 C  C6  . A1H2U D 3 .   ? 13.764  20.420 22.368  1.00 21.94  ? 402 A1H2U A C6  1 
HETATM 5212 C  C7  . A1H2U D 3 .   ? 11.870  16.043 18.009  1.00 21.76  ? 402 A1H2U A C7  1 
HETATM 5213 C  C8  . A1H2U D 3 .   ? 13.645  19.412 18.961  1.00 22.80  ? 402 A1H2U A C8  1 
HETATM 5214 C  C10 . A1H2U D 3 .   ? 13.346  17.914 19.101  1.00 21.54  ? 402 A1H2U A C10 1 
HETATM 5215 C  C13 . A1H2U D 3 .   ? 12.761  17.592 20.460  1.00 21.85  ? 402 A1H2U A C13 1 
HETATM 5216 C  C15 . A1H2U D 3 .   ? 13.676  18.112 21.551  1.00 21.39  ? 402 A1H2U A C15 1 
HETATM 5217 C  C17 . A1H2U D 3 .   ? 14.041  19.554 21.390  1.00 22.38  ? 402 A1H2U A C17 1 
HETATM 5218 C  C20 . A1H2U D 3 .   ? 10.681  18.832 14.357  1.00 24.48  ? 402 A1H2U A C20 1 
HETATM 5219 C  C21 . A1H2U D 3 .   ? 11.685  19.737 12.323  1.00 25.44  ? 402 A1H2U A C21 1 
HETATM 5220 C  C22 . A1H2U D 3 .   ? 10.985  20.858 12.530  1.00 25.16  ? 402 A1H2U A C22 1 
HETATM 5221 C  C24 . A1H2U D 3 .   ? 10.014  19.937 14.554  1.00 25.60  ? 402 A1H2U A C24 1 
HETATM 5222 O  O1  . A1H2U D 3 .   ? 12.761  22.238 24.180  1.00 21.44  ? 402 A1H2U A O1  1 
HETATM 5223 N  N   . A1H2U D 3 .   ? 13.584  22.733 23.134  1.00 22.02  ? 402 A1H2U A N   1 
HETATM 5224 C  C11 . A1H2U D 3 .   ? 14.090  21.868 22.295  1.00 21.68  ? 402 A1H2U A C11 1 
HETATM 5225 C  C16 . A1H2U D 3 .   ? 14.975  22.253 21.169  1.00 23.05  ? 402 A1H2U A C16 1 
HETATM 5226 C  C9  . A1H2U D 3 .   ? 12.391  17.461 17.982  1.00 22.18  ? 402 A1H2U A C9  1 
HETATM 5227 C  C3  . A1H2U D 3 .   ? 11.442  15.700 16.579  1.00 23.31  ? 402 A1H2U A C3  1 
HETATM 5228 C  C18 . A1H2U D 3 .   ? 14.673  19.923 20.050  1.00 22.81  ? 402 A1H2U A C18 1 
HETATM 5229 C  C14 . A1H2U D 3 .   ? 13.992  19.816 17.472  1.00 23.17  ? 402 A1H2U A C14 1 
HETATM 5230 C  C12 . A1H2U D 3 .   ? 13.136  19.190 16.367  1.00 21.71  ? 402 A1H2U A C12 1 
HETATM 5231 C  C   . A1H2U D 3 .   ? 12.909  17.675 16.521  1.00 22.05  ? 402 A1H2U A C   1 
HETATM 5232 C  C1  . A1H2U D 3 .   ? 14.289  17.002 16.266  1.00 20.40  ? 402 A1H2U A C1  1 
HETATM 5233 C  C2  . A1H2U D 3 .   ? 11.805  16.907 15.682  1.00 23.56  ? 402 A1H2U A C2  1 
HETATM 5234 O  O   . A1H2U D 3 .   ? 12.261  16.434 14.395  1.00 24.37  ? 402 A1H2U A O   1 
HETATM 5235 C  C19 . A1H2U D 3 .   ? 10.506  17.729 15.362  1.00 25.63  ? 402 A1H2U A C19 1 
HETATM 5236 C  C23 . A1H2U D 3 .   ? 10.162  20.932 13.665  1.00 26.42  ? 402 A1H2U A C23 1 
HETATM 5237 NA NA  . NA    E 4 .   ? 10.604  16.700 22.853  1.00 31.03  ? 403 NA    A NA  1 
HETATM 5238 NA NA  . NA    F 4 .   ? -6.586  10.260 6.045   1.00 48.78  ? 404 NA    A NA  1 
HETATM 5239 NA NA  . NA    G 4 .   ? 12.550  29.776 13.298  1.00 52.20  ? 405 NA    A NA  1 
HETATM 5240 NA NA  . NA    H 4 .   ? 5.705   21.633 -0.718  1.00 54.44  ? 406 NA    A NA  1 
HETATM 5241 NA NA  . NA    I 4 .   ? 6.072   25.051 7.403   1.00 49.03  ? 407 NA    A NA  1 
HETATM 5242 P  PA  . NAP   J 2 .   ? -8.183  42.751 -5.476  1.00 16.90  ? 401 NAP   B PA  1 
HETATM 5243 O  O1A . NAP   J 2 .   ? -7.204  43.083 -6.523  1.00 15.53  ? 401 NAP   B O1A 1 
HETATM 5244 O  O2A . NAP   J 2 .   ? -7.671  42.104 -4.256  1.00 17.05  ? 401 NAP   B O2A 1 
HETATM 5245 O  O5B . NAP   J 2 .   ? -8.946  44.088 -5.099  1.00 16.34  ? 401 NAP   B O5B 1 
HETATM 5246 C  C5B . NAP   J 2 .   ? -9.916  44.068 -4.078  1.00 17.38  ? 401 NAP   B C5B 1 
HETATM 5247 C  C4B . NAP   J 2 .   ? -10.609 45.408 -3.949  1.00 17.62  ? 401 NAP   B C4B 1 
HETATM 5248 O  O4B . NAP   J 2 .   ? -9.672  46.461 -3.788  1.00 21.06  ? 401 NAP   B O4B 1 
HETATM 5249 C  C3B . NAP   J 2 .   ? -11.425 45.777 -5.175  1.00 18.85  ? 401 NAP   B C3B 1 
HETATM 5250 O  O3B . NAP   J 2 .   ? -12.761 45.308 -5.041  1.00 18.32  ? 401 NAP   B O3B 1 
HETATM 5251 C  C2B . NAP   J 2 .   ? -11.298 47.294 -5.274  1.00 19.37  ? 401 NAP   B C2B 1 
HETATM 5252 O  O2B . NAP   J 2 .   ? -12.538 47.934 -5.064  1.00 19.93  ? 401 NAP   B O2B 1 
HETATM 5253 C  C1B . NAP   J 2 .   ? -10.313 47.669 -4.175  1.00 19.57  ? 401 NAP   B C1B 1 
HETATM 5254 N  N9A . NAP   J 2 .   ? -9.293  48.605 -4.663  1.00 20.27  ? 401 NAP   B N9A 1 
HETATM 5255 C  C8A . NAP   J 2 .   ? -8.623  48.517 -5.809  1.00 19.27  ? 401 NAP   B C8A 1 
HETATM 5256 N  N7A . NAP   J 2 .   ? -7.756  49.528 -5.936  1.00 20.43  ? 401 NAP   B N7A 1 
HETATM 5257 C  C5A . NAP   J 2 .   ? -7.866  50.288 -4.845  1.00 21.01  ? 401 NAP   B C5A 1 
HETATM 5258 C  C6A . NAP   J 2 .   ? -7.253  51.522 -4.334  1.00 20.31  ? 401 NAP   B C6A 1 
HETATM 5259 N  N6A . NAP   J 2 .   ? -6.310  52.167 -5.027  1.00 22.60  ? 401 NAP   B N6A 1 
HETATM 5260 N  N1A . NAP   J 2 .   ? -7.661  51.968 -3.141  1.00 20.85  ? 401 NAP   B N1A 1 
HETATM 5261 C  C2A . NAP   J 2 .   ? -8.601  51.353 -2.420  1.00 20.93  ? 401 NAP   B C2A 1 
HETATM 5262 N  N3A . NAP   J 2 .   ? -9.205  50.224 -2.816  1.00 21.56  ? 401 NAP   B N3A 1 
HETATM 5263 C  C4A . NAP   J 2 .   ? -8.884  49.667 -4.002  1.00 20.80  ? 401 NAP   B C4A 1 
HETATM 5264 O  O3  . NAP   J 2 .   ? -9.445  41.883 -6.003  1.00 16.27  ? 401 NAP   B O3  1 
HETATM 5265 P  PN  . NAP   J 2 .   ? -9.577  40.337 -6.457  1.00 16.85  ? 401 NAP   B PN  1 
HETATM 5266 O  O1N . NAP   J 2 .   ? -10.696 40.302 -7.405  1.00 17.02  ? 401 NAP   B O1N 1 
HETATM 5267 O  O2N . NAP   J 2 .   ? -9.720  39.488 -5.256  1.00 16.31  ? 401 NAP   B O2N 1 
HETATM 5268 O  O5D . NAP   J 2 .   ? -8.252  39.993 -7.239  1.00 14.80  ? 401 NAP   B O5D 1 
HETATM 5269 C  C5D . NAP   J 2 .   ? -7.942  40.702 -8.422  1.00 15.44  ? 401 NAP   B C5D 1 
HETATM 5270 C  C4D . NAP   J 2 .   ? -8.115  39.862 -9.684  1.00 14.79  ? 401 NAP   B C4D 1 
HETATM 5271 O  O4D . NAP   J 2 .   ? -7.414  38.621 -9.645  1.00 15.71  ? 401 NAP   B O4D 1 
HETATM 5272 C  C3D . NAP   J 2 .   ? -9.549  39.496 -10.048 1.00 15.82  ? 401 NAP   B C3D 1 
HETATM 5273 O  O3D . NAP   J 2 .   ? -10.268 40.579 -10.607 1.00 17.35  ? 401 NAP   B O3D 1 
HETATM 5274 C  C2D . NAP   J 2 .   ? -9.295  38.382 -11.036 1.00 15.55  ? 401 NAP   B C2D 1 
HETATM 5275 O  O2D . NAP   J 2 .   ? -8.938  38.931 -12.300 1.00 15.12  ? 401 NAP   B O2D 1 
HETATM 5276 C  C1D . NAP   J 2 .   ? -8.083  37.653 -10.446 1.00 15.53  ? 401 NAP   B C1D 1 
HETATM 5277 N  N1N . NAP   J 2 .   ? -8.467  36.507 -9.618  1.00 14.71  ? 401 NAP   B N1N 1 
HETATM 5278 C  C2N . NAP   J 2 .   ? -8.052  35.282 -9.939  1.00 15.61  ? 401 NAP   B C2N 1 
HETATM 5279 C  C3N . NAP   J 2 .   ? -8.390  34.168 -9.183  1.00 13.97  ? 401 NAP   B C3N 1 
HETATM 5280 C  C7N . NAP   J 2 .   ? -7.901  32.794 -9.551  1.00 14.02  ? 401 NAP   B C7N 1 
HETATM 5281 O  O7N . NAP   J 2 .   ? -8.395  31.845 -9.014  1.00 15.52  ? 401 NAP   B O7N 1 
HETATM 5282 N  N7N . NAP   J 2 .   ? -6.909  32.660 -10.416 1.00 14.03  ? 401 NAP   B N7N 1 
HETATM 5283 C  C4N . NAP   J 2 .   ? -9.177  34.347 -8.062  1.00 13.26  ? 401 NAP   B C4N 1 
HETATM 5284 C  C5N . NAP   J 2 .   ? -9.590  35.628 -7.746  1.00 13.83  ? 401 NAP   B C5N 1 
HETATM 5285 C  C6N . NAP   J 2 .   ? -9.216  36.689 -8.542  1.00 13.93  ? 401 NAP   B C6N 1 
HETATM 5286 P  P2B . NAP   J 2 .   ? -13.176 48.940 -6.130  1.00 20.80  ? 401 NAP   B P2B 1 
HETATM 5287 O  O1X . NAP   J 2 .   ? -13.509 48.091 -7.300  1.00 19.50  ? 401 NAP   B O1X 1 
HETATM 5288 O  O2X . NAP   J 2 .   ? -14.372 49.460 -5.420  1.00 22.03  ? 401 NAP   B O2X 1 
HETATM 5289 O  O3X . NAP   J 2 .   ? -12.113 49.930 -6.389  1.00 18.19  ? 401 NAP   B O3X 1 
HETATM 5290 N  N1  . A1H2U K 3 .   ? -11.211 27.243 -4.063  1.00 35.34  ? 402 A1H2U B N1  1 
HETATM 5291 C  C4  . A1H2U K 3 .   ? -15.517 33.189 -7.641  1.00 23.74  ? 402 A1H2U B C4  1 
HETATM 5292 C  C5  . A1H2U K 3 .   ? -14.103 34.289 -5.859  1.00 22.17  ? 402 A1H2U B C5  1 
HETATM 5293 C  C6  . A1H2U K 3 .   ? -12.993 35.565 -8.085  1.00 21.96  ? 402 A1H2U B C6  1 
HETATM 5294 C  C7  . A1H2U K 3 .   ? -11.349 29.372 -8.990  1.00 25.33  ? 402 A1H2U B C7  1 
HETATM 5295 C  C8  . A1H2U K 3 .   ? -13.156 32.204 -6.902  1.00 23.04  ? 402 A1H2U B C8  1 
HETATM 5296 C  C10 . A1H2U K 3 .   ? -12.778 31.405 -8.168  1.00 22.88  ? 402 A1H2U B C10 1 
HETATM 5297 C  C13 . A1H2U K 3 .   ? -12.057 32.308 -9.129  1.00 22.45  ? 402 A1H2U B C13 1 
HETATM 5298 C  C15 . A1H2U K 3 .   ? -12.909 33.520 -9.441  1.00 21.11  ? 402 A1H2U B C15 1 
HETATM 5299 C  C17 . A1H2U K 3 .   ? -13.334 34.271 -8.223  1.00 22.33  ? 402 A1H2U B C17 1 
HETATM 5300 C  C20 . A1H2U K 3 .   ? -10.218 28.108 -4.597  1.00 33.73  ? 402 A1H2U B C20 1 
HETATM 5301 C  C21 . A1H2U K 3 .   ? -11.313 27.090 -2.680  1.00 35.60  ? 402 A1H2U B C21 1 
HETATM 5302 C  C22 . A1H2U K 3 .   ? -10.461 27.764 -1.894  1.00 36.18  ? 402 A1H2U B C22 1 
HETATM 5303 C  C24 . A1H2U K 3 .   ? -9.391  28.762 -3.824  1.00 37.19  ? 402 A1H2U B C24 1 
HETATM 5304 O  O1  . A1H2U K 3 .   ? -11.965 38.068 -7.661  1.00 20.01  ? 402 A1H2U B O1  1 
HETATM 5305 N  N   . A1H2U K 3 .   ? -12.913 37.600 -6.727  1.00 21.72  ? 402 A1H2U B N   1 
HETATM 5306 C  C11 . A1H2U K 3 .   ? -13.400 36.399 -6.943  1.00 20.90  ? 402 A1H2U B C11 1 
HETATM 5307 C  C16 . A1H2U K 3 .   ? -14.402 35.756 -6.082  1.00 21.96  ? 402 A1H2U B C16 1 
HETATM 5308 C  C9  . A1H2U K 3 .   ? -11.877 30.222 -7.842  1.00 24.25  ? 402 A1H2U B C9  1 
HETATM 5309 C  C3  . A1H2U K 3 .   ? -10.926 28.057 -8.360  1.00 26.33  ? 402 A1H2U B C3  1 
HETATM 5310 C  C18 . A1H2U K 3 .   ? -14.080 33.463 -7.176  1.00 22.66  ? 402 A1H2U B C18 1 
HETATM 5311 C  C14 . A1H2U K 3 .   ? -13.596 31.291 -5.705  1.00 24.34  ? 402 A1H2U B C14 1 
HETATM 5312 C  C12 . A1H2U K 3 .   ? -12.719 30.045 -5.525  1.00 24.38  ? 402 A1H2U B C12 1 
HETATM 5313 C  C   . A1H2U K 3 .   ? -12.461 29.232 -6.810  1.00 25.35  ? 402 A1H2U B C   1 
HETATM 5314 C  C1  . A1H2U K 3 .   ? -13.843 28.646 -7.229  1.00 25.44  ? 402 A1H2U B C1  1 
HETATM 5315 C  C2  . A1H2U K 3 .   ? -11.348 28.100 -6.893  1.00 27.85  ? 402 A1H2U B C2  1 
HETATM 5316 O  O   . A1H2U K 3 .   ? -11.801 26.785 -6.519  1.00 28.32  ? 402 A1H2U B O   1 
HETATM 5317 C  C19 . A1H2U K 3 .   ? -10.049 28.337 -6.060  1.00 31.64  ? 402 A1H2U B C19 1 
HETATM 5318 C  C23 . A1H2U K 3 .   ? -9.511  28.601 -2.499  1.00 38.92  ? 402 A1H2U B C23 1 
HETATM 5319 NA NA  . NA    L 4 .   ? -10.059 33.616 -11.470 1.00 26.84  ? 403 NA    B NA  1 
HETATM 5320 NA NA  . NA    M 4 .   ? 5.864   58.455 -2.211  1.00 43.65  ? 404 NA    B NA  1 
HETATM 5321 NA NA  . NA    N 4 .   ? -18.935 22.684 -18.726 1.00 51.84  ? 405 NA    B NA  1 
HETATM 5322 NA NA  . NA    O 4 .   ? -5.774  50.573 10.730  1.00 46.04  ? 406 NA    B NA  1 
HETATM 5323 NA NA  . NA    P 4 .   ? -10.107 27.535 -34.304 1.00 49.03  ? 407 NA    B NA  1 
HETATM 5324 NA NA  . NA    Q 4 .   ? 0.453   52.186 -28.527 1.00 53.62  ? 408 NA    B NA  1 
HETATM 5325 O  O   . HOH   R 5 .   ? -6.396  39.380 35.836  1.00 27.29  ? 501 HOH   A O   1 
HETATM 5326 O  O   . HOH   R 5 .   ? -2.067  -4.655 23.165  1.00 38.54  ? 502 HOH   A O   1 
HETATM 5327 O  O   . HOH   R 5 .   ? 4.215   28.773 6.567   1.00 48.07  ? 503 HOH   A O   1 
HETATM 5328 O  O   . HOH   R 5 .   ? -1.271  15.137 41.114  1.00 31.30  ? 504 HOH   A O   1 
HETATM 5329 O  O   . HOH   R 5 .   ? 17.391  14.645 46.707  1.00 28.33  ? 505 HOH   A O   1 
HETATM 5330 O  O   . HOH   R 5 .   ? 11.899  6.021  25.617  1.00 15.78  ? 506 HOH   A O   1 
HETATM 5331 O  O   . HOH   R 5 .   ? 9.364   28.610 10.580  1.00 26.34  ? 507 HOH   A O   1 
HETATM 5332 O  O   . HOH   R 5 .   ? -10.547 41.449 21.366  1.00 28.70  ? 508 HOH   A O   1 
HETATM 5333 O  O   . HOH   R 5 .   ? 21.436  4.028  21.035  1.00 42.38  ? 509 HOH   A O   1 
HETATM 5334 O  O   . HOH   R 5 .   ? 21.171  12.207 32.085  1.00 27.93  ? 510 HOH   A O   1 
HETATM 5335 O  O   . HOH   R 5 .   ? 11.600  -5.847 26.320  1.00 45.44  ? 511 HOH   A O   1 
HETATM 5336 O  O   . HOH   R 5 .   ? 1.657   5.219  46.519  1.00 49.41  ? 512 HOH   A O   1 
HETATM 5337 O  O   . HOH   R 5 .   ? 16.067  35.345 8.883   1.00 39.23  ? 513 HOH   A O   1 
HETATM 5338 O  O   . HOH   R 5 .   ? 24.922  7.741  37.334  1.00 39.92  ? 514 HOH   A O   1 
HETATM 5339 O  O   . HOH   R 5 .   ? 13.851  38.426 15.852  1.00 41.11  ? 515 HOH   A O   1 
HETATM 5340 O  O   . HOH   R 5 .   ? 0.052   25.848 4.513   1.00 29.88  ? 516 HOH   A O   1 
HETATM 5341 O  O   . HOH   R 5 .   ? 1.003   8.109  38.549  1.00 17.09  ? 517 HOH   A O   1 
HETATM 5342 O  O   . HOH   R 5 .   ? 13.557  15.591 47.971  1.00 36.73  ? 518 HOH   A O   1 
HETATM 5343 O  O   . HOH   R 5 .   ? -4.245  39.173 37.162  1.00 20.08  ? 519 HOH   A O   1 
HETATM 5344 O  O   . HOH   R 5 .   ? 1.307   25.479 43.451  1.00 40.64  ? 520 HOH   A O   1 
HETATM 5345 O  O   . HOH   R 5 .   ? 14.312  -4.743 27.710  1.00 38.80  ? 521 HOH   A O   1 
HETATM 5346 O  O   . HOH   R 5 .   ? 17.904  27.610 26.880  1.00 21.29  ? 522 HOH   A O   1 
HETATM 5347 O  O   . HOH   R 5 .   ? -10.924 34.458 17.641  1.00 30.18  ? 523 HOH   A O   1 
HETATM 5348 O  O   . HOH   R 5 .   ? 21.264  19.197 41.289  1.00 28.72  ? 524 HOH   A O   1 
HETATM 5349 O  O   . HOH   R 5 .   ? -10.391 5.400  15.885  1.00 27.80  ? 525 HOH   A O   1 
HETATM 5350 O  O   . HOH   R 5 .   ? -4.509  40.638 17.827  1.00 29.75  ? 526 HOH   A O   1 
HETATM 5351 O  O   . HOH   R 5 .   ? -8.685  6.975  36.093  1.00 31.29  ? 527 HOH   A O   1 
HETATM 5352 O  O   . HOH   R 5 .   ? 7.842   22.016 15.638  1.00 18.86  ? 528 HOH   A O   1 
HETATM 5353 O  O   . HOH   R 5 .   ? -1.480  -5.869 19.219  1.00 36.15  ? 529 HOH   A O   1 
HETATM 5354 O  O   . HOH   R 5 .   ? -13.965 20.036 17.300  1.00 31.74  ? 530 HOH   A O   1 
HETATM 5355 O  O   . HOH   R 5 .   ? 17.082  29.689 39.974  1.00 38.16  ? 531 HOH   A O   1 
HETATM 5356 O  O   . HOH   R 5 .   ? 14.854  2.003  42.404  1.00 20.58  ? 532 HOH   A O   1 
HETATM 5357 O  O   . HOH   R 5 .   ? 8.413   -3.959 21.398  1.00 20.87  ? 533 HOH   A O   1 
HETATM 5358 O  O   . HOH   R 5 .   ? 8.766   40.375 28.017  1.00 32.04  ? 534 HOH   A O   1 
HETATM 5359 O  O   . HOH   R 5 .   ? 17.496  30.182 30.304  1.00 35.98  ? 535 HOH   A O   1 
HETATM 5360 O  O   . HOH   R 5 .   ? 23.346  22.260 39.267  1.00 35.44  ? 536 HOH   A O   1 
HETATM 5361 O  O   . HOH   R 5 .   ? 30.496  2.570  21.150  1.00 45.60  ? 537 HOH   A O   1 
HETATM 5362 O  O   . HOH   R 5 .   ? 8.281   5.798  9.069   1.00 25.85  ? 538 HOH   A O   1 
HETATM 5363 O  O   . HOH   R 5 .   ? -4.111  9.056  7.170   1.00 31.83  ? 539 HOH   A O   1 
HETATM 5364 O  O   . HOH   R 5 .   ? -12.655 34.942 22.508  1.00 29.07  ? 540 HOH   A O   1 
HETATM 5365 O  O   . HOH   R 5 .   ? 10.768  32.111 24.870  1.00 24.94  ? 541 HOH   A O   1 
HETATM 5366 O  O   . HOH   R 5 .   ? 21.264  4.994  14.633  1.00 34.46  ? 542 HOH   A O   1 
HETATM 5367 O  O   . HOH   R 5 .   ? 4.361   14.004 5.616   1.00 25.61  ? 543 HOH   A O   1 
HETATM 5368 O  O   . HOH   R 5 .   ? 17.248  27.671 12.264  1.00 44.39  ? 544 HOH   A O   1 
HETATM 5369 O  O   . HOH   R 5 .   ? -4.382  28.506 13.191  1.00 27.74  ? 545 HOH   A O   1 
HETATM 5370 O  O   . HOH   R 5 .   ? 23.568  10.960 17.629  1.00 41.13  ? 546 HOH   A O   1 
HETATM 5371 O  O   . HOH   R 5 .   ? -10.393 38.666 33.595  1.00 32.65  ? 547 HOH   A O   1 
HETATM 5372 O  O   . HOH   R 5 .   ? -4.240  -2.607 17.317  1.00 22.43  ? 548 HOH   A O   1 
HETATM 5373 O  O   . HOH   R 5 .   ? 2.315   40.879 17.130  1.00 32.23  ? 549 HOH   A O   1 
HETATM 5374 O  O   . HOH   R 5 .   ? 17.883  31.493 17.766  1.00 30.57  ? 550 HOH   A O   1 
HETATM 5375 O  O   . HOH   R 5 .   ? -12.105 4.643  11.143  1.00 33.40  ? 551 HOH   A O   1 
HETATM 5376 O  O   . HOH   R 5 .   ? -3.125  -4.013 20.302  1.00 35.49  ? 552 HOH   A O   1 
HETATM 5377 O  O   . HOH   R 5 .   ? -7.665  -4.633 18.961  1.00 34.84  ? 553 HOH   A O   1 
HETATM 5378 O  O   . HOH   R 5 .   ? -11.073 -1.325 16.809  1.00 33.45  ? 554 HOH   A O   1 
HETATM 5379 O  O   . HOH   R 5 .   ? 17.888  17.979 28.475  1.00 16.51  ? 555 HOH   A O   1 
HETATM 5380 O  O   . HOH   R 5 .   ? 9.015   15.932 3.138   1.00 37.86  ? 556 HOH   A O   1 
HETATM 5381 O  O   . HOH   R 5 .   ? -10.434 15.242 27.367  1.00 41.10  ? 557 HOH   A O   1 
HETATM 5382 O  O   . HOH   R 5 .   ? 16.703  7.386  28.957  1.00 38.34  ? 558 HOH   A O   1 
HETATM 5383 O  O   . HOH   R 5 .   ? -7.266  2.818  30.315  1.00 24.88  ? 559 HOH   A O   1 
HETATM 5384 O  O   . HOH   R 5 .   ? 0.550   13.524 48.657  1.00 36.60  ? 560 HOH   A O   1 
HETATM 5385 O  O   . HOH   R 5 .   ? 5.494   9.861  49.607  1.00 26.32  ? 561 HOH   A O   1 
HETATM 5386 O  O   . HOH   R 5 .   ? 20.954  15.465 14.381  1.00 37.85  ? 562 HOH   A O   1 
HETATM 5387 O  O   . HOH   R 5 .   ? 14.833  4.375  25.753  1.00 21.05  ? 563 HOH   A O   1 
HETATM 5388 O  O   . HOH   R 5 .   ? -10.303 21.047 12.058  1.00 22.62  ? 564 HOH   A O   1 
HETATM 5389 O  O   . HOH   R 5 .   ? 6.711   44.852 22.811  1.00 27.84  ? 565 HOH   A O   1 
HETATM 5390 O  O   . HOH   R 5 .   ? -2.782  33.089 18.236  1.00 19.00  ? 566 HOH   A O   1 
HETATM 5391 O  O   . HOH   R 5 .   ? 6.116   25.194 26.389  1.00 10.15  ? 567 HOH   A O   1 
HETATM 5392 O  O   . HOH   R 5 .   ? -1.390  0.748  31.609  1.00 26.90  ? 568 HOH   A O   1 
HETATM 5393 O  O   . HOH   R 5 .   ? 1.496   32.130 43.666  1.00 30.63  ? 569 HOH   A O   1 
HETATM 5394 O  O   . HOH   R 5 .   ? -6.621  34.783 42.253  1.00 32.42  ? 570 HOH   A O   1 
HETATM 5395 O  O   . HOH   R 5 .   ? 12.935  -1.326 33.188  1.00 29.75  ? 571 HOH   A O   1 
HETATM 5396 O  O   . HOH   R 5 .   ? 20.184  19.554 33.286  1.00 23.96  ? 572 HOH   A O   1 
HETATM 5397 O  O   . HOH   R 5 .   ? 12.370  12.013 14.146  1.00 21.41  ? 573 HOH   A O   1 
HETATM 5398 O  O   . HOH   R 5 .   ? -11.105 33.025 21.308  1.00 31.10  ? 574 HOH   A O   1 
HETATM 5399 O  O   . HOH   R 5 .   ? 8.781   19.624 3.042   1.00 40.63  ? 575 HOH   A O   1 
HETATM 5400 O  O   . HOH   R 5 .   ? 4.725   20.161 16.202  1.00 22.90  ? 576 HOH   A O   1 
HETATM 5401 O  O   . HOH   R 5 .   ? 13.934  2.102  5.669   1.00 45.78  ? 577 HOH   A O   1 
HETATM 5402 O  O   . HOH   R 5 .   ? -9.689  2.209  13.281  1.00 25.19  ? 578 HOH   A O   1 
HETATM 5403 O  O   . HOH   R 5 .   ? 12.260  0.448  36.754  1.00 29.88  ? 579 HOH   A O   1 
HETATM 5404 O  O   . HOH   R 5 .   ? 15.707  -2.414 27.519  1.00 24.46  ? 580 HOH   A O   1 
HETATM 5405 O  O   . HOH   R 5 .   ? 10.642  7.531  52.245  1.00 39.37  ? 581 HOH   A O   1 
HETATM 5406 O  O   . HOH   R 5 .   ? 2.863   46.578 24.569  1.00 23.76  ? 582 HOH   A O   1 
HETATM 5407 O  O   . HOH   R 5 .   ? 3.709   15.256 28.584  1.00 12.53  ? 583 HOH   A O   1 
HETATM 5408 O  O   . HOH   R 5 .   ? 14.800  21.451 46.304  1.00 37.58  ? 584 HOH   A O   1 
HETATM 5409 O  O   . HOH   R 5 .   ? 5.440   -3.850 22.356  1.00 29.11  ? 585 HOH   A O   1 
HETATM 5410 O  O   . HOH   R 5 .   ? 12.997  25.510 22.680  1.00 16.83  ? 586 HOH   A O   1 
HETATM 5411 O  O   . HOH   R 5 .   ? -1.951  8.236  32.287  1.00 14.34  ? 587 HOH   A O   1 
HETATM 5412 O  O   . HOH   R 5 .   ? -11.138 42.755 27.886  1.00 30.05  ? 588 HOH   A O   1 
HETATM 5413 O  O   . HOH   R 5 .   ? -6.856  19.664 23.763  1.00 15.70  ? 589 HOH   A O   1 
HETATM 5414 O  O   . HOH   R 5 .   ? 23.124  26.175 25.113  1.00 35.55  ? 590 HOH   A O   1 
HETATM 5415 O  O   . HOH   R 5 .   ? 0.988   20.075 37.200  1.00 15.96  ? 591 HOH   A O   1 
HETATM 5416 O  O   . HOH   R 5 .   ? -8.761  37.571 16.497  1.00 34.54  ? 592 HOH   A O   1 
HETATM 5417 O  O   . HOH   R 5 .   ? -12.672 7.927  22.504  1.00 24.31  ? 593 HOH   A O   1 
HETATM 5418 O  O   . HOH   R 5 .   ? 11.047  7.180  45.989  1.00 21.88  ? 594 HOH   A O   1 
HETATM 5419 O  O   . HOH   R 5 .   ? -8.109  28.858 18.507  1.00 27.78  ? 595 HOH   A O   1 
HETATM 5420 O  O   . HOH   R 5 .   ? -6.283  5.655  24.675  1.00 14.54  ? 596 HOH   A O   1 
HETATM 5421 O  O   . HOH   R 5 .   ? -7.567  11.944 25.470  1.00 15.42  ? 597 HOH   A O   1 
HETATM 5422 O  O   . HOH   R 5 .   ? 1.597   -6.547 26.528  1.00 28.23  ? 598 HOH   A O   1 
HETATM 5423 O  O   . HOH   R 5 .   ? 15.105  -0.776 21.765  1.00 22.97  ? 599 HOH   A O   1 
HETATM 5424 O  O   . HOH   R 5 .   ? 17.322  29.524 33.374  1.00 25.94  ? 600 HOH   A O   1 
HETATM 5425 O  O   . HOH   R 5 .   ? 13.077  3.414  12.773  1.00 19.32  ? 601 HOH   A O   1 
HETATM 5426 O  O   . HOH   R 5 .   ? 7.325   39.817 19.416  1.00 29.40  ? 602 HOH   A O   1 
HETATM 5427 O  O   . HOH   R 5 .   ? -1.926  47.431 29.054  1.00 26.57  ? 603 HOH   A O   1 
HETATM 5428 O  O   . HOH   R 5 .   ? 25.520  18.478 7.630   1.00 35.29  ? 604 HOH   A O   1 
HETATM 5429 O  O   . HOH   R 5 .   ? 17.173  7.813  38.197  1.00 17.65  ? 605 HOH   A O   1 
HETATM 5430 O  O   . HOH   R 5 .   ? 11.955  22.800 8.739   1.00 25.89  ? 606 HOH   A O   1 
HETATM 5431 O  O   . HOH   R 5 .   ? 13.913  14.266 14.087  1.00 22.44  ? 607 HOH   A O   1 
HETATM 5432 O  O   . HOH   R 5 .   ? -5.456  8.970  36.103  1.00 31.83  ? 608 HOH   A O   1 
HETATM 5433 O  O   . HOH   R 5 .   ? 4.486   41.195 14.128  1.00 38.42  ? 609 HOH   A O   1 
HETATM 5434 O  O   . HOH   R 5 .   ? 16.801  11.163 28.957  1.00 17.36  ? 610 HOH   A O   1 
HETATM 5435 O  O   . HOH   R 5 .   ? 15.196  32.777 40.673  1.00 25.92  ? 611 HOH   A O   1 
HETATM 5436 O  O   . HOH   R 5 .   ? 22.456  17.562 9.682   1.00 36.92  ? 612 HOH   A O   1 
HETATM 5437 O  O   . HOH   R 5 .   ? 6.683   -1.092 8.547   1.00 27.95  ? 613 HOH   A O   1 
HETATM 5438 O  O   . HOH   R 5 .   ? -12.111 11.727 27.500  1.00 34.46  ? 614 HOH   A O   1 
HETATM 5439 O  O   . HOH   R 5 .   ? 9.938   9.151  17.702  1.00 9.62   ? 615 HOH   A O   1 
HETATM 5440 O  O   . HOH   R 5 .   ? 8.173   26.157 34.274  1.00 16.67  ? 616 HOH   A O   1 
HETATM 5441 O  O   . HOH   R 5 .   ? -3.896  5.332  26.378  1.00 11.77  ? 617 HOH   A O   1 
HETATM 5442 O  O   . HOH   R 5 .   ? 9.253   36.488 34.138  1.00 20.62  ? 618 HOH   A O   1 
HETATM 5443 O  O   . HOH   R 5 .   ? 19.097  22.698 21.863  1.00 15.82  ? 619 HOH   A O   1 
HETATM 5444 O  O   . HOH   R 5 .   ? 1.049   29.667 24.478  1.00 11.90  ? 620 HOH   A O   1 
HETATM 5445 O  O   . HOH   R 5 .   ? -8.566  4.203  33.133  1.00 56.08  ? 621 HOH   A O   1 
HETATM 5446 O  O   . HOH   R 5 .   ? 3.683   21.308 45.857  1.00 28.95  ? 622 HOH   A O   1 
HETATM 5447 O  O   . HOH   R 5 .   ? 15.406  33.028 30.039  1.00 32.84  ? 623 HOH   A O   1 
HETATM 5448 O  O   . HOH   R 5 .   ? 12.731  10.473 22.954  1.00 13.47  ? 624 HOH   A O   1 
HETATM 5449 O  O   . HOH   R 5 .   ? -1.444  28.759 41.694  1.00 40.68  ? 625 HOH   A O   1 
HETATM 5450 O  O   . HOH   R 5 .   ? 7.133   -2.397 10.695  1.00 28.49  ? 626 HOH   A O   1 
HETATM 5451 O  O   . HOH   R 5 .   ? 3.598   -4.193 15.829  1.00 28.03  ? 627 HOH   A O   1 
HETATM 5452 O  O   . HOH   R 5 .   ? -0.133  1.950  39.544  1.00 41.50  ? 628 HOH   A O   1 
HETATM 5453 O  O   . HOH   R 5 .   ? -1.561  7.964  34.983  1.00 19.99  ? 629 HOH   A O   1 
HETATM 5454 O  O   . HOH   R 5 .   ? 17.693  1.513  17.428  1.00 29.82  ? 630 HOH   A O   1 
HETATM 5455 O  O   . HOH   R 5 .   ? 18.230  26.312 30.463  1.00 16.21  ? 631 HOH   A O   1 
HETATM 5456 O  O   . HOH   R 5 .   ? -8.323  30.214 21.126  1.00 24.68  ? 632 HOH   A O   1 
HETATM 5457 O  O   . HOH   R 5 .   ? 0.588   47.236 35.216  1.00 44.46  ? 633 HOH   A O   1 
HETATM 5458 O  O   . HOH   R 5 .   ? -9.276  45.921 27.849  1.00 32.79  ? 634 HOH   A O   1 
HETATM 5459 O  O   . HOH   R 5 .   ? 11.364  7.473  5.717   1.00 35.00  ? 635 HOH   A O   1 
HETATM 5460 O  O   . HOH   R 5 .   ? 12.417  34.391 29.034  1.00 24.18  ? 636 HOH   A O   1 
HETATM 5461 O  O   . HOH   R 5 .   ? -0.657  11.055 38.014  1.00 30.63  ? 637 HOH   A O   1 
HETATM 5462 O  O   . HOH   R 5 .   ? 4.582   -6.238 32.709  1.00 35.01  ? 638 HOH   A O   1 
HETATM 5463 O  O   . HOH   R 5 .   ? 12.495  18.299 50.846  1.00 37.07  ? 639 HOH   A O   1 
HETATM 5464 O  O   . HOH   R 5 .   ? 13.642  1.582  14.612  1.00 18.36  ? 640 HOH   A O   1 
HETATM 5465 O  O   . HOH   R 5 .   ? 8.386   43.410 20.166  1.00 31.13  ? 641 HOH   A O   1 
HETATM 5466 O  O   . HOH   R 5 .   ? 28.459  17.736 8.166   1.00 34.13  ? 642 HOH   A O   1 
HETATM 5467 O  O   . HOH   R 5 .   ? -11.797 16.427 31.286  1.00 30.87  ? 643 HOH   A O   1 
HETATM 5468 O  O   . HOH   R 5 .   ? 14.792  31.422 27.601  1.00 32.19  ? 644 HOH   A O   1 
HETATM 5469 O  O   . HOH   R 5 .   ? 8.819   -1.767 35.406  1.00 21.49  ? 645 HOH   A O   1 
HETATM 5470 O  O   . HOH   R 5 .   ? 5.805   38.030 12.143  1.00 35.92  ? 646 HOH   A O   1 
HETATM 5471 O  O   . HOH   R 5 .   ? -1.380  22.805 12.366  1.00 19.49  ? 647 HOH   A O   1 
HETATM 5472 O  O   . HOH   R 5 .   ? 25.992  17.965 36.140  1.00 35.24  ? 648 HOH   A O   1 
HETATM 5473 O  O   . HOH   R 5 .   ? -5.885  34.556 13.629  1.00 26.64  ? 649 HOH   A O   1 
HETATM 5474 O  O   . HOH   R 5 .   ? 3.921   32.178 42.414  1.00 33.90  ? 650 HOH   A O   1 
HETATM 5475 O  O   . HOH   R 5 .   ? 5.521   2.456  41.002  1.00 29.65  ? 651 HOH   A O   1 
HETATM 5476 O  O   . HOH   R 5 .   ? -4.493  -7.828 24.387  1.00 40.38  ? 652 HOH   A O   1 
HETATM 5477 O  O   . HOH   R 5 .   ? 8.311   19.865 48.679  1.00 44.66  ? 653 HOH   A O   1 
HETATM 5478 O  O   . HOH   R 5 .   ? 8.057   33.457 41.875  1.00 27.07  ? 654 HOH   A O   1 
HETATM 5479 O  O   . HOH   R 5 .   ? 2.415   18.844 14.099  1.00 30.54  ? 655 HOH   A O   1 
HETATM 5480 O  O   . HOH   R 5 .   ? 20.322  17.991 26.524  1.00 21.98  ? 656 HOH   A O   1 
HETATM 5481 O  O   . HOH   R 5 .   ? -9.279  4.365  22.599  1.00 28.60  ? 657 HOH   A O   1 
HETATM 5482 O  O   . HOH   R 5 .   ? -4.298  36.324 42.427  1.00 28.52  ? 658 HOH   A O   1 
HETATM 5483 O  O   . HOH   R 5 .   ? 13.317  5.909  23.177  1.00 15.70  ? 659 HOH   A O   1 
HETATM 5484 O  O   . HOH   R 5 .   ? -2.772  12.902 37.227  1.00 32.27  ? 660 HOH   A O   1 
HETATM 5485 O  O   . HOH   R 5 .   ? 4.136   6.680  46.513  1.00 18.79  ? 661 HOH   A O   1 
HETATM 5486 O  O   . HOH   R 5 .   ? -4.332  -4.709 29.825  1.00 43.85  ? 662 HOH   A O   1 
HETATM 5487 O  O   . HOH   R 5 .   ? 16.691  34.762 39.070  1.00 33.00  ? 663 HOH   A O   1 
HETATM 5488 O  O   . HOH   R 5 .   ? -3.864  1.375  31.648  1.00 30.89  ? 664 HOH   A O   1 
HETATM 5489 O  O   . HOH   R 5 .   ? 16.140  21.833 44.264  1.00 23.09  ? 665 HOH   A O   1 
HETATM 5490 O  O   . HOH   R 5 .   ? -1.899  27.821 13.538  1.00 25.12  ? 666 HOH   A O   1 
HETATM 5491 O  O   . HOH   R 5 .   ? 2.883   21.269 -2.654  1.00 20.46  ? 667 HOH   A O   1 
HETATM 5492 O  O   . HOH   R 5 .   ? 10.443  33.485 20.916  1.00 17.62  ? 668 HOH   A O   1 
HETATM 5493 O  O   . HOH   R 5 .   ? 18.049  31.248 35.469  1.00 28.06  ? 669 HOH   A O   1 
HETATM 5494 O  O   . HOH   R 5 .   ? -13.913 10.815 19.916  1.00 27.43  ? 670 HOH   A O   1 
HETATM 5495 O  O   . HOH   R 5 .   ? 19.458  9.942  31.750  1.00 23.08  ? 671 HOH   A O   1 
HETATM 5496 O  O   . HOH   R 5 .   ? 26.662  17.737 33.103  1.00 36.51  ? 672 HOH   A O   1 
HETATM 5497 O  O   . HOH   R 5 .   ? -8.583  37.377 36.762  1.00 20.39  ? 673 HOH   A O   1 
HETATM 5498 O  O   . HOH   R 5 .   ? -7.048  31.266 15.488  1.00 32.85  ? 674 HOH   A O   1 
HETATM 5499 O  O   . HOH   R 5 .   ? -6.705  23.064 29.372  1.00 23.11  ? 675 HOH   A O   1 
HETATM 5500 O  O   . HOH   R 5 .   ? 2.113   15.116 26.248  1.00 9.30   ? 676 HOH   A O   1 
HETATM 5501 O  O   . HOH   R 5 .   ? 19.894  10.462 25.485  1.00 33.13  ? 677 HOH   A O   1 
HETATM 5502 O  O   . HOH   R 5 .   ? 7.095   4.354  39.658  1.00 23.05  ? 678 HOH   A O   1 
HETATM 5503 O  O   . HOH   R 5 .   ? -11.716 30.247 25.067  1.00 30.33  ? 679 HOH   A O   1 
HETATM 5504 O  O   . HOH   R 5 .   ? -7.506  37.096 39.492  1.00 22.43  ? 680 HOH   A O   1 
HETATM 5505 O  O   . HOH   R 5 .   ? 0.749   20.440 9.088   1.00 33.53  ? 681 HOH   A O   1 
HETATM 5506 O  O   . HOH   R 5 .   ? 1.340   26.571 -1.826  1.00 35.00  ? 682 HOH   A O   1 
HETATM 5507 O  O   . HOH   R 5 .   ? 8.146   36.505 39.434  1.00 26.29  ? 683 HOH   A O   1 
HETATM 5508 O  O   . HOH   R 5 .   ? 10.840  40.196 17.869  1.00 35.56  ? 684 HOH   A O   1 
HETATM 5509 O  O   . HOH   R 5 .   ? -11.830 31.890 27.229  1.00 25.71  ? 685 HOH   A O   1 
HETATM 5510 O  O   . HOH   R 5 .   ? 11.798  36.617 35.261  1.00 30.16  ? 686 HOH   A O   1 
HETATM 5511 O  O   . HOH   R 5 .   ? 24.496  10.869 38.504  1.00 28.43  ? 687 HOH   A O   1 
HETATM 5512 O  O   . HOH   R 5 .   ? 17.756  9.081  4.367   1.00 32.19  ? 688 HOH   A O   1 
HETATM 5513 O  O   . HOH   R 5 .   ? -11.262 30.828 32.235  1.00 21.17  ? 689 HOH   A O   1 
HETATM 5514 O  O   . HOH   R 5 .   ? 27.237  20.018 37.924  1.00 49.39  ? 690 HOH   A O   1 
HETATM 5515 O  O   . HOH   R 5 .   ? 18.338  18.469 31.255  1.00 17.08  ? 691 HOH   A O   1 
HETATM 5516 O  O   . HOH   R 5 .   ? 20.599  5.678  23.051  1.00 44.20  ? 692 HOH   A O   1 
HETATM 5517 O  O   . HOH   R 5 .   ? -15.086 37.837 29.038  1.00 29.12  ? 693 HOH   A O   1 
HETATM 5518 O  O   . HOH   R 5 .   ? -10.995 -2.476 12.738  1.00 28.76  ? 694 HOH   A O   1 
HETATM 5519 O  O   . HOH   R 5 .   ? 22.626  16.440 26.887  1.00 26.86  ? 695 HOH   A O   1 
HETATM 5520 O  O   . HOH   R 5 .   ? 2.514   38.293 38.354  1.00 32.53  ? 696 HOH   A O   1 
HETATM 5521 O  O   . HOH   R 5 .   ? -2.261  21.085 36.349  1.00 20.18  ? 697 HOH   A O   1 
HETATM 5522 O  O   . HOH   R 5 .   ? 3.571   -5.381 18.189  1.00 40.37  ? 698 HOH   A O   1 
HETATM 5523 O  O   . HOH   R 5 .   ? 5.537   8.108  4.910   1.00 40.68  ? 699 HOH   A O   1 
HETATM 5524 O  O   . HOH   R 5 .   ? 7.232   36.783 30.838  1.00 17.95  ? 700 HOH   A O   1 
HETATM 5525 O  O   . HOH   R 5 .   ? 15.391  26.022 21.290  1.00 15.99  ? 701 HOH   A O   1 
HETATM 5526 O  O   . HOH   R 5 .   ? -12.795 9.033  28.716  1.00 32.08  ? 702 HOH   A O   1 
HETATM 5527 O  O   . HOH   R 5 .   ? 18.010  14.812 16.908  1.00 35.70  ? 703 HOH   A O   1 
HETATM 5528 O  O   . HOH   R 5 .   ? -10.003 19.290 36.851  1.00 33.93  ? 704 HOH   A O   1 
HETATM 5529 O  O   . HOH   R 5 .   ? -3.823  23.899 12.905  1.00 17.09  ? 705 HOH   A O   1 
HETATM 5530 O  O   . HOH   R 5 .   ? -9.724  -3.633 19.551  1.00 25.79  ? 706 HOH   A O   1 
HETATM 5531 O  O   . HOH   R 5 .   ? -3.293  47.174 35.774  1.00 39.39  ? 707 HOH   A O   1 
HETATM 5532 O  O   . HOH   R 5 .   ? 4.699   43.386 30.041  1.00 35.87  ? 708 HOH   A O   1 
HETATM 5533 O  O   . HOH   R 5 .   ? 15.616  7.754  40.218  1.00 18.17  ? 709 HOH   A O   1 
HETATM 5534 O  O   . HOH   R 5 .   ? -1.019  16.441 44.173  1.00 33.32  ? 710 HOH   A O   1 
HETATM 5535 O  O   . HOH   R 5 .   ? 10.859  39.385 13.627  1.00 40.91  ? 711 HOH   A O   1 
HETATM 5536 O  O   . HOH   R 5 .   ? -11.380 12.059 10.329  1.00 36.22  ? 712 HOH   A O   1 
HETATM 5537 O  O   . HOH   R 5 .   ? -10.786 28.706 35.520  1.00 46.15  ? 713 HOH   A O   1 
HETATM 5538 O  O   . HOH   R 5 .   ? 10.185  34.452 23.527  1.00 21.76  ? 714 HOH   A O   1 
HETATM 5539 O  O   . HOH   R 5 .   ? -3.221  43.975 24.542  1.00 26.00  ? 715 HOH   A O   1 
HETATM 5540 O  O   . HOH   R 5 .   ? -4.734  26.349 12.179  1.00 27.05  ? 716 HOH   A O   1 
HETATM 5541 O  O   . HOH   R 5 .   ? -4.986  32.928 11.942  1.00 40.36  ? 717 HOH   A O   1 
HETATM 5542 O  O   . HOH   R 5 .   ? 19.549  18.769 43.936  1.00 29.97  ? 718 HOH   A O   1 
HETATM 5543 O  O   . HOH   R 5 .   ? -15.350 12.985 14.526  1.00 41.13  ? 719 HOH   A O   1 
HETATM 5544 O  O   . HOH   R 5 .   ? -10.309 26.859 30.982  1.00 38.10  ? 720 HOH   A O   1 
HETATM 5545 O  O   . HOH   R 5 .   ? 2.445   12.645 50.228  1.00 44.93  ? 721 HOH   A O   1 
HETATM 5546 O  O   . HOH   R 5 .   ? 4.511   42.817 32.723  1.00 39.13  ? 722 HOH   A O   1 
HETATM 5547 O  O   . HOH   R 5 .   ? -3.364  34.432 44.385  1.00 21.15  ? 723 HOH   A O   1 
HETATM 5548 O  O   . HOH   R 5 .   ? 3.567   5.616  8.544   1.00 28.18  ? 724 HOH   A O   1 
HETATM 5549 O  O   . HOH   R 5 .   ? -4.557  45.256 40.885  1.00 26.91  ? 725 HOH   A O   1 
HETATM 5550 O  O   . HOH   R 5 .   ? 19.838  16.391 24.702  1.00 31.09  ? 726 HOH   A O   1 
HETATM 5551 O  O   . HOH   R 5 .   ? 16.987  2.540  24.661  1.00 27.97  ? 727 HOH   A O   1 
HETATM 5552 O  O   . HOH   R 5 .   ? 7.746   -6.682 18.197  1.00 35.41  ? 728 HOH   A O   1 
HETATM 5553 O  O   . HOH   R 5 .   ? -13.227 6.993  30.657  1.00 49.55  ? 729 HOH   A O   1 
HETATM 5554 O  O   . HOH   R 5 .   ? -9.493  21.067 32.462  1.00 44.23  ? 730 HOH   A O   1 
HETATM 5555 O  O   . HOH   R 5 .   ? -10.215 30.550 36.897  1.00 32.48  ? 731 HOH   A O   1 
HETATM 5556 O  O   . HOH   R 5 .   ? -13.014 16.751 10.205  1.00 37.16  ? 732 HOH   A O   1 
HETATM 5557 O  O   . HOH   R 5 .   ? 28.372  14.414 10.665  1.00 35.38  ? 733 HOH   A O   1 
HETATM 5558 O  O   . HOH   R 5 .   ? -15.232 13.424 25.589  1.00 40.95  ? 734 HOH   A O   1 
HETATM 5559 O  O   . HOH   R 5 .   ? 10.944  31.457 46.885  1.00 38.20  ? 735 HOH   A O   1 
HETATM 5560 O  O   . HOH   R 5 .   ? 16.429  24.710 23.331  1.00 24.88  ? 736 HOH   A O   1 
HETATM 5561 O  O   . HOH   R 5 .   ? 4.690   -2.148 36.257  1.00 42.07  ? 737 HOH   A O   1 
HETATM 5562 O  O   . HOH   R 5 .   ? -7.476  -5.957 12.162  1.00 26.70  ? 738 HOH   A O   1 
HETATM 5563 O  O   . HOH   R 5 .   ? -3.987  -1.897 31.083  1.00 42.46  ? 739 HOH   A O   1 
HETATM 5564 O  O   . HOH   R 5 .   ? -2.444  -2.947 32.618  1.00 55.62  ? 740 HOH   A O   1 
HETATM 5565 O  O   . HOH   R 5 .   ? -2.698  6.134  36.778  1.00 31.20  ? 741 HOH   A O   1 
HETATM 5566 O  O   . HOH   R 5 .   ? -0.790  -4.546 33.721  1.00 60.58  ? 742 HOH   A O   1 
HETATM 5567 O  O   . HOH   R 5 .   ? -0.251  46.096 21.373  1.00 34.42  ? 743 HOH   A O   1 
HETATM 5568 O  O   . HOH   R 5 .   ? 17.169  14.584 14.801  1.00 29.55  ? 744 HOH   A O   1 
HETATM 5569 O  O   . HOH   R 5 .   ? -2.893  -5.319 17.231  1.00 37.41  ? 745 HOH   A O   1 
HETATM 5570 O  O   . HOH   R 5 .   ? 8.809   7.130  6.278   1.00 29.38  ? 746 HOH   A O   1 
HETATM 5571 O  O   . HOH   R 5 .   ? -9.686  -6.189 13.575  1.00 36.39  ? 747 HOH   A O   1 
HETATM 5572 O  O   . HOH   R 5 .   ? 18.725  20.914 44.786  1.00 38.08  ? 748 HOH   A O   1 
HETATM 5573 O  O   . HOH   R 5 .   ? -12.552 37.544 32.464  1.00 32.66  ? 749 HOH   A O   1 
HETATM 5574 O  O   . HOH   R 5 .   ? -4.373  44.879 26.797  1.00 28.84  ? 750 HOH   A O   1 
HETATM 5575 O  O   . HOH   R 5 .   ? 0.712   49.193 33.673  1.00 39.54  ? 751 HOH   A O   1 
HETATM 5576 O  O   . HOH   R 5 .   ? 14.043  -1.000 35.602  1.00 30.14  ? 752 HOH   A O   1 
HETATM 5577 O  O   . HOH   R 5 .   ? 1.456   8.590  7.948   1.00 36.79  ? 753 HOH   A O   1 
HETATM 5578 O  O   . HOH   R 5 .   ? -2.878  48.605 31.552  1.00 31.29  ? 754 HOH   A O   1 
HETATM 5579 O  O   . HOH   R 5 .   ? -9.022  30.452 17.005  1.00 36.36  ? 755 HOH   A O   1 
HETATM 5580 O  O   . HOH   R 5 .   ? 16.670  -1.956 30.060  1.00 35.42  ? 756 HOH   A O   1 
HETATM 5581 O  O   . HOH   R 5 .   ? -12.331 29.817 29.954  1.00 43.15  ? 757 HOH   A O   1 
HETATM 5582 O  O   A HOH   R 5 .   ? 3.172   47.264 27.241  0.60 25.89  ? 758 HOH   A O   1 
HETATM 5583 O  O   . HOH   R 5 .   ? -11.664 18.654 12.140  1.00 29.48  ? 759 HOH   A O   1 
HETATM 5584 O  O   . HOH   R 5 .   ? 18.338  9.408  29.210  1.00 25.94  ? 760 HOH   A O   1 
HETATM 5585 O  O   . HOH   R 5 .   ? -15.631 18.854 19.058  1.00 34.95  ? 761 HOH   A O   1 
HETATM 5586 O  O   . HOH   R 5 .   ? -11.496 -4.686 13.786  1.00 41.36  ? 762 HOH   A O   1 
HETATM 5587 O  O   . HOH   R 5 .   ? 19.416  -1.504 26.680  1.00 43.17  ? 763 HOH   A O   1 
HETATM 5588 O  O   . HOH   R 5 .   ? -10.307 26.886 33.778  1.00 35.65  ? 764 HOH   A O   1 
HETATM 5589 O  O   . HOH   R 5 .   ? 17.494  -2.132 25.604  1.00 31.15  ? 765 HOH   A O   1 
HETATM 5590 O  O   . HOH   R 5 .   ? 12.633  33.334 26.440  1.00 27.03  ? 766 HOH   A O   1 
HETATM 5591 O  O   . HOH   R 5 .   ? -10.294 2.234  32.797  1.00 56.28  ? 767 HOH   A O   1 
HETATM 5592 O  O   . HOH   R 5 .   ? -2.093  3.732  39.976  1.00 48.93  ? 768 HOH   A O   1 
HETATM 5593 O  O   . HOH   R 5 .   ? 11.800  37.869 25.914  1.00 29.58  ? 769 HOH   A O   1 
HETATM 5594 O  O   . HOH   R 5 .   ? 5.446   -6.244 24.099  1.00 25.78  ? 770 HOH   A O   1 
HETATM 5595 O  O   . HOH   R 5 .   ? 16.772  0.251  23.673  1.00 28.34  ? 771 HOH   A O   1 
HETATM 5596 O  O   . HOH   R 5 .   ? -3.982  47.519 27.898  1.00 37.04  ? 772 HOH   A O   1 
HETATM 5597 O  O   . HOH   R 5 .   ? 12.742  44.448 24.642  1.00 34.67  ? 773 HOH   A O   1 
HETATM 5598 O  O   . HOH   R 5 .   ? -9.542  32.281 38.461  1.00 38.24  ? 774 HOH   A O   1 
HETATM 5599 O  O   . HOH   R 5 .   ? 24.214  3.428  23.073  1.00 50.29  ? 775 HOH   A O   1 
HETATM 5600 O  O   . HOH   R 5 .   ? 0.198   49.113 37.393  1.00 38.15  ? 776 HOH   A O   1 
HETATM 5601 O  O   . HOH   R 5 .   ? -1.339  20.332 38.790  1.00 36.27  ? 777 HOH   A O   1 
HETATM 5602 O  O   . HOH   R 5 .   ? 15.086  36.411 23.500  1.00 37.13  ? 778 HOH   A O   1 
HETATM 5603 O  O   . HOH   R 5 .   ? 0.118   48.668 27.756  1.00 34.06  ? 779 HOH   A O   1 
HETATM 5604 O  O   . HOH   R 5 .   ? -8.342  3.833  24.882  1.00 32.39  ? 780 HOH   A O   1 
HETATM 5605 O  O   . HOH   R 5 .   ? -5.626  45.914 38.152  1.00 41.39  ? 781 HOH   A O   1 
HETATM 5606 O  O   . HOH   R 5 .   ? 8.484   4.683  41.701  1.00 31.16  ? 782 HOH   A O   1 
HETATM 5607 O  O   . HOH   R 5 .   ? -10.045 41.540 33.433  1.00 37.04  ? 783 HOH   A O   1 
HETATM 5608 O  O   . HOH   R 5 .   ? 21.941  20.710 9.030   1.00 44.44  ? 784 HOH   A O   1 
HETATM 5609 O  O   . HOH   R 5 .   ? -10.677 -4.882 17.649  1.00 34.55  ? 785 HOH   A O   1 
HETATM 5610 O  O   . HOH   R 5 .   ? -9.349  2.408  27.156  1.00 30.60  ? 786 HOH   A O   1 
HETATM 5611 O  O   . HOH   R 5 .   ? 11.909  36.841 28.549  1.00 33.22  ? 787 HOH   A O   1 
HETATM 5612 O  O   . HOH   R 5 .   ? 18.610  -0.931 17.757  1.00 31.63  ? 788 HOH   A O   1 
HETATM 5613 O  O   . HOH   R 5 .   ? 20.610  19.074 10.463  1.00 40.88  ? 789 HOH   A O   1 
HETATM 5614 O  O   . HOH   R 5 .   ? 7.188   45.960 20.264  1.00 36.01  ? 790 HOH   A O   1 
HETATM 5615 O  O   . HOH   R 5 .   ? 9.083   38.282 29.845  1.00 33.77  ? 791 HOH   A O   1 
HETATM 5616 O  O   . HOH   R 5 .   ? 10.431  33.878 11.564  1.00 38.11  ? 792 HOH   A O   1 
HETATM 5617 O  O   . HOH   R 5 .   ? 4.396   7.588  49.034  1.00 25.76  ? 793 HOH   A O   1 
HETATM 5618 O  O   . HOH   R 5 .   ? -9.181  -6.641 16.401  1.00 34.41  ? 794 HOH   A O   1 
HETATM 5619 O  O   . HOH   R 5 .   ? 12.252  26.743 1.561   1.00 47.07  ? 795 HOH   A O   1 
HETATM 5620 O  O   . HOH   R 5 .   ? 9.021   38.657 33.086  1.00 40.99  ? 796 HOH   A O   1 
HETATM 5621 O  O   . HOH   R 5 .   ? 10.555  -2.210 32.930  1.00 24.45  ? 797 HOH   A O   1 
HETATM 5622 O  O   . HOH   R 5 .   ? 9.830   32.952 44.126  1.00 26.15  ? 798 HOH   A O   1 
HETATM 5623 O  O   . HOH   R 5 .   ? 3.468   0.038  40.298  1.00 40.43  ? 799 HOH   A O   1 
HETATM 5624 O  O   . HOH   R 5 .   ? 6.171   -3.106 38.030  1.00 42.56  ? 800 HOH   A O   1 
HETATM 5625 O  O   . HOH   R 5 .   ? -13.368 35.229 18.437  1.00 38.25  ? 801 HOH   A O   1 
HETATM 5626 O  O   . HOH   R 5 .   ? 20.057  27.123 28.490  1.00 23.15  ? 802 HOH   A O   1 
HETATM 5627 O  O   . HOH   R 5 .   ? -10.648 30.447 22.408  1.00 25.01  ? 803 HOH   A O   1 
HETATM 5628 O  O   . HOH   R 5 .   ? -5.403  48.661 32.288  1.00 33.01  ? 804 HOH   A O   1 
HETATM 5629 O  O   . HOH   R 5 .   ? 9.037   -8.135 19.835  1.00 33.78  ? 805 HOH   A O   1 
HETATM 5630 O  O   . HOH   R 5 .   ? -2.484  45.675 22.821  1.00 31.75  ? 806 HOH   A O   1 
HETATM 5631 O  O   . HOH   R 5 .   ? 19.840  17.468 12.605  1.00 37.68  ? 807 HOH   A O   1 
HETATM 5632 O  O   . HOH   R 5 .   ? 16.109  -3.351 21.539  1.00 26.44  ? 808 HOH   A O   1 
HETATM 5633 O  O   . HOH   R 5 .   ? 5.938   4.891  45.822  1.00 32.00  ? 809 HOH   A O   1 
HETATM 5634 O  O   . HOH   R 5 .   ? 19.245  27.599 32.550  1.00 33.03  ? 810 HOH   A O   1 
HETATM 5635 O  O   . HOH   R 5 .   ? 9.713   -2.276 10.970  1.00 29.11  ? 811 HOH   A O   1 
HETATM 5636 O  O   . HOH   R 5 .   ? 26.896  15.491 31.561  1.00 37.35  ? 812 HOH   A O   1 
HETATM 5637 O  O   . HOH   R 5 .   ? 0.414   45.065 18.022  1.00 36.97  ? 813 HOH   A O   1 
HETATM 5638 O  O   . HOH   R 5 .   ? 22.366  26.912 27.568  1.00 33.51  ? 814 HOH   A O   1 
HETATM 5639 O  O   . HOH   R 5 .   ? 7.302   9.836  0.641   1.00 51.75  ? 815 HOH   A O   1 
HETATM 5640 O  O   . HOH   R 5 .   ? -5.286  42.880 23.559  1.00 30.20  ? 816 HOH   A O   1 
HETATM 5641 O  O   . HOH   R 5 .   ? -2.248  17.575 39.603  1.00 35.30  ? 817 HOH   A O   1 
HETATM 5642 O  O   . HOH   R 5 .   ? 12.664  7.374  3.292   1.00 29.57  ? 818 HOH   A O   1 
HETATM 5643 O  O   . HOH   R 5 .   ? 9.499   9.795  -0.220  1.00 41.71  ? 819 HOH   A O   1 
HETATM 5644 O  O   . HOH   R 5 .   ? 6.952   42.963 29.340  1.00 44.20  ? 820 HOH   A O   1 
HETATM 5645 O  O   . HOH   R 5 .   ? -0.033  42.806 16.948  1.00 31.66  ? 821 HOH   A O   1 
HETATM 5646 O  O   . HOH   R 5 .   ? 12.722  35.629 24.751  1.00 28.95  ? 822 HOH   A O   1 
HETATM 5647 O  O   . HOH   R 5 .   ? 7.237   5.176  48.354  1.00 31.33  ? 823 HOH   A O   1 
HETATM 5648 O  O   . HOH   R 5 .   ? 19.357  -0.068 22.247  1.00 36.01  ? 824 HOH   A O   1 
HETATM 5649 O  O   . HOH   R 5 .   ? -0.580  49.318 25.170  1.00 32.36  ? 825 HOH   A O   1 
HETATM 5650 O  O   . HOH   R 5 .   ? -5.650  44.002 21.460  1.00 38.77  ? 826 HOH   A O   1 
HETATM 5651 O  O   . HOH   R 5 .   ? 17.670  -4.166 23.825  1.00 30.58  ? 827 HOH   A O   1 
HETATM 5652 O  O   . HOH   R 5 .   ? 20.228  -4.634 23.846  1.00 45.00  ? 828 HOH   A O   1 
HETATM 5653 O  O   . HOH   S 5 .   ? -10.406 46.472 10.377  1.00 37.48  ? 501 HOH   B O   1 
HETATM 5654 O  O   . HOH   S 5 .   ? 4.364   17.512 -23.277 1.00 29.31  ? 502 HOH   B O   1 
HETATM 5655 O  O   . HOH   S 5 .   ? 7.735   57.438 -1.078  1.00 30.92  ? 503 HOH   B O   1 
HETATM 5656 O  O   . HOH   S 5 .   ? 12.180  37.203 -26.306 1.00 31.02  ? 504 HOH   B O   1 
HETATM 5657 O  O   . HOH   S 5 .   ? -16.408 48.287 -4.673  1.00 31.14  ? 505 HOH   B O   1 
HETATM 5658 O  O   . HOH   S 5 .   ? -8.575  55.813 -17.092 1.00 32.58  ? 506 HOH   B O   1 
HETATM 5659 O  O   . HOH   S 5 .   ? -12.829 30.808 -31.804 1.00 22.24  ? 507 HOH   B O   1 
HETATM 5660 O  O   . HOH   S 5 .   ? 9.426   33.865 -10.471 1.00 33.21  ? 508 HOH   B O   1 
HETATM 5661 O  O   . HOH   S 5 .   ? -20.517 24.442 -20.121 1.00 34.24  ? 509 HOH   B O   1 
HETATM 5662 O  O   . HOH   S 5 .   ? -0.377  40.761 -27.834 1.00 18.32  ? 510 HOH   B O   1 
HETATM 5663 O  O   . HOH   S 5 .   ? -8.092  17.749 0.207   1.00 40.86  ? 511 HOH   B O   1 
HETATM 5664 O  O   . HOH   S 5 .   ? -7.807  15.636 -11.696 1.00 27.94  ? 512 HOH   B O   1 
HETATM 5665 O  O   . HOH   S 5 .   ? 3.582   39.329 4.383   1.00 16.79  ? 513 HOH   B O   1 
HETATM 5666 O  O   . HOH   S 5 .   ? -0.206  46.752 -17.431 1.00 19.78  ? 514 HOH   B O   1 
HETATM 5667 O  O   . HOH   S 5 .   ? 14.093  30.075 -18.388 1.00 30.94  ? 515 HOH   B O   1 
HETATM 5668 O  O   . HOH   S 5 .   ? 12.871  34.195 -18.476 1.00 34.03  ? 516 HOH   B O   1 
HETATM 5669 O  O   . HOH   S 5 .   ? -0.875  33.523 -32.786 1.00 42.51  ? 517 HOH   B O   1 
HETATM 5670 O  O   . HOH   S 5 .   ? -4.092  17.986 -3.290  1.00 29.86  ? 518 HOH   B O   1 
HETATM 5671 O  O   . HOH   S 5 .   ? -4.927  38.097 11.484  1.00 41.98  ? 519 HOH   B O   1 
HETATM 5672 O  O   . HOH   S 5 .   ? -11.049 26.198 1.655   1.00 36.57  ? 520 HOH   B O   1 
HETATM 5673 O  O   . HOH   S 5 .   ? 11.776  39.944 5.754   1.00 33.73  ? 521 HOH   B O   1 
HETATM 5674 O  O   . HOH   S 5 .   ? -5.072  39.391 -33.928 1.00 31.85  ? 522 HOH   B O   1 
HETATM 5675 O  O   . HOH   S 5 .   ? -24.274 39.311 -23.729 1.00 33.31  ? 523 HOH   B O   1 
HETATM 5676 O  O   . HOH   S 5 .   ? 3.728   39.642 -24.788 1.00 37.43  ? 524 HOH   B O   1 
HETATM 5677 O  O   . HOH   S 5 .   ? 5.415   43.634 10.608  1.00 23.38  ? 525 HOH   B O   1 
HETATM 5678 O  O   . HOH   S 5 .   ? -11.523 29.505 -21.557 1.00 14.59  ? 526 HOH   B O   1 
HETATM 5679 O  O   . HOH   S 5 .   ? 11.724  54.690 -0.342  1.00 39.83  ? 527 HOH   B O   1 
HETATM 5680 O  O   . HOH   S 5 .   ? -15.051 53.717 -20.060 1.00 26.99  ? 528 HOH   B O   1 
HETATM 5681 O  O   . HOH   S 5 .   ? -12.064 38.922 -4.345  1.00 18.55  ? 529 HOH   B O   1 
HETATM 5682 O  O   . HOH   S 5 .   ? 12.081  52.621 6.601   1.00 31.05  ? 530 HOH   B O   1 
HETATM 5683 O  O   . HOH   S 5 .   ? 6.898   36.774 8.004   1.00 29.69  ? 531 HOH   B O   1 
HETATM 5684 O  O   . HOH   S 5 .   ? -6.313  44.958 9.015   1.00 28.74  ? 532 HOH   B O   1 
HETATM 5685 O  O   . HOH   S 5 .   ? -0.573  58.192 -5.080  1.00 36.35  ? 533 HOH   B O   1 
HETATM 5686 O  O   . HOH   S 5 .   ? 17.310  47.026 7.199   1.00 42.15  ? 534 HOH   B O   1 
HETATM 5687 O  O   . HOH   S 5 .   ? -15.101 41.996 -29.032 1.00 22.35  ? 535 HOH   B O   1 
HETATM 5688 O  O   . HOH   S 5 .   ? -16.070 32.965 -22.391 1.00 25.50  ? 536 HOH   B O   1 
HETATM 5689 O  O   . HOH   S 5 .   ? 2.562   18.625 -26.465 1.00 21.76  ? 537 HOH   B O   1 
HETATM 5690 O  O   . HOH   S 5 .   ? -15.387 54.822 -25.420 1.00 49.04  ? 538 HOH   B O   1 
HETATM 5691 O  O   . HOH   S 5 .   ? -11.898 23.834 -9.818  1.00 20.27  ? 539 HOH   B O   1 
HETATM 5692 O  O   . HOH   S 5 .   ? 1.834   30.422 -29.665 1.00 24.50  ? 540 HOH   B O   1 
HETATM 5693 O  O   . HOH   S 5 .   ? -20.309 20.006 -16.013 1.00 28.94  ? 541 HOH   B O   1 
HETATM 5694 O  O   . HOH   S 5 .   ? 4.693   60.191 -7.986  1.00 32.50  ? 542 HOH   B O   1 
HETATM 5695 O  O   . HOH   S 5 .   ? 10.947  46.565 9.468   1.00 26.16  ? 543 HOH   B O   1 
HETATM 5696 O  O   . HOH   S 5 .   ? -9.659  44.709 -0.350  1.00 21.56  ? 544 HOH   B O   1 
HETATM 5697 O  O   . HOH   S 5 .   ? -12.930 17.675 -15.819 1.00 24.22  ? 545 HOH   B O   1 
HETATM 5698 O  O   . HOH   S 5 .   ? -2.417  16.484 7.770   1.00 19.79  ? 546 HOH   B O   1 
HETATM 5699 O  O   . HOH   S 5 .   ? 4.774   36.078 9.308   1.00 35.26  ? 547 HOH   B O   1 
HETATM 5700 O  O   . HOH   S 5 .   ? -5.251  41.373 -6.901  1.00 12.35  ? 548 HOH   B O   1 
HETATM 5701 O  O   . HOH   S 5 .   ? -14.293 18.559 -27.687 1.00 31.44  ? 549 HOH   B O   1 
HETATM 5702 O  O   . HOH   S 5 .   ? 4.804   16.224 -7.736  1.00 25.53  ? 550 HOH   B O   1 
HETATM 5703 O  O   . HOH   S 5 .   ? -20.630 38.341 -20.304 1.00 24.40  ? 551 HOH   B O   1 
HETATM 5704 O  O   . HOH   S 5 .   ? 5.326   14.132 -13.967 1.00 29.55  ? 552 HOH   B O   1 
HETATM 5705 O  O   . HOH   S 5 .   ? 9.985   16.902 -17.663 1.00 24.00  ? 553 HOH   B O   1 
HETATM 5706 O  O   . HOH   S 5 .   ? -15.387 25.958 -29.313 1.00 21.58  ? 554 HOH   B O   1 
HETATM 5707 O  O   . HOH   S 5 .   ? -4.601  51.104 -32.829 1.00 31.10  ? 555 HOH   B O   1 
HETATM 5708 O  O   . HOH   S 5 .   ? 12.010  41.688 2.182   1.00 30.84  ? 556 HOH   B O   1 
HETATM 5709 O  O   . HOH   S 5 .   ? 8.094   32.483 -16.989 1.00 18.16  ? 557 HOH   B O   1 
HETATM 5710 O  O   . HOH   S 5 .   ? -9.358  24.901 -14.430 1.00 12.79  ? 558 HOH   B O   1 
HETATM 5711 O  O   . HOH   S 5 .   ? 10.367  34.445 -16.190 1.00 34.67  ? 559 HOH   B O   1 
HETATM 5712 O  O   . HOH   S 5 .   ? 7.429   36.214 4.806   1.00 29.71  ? 560 HOH   B O   1 
HETATM 5713 O  O   . HOH   S 5 .   ? 7.697   35.780 -9.841  1.00 22.82  ? 561 HOH   B O   1 
HETATM 5714 O  O   . HOH   S 5 .   ? -6.715  58.656 -8.895  1.00 29.18  ? 562 HOH   B O   1 
HETATM 5715 O  O   . HOH   S 5 .   ? 10.843  20.991 -16.469 1.00 29.31  ? 563 HOH   B O   1 
HETATM 5716 O  O   . HOH   S 5 .   ? -2.573  54.487 -22.028 1.00 34.09  ? 564 HOH   B O   1 
HETATM 5717 O  O   . HOH   S 5 .   ? 9.312   39.800 0.313   1.00 22.59  ? 565 HOH   B O   1 
HETATM 5718 O  O   . HOH   S 5 .   ? 11.182  14.030 -21.601 1.00 48.86  ? 566 HOH   B O   1 
HETATM 5719 O  O   . HOH   S 5 .   ? -8.191  19.922 -27.153 1.00 16.90  ? 567 HOH   B O   1 
HETATM 5720 O  O   . HOH   S 5 .   ? -4.424  22.286 -32.015 1.00 27.17  ? 568 HOH   B O   1 
HETATM 5721 O  O   . HOH   S 5 .   ? -7.561  31.085 5.404   1.00 41.68  ? 569 HOH   B O   1 
HETATM 5722 O  O   . HOH   S 5 .   ? -20.166 50.140 -20.618 1.00 30.85  ? 570 HOH   B O   1 
HETATM 5723 O  O   . HOH   S 5 .   ? 7.478   30.711 -27.329 1.00 24.80  ? 571 HOH   B O   1 
HETATM 5724 O  O   . HOH   S 5 .   ? -7.136  30.804 -2.881  1.00 31.20  ? 572 HOH   B O   1 
HETATM 5725 O  O   . HOH   S 5 .   ? -19.190 32.279 -18.005 1.00 26.70  ? 573 HOH   B O   1 
HETATM 5726 O  O   . HOH   S 5 .   ? -2.998  37.194 -16.066 1.00 11.15  ? 574 HOH   B O   1 
HETATM 5727 O  O   . HOH   S 5 .   ? -16.662 40.615 -27.612 1.00 16.10  ? 575 HOH   B O   1 
HETATM 5728 O  O   . HOH   S 5 .   ? -1.189  52.706 11.381  1.00 31.82  ? 576 HOH   B O   1 
HETATM 5729 O  O   . HOH   S 5 .   ? 9.137   58.404 -5.770  1.00 41.82  ? 577 HOH   B O   1 
HETATM 5730 O  O   . HOH   S 5 .   ? -10.826 12.290 -22.006 1.00 41.49  ? 578 HOH   B O   1 
HETATM 5731 O  O   . HOH   S 5 .   ? -17.203 39.130 -13.659 1.00 18.53  ? 579 HOH   B O   1 
HETATM 5732 O  O   . HOH   S 5 .   ? -5.286  14.757 -11.028 1.00 35.73  ? 580 HOH   B O   1 
HETATM 5733 O  O   . HOH   S 5 .   ? 13.782  43.652 3.355   1.00 27.42  ? 581 HOH   B O   1 
HETATM 5734 O  O   . HOH   S 5 .   ? -3.861  30.343 -34.837 1.00 43.53  ? 582 HOH   B O   1 
HETATM 5735 O  O   . HOH   S 5 .   ? -13.347 25.182 -8.067  1.00 28.51  ? 583 HOH   B O   1 
HETATM 5736 O  O   . HOH   S 5 .   ? -10.253 40.407 -33.492 1.00 37.90  ? 584 HOH   B O   1 
HETATM 5737 O  O   . HOH   S 5 .   ? -6.822  12.416 -19.871 1.00 39.91  ? 585 HOH   B O   1 
HETATM 5738 O  O   . HOH   S 5 .   ? -17.100 13.575 -12.847 1.00 42.64  ? 586 HOH   B O   1 
HETATM 5739 O  O   . HOH   S 5 .   ? -8.010  54.579 -2.454  1.00 28.01  ? 587 HOH   B O   1 
HETATM 5740 O  O   . HOH   S 5 .   ? -17.573 20.540 -19.683 1.00 29.01  ? 588 HOH   B O   1 
HETATM 5741 O  O   . HOH   S 5 .   ? -29.102 22.565 -14.601 1.00 31.96  ? 589 HOH   B O   1 
HETATM 5742 O  O   . HOH   S 5 .   ? -14.498 28.562 -22.887 1.00 22.49  ? 590 HOH   B O   1 
HETATM 5743 O  O   . HOH   S 5 .   ? -26.565 27.748 -14.885 1.00 36.12  ? 591 HOH   B O   1 
HETATM 5744 O  O   . HOH   S 5 .   ? 6.744   28.119 -21.638 1.00 22.81  ? 592 HOH   B O   1 
HETATM 5745 O  O   . HOH   S 5 .   ? -3.937  30.203 -4.854  1.00 17.71  ? 593 HOH   B O   1 
HETATM 5746 O  O   . HOH   S 5 .   ? -19.913 27.292 -20.290 1.00 36.40  ? 594 HOH   B O   1 
HETATM 5747 O  O   . HOH   S 5 .   ? 9.976   40.348 8.581   1.00 38.67  ? 595 HOH   B O   1 
HETATM 5748 O  O   . HOH   S 5 .   ? -13.059 53.309 -27.514 1.00 42.80  ? 596 HOH   B O   1 
HETATM 5749 O  O   . HOH   S 5 .   ? 5.232   49.655 -19.884 1.00 45.65  ? 597 HOH   B O   1 
HETATM 5750 O  O   . HOH   S 5 .   ? -12.341 33.979 4.735   1.00 30.60  ? 598 HOH   B O   1 
HETATM 5751 O  O   . HOH   S 5 .   ? -13.796 49.408 -2.716  1.00 34.81  ? 599 HOH   B O   1 
HETATM 5752 O  O   . HOH   S 5 .   ? -3.548  15.439 -23.968 1.00 27.91  ? 600 HOH   B O   1 
HETATM 5753 O  O   . HOH   S 5 .   ? -17.193 43.490 -5.008  1.00 26.80  ? 601 HOH   B O   1 
HETATM 5754 O  O   . HOH   S 5 .   ? -0.122  42.425 -2.162  1.00 13.43  ? 602 HOH   B O   1 
HETATM 5755 O  O   . HOH   S 5 .   ? -11.025 23.535 -34.177 1.00 32.91  ? 603 HOH   B O   1 
HETATM 5756 O  O   . HOH   S 5 .   ? 9.835   22.599 -26.722 1.00 45.46  ? 604 HOH   B O   1 
HETATM 5757 O  O   . HOH   S 5 .   ? -12.060 35.056 -32.810 1.00 40.19  ? 605 HOH   B O   1 
HETATM 5758 O  O   . HOH   S 5 .   ? 8.926   37.294 0.765   1.00 25.37  ? 606 HOH   B O   1 
HETATM 5759 O  O   . HOH   S 5 .   ? 12.339  20.444 -7.930  1.00 52.76  ? 607 HOH   B O   1 
HETATM 5760 O  O   . HOH   S 5 .   ? -19.163 43.964 -15.334 1.00 23.36  ? 608 HOH   B O   1 
HETATM 5761 O  O   . HOH   S 5 .   ? -12.283 29.897 -16.389 1.00 13.63  ? 609 HOH   B O   1 
HETATM 5762 O  O   . HOH   S 5 .   ? -5.225  20.591 -27.681 1.00 26.71  ? 610 HOH   B O   1 
HETATM 5763 O  O   . HOH   S 5 .   ? -14.397 40.721 -34.697 1.00 24.26  ? 611 HOH   B O   1 
HETATM 5764 O  O   . HOH   S 5 .   ? 11.147  27.196 -1.703  1.00 27.07  ? 612 HOH   B O   1 
HETATM 5765 O  O   . HOH   S 5 .   ? -0.695  20.453 11.559  1.00 21.17  ? 613 HOH   B O   1 
HETATM 5766 O  O   . HOH   S 5 .   ? -10.290 46.377 -33.068 1.00 18.63  ? 614 HOH   B O   1 
HETATM 5767 O  O   . HOH   S 5 .   ? -16.050 35.287 -19.396 1.00 15.86  ? 615 HOH   B O   1 
HETATM 5768 O  O   . HOH   S 5 .   ? 2.770   32.249 2.634   1.00 34.95  ? 616 HOH   B O   1 
HETATM 5769 O  O   . HOH   S 5 .   ? 13.226  27.950 -18.523 1.00 26.54  ? 617 HOH   B O   1 
HETATM 5770 O  O   . HOH   S 5 .   ? -10.076 51.171 -36.475 1.00 37.28  ? 618 HOH   B O   1 
HETATM 5771 O  O   . HOH   S 5 .   ? -23.699 42.713 -25.481 1.00 23.17  ? 619 HOH   B O   1 
HETATM 5772 O  O   . HOH   S 5 .   ? -23.207 26.054 -12.890 1.00 39.67  ? 620 HOH   B O   1 
HETATM 5773 O  O   . HOH   S 5 .   ? 2.534   35.907 -23.925 1.00 17.05  ? 621 HOH   B O   1 
HETATM 5774 O  O   . HOH   S 5 .   ? -1.635  42.913 11.399  1.00 30.66  ? 622 HOH   B O   1 
HETATM 5775 O  O   . HOH   S 5 .   ? -17.712 41.898 -2.963  1.00 36.30  ? 623 HOH   B O   1 
HETATM 5776 O  O   . HOH   S 5 .   ? 10.852  45.786 -17.899 1.00 35.66  ? 624 HOH   B O   1 
HETATM 5777 O  O   . HOH   S 5 .   ? -22.942 26.999 -15.525 1.00 39.10  ? 625 HOH   B O   1 
HETATM 5778 O  O   . HOH   S 5 .   ? -11.376 14.551 -8.116  1.00 30.72  ? 626 HOH   B O   1 
HETATM 5779 O  O   . HOH   S 5 .   ? -11.328 49.382 -1.120  1.00 29.87  ? 627 HOH   B O   1 
HETATM 5780 O  O   . HOH   S 5 .   ? 4.259   30.871 -29.175 1.00 33.40  ? 628 HOH   B O   1 
HETATM 5781 O  O   . HOH   S 5 .   ? -18.816 36.799 -22.083 1.00 22.15  ? 629 HOH   B O   1 
HETATM 5782 O  O   . HOH   S 5 .   ? -9.931  57.607 -18.760 1.00 32.79  ? 630 HOH   B O   1 
HETATM 5783 O  O   . HOH   S 5 .   ? 10.332  43.436 -14.481 1.00 47.31  ? 631 HOH   B O   1 
HETATM 5784 O  O   . HOH   S 5 .   ? 4.284   29.155 -22.857 1.00 16.03  ? 632 HOH   B O   1 
HETATM 5785 O  O   . HOH   S 5 .   ? -9.408  42.317 3.106   1.00 19.34  ? 633 HOH   B O   1 
HETATM 5786 O  O   . HOH   S 5 .   ? -12.938 27.363 -20.085 1.00 13.55  ? 634 HOH   B O   1 
HETATM 5787 O  O   . HOH   S 5 .   ? -11.223 18.159 -29.605 1.00 30.52  ? 635 HOH   B O   1 
HETATM 5788 O  O   . HOH   S 5 .   ? -3.519  46.408 -33.732 1.00 24.82  ? 636 HOH   B O   1 
HETATM 5789 O  O   . HOH   S 5 .   ? 12.773  45.623 -2.251  1.00 30.02  ? 637 HOH   B O   1 
HETATM 5790 O  O   A HOH   S 5 .   ? -1.882  27.199 3.153   0.53 24.19  ? 638 HOH   B O   1 
HETATM 5791 O  O   . HOH   S 5 .   ? 10.517  56.393 -3.793  1.00 37.83  ? 639 HOH   B O   1 
HETATM 5792 O  O   . HOH   S 5 .   ? -13.358 17.850 -18.314 1.00 17.67  ? 640 HOH   B O   1 
HETATM 5793 O  O   . HOH   S 5 .   ? -6.407  39.473 -31.385 1.00 22.89  ? 641 HOH   B O   1 
HETATM 5794 O  O   . HOH   S 5 .   ? 11.208  27.303 -20.841 1.00 36.89  ? 642 HOH   B O   1 
HETATM 5795 O  O   . HOH   S 5 .   ? -20.937 36.624 -23.730 1.00 30.18  ? 643 HOH   B O   1 
HETATM 5796 O  O   . HOH   S 5 .   ? -3.250  15.138 -12.083 1.00 23.50  ? 644 HOH   B O   1 
HETATM 5797 O  O   . HOH   S 5 .   ? -1.497  35.145 -14.863 1.00 12.80  ? 645 HOH   B O   1 
HETATM 5798 O  O   . HOH   S 5 .   ? 3.235   46.735 -16.144 1.00 23.40  ? 646 HOH   B O   1 
HETATM 5799 O  O   . HOH   S 5 .   ? -17.455 41.588 -14.870 1.00 18.41  ? 647 HOH   B O   1 
HETATM 5800 O  O   . HOH   S 5 .   ? 9.624   25.575 -21.579 1.00 28.05  ? 648 HOH   B O   1 
HETATM 5801 O  O   . HOH   S 5 .   ? 15.105  30.711 -5.779  1.00 34.12  ? 649 HOH   B O   1 
HETATM 5802 O  O   . HOH   S 5 .   ? -14.928 22.236 -24.602 1.00 22.74  ? 650 HOH   B O   1 
HETATM 5803 O  O   . HOH   S 5 .   ? -22.795 12.902 -12.541 1.00 35.10  ? 651 HOH   B O   1 
HETATM 5804 O  O   . HOH   S 5 .   ? -16.026 50.012 -7.760  1.00 37.52  ? 652 HOH   B O   1 
HETATM 5805 O  O   . HOH   S 5 .   ? -1.263  22.253 -32.498 1.00 25.06  ? 653 HOH   B O   1 
HETATM 5806 O  O   . HOH   S 5 .   ? 10.082  51.251 7.977   1.00 31.42  ? 654 HOH   B O   1 
HETATM 5807 O  O   . HOH   S 5 .   ? -27.722 22.398 -1.227  1.00 47.95  ? 655 HOH   B O   1 
HETATM 5808 O  O   . HOH   S 5 .   ? -1.674  27.611 -4.730  1.00 28.52  ? 656 HOH   B O   1 
HETATM 5809 O  O   . HOH   S 5 .   ? -6.913  11.422 -17.191 1.00 32.96  ? 657 HOH   B O   1 
HETATM 5810 O  O   . HOH   S 5 .   ? -16.151 42.026 5.228   1.00 44.25  ? 658 HOH   B O   1 
HETATM 5811 O  O   . HOH   S 5 .   ? -20.550 40.737 0.062   1.00 36.28  ? 659 HOH   B O   1 
HETATM 5812 O  O   . HOH   S 5 .   ? -25.207 45.068 -18.288 1.00 34.66  ? 660 HOH   B O   1 
HETATM 5813 O  O   . HOH   S 5 .   ? 7.572   42.125 -10.624 1.00 29.37  ? 661 HOH   B O   1 
HETATM 5814 O  O   . HOH   S 5 .   ? -17.302 45.557 -8.356  1.00 18.18  ? 662 HOH   B O   1 
HETATM 5815 O  O   . HOH   S 5 .   ? 12.727  21.150 -12.636 1.00 34.35  ? 663 HOH   B O   1 
HETATM 5816 O  O   . HOH   S 5 .   ? -25.899 42.731 -16.824 1.00 28.24  ? 664 HOH   B O   1 
HETATM 5817 O  O   . HOH   S 5 .   ? -9.736  43.581 10.414  1.00 38.66  ? 665 HOH   B O   1 
HETATM 5818 O  O   . HOH   S 5 .   ? -16.862 52.580 -7.207  1.00 30.36  ? 666 HOH   B O   1 
HETATM 5819 O  O   . HOH   S 5 .   ? 16.313  50.529 1.938   1.00 38.64  ? 667 HOH   B O   1 
HETATM 5820 O  O   . HOH   S 5 .   ? -4.993  20.228 6.147   1.00 43.04  ? 668 HOH   B O   1 
HETATM 5821 O  O   . HOH   S 5 .   ? -19.178 38.131 -28.808 1.00 22.45  ? 669 HOH   B O   1 
HETATM 5822 O  O   . HOH   S 5 .   ? -7.041  48.490 -10.906 1.00 20.45  ? 670 HOH   B O   1 
HETATM 5823 O  O   . HOH   S 5 .   ? -9.036  14.830 -9.413  1.00 41.03  ? 671 HOH   B O   1 
HETATM 5824 O  O   . HOH   S 5 .   ? -9.470  11.066 -16.925 1.00 39.76  ? 672 HOH   B O   1 
HETATM 5825 O  O   . HOH   S 5 .   ? -14.527 38.248 -2.835  1.00 20.44  ? 673 HOH   B O   1 
HETATM 5826 O  O   . HOH   S 5 .   ? 1.738   50.143 -24.692 1.00 35.00  ? 674 HOH   B O   1 
HETATM 5827 O  O   . HOH   S 5 .   ? -0.014  24.784 -0.569  1.00 28.70  ? 675 HOH   B O   1 
HETATM 5828 O  O   . HOH   S 5 .   ? 2.292   28.544 -0.366  1.00 27.98  ? 676 HOH   B O   1 
HETATM 5829 O  O   . HOH   S 5 .   ? -19.955 20.746 -2.424  1.00 41.49  ? 677 HOH   B O   1 
HETATM 5830 O  O   . HOH   S 5 .   ? 13.368  33.344 -21.733 1.00 45.17  ? 678 HOH   B O   1 
HETATM 5831 O  O   . HOH   S 5 .   ? -5.973  52.051 -0.092  1.00 27.72  ? 679 HOH   B O   1 
HETATM 5832 O  O   . HOH   S 5 .   ? 15.396  33.570 -15.280 1.00 47.95  ? 680 HOH   B O   1 
HETATM 5833 O  O   . HOH   S 5 .   ? -19.731 37.367 -12.517 1.00 25.15  ? 681 HOH   B O   1 
HETATM 5834 O  O   . HOH   S 5 .   ? 1.542   31.113 5.104   1.00 33.55  ? 682 HOH   B O   1 
HETATM 5835 O  O   . HOH   S 5 .   ? -19.118 34.910 -12.755 1.00 25.20  ? 683 HOH   B O   1 
HETATM 5836 O  O   . HOH   S 5 .   ? -19.758 36.389 12.969  1.00 36.66  ? 684 HOH   B O   1 
HETATM 5837 O  O   . HOH   S 5 .   ? 2.324   37.625 -25.749 1.00 23.96  ? 685 HOH   B O   1 
HETATM 5838 O  O   . HOH   S 5 .   ? -22.071 36.719 -13.869 1.00 24.38  ? 686 HOH   B O   1 
HETATM 5839 O  O   . HOH   S 5 .   ? 17.447  43.279 8.643   1.00 46.43  ? 687 HOH   B O   1 
HETATM 5840 O  O   . HOH   S 5 .   ? 1.665   51.530 -20.348 1.00 39.45  ? 688 HOH   B O   1 
HETATM 5841 O  O   . HOH   S 5 .   ? 12.341  49.537 11.547  1.00 37.76  ? 689 HOH   B O   1 
HETATM 5842 O  O   . HOH   S 5 .   ? 1.458   41.886 -25.178 1.00 36.97  ? 690 HOH   B O   1 
HETATM 5843 O  O   . HOH   S 5 .   ? -20.815 24.064 0.339   1.00 38.53  ? 691 HOH   B O   1 
HETATM 5844 O  O   . HOH   S 5 .   ? 0.899   20.663 -32.323 1.00 43.47  ? 692 HOH   B O   1 
HETATM 5845 O  O   . HOH   S 5 .   ? -4.298  32.561 -34.044 1.00 26.99  ? 693 HOH   B O   1 
HETATM 5846 O  O   . HOH   S 5 .   ? -17.866 37.239 -5.780  1.00 28.08  ? 694 HOH   B O   1 
HETATM 5847 O  O   . HOH   S 5 .   ? 4.446   29.579 0.085   1.00 19.39  ? 695 HOH   B O   1 
HETATM 5848 O  O   . HOH   S 5 .   ? -6.866  15.945 2.842   1.00 44.74  ? 696 HOH   B O   1 
HETATM 5849 O  O   . HOH   S 5 .   ? -4.991  32.707 9.095   1.00 39.61  ? 697 HOH   B O   1 
HETATM 5850 O  O   . HOH   S 5 .   ? -9.181  45.021 2.236   1.00 21.18  ? 698 HOH   B O   1 
HETATM 5851 O  O   . HOH   S 5 .   ? -28.903 17.790 -9.184  1.00 37.46  ? 699 HOH   B O   1 
HETATM 5852 O  O   . HOH   S 5 .   ? 13.432  44.543 -6.812  1.00 39.90  ? 700 HOH   B O   1 
HETATM 5853 O  O   . HOH   S 5 .   ? 5.463   30.643 2.415   1.00 29.82  ? 701 HOH   B O   1 
HETATM 5854 O  O   . HOH   S 5 .   ? 6.037   38.807 -26.393 1.00 38.63  ? 702 HOH   B O   1 
HETATM 5855 O  O   . HOH   S 5 .   ? 12.504  49.221 -5.547  1.00 40.64  ? 703 HOH   B O   1 
HETATM 5856 O  O   . HOH   S 5 .   ? 4.682   34.697 -31.709 1.00 38.30  ? 704 HOH   B O   1 
HETATM 5857 O  O   . HOH   S 5 .   ? 2.604   61.788 -3.193  1.00 40.08  ? 705 HOH   B O   1 
HETATM 5858 O  O   . HOH   S 5 .   ? -18.815 51.759 -22.443 1.00 25.58  ? 706 HOH   B O   1 
HETATM 5859 O  O   . HOH   S 5 .   ? -15.634 38.781 -5.194  1.00 23.55  ? 707 HOH   B O   1 
HETATM 5860 O  O   . HOH   S 5 .   ? 7.356   59.984 -9.522  1.00 57.59  ? 708 HOH   B O   1 
HETATM 5861 O  O   . HOH   S 5 .   ? 10.735  21.312 -21.815 1.00 45.60  ? 709 HOH   B O   1 
HETATM 5862 O  O   . HOH   S 5 .   ? 0.010   55.193 -24.703 1.00 44.50  ? 710 HOH   B O   1 
HETATM 5863 O  O   . HOH   S 5 .   ? -2.791  16.523 -26.416 1.00 35.39  ? 711 HOH   B O   1 
HETATM 5864 O  O   . HOH   S 5 .   ? 12.667  26.435 -3.615  1.00 38.96  ? 712 HOH   B O   1 
HETATM 5865 O  O   . HOH   S 5 .   ? -18.969 27.046 -22.603 1.00 43.33  ? 713 HOH   B O   1 
HETATM 5866 O  O   . HOH   S 5 .   ? 10.570  53.809 -8.433  1.00 47.60  ? 714 HOH   B O   1 
HETATM 5867 O  O   . HOH   S 5 .   ? -16.978 24.933 -27.843 1.00 27.72  ? 715 HOH   B O   1 
HETATM 5868 O  O   . HOH   S 5 .   ? 16.191  31.144 -8.306  1.00 29.63  ? 716 HOH   B O   1 
HETATM 5869 O  O   . HOH   S 5 .   ? -16.008 28.248 -30.584 1.00 30.47  ? 717 HOH   B O   1 
HETATM 5870 O  O   . HOH   S 5 .   ? -16.659 26.471 -23.749 1.00 31.47  ? 718 HOH   B O   1 
HETATM 5871 O  O   . HOH   S 5 .   ? 4.637   62.257 -7.069  1.00 36.42  ? 719 HOH   B O   1 
HETATM 5872 O  O   . HOH   S 5 .   ? 3.606   42.508 12.134  1.00 39.74  ? 720 HOH   B O   1 
HETATM 5873 O  O   . HOH   S 5 .   ? 9.133   37.987 8.074   1.00 39.67  ? 721 HOH   B O   1 
HETATM 5874 O  O   . HOH   S 5 .   ? -6.989  21.814 4.670   1.00 54.37  ? 722 HOH   B O   1 
HETATM 5875 O  O   . HOH   S 5 .   ? -18.081 32.788 -34.609 1.00 41.51  ? 723 HOH   B O   1 
HETATM 5876 O  O   . HOH   S 5 .   ? 13.711  53.402 -0.799  1.00 44.55  ? 724 HOH   B O   1 
HETATM 5877 O  O   . HOH   S 5 .   ? -0.100  23.320 -35.051 1.00 21.91  ? 725 HOH   B O   1 
HETATM 5878 O  O   . HOH   S 5 .   ? 3.230   37.873 -28.431 1.00 28.09  ? 726 HOH   B O   1 
HETATM 5879 O  O   . HOH   S 5 .   ? -16.280 24.155 -24.932 1.00 29.06  ? 727 HOH   B O   1 
HETATM 5880 O  O   . HOH   S 5 .   ? 7.864   42.765 11.230  1.00 32.62  ? 728 HOH   B O   1 
HETATM 5881 O  O   . HOH   S 5 .   ? -17.854 34.342 -21.070 1.00 25.68  ? 729 HOH   B O   1 
HETATM 5882 O  O   . HOH   S 5 .   ? -11.230 46.736 -0.193  1.00 29.37  ? 730 HOH   B O   1 
HETATM 5883 O  O   . HOH   S 5 .   ? 8.723   27.293 -23.282 1.00 46.81  ? 731 HOH   B O   1 
HETATM 5884 O  O   . HOH   S 5 .   ? 2.290   48.312 -18.069 1.00 32.03  ? 732 HOH   B O   1 
HETATM 5885 O  O   . HOH   S 5 .   ? 2.801   40.302 -28.897 1.00 38.66  ? 733 HOH   B O   1 
HETATM 5886 O  O   . HOH   S 5 .   ? 5.593   62.521 -4.427  1.00 39.05  ? 734 HOH   B O   1 
HETATM 5887 O  O   . HOH   S 5 .   ? 9.756   44.224 11.167  1.00 32.12  ? 735 HOH   B O   1 
HETATM 5888 O  O   . HOH   S 5 .   ? -19.447 48.953 -10.692 1.00 39.66  ? 736 HOH   B O   1 
HETATM 5889 O  O   . HOH   S 5 .   ? 11.368  41.095 -0.244  1.00 25.41  ? 737 HOH   B O   1 
HETATM 5890 O  O   . HOH   S 5 .   ? -4.554  17.759 -27.518 1.00 37.07  ? 738 HOH   B O   1 
HETATM 5891 O  O   . HOH   S 5 .   ? -7.923  59.120 -22.338 1.00 43.93  ? 739 HOH   B O   1 
HETATM 5892 O  O   . HOH   S 5 .   ? 10.018  27.963 -25.614 1.00 31.37  ? 740 HOH   B O   1 
HETATM 5893 O  O   . HOH   S 5 .   ? -18.945 44.774 -6.547  1.00 32.87  ? 741 HOH   B O   1 
HETATM 5894 O  O   . HOH   S 5 .   ? -26.941 40.693 5.791   1.00 39.80  ? 742 HOH   B O   1 
HETATM 5895 O  O   . HOH   S 5 .   ? -7.017  47.848 -36.041 1.00 40.04  ? 743 HOH   B O   1 
HETATM 5896 O  O   . HOH   S 5 .   ? -18.207 48.192 -8.789  1.00 32.82  ? 744 HOH   B O   1 
HETATM 5897 O  O   . HOH   S 5 .   ? 0.720   44.047 12.453  1.00 59.36  ? 745 HOH   B O   1 
HETATM 5898 O  O   . HOH   S 5 .   ? -15.919 20.758 -26.564 1.00 33.82  ? 746 HOH   B O   1 
HETATM 5899 O  O   . HOH   S 5 .   ? -11.328 46.883 2.579   1.00 37.40  ? 747 HOH   B O   1 
HETATM 5900 O  O   . HOH   S 5 .   ? -22.023 48.483 -10.411 1.00 36.22  ? 748 HOH   B O   1 
HETATM 5901 O  O   . HOH   S 5 .   ? -7.612  60.638 -11.538 1.00 35.76  ? 749 HOH   B O   1 
HETATM 5902 O  O   . HOH   S 5 .   ? -22.940 29.222 -16.707 1.00 44.25  ? 750 HOH   B O   1 
HETATM 5903 O  O   . HOH   S 5 .   ? -17.057 21.984 -28.535 1.00 33.46  ? 751 HOH   B O   1 
HETATM 5904 O  O   . HOH   S 5 .   ? -15.834 21.383 -30.598 1.00 44.04  ? 752 HOH   B O   1 
HETATM 5905 O  O   . HOH   S 5 .   ? -18.970 22.864 -24.312 1.00 37.65  ? 753 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   . GLN A 9   ? 0.5186 0.4597 0.3941 -0.0260 -0.0008 -0.0141 6   GLN A N   
2    C CA  . GLN A 9   ? 0.5166 0.4626 0.4024 -0.0229 -0.0027 -0.0152 6   GLN A CA  
3    C C   . GLN A 9   ? 0.4605 0.4042 0.3508 -0.0279 -0.0054 -0.0110 6   GLN A C   
4    O O   . GLN A 9   ? 0.4312 0.3648 0.3183 -0.0287 -0.0094 -0.0091 6   GLN A O   
5    C CB  . GLN A 9   ? 0.5863 0.5245 0.4702 -0.0163 -0.0064 -0.0185 6   GLN A CB  
6    C CG  . GLN A 9   ? 0.6539 0.5951 0.5343 -0.0100 -0.0034 -0.0238 6   GLN A CG  
7    C CD  . GLN A 9   ? 0.7207 0.6792 0.6095 -0.0078 0.0017  -0.0258 6   GLN A CD  
8    O OE1 . GLN A 9   ? 0.7864 0.7526 0.6851 -0.0054 0.0006  -0.0260 6   GLN A OE1 
9    N NE2 . GLN A 9   ? 0.7365 0.7022 0.6214 -0.0086 0.0074  -0.0274 6   GLN A NE2 
10   N N   . CYS A 10  ? 0.4457 0.3991 0.3425 -0.0317 -0.0027 -0.0097 7   CYS A N   
11   C CA  A CYS A 10  ? 0.4336 0.3852 0.3336 -0.0373 -0.0041 -0.0061 7   CYS A CA  
12   C CA  B CYS A 10  ? 0.4335 0.3845 0.3335 -0.0369 -0.0046 -0.0062 7   CYS A CA  
13   C C   . CYS A 10  ? 0.4273 0.3894 0.3378 -0.0371 -0.0046 -0.0073 7   CYS A C   
14   O O   . CYS A 10  ? 0.4340 0.4069 0.3496 -0.0336 -0.0026 -0.0103 7   CYS A O   
15   C CB  A CYS A 10  ? 0.4328 0.3846 0.3286 -0.0438 -0.0004 -0.0031 7   CYS A CB  
16   C CB  B CYS A 10  ? 0.4338 0.3826 0.3289 -0.0433 -0.0017 -0.0028 7   CYS A CB  
17   S SG  A CYS A 10  ? 0.4327 0.3710 0.3156 -0.0448 -0.0015 -0.0002 7   CYS A SG  
18   S SG  B CYS A 10  ? 0.4531 0.4160 0.3505 -0.0466 0.0052  -0.0038 7   CYS A SG  
19   N N   . VAL A 11  ? 0.4009 0.3603 0.3142 -0.0407 -0.0070 -0.0052 8   VAL A N   
20   C CA  . VAL A 11  ? 0.4057 0.3749 0.3281 -0.0419 -0.0078 -0.0062 8   VAL A CA  
21   C C   . VAL A 11  ? 0.3951 0.3640 0.3174 -0.0501 -0.0059 -0.0038 8   VAL A C   
22   O O   . VAL A 11  ? 0.3865 0.3438 0.3014 -0.0528 -0.0060 -0.0010 8   VAL A O   
23   C CB  . VAL A 11  ? 0.4166 0.3815 0.3409 -0.0383 -0.0130 -0.0064 8   VAL A CB  
24   C CG1 . VAL A 11  ? 0.4500 0.4132 0.3732 -0.0306 -0.0147 -0.0084 8   VAL A CG1 
25   C CG2 . VAL A 11  ? 0.4139 0.3660 0.3326 -0.0406 -0.0155 -0.0036 8   VAL A CG2 
26   N N   . LYS A 12  ? 0.3930 0.3743 0.3229 -0.0536 -0.0042 -0.0050 9   LYS A N   
27   C CA  . LYS A 12  ? 0.4117 0.3925 0.3419 -0.0623 -0.0026 -0.0031 9   LYS A CA  
28   C C   . LYS A 12  ? 0.3862 0.3608 0.3173 -0.0634 -0.0072 -0.0030 9   LYS A C   
29   O O   . LYS A 12  ? 0.3920 0.3744 0.3297 -0.0603 -0.0102 -0.0053 9   LYS A O   
30   C CB  . LYS A 12  ? 0.4397 0.4378 0.3782 -0.0666 0.0012  -0.0048 9   LYS A CB  
31   C CG  . LYS A 12  ? 0.4840 0.4798 0.4205 -0.0769 0.0040  -0.0024 9   LYS A CG  
32   C CD  . LYS A 12  ? 0.5270 0.5418 0.4734 -0.0822 0.0074  -0.0041 9   LYS A CD  
33   C CE  . LYS A 12  ? 0.5686 0.5797 0.5115 -0.0935 0.0110  -0.0012 9   LYS A CE  
34   N NZ  . LYS A 12  ? 0.6114 0.6423 0.5661 -0.1000 0.0130  -0.0033 9   LYS A NZ  
35   N N   . LEU A 13  ? 0.3693 0.3300 0.2933 -0.0668 -0.0078 -0.0004 10  LEU A N   
36   C CA  . LEU A 13  ? 0.3521 0.3059 0.2756 -0.0677 -0.0116 -0.0006 10  LEU A CA  
37   C C   . LEU A 13  ? 0.3602 0.3196 0.2881 -0.0753 -0.0110 -0.0017 10  LEU A C   
38   O O   . LEU A 13  ? 0.3717 0.3383 0.3019 -0.0808 -0.0071 -0.0013 10  LEU A O   
39   C CB  . LEU A 13  ? 0.3500 0.2875 0.2646 -0.0673 -0.0122 0.0021  10  LEU A CB  
40   C CG  . LEU A 13  ? 0.3419 0.2742 0.2521 -0.0611 -0.0130 0.0033  10  LEU A CG  
41   C CD1 . LEU A 13  ? 0.3447 0.2636 0.2475 -0.0612 -0.0136 0.0060  10  LEU A CD1 
42   C CD2 . LEU A 13  ? 0.3432 0.2782 0.2565 -0.0554 -0.0163 0.0017  10  LEU A CD2 
43   N N   . ASN A 14  ? 0.3531 0.3096 0.2816 -0.0762 -0.0145 -0.0030 11  ASN A N   
44   C CA  . ASN A 14  ? 0.3719 0.3349 0.3052 -0.0836 -0.0151 -0.0050 11  ASN A CA  
45   C C   . ASN A 14  ? 0.3905 0.3416 0.3174 -0.0917 -0.0127 -0.0031 11  ASN A C   
46   O O   . ASN A 14  ? 0.3949 0.3500 0.3250 -0.0993 -0.0129 -0.0046 11  ASN A O   
47   C CB  . ASN A 14  ? 0.3699 0.3344 0.3052 -0.0817 -0.0200 -0.0076 11  ASN A CB  
48   C CG  . ASN A 14  ? 0.3702 0.3180 0.2967 -0.0796 -0.0220 -0.0068 11  ASN A CG  
49   O OD1 . ASN A 14  ? 0.3999 0.3350 0.3198 -0.0826 -0.0202 -0.0051 11  ASN A OD1 
50   N ND2 . ASN A 14  ? 0.3506 0.2987 0.2768 -0.0743 -0.0255 -0.0080 11  ASN A ND2 
51   N N   . ASP A 15  ? 0.3866 0.3236 0.3048 -0.0904 -0.0109 0.0001  12  ASP A N   
52   C CA  . ASP A 15  ? 0.4106 0.3348 0.3214 -0.0973 -0.0083 0.0028  12  ASP A CA  
53   C C   . ASP A 15  ? 0.4242 0.3525 0.3337 -0.1000 -0.0035 0.0057  12  ASP A C   
54   O O   . ASP A 15  ? 0.4332 0.3493 0.3347 -0.1050 -0.0014 0.0090  12  ASP A O   
55   C CB  . ASP A 15  ? 0.4061 0.3112 0.3071 -0.0936 -0.0100 0.0048  12  ASP A CB  
56   C CG  . ASP A 15  ? 0.3904 0.2929 0.2881 -0.0857 -0.0099 0.0070  12  ASP A CG  
57   O OD1 . ASP A 15  ? 0.3677 0.2817 0.2697 -0.0830 -0.0086 0.0067  12  ASP A OD1 
58   O OD2 . ASP A 15  ? 0.3884 0.2777 0.2794 -0.0822 -0.0112 0.0087  12  ASP A OD2 
59   N N   . GLY A 16  ? 0.4278 0.3715 0.3436 -0.0965 -0.0019 0.0046  13  GLY A N   
60   C CA  . GLY A 16  ? 0.4428 0.3926 0.3574 -0.0989 0.0033  0.0066  13  GLY A CA  
61   C C   . GLY A 16  ? 0.4386 0.3794 0.3446 -0.0929 0.0040  0.0092  13  GLY A C   
62   O O   . GLY A 16  ? 0.4295 0.3761 0.3336 -0.0935 0.0081  0.0104  13  GLY A O   
63   N N   . HIS A 17  ? 0.4332 0.3612 0.3339 -0.0873 0.0002  0.0100  14  HIS A N   
64   C CA  . HIS A 17  ? 0.4372 0.3590 0.3312 -0.0809 -0.0002 0.0118  14  HIS A CA  
65   C C   . HIS A 17  ? 0.4241 0.3570 0.3239 -0.0740 -0.0012 0.0087  14  HIS A C   
66   O O   . HIS A 17  ? 0.4136 0.3570 0.3220 -0.0730 -0.0023 0.0056  14  HIS A O   
67   C CB  . HIS A 17  ? 0.4436 0.3499 0.3312 -0.0777 -0.0038 0.0137  14  HIS A CB  
68   C CG  . HIS A 17  ? 0.4800 0.3728 0.3600 -0.0829 -0.0029 0.0171  14  HIS A CG  
69   N ND1 . HIS A 17  ? 0.5166 0.4045 0.3888 -0.0864 0.0003  0.0209  14  HIS A ND1 
70   C CD2 . HIS A 17  ? 0.4936 0.3754 0.3713 -0.0850 -0.0047 0.0173  14  HIS A CD2 
71   C CE1 . HIS A 17  ? 0.5353 0.4091 0.4008 -0.0907 0.0002  0.0236  14  HIS A CE1 
72   N NE2 . HIS A 17  ? 0.5287 0.3982 0.3975 -0.0897 -0.0029 0.0212  14  HIS A NE2 
73   N N   . PHE A 18  ? 0.4022 0.3321 0.2964 -0.0695 -0.0010 0.0096  15  PHE A N   
74   C CA  . PHE A 18  ? 0.3945 0.3319 0.2915 -0.0632 -0.0015 0.0068  15  PHE A CA  
75   C C   . PHE A 18  ? 0.3729 0.3010 0.2658 -0.0578 -0.0056 0.0073  15  PHE A C   
76   O O   . PHE A 18  ? 0.3694 0.2878 0.2549 -0.0579 -0.0065 0.0101  15  PHE A O   
77   C CB  . PHE A 18  ? 0.4211 0.3647 0.3149 -0.0637 0.0030  0.0066  15  PHE A CB  
78   C CG  . PHE A 18  ? 0.4466 0.4039 0.3470 -0.0683 0.0074  0.0053  15  PHE A CG  
79   C CD1 . PHE A 18  ? 0.4602 0.4317 0.3702 -0.0648 0.0077  0.0013  15  PHE A CD1 
80   C CD2 . PHE A 18  ? 0.4746 0.4307 0.3721 -0.0764 0.0110  0.0083  15  PHE A CD2 
81   C CE1 . PHE A 18  ? 0.4775 0.4644 0.3953 -0.0691 0.0117  0.0000  15  PHE A CE1 
82   C CE2 . PHE A 18  ? 0.4858 0.4561 0.3905 -0.0819 0.0151  0.0072  15  PHE A CE2 
83   C CZ  . PHE A 18  ? 0.4851 0.4721 0.4006 -0.0781 0.0156  0.0029  15  PHE A CZ  
84   N N   . MET A 19  ? 0.3490 0.2808 0.2469 -0.0531 -0.0082 0.0046  16  MET A N   
85   C CA  . MET A 19  ? 0.3453 0.2698 0.2406 -0.0489 -0.0121 0.0049  16  MET A CA  
86   C C   . MET A 19  ? 0.3386 0.2654 0.2330 -0.0442 -0.0124 0.0025  16  MET A C   
87   O O   . MET A 19  ? 0.3363 0.2705 0.2356 -0.0417 -0.0119 -0.0003 16  MET A O   
88   C CB  . MET A 19  ? 0.3382 0.2624 0.2386 -0.0479 -0.0151 0.0043  16  MET A CB  
89   C CG  . MET A 19  ? 0.3484 0.2666 0.2469 -0.0443 -0.0186 0.0047  16  MET A CG  
90   S SD  . MET A 19  ? 0.3635 0.2829 0.2670 -0.0429 -0.0216 0.0039  16  MET A SD  
91   C CE  . MET A 19  ? 0.3492 0.2628 0.2508 -0.0462 -0.0214 0.0059  16  MET A CE  
92   N N   . PRO A 20  ? 0.3380 0.2584 0.2256 -0.0427 -0.0136 0.0031  17  PRO A N   
93   C CA  . PRO A 20  ? 0.3365 0.2568 0.2224 -0.0385 -0.0146 0.0002  17  PRO A CA  
94   C C   . PRO A 20  ? 0.3220 0.2408 0.2123 -0.0354 -0.0180 -0.0010 17  PRO A C   
95   O O   . PRO A 20  ? 0.3099 0.2252 0.2017 -0.0365 -0.0204 0.0010  17  PRO A O   
96   C CB  . PRO A 20  ? 0.3433 0.2562 0.2210 -0.0387 -0.0162 0.0014  17  PRO A CB  
97   C CG  . PRO A 20  ? 0.3411 0.2524 0.2156 -0.0427 -0.0145 0.0051  17  PRO A CG  
98   C CD  . PRO A 20  ? 0.3395 0.2525 0.2207 -0.0447 -0.0144 0.0063  17  PRO A CD  
99   N N   . VAL A 21  ? 0.3259 0.2471 0.2175 -0.0312 -0.0180 -0.0041 18  VAL A N   
100  C CA  . VAL A 21  ? 0.3303 0.2507 0.2259 -0.0280 -0.0209 -0.0049 18  VAL A CA  
101  C C   . VAL A 21  ? 0.3292 0.2392 0.2199 -0.0273 -0.0245 -0.0044 18  VAL A C   
102  O O   . VAL A 21  ? 0.3243 0.2311 0.2168 -0.0258 -0.0272 -0.0039 18  VAL A O   
103  C CB  . VAL A 21  ? 0.3462 0.2730 0.2454 -0.0229 -0.0199 -0.0083 18  VAL A CB  
104  C CG1 . VAL A 21  ? 0.3515 0.2914 0.2575 -0.0245 -0.0165 -0.0088 18  VAL A CG1 
105  C CG2 . VAL A 21  ? 0.3546 0.2776 0.2480 -0.0189 -0.0190 -0.0115 18  VAL A CG2 
106  N N   . LEU A 22  ? 0.3288 0.2337 0.2131 -0.0285 -0.0246 -0.0045 19  LEU A N   
107  C CA  . LEU A 22  ? 0.3247 0.2209 0.2051 -0.0296 -0.0283 -0.0037 19  LEU A CA  
108  C C   . LEU A 22  ? 0.3216 0.2177 0.2014 -0.0336 -0.0290 -0.0005 19  LEU A C   
109  O O   . LEU A 22  ? 0.3216 0.2193 0.1982 -0.0348 -0.0273 0.0001  19  LEU A O   
110  C CB  . LEU A 22  ? 0.3375 0.2279 0.2109 -0.0277 -0.0290 -0.0068 19  LEU A CB  
111  C CG  . LEU A 22  ? 0.3486 0.2304 0.2176 -0.0300 -0.0329 -0.0064 19  LEU A CG  
112  C CD1 . LEU A 22  ? 0.3504 0.2275 0.2222 -0.0297 -0.0354 -0.0054 19  LEU A CD1 
113  C CD2 . LEU A 22  ? 0.3644 0.2401 0.2251 -0.0287 -0.0335 -0.0102 19  LEU A CD2 
114  N N   . GLY A 23  ? 0.3119 0.2059 0.1940 -0.0352 -0.0314 0.0017  20  GLY A N   
115  C CA  . GLY A 23  ? 0.3028 0.1978 0.1853 -0.0378 -0.0323 0.0045  20  GLY A CA  
116  C C   . GLY A 23  ? 0.3136 0.2053 0.1947 -0.0395 -0.0356 0.0052  20  GLY A C   
117  O O   . GLY A 23  ? 0.3127 0.2006 0.1938 -0.0397 -0.0373 0.0044  20  GLY A O   
118  N N   . PHE A 24  ? 0.3176 0.2108 0.1975 -0.0410 -0.0369 0.0068  21  PHE A N   
119  C CA  . PHE A 24  ? 0.3184 0.2111 0.1982 -0.0433 -0.0403 0.0075  21  PHE A CA  
120  C C   . PHE A 24  ? 0.3041 0.2014 0.1902 -0.0442 -0.0406 0.0101  21  PHE A C   
121  O O   . PHE A 24  ? 0.2955 0.1963 0.1838 -0.0428 -0.0394 0.0119  21  PHE A O   
122  C CB  . PHE A 24  ? 0.3311 0.2244 0.2063 -0.0440 -0.0423 0.0075  21  PHE A CB  
123  C CG  . PHE A 24  ? 0.3379 0.2327 0.2138 -0.0469 -0.0464 0.0079  21  PHE A CG  
124  C CD1 . PHE A 24  ? 0.3531 0.2430 0.2268 -0.0494 -0.0485 0.0057  21  PHE A CD1 
125  C CD2 . PHE A 24  ? 0.3362 0.2372 0.2153 -0.0472 -0.0483 0.0104  21  PHE A CD2 
126  C CE1 . PHE A 24  ? 0.3563 0.2481 0.2310 -0.0534 -0.0524 0.0059  21  PHE A CE1 
127  C CE2 . PHE A 24  ? 0.3451 0.2502 0.2265 -0.0503 -0.0521 0.0107  21  PHE A CE2 
128  C CZ  . PHE A 24  ? 0.3514 0.2521 0.2308 -0.0540 -0.0542 0.0085  21  PHE A CZ  
129  N N   . GLY A 25  ? 0.3125 0.2092 0.2009 -0.0463 -0.0419 0.0103  22  GLY A N   
130  C CA  . GLY A 25  ? 0.3114 0.2136 0.2055 -0.0472 -0.0416 0.0127  22  GLY A CA  
131  C C   . GLY A 25  ? 0.3109 0.2191 0.2075 -0.0491 -0.0440 0.0139  22  GLY A C   
132  O O   . GLY A 25  ? 0.3383 0.2451 0.2331 -0.0522 -0.0468 0.0131  22  GLY A O   
133  N N   . THR A 26  ? 0.3055 0.2200 0.2060 -0.0470 -0.0432 0.0156  23  THR A N   
134  C CA  . THR A 26  ? 0.3051 0.2271 0.2088 -0.0474 -0.0459 0.0168  23  THR A CA  
135  C C   . THR A 26  ? 0.3090 0.2399 0.2200 -0.0491 -0.0457 0.0182  23  THR A C   
136  O O   . THR A 26  ? 0.3189 0.2583 0.2341 -0.0498 -0.0482 0.0191  23  THR A O   
137  C CB  . THR A 26  ? 0.3012 0.2248 0.2041 -0.0430 -0.0459 0.0180  23  THR A CB  
138  O OG1 . THR A 26  ? 0.2913 0.2153 0.1967 -0.0397 -0.0428 0.0188  23  THR A OG1 
139  C CG2 . THR A 26  ? 0.3055 0.2218 0.2008 -0.0421 -0.0459 0.0171  23  THR A CG2 
140  N N   . TYR A 27  ? 0.3170 0.2473 0.2297 -0.0497 -0.0429 0.0186  24  TYR A N   
141  C CA  . TYR A 27  ? 0.3242 0.2641 0.2435 -0.0516 -0.0419 0.0201  24  TYR A CA  
142  C C   . TYR A 27  ? 0.3346 0.2774 0.2555 -0.0580 -0.0447 0.0204  24  TYR A C   
143  O O   . TYR A 27  ? 0.3363 0.2702 0.2524 -0.0618 -0.0456 0.0197  24  TYR A O   
144  C CB  . TYR A 27  ? 0.3262 0.2644 0.2453 -0.0518 -0.0384 0.0206  24  TYR A CB  
145  C CG  . TYR A 27  ? 0.3346 0.2840 0.2600 -0.0536 -0.0367 0.0221  24  TYR A CG  
146  C CD1 . TYR A 27  ? 0.3421 0.3008 0.2727 -0.0491 -0.0349 0.0223  24  TYR A CD1 
147  C CD2 . TYR A 27  ? 0.3423 0.2932 0.2686 -0.0600 -0.0370 0.0235  24  TYR A CD2 
148  C CE1 . TYR A 27  ? 0.3545 0.3255 0.2915 -0.0504 -0.0328 0.0235  24  TYR A CE1 
149  C CE2 . TYR A 27  ? 0.3510 0.3137 0.2833 -0.0626 -0.0349 0.0251  24  TYR A CE2 
150  C CZ  . TYR A 27  ? 0.3660 0.3400 0.3042 -0.0576 -0.0326 0.0250  24  TYR A CZ  
151  O OH  . TYR A 27  ? 0.3877 0.3751 0.3324 -0.0598 -0.0300 0.0264  24  TYR A OH  
152  N N   . ALA A 28  ? 0.3457 0.3012 0.2738 -0.0593 -0.0458 0.0214  25  ALA A N   
153  C CA  . ALA A 28  ? 0.3605 0.3222 0.2924 -0.0667 -0.0477 0.0221  25  ALA A CA  
154  C C   . ALA A 28  ? 0.3694 0.3462 0.3104 -0.0670 -0.0449 0.0239  25  ALA A C   
155  O O   . ALA A 28  ? 0.3755 0.3596 0.3204 -0.0606 -0.0432 0.0241  25  ALA A O   
156  C CB  . ALA A 28  ? 0.3663 0.3312 0.2986 -0.0689 -0.0528 0.0211  25  ALA A CB  
157  N N   . PRO A 29  ? 0.3941 0.3748 0.3376 -0.0744 -0.0441 0.0254  26  PRO A N   
158  C CA  . PRO A 29  ? 0.4168 0.4131 0.3689 -0.0755 -0.0407 0.0271  26  PRO A CA  
159  C C   . PRO A 29  ? 0.4308 0.4446 0.3927 -0.0723 -0.0426 0.0268  26  PRO A C   
160  O O   . PRO A 29  ? 0.4133 0.4281 0.3757 -0.0732 -0.0476 0.0259  26  PRO A O   
161  C CB  . PRO A 29  ? 0.4320 0.4283 0.3841 -0.0859 -0.0404 0.0289  26  PRO A CB  
162  C CG  . PRO A 29  ? 0.4367 0.4145 0.3792 -0.0899 -0.0441 0.0278  26  PRO A CG  
163  C CD  . PRO A 29  ? 0.4132 0.3824 0.3507 -0.0821 -0.0461 0.0253  26  PRO A CD  
164  N N   . PRO A 30  ? 0.4691 0.4984 0.4393 -0.0690 -0.0390 0.0276  27  PRO A N   
165  C CA  . PRO A 30  ? 0.4905 0.5375 0.4708 -0.0642 -0.0407 0.0273  27  PRO A CA  
166  C C   . PRO A 30  ? 0.5074 0.5670 0.4950 -0.0716 -0.0455 0.0276  27  PRO A C   
167  O O   . PRO A 30  ? 0.5369 0.6083 0.5310 -0.0673 -0.0490 0.0272  27  PRO A O   
168  C CB  . PRO A 30  ? 0.4993 0.5608 0.4869 -0.0607 -0.0349 0.0278  27  PRO A CB  
169  C CG  . PRO A 30  ? 0.4962 0.5438 0.4748 -0.0616 -0.0302 0.0281  27  PRO A CG  
170  C CD  . PRO A 30  ? 0.4867 0.5177 0.4566 -0.0694 -0.0330 0.0287  27  PRO A CD  
171  N N   . GLU A 31  ? 0.5128 0.5698 0.4991 -0.0825 -0.0460 0.0285  28  GLU A N   
172  C CA  . GLU A 31  ? 0.5139 0.5832 0.5073 -0.0914 -0.0505 0.0287  28  GLU A CA  
173  C C   . GLU A 31  ? 0.5106 0.5702 0.4979 -0.0911 -0.0575 0.0267  28  GLU A C   
174  O O   . GLU A 31  ? 0.5168 0.5880 0.5101 -0.0961 -0.0626 0.0262  28  GLU A O   
175  C CB  . GLU A 31  ? 0.5356 0.6014 0.5274 -0.1039 -0.0488 0.0303  28  GLU A CB  
176  C CG  . GLU A 31  ? 0.5454 0.6239 0.5435 -0.1060 -0.0420 0.0327  28  GLU A CG  
177  C CD  . GLU A 31  ? 0.5432 0.6111 0.5342 -0.0986 -0.0362 0.0331  28  GLU A CD  
178  O OE1 . GLU A 31  ? 0.5055 0.5516 0.4846 -0.0960 -0.0371 0.0323  28  GLU A OE1 
179  O OE2 . GLU A 31  ? 0.5386 0.6208 0.5360 -0.0955 -0.0309 0.0339  28  GLU A OE2 
180  N N   . VAL A 32  ? 0.4861 0.5257 0.4617 -0.0858 -0.0577 0.0255  29  VAL A N   
181  C CA  . VAL A 32  ? 0.4764 0.5048 0.4439 -0.0851 -0.0634 0.0235  29  VAL A CA  
182  C C   . VAL A 32  ? 0.4655 0.5030 0.4365 -0.0757 -0.0659 0.0234  29  VAL A C   
183  O O   . VAL A 32  ? 0.4552 0.4924 0.4265 -0.0669 -0.0625 0.0242  29  VAL A O   
184  C CB  . VAL A 32  ? 0.4785 0.4833 0.4326 -0.0837 -0.0618 0.0224  29  VAL A CB  
185  C CG1 . VAL A 32  ? 0.4817 0.4760 0.4269 -0.0819 -0.0667 0.0201  29  VAL A CG1 
186  C CG2 . VAL A 32  ? 0.4946 0.4890 0.4444 -0.0921 -0.0599 0.0228  29  VAL A CG2 
187  N N   . PRO A 33  ? 0.4719 0.5176 0.4451 -0.0773 -0.0723 0.0227  30  PRO A N   
188  C CA  . PRO A 33  ? 0.4764 0.5308 0.4525 -0.0681 -0.0754 0.0232  30  PRO A CA  
189  C C   . PRO A 33  ? 0.4541 0.4909 0.4188 -0.0597 -0.0738 0.0232  30  PRO A C   
190  O O   . PRO A 33  ? 0.4309 0.4508 0.3849 -0.0624 -0.0735 0.0219  30  PRO A O   
191  C CB  . PRO A 33  ? 0.4990 0.5600 0.4753 -0.0730 -0.0833 0.0220  30  PRO A CB  
192  C CG  . PRO A 33  ? 0.5122 0.5730 0.4896 -0.0860 -0.0840 0.0208  30  PRO A CG  
193  C CD  . PRO A 33  ? 0.4962 0.5424 0.4686 -0.0880 -0.0772 0.0212  30  PRO A CD  
194  N N   . ARG A 34  ? 0.4455 0.4870 0.4129 -0.0498 -0.0729 0.0246  31  ARG A N   
195  C CA  . ARG A 34  ? 0.4389 0.4644 0.3960 -0.0422 -0.0715 0.0251  31  ARG A CA  
196  C C   . ARG A 34  ? 0.4385 0.4542 0.3849 -0.0431 -0.0765 0.0245  31  ARG A C   
197  O O   . ARG A 34  ? 0.4354 0.4346 0.3710 -0.0408 -0.0743 0.0244  31  ARG A O   
198  C CB  . ARG A 34  ? 0.4449 0.4774 0.4069 -0.0317 -0.0706 0.0267  31  ARG A CB  
199  C CG  . ARG A 34  ? 0.4528 0.4937 0.4235 -0.0294 -0.0649 0.0268  31  ARG A CG  
200  C CD  . ARG A 34  ? 0.4335 0.4609 0.3985 -0.0323 -0.0589 0.0259  31  ARG A CD  
201  N NE  . ARG A 34  ? 0.4330 0.4631 0.4005 -0.0421 -0.0577 0.0252  31  ARG A NE  
202  C CZ  . ARG A 34  ? 0.4177 0.4370 0.3803 -0.0456 -0.0533 0.0247  31  ARG A CZ  
203  N NH1 . ARG A 34  ? 0.4166 0.4368 0.3803 -0.0544 -0.0526 0.0246  31  ARG A NH1 
204  N NH2 . ARG A 34  ? 0.4188 0.4258 0.3750 -0.0404 -0.0500 0.0244  31  ARG A NH2 
205  N N   . SER A 35  ? 0.4479 0.4735 0.3965 -0.0467 -0.0829 0.0241  32  SER A N   
206  C CA  . SER A 35  ? 0.4561 0.4722 0.3930 -0.0481 -0.0878 0.0231  32  SER A CA  
207  C C   . SER A 35  ? 0.4543 0.4524 0.3805 -0.0537 -0.0851 0.0206  32  SER A C   
208  O O   . SER A 35  ? 0.4549 0.4410 0.3691 -0.0524 -0.0862 0.0199  32  SER A O   
209  C CB  . SER A 35  ? 0.4731 0.5030 0.4143 -0.0527 -0.0952 0.0222  32  SER A CB  
210  O OG  . SER A 35  ? 0.4730 0.5077 0.4200 -0.0628 -0.0951 0.0202  32  SER A OG  
211  N N   . LYS A 36  ? 0.4439 0.4405 0.3738 -0.0598 -0.0817 0.0194  33  LYS A N   
212  C CA  . LYS A 36  ? 0.4562 0.4364 0.3766 -0.0647 -0.0798 0.0169  33  LYS A CA  
213  C C   . LYS A 36  ? 0.4258 0.3923 0.3382 -0.0587 -0.0751 0.0173  33  LYS A C   
214  O O   . LYS A 36  ? 0.4191 0.3733 0.3211 -0.0596 -0.0752 0.0152  33  LYS A O   
215  C CB  . LYS A 36  ? 0.4787 0.4604 0.4049 -0.0721 -0.0777 0.0164  33  LYS A CB  
216  C CG  . LYS A 36  ? 0.5287 0.5150 0.4562 -0.0813 -0.0829 0.0145  33  LYS A CG  
217  C CD  . LYS A 36  ? 0.5555 0.5235 0.4703 -0.0853 -0.0842 0.0112  33  LYS A CD  
218  C CE  . LYS A 36  ? 0.5988 0.5682 0.5123 -0.0945 -0.0902 0.0086  33  LYS A CE  
219  N NZ  . LYS A 36  ? 0.6349 0.5853 0.5339 -0.0962 -0.0915 0.0047  33  LYS A NZ  
220  N N   . ALA A 37  ? 0.4097 0.3786 0.3267 -0.0529 -0.0710 0.0195  34  ALA A N   
221  C CA  . ALA A 37  ? 0.4104 0.3668 0.3206 -0.0485 -0.0664 0.0197  34  ALA A CA  
222  C C   . ALA A 37  ? 0.4071 0.3568 0.3075 -0.0452 -0.0685 0.0200  34  ALA A C   
223  O O   . ALA A 37  ? 0.3803 0.3185 0.2726 -0.0447 -0.0656 0.0190  34  ALA A O   
224  C CB  . ALA A 37  ? 0.4074 0.3675 0.3237 -0.0433 -0.0625 0.0216  34  ALA A CB  
225  N N   . LEU A 38  ? 0.4239 0.3814 0.3250 -0.0427 -0.0732 0.0215  35  LEU A N   
226  C CA  . LEU A 38  ? 0.4313 0.3825 0.3215 -0.0400 -0.0758 0.0223  35  LEU A CA  
227  C C   . LEU A 38  ? 0.4304 0.3751 0.3121 -0.0456 -0.0776 0.0190  35  LEU A C   
228  O O   . LEU A 38  ? 0.4188 0.3527 0.2907 -0.0450 -0.0751 0.0181  35  LEU A O   
229  C CB  . LEU A 38  ? 0.4537 0.4153 0.3466 -0.0357 -0.0813 0.0250  35  LEU A CB  
230  C CG  . LEU A 38  ? 0.4704 0.4277 0.3514 -0.0346 -0.0859 0.0257  35  LEU A CG  
231  C CD1 . LEU A 38  ? 0.4763 0.4192 0.3456 -0.0314 -0.0819 0.0273  35  LEU A CD1 
232  C CD2 . LEU A 38  ? 0.4951 0.4643 0.3800 -0.0300 -0.0922 0.0284  35  LEU A CD2 
233  N N   . GLU A 39  ? 0.4367 0.3877 0.3222 -0.0513 -0.0815 0.0168  36  GLU A N   
234  C CA  . GLU A 39  ? 0.4636 0.4074 0.3401 -0.0567 -0.0841 0.0129  36  GLU A CA  
235  C C   . GLU A 39  ? 0.4301 0.3604 0.3009 -0.0576 -0.0786 0.0106  36  GLU A C   
236  O O   . GLU A 39  ? 0.4206 0.3415 0.2802 -0.0570 -0.0780 0.0084  36  GLU A O   
237  C CB  . GLU A 39  ? 0.5043 0.4575 0.3879 -0.0635 -0.0890 0.0113  36  GLU A CB  
238  C CG  . GLU A 39  ? 0.5617 0.5057 0.4369 -0.0701 -0.0915 0.0067  36  GLU A CG  
239  C CD  . GLU A 39  ? 0.6080 0.5601 0.4909 -0.0784 -0.0956 0.0053  36  GLU A CD  
240  O OE1 . GLU A 39  ? 0.6490 0.5950 0.5339 -0.0831 -0.0930 0.0041  36  GLU A OE1 
241  O OE2 . GLU A 39  ? 0.6797 0.6447 0.5671 -0.0801 -0.1015 0.0059  36  GLU A OE2 
242  N N   . VAL A 40  ? 0.4213 0.3510 0.2994 -0.0586 -0.0746 0.0108  37  VAL A N   
243  C CA  . VAL A 40  ? 0.4060 0.3238 0.2793 -0.0598 -0.0706 0.0082  37  VAL A CA  
244  C C   . VAL A 40  ? 0.3902 0.3024 0.2594 -0.0543 -0.0656 0.0092  37  VAL A C   
245  O O   . VAL A 40  ? 0.3918 0.2949 0.2541 -0.0541 -0.0633 0.0065  37  VAL A O   
246  C CB  . VAL A 40  ? 0.4071 0.3255 0.2881 -0.0633 -0.0689 0.0083  37  VAL A CB  
247  C CG1 . VAL A 40  ? 0.4231 0.3471 0.3076 -0.0701 -0.0738 0.0075  37  VAL A CG1 
248  C CG2 . VAL A 40  ? 0.3917 0.3166 0.2813 -0.0598 -0.0651 0.0116  37  VAL A CG2 
249  N N   . THR A 41  ? 0.3763 0.2934 0.2493 -0.0502 -0.0642 0.0126  38  THR A N   
250  C CA  . THR A 41  ? 0.3753 0.2868 0.2442 -0.0462 -0.0596 0.0138  38  THR A CA  
251  C C   . THR A 41  ? 0.3938 0.3000 0.2509 -0.0455 -0.0603 0.0128  38  THR A C   
252  O O   . THR A 41  ? 0.3908 0.2906 0.2424 -0.0448 -0.0563 0.0114  38  THR A O   
253  C CB  . THR A 41  ? 0.3669 0.2826 0.2415 -0.0423 -0.0580 0.0174  38  THR A CB  
254  O OG1 . THR A 41  ? 0.3519 0.2726 0.2363 -0.0428 -0.0566 0.0178  38  THR A OG1 
255  C CG2 . THR A 41  ? 0.3638 0.2725 0.2335 -0.0397 -0.0535 0.0184  38  THR A CG2 
256  N N   . LYS A 42  ? 0.4089 0.3185 0.2621 -0.0459 -0.0654 0.0134  39  LYS A N   
257  C CA  . LYS A 42  ? 0.4361 0.3407 0.2765 -0.0458 -0.0666 0.0121  39  LYS A CA  
258  C C   . LYS A 42  ? 0.4331 0.3313 0.2679 -0.0488 -0.0658 0.0069  39  LYS A C   
259  O O   . LYS A 42  ? 0.4378 0.3301 0.2637 -0.0476 -0.0625 0.0053  39  LYS A O   
260  C CB  . LYS A 42  ? 0.4696 0.3801 0.3072 -0.0459 -0.0733 0.0134  39  LYS A CB  
261  C CG  . LYS A 42  ? 0.4764 0.3913 0.3166 -0.0413 -0.0743 0.0187  39  LYS A CG  
262  C CD  . LYS A 42  ? 0.5137 0.4324 0.3472 -0.0402 -0.0808 0.0203  39  LYS A CD  
263  C CE  . LYS A 42  ? 0.5412 0.4706 0.3821 -0.0432 -0.0874 0.0186  39  LYS A CE  
264  N NZ  . LYS A 42  ? 0.5821 0.5160 0.4158 -0.0420 -0.0944 0.0199  39  LYS A NZ  
265  N N   . LEU A 43  ? 0.4274 0.3264 0.2670 -0.0526 -0.0685 0.0043  40  LEU A N   
266  C CA  . LEU A 43  ? 0.4481 0.3384 0.2817 -0.0549 -0.0680 -0.0009 40  LEU A CA  
267  C C   . LEU A 43  ? 0.4264 0.3114 0.2608 -0.0519 -0.0615 -0.0016 40  LEU A C   
268  O O   . LEU A 43  ? 0.4317 0.3100 0.2579 -0.0507 -0.0594 -0.0052 40  LEU A O   
269  C CB  . LEU A 43  ? 0.4625 0.3532 0.3017 -0.0601 -0.0718 -0.0025 40  LEU A CB  
270  C CG  . LEU A 43  ? 0.4931 0.3891 0.3310 -0.0643 -0.0788 -0.0032 40  LEU A CG  
271  C CD1 . LEU A 43  ? 0.5002 0.3982 0.3460 -0.0705 -0.0816 -0.0039 40  LEU A CD1 
272  C CD2 . LEU A 43  ? 0.5239 0.4126 0.3475 -0.0650 -0.0814 -0.0076 40  LEU A CD2 
273  N N   . ALA A 44  ? 0.3928 0.2812 0.2368 -0.0507 -0.0586 0.0013  41  ALA A N   
274  C CA  . ALA A 44  ? 0.3767 0.2618 0.2226 -0.0481 -0.0531 0.0007  41  ALA A CA  
275  C C   . ALA A 44  ? 0.3820 0.2660 0.2208 -0.0453 -0.0494 0.0006  41  ALA A C   
276  O O   . ALA A 44  ? 0.3783 0.2585 0.2133 -0.0436 -0.0460 -0.0026 41  ALA A O   
277  C CB  . ALA A 44  ? 0.3586 0.2481 0.2148 -0.0476 -0.0512 0.0039  41  ALA A CB  
278  N N   . ILE A 45  ? 0.3910 0.2784 0.2277 -0.0446 -0.0499 0.0040  42  ILE A N   
279  C CA  . ILE A 45  ? 0.4052 0.2914 0.2343 -0.0429 -0.0462 0.0049  42  ILE A CA  
280  C C   . ILE A 45  ? 0.4300 0.3124 0.2476 -0.0431 -0.0466 0.0009  42  ILE A C   
281  O O   . ILE A 45  ? 0.4370 0.3180 0.2499 -0.0417 -0.0419 -0.0009 42  ILE A O   
282  C CB  . ILE A 45  ? 0.4092 0.2978 0.2373 -0.0421 -0.0473 0.0101  42  ILE A CB  
283  C CG1 . ILE A 45  ? 0.3986 0.2895 0.2370 -0.0413 -0.0455 0.0130  42  ILE A CG1 
284  C CG2 . ILE A 45  ? 0.4307 0.3168 0.2484 -0.0415 -0.0441 0.0115  42  ILE A CG2 
285  C CD1 . ILE A 45  ? 0.4078 0.2997 0.2466 -0.0396 -0.0474 0.0178  42  ILE A CD1 
286  N N   . GLU A 46  ? 0.4519 0.3332 0.2650 -0.0449 -0.0521 -0.0007 43  GLU A N   
287  C CA  . GLU A 46  ? 0.4960 0.3724 0.2970 -0.0452 -0.0531 -0.0055 43  GLU A CA  
288  C C   . GLU A 46  ? 0.4858 0.3570 0.2867 -0.0439 -0.0497 -0.0106 43  GLU A C   
289  O O   . GLU A 46  ? 0.5157 0.3844 0.3075 -0.0419 -0.0465 -0.0138 43  GLU A O   
290  C CB  . GLU A 46  ? 0.5331 0.4092 0.3309 -0.0483 -0.0604 -0.0069 43  GLU A CB  
291  C CG  . GLU A 46  ? 0.5768 0.4582 0.3718 -0.0482 -0.0640 -0.0024 43  GLU A CG  
292  C CD  . GLU A 46  ? 0.6390 0.5239 0.4344 -0.0514 -0.0721 -0.0028 43  GLU A CD  
293  O OE1 . GLU A 46  ? 0.6916 0.5726 0.4848 -0.0547 -0.0752 -0.0079 43  GLU A OE1 
294  O OE2 . GLU A 46  ? 0.6966 0.5880 0.4939 -0.0504 -0.0755 0.0018  43  GLU A OE2 
295  N N   . ALA A 47  ? 0.4583 0.3281 0.2684 -0.0445 -0.0504 -0.0112 44  ALA A N   
296  C CA  . ALA A 47  ? 0.4598 0.3234 0.2700 -0.0427 -0.0482 -0.0158 44  ALA A CA  
297  C C   . ALA A 47  ? 0.4514 0.3183 0.2644 -0.0386 -0.0416 -0.0156 44  ALA A C   
298  O O   . ALA A 47  ? 0.4745 0.3374 0.2855 -0.0355 -0.0392 -0.0199 44  ALA A O   
299  C CB  . ALA A 47  ? 0.4480 0.3092 0.2668 -0.0449 -0.0510 -0.0151 44  ALA A CB  
300  N N   . GLY A 48  ? 0.4363 0.3103 0.2545 -0.0387 -0.0389 -0.0108 45  GLY A N   
301  C CA  . GLY A 48  ? 0.4200 0.2987 0.2412 -0.0363 -0.0327 -0.0103 45  GLY A CA  
302  C C   . GLY A 48  ? 0.3887 0.2717 0.2217 -0.0365 -0.0315 -0.0068 45  GLY A C   
303  O O   . GLY A 48  ? 0.3779 0.2656 0.2146 -0.0351 -0.0268 -0.0066 45  GLY A O   
304  N N   . PHE A 49  ? 0.3717 0.2542 0.2104 -0.0385 -0.0353 -0.0042 46  PHE A N   
305  C CA  . PHE A 49  ? 0.3569 0.2434 0.2054 -0.0387 -0.0340 -0.0009 46  PHE A CA  
306  C C   . PHE A 49  ? 0.3591 0.2489 0.2065 -0.0395 -0.0316 0.0029  46  PHE A C   
307  O O   . PHE A 49  ? 0.3582 0.2469 0.1989 -0.0403 -0.0333 0.0045  46  PHE A O   
308  C CB  . PHE A 49  ? 0.3494 0.2355 0.2034 -0.0406 -0.0381 0.0010  46  PHE A CB  
309  C CG  . PHE A 49  ? 0.3459 0.2278 0.2022 -0.0406 -0.0397 -0.0015 46  PHE A CG  
310  C CD1 . PHE A 49  ? 0.3597 0.2359 0.2104 -0.0420 -0.0432 -0.0042 46  PHE A CD1 
311  C CD2 . PHE A 49  ? 0.3325 0.2154 0.1955 -0.0395 -0.0383 -0.0009 46  PHE A CD2 
312  C CE1 . PHE A 49  ? 0.3637 0.2340 0.2155 -0.0426 -0.0448 -0.0060 46  PHE A CE1 
313  C CE2 . PHE A 49  ? 0.3348 0.2123 0.1985 -0.0395 -0.0400 -0.0024 46  PHE A CE2 
314  C CZ  . PHE A 49  ? 0.3530 0.2235 0.2109 -0.0410 -0.0431 -0.0049 46  PHE A CZ  
315  N N   . ARG A 50  ? 0.3622 0.2552 0.2151 -0.0394 -0.0281 0.0041  47  ARG A N   
316  C CA  . ARG A 50  ? 0.3682 0.2624 0.2201 -0.0408 -0.0256 0.0078  47  ARG A CA  
317  C C   . ARG A 50  ? 0.3628 0.2578 0.2227 -0.0413 -0.0258 0.0100  47  ARG A C   
318  O O   . ARG A 50  ? 0.3902 0.2833 0.2491 -0.0422 -0.0259 0.0134  47  ARG A O   
319  C CB  . ARG A 50  ? 0.3833 0.2806 0.2324 -0.0412 -0.0204 0.0065  47  ARG A CB  
320  C CG  . ARG A 50  ? 0.4016 0.2980 0.2408 -0.0405 -0.0196 0.0044  47  ARG A CG  
321  C CD  . ARG A 50  ? 0.4222 0.3150 0.2521 -0.0421 -0.0208 0.0080  47  ARG A CD  
322  N NE  . ARG A 50  ? 0.4436 0.3352 0.2626 -0.0414 -0.0206 0.0056  47  ARG A NE  
323  C CZ  . ARG A 50  ? 0.4545 0.3429 0.2688 -0.0403 -0.0250 0.0031  47  ARG A CZ  
324  N NH1 . ARG A 50  ? 0.4437 0.3305 0.2639 -0.0401 -0.0298 0.0025  47  ARG A NH1 
325  N NH2 . ARG A 50  ? 0.4708 0.3578 0.2739 -0.0399 -0.0243 0.0007  47  ARG A NH2 
326  N N   . HIS A 51  ? 0.3502 0.2469 0.2170 -0.0405 -0.0264 0.0082  48  HIS A N   
327  C CA  . HIS A 51  ? 0.3273 0.2248 0.2010 -0.0407 -0.0269 0.0097  48  HIS A CA  
328  C C   . HIS A 51  ? 0.3160 0.2124 0.1913 -0.0403 -0.0308 0.0106  48  HIS A C   
329  O O   . HIS A 51  ? 0.3173 0.2129 0.1923 -0.0401 -0.0329 0.0087  48  HIS A O   
330  C CB  . HIS A 51  ? 0.3256 0.2263 0.2045 -0.0400 -0.0253 0.0073  48  HIS A CB  
331  C CG  . HIS A 51  ? 0.3181 0.2200 0.2031 -0.0401 -0.0258 0.0079  48  HIS A CG  
332  N ND1 . HIS A 51  ? 0.3026 0.2082 0.1919 -0.0394 -0.0246 0.0061  48  HIS A ND1 
333  C CD2 . HIS A 51  ? 0.3209 0.2215 0.2082 -0.0403 -0.0275 0.0097  48  HIS A CD2 
334  C CE1 . HIS A 51  ? 0.3090 0.2148 0.2020 -0.0397 -0.0256 0.0069  48  HIS A CE1 
335  N NE2 . HIS A 51  ? 0.3069 0.2095 0.1987 -0.0402 -0.0270 0.0090  48  HIS A NE2 
336  N N   A ILE A 52  ? 0.3152 0.2114 0.1918 -0.0402 -0.0318 0.0133  49  ILE A N   
337  N N   B ILE A 52  ? 0.3123 0.2085 0.1890 -0.0402 -0.0318 0.0133  49  ILE A N   
338  C CA  A ILE A 52  ? 0.3175 0.2153 0.1967 -0.0397 -0.0352 0.0144  49  ILE A CA  
339  C CA  B ILE A 52  ? 0.3135 0.2113 0.1927 -0.0397 -0.0352 0.0145  49  ILE A CA  
340  C C   A ILE A 52  ? 0.3084 0.2078 0.1935 -0.0389 -0.0345 0.0154  49  ILE A C   
341  C C   B ILE A 52  ? 0.3063 0.2057 0.1915 -0.0389 -0.0344 0.0154  49  ILE A C   
342  O O   A ILE A 52  ? 0.3128 0.2101 0.1973 -0.0382 -0.0328 0.0167  49  ILE A O   
343  O O   B ILE A 52  ? 0.3114 0.2087 0.1960 -0.0382 -0.0327 0.0166  49  ILE A O   
344  C CB  A ILE A 52  ? 0.3285 0.2259 0.2032 -0.0390 -0.0376 0.0165  49  ILE A CB  
345  C CB  B ILE A 52  ? 0.3211 0.2183 0.1959 -0.0388 -0.0374 0.0168  49  ILE A CB  
346  C CG1 A ILE A 52  ? 0.3347 0.2305 0.2023 -0.0399 -0.0387 0.0150  49  ILE A CG1 
347  C CG1 B ILE A 52  ? 0.3263 0.2211 0.1929 -0.0396 -0.0375 0.0160  49  ILE A CG1 
348  C CG2 A ILE A 52  ? 0.3301 0.2318 0.2094 -0.0381 -0.0410 0.0179  49  ILE A CG2 
349  C CG2 B ILE A 52  ? 0.3235 0.2252 0.2022 -0.0384 -0.0412 0.0176  49  ILE A CG2 
350  C CD1 A ILE A 52  ? 0.3494 0.2443 0.2108 -0.0391 -0.0409 0.0174  49  ILE A CD1 
351  C CD1 B ILE A 52  ? 0.3237 0.2189 0.1889 -0.0407 -0.0395 0.0130  49  ILE A CD1 
352  N N   . ASP A 53  ? 0.2961 0.1981 0.1856 -0.0394 -0.0355 0.0147  50  ASP A N   
353  C CA  . ASP A 53  ? 0.2962 0.2002 0.1905 -0.0388 -0.0343 0.0151  50  ASP A CA  
354  C C   . ASP A 53  ? 0.3028 0.2114 0.2006 -0.0378 -0.0359 0.0166  50  ASP A C   
355  O O   . ASP A 53  ? 0.3161 0.2284 0.2161 -0.0395 -0.0379 0.0167  50  ASP A O   
356  C CB  . ASP A 53  ? 0.2869 0.1910 0.1830 -0.0399 -0.0338 0.0136  50  ASP A CB  
357  C CG  . ASP A 53  ? 0.2850 0.1908 0.1843 -0.0392 -0.0324 0.0139  50  ASP A CG  
358  O OD1 . ASP A 53  ? 0.3146 0.2188 0.2134 -0.0387 -0.0307 0.0132  50  ASP A OD1 
359  O OD2 . ASP A 53  ? 0.2697 0.1787 0.1716 -0.0396 -0.0330 0.0148  50  ASP A OD2 
360  N N   . SER A 54  ? 0.2997 0.2080 0.1981 -0.0352 -0.0350 0.0177  51  SER A N   
361  C CA  . SER A 54  ? 0.3006 0.2146 0.2033 -0.0328 -0.0360 0.0189  51  SER A CA  
362  C C   . SER A 54  ? 0.2951 0.2083 0.1994 -0.0304 -0.0335 0.0184  51  SER A C   
363  O O   . SER A 54  ? 0.3030 0.2120 0.2055 -0.0316 -0.0315 0.0171  51  SER A O   
364  C CB  . SER A 54  ? 0.3059 0.2199 0.2065 -0.0305 -0.0384 0.0206  51  SER A CB  
365  O OG  . SER A 54  ? 0.3200 0.2416 0.2257 -0.0275 -0.0398 0.0217  51  SER A OG  
366  N N   . ALA A 55  ? 0.3013 0.2195 0.2092 -0.0269 -0.0337 0.0191  52  ALA A N   
367  C CA  . ALA A 55  ? 0.3034 0.2216 0.2126 -0.0240 -0.0312 0.0180  52  ALA A CA  
368  C C   . ALA A 55  ? 0.3183 0.2432 0.2317 -0.0190 -0.0319 0.0188  52  ALA A C   
369  O O   . ALA A 55  ? 0.3153 0.2490 0.2330 -0.0195 -0.0342 0.0201  52  ALA A O   
370  C CB  . ALA A 55  ? 0.2980 0.2203 0.2094 -0.0268 -0.0295 0.0168  52  ALA A CB  
371  N N   . HIS A 56  ? 0.3383 0.2599 0.2506 -0.0142 -0.0300 0.0178  53  HIS A N   
372  C CA  . HIS A 56  ? 0.3638 0.2931 0.2809 -0.0081 -0.0301 0.0179  53  HIS A CA  
373  C C   . HIS A 56  ? 0.3526 0.2970 0.2776 -0.0104 -0.0295 0.0180  53  HIS A C   
374  O O   . HIS A 56  ? 0.3557 0.3110 0.2868 -0.0084 -0.0313 0.0192  53  HIS A O   
375  C CB  . HIS A 56  ? 0.4076 0.3296 0.3214 -0.0029 -0.0275 0.0158  53  HIS A CB  
376  C CG  . HIS A 56  ? 0.4514 0.3815 0.3702 0.0046  -0.0272 0.0155  53  HIS A CG  
377  N ND1 . HIS A 56  ? 0.5068 0.4378 0.4267 0.0099  -0.0303 0.0176  53  HIS A ND1 
378  C CD2 . HIS A 56  ? 0.4904 0.4301 0.4138 0.0080  -0.0243 0.0136  53  HIS A CD2 
379  C CE1 . HIS A 56  ? 0.5228 0.4632 0.4484 0.0170  -0.0295 0.0167  53  HIS A CE1 
380  N NE2 . HIS A 56  ? 0.5110 0.4576 0.4391 0.0157  -0.0255 0.0142  53  HIS A NE2 
381  N N   . LEU A 57  ? 0.3450 0.2901 0.2695 -0.0149 -0.0272 0.0170  54  LEU A N   
382  C CA  . LEU A 57  ? 0.3451 0.3031 0.2757 -0.0174 -0.0255 0.0173  54  LEU A CA  
383  C C   . LEU A 57  ? 0.3400 0.3062 0.2755 -0.0217 -0.0286 0.0193  54  LEU A C   
384  O O   . LEU A 57  ? 0.3397 0.3189 0.2819 -0.0232 -0.0279 0.0200  54  LEU A O   
385  C CB  . LEU A 57  ? 0.3414 0.2956 0.2682 -0.0218 -0.0231 0.0164  54  LEU A CB  
386  C CG  . LEU A 57  ? 0.3562 0.3214 0.2871 -0.0253 -0.0209 0.0172  54  LEU A CG  
387  C CD1 . LEU A 57  ? 0.3772 0.3525 0.3122 -0.0201 -0.0175 0.0161  54  LEU A CD1 
388  C CD2 . LEU A 57  ? 0.3552 0.3138 0.2804 -0.0300 -0.0197 0.0172  54  LEU A CD2 
389  N N   . TYR A 58  ? 0.3387 0.2977 0.2705 -0.0243 -0.0318 0.0200  55  TYR A N   
390  C CA  . TYR A 58  ? 0.3345 0.2986 0.2688 -0.0297 -0.0349 0.0212  55  TYR A CA  
391  C C   . TYR A 58  ? 0.3464 0.3217 0.2869 -0.0271 -0.0380 0.0223  55  TYR A C   
392  O O   . TYR A 58  ? 0.3504 0.3317 0.2938 -0.0319 -0.0408 0.0229  55  TYR A O   
393  C CB  . TYR A 58  ? 0.3324 0.2849 0.2596 -0.0325 -0.0370 0.0210  55  TYR A CB  
394  C CG  . TYR A 58  ? 0.3195 0.2625 0.2416 -0.0349 -0.0349 0.0199  55  TYR A CG  
395  C CD1 . TYR A 58  ? 0.3208 0.2650 0.2435 -0.0357 -0.0319 0.0195  55  TYR A CD1 
396  C CD2 . TYR A 58  ? 0.3274 0.2611 0.2436 -0.0364 -0.0361 0.0193  55  TYR A CD2 
397  C CE1 . TYR A 58  ? 0.3093 0.2457 0.2274 -0.0378 -0.0308 0.0187  55  TYR A CE1 
398  C CE2 . TYR A 58  ? 0.3130 0.2398 0.2255 -0.0381 -0.0345 0.0183  55  TYR A CE2 
399  C CZ  . TYR A 58  ? 0.3127 0.2408 0.2263 -0.0386 -0.0322 0.0180  55  TYR A CZ  
400  O OH  . TYR A 58  ? 0.3135 0.2355 0.2235 -0.0396 -0.0314 0.0171  55  TYR A OH  
401  N N   . ASN A 59  ? 0.3542 0.3311 0.2960 -0.0196 -0.0380 0.0223  56  ASN A N   
402  C CA  . ASN A 59  ? 0.3635 0.3514 0.3111 -0.0154 -0.0415 0.0235  56  ASN A CA  
403  C C   . ASN A 59  ? 0.3614 0.3457 0.3053 -0.0188 -0.0464 0.0246  56  ASN A C   
404  O O   . ASN A 59  ? 0.3751 0.3712 0.3247 -0.0215 -0.0500 0.0252  56  ASN A O   
405  C CB  . ASN A 59  ? 0.3859 0.3931 0.3448 -0.0170 -0.0406 0.0236  56  ASN A CB  
406  C CG  . ASN A 59  ? 0.4044 0.4264 0.3714 -0.0119 -0.0441 0.0245  56  ASN A CG  
407  O OD1 . ASN A 59  ? 0.4543 0.4722 0.4191 -0.0037 -0.0458 0.0250  56  ASN A OD1 
408  N ND2 . ASN A 59  ? 0.4063 0.4455 0.3827 -0.0166 -0.0457 0.0250  56  ASN A ND2 
409  N N   . ASN A 60  ? 0.3476 0.3168 0.2819 -0.0196 -0.0466 0.0245  57  ASN A N   
410  C CA  . ASN A 60  ? 0.3526 0.3184 0.2821 -0.0226 -0.0508 0.0252  57  ASN A CA  
411  C C   . ASN A 60  ? 0.3578 0.3103 0.2778 -0.0190 -0.0512 0.0262  57  ASN A C   
412  O O   . ASN A 60  ? 0.3454 0.2936 0.2594 -0.0214 -0.0541 0.0266  57  ASN A O   
413  C CB  . ASN A 60  ? 0.3453 0.3087 0.2730 -0.0306 -0.0508 0.0238  57  ASN A CB  
414  C CG  . ASN A 60  ? 0.3275 0.2779 0.2486 -0.0322 -0.0472 0.0227  57  ASN A CG  
415  O OD1 . ASN A 60  ? 0.3243 0.2674 0.2419 -0.0284 -0.0449 0.0228  57  ASN A OD1 
416  N ND2 . ASN A 60  ? 0.3381 0.2858 0.2578 -0.0379 -0.0470 0.0215  57  ASN A ND2 
417  N N   . GLU A 61  ? 0.3636 0.3089 0.2812 -0.0138 -0.0485 0.0265  58  GLU A N   
418  C CA  . GLU A 61  ? 0.3850 0.3157 0.2926 -0.0127 -0.0482 0.0276  58  GLU A CA  
419  C C   . GLU A 61  ? 0.3997 0.3303 0.3033 -0.0093 -0.0529 0.0302  58  GLU A C   
420  O O   . GLU A 61  ? 0.3813 0.3024 0.2758 -0.0112 -0.0534 0.0313  58  GLU A O   
421  C CB  . GLU A 61  ? 0.3942 0.3156 0.2993 -0.0088 -0.0447 0.0272  58  GLU A CB  
422  C CG  . GLU A 61  ? 0.4029 0.3213 0.3084 -0.0131 -0.0406 0.0247  58  GLU A CG  
423  C CD  . GLU A 61  ? 0.4176 0.3256 0.3193 -0.0108 -0.0375 0.0238  58  GLU A CD  
424  O OE1 . GLU A 61  ? 0.4213 0.3310 0.3258 -0.0059 -0.0364 0.0230  58  GLU A OE1 
425  O OE2 . GLU A 61  ? 0.4490 0.3472 0.3446 -0.0141 -0.0362 0.0236  58  GLU A OE2 
426  N N   . GLU A 62  ? 0.4199 0.3615 0.3300 -0.0044 -0.0560 0.0313  59  GLU A N   
427  C CA  . GLU A 62  ? 0.4428 0.3866 0.3499 -0.0005 -0.0616 0.0340  59  GLU A CA  
428  C C   . GLU A 62  ? 0.4241 0.3688 0.3267 -0.0071 -0.0645 0.0336  59  GLU A C   
429  O O   . GLU A 62  ? 0.4233 0.3592 0.3156 -0.0067 -0.0665 0.0356  59  GLU A O   
430  C CB  . GLU A 62  ? 0.4717 0.4322 0.3895 0.0049  -0.0649 0.0344  59  GLU A CB  
431  C CG  . GLU A 62  ? 0.5138 0.4774 0.4286 0.0097  -0.0713 0.0374  59  GLU A CG  
432  C CD  . GLU A 62  ? 0.5583 0.5419 0.4853 0.0149  -0.0754 0.0377  59  GLU A CD  
433  O OE1 . GLU A 62  ? 0.5853 0.5812 0.5237 0.0151  -0.0725 0.0356  59  GLU A OE1 
434  O OE2 . GLU A 62  ? 0.5890 0.5771 0.5142 0.0187  -0.0815 0.0401  59  GLU A OE2 
435  N N   . GLN A 63  ? 0.4037 0.3575 0.3127 -0.0131 -0.0644 0.0312  60  GLN A N   
436  C CA  . GLN A 63  ? 0.4024 0.3571 0.3074 -0.0195 -0.0675 0.0300  60  GLN A CA  
437  C C   . GLN A 63  ? 0.3877 0.3283 0.2827 -0.0233 -0.0642 0.0288  60  GLN A C   
438  O O   . GLN A 63  ? 0.3759 0.3124 0.2626 -0.0251 -0.0667 0.0289  60  GLN A O   
439  C CB  . GLN A 63  ? 0.4047 0.3720 0.3193 -0.0249 -0.0685 0.0279  60  GLN A CB  
440  C CG  . GLN A 63  ? 0.4253 0.4096 0.3501 -0.0217 -0.0725 0.0290  60  GLN A CG  
441  C CD  . GLN A 63  ? 0.4255 0.4169 0.3595 -0.0165 -0.0690 0.0295  60  GLN A CD  
442  O OE1 . GLN A 63  ? 0.4207 0.4049 0.3540 -0.0164 -0.0636 0.0287  60  GLN A OE1 
443  N NE2 . GLN A 63  ? 0.4652 0.4718 0.4079 -0.0118 -0.0723 0.0306  60  GLN A NE2 
444  N N   . VAL A 64  ? 0.3718 0.3066 0.2678 -0.0246 -0.0590 0.0276  61  VAL A N   
445  C CA  . VAL A 64  ? 0.3647 0.2884 0.2529 -0.0279 -0.0556 0.0263  61  VAL A CA  
446  C C   . VAL A 64  ? 0.3731 0.2873 0.2516 -0.0250 -0.0553 0.0288  61  VAL A C   
447  O O   . VAL A 64  ? 0.3719 0.2808 0.2419 -0.0274 -0.0553 0.0285  61  VAL A O   
448  C CB  . VAL A 64  ? 0.3483 0.2695 0.2405 -0.0292 -0.0508 0.0247  61  VAL A CB  
449  C CG1 . VAL A 64  ? 0.3452 0.2573 0.2309 -0.0317 -0.0476 0.0234  61  VAL A CG1 
450  C CG2 . VAL A 64  ? 0.3497 0.2791 0.2497 -0.0325 -0.0511 0.0230  61  VAL A CG2 
451  N N   . GLY A 65  ? 0.3761 0.2881 0.2553 -0.0198 -0.0551 0.0312  62  GLY A N   
452  C CA  . GLY A 65  ? 0.3990 0.3005 0.2685 -0.0170 -0.0550 0.0344  62  GLY A CA  
453  C C   . GLY A 65  ? 0.4137 0.3160 0.2758 -0.0168 -0.0596 0.0363  62  GLY A C   
454  O O   . GLY A 65  ? 0.4252 0.3188 0.2766 -0.0185 -0.0584 0.0377  62  GLY A O   
455  N N   . LEU A 66  ? 0.4172 0.3305 0.2849 -0.0149 -0.0646 0.0363  63  LEU A N   
456  C CA  . LEU A 66  ? 0.4432 0.3591 0.3043 -0.0141 -0.0703 0.0380  63  LEU A CA  
457  C C   . LEU A 66  ? 0.4303 0.3445 0.2849 -0.0205 -0.0700 0.0352  63  LEU A C   
458  O O   . LEU A 66  ? 0.4355 0.3438 0.2784 -0.0206 -0.0714 0.0369  63  LEU A O   
459  C CB  . LEU A 66  ? 0.4688 0.3994 0.3402 -0.0108 -0.0755 0.0381  63  LEU A CB  
460  C CG  . LEU A 66  ? 0.5139 0.4509 0.3814 -0.0092 -0.0828 0.0398  63  LEU A CG  
461  C CD1 . LEU A 66  ? 0.5452 0.4706 0.3995 -0.0044 -0.0843 0.0444  63  LEU A CD1 
462  C CD2 . LEU A 66  ? 0.5253 0.4791 0.4062 -0.0053 -0.0871 0.0399  63  LEU A CD2 
463  N N   . ALA A 67  ? 0.3974 0.3143 0.2576 -0.0253 -0.0674 0.0313  64  ALA A N   
464  C CA  . ALA A 67  ? 0.4011 0.3143 0.2544 -0.0304 -0.0666 0.0281  64  ALA A CA  
465  C C   . ALA A 67  ? 0.3953 0.2976 0.2387 -0.0306 -0.0617 0.0290  64  ALA A C   
466  O O   . ALA A 67  ? 0.4068 0.3054 0.2395 -0.0321 -0.0622 0.0286  64  ALA A O   
467  C CB  . ALA A 67  ? 0.3975 0.3140 0.2585 -0.0346 -0.0648 0.0241  64  ALA A CB  
468  N N   . ILE A 68  ? 0.3878 0.2854 0.2339 -0.0294 -0.0571 0.0303  65  ILE A N   
469  C CA  . ILE A 68  ? 0.3971 0.2855 0.2351 -0.0307 -0.0520 0.0313  65  ILE A CA  
470  C C   . ILE A 68  ? 0.4299 0.3124 0.2564 -0.0286 -0.0538 0.0358  65  ILE A C   
471  O O   . ILE A 68  ? 0.4428 0.3209 0.2587 -0.0310 -0.0518 0.0360  65  ILE A O   
472  C CB  . ILE A 68  ? 0.3782 0.2635 0.2223 -0.0306 -0.0473 0.0314  65  ILE A CB  
473  C CG1 . ILE A 68  ? 0.3609 0.2512 0.2138 -0.0330 -0.0454 0.0272  65  ILE A CG1 
474  C CG2 . ILE A 68  ? 0.3857 0.2622 0.2217 -0.0322 -0.0429 0.0335  65  ILE A CG2 
475  C CD1 . ILE A 68  ? 0.3499 0.2393 0.2099 -0.0326 -0.0422 0.0268  65  ILE A CD1 
476  N N   . ARG A 69  ? 0.4451 0.3275 0.2730 -0.0239 -0.0574 0.0393  66  ARG A N   
477  C CA  . ARG A 69  ? 0.4738 0.3490 0.2899 -0.0210 -0.0599 0.0444  66  ARG A CA  
478  C C   . ARG A 69  ? 0.4810 0.3593 0.2881 -0.0223 -0.0639 0.0440  66  ARG A C   
479  O O   . ARG A 69  ? 0.4770 0.3479 0.2708 -0.0231 -0.0631 0.0469  66  ARG A O   
480  C CB  . ARG A 69  ? 0.4981 0.3743 0.3190 -0.0144 -0.0640 0.0475  66  ARG A CB  
481  C CG  . ARG A 69  ? 0.5127 0.3810 0.3371 -0.0123 -0.0601 0.0487  66  ARG A CG  
482  C CD  . ARG A 69  ? 0.5566 0.4105 0.3695 -0.0148 -0.0559 0.0519  66  ARG A CD  
483  N NE  . ARG A 69  ? 0.6083 0.4540 0.4078 -0.0120 -0.0592 0.0573  66  ARG A NE  
484  C CZ  . ARG A 69  ? 0.6488 0.4875 0.4452 -0.0054 -0.0627 0.0617  66  ARG A CZ  
485  N NH1 . ARG A 69  ? 0.6551 0.4952 0.4615 -0.0005 -0.0632 0.0606  66  ARG A NH1 
486  N NH2 . ARG A 69  ? 0.6836 0.5142 0.4665 -0.0030 -0.0660 0.0671  66  ARG A NH2 
487  N N   . SER A 70  ? 0.4781 0.3668 0.2921 -0.0232 -0.0678 0.0403  67  SER A N   
488  C CA  . SER A 70  ? 0.5032 0.3958 0.3098 -0.0249 -0.0725 0.0388  67  SER A CA  
489  C C   . SER A 70  ? 0.4975 0.3844 0.2940 -0.0294 -0.0679 0.0361  67  SER A C   
490  O O   . SER A 70  ? 0.5153 0.3990 0.2985 -0.0297 -0.0695 0.0372  67  SER A O   
491  C CB  . SER A 70  ? 0.4993 0.4036 0.3171 -0.0262 -0.0770 0.0351  67  SER A CB  
492  O OG  . SER A 70  ? 0.5586 0.4669 0.3693 -0.0270 -0.0833 0.0344  67  SER A OG  
493  N N   . LYS A 71  ? 0.4821 0.3684 0.2846 -0.0322 -0.0623 0.0325  68  LYS A N   
494  C CA  . LYS A 71  ? 0.4850 0.3681 0.2799 -0.0356 -0.0578 0.0290  68  LYS A CA  
495  C C   . LYS A 71  ? 0.4843 0.3601 0.2699 -0.0360 -0.0523 0.0326  68  LYS A C   
496  O O   . LYS A 71  ? 0.4966 0.3704 0.2724 -0.0381 -0.0491 0.0309  68  LYS A O   
497  C CB  . LYS A 71  ? 0.4712 0.3569 0.2761 -0.0378 -0.0544 0.0239  68  LYS A CB  
498  C CG  . LYS A 71  ? 0.4765 0.3681 0.2894 -0.0387 -0.0594 0.0207  68  LYS A CG  
499  C CD  . LYS A 71  ? 0.5091 0.4018 0.3136 -0.0402 -0.0644 0.0181  68  LYS A CD  
500  C CE  . LYS A 71  ? 0.5310 0.4186 0.3259 -0.0420 -0.0610 0.0136  68  LYS A CE  
501  N NZ  . LYS A 71  ? 0.5648 0.4524 0.3508 -0.0437 -0.0664 0.0102  68  LYS A NZ  
502  N N   . ILE A 72  ? 0.4754 0.3469 0.2632 -0.0342 -0.0513 0.0374  69  ILE A N   
503  C CA  . ILE A 72  ? 0.4966 0.3595 0.2736 -0.0354 -0.0468 0.0418  69  ILE A CA  
504  C C   . ILE A 72  ? 0.5246 0.3834 0.2867 -0.0337 -0.0511 0.0462  69  ILE A C   
505  O O   . ILE A 72  ? 0.5361 0.3903 0.2850 -0.0362 -0.0477 0.0478  69  ILE A O   
506  C CB  . ILE A 72  ? 0.4884 0.3458 0.2714 -0.0346 -0.0444 0.0451  69  ILE A CB  
507  C CG1 . ILE A 72  ? 0.4686 0.3302 0.2646 -0.0367 -0.0402 0.0408  69  ILE A CG1 
508  C CG2 . ILE A 72  ? 0.5118 0.3587 0.2825 -0.0366 -0.0407 0.0505  69  ILE A CG2 
509  C CD1 . ILE A 72  ? 0.4630 0.3206 0.2666 -0.0349 -0.0399 0.0428  69  ILE A CD1 
510  N N   . ALA A 73  ? 0.5329 0.3937 0.2970 -0.0294 -0.0583 0.0483  70  ALA A N   
511  C CA  . ALA A 73  ? 0.5681 0.4250 0.3186 -0.0265 -0.0636 0.0533  70  ALA A CA  
512  C C   . ALA A 73  ? 0.5910 0.4524 0.3321 -0.0288 -0.0658 0.0497  70  ALA A C   
513  O O   . ALA A 73  ? 0.6113 0.4676 0.3364 -0.0287 -0.0670 0.0532  70  ALA A O   
514  C CB  . ALA A 73  ? 0.5674 0.4276 0.3250 -0.0205 -0.0709 0.0560  70  ALA A CB  
515  N N   . ASP A 74  ? 0.5868 0.4560 0.3361 -0.0311 -0.0660 0.0429  71  ASP A N   
516  C CA  . ASP A 74  ? 0.6153 0.4871 0.3550 -0.0333 -0.0681 0.0385  71  ASP A CA  
517  C C   . ASP A 74  ? 0.6167 0.4839 0.3461 -0.0366 -0.0602 0.0367  71  ASP A C   
518  O O   . ASP A 74  ? 0.6291 0.4968 0.3474 -0.0379 -0.0611 0.0331  71  ASP A O   
519  C CB  . ASP A 74  ? 0.6161 0.4964 0.3669 -0.0344 -0.0726 0.0325  71  ASP A CB  
520  C CG  . ASP A 74  ? 0.6135 0.4950 0.3731 -0.0373 -0.0675 0.0264  71  ASP A CG  
521  O OD1 . ASP A 74  ? 0.6272 0.5047 0.3834 -0.0386 -0.0603 0.0255  71  ASP A OD1 
522  O OD2 . ASP A 74  ? 0.6386 0.5256 0.4080 -0.0384 -0.0712 0.0225  71  ASP A OD2 
523  N N   . GLY A 75  ? 0.6124 0.4758 0.3447 -0.0379 -0.0528 0.0388  72  GLY A N   
524  C CA  . GLY A 75  ? 0.6177 0.4789 0.3417 -0.0411 -0.0446 0.0376  72  GLY A CA  
525  C C   . GLY A 75  ? 0.6002 0.4668 0.3339 -0.0426 -0.0402 0.0303  72  GLY A C   
526  O O   . GLY A 75  ? 0.6046 0.4717 0.3333 -0.0446 -0.0333 0.0285  72  GLY A O   
527  N N   . SER A 76  ? 0.5815 0.4522 0.3287 -0.0415 -0.0437 0.0266  73  SER A N   
528  C CA  . SER A 76  ? 0.5779 0.4523 0.3339 -0.0422 -0.0407 0.0198  73  SER A CA  
529  C C   . SER A 76  ? 0.5655 0.4409 0.3299 -0.0433 -0.0334 0.0203  73  SER A C   
530  O O   . SER A 76  ? 0.5707 0.4487 0.3359 -0.0437 -0.0285 0.0158  73  SER A O   
531  C CB  . SER A 76  ? 0.5668 0.4443 0.3345 -0.0415 -0.0464 0.0171  73  SER A CB  
532  O OG  . SER A 76  ? 0.5849 0.4627 0.3456 -0.0416 -0.0526 0.0145  73  SER A OG  
533  N N   . VAL A 77  ? 0.5520 0.4257 0.3228 -0.0433 -0.0332 0.0253  74  VAL A N   
534  C CA  . VAL A 77  ? 0.5347 0.4094 0.3146 -0.0449 -0.0274 0.0257  74  VAL A CA  
535  C C   . VAL A 77  ? 0.5418 0.4104 0.3176 -0.0459 -0.0264 0.0325  74  VAL A C   
536  O O   . VAL A 77  ? 0.5510 0.4151 0.3208 -0.0440 -0.0315 0.0366  74  VAL A O   
537  C CB  . VAL A 77  ? 0.5153 0.3933 0.3106 -0.0437 -0.0290 0.0232  74  VAL A CB  
538  C CG1 . VAL A 77  ? 0.5179 0.3999 0.3169 -0.0431 -0.0292 0.0167  74  VAL A CG1 
539  C CG2 . VAL A 77  ? 0.4985 0.3752 0.2984 -0.0416 -0.0353 0.0259  74  VAL A CG2 
540  N N   . LYS A 78  ? 0.5328 0.4013 0.3124 -0.0488 -0.0206 0.0335  75  LYS A N   
541  C CA  . LYS A 78  ? 0.5599 0.4207 0.3378 -0.0505 -0.0196 0.0394  75  LYS A CA  
542  C C   . LYS A 78  ? 0.5304 0.3921 0.3225 -0.0496 -0.0204 0.0381  75  LYS A C   
543  O O   . LYS A 78  ? 0.4888 0.3579 0.2912 -0.0489 -0.0202 0.0329  75  LYS A O   
544  C CB  . LYS A 78  ? 0.6184 0.4776 0.3882 -0.0557 -0.0126 0.0419  75  LYS A CB  
545  C CG  . LYS A 78  ? 0.6414 0.5093 0.4199 -0.0591 -0.0061 0.0379  75  LYS A CG  
546  C CD  . LYS A 78  ? 0.7041 0.5719 0.4734 -0.0647 0.0008  0.0409  75  LYS A CD  
547  C CE  . LYS A 78  ? 0.7152 0.5927 0.4950 -0.0687 0.0072  0.0378  75  LYS A CE  
548  N NZ  . LYS A 78  ? 0.7429 0.6145 0.5211 -0.0752 0.0107  0.0429  75  LYS A NZ  
549  N N   . ARG A 79  ? 0.5167 0.3700 0.3078 -0.0492 -0.0218 0.0427  76  ARG A N   
550  C CA  . ARG A 79  ? 0.4968 0.3492 0.2993 -0.0480 -0.0228 0.0417  76  ARG A CA  
551  C C   . ARG A 79  ? 0.4751 0.3339 0.2865 -0.0518 -0.0178 0.0378  76  ARG A C   
552  O O   . ARG A 79  ? 0.4614 0.3252 0.2835 -0.0500 -0.0192 0.0343  76  ARG A O   
553  C CB  . ARG A 79  ? 0.5074 0.3476 0.3052 -0.0475 -0.0238 0.0470  76  ARG A CB  
554  C CG  . ARG A 79  ? 0.4875 0.3262 0.2957 -0.0460 -0.0245 0.0454  76  ARG A CG  
555  C CD  . ARG A 79  ? 0.4685 0.3148 0.2862 -0.0408 -0.0289 0.0423  76  ARG A CD  
556  N NE  . ARG A 79  ? 0.4427 0.2893 0.2701 -0.0398 -0.0286 0.0400  76  ARG A NE  
557  C CZ  . ARG A 79  ? 0.4295 0.2829 0.2656 -0.0422 -0.0262 0.0359  76  ARG A CZ  
558  N NH1 . ARG A 79  ? 0.4196 0.2806 0.2573 -0.0451 -0.0238 0.0331  76  ARG A NH1 
559  N NH2 . ARG A 79  ? 0.4240 0.2767 0.2670 -0.0409 -0.0264 0.0342  76  ARG A NH2 
560  N N   . GLU A 80  ? 0.4928 0.3523 0.2998 -0.0568 -0.0124 0.0385  77  GLU A N   
561  C CA  . GLU A 80  ? 0.4927 0.3594 0.3085 -0.0607 -0.0076 0.0353  77  GLU A CA  
562  C C   . GLU A 80  ? 0.4663 0.3446 0.2893 -0.0584 -0.0073 0.0295  77  GLU A C   
563  O O   . GLU A 80  ? 0.4456 0.3307 0.2783 -0.0598 -0.0050 0.0263  77  GLU A O   
564  C CB  . GLU A 80  ? 0.5407 0.4067 0.3499 -0.0671 -0.0017 0.0379  77  GLU A CB  
565  C CG  . GLU A 80  ? 0.6010 0.4533 0.4029 -0.0704 -0.0017 0.0438  77  GLU A CG  
566  C CD  . GLU A 80  ? 0.6496 0.4911 0.4368 -0.0685 -0.0041 0.0493  77  GLU A CD  
567  O OE1 . GLU A 80  ? 0.7224 0.5509 0.5019 -0.0711 -0.0039 0.0546  77  GLU A OE1 
568  O OE2 . GLU A 80  ? 0.6575 0.5028 0.4404 -0.0643 -0.0067 0.0484  77  GLU A OE2 
569  N N   . ASP A 81  ? 0.4563 0.3362 0.2745 -0.0550 -0.0097 0.0280  78  ASP A N   
570  C CA  . ASP A 81  ? 0.4444 0.3322 0.2678 -0.0523 -0.0101 0.0223  78  ASP A CA  
571  C C   . ASP A 81  ? 0.4215 0.3095 0.2544 -0.0492 -0.0147 0.0204  78  ASP A C   
572  O O   . ASP A 81  ? 0.4185 0.3114 0.2567 -0.0474 -0.0150 0.0162  78  ASP A O   
573  C CB  . ASP A 81  ? 0.4633 0.3506 0.2770 -0.0502 -0.0119 0.0210  78  ASP A CB  
574  C CG  . ASP A 81  ? 0.5053 0.3934 0.3078 -0.0526 -0.0072 0.0222  78  ASP A CG  
575  O OD1 . ASP A 81  ? 0.5373 0.4302 0.3423 -0.0557 -0.0013 0.0220  78  ASP A OD1 
576  O OD2 . ASP A 81  ? 0.5226 0.4072 0.3136 -0.0514 -0.0094 0.0230  78  ASP A OD2 
577  N N   . ILE A 82  ? 0.3996 0.2822 0.2334 -0.0482 -0.0183 0.0235  79  ILE A N   
578  C CA  . ILE A 82  ? 0.3884 0.2720 0.2304 -0.0455 -0.0224 0.0220  79  ILE A CA  
579  C C   . ILE A 82  ? 0.3702 0.2541 0.2202 -0.0467 -0.0207 0.0219  79  ILE A C   
580  O O   . ILE A 82  ? 0.3835 0.2628 0.2310 -0.0491 -0.0185 0.0245  79  ILE A O   
581  C CB  . ILE A 82  ? 0.3971 0.2768 0.2360 -0.0429 -0.0274 0.0249  79  ILE A CB  
582  C CG1 . ILE A 82  ? 0.4094 0.2898 0.2405 -0.0420 -0.0300 0.0245  79  ILE A CG1 
583  C CG2 . ILE A 82  ? 0.3826 0.2647 0.2308 -0.0407 -0.0305 0.0240  79  ILE A CG2 
584  C CD1 . ILE A 82  ? 0.4142 0.2993 0.2491 -0.0415 -0.0317 0.0198  79  ILE A CD1 
585  N N   . PHE A 83  ? 0.3482 0.2364 0.2064 -0.0454 -0.0217 0.0189  80  PHE A N   
586  C CA  . PHE A 83  ? 0.3392 0.2283 0.2048 -0.0461 -0.0209 0.0182  80  PHE A CA  
587  C C   . PHE A 83  ? 0.3262 0.2145 0.1957 -0.0432 -0.0246 0.0185  80  PHE A C   
588  O O   . PHE A 83  ? 0.3091 0.2011 0.1819 -0.0419 -0.0265 0.0164  80  PHE A O   
589  C CB  . PHE A 83  ? 0.3402 0.2361 0.2117 -0.0467 -0.0188 0.0146  80  PHE A CB  
590  C CG  . PHE A 83  ? 0.3276 0.2250 0.2056 -0.0479 -0.0182 0.0138  80  PHE A CG  
591  C CD1 . PHE A 83  ? 0.3190 0.2160 0.2014 -0.0459 -0.0208 0.0132  80  PHE A CD1 
592  C CD2 . PHE A 83  ? 0.3364 0.2362 0.2159 -0.0515 -0.0150 0.0135  80  PHE A CD2 
593  C CE1 . PHE A 83  ? 0.3220 0.2202 0.2090 -0.0470 -0.0204 0.0122  80  PHE A CE1 
594  C CE2 . PHE A 83  ? 0.3286 0.2297 0.2135 -0.0530 -0.0151 0.0125  80  PHE A CE2 
595  C CZ  . PHE A 83  ? 0.3216 0.2217 0.2098 -0.0505 -0.0179 0.0117  80  PHE A CZ  
596  N N   . TYR A 84  ? 0.3325 0.2157 0.2004 -0.0422 -0.0257 0.0211  81  TYR A N   
597  C CA  . TYR A 84  ? 0.3297 0.2136 0.2016 -0.0390 -0.0287 0.0216  81  TYR A CA  
598  C C   . TYR A 84  ? 0.3161 0.1997 0.1932 -0.0389 -0.0276 0.0203  81  TYR A C   
599  O O   . TYR A 84  ? 0.3130 0.1909 0.1879 -0.0402 -0.0259 0.0210  81  TYR A O   
600  C CB  . TYR A 84  ? 0.3513 0.2304 0.2181 -0.0364 -0.0310 0.0250  81  TYR A CB  
601  C CG  . TYR A 84  ? 0.3554 0.2376 0.2273 -0.0325 -0.0338 0.0253  81  TYR A CG  
602  C CD1 . TYR A 84  ? 0.3656 0.2553 0.2414 -0.0317 -0.0366 0.0244  81  TYR A CD1 
603  C CD2 . TYR A 84  ? 0.3771 0.2550 0.2501 -0.0298 -0.0335 0.0261  81  TYR A CD2 
604  C CE1 . TYR A 84  ? 0.3684 0.2632 0.2499 -0.0286 -0.0387 0.0247  81  TYR A CE1 
605  C CE2 . TYR A 84  ? 0.3744 0.2569 0.2527 -0.0257 -0.0354 0.0260  81  TYR A CE2 
606  C CZ  . TYR A 84  ? 0.3740 0.2660 0.2571 -0.0252 -0.0379 0.0255  81  TYR A CZ  
607  O OH  . TYR A 84  ? 0.3837 0.2822 0.2728 -0.0216 -0.0393 0.0255  81  TYR A OH  
608  N N   . THR A 85  ? 0.3127 0.2014 0.1955 -0.0376 -0.0289 0.0187  82  THR A N   
609  C CA  . THR A 85  ? 0.2987 0.1882 0.1858 -0.0372 -0.0281 0.0173  82  THR A CA  
610  C C   . THR A 85  ? 0.3024 0.1930 0.1916 -0.0336 -0.0297 0.0182  82  THR A C   
611  O O   . THR A 85  ? 0.2949 0.1906 0.1863 -0.0324 -0.0317 0.0189  82  THR A O   
612  C CB  . THR A 85  ? 0.2947 0.1894 0.1858 -0.0385 -0.0279 0.0150  82  THR A CB  
613  O OG1 . THR A 85  ? 0.2902 0.1852 0.1803 -0.0408 -0.0263 0.0138  82  THR A OG1 
614  C CG2 . THR A 85  ? 0.2913 0.1868 0.1855 -0.0379 -0.0274 0.0138  82  THR A CG2 
615  N N   . SER A 86  ? 0.2978 0.1840 0.1865 -0.0319 -0.0287 0.0181  83  SER A N   
616  C CA  . SER A 86  ? 0.3054 0.1945 0.1973 -0.0279 -0.0293 0.0180  83  SER A CA  
617  C C   . SER A 86  ? 0.2963 0.1852 0.1897 -0.0284 -0.0274 0.0154  83  SER A C   
618  O O   . SER A 86  ? 0.3005 0.1863 0.1922 -0.0318 -0.0263 0.0140  83  SER A O   
619  C CB  . SER A 86  ? 0.3191 0.2033 0.2084 -0.0233 -0.0303 0.0198  83  SER A CB  
620  O OG  . SER A 86  ? 0.3223 0.2133 0.2166 -0.0190 -0.0308 0.0194  83  SER A OG  
621  N N   . LYS A 87  ? 0.3000 0.1933 0.1965 -0.0251 -0.0272 0.0148  84  LYS A N   
622  C CA  . LYS A 87  ? 0.3095 0.2038 0.2066 -0.0253 -0.0255 0.0123  84  LYS A CA  
623  C C   . LYS A 87  ? 0.3218 0.2149 0.2186 -0.0200 -0.0244 0.0113  84  LYS A C   
624  O O   . LYS A 87  ? 0.3229 0.2213 0.2229 -0.0160 -0.0251 0.0126  84  LYS A O   
625  C CB  . LYS A 87  ? 0.3028 0.2056 0.2036 -0.0276 -0.0255 0.0122  84  LYS A CB  
626  C CG  . LYS A 87  ? 0.2977 0.2013 0.1986 -0.0314 -0.0267 0.0129  84  LYS A CG  
627  C CD  . LYS A 87  ? 0.3089 0.2176 0.2119 -0.0333 -0.0268 0.0128  84  LYS A CD  
628  C CE  . LYS A 87  ? 0.3145 0.2231 0.2173 -0.0359 -0.0283 0.0133  84  LYS A CE  
629  N NZ  . LYS A 87  ? 0.3240 0.2353 0.2283 -0.0362 -0.0298 0.0148  84  LYS A NZ  
630  N N   . LEU A 88  ? 0.3299 0.2163 0.2228 -0.0200 -0.0230 0.0087  85  LEU A N   
631  C CA  . LEU A 88  ? 0.3418 0.2255 0.2330 -0.0148 -0.0215 0.0065  85  LEU A CA  
632  C C   . LEU A 88  ? 0.3316 0.2265 0.2267 -0.0136 -0.0199 0.0054  85  LEU A C   
633  O O   . LEU A 88  ? 0.3240 0.2211 0.2181 -0.0174 -0.0193 0.0042  85  LEU A O   
634  C CB  . LEU A 88  ? 0.3605 0.2328 0.2453 -0.0170 -0.0209 0.0035  85  LEU A CB  
635  C CG  . LEU A 88  ? 0.3865 0.2528 0.2672 -0.0121 -0.0193 0.0001  85  LEU A CG  
636  C CD1 . LEU A 88  ? 0.4033 0.2604 0.2813 -0.0063 -0.0199 0.0010  85  LEU A CD1 
637  C CD2 . LEU A 88  ? 0.3874 0.2453 0.2623 -0.0164 -0.0191 -0.0034 85  LEU A CD2 
638  N N   . TRP A 89  ? 0.3332 0.2352 0.2321 -0.0085 -0.0191 0.0059  86  TRP A N   
639  C CA  . TRP A 89  ? 0.3378 0.2521 0.2408 -0.0083 -0.0169 0.0054  86  TRP A CA  
640  C C   . TRP A 89  ? 0.3598 0.2707 0.2577 -0.0056 -0.0141 0.0015  86  TRP A C   
641  O O   . TRP A 89  ? 0.3689 0.2682 0.2613 -0.0025 -0.0141 -0.0010 86  TRP A O   
642  C CB  . TRP A 89  ? 0.3432 0.2700 0.2539 -0.0051 -0.0171 0.0076  86  TRP A CB  
643  C CG  . TRP A 89  ? 0.3428 0.2826 0.2575 -0.0063 -0.0145 0.0075  86  TRP A CG  
644  C CD1 . TRP A 89  ? 0.3630 0.3128 0.2816 -0.0012 -0.0116 0.0063  86  TRP A CD1 
645  C CD2 . TRP A 89  ? 0.3406 0.2837 0.2547 -0.0129 -0.0139 0.0085  86  TRP A CD2 
646  N NE1 . TRP A 89  ? 0.3686 0.3284 0.2891 -0.0050 -0.0090 0.0068  86  TRP A NE1 
647  C CE2 . TRP A 89  ? 0.3517 0.3064 0.2687 -0.0121 -0.0105 0.0083  86  TRP A CE2 
648  C CE3 . TRP A 89  ? 0.3254 0.2627 0.2365 -0.0187 -0.0159 0.0096  86  TRP A CE3 
649  C CZ2 . TRP A 89  ? 0.3521 0.3110 0.2678 -0.0176 -0.0092 0.0096  86  TRP A CZ2 
650  C CZ3 . TRP A 89  ? 0.3365 0.2778 0.2468 -0.0233 -0.0150 0.0107  86  TRP A CZ3 
651  C CH2 . TRP A 89  ? 0.3445 0.2957 0.2565 -0.0230 -0.0117 0.0110  86  TRP A CH2 
652  N N   . SER A 90  ? 0.3600 0.2794 0.2587 -0.0076 -0.0120 0.0011  87  SER A N   
653  C CA  . SER A 90  ? 0.3794 0.2969 0.2720 -0.0069 -0.0095 -0.0025 87  SER A CA  
654  C C   . SER A 90  ? 0.3984 0.3152 0.2893 0.0009  -0.0067 -0.0059 87  SER A C   
655  O O   . SER A 90  ? 0.3973 0.3077 0.2806 0.0019  -0.0051 -0.0099 87  SER A O   
656  C CB  . SER A 90  ? 0.3812 0.3087 0.2750 -0.0110 -0.0081 -0.0008 87  SER A CB  
657  O OG  . SER A 90  ? 0.3820 0.3070 0.2762 -0.0169 -0.0111 0.0018  87  SER A OG  
658  N N   . THR A 91  ? 0.3920 0.3142 0.2889 0.0065  -0.0065 -0.0047 88  THR A N   
659  C CA  . THR A 91  ? 0.4112 0.3319 0.3070 0.0157  -0.0043 -0.0080 88  THR A CA  
660  C C   . THR A 91  ? 0.4139 0.3155 0.3027 0.0190  -0.0064 -0.0100 88  THR A C   
661  O O   . THR A 91  ? 0.4436 0.3404 0.3294 0.0271  -0.0047 -0.0133 88  THR A O   
662  C CB  . THR A 91  ? 0.4095 0.3459 0.3155 0.0208  -0.0035 -0.0058 88  THR A CB  
663  O OG1 . THR A 91  ? 0.3990 0.3336 0.3089 0.0185  -0.0077 -0.0019 88  THR A OG1 
664  C CG2 . THR A 91  ? 0.4092 0.3638 0.3209 0.0174  -0.0002 -0.0046 88  THR A CG2 
665  N N   . PHE A 92  ? 0.4070 0.2979 0.2926 0.0130  -0.0096 -0.0083 89  PHE A N   
666  C CA  . PHE A 92  ? 0.4191 0.2917 0.2983 0.0139  -0.0118 -0.0089 89  PHE A CA  
667  C C   . PHE A 92  ? 0.4258 0.2869 0.2975 0.0068  -0.0127 -0.0112 89  PHE A C   
668  O O   . PHE A 92  ? 0.4345 0.2821 0.3019 0.0041  -0.0147 -0.0105 89  PHE A O   
669  C CB  . PHE A 92  ? 0.4135 0.2861 0.2967 0.0126  -0.0149 -0.0039 89  PHE A CB  
670  C CG  . PHE A 92  ? 0.4214 0.3066 0.3126 0.0190  -0.0151 -0.0016 89  PHE A CG  
671  C CD1 . PHE A 92  ? 0.4565 0.3382 0.3470 0.0288  -0.0148 -0.0028 89  PHE A CD1 
672  C CD2 . PHE A 92  ? 0.4094 0.3099 0.3088 0.0154  -0.0159 0.0017  89  PHE A CD2 
673  C CE1 . PHE A 92  ? 0.4643 0.3601 0.3634 0.0351  -0.0153 -0.0008 89  PHE A CE1 
674  C CE2 . PHE A 92  ? 0.4263 0.3400 0.3338 0.0206  -0.0165 0.0037  89  PHE A CE2 
675  C CZ  . PHE A 92  ? 0.4468 0.3594 0.3548 0.0306  -0.0162 0.0025  89  PHE A CZ  
676  N N   . HIS A 93  ? 0.4276 0.2937 0.2973 0.0038  -0.0111 -0.0138 90  HIS A N   
677  C CA  . HIS A 93  ? 0.4322 0.2891 0.2949 -0.0024 -0.0123 -0.0167 90  HIS A CA  
678  C C   . HIS A 93  ? 0.4632 0.3026 0.3165 0.0005  -0.0121 -0.0215 90  HIS A C   
679  O O   . HIS A 93  ? 0.4726 0.3012 0.3205 -0.0056 -0.0141 -0.0233 90  HIS A O   
680  C CB  . HIS A 93  ? 0.4277 0.2954 0.2901 -0.0051 -0.0109 -0.0179 90  HIS A CB  
681  C CG  . HIS A 93  ? 0.4092 0.2881 0.2781 -0.0103 -0.0122 -0.0135 90  HIS A CG  
682  N ND1 . HIS A 93  ? 0.4101 0.2966 0.2779 -0.0138 -0.0119 -0.0135 90  HIS A ND1 
683  C CD2 . HIS A 93  ? 0.4016 0.2837 0.2768 -0.0127 -0.0140 -0.0092 90  HIS A CD2 
684  C CE1 . HIS A 93  ? 0.4032 0.2966 0.2767 -0.0175 -0.0134 -0.0093 90  HIS A CE1 
685  N NE2 . HIS A 93  ? 0.3898 0.2809 0.2680 -0.0171 -0.0146 -0.0069 90  HIS A NE2 
686  N N   . ARG A 94  ? 0.4827 0.3196 0.3336 0.0091  -0.0099 -0.0243 91  ARG A N   
687  C CA  . ARG A 94  ? 0.5309 0.3484 0.3712 0.0119  -0.0099 -0.0295 91  ARG A CA  
688  C C   . ARG A 94  ? 0.5383 0.3405 0.3764 0.0091  -0.0128 -0.0268 91  ARG A C   
689  O O   . ARG A 94  ? 0.5107 0.3169 0.3548 0.0110  -0.0137 -0.0218 91  ARG A O   
690  C CB  . ARG A 94  ? 0.5699 0.3864 0.4079 0.0232  -0.0069 -0.0330 91  ARG A CB  
691  C CG  . ARG A 94  ? 0.5760 0.4075 0.4148 0.0253  -0.0033 -0.0359 91  ARG A CG  
692  C CD  . ARG A 94  ? 0.6124 0.4462 0.4507 0.0371  0.0003  -0.0392 91  ARG A CD  
693  N NE  . ARG A 94  ? 0.6112 0.4590 0.4488 0.0375  0.0042  -0.0419 91  ARG A NE  
694  C CZ  . ARG A 94  ? 0.6571 0.5051 0.4894 0.0455  0.0082  -0.0475 91  ARG A CZ  
695  N NH1 . ARG A 94  ? 0.6874 0.5214 0.5147 0.0547  0.0085  -0.0513 91  ARG A NH1 
696  N NH2 . ARG A 94  ? 0.6646 0.5258 0.4953 0.0445  0.0119  -0.0493 91  ARG A NH2 
697  N N   . PRO A 95  ? 0.5507 0.3373 0.3806 0.0026  -0.0146 -0.0296 92  PRO A N   
698  C CA  . PRO A 95  ? 0.5491 0.3245 0.3777 -0.0037 -0.0170 -0.0263 92  PRO A CA  
699  C C   . PRO A 95  ? 0.5647 0.3288 0.3917 0.0028  -0.0175 -0.0230 92  PRO A C   
700  O O   . PRO A 95  ? 0.5428 0.3054 0.3720 -0.0012 -0.0190 -0.0180 92  PRO A O   
701  C CB  . PRO A 95  ? 0.5810 0.3396 0.3996 -0.0103 -0.0183 -0.0312 92  PRO A CB  
702  C CG  . PRO A 95  ? 0.5968 0.3571 0.4105 -0.0066 -0.0168 -0.0378 92  PRO A CG  
703  C CD  . PRO A 95  ? 0.5733 0.3543 0.3952 -0.0001 -0.0143 -0.0360 92  PRO A CD  
704  N N   . GLU A 96  ? 0.5978 0.3539 0.4203 0.0130  -0.0163 -0.0259 93  GLU A N   
705  C CA  . GLU A 96  ? 0.6269 0.3701 0.4464 0.0208  -0.0173 -0.0231 93  GLU A CA  
706  C C   . GLU A 96  ? 0.5931 0.3549 0.4238 0.0254  -0.0175 -0.0174 93  GLU A C   
707  O O   . GLU A 96  ? 0.5965 0.3513 0.4263 0.0305  -0.0192 -0.0136 93  GLU A O   
708  C CB  . GLU A 96  ? 0.6808 0.4100 0.4922 0.0314  -0.0161 -0.0285 93  GLU A CB  
709  C CG  . GLU A 96  ? 0.6980 0.4454 0.5158 0.0412  -0.0130 -0.0314 93  GLU A CG  
710  C CD  . GLU A 96  ? 0.7150 0.4734 0.5326 0.0380  -0.0104 -0.0367 93  GLU A CD  
711  O OE1 . GLU A 96  ? 0.7145 0.4668 0.5268 0.0278  -0.0114 -0.0390 93  GLU A OE1 
712  O OE2 . GLU A 96  ? 0.7350 0.5095 0.5580 0.0456  -0.0073 -0.0384 93  GLU A OE2 
713  N N   . LEU A 97  ? 0.5492 0.3334 0.3894 0.0233  -0.0162 -0.0170 94  LEU A N   
714  C CA  . LEU A 97  ? 0.5252 0.3284 0.3763 0.0267  -0.0164 -0.0123 94  LEU A CA  
715  C C   . LEU A 97  ? 0.4986 0.3066 0.3536 0.0178  -0.0185 -0.0071 94  LEU A C   
716  O O   . LEU A 97  ? 0.4762 0.2948 0.3379 0.0198  -0.0198 -0.0028 94  LEU A O   
717  C CB  . LEU A 97  ? 0.5059 0.3293 0.3641 0.0286  -0.0135 -0.0146 94  LEU A CB  
718  C CG  . LEU A 97  ? 0.5270 0.3499 0.3827 0.0387  -0.0107 -0.0196 94  LEU A CG  
719  C CD1 . LEU A 97  ? 0.5046 0.3501 0.3683 0.0402  -0.0074 -0.0206 94  LEU A CD1 
720  C CD2 . LEU A 97  ? 0.5494 0.3659 0.4052 0.0497  -0.0118 -0.0183 94  LEU A CD2 
721  N N   . VAL A 98  ? 0.4933 0.2935 0.3440 0.0084  -0.0191 -0.0077 95  VAL A N   
722  C CA  . VAL A 98  ? 0.4676 0.2759 0.3229 -0.0001 -0.0202 -0.0039 95  VAL A CA  
723  C C   . VAL A 98  ? 0.4786 0.2796 0.3321 0.0000  -0.0222 0.0012  95  VAL A C   
724  O O   . VAL A 98  ? 0.4507 0.2635 0.3103 -0.0002 -0.0231 0.0050  95  VAL A O   
725  C CB  . VAL A 98  ? 0.4603 0.2646 0.3124 -0.0096 -0.0202 -0.0064 95  VAL A CB  
726  C CG1 . VAL A 98  ? 0.4409 0.2505 0.2966 -0.0173 -0.0212 -0.0026 95  VAL A CG1 
727  C CG2 . VAL A 98  ? 0.4481 0.2632 0.3026 -0.0101 -0.0188 -0.0103 95  VAL A CG2 
728  N N   . ARG A 99  ? 0.5091 0.2903 0.3535 0.0002  -0.0229 0.0015  96  ARG A N   
729  C CA  . ARG A 99  ? 0.5362 0.3093 0.3772 -0.0008 -0.0247 0.0070  96  ARG A CA  
730  C C   . ARG A 99  ? 0.5321 0.3114 0.3765 0.0090  -0.0262 0.0102  96  ARG A C   
731  O O   . ARG A 99  ? 0.5193 0.3055 0.3665 0.0076  -0.0278 0.0147  96  ARG A O   
732  C CB  . ARG A 99  ? 0.5894 0.3384 0.4187 -0.0039 -0.0250 0.0070  96  ARG A CB  
733  C CG  . ARG A 99  ? 0.6143 0.3545 0.4388 -0.0044 -0.0266 0.0133  96  ARG A CG  
734  C CD  . ARG A 99  ? 0.6711 0.3883 0.4841 -0.0106 -0.0266 0.0142  96  ARG A CD  
735  N NE  . ARG A 99  ? 0.7081 0.4162 0.5152 -0.0086 -0.0282 0.0207  96  ARG A NE  
736  C CZ  . ARG A 99  ? 0.7503 0.4397 0.5470 -0.0149 -0.0282 0.0241  96  ARG A CZ  
737  N NH1 . ARG A 99  ? 0.7574 0.4359 0.5497 -0.0238 -0.0267 0.0209  96  ARG A NH1 
738  N NH2 . ARG A 99  ? 0.7646 0.4467 0.5552 -0.0128 -0.0298 0.0305  96  ARG A NH2 
739  N N   . PRO A 100 ? 0.5544 0.3333 0.3994 0.0192  -0.0260 0.0077  97  PRO A N   
740  C CA  . PRO A 100 ? 0.5445 0.3331 0.3948 0.0286  -0.0279 0.0106  97  PRO A CA  
741  C C   . PRO A 100 ? 0.5012 0.3142 0.3632 0.0260  -0.0279 0.0120  97  PRO A C   
742  O O   . PRO A 100 ? 0.4737 0.2947 0.3395 0.0287  -0.0305 0.0161  97  PRO A O   
743  C CB  . PRO A 100 ? 0.5745 0.3602 0.4243 0.0394  -0.0267 0.0065  97  PRO A CB  
744  C CG  . PRO A 100 ? 0.6033 0.3678 0.4423 0.0362  -0.0253 0.0024  97  PRO A CG  
745  C CD  . PRO A 100 ? 0.5812 0.3494 0.4210 0.0230  -0.0243 0.0021  97  PRO A CD  
746  N N   . ALA A 101 ? 0.4683 0.2917 0.3349 0.0200  -0.0256 0.0090  98  ALA A N   
747  C CA  . ALA A 101 ? 0.4399 0.2838 0.3163 0.0164  -0.0256 0.0103  98  ALA A CA  
748  C C   . ALA A 101 ? 0.4301 0.2729 0.3052 0.0097  -0.0277 0.0144  98  ALA A C   
749  O O   . ALA A 101 ? 0.4132 0.2673 0.2936 0.0104  -0.0296 0.0171  98  ALA A O   
750  C CB  . ALA A 101 ? 0.4223 0.2750 0.3020 0.0121  -0.0229 0.0067  98  ALA A CB  
751  N N   . LEU A 102 ? 0.4376 0.2674 0.3057 0.0032  -0.0272 0.0146  99  LEU A N   
752  C CA  . LEU A 102 ? 0.4351 0.2644 0.3015 -0.0031 -0.0284 0.0182  99  LEU A CA  
753  C C   . LEU A 102 ? 0.4554 0.2787 0.3176 0.0019  -0.0311 0.0227  99  LEU A C   
754  O O   . LEU A 102 ? 0.4415 0.2734 0.3062 0.0009  -0.0329 0.0254  99  LEU A O   
755  C CB  . LEU A 102 ? 0.4395 0.2575 0.2999 -0.0110 -0.0268 0.0172  99  LEU A CB  
756  C CG  . LEU A 102 ? 0.4297 0.2459 0.2872 -0.0176 -0.0270 0.0206  99  LEU A CG  
757  C CD1 . LEU A 102 ? 0.4004 0.2328 0.2647 -0.0198 -0.0275 0.0214  99  LEU A CD1 
758  C CD2 . LEU A 102 ? 0.4416 0.2502 0.2954 -0.0259 -0.0251 0.0189  99  LEU A CD2 
759  N N   . GLU A 103 ? 0.4880 0.2969 0.3437 0.0078  -0.0318 0.0232  100 GLU A N   
760  C CA  . GLU A 103 ? 0.5269 0.3282 0.3772 0.0135  -0.0349 0.0279  100 GLU A CA  
761  C C   . GLU A 103 ? 0.5111 0.3305 0.3703 0.0199  -0.0375 0.0290  100 GLU A C   
762  O O   . GLU A 103 ? 0.5048 0.3258 0.3621 0.0207  -0.0406 0.0332  100 GLU A O   
763  C CB  . GLU A 103 ? 0.5769 0.3573 0.4179 0.0193  -0.0352 0.0278  100 GLU A CB  
764  C CG  . GLU A 103 ? 0.6144 0.3752 0.4450 0.0111  -0.0336 0.0282  100 GLU A CG  
765  C CD  . GLU A 103 ? 0.6745 0.4117 0.4946 0.0153  -0.0337 0.0274  100 GLU A CD  
766  O OE1 . GLU A 103 ? 0.7150 0.4512 0.5367 0.0250  -0.0340 0.0244  100 GLU A OE1 
767  O OE2 . GLU A 103 ? 0.7182 0.4376 0.5284 0.0085  -0.0331 0.0295  100 GLU A OE2 
768  N N   . ASN A 104 ? 0.5123 0.3457 0.3809 0.0235  -0.0362 0.0254  101 ASN A N   
769  C CA  . ASN A 104 ? 0.5119 0.3651 0.3908 0.0286  -0.0382 0.0259  101 ASN A CA  
770  C C   . ASN A 104 ? 0.4779 0.3429 0.3607 0.0207  -0.0393 0.0274  101 ASN A C   
771  O O   . ASN A 104 ? 0.4615 0.3338 0.3462 0.0225  -0.0428 0.0304  101 ASN A O   
772  C CB  . ASN A 104 ? 0.5429 0.4078 0.4300 0.0331  -0.0357 0.0217  101 ASN A CB  
773  C CG  . ASN A 104 ? 0.5801 0.4669 0.4787 0.0370  -0.0375 0.0225  101 ASN A CG  
774  O OD1 . ASN A 104 ? 0.6398 0.5416 0.5458 0.0313  -0.0365 0.0217  101 ASN A OD1 
775  N ND2 . ASN A 104 ? 0.6094 0.4981 0.5093 0.0465  -0.0405 0.0243  101 ASN A ND2 
776  N N   . SER A 105 ? 0.4543 0.3195 0.3371 0.0122  -0.0366 0.0256  102 SER A N   
777  C CA  . SER A 105 ? 0.4327 0.3071 0.3182 0.0052  -0.0375 0.0266  102 SER A CA  
778  C C   . SER A 105 ? 0.4315 0.2975 0.3091 0.0037  -0.0400 0.0305  102 SER A C   
779  O O   . SER A 105 ? 0.4157 0.2905 0.2952 0.0024  -0.0426 0.0321  102 SER A O   
780  C CB  . SER A 105 ? 0.4215 0.2969 0.3081 -0.0022 -0.0345 0.0239  102 SER A CB  
781  O OG  . SER A 105 ? 0.4442 0.3311 0.3384 -0.0016 -0.0329 0.0212  102 SER A OG  
782  N N   . LEU A 106 ? 0.4394 0.2886 0.3075 0.0027  -0.0389 0.0319  103 LEU A N   
783  C CA  . LEU A 106 ? 0.4525 0.2929 0.3114 0.0005  -0.0406 0.0360  103 LEU A CA  
784  C C   . LEU A 106 ? 0.4802 0.3228 0.3380 0.0081  -0.0452 0.0395  103 LEU A C   
785  O O   . LEU A 106 ? 0.4766 0.3220 0.3311 0.0064  -0.0476 0.0422  103 LEU A O   
786  C CB  . LEU A 106 ? 0.4637 0.2852 0.3128 -0.0023 -0.0383 0.0370  103 LEU A CB  
787  C CG  . LEU A 106 ? 0.4484 0.2694 0.2986 -0.0108 -0.0343 0.0340  103 LEU A CG  
788  C CD1 . LEU A 106 ? 0.4697 0.2728 0.3116 -0.0138 -0.0323 0.0343  103 LEU A CD1 
789  C CD2 . LEU A 106 ? 0.4326 0.2618 0.2834 -0.0175 -0.0336 0.0346  103 LEU A CD2 
790  N N   . LYS A 107 ? 0.5013 0.3431 0.3616 0.0168  -0.0465 0.0392  104 LYS A N   
791  C CA  . LYS A 107 ? 0.5377 0.3839 0.3986 0.0254  -0.0514 0.0423  104 LYS A CA  
792  C C   . LYS A 107 ? 0.5142 0.3819 0.3850 0.0240  -0.0540 0.0416  104 LYS A C   
793  O O   . LYS A 107 ? 0.4947 0.3655 0.3626 0.0256  -0.0585 0.0449  104 LYS A O   
794  C CB  . LYS A 107 ? 0.5707 0.4145 0.4345 0.0356  -0.0516 0.0409  104 LYS A CB  
795  C CG  . LYS A 107 ? 0.6147 0.4599 0.4774 0.0457  -0.0570 0.0447  104 LYS A CG  
796  C CD  . LYS A 107 ? 0.6624 0.5117 0.5314 0.0574  -0.0575 0.0428  104 LYS A CD  
797  C CE  . LYS A 107 ? 0.7360 0.5643 0.5942 0.0667  -0.0594 0.0454  104 LYS A CE  
798  N NZ  . LYS A 107 ? 0.7836 0.6054 0.6332 0.0697  -0.0650 0.0517  104 LYS A NZ  
799  N N   . LYS A 108 ? 0.4978 0.3792 0.3790 0.0210  -0.0516 0.0377  105 LYS A N   
800  C CA  . LYS A 108 ? 0.4826 0.3838 0.3735 0.0189  -0.0540 0.0369  105 LYS A CA  
801  C C   . LYS A 108 ? 0.4522 0.3522 0.3377 0.0111  -0.0552 0.0380  105 LYS A C   
802  O O   . LYS A 108 ? 0.4321 0.3409 0.3188 0.0114  -0.0596 0.0394  105 LYS A O   
803  C CB  . LYS A 108 ? 0.4968 0.4107 0.3982 0.0157  -0.0507 0.0330  105 LYS A CB  
804  C CG  . LYS A 108 ? 0.5465 0.4650 0.4543 0.0227  -0.0485 0.0309  105 LYS A CG  
805  C CD  . LYS A 108 ? 0.6123 0.5358 0.5230 0.0331  -0.0521 0.0327  105 LYS A CD  
806  C CE  . LYS A 108 ? 0.6516 0.5901 0.5735 0.0391  -0.0502 0.0300  105 LYS A CE  
807  N NZ  . LYS A 108 ? 0.6719 0.6332 0.6055 0.0386  -0.0532 0.0305  105 LYS A NZ  
808  N N   . ALA A 109 ? 0.4298 0.3196 0.3094 0.0048  -0.0515 0.0371  106 ALA A N   
809  C CA  . ALA A 109 ? 0.4255 0.3144 0.3000 -0.0023 -0.0516 0.0373  106 ALA A CA  
810  C C   . ALA A 109 ? 0.4457 0.3238 0.3083 -0.0012 -0.0539 0.0415  106 ALA A C   
811  O O   . ALA A 109 ? 0.4400 0.3185 0.2974 -0.0059 -0.0545 0.0419  106 ALA A O   
812  C CB  . ALA A 109 ? 0.4044 0.2881 0.2779 -0.0087 -0.0468 0.0348  106 ALA A CB  
813  N N   . GLN A 110 ? 0.4633 0.3309 0.3206 0.0047  -0.0547 0.0444  107 GLN A N   
814  C CA  . GLN A 110 ? 0.5055 0.3594 0.3495 0.0055  -0.0562 0.0491  107 GLN A CA  
815  C C   . GLN A 110 ? 0.4878 0.3339 0.3241 -0.0031 -0.0520 0.0490  107 GLN A C   
816  O O   . GLN A 110 ? 0.4787 0.3218 0.3058 -0.0054 -0.0533 0.0518  107 GLN A O   
817  C CB  . GLN A 110 ? 0.5478 0.4086 0.3895 0.0097  -0.0625 0.0521  107 GLN A CB  
818  C CG  . GLN A 110 ? 0.5975 0.4615 0.4437 0.0199  -0.0666 0.0536  107 GLN A CG  
819  C CD  . GLN A 110 ? 0.6301 0.4747 0.4672 0.0250  -0.0656 0.0568  107 GLN A CD  
820  O OE1 . GLN A 110 ? 0.6872 0.5178 0.5109 0.0242  -0.0665 0.0612  107 GLN A OE1 
821  N NE2 . GLN A 110 ? 0.6188 0.4613 0.4617 0.0303  -0.0638 0.0546  107 GLN A NE2 
822  N N   . LEU A 111 ? 0.4643 0.3063 0.3032 -0.0072 -0.0472 0.0463  108 LEU A N   
823  C CA  . LEU A 111 ? 0.4741 0.3083 0.3067 -0.0148 -0.0427 0.0463  108 LEU A CA  
824  C C   . LEU A 111 ? 0.4921 0.3103 0.3192 -0.0146 -0.0405 0.0478  108 LEU A C   
825  O O   . LEU A 111 ? 0.4969 0.3131 0.3282 -0.0091 -0.0415 0.0466  108 LEU A O   
826  C CB  . LEU A 111 ? 0.4599 0.3045 0.3015 -0.0198 -0.0397 0.0414  108 LEU A CB  
827  C CG  . LEU A 111 ? 0.4633 0.3210 0.3091 -0.0208 -0.0418 0.0396  108 LEU A CG  
828  C CD1 . LEU A 111 ? 0.4443 0.3105 0.2992 -0.0241 -0.0394 0.0350  108 LEU A CD1 
829  C CD2 . LEU A 111 ? 0.4830 0.3382 0.3191 -0.0242 -0.0417 0.0415  108 LEU A CD2 
830  N N   . ASP A 112 ? 0.5032 0.3113 0.3217 -0.0207 -0.0374 0.0498  109 ASP A N   
831  C CA  . ASP A 112 ? 0.5420 0.3332 0.3542 -0.0226 -0.0351 0.0512  109 ASP A CA  
832  C C   . ASP A 112 ? 0.5237 0.3181 0.3437 -0.0275 -0.0314 0.0461  109 ASP A C   
833  O O   . ASP A 112 ? 0.5403 0.3230 0.3582 -0.0275 -0.0304 0.0454  109 ASP A O   
834  C CB  . ASP A 112 ? 0.5787 0.3585 0.3779 -0.0281 -0.0333 0.0562  109 ASP A CB  
835  C CG  . ASP A 112 ? 0.6161 0.3907 0.4058 -0.0226 -0.0376 0.0616  109 ASP A CG  
836  O OD1 . ASP A 112 ? 0.6311 0.4009 0.4207 -0.0142 -0.0416 0.0629  109 ASP A OD1 
837  O OD2 . ASP A 112 ? 0.6515 0.4284 0.4344 -0.0261 -0.0371 0.0642  109 ASP A OD2 
838  N N   . TYR A 113 ? 0.4884 0.2973 0.3163 -0.0314 -0.0297 0.0427  110 TYR A N   
839  C CA  . TYR A 113 ? 0.4812 0.2944 0.3161 -0.0363 -0.0266 0.0382  110 TYR A CA  
840  C C   . TYR A 113 ? 0.4500 0.2800 0.2947 -0.0355 -0.0271 0.0347  110 TYR A C   
841  O O   . TYR A 113 ? 0.4469 0.2834 0.2911 -0.0339 -0.0288 0.0359  110 TYR A O   
842  C CB  . TYR A 113 ? 0.4989 0.3069 0.3290 -0.0450 -0.0227 0.0390  110 TYR A CB  
843  C CG  . TYR A 113 ? 0.4993 0.3160 0.3281 -0.0489 -0.0209 0.0400  110 TYR A CG  
844  C CD1 . TYR A 113 ? 0.4780 0.3090 0.3151 -0.0514 -0.0193 0.0361  110 TYR A CD1 
845  C CD2 . TYR A 113 ? 0.5352 0.3451 0.3533 -0.0498 -0.0209 0.0449  110 TYR A CD2 
846  C CE1 . TYR A 113 ? 0.4894 0.3280 0.3248 -0.0539 -0.0175 0.0364  110 TYR A CE1 
847  C CE2 . TYR A 113 ? 0.5310 0.3491 0.3469 -0.0530 -0.0189 0.0453  110 TYR A CE2 
848  C CZ  . TYR A 113 ? 0.5059 0.3385 0.3306 -0.0547 -0.0172 0.0408  110 TYR A CZ  
849  O OH  . TYR A 113 ? 0.5186 0.3587 0.3406 -0.0569 -0.0152 0.0406  110 TYR A OH  
850  N N   . VAL A 114 ? 0.4200 0.2557 0.2722 -0.0367 -0.0259 0.0306  111 VAL A N   
851  C CA  . VAL A 114 ? 0.3901 0.2399 0.2502 -0.0378 -0.0257 0.0276  111 VAL A CA  
852  C C   . VAL A 114 ? 0.3923 0.2444 0.2533 -0.0444 -0.0224 0.0259  111 VAL A C   
853  O O   . VAL A 114 ? 0.4002 0.2452 0.2587 -0.0481 -0.0206 0.0259  111 VAL A O   
854  C CB  . VAL A 114 ? 0.3733 0.2289 0.2409 -0.0344 -0.0267 0.0247  111 VAL A CB  
855  C CG1 . VAL A 114 ? 0.3741 0.2292 0.2420 -0.0277 -0.0294 0.0262  111 VAL A CG1 
856  C CG2 . VAL A 114 ? 0.3761 0.2270 0.2445 -0.0365 -0.0249 0.0222  111 VAL A CG2 
857  N N   . ASP A 115 ? 0.3742 0.2361 0.2385 -0.0458 -0.0219 0.0245  112 ASP A N   
858  C CA  . ASP A 115 ? 0.3686 0.2357 0.2356 -0.0509 -0.0189 0.0224  112 ASP A CA  
859  C C   . ASP A 115 ? 0.3564 0.2268 0.2301 -0.0513 -0.0190 0.0191  112 ASP A C   
860  O O   . ASP A 115 ? 0.3590 0.2318 0.2349 -0.0557 -0.0171 0.0175  112 ASP A O   
861  C CB  . ASP A 115 ? 0.3640 0.2396 0.2320 -0.0508 -0.0184 0.0214  112 ASP A CB  
862  C CG  . ASP A 115 ? 0.3805 0.2519 0.2399 -0.0510 -0.0181 0.0247  112 ASP A CG  
863  O OD1 . ASP A 115 ? 0.3705 0.2401 0.2271 -0.0471 -0.0212 0.0262  112 ASP A OD1 
864  O OD2 . ASP A 115 ? 0.4024 0.2723 0.2578 -0.0553 -0.0149 0.0259  112 ASP A OD2 
865  N N   . LEU A 116 ? 0.3446 0.2170 0.2217 -0.0470 -0.0213 0.0180  113 LEU A N   
866  C CA  . LEU A 116 ? 0.3354 0.2117 0.2179 -0.0470 -0.0216 0.0150  113 LEU A CA  
867  C C   . LEU A 116 ? 0.3321 0.2054 0.2148 -0.0426 -0.0231 0.0149  113 LEU A C   
868  O O   . LEU A 116 ? 0.3421 0.2173 0.2252 -0.0390 -0.0247 0.0163  113 LEU A O   
869  C CB  . LEU A 116 ? 0.3200 0.2061 0.2075 -0.0467 -0.0219 0.0132  113 LEU A CB  
870  C CG  . LEU A 116 ? 0.3072 0.1978 0.1993 -0.0466 -0.0226 0.0106  113 LEU A CG  
871  C CD1 . LEU A 116 ? 0.3194 0.2095 0.2121 -0.0506 -0.0214 0.0089  113 LEU A CD1 
872  C CD2 . LEU A 116 ? 0.3026 0.2007 0.1982 -0.0454 -0.0234 0.0095  113 LEU A CD2 
873  N N   . TYR A 117 ? 0.3390 0.2081 0.2214 -0.0431 -0.0227 0.0131  114 TYR A N   
874  C CA  . TYR A 117 ? 0.3374 0.2052 0.2203 -0.0387 -0.0235 0.0121  114 TYR A CA  
875  C C   . TYR A 117 ? 0.3266 0.1997 0.2128 -0.0397 -0.0234 0.0090  114 TYR A C   
876  O O   . TYR A 117 ? 0.3174 0.1888 0.2029 -0.0437 -0.0229 0.0071  114 TYR A O   
877  C CB  . TYR A 117 ? 0.3583 0.2139 0.2356 -0.0370 -0.0233 0.0124  114 TYR A CB  
878  C CG  . TYR A 117 ? 0.3593 0.2142 0.2370 -0.0303 -0.0240 0.0122  114 TYR A CG  
879  C CD1 . TYR A 117 ? 0.3474 0.2100 0.2287 -0.0264 -0.0252 0.0140  114 TYR A CD1 
880  C CD2 . TYR A 117 ? 0.3691 0.2157 0.2434 -0.0278 -0.0235 0.0100  114 TYR A CD2 
881  C CE1 . TYR A 117 ? 0.3517 0.2163 0.2347 -0.0202 -0.0256 0.0139  114 TYR A CE1 
882  C CE2 . TYR A 117 ? 0.3733 0.2204 0.2482 -0.0208 -0.0237 0.0095  114 TYR A CE2 
883  C CZ  . TYR A 117 ? 0.3694 0.2261 0.2492 -0.0168 -0.0247 0.0118  114 TYR A CZ  
884  O OH  . TYR A 117 ? 0.3864 0.2464 0.2683 -0.0099 -0.0247 0.0112  114 TYR A OH  
885  N N   . LEU A 118 ? 0.3176 0.1972 0.2069 -0.0367 -0.0240 0.0087  115 LEU A N   
886  C CA  . LEU A 118 ? 0.3128 0.1972 0.2039 -0.0372 -0.0240 0.0064  115 LEU A CA  
887  C C   . LEU A 118 ? 0.3165 0.1992 0.2060 -0.0337 -0.0234 0.0050  115 LEU A C   
888  O O   . LEU A 118 ? 0.3158 0.1993 0.2061 -0.0299 -0.0231 0.0062  115 LEU A O   
889  C CB  . LEU A 118 ? 0.3045 0.1973 0.1994 -0.0371 -0.0249 0.0076  115 LEU A CB  
890  C CG  . LEU A 118 ? 0.2961 0.1910 0.1923 -0.0393 -0.0254 0.0085  115 LEU A CG  
891  C CD1 . LEU A 118 ? 0.2922 0.1927 0.1908 -0.0388 -0.0265 0.0091  115 LEU A CD1 
892  C CD2 . LEU A 118 ? 0.2962 0.1907 0.1922 -0.0427 -0.0250 0.0069  115 LEU A CD2 
893  N N   . ILE A 119 ? 0.3214 0.2041 0.2092 -0.0349 -0.0232 0.0022  116 ILE A N   
894  C CA  . ILE A 119 ? 0.3246 0.2098 0.2113 -0.0317 -0.0222 0.0008  116 ILE A CA  
895  C C   . ILE A 119 ? 0.3095 0.2043 0.2003 -0.0316 -0.0225 0.0030  116 ILE A C   
896  O O   . ILE A 119 ? 0.3086 0.2066 0.2001 -0.0344 -0.0236 0.0032  116 ILE A O   
897  C CB  . ILE A 119 ? 0.3453 0.2274 0.2277 -0.0336 -0.0224 -0.0029 116 ILE A CB  
898  C CG1 . ILE A 119 ? 0.3699 0.2408 0.2479 -0.0350 -0.0224 -0.0051 116 ILE A CG1 
899  C CG2 . ILE A 119 ? 0.3521 0.2376 0.2323 -0.0303 -0.0210 -0.0043 116 ILE A CG2 
900  C CD1 . ILE A 119 ? 0.3906 0.2573 0.2634 -0.0370 -0.0229 -0.0094 116 ILE A CD1 
901  N N   . HIS A 120 ? 0.2996 0.1989 0.1929 -0.0286 -0.0216 0.0046  117 HIS A N   
902  C CA  . HIS A 120 ? 0.2975 0.2048 0.1946 -0.0295 -0.0219 0.0071  117 HIS A CA  
903  C C   . HIS A 120 ? 0.2944 0.2051 0.1895 -0.0310 -0.0214 0.0066  117 HIS A C   
904  O O   . HIS A 120 ? 0.2776 0.1913 0.1737 -0.0334 -0.0225 0.0086  117 HIS A O   
905  C CB  . HIS A 120 ? 0.3031 0.2159 0.2039 -0.0263 -0.0210 0.0085  117 HIS A CB  
906  C CG  . HIS A 120 ? 0.2977 0.2169 0.2028 -0.0285 -0.0223 0.0113  117 HIS A CG  
907  N ND1 . HIS A 120 ? 0.3078 0.2316 0.2169 -0.0269 -0.0230 0.0128  117 HIS A ND1 
908  C CD2 . HIS A 120 ? 0.2894 0.2103 0.1947 -0.0323 -0.0232 0.0125  117 HIS A CD2 
909  C CE1 . HIS A 120 ? 0.2966 0.2246 0.2082 -0.0303 -0.0244 0.0146  117 HIS A CE1 
910  N NE2 . HIS A 120 ? 0.2837 0.2090 0.1926 -0.0335 -0.0244 0.0146  117 HIS A NE2 
911  N N   . SER A 121 ? 0.3035 0.2128 0.1947 -0.0294 -0.0199 0.0040  118 SER A N   
912  C CA  . SER A 121 ? 0.3123 0.2252 0.2002 -0.0303 -0.0191 0.0039  118 SER A CA  
913  C C   . SER A 121 ? 0.3293 0.2378 0.2112 -0.0290 -0.0183 0.0000  118 SER A C   
914  O O   . SER A 121 ? 0.3392 0.2438 0.2202 -0.0261 -0.0171 -0.0023 118 SER A O   
915  C CB  . SER A 121 ? 0.3155 0.2360 0.2057 -0.0292 -0.0168 0.0058  118 SER A CB  
916  O OG  . SER A 121 ? 0.3286 0.2521 0.2141 -0.0295 -0.0150 0.0053  118 SER A OG  
917  N N   . PRO A 122 ? 0.3380 0.2466 0.2151 -0.0309 -0.0193 -0.0010 119 PRO A N   
918  C CA  . PRO A 122 ? 0.3504 0.2548 0.2207 -0.0300 -0.0189 -0.0053 119 PRO A CA  
919  C C   . PRO A 122 ? 0.3733 0.2809 0.2399 -0.0266 -0.0152 -0.0066 119 PRO A C   
920  O O   . PRO A 122 ? 0.3883 0.2912 0.2486 -0.0249 -0.0143 -0.0109 119 PRO A O   
921  C CB  . PRO A 122 ? 0.3497 0.2550 0.2167 -0.0332 -0.0219 -0.0053 119 PRO A CB  
922  C CG  . PRO A 122 ? 0.3381 0.2487 0.2077 -0.0341 -0.0224 -0.0007 119 PRO A CG  
923  C CD  . PRO A 122 ? 0.3291 0.2408 0.2059 -0.0336 -0.0214 0.0017  119 PRO A CD  
924  N N   . MET A 123 ? 0.3694 0.2848 0.2400 -0.0257 -0.0128 -0.0033 120 MET A N   
925  C CA  . MET A 123 ? 0.3839 0.3058 0.2520 -0.0231 -0.0086 -0.0038 120 MET A CA  
926  C C   . MET A 123 ? 0.3854 0.3079 0.2568 -0.0177 -0.0060 -0.0061 120 MET A C   
927  O O   . MET A 123 ? 0.3842 0.3145 0.2628 -0.0166 -0.0045 -0.0034 120 MET A O   
928  C CB  . MET A 123 ? 0.3872 0.3180 0.2587 -0.0260 -0.0076 0.0012  120 MET A CB  
929  C CG  . MET A 123 ? 0.3997 0.3284 0.2657 -0.0300 -0.0101 0.0032  120 MET A CG  
930  S SD  . MET A 123 ? 0.4033 0.3381 0.2703 -0.0341 -0.0092 0.0094  120 MET A SD  
931  C CE  . MET A 123 ? 0.4111 0.3453 0.2879 -0.0359 -0.0119 0.0121  120 MET A CE  
932  N N   . SER A 124 ? 0.3893 0.3031 0.2554 -0.0146 -0.0059 -0.0109 121 SER A N   
933  C CA  . SER A 124 ? 0.4041 0.3152 0.2711 -0.0080 -0.0036 -0.0138 121 SER A CA  
934  C C   . SER A 124 ? 0.4188 0.3428 0.2893 -0.0037 0.0011  -0.0132 121 SER A C   
935  O O   . SER A 124 ? 0.4370 0.3671 0.3029 -0.0046 0.0039  -0.0139 121 SER A O   
936  C CB  . SER A 124 ? 0.4176 0.3168 0.2754 -0.0061 -0.0038 -0.0195 121 SER A CB  
937  O OG  . SER A 124 ? 0.4183 0.3082 0.2736 -0.0114 -0.0080 -0.0199 121 SER A OG  
938  N N   . LEU A 125 ? 0.4223 0.3502 0.3001 0.0012  0.0020  -0.0125 122 LEU A N   
939  C CA  . LEU A 125 ? 0.4343 0.3763 0.3172 0.0064  0.0065  -0.0126 122 LEU A CA  
940  C C   . LEU A 125 ? 0.4606 0.3970 0.3424 0.0158  0.0079  -0.0169 122 LEU A C   
941  O O   . LEU A 125 ? 0.4583 0.3804 0.3375 0.0175  0.0047  -0.0181 122 LEU A O   
942  C CB  . LEU A 125 ? 0.4144 0.3690 0.3088 0.0040  0.0057  -0.0073 122 LEU A CB  
943  C CG  . LEU A 125 ? 0.4085 0.3657 0.3038 -0.0048 0.0037  -0.0028 122 LEU A CG  
944  C CD1 . LEU A 125 ? 0.4076 0.3756 0.3134 -0.0071 0.0026  0.0016  122 LEU A CD1 
945  C CD2 . LEU A 125 ? 0.4158 0.3782 0.3055 -0.0084 0.0068  -0.0024 122 LEU A CD2 
946  N N   . LYS A 126 ? 0.5004 0.4479 0.3837 0.0217  0.0128  -0.0191 123 LYS A N   
947  C CA  . LYS A 126 ? 0.5545 0.4984 0.4365 0.0324  0.0150  -0.0238 123 LYS A CA  
948  C C   . LYS A 126 ? 0.5471 0.4886 0.4368 0.0364  0.0115  -0.0214 123 LYS A C   
949  O O   . LYS A 126 ? 0.5318 0.4864 0.4318 0.0341  0.0105  -0.0167 123 LYS A O   
950  C CB  . LYS A 126 ? 0.5941 0.5566 0.4799 0.0374  0.0213  -0.0253 123 LYS A CB  
951  C CG  . LYS A 126 ? 0.6423 0.6047 0.5283 0.0500  0.0243  -0.0304 123 LYS A CG  
952  C CD  . LYS A 126 ? 0.6761 0.6573 0.5643 0.0546  0.0314  -0.0328 123 LYS A CD  
953  C CE  . LYS A 126 ? 0.7205 0.7034 0.6101 0.0685  0.0345  -0.0379 123 LYS A CE  
954  N NZ  . LYS A 126 ? 0.7351 0.7360 0.6407 0.0736  0.0343  -0.0345 123 LYS A NZ  
955  N N   . PRO A 127 ? 0.5948 0.5199 0.4792 0.0428  0.0097  -0.0244 124 PRO A N   
956  C CA  . PRO A 127 ? 0.6215 0.5439 0.5119 0.0476  0.0064  -0.0217 124 PRO A CA  
957  C C   . PRO A 127 ? 0.6578 0.5994 0.5587 0.0564  0.0092  -0.0215 124 PRO A C   
958  O O   . PRO A 127 ? 0.6432 0.5961 0.5447 0.0599  0.0142  -0.0245 124 PRO A O   
959  C CB  . PRO A 127 ? 0.6405 0.5390 0.5202 0.0529  0.0046  -0.0257 124 PRO A CB  
960  C CG  . PRO A 127 ? 0.6422 0.5299 0.5105 0.0478  0.0059  -0.0301 124 PRO A CG  
961  C CD  . PRO A 127 ? 0.6334 0.5401 0.5048 0.0451  0.0102  -0.0304 124 PRO A CD  
962  N N   . GLY A 128 ? 1.1782 0.8899 0.9706 -0.0764 0.0215  0.0329  125 GLY A N   
963  C CA  . GLY A 128 ? 1.2416 0.9709 1.0438 -0.0070 0.0517  0.0506  125 GLY A CA  
964  C C   . GLY A 128 ? 1.1941 1.0359 1.0790 0.0293  0.0437  0.0635  125 GLY A C   
965  O O   . GLY A 128 ? 1.1962 1.0701 1.1143 0.0066  0.0239  0.0568  125 GLY A O   
966  N N   . GLU A 129 ? 1.2085 1.1174 1.1234 0.0804  0.0586  0.0847  126 GLU A N   
967  C CA  . GLU A 129 ? 1.1263 1.1669 1.1200 0.0997  0.0423  0.0952  126 GLU A CA  
968  C C   . GLU A 129 ? 0.9919 1.1045 1.0551 0.0560  -0.0023 0.0696  126 GLU A C   
969  O O   . GLU A 129 ? 0.9062 1.0721 1.0082 0.0437  -0.0199 0.0625  126 GLU A O   
970  C CB  . GLU A 129 ? 1.1909 1.3078 1.1961 0.1557  0.0678  0.1321  126 GLU A CB  
971  C CG  . GLU A 129 ? 1.1718 1.4168 1.2296 0.1750  0.0598  0.1518  126 GLU A CG  
972  C CD  . GLU A 129 ? 1.2643 1.6051 1.3287 0.2371  0.0909  0.2049  126 GLU A CD  
973  O OE1 . GLU A 129 ? 1.2044 1.6859 1.3276 0.2248  0.0677  0.2152  126 GLU A OE1 
974  O OE2 . GLU A 129 ? 1.4237 1.6985 1.4279 0.2971  0.1427  0.2401  126 GLU A OE2 
975  N N   . GLU A 130 ? 0.9634 1.0633 1.0304 0.0367  -0.0131 0.0580  127 GLU A N   
976  C CA  . GLU A 130 ? 0.8621 1.0189 0.9824 0.0065  -0.0413 0.0401  127 GLU A CA  
977  C C   . GLU A 130 ? 0.8251 0.9542 0.9544 -0.0259 -0.0600 0.0251  127 GLU A C   
978  O O   . GLU A 130 ? 0.8455 0.9139 0.9396 -0.0428 -0.0611 0.0246  127 GLU A O   
979  C CB  . GLU A 130 ? 0.8816 1.0367 1.0002 0.0062  -0.0389 0.0400  127 GLU A CB  
980  C CG  . GLU A 130 ? 0.9302 1.1598 1.0636 0.0348  -0.0243 0.0625  127 GLU A CG  
981  C CD  . GLU A 130 ? 0.9114 1.2501 1.0933 0.0141  -0.0405 0.0598  127 GLU A CD  
982  O OE1 . GLU A 130 ? 0.9046 1.3374 1.1026 0.0323  -0.0322 0.0869  127 GLU A OE1 
983  O OE2 . GLU A 130 ? 0.8761 1.2069 1.0719 -0.0218 -0.0579 0.0343  127 GLU A OE2 
984  N N   . LEU A 131 ? 0.7243 0.8994 0.8918 -0.0364 -0.0711 0.0173  128 LEU A N   
985  C CA  . LEU A 131 ? 0.6578 0.8263 0.8424 -0.0540 -0.0809 0.0145  128 LEU A CA  
986  C C   . LEU A 131 ? 0.6172 0.7747 0.8072 -0.0653 -0.0852 0.0132  128 LEU A C   
987  O O   . LEU A 131 ? 0.5378 0.6946 0.7338 -0.0748 -0.0919 0.0245  128 LEU A O   
988  C CB  . LEU A 131 ? 0.6350 0.8348 0.8393 -0.0530 -0.0781 0.0086  128 LEU A CB  
989  C CG  . LEU A 131 ? 0.6209 0.8384 0.8232 -0.0416 -0.0753 0.0132  128 LEU A CG  
990  C CD1 . LEU A 131 ? 0.6045 0.8352 0.8132 -0.0458 -0.0706 0.0062  128 LEU A CD1 
991  C CD2 . LEU A 131 ? 0.6408 0.8284 0.8319 -0.0409 -0.0758 0.0260  128 LEU A CD2 
992  N N   . SER A 132 ? 0.6335 0.7951 0.8235 -0.0642 -0.0805 0.0052  129 SER A N   
993  C CA  . SER A 132 ? 0.6705 0.8131 0.8563 -0.0697 -0.0810 0.0059  129 SER A CA  
994  C C   . SER A 132 ? 0.7304 0.8536 0.8900 -0.0627 -0.0775 0.0072  129 SER A C   
995  O O   . SER A 132 ? 0.6826 0.8289 0.8480 -0.0557 -0.0697 0.0056  129 SER A O   
996  C CB  . SER A 132 ? 0.6755 0.8219 0.8718 -0.0747 -0.0700 -0.0026 129 SER A CB  
997  O OG  . SER A 132 ? 0.6814 0.8200 0.8847 -0.0711 -0.0613 0.0035  129 SER A OG  
998  N N   . PRO A 133 ? 0.8042 0.8820 0.9248 -0.0669 -0.0792 0.0129  130 PRO A N   
999  C CA  . PRO A 133 ? 0.8733 0.9048 0.9477 -0.0554 -0.0649 0.0159  130 PRO A CA  
1000 C C   . PRO A 133 ? 0.8554 0.8843 0.9337 -0.0620 -0.0687 0.0136  130 PRO A C   
1001 O O   . PRO A 133 ? 0.8586 0.8882 0.9400 -0.0824 -0.0831 0.0148  130 PRO A O   
1002 C CB  . PRO A 133 ? 0.9767 0.9362 0.9860 -0.0732 -0.0617 0.0170  130 PRO A CB  
1003 C CG  . PRO A 133 ? 0.9418 0.9357 0.9783 -0.1065 -0.0868 0.0180  130 PRO A CG  
1004 C CD  . PRO A 133 ? 0.8503 0.9143 0.9575 -0.0895 -0.0912 0.0184  130 PRO A CD  
1005 N N   . THR A 134 ? 0.8305 0.8695 0.9119 -0.0428 -0.0547 0.0167  131 THR A N   
1006 C CA  . THR A 134 ? 0.8108 0.8492 0.8986 -0.0459 -0.0540 0.0155  131 THR A CA  
1007 C C   . THR A 134 ? 0.8793 0.8782 0.9232 -0.0240 -0.0335 0.0254  131 THR A C   
1008 O O   . THR A 134 ? 0.8901 0.8981 0.9237 0.0037  -0.0141 0.0391  131 THR A O   
1009 C CB  . THR A 134 ? 0.7502 0.8461 0.8877 -0.0520 -0.0532 0.0102  131 THR A CB  
1010 O OG1 . THR A 134 ? 0.7250 0.8702 0.8739 -0.0391 -0.0430 0.0191  131 THR A OG1 
1011 C CG2 . THR A 134 ? 0.7105 0.8212 0.8718 -0.0666 -0.0613 0.0022  131 THR A CG2 
1012 N N   . ASP A 135 ? 0.9014 0.8608 0.9175 -0.0305 -0.0334 0.0240  132 ASP A N   
1013 C CA  . ASP A 135 ? 0.9846 0.9016 0.9569 -0.0070 -0.0095 0.0345  132 ASP A CA  
1014 C C   . ASP A 135 ? 0.9443 0.9360 0.9726 0.0100  0.0008  0.0456  132 ASP A C   
1015 O O   . ASP A 135 ? 0.8740 0.9371 0.9608 -0.0060 -0.0111 0.0400  132 ASP A O   
1016 C CB  . ASP A 135 ? 1.0486 0.9053 0.9703 -0.0269 -0.0166 0.0283  132 ASP A CB  
1017 C CG  . ASP A 135 ? 0.9823 0.8837 0.9520 -0.0369 -0.0301 0.0270  132 ASP A CG  
1018 O OD1 . ASP A 135 ? 0.9065 0.8666 0.9386 -0.0323 -0.0287 0.0267  132 ASP A OD1 
1019 O OD2 . ASP A 135 ? 1.0602 0.9322 0.9942 -0.0519 -0.0387 0.0275  132 ASP A OD2 
1020 N N   . GLU A 136 ? 0.9970 0.9678 0.9984 0.0351  0.0239  0.0610  133 GLU A N   
1021 C CA  . GLU A 136 ? 0.9956 1.0447 1.0430 0.0492  0.0374  0.0798  133 GLU A CA  
1022 C C   . GLU A 136 ? 0.9310 1.0200 1.0274 0.0123  0.0206  0.0635  133 GLU A C   
1023 O O   . GLU A 136 ? 0.8930 1.0606 1.0312 0.0028  0.0269  0.0742  133 GLU A O   
1024 C CB  . GLU A 136 ? 1.0980 1.0890 1.0897 0.0862  0.0690  0.1001  133 GLU A CB  
1025 C CG  . GLU A 136 ? 1.1284 1.2093 1.1639 0.1085  0.0889  0.1313  133 GLU A CG  
1026 C CD  . GLU A 136 ? 1.1221 1.1911 1.1629 0.0968  0.0902  0.1270  133 GLU A CD  
1027 O OE1 . GLU A 136 ? 1.1240 1.1145 1.1325 0.0760  0.0759  0.1013  133 GLU A OE1 
1028 O OE2 . GLU A 136 ? 1.1404 1.2862 1.2157 0.1110  0.1078  0.1554  133 GLU A OE2 
1029 N N   . ASN A 137 ? 0.9066 0.9466 0.9926 -0.0089 0.0047  0.0437  134 ASN A N   
1030 C CA  . ASN A 137 ? 0.8951 0.9469 1.0103 -0.0335 0.0024  0.0329  134 ASN A CA  
1031 C C   . ASN A 137 ? 0.8501 0.9125 0.9857 -0.0551 -0.0092 0.0186  134 ASN A C   
1032 O O   . ASN A 137 ? 0.8328 0.8748 0.9723 -0.0673 -0.0019 0.0122  134 ASN A O   
1033 C CB  . ASN A 137 ? 0.9235 0.9215 1.0098 -0.0265 0.0051  0.0351  134 ASN A CB  
1034 C CG  . ASN A 137 ? 0.9644 0.9430 1.0221 -0.0037 0.0216  0.0488  134 ASN A CG  
1035 O OD1 . ASN A 137 ? 1.0147 0.9369 1.0169 0.0091  0.0219  0.0519  134 ASN A OD1 
1036 N ND2 . ASN A 137 ? 0.9394 0.9628 1.0260 -0.0026 0.0382  0.0588  134 ASN A ND2 
1037 N N   . GLY A 138 ? 0.8099 0.8966 0.9519 -0.0545 -0.0192 0.0170  135 GLY A N   
1038 C CA  . GLY A 138 ? 0.8015 0.8923 0.9565 -0.0696 -0.0282 0.0058  135 GLY A CA  
1039 C C   . GLY A 138 ? 0.7935 0.8475 0.9362 -0.0642 -0.0370 0.0091  135 GLY A C   
1040 O O   . GLY A 138 ? 0.7524 0.8076 0.9069 -0.0692 -0.0353 0.0073  135 GLY A O   
1041 N N   . LYS A 139 ? 0.8296 0.8567 0.9435 -0.0564 -0.0439 0.0176  136 LYS A N   
1042 C CA  . LYS A 139 ? 0.8438 0.8671 0.9453 -0.0625 -0.0594 0.0278  136 LYS A CA  
1043 C C   . LYS A 139 ? 0.7920 0.8164 0.8810 -0.0736 -0.0737 0.0251  136 LYS A C   
1044 O O   . LYS A 139 ? 0.7608 0.7506 0.8124 -0.0723 -0.0698 0.0199  136 LYS A O   
1045 C CB  . LYS A 139 ? 0.9448 0.9449 1.0088 -0.0644 -0.0636 0.0372  136 LYS A CB  
1046 C CG  . LYS A 139 ? 0.9943 0.9897 1.0689 -0.0500 -0.0462 0.0427  136 LYS A CG  
1047 C CD  . LYS A 139 ? 1.0094 1.0207 1.1189 -0.0400 -0.0292 0.0497  136 LYS A CD  
1048 C CE  . LYS A 139 ? 1.0484 1.0330 1.1595 -0.0343 -0.0015 0.0444  136 LYS A CE  
1049 N NZ  . LYS A 139 ? 1.0806 1.0489 1.1684 -0.0283 -0.0016 0.0484  136 LYS A NZ  
1050 N N   . VAL A 140 ? 0.7419 0.7993 0.8581 -0.0785 -0.0816 0.0319  137 VAL A N   
1051 C CA  . VAL A 140 ? 0.7222 0.7889 0.8321 -0.0929 -0.0954 0.0333  137 VAL A CA  
1052 C C   . VAL A 140 ? 0.7725 0.8104 0.8246 -0.1216 -0.1098 0.0370  137 VAL A C   
1053 O O   . VAL A 140 ? 0.8025 0.8553 0.8413 -0.1338 -0.1192 0.0499  137 VAL A O   
1054 C CB  . VAL A 140 ? 0.7113 0.8283 0.8617 -0.0894 -0.0982 0.0503  137 VAL A CB  
1055 C CG1 . VAL A 140 ? 0.7080 0.8390 0.8584 -0.1038 -0.1098 0.0518  137 VAL A CG1 
1056 C CG2 . VAL A 140 ? 0.6828 0.7979 0.8615 -0.0675 -0.0746 0.0453  137 VAL A CG2 
1057 N N   . ILE A 141 ? 0.7021 0.6854 0.6121 0.0163  0.0630  -0.0163 138 ILE A N   
1058 C CA  . ILE A 141 ? 0.7012 0.6705 0.5931 0.0217  0.0642  -0.0227 138 ILE A CA  
1059 C C   . ILE A 141 ? 0.6658 0.6183 0.5456 0.0182  0.0542  -0.0241 138 ILE A C   
1060 O O   . ILE A 141 ? 0.6872 0.6370 0.5755 0.0181  0.0471  -0.0236 138 ILE A O   
1061 C CB  . ILE A 141 ? 0.7234 0.6949 0.6229 0.0316  0.0676  -0.0276 138 ILE A CB  
1062 C CG1 . ILE A 141 ? 0.7388 0.7296 0.6530 0.0349  0.0778  -0.0261 138 ILE A CG1 
1063 C CG2 . ILE A 141 ? 0.7516 0.7064 0.6314 0.0369  0.0683  -0.0347 138 ILE A CG2 
1064 C CD1 . ILE A 141 ? 0.7657 0.7597 0.6863 0.0460  0.0829  -0.0315 138 ILE A CD1 
1065 N N   . PHE A 142 ? 0.6291 0.5714 0.4899 0.0155  0.0538  -0.0258 139 PHE A N   
1066 C CA  . PHE A 142 ? 0.6048 0.5331 0.4546 0.0112  0.0447  -0.0270 139 PHE A CA  
1067 C C   . PHE A 142 ? 0.6083 0.5228 0.4493 0.0165  0.0425  -0.0340 139 PHE A C   
1068 O O   . PHE A 142 ? 0.6304 0.5440 0.4679 0.0235  0.0488  -0.0385 139 PHE A O   
1069 C CB  . PHE A 142 ? 0.6053 0.5297 0.4394 0.0061  0.0442  -0.0257 139 PHE A CB  
1070 C CG  . PHE A 142 ? 0.5960 0.5308 0.4349 0.0010  0.0467  -0.0188 139 PHE A CG  
1071 C CD1 . PHE A 142 ? 0.5739 0.5196 0.4311 -0.0014 0.0464  -0.0137 139 PHE A CD1 
1072 C CD2 . PHE A 142 ? 0.6008 0.5330 0.4245 -0.0016 0.0487  -0.0173 139 PHE A CD2 
1073 C CE1 . PHE A 142 ? 0.5624 0.5155 0.4230 -0.0067 0.0485  -0.0075 139 PHE A CE1 
1074 C CE2 . PHE A 142 ? 0.6015 0.5411 0.4282 -0.0063 0.0511  -0.0106 139 PHE A CE2 
1075 C CZ  . PHE A 142 ? 0.5826 0.5323 0.4278 -0.0090 0.0512  -0.0058 139 PHE A CZ  
1076 N N   . ASP A 143 ? 0.5830 0.4863 0.4195 0.0128  0.0341  -0.0350 140 ASP A N   
1077 C CA  . ASP A 143 ? 0.5846 0.4717 0.4110 0.0155  0.0305  -0.0413 140 ASP A CA  
1078 C C   . ASP A 143 ? 0.5808 0.4580 0.3924 0.0092  0.0249  -0.0429 140 ASP A C   
1079 O O   . ASP A 143 ? 0.5571 0.4392 0.3714 0.0027  0.0210  -0.0383 140 ASP A O   
1080 C CB  . ASP A 143 ? 0.5712 0.4546 0.4090 0.0164  0.0253  -0.0402 140 ASP A CB  
1081 C CG  . ASP A 143 ? 0.5912 0.4586 0.4214 0.0214  0.0238  -0.0463 140 ASP A CG  
1082 O OD1 . ASP A 143 ? 0.6112 0.4733 0.4311 0.0268  0.0287  -0.0519 140 ASP A OD1 
1083 O OD2 . ASP A 143 ? 0.5809 0.4400 0.4142 0.0198  0.0178  -0.0456 140 ASP A OD2 
1084 N N   . ILE A 144 ? 0.6106 0.4745 0.4070 0.0110  0.0243  -0.0496 141 ILE A N   
1085 C CA  . ILE A 144 ? 0.6235 0.4782 0.4071 0.0046  0.0176  -0.0518 141 ILE A CA  
1086 C C   . ILE A 144 ? 0.6256 0.4680 0.4110 0.0025  0.0110  -0.0542 141 ILE A C   
1087 O O   . ILE A 144 ? 0.6546 0.4851 0.4344 0.0073  0.0122  -0.0597 141 ILE A O   
1088 C CB  . ILE A 144 ? 0.6652 0.5123 0.4289 0.0065  0.0199  -0.0577 141 ILE A CB  
1089 C CG1 . ILE A 144 ? 0.6768 0.5350 0.4366 0.0085  0.0273  -0.0549 141 ILE A CG1 
1090 C CG2 . ILE A 144 ? 0.6624 0.5006 0.4150 -0.0003 0.0114  -0.0602 141 ILE A CG2 
1091 C CD1 . ILE A 144 ? 0.7153 0.5653 0.4542 0.0125  0.0316  -0.0613 141 ILE A CD1 
1092 N N   . VAL A 145 ? 0.5921 0.4370 0.3850 -0.0042 0.0051  -0.0500 142 VAL A N   
1093 C CA  . VAL A 145 ? 0.5839 0.4185 0.3797 -0.0078 -0.0008 -0.0508 142 VAL A CA  
1094 C C   . VAL A 145 ? 0.5711 0.4055 0.3635 -0.0162 -0.0072 -0.0503 142 VAL A C   
1095 O O   . VAL A 145 ? 0.5389 0.3850 0.3367 -0.0194 -0.0080 -0.0453 142 VAL A O   
1096 C CB  . VAL A 145 ? 0.5607 0.4006 0.3718 -0.0070 -0.0011 -0.0454 142 VAL A CB  
1097 C CG1 . VAL A 145 ? 0.5656 0.3936 0.3770 -0.0109 -0.0065 -0.0459 142 VAL A CG1 
1098 C CG2 . VAL A 145 ? 0.5737 0.4168 0.3910 0.0016  0.0045  -0.0454 142 VAL A CG2 
1099 N N   . ASP A 146 ? 0.5903 0.4117 0.3745 -0.0199 -0.0118 -0.0552 143 ASP A N   
1100 C CA  . ASP A 146 ? 0.5892 0.4118 0.3737 -0.0284 -0.0184 -0.0545 143 ASP A CA  
1101 C C   . ASP A 146 ? 0.5502 0.3774 0.3487 -0.0319 -0.0201 -0.0488 143 ASP A C   
1102 O O   . ASP A 146 ? 0.5379 0.3552 0.3384 -0.0317 -0.0204 -0.0495 143 ASP A O   
1103 C CB  . ASP A 146 ? 0.6287 0.4366 0.4020 -0.0324 -0.0231 -0.0614 143 ASP A CB  
1104 C CG  . ASP A 146 ? 0.6398 0.4513 0.4150 -0.0413 -0.0300 -0.0611 143 ASP A CG  
1105 O OD1 . ASP A 146 ? 0.6477 0.4712 0.4345 -0.0444 -0.0311 -0.0552 143 ASP A OD1 
1106 O OD2 . ASP A 146 ? 0.6826 0.4854 0.4480 -0.0450 -0.0345 -0.0669 143 ASP A OD2 
1107 N N   . LEU A 147 ? 0.5274 0.3680 0.3343 -0.0343 -0.0207 -0.0434 144 LEU A N   
1108 C CA  . LEU A 147 ? 0.5073 0.3526 0.3266 -0.0369 -0.0215 -0.0380 144 LEU A CA  
1109 C C   . LEU A 147 ? 0.5078 0.3463 0.3283 -0.0438 -0.0260 -0.0390 144 LEU A C   
1110 O O   . LEU A 147 ? 0.4700 0.3091 0.2980 -0.0455 -0.0260 -0.0354 144 LEU A O   
1111 C CB  . LEU A 147 ? 0.5008 0.3606 0.3272 -0.0379 -0.0213 -0.0328 144 LEU A CB  
1112 C CG  . LEU A 147 ? 0.5051 0.3725 0.3325 -0.0323 -0.0163 -0.0304 144 LEU A CG  
1113 C CD1 . LEU A 147 ? 0.4834 0.3623 0.3160 -0.0342 -0.0169 -0.0256 144 LEU A CD1 
1114 C CD2 . LEU A 147 ? 0.5128 0.3794 0.3469 -0.0276 -0.0128 -0.0289 144 LEU A CD2 
1115 N N   . CYS A 148 ? 0.5298 0.3623 0.3430 -0.0482 -0.0298 -0.0438 145 CYS A N   
1116 C CA  . CYS A 148 ? 0.5493 0.3737 0.3639 -0.0554 -0.0334 -0.0453 145 CYS A CA  
1117 C C   . CYS A 148 ? 0.5498 0.3590 0.3622 -0.0533 -0.0315 -0.0461 145 CYS A C   
1118 O O   . CYS A 148 ? 0.5308 0.3357 0.3478 -0.0585 -0.0327 -0.0439 145 CYS A O   
1119 C CB  . CYS A 148 ? 0.5923 0.4128 0.3992 -0.0603 -0.0383 -0.0511 145 CYS A CB  
1120 S SG  . CYS A 148 ? 0.6512 0.4902 0.4638 -0.0638 -0.0421 -0.0486 145 CYS A SG  
1121 N N   . THR A 149 ? 0.5614 0.3625 0.3665 -0.0461 -0.0286 -0.0491 146 THR A N   
1122 C CA  . THR A 149 ? 0.5787 0.3649 0.3813 -0.0423 -0.0269 -0.0499 146 THR A CA  
1123 C C   . THR A 149 ? 0.5483 0.3416 0.3613 -0.0392 -0.0247 -0.0432 146 THR A C   
1124 O O   . THR A 149 ? 0.5504 0.3343 0.3645 -0.0406 -0.0254 -0.0410 146 THR A O   
1125 C CB  . THR A 149 ? 0.6113 0.3878 0.4045 -0.0341 -0.0241 -0.0551 146 THR A CB  
1126 O OG1 . THR A 149 ? 0.5868 0.3758 0.3832 -0.0268 -0.0196 -0.0534 146 THR A OG1 
1127 C CG2 . THR A 149 ? 0.6446 0.4111 0.4251 -0.0368 -0.0266 -0.0626 146 THR A CG2 
1128 N N   . THR A 150 ? 0.5263 0.3351 0.3458 -0.0357 -0.0224 -0.0398 147 THR A N   
1129 C CA  . THR A 150 ? 0.4958 0.3125 0.3253 -0.0341 -0.0213 -0.0336 147 THR A CA  
1130 C C   . THR A 150 ? 0.4858 0.3033 0.3195 -0.0418 -0.0239 -0.0302 147 THR A C   
1131 O O   . THR A 150 ? 0.4860 0.2988 0.3224 -0.0417 -0.0239 -0.0267 147 THR A O   
1132 C CB  . THR A 150 ? 0.4705 0.3034 0.3058 -0.0308 -0.0188 -0.0309 147 THR A CB  
1133 O OG1 . THR A 150 ? 0.4713 0.3035 0.3015 -0.0248 -0.0157 -0.0347 147 THR A OG1 
1134 C CG2 . THR A 150 ? 0.4494 0.2888 0.2941 -0.0283 -0.0180 -0.0256 147 THR A CG2 
1135 N N   . TRP A 151 ? 0.4722 0.2959 0.3064 -0.0480 -0.0259 -0.0310 148 TRP A N   
1136 C CA  . TRP A 151 ? 0.4595 0.2862 0.2992 -0.0552 -0.0277 -0.0280 148 TRP A CA  
1137 C C   . TRP A 151 ? 0.4845 0.2957 0.3204 -0.0595 -0.0286 -0.0288 148 TRP A C   
1138 O O   . TRP A 151 ? 0.4833 0.2938 0.3230 -0.0622 -0.0279 -0.0245 148 TRP A O   
1139 C CB  . TRP A 151 ? 0.4478 0.2850 0.2899 -0.0603 -0.0301 -0.0292 148 TRP A CB  
1140 C CG  . TRP A 151 ? 0.4301 0.2739 0.2801 -0.0661 -0.0306 -0.0257 148 TRP A CG  
1141 C CD1 . TRP A 151 ? 0.4445 0.2861 0.2962 -0.0739 -0.0326 -0.0269 148 TRP A CD1 
1142 C CD2 . TRP A 151 ? 0.4063 0.2590 0.2634 -0.0648 -0.0288 -0.0205 148 TRP A CD2 
1143 N NE1 . TRP A 151 ? 0.4234 0.2731 0.2832 -0.0771 -0.0314 -0.0227 148 TRP A NE1 
1144 C CE2 . TRP A 151 ? 0.4072 0.2631 0.2696 -0.0714 -0.0292 -0.0190 148 TRP A CE2 
1145 C CE3 . TRP A 151 ? 0.3876 0.2459 0.2472 -0.0590 -0.0268 -0.0174 148 TRP A CE3 
1146 C CZ2 . TRP A 151 ? 0.3950 0.2588 0.2637 -0.0715 -0.0274 -0.0146 148 TRP A CZ2 
1147 C CZ3 . TRP A 151 ? 0.3732 0.2385 0.2389 -0.0597 -0.0258 -0.0132 148 TRP A CZ3 
1148 C CH2 . TRP A 151 ? 0.3740 0.2416 0.2435 -0.0655 -0.0260 -0.0120 148 TRP A CH2 
1149 N N   . GLU A 152 ? 0.5105 0.3085 0.3381 -0.0602 -0.0298 -0.0339 149 GLU A N   
1150 C CA  . GLU A 152 ? 0.5467 0.3276 0.3698 -0.0647 -0.0307 -0.0345 149 GLU A CA  
1151 C C   . GLU A 152 ? 0.5306 0.3033 0.3531 -0.0593 -0.0287 -0.0304 149 GLU A C   
1152 O O   . GLU A 152 ? 0.5261 0.2905 0.3481 -0.0637 -0.0287 -0.0273 149 GLU A O   
1153 C CB  . GLU A 152 ? 0.6120 0.3778 0.4250 -0.0652 -0.0325 -0.0412 149 GLU A CB  
1154 C CG  . GLU A 152 ? 0.6524 0.4260 0.4647 -0.0703 -0.0355 -0.0457 149 GLU A CG  
1155 C CD  . GLU A 152 ? 0.7145 0.4737 0.5157 -0.0716 -0.0381 -0.0533 149 GLU A CD  
1156 O OE1 . GLU A 152 ? 0.7165 0.4781 0.5178 -0.0796 -0.0420 -0.0564 149 GLU A OE1 
1157 O OE2 . GLU A 152 ? 0.7918 0.5378 0.5843 -0.0646 -0.0364 -0.0563 149 GLU A OE2 
1158 N N   . ALA A 153 ? 0.5219 0.2969 0.3443 -0.0499 -0.0271 -0.0302 150 ALA A N   
1159 C CA  . ALA A 153 ? 0.5268 0.2956 0.3496 -0.0438 -0.0261 -0.0262 150 ALA A CA  
1160 C C   . ALA A 153 ? 0.5073 0.2868 0.3373 -0.0459 -0.0258 -0.0199 150 ALA A C   
1161 O O   . ALA A 153 ? 0.5150 0.2854 0.3429 -0.0455 -0.0262 -0.0161 150 ALA A O   
1162 C CB  . ALA A 153 ? 0.5300 0.3011 0.3531 -0.0334 -0.0246 -0.0280 150 ALA A CB  
1163 N N   . MET A 154 ? 0.4748 0.2716 0.3118 -0.0480 -0.0254 -0.0189 151 MET A N   
1164 C CA  . MET A 154 ? 0.4538 0.2600 0.2966 -0.0510 -0.0250 -0.0138 151 MET A CA  
1165 C C   . MET A 154 ? 0.4612 0.2597 0.3018 -0.0593 -0.0251 -0.0122 151 MET A C   
1166 O O   . MET A 154 ? 0.4531 0.2489 0.2933 -0.0602 -0.0244 -0.0078 151 MET A O   
1167 C CB  . MET A 154 ? 0.4375 0.2614 0.2871 -0.0521 -0.0247 -0.0139 151 MET A CB  
1168 C CG  . MET A 154 ? 0.4327 0.2647 0.2848 -0.0451 -0.0238 -0.0147 151 MET A CG  
1169 S SD  . MET A 154 ? 0.4341 0.2710 0.2914 -0.0392 -0.0234 -0.0100 151 MET A SD  
1170 C CE  . MET A 154 ? 0.4080 0.2578 0.2712 -0.0440 -0.0234 -0.0067 151 MET A CE  
1171 N N   . GLU A 155 ? 0.4643 0.2593 0.3032 -0.0655 -0.0259 -0.0158 152 GLU A N   
1172 C CA  . GLU A 155 ? 0.4809 0.2709 0.3197 -0.0748 -0.0255 -0.0144 152 GLU A CA  
1173 C C   . GLU A 155 ? 0.5069 0.2776 0.3377 -0.0746 -0.0249 -0.0119 152 GLU A C   
1174 O O   . GLU A 155 ? 0.5073 0.2750 0.3377 -0.0795 -0.0231 -0.0074 152 GLU A O   
1175 C CB  . GLU A 155 ? 0.4960 0.2853 0.3348 -0.0814 -0.0274 -0.0195 152 GLU A CB  
1176 C CG  . GLU A 155 ? 0.4833 0.2912 0.3299 -0.0831 -0.0285 -0.0211 152 GLU A CG  
1177 C CD  . GLU A 155 ? 0.5072 0.3150 0.3535 -0.0893 -0.0317 -0.0264 152 GLU A CD  
1178 O OE1 . GLU A 155 ? 0.5226 0.3154 0.3607 -0.0896 -0.0332 -0.0304 152 GLU A OE1 
1179 O OE2 . GLU A 155 ? 0.5134 0.3359 0.3675 -0.0934 -0.0330 -0.0267 152 GLU A OE2 
1180 N N   . LYS A 156 ? 0.5288 0.2867 0.3530 -0.0685 -0.0261 -0.0143 153 LYS A N   
1181 C CA  . LYS A 156 ? 0.5672 0.3048 0.3828 -0.0669 -0.0261 -0.0117 153 LYS A CA  
1182 C C   . LYS A 156 ? 0.5535 0.2950 0.3701 -0.0623 -0.0255 -0.0056 153 LYS A C   
1183 O O   . LYS A 156 ? 0.5701 0.2986 0.3803 -0.0645 -0.0250 -0.0014 153 LYS A O   
1184 C CB  . LYS A 156 ? 0.6057 0.3292 0.4144 -0.0600 -0.0275 -0.0159 153 LYS A CB  
1185 C CG  . LYS A 156 ? 0.6422 0.3568 0.4466 -0.0655 -0.0286 -0.0221 153 LYS A CG  
1186 C CD  . LYS A 156 ? 0.6823 0.3851 0.4799 -0.0571 -0.0295 -0.0272 153 LYS A CD  
1187 C CE  . LYS A 156 ? 0.7252 0.4146 0.5157 -0.0623 -0.0311 -0.0338 153 LYS A CE  
1188 N NZ  . LYS A 156 ? 0.7228 0.4284 0.5182 -0.0675 -0.0320 -0.0377 153 LYS A NZ  
1189 N N   . CYS A 157 ? 0.5209 0.2781 0.3441 -0.0563 -0.0256 -0.0052 154 CYS A N   
1190 C CA  . CYS A 157 ? 0.5167 0.2784 0.3410 -0.0521 -0.0258 -0.0001 154 CYS A CA  
1191 C C   . CYS A 157 ? 0.5140 0.2785 0.3381 -0.0596 -0.0239 0.0041  154 CYS A C   
1192 O O   . CYS A 157 ? 0.5208 0.2768 0.3388 -0.0589 -0.0240 0.0087  154 CYS A O   
1193 C CB  . CYS A 157 ? 0.4934 0.2723 0.3259 -0.0461 -0.0263 -0.0009 154 CYS A CB  
1194 S SG  . CYS A 157 ? 0.5234 0.2991 0.3562 -0.0354 -0.0276 -0.0041 154 CYS A SG  
1195 N N   . LYS A 158 ? 0.4956 0.2713 0.3257 -0.0663 -0.0222 0.0024  155 LYS A N   
1196 C CA  . LYS A 158 ? 0.5064 0.2856 0.3375 -0.0739 -0.0194 0.0055  155 LYS A CA  
1197 C C   . LYS A 158 ? 0.5472 0.3082 0.3699 -0.0800 -0.0181 0.0075  155 LYS A C   
1198 O O   . LYS A 158 ? 0.5406 0.2965 0.3584 -0.0821 -0.0160 0.0122  155 LYS A O   
1199 C CB  . LYS A 158 ? 0.4897 0.2856 0.3304 -0.0789 -0.0184 0.0027  155 LYS A CB  
1200 C CG  . LYS A 158 ? 0.4937 0.2950 0.3374 -0.0867 -0.0149 0.0053  155 LYS A CG  
1201 C CD  . LYS A 158 ? 0.4726 0.2933 0.3274 -0.0887 -0.0146 0.0030  155 LYS A CD  
1202 C CE  . LYS A 158 ? 0.4878 0.3155 0.3482 -0.0969 -0.0111 0.0041  155 LYS A CE  
1203 N NZ  . LYS A 158 ? 0.4929 0.3225 0.3511 -0.0963 -0.0073 0.0086  155 LYS A NZ  
1204 N N   . ASP A 159 ? 0.5762 0.3260 0.3961 -0.0827 -0.0193 0.0040  156 ASP A N   
1205 C CA  . ASP A 159 ? 0.6222 0.3532 0.4340 -0.0896 -0.0179 0.0062  156 ASP A CA  
1206 C C   . ASP A 159 ? 0.6246 0.3387 0.4252 -0.0837 -0.0185 0.0111  156 ASP A C   
1207 O O   . ASP A 159 ? 0.6362 0.3379 0.4294 -0.0891 -0.0163 0.0156  156 ASP A O   
1208 C CB  . ASP A 159 ? 0.6645 0.3863 0.4754 -0.0942 -0.0195 0.0009  156 ASP A CB  
1209 C CG  . ASP A 159 ? 0.6877 0.4252 0.5090 -0.1029 -0.0187 -0.0022 156 ASP A CG  
1210 O OD1 . ASP A 159 ? 0.7128 0.4614 0.5397 -0.1082 -0.0156 0.0010  156 ASP A OD1 
1211 O OD2 . ASP A 159 ? 0.7149 0.4543 0.5384 -0.1038 -0.0214 -0.0079 156 ASP A OD2 
1212 N N   . ALA A 160 ? 0.5994 0.3138 0.3990 -0.0730 -0.0215 0.0106  157 ALA A N   
1213 C CA  . ALA A 160 ? 0.6094 0.3093 0.3995 -0.0660 -0.0235 0.0150  157 ALA A CA  
1214 C C   . ALA A 160 ? 0.6037 0.3109 0.3924 -0.0657 -0.0224 0.0204  157 ALA A C   
1215 O O   . ALA A 160 ? 0.6210 0.3164 0.4006 -0.0606 -0.0245 0.0248  157 ALA A O   
1216 C CB  . ALA A 160 ? 0.6053 0.3054 0.3972 -0.0547 -0.0271 0.0121  157 ALA A CB  
1217 N N   . GLY A 161 ? 0.5754 0.3008 0.3722 -0.0702 -0.0198 0.0201  158 GLY A N   
1218 C CA  . GLY A 161 ? 0.5666 0.2988 0.3613 -0.0694 -0.0187 0.0244  158 GLY A CA  
1219 C C   . GLY A 161 ? 0.5511 0.2927 0.3492 -0.0598 -0.0227 0.0240  158 GLY A C   
1220 O O   . GLY A 161 ? 0.5520 0.2960 0.3462 -0.0580 -0.0231 0.0274  158 GLY A O   
1221 N N   . LEU A 162 ? 0.5341 0.2809 0.3390 -0.0539 -0.0254 0.0200  159 LEU A N   
1222 C CA  . LEU A 162 ? 0.5224 0.2788 0.3322 -0.0453 -0.0291 0.0197  159 LEU A CA  
1223 C C   . LEU A 162 ? 0.4874 0.2638 0.3071 -0.0472 -0.0276 0.0178  159 LEU A C   
1224 O O   . LEU A 162 ? 0.4585 0.2438 0.2818 -0.0424 -0.0301 0.0185  159 LEU A O   
1225 C CB  . LEU A 162 ? 0.5376 0.2914 0.3508 -0.0384 -0.0315 0.0162  159 LEU A CB  
1226 C CG  . LEU A 162 ? 0.5818 0.3147 0.3853 -0.0346 -0.0335 0.0177  159 LEU A CG  
1227 C CD1 . LEU A 162 ? 0.5921 0.3256 0.4007 -0.0274 -0.0349 0.0131  159 LEU A CD1 
1228 C CD2 . LEU A 162 ? 0.5973 0.3229 0.3936 -0.0295 -0.0371 0.0230  159 LEU A CD2 
1229 N N   . ALA A 163 ? 0.4849 0.2683 0.3096 -0.0536 -0.0244 0.0153  160 ALA A N   
1230 C CA  . ALA A 163 ? 0.4562 0.2572 0.2896 -0.0555 -0.0229 0.0139  160 ALA A CA  
1231 C C   . ALA A 163 ? 0.4586 0.2612 0.2916 -0.0638 -0.0189 0.0148  160 ALA A C   
1232 O O   . ALA A 163 ? 0.4630 0.2593 0.2951 -0.0688 -0.0175 0.0135  160 ALA A O   
1233 C CB  . ALA A 163 ? 0.4454 0.2560 0.2871 -0.0537 -0.0235 0.0095  160 ALA A CB  
1234 N N   . LYS A 164 ? 0.4415 0.2519 0.2753 -0.0652 -0.0169 0.0166  161 LYS A N   
1235 C CA  . LYS A 164 ? 0.4536 0.2676 0.2887 -0.0726 -0.0122 0.0173  161 LYS A CA  
1236 C C   . LYS A 164 ? 0.4288 0.2558 0.2751 -0.0754 -0.0118 0.0133  161 LYS A C   
1237 O O   . LYS A 164 ? 0.4204 0.2474 0.2693 -0.0823 -0.0094 0.0124  161 LYS A O   
1238 C CB  . LYS A 164 ? 0.4678 0.2866 0.3001 -0.0723 -0.0099 0.0198  161 LYS A CB  
1239 C CG  . LYS A 164 ? 0.5181 0.3236 0.3373 -0.0703 -0.0104 0.0240  161 LYS A CG  
1240 C CD  . LYS A 164 ? 0.5788 0.3676 0.3884 -0.0744 -0.0087 0.0270  161 LYS A CD  
1241 C CE  . LYS A 164 ? 0.6385 0.4153 0.4337 -0.0728 -0.0086 0.0318  161 LYS A CE  
1242 N NZ  . LYS A 164 ? 0.6929 0.4543 0.4781 -0.0785 -0.0051 0.0356  161 LYS A NZ  
1243 N N   . SER A 165 ? 0.3938 0.2311 0.2462 -0.0705 -0.0142 0.0111  162 SER A N   
1244 C CA  . SER A 165 ? 0.3754 0.2249 0.2370 -0.0717 -0.0147 0.0077  162 SER A CA  
1245 C C   . SER A 165 ? 0.3581 0.2084 0.2209 -0.0664 -0.0180 0.0053  162 SER A C   
1246 O O   . SER A 165 ? 0.3529 0.1994 0.2129 -0.0609 -0.0197 0.0064  162 SER A O   
1247 C CB  . SER A 165 ? 0.3646 0.2271 0.2320 -0.0717 -0.0130 0.0080  162 SER A CB  
1248 O OG  . SER A 165 ? 0.3825 0.2451 0.2491 -0.0764 -0.0089 0.0099  162 SER A OG  
1249 N N   . ILE A 166 ? 0.3561 0.2121 0.2235 -0.0679 -0.0188 0.0021  163 ILE A N   
1250 C CA  . ILE A 166 ? 0.3501 0.2083 0.2184 -0.0633 -0.0210 -0.0005 163 ILE A CA  
1251 C C   . ILE A 166 ? 0.3326 0.2041 0.2073 -0.0636 -0.0215 -0.0020 163 ILE A C   
1252 O O   . ILE A 166 ? 0.3390 0.2167 0.2177 -0.0680 -0.0211 -0.0026 163 ILE A O   
1253 C CB  . ILE A 166 ? 0.3693 0.2164 0.2327 -0.0643 -0.0220 -0.0032 163 ILE A CB  
1254 C CG1 . ILE A 166 ? 0.3855 0.2315 0.2498 -0.0718 -0.0218 -0.0051 163 ILE A CG1 
1255 C CG2 . ILE A 166 ? 0.3758 0.2091 0.2325 -0.0618 -0.0220 -0.0012 163 ILE A CG2 
1256 C CD1 . ILE A 166 ? 0.4113 0.2447 0.2697 -0.0730 -0.0232 -0.0085 163 ILE A CD1 
1257 N N   . GLY A 167 ? 0.3242 0.2002 0.1999 -0.0588 -0.0224 -0.0024 164 GLY A N   
1258 C CA  . GLY A 167 ? 0.3169 0.2039 0.1969 -0.0581 -0.0231 -0.0032 164 GLY A CA  
1259 C C   . GLY A 167 ? 0.3213 0.2090 0.1997 -0.0536 -0.0235 -0.0041 164 GLY A C   
1260 O O   . GLY A 167 ? 0.3274 0.2078 0.2021 -0.0512 -0.0233 -0.0052 164 GLY A O   
1261 N N   . VAL A 168 ? 0.3187 0.2148 0.1996 -0.0523 -0.0238 -0.0037 165 VAL A N   
1262 C CA  . VAL A 168 ? 0.3180 0.2159 0.1970 -0.0486 -0.0234 -0.0044 165 VAL A CA  
1263 C C   . VAL A 168 ? 0.3088 0.2135 0.1915 -0.0468 -0.0228 -0.0014 165 VAL A C   
1264 O O   . VAL A 168 ? 0.2951 0.2026 0.1810 -0.0481 -0.0232 0.0004  165 VAL A O   
1265 C CB  . VAL A 168 ? 0.3333 0.2323 0.2085 -0.0497 -0.0247 -0.0074 165 VAL A CB  
1266 C CG1 . VAL A 168 ? 0.3536 0.2445 0.2246 -0.0523 -0.0257 -0.0109 165 VAL A CG1 
1267 C CG2 . VAL A 168 ? 0.3320 0.2387 0.2101 -0.0517 -0.0266 -0.0065 165 VAL A CG2 
1268 N N   . SER A 169 ? 0.3047 0.2116 0.1866 -0.0440 -0.0216 -0.0011 166 SER A N   
1269 C CA  . SER A 169 ? 0.3009 0.2130 0.1861 -0.0428 -0.0208 0.0018  166 SER A CA  
1270 C C   . SER A 169 ? 0.3009 0.2156 0.1828 -0.0412 -0.0193 0.0017  166 SER A C   
1271 O O   . SER A 169 ? 0.3188 0.2312 0.1970 -0.0397 -0.0179 -0.0007 166 SER A O   
1272 C CB  . SER A 169 ? 0.3006 0.2122 0.1898 -0.0413 -0.0201 0.0033  166 SER A CB  
1273 O OG  . SER A 169 ? 0.2980 0.2137 0.1907 -0.0411 -0.0197 0.0060  166 SER A OG  
1274 N N   . ASN A 170 ? 0.2972 0.2157 0.1796 -0.0414 -0.0192 0.0042  167 ASN A N   
1275 C CA  . ASN A 170 ? 0.2991 0.2196 0.1770 -0.0401 -0.0173 0.0052  167 ASN A CA  
1276 C C   . ASN A 170 ? 0.3131 0.2322 0.1831 -0.0400 -0.0186 0.0025  167 ASN A C   
1277 O O   . ASN A 170 ? 0.3265 0.2457 0.1907 -0.0385 -0.0161 0.0023  167 ASN A O   
1278 C CB  . ASN A 170 ? 0.3062 0.2280 0.1862 -0.0384 -0.0136 0.0055  167 ASN A CB  
1279 C CG  . ASN A 170 ? 0.2982 0.2225 0.1860 -0.0391 -0.0132 0.0085  167 ASN A CG  
1280 O OD1 . ASN A 170 ? 0.3143 0.2396 0.2026 -0.0404 -0.0137 0.0113  167 ASN A OD1 
1281 N ND2 . ASN A 170 ? 0.2909 0.2153 0.1840 -0.0383 -0.0133 0.0077  167 ASN A ND2 
1282 N N   . PHE A 171 ? 0.3106 0.2286 0.1804 -0.0418 -0.0219 0.0002  168 PHE A N   
1283 C CA  . PHE A 171 ? 0.3298 0.2467 0.1927 -0.0425 -0.0244 -0.0028 168 PHE A CA  
1284 C C   . PHE A 171 ? 0.3426 0.2637 0.2042 -0.0425 -0.0274 -0.0006 168 PHE A C   
1285 O O   . PHE A 171 ? 0.3413 0.2653 0.2092 -0.0428 -0.0283 0.0020  168 PHE A O   
1286 C CB  . PHE A 171 ? 0.3297 0.2440 0.1943 -0.0453 -0.0270 -0.0062 168 PHE A CB  
1287 C CG  . PHE A 171 ? 0.3326 0.2401 0.1951 -0.0452 -0.0253 -0.0093 168 PHE A CG  
1288 C CD1 . PHE A 171 ? 0.3295 0.2352 0.1941 -0.0425 -0.0218 -0.0081 168 PHE A CD1 
1289 C CD2 . PHE A 171 ? 0.3490 0.2516 0.2072 -0.0474 -0.0276 -0.0135 168 PHE A CD2 
1290 C CE1 . PHE A 171 ? 0.3413 0.2402 0.2041 -0.0414 -0.0207 -0.0108 168 PHE A CE1 
1291 C CE2 . PHE A 171 ? 0.3592 0.2536 0.2146 -0.0469 -0.0262 -0.0163 168 PHE A CE2 
1292 C CZ  . PHE A 171 ? 0.3601 0.2525 0.2174 -0.0433 -0.0226 -0.0149 168 PHE A CZ  
1293 N N   . ASN A 172 ? 0.3620 0.2826 0.2148 -0.0417 -0.0290 -0.0018 169 ASN A N   
1294 C CA  . ASN A 172 ? 0.3734 0.2975 0.2237 -0.0412 -0.0331 0.0000  169 ASN A CA  
1295 C C   . ASN A 172 ? 0.3838 0.3102 0.2361 -0.0436 -0.0383 -0.0038 169 ASN A C   
1296 O O   . ASN A 172 ? 0.3681 0.2919 0.2226 -0.0462 -0.0380 -0.0074 169 ASN A O   
1297 C CB  . ASN A 172 ? 0.3907 0.3128 0.2296 -0.0389 -0.0321 0.0018  169 ASN A CB  
1298 C CG  . ASN A 172 ? 0.4061 0.3243 0.2345 -0.0388 -0.0320 -0.0026 169 ASN A CG  
1299 O OD1 . ASN A 172 ? 0.4044 0.3213 0.2337 -0.0408 -0.0347 -0.0071 169 ASN A OD1 
1300 N ND2 . ASN A 172 ? 0.4275 0.3429 0.2457 -0.0367 -0.0284 -0.0014 169 ASN A ND2 
1301 N N   . ARG A 173 ? 0.4031 0.3341 0.2550 -0.0431 -0.0433 -0.0030 170 ARG A N   
1302 C CA  . ARG A 173 ? 0.4396 0.3749 0.2953 -0.0459 -0.0488 -0.0066 170 ARG A CA  
1303 C C   . ARG A 173 ? 0.4441 0.3742 0.2913 -0.0482 -0.0502 -0.0118 170 ARG A C   
1304 O O   . ARG A 173 ? 0.4381 0.3684 0.2903 -0.0522 -0.0519 -0.0153 170 ARG A O   
1305 C CB  . ARG A 173 ? 0.4908 0.4324 0.3465 -0.0439 -0.0545 -0.0048 170 ARG A CB  
1306 C CG  . ARG A 173 ? 0.5448 0.4915 0.4022 -0.0468 -0.0612 -0.0091 170 ARG A CG  
1307 C CD  . ARG A 173 ? 0.5867 0.5414 0.4469 -0.0441 -0.0673 -0.0070 170 ARG A CD  
1308 N NE  . ARG A 173 ? 0.6361 0.5971 0.5000 -0.0475 -0.0741 -0.0113 170 ARG A NE  
1309 C CZ  . ARG A 173 ? 0.6894 0.6587 0.5557 -0.0456 -0.0815 -0.0109 170 ARG A CZ  
1310 N NH1 . ARG A 173 ? 0.7253 0.7014 0.5964 -0.0495 -0.0881 -0.0153 170 ARG A NH1 
1311 N NH2 . ARG A 173 ? 0.6987 0.6691 0.5629 -0.0398 -0.0824 -0.0061 170 ARG A NH2 
1312 N N   . ARG A 174 ? 0.4587 0.3839 0.2927 -0.0459 -0.0497 -0.0123 171 ARG A N   
1313 C CA  . ARG A 174 ? 0.4973 0.4164 0.3211 -0.0475 -0.0514 -0.0179 171 ARG A CA  
1314 C C   . ARG A 174 ? 0.4678 0.3809 0.2953 -0.0494 -0.0470 -0.0207 171 ARG A C   
1315 O O   . ARG A 174 ? 0.4777 0.3867 0.3036 -0.0528 -0.0497 -0.0256 171 ARG A O   
1316 C CB  . ARG A 174 ? 0.5433 0.4577 0.3512 -0.0439 -0.0499 -0.0175 171 ARG A CB  
1317 C CG  . ARG A 174 ? 0.6079 0.5147 0.4029 -0.0447 -0.0510 -0.0237 171 ARG A CG  
1318 C CD  . ARG A 174 ? 0.6675 0.5693 0.4455 -0.0408 -0.0481 -0.0232 171 ARG A CD  
1319 N NE  . ARG A 174 ? 0.6874 0.5906 0.4676 -0.0377 -0.0406 -0.0175 171 ARG A NE  
1320 C CZ  . ARG A 174 ? 0.6756 0.5766 0.4599 -0.0365 -0.0332 -0.0173 171 ARG A CZ  
1321 N NH1 . ARG A 174 ? 0.6306 0.5344 0.4183 -0.0345 -0.0275 -0.0119 171 ARG A NH1 
1322 N NH2 . ARG A 174 ? 0.6810 0.5769 0.4659 -0.0372 -0.0317 -0.0225 171 ARG A NH2 
1323 N N   . GLN A 175 ? 0.4328 0.3448 0.2646 -0.0473 -0.0410 -0.0175 172 GLN A N   
1324 C CA  . GLN A 175 ? 0.4312 0.3370 0.2656 -0.0479 -0.0371 -0.0196 172 GLN A CA  
1325 C C   . GLN A 175 ? 0.4202 0.3275 0.2653 -0.0522 -0.0390 -0.0200 172 GLN A C   
1326 O O   . GLN A 175 ? 0.4370 0.3373 0.2813 -0.0543 -0.0387 -0.0234 172 GLN A O   
1327 C CB  . GLN A 175 ? 0.4168 0.3225 0.2534 -0.0443 -0.0309 -0.0161 172 GLN A CB  
1328 C CG  . GLN A 175 ? 0.4316 0.3358 0.2577 -0.0407 -0.0277 -0.0158 172 GLN A CG  
1329 C CD  . GLN A 175 ? 0.4227 0.3303 0.2535 -0.0381 -0.0223 -0.0111 172 GLN A CD  
1330 O OE1 . GLN A 175 ? 0.4106 0.3225 0.2505 -0.0390 -0.0224 -0.0072 172 GLN A OE1 
1331 N NE2 . GLN A 175 ? 0.4234 0.3290 0.2479 -0.0352 -0.0173 -0.0119 172 GLN A NE2 
1332 N N   . LEU A 176 ? 0.4081 0.3233 0.2622 -0.0531 -0.0404 -0.0167 173 LEU A N   
1333 C CA  . LEU A 176 ? 0.4119 0.3296 0.2756 -0.0576 -0.0419 -0.0173 173 LEU A CA  
1334 C C   . LEU A 176 ? 0.4345 0.3514 0.2963 -0.0621 -0.0469 -0.0220 173 LEU A C   
1335 O O   . LEU A 176 ? 0.4347 0.3473 0.2996 -0.0664 -0.0466 -0.0241 173 LEU A O   
1336 C CB  . LEU A 176 ? 0.4069 0.3343 0.2798 -0.0571 -0.0428 -0.0136 173 LEU A CB  
1337 C CG  . LEU A 176 ? 0.3958 0.3232 0.2724 -0.0541 -0.0384 -0.0094 173 LEU A CG  
1338 C CD1 . LEU A 176 ? 0.3956 0.3313 0.2799 -0.0531 -0.0395 -0.0064 173 LEU A CD1 
1339 C CD2 . LEU A 176 ? 0.3883 0.3100 0.2674 -0.0559 -0.0351 -0.0096 173 LEU A CD2 
1340 N N   . GLU A 177 ? 0.4608 0.3820 0.3179 -0.0615 -0.0517 -0.0233 174 GLU A N   
1341 C CA  . GLU A 177 ? 0.5042 0.4261 0.3600 -0.0662 -0.0579 -0.0281 174 GLU A CA  
1342 C C   . GLU A 177 ? 0.5280 0.4368 0.3741 -0.0680 -0.0569 -0.0330 174 GLU A C   
1343 O O   . GLU A 177 ? 0.5051 0.4112 0.3529 -0.0737 -0.0601 -0.0370 174 GLU A O   
1344 C CB  . GLU A 177 ? 0.5420 0.4690 0.3912 -0.0640 -0.0637 -0.0287 174 GLU A CB  
1345 C CG  . GLU A 177 ? 0.5680 0.5081 0.4277 -0.0630 -0.0672 -0.0252 174 GLU A CG  
1346 C CD  . GLU A 177 ? 0.6327 0.5770 0.4849 -0.0594 -0.0729 -0.0243 174 GLU A CD  
1347 O OE1 . GLU A 177 ? 0.7191 0.6554 0.5557 -0.0570 -0.0728 -0.0256 174 GLU A OE1 
1348 O OE2 . GLU A 177 ? 0.6698 0.6253 0.5313 -0.0584 -0.0772 -0.0222 174 GLU A OE2 
1349 N N   . MET A 178 ? 0.5505 0.4515 0.3871 -0.0633 -0.0524 -0.0329 175 MET A N   
1350 C CA  . MET A 178 ? 0.5961 0.4838 0.4235 -0.0638 -0.0509 -0.0378 175 MET A CA  
1351 C C   . MET A 178 ? 0.5447 0.4272 0.3800 -0.0680 -0.0492 -0.0381 175 MET A C   
1352 O O   . MET A 178 ? 0.5456 0.4180 0.3759 -0.0716 -0.0510 -0.0429 175 MET A O   
1353 C CB  . MET A 178 ? 0.6875 0.5704 0.5070 -0.0572 -0.0451 -0.0368 175 MET A CB  
1354 C CG  . MET A 178 ? 0.7944 0.6639 0.6050 -0.0559 -0.0427 -0.0416 175 MET A CG  
1355 S SD  . MET A 178 ? 0.9891 0.8575 0.7943 -0.0476 -0.0349 -0.0395 175 MET A SD  
1356 C CE  . MET A 178 ? 0.9213 0.7989 0.7419 -0.0467 -0.0315 -0.0321 175 MET A CE  
1357 N N   . ILE A 179 ? 0.5033 0.3906 0.3488 -0.0675 -0.0458 -0.0331 176 ILE A N   
1358 C CA  . ILE A 179 ? 0.4883 0.3698 0.3397 -0.0713 -0.0438 -0.0326 176 ILE A CA  
1359 C C   . ILE A 179 ? 0.4752 0.3630 0.3349 -0.0788 -0.0477 -0.0335 176 ILE A C   
1360 O O   . ILE A 179 ? 0.4914 0.3710 0.3507 -0.0843 -0.0485 -0.0362 176 ILE A O   
1361 C CB  . ILE A 179 ? 0.4742 0.3580 0.3318 -0.0682 -0.0389 -0.0272 176 ILE A CB  
1362 C CG1 . ILE A 179 ? 0.4786 0.3590 0.3309 -0.0612 -0.0352 -0.0260 176 ILE A CG1 
1363 C CG2 . ILE A 179 ? 0.4701 0.3472 0.3316 -0.0722 -0.0372 -0.0263 176 ILE A CG2 
1364 C CD1 . ILE A 179 ? 0.5138 0.3818 0.3571 -0.0590 -0.0340 -0.0299 176 ILE A CD1 
1365 N N   . LEU A 180 ? 0.4562 0.3579 0.3235 -0.0790 -0.0501 -0.0314 177 LEU A N   
1366 C CA  . LEU A 180 ? 0.4610 0.3718 0.3393 -0.0857 -0.0533 -0.0320 177 LEU A CA  
1367 C C   . LEU A 180 ? 0.4914 0.3980 0.3658 -0.0916 -0.0590 -0.0379 177 LEU A C   
1368 O O   . LEU A 180 ? 0.5099 0.4186 0.3926 -0.0991 -0.0603 -0.0390 177 LEU A O   
1369 C CB  . LEU A 180 ? 0.4446 0.3712 0.3310 -0.0832 -0.0555 -0.0292 177 LEU A CB  
1370 C CG  . LEU A 180 ? 0.4247 0.3554 0.3166 -0.0789 -0.0503 -0.0238 177 LEU A CG  
1371 C CD1 . LEU A 180 ? 0.4182 0.3613 0.3148 -0.0747 -0.0527 -0.0214 177 LEU A CD1 
1372 C CD2 . LEU A 180 ? 0.4174 0.3490 0.3184 -0.0833 -0.0464 -0.0220 177 LEU A CD2 
1373 N N   . ASN A 181 ? 0.5062 0.4069 0.3681 -0.0886 -0.0620 -0.0414 178 ASN A N   
1374 C CA  . ASN A 181 ? 0.5534 0.4488 0.4087 -0.0935 -0.0683 -0.0478 178 ASN A CA  
1375 C C   . ASN A 181 ? 0.5733 0.4496 0.4172 -0.0944 -0.0661 -0.0519 178 ASN A C   
1376 O O   . ASN A 181 ? 0.5951 0.4640 0.4304 -0.0975 -0.0710 -0.0578 178 ASN A O   
1377 C CB  . ASN A 181 ? 0.5804 0.4804 0.4268 -0.0893 -0.0733 -0.0496 178 ASN A CB  
1378 C CG  . ASN A 181 ? 0.5937 0.5115 0.4511 -0.0883 -0.0767 -0.0459 178 ASN A CG  
1379 O OD1 . ASN A 181 ? 0.6123 0.5404 0.4842 -0.0936 -0.0787 -0.0453 178 ASN A OD1 
1380 N ND2 . ASN A 181 ? 0.6116 0.5332 0.4629 -0.0812 -0.0765 -0.0430 178 ASN A ND2 
1381 N N   . LYS A 182 ? 0.5660 0.4340 0.4095 -0.0916 -0.0596 -0.0490 179 LYS A N   
1382 C CA  . LYS A 182 ? 0.5902 0.4393 0.4235 -0.0914 -0.0575 -0.0525 179 LYS A CA  
1383 C C   . LYS A 182 ? 0.5996 0.4416 0.4356 -0.1013 -0.0610 -0.0561 179 LYS A C   
1384 O O   . LYS A 182 ? 0.5820 0.4306 0.4301 -0.1075 -0.0605 -0.0531 179 LYS A O   
1385 C CB  . LYS A 182 ? 0.5994 0.4422 0.4336 -0.0866 -0.0507 -0.0482 179 LYS A CB  
1386 C CG  . LYS A 182 ? 0.6474 0.4706 0.4708 -0.0847 -0.0489 -0.0518 179 LYS A CG  
1387 C CD  . LYS A 182 ? 0.6568 0.4740 0.4815 -0.0797 -0.0433 -0.0475 179 LYS A CD  
1388 C CE  . LYS A 182 ? 0.6821 0.4918 0.5117 -0.0860 -0.0426 -0.0453 179 LYS A CE  
1389 N NZ  . LYS A 182 ? 0.7279 0.5211 0.5500 -0.0918 -0.0454 -0.0508 179 LYS A NZ  
1390 N N   . PRO A 183 ? 0.6366 0.4649 0.4611 -0.1035 -0.0645 -0.0627 180 PRO A N   
1391 C CA  . PRO A 183 ? 0.6468 0.4643 0.4722 -0.1132 -0.0673 -0.0663 180 PRO A CA  
1392 C C   . PRO A 183 ? 0.6267 0.4344 0.4561 -0.1148 -0.0615 -0.0621 180 PRO A C   
1393 O O   . PRO A 183 ? 0.6198 0.4184 0.4426 -0.1074 -0.0569 -0.0604 180 PRO A O   
1394 C CB  . PRO A 183 ? 0.6880 0.4875 0.4962 -0.1115 -0.0699 -0.0739 180 PRO A CB  
1395 C CG  . PRO A 183 ? 0.6826 0.4903 0.4830 -0.1036 -0.0711 -0.0751 180 PRO A CG  
1396 C CD  . PRO A 183 ? 0.6508 0.4728 0.4601 -0.0971 -0.0658 -0.0674 180 PRO A CD  
1397 N N   . GLY A 184 ? 0.6196 0.4298 0.4594 -0.1244 -0.0619 -0.0603 181 GLY A N   
1398 C CA  . GLY A 184 ? 0.6148 0.4140 0.4565 -0.1271 -0.0567 -0.0561 181 GLY A CA  
1399 C C   . GLY A 184 ? 0.5846 0.3940 0.4331 -0.1211 -0.0509 -0.0487 181 GLY A C   
1400 O O   . GLY A 184 ? 0.5894 0.3874 0.4354 -0.1201 -0.0464 -0.0450 181 GLY A O   
1401 N N   . LEU A 185 ? 0.5559 0.3847 0.4115 -0.1168 -0.0512 -0.0465 182 LEU A N   
1402 C CA  . LEU A 185 ? 0.5223 0.3607 0.3842 -0.1114 -0.0462 -0.0399 182 LEU A CA  
1403 C C   . LEU A 185 ? 0.5274 0.3629 0.3956 -0.1180 -0.0423 -0.0357 182 LEU A C   
1404 O O   . LEU A 185 ? 0.5285 0.3695 0.4048 -0.1274 -0.0440 -0.0368 182 LEU A O   
1405 C CB  . LEU A 185 ? 0.4978 0.3575 0.3689 -0.1091 -0.0477 -0.0382 182 LEU A CB  
1406 C CG  . LEU A 185 ? 0.4748 0.3430 0.3510 -0.1032 -0.0429 -0.0322 182 LEU A CG  
1407 C CD1 . LEU A 185 ? 0.4607 0.3215 0.3276 -0.0940 -0.0407 -0.0313 182 LEU A CD1 
1408 C CD2 . LEU A 185 ? 0.4609 0.3489 0.3473 -0.1023 -0.0447 -0.0307 182 LEU A CD2 
1409 N N   . LYS A 186 ? 0.5204 0.3487 0.3852 -0.1134 -0.0375 -0.0311 183 LYS A N   
1410 C CA  . LYS A 186 ? 0.5305 0.3562 0.3994 -0.1186 -0.0332 -0.0263 183 LYS A CA  
1411 C C   . LYS A 186 ? 0.5067 0.3481 0.3834 -0.1148 -0.0298 -0.0213 183 LYS A C   
1412 O O   . LYS A 186 ? 0.4985 0.3482 0.3836 -0.1205 -0.0271 -0.0186 183 LYS A O   
1413 C CB  . LYS A 186 ? 0.5603 0.3646 0.4180 -0.1162 -0.0308 -0.0244 183 LYS A CB  
1414 C CG  . LYS A 186 ? 0.5824 0.3798 0.4413 -0.1234 -0.0268 -0.0198 183 LYS A CG  
1415 C CD  . LYS A 186 ? 0.6151 0.3893 0.4617 -0.1211 -0.0252 -0.0177 183 LYS A CD  
1416 C CE  . LYS A 186 ? 0.6493 0.4152 0.4954 -0.1295 -0.0212 -0.0129 183 LYS A CE  
1417 N NZ  . LYS A 186 ? 0.6803 0.4207 0.5129 -0.1279 -0.0205 -0.0110 183 LYS A NZ  
1418 N N   . TYR A 187 ? 0.4800 0.3244 0.3536 -0.1054 -0.0295 -0.0202 184 TYR A N   
1419 C CA  . TYR A 187 ? 0.4604 0.3169 0.3395 -0.1011 -0.0265 -0.0158 184 TYR A CA  
1420 C C   . TYR A 187 ? 0.4428 0.3120 0.3248 -0.0951 -0.0290 -0.0171 184 TYR A C   
1421 O O   . TYR A 187 ? 0.4634 0.3280 0.3390 -0.0890 -0.0302 -0.0185 184 TYR A O   
1422 C CB  . TYR A 187 ? 0.4599 0.3059 0.3323 -0.0962 -0.0233 -0.0118 184 TYR A CB  
1423 C CG  . TYR A 187 ? 0.4872 0.3188 0.3546 -0.1015 -0.0209 -0.0095 184 TYR A CG  
1424 C CD1 . TYR A 187 ? 0.5107 0.3463 0.3837 -0.1097 -0.0180 -0.0075 184 TYR A CD1 
1425 C CD2 . TYR A 187 ? 0.5033 0.3167 0.3603 -0.0983 -0.0212 -0.0092 184 TYR A CD2 
1426 C CE1 . TYR A 187 ? 0.5287 0.3498 0.3960 -0.1152 -0.0152 -0.0048 184 TYR A CE1 
1427 C CE2 . TYR A 187 ? 0.5307 0.3289 0.3818 -0.1030 -0.0191 -0.0066 184 TYR A CE2 
1428 C CZ  . TYR A 187 ? 0.5433 0.3448 0.3989 -0.1118 -0.0160 -0.0042 184 TYR A CZ  
1429 O OH  . TYR A 187 ? 0.5782 0.3632 0.4265 -0.1169 -0.0135 -0.0011 184 TYR A OH  
1430 N N   . LYS A 188 ? 0.4391 0.3243 0.3309 -0.0965 -0.0293 -0.0164 185 LYS A N   
1431 C CA  . LYS A 188 ? 0.4326 0.3297 0.3270 -0.0903 -0.0310 -0.0161 185 LYS A CA  
1432 C C   . LYS A 188 ? 0.4123 0.3061 0.3027 -0.0834 -0.0281 -0.0127 185 LYS A C   
1433 O O   . LYS A 188 ? 0.4132 0.3014 0.3022 -0.0837 -0.0249 -0.0100 185 LYS A O   
1434 C CB  . LYS A 188 ? 0.4432 0.3570 0.3493 -0.0924 -0.0314 -0.0153 185 LYS A CB  
1435 C CG  . LYS A 188 ? 0.4919 0.4115 0.4044 -0.0997 -0.0350 -0.0187 185 LYS A CG  
1436 C CD  . LYS A 188 ? 0.5090 0.4466 0.4321 -0.0991 -0.0384 -0.0194 185 LYS A CD  
1437 C CE  . LYS A 188 ? 0.5167 0.4658 0.4478 -0.0952 -0.0350 -0.0158 185 LYS A CE  
1438 N NZ  . LYS A 188 ? 0.5342 0.5006 0.4794 -0.0981 -0.0372 -0.0167 185 LYS A NZ  
1439 N N   . PRO A 189 ? 0.4022 0.2994 0.2904 -0.0772 -0.0292 -0.0127 186 PRO A N   
1440 C CA  . PRO A 189 ? 0.3820 0.2796 0.2695 -0.0718 -0.0268 -0.0093 186 PRO A CA  
1441 C C   . PRO A 189 ? 0.3683 0.2747 0.2628 -0.0728 -0.0248 -0.0065 186 PRO A C   
1442 O O   . PRO A 189 ? 0.3577 0.2748 0.2589 -0.0742 -0.0261 -0.0072 186 PRO A O   
1443 C CB  . PRO A 189 ? 0.3783 0.2806 0.2641 -0.0666 -0.0284 -0.0097 186 PRO A CB  
1444 C CG  . PRO A 189 ? 0.4015 0.3068 0.2864 -0.0689 -0.0319 -0.0132 186 PRO A CG  
1445 C CD  . PRO A 189 ? 0.4081 0.3095 0.2943 -0.0756 -0.0329 -0.0156 186 PRO A CD  
1446 N N   . VAL A 190 ? 0.3454 0.2474 0.2382 -0.0718 -0.0218 -0.0037 187 VAL A N   
1447 C CA  . VAL A 190 ? 0.3429 0.2524 0.2408 -0.0718 -0.0194 -0.0015 187 VAL A CA  
1448 C C   . VAL A 190 ? 0.3237 0.2404 0.2238 -0.0665 -0.0205 -0.0008 187 VAL A C   
1449 O O   . VAL A 190 ? 0.3131 0.2375 0.2184 -0.0660 -0.0193 0.0000  187 VAL A O   
1450 C CB  . VAL A 190 ? 0.3491 0.2511 0.2425 -0.0720 -0.0161 0.0012  187 VAL A CB  
1451 C CG1 . VAL A 190 ? 0.3636 0.2569 0.2539 -0.0776 -0.0146 0.0012  187 VAL A CG1 
1452 C CG2 . VAL A 190 ? 0.3384 0.2337 0.2259 -0.0668 -0.0170 0.0025  187 VAL A CG2 
1453 N N   . CYS A 191 ? 0.3216 0.2351 0.2177 -0.0627 -0.0221 -0.0008 188 CYS A N   
1454 C CA  . CYS A 191 ? 0.3122 0.2307 0.2097 -0.0583 -0.0228 0.0005  188 CYS A CA  
1455 C C   . CYS A 191 ? 0.3103 0.2278 0.2045 -0.0558 -0.0246 -0.0003 188 CYS A C   
1456 O O   . CYS A 191 ? 0.3102 0.2220 0.2004 -0.0565 -0.0250 -0.0020 188 CYS A O   
1457 C CB  . CYS A 191 ? 0.3140 0.2290 0.2096 -0.0559 -0.0211 0.0027  188 CYS A CB  
1458 S SG  . CYS A 191 ? 0.3302 0.2353 0.2200 -0.0545 -0.0213 0.0032  188 CYS A SG  
1459 N N   . ASN A 192 ? 0.2974 0.2195 0.1927 -0.0529 -0.0254 0.0009  189 ASN A N   
1460 C CA  . ASN A 192 ? 0.3000 0.2211 0.1916 -0.0502 -0.0259 0.0013  189 ASN A CA  
1461 C C   . ASN A 192 ? 0.2904 0.2115 0.1831 -0.0477 -0.0248 0.0041  189 ASN A C   
1462 O O   . ASN A 192 ? 0.2748 0.1993 0.1700 -0.0469 -0.0253 0.0053  189 ASN A O   
1463 C CB  . ASN A 192 ? 0.3153 0.2410 0.2057 -0.0498 -0.0284 0.0004  189 ASN A CB  
1464 C CG  . ASN A 192 ? 0.3169 0.2409 0.2018 -0.0475 -0.0281 0.0008  189 ASN A CG  
1465 O OD1 . ASN A 192 ? 0.3187 0.2387 0.2016 -0.0464 -0.0258 0.0009  189 ASN A OD1 
1466 N ND2 . ASN A 192 ? 0.3225 0.2500 0.2049 -0.0463 -0.0302 0.0013  189 ASN A ND2 
1467 N N   . GLN A 193 ? 0.2894 0.2067 0.1810 -0.0467 -0.0237 0.0048  190 GLN A N   
1468 C CA  . GLN A 193 ? 0.2893 0.2063 0.1824 -0.0453 -0.0232 0.0070  190 GLN A CA  
1469 C C   . GLN A 193 ? 0.2874 0.2065 0.1796 -0.0440 -0.0227 0.0083  190 GLN A C   
1470 O O   . GLN A 193 ? 0.3124 0.2313 0.2031 -0.0433 -0.0215 0.0076  190 GLN A O   
1471 C CB  . GLN A 193 ? 0.2830 0.1962 0.1765 -0.0450 -0.0229 0.0072  190 GLN A CB  
1472 C CG  . GLN A 193 ? 0.2925 0.2057 0.1881 -0.0444 -0.0233 0.0091  190 GLN A CG  
1473 C CD  . GLN A 193 ? 0.2834 0.1939 0.1798 -0.0439 -0.0241 0.0093  190 GLN A CD  
1474 O OE1 . GLN A 193 ? 0.2915 0.2042 0.1911 -0.0431 -0.0243 0.0101  190 GLN A OE1 
1475 N NE2 . GLN A 193 ? 0.2763 0.1826 0.1700 -0.0443 -0.0246 0.0087  190 GLN A NE2 
1476 N N   . VAL A 194 ? 0.2912 0.2117 0.1838 -0.0434 -0.0232 0.0102  191 VAL A N   
1477 C CA  . VAL A 194 ? 0.3025 0.2241 0.1927 -0.0425 -0.0226 0.0121  191 VAL A CA  
1478 C C   . VAL A 194 ? 0.3021 0.2219 0.1940 -0.0425 -0.0225 0.0148  191 VAL A C   
1479 O O   . VAL A 194 ? 0.2975 0.2156 0.1914 -0.0425 -0.0235 0.0147  191 VAL A O   
1480 C CB  . VAL A 194 ? 0.3130 0.2367 0.1998 -0.0418 -0.0244 0.0118  191 VAL A CB  
1481 C CG1 . VAL A 194 ? 0.3123 0.2368 0.1971 -0.0426 -0.0251 0.0085  191 VAL A CG1 
1482 C CG2 . VAL A 194 ? 0.3164 0.2413 0.2054 -0.0408 -0.0265 0.0125  191 VAL A CG2 
1483 N N   . GLU A 195 ? 0.3117 0.2314 0.2018 -0.0426 -0.0211 0.0172  192 GLU A N   
1484 C CA  . GLU A 195 ? 0.3161 0.2328 0.2069 -0.0432 -0.0210 0.0202  192 GLU A CA  
1485 C C   . GLU A 195 ? 0.3261 0.2404 0.2146 -0.0414 -0.0232 0.0210  192 GLU A C   
1486 O O   . GLU A 195 ? 0.3229 0.2386 0.2073 -0.0398 -0.0241 0.0215  192 GLU A O   
1487 C CB  . GLU A 195 ? 0.3332 0.2501 0.2218 -0.0442 -0.0183 0.0231  192 GLU A CB  
1488 C CG  . GLU A 195 ? 0.3425 0.2553 0.2327 -0.0461 -0.0180 0.0262  192 GLU A CG  
1489 C CD  . GLU A 195 ? 0.3629 0.2755 0.2512 -0.0480 -0.0147 0.0298  192 GLU A CD  
1490 O OE1 . GLU A 195 ? 0.3760 0.2933 0.2636 -0.0479 -0.0116 0.0293  192 GLU A OE1 
1491 O OE2 . GLU A 195 ? 0.3719 0.2791 0.2593 -0.0497 -0.0147 0.0329  192 GLU A OE2 
1492 N N   . CYS A 196 ? 0.3130 0.2240 0.2036 -0.0412 -0.0243 0.0209  193 CYS A N   
1493 C CA  . CYS A 196 ? 0.3253 0.2345 0.2146 -0.0384 -0.0262 0.0212  193 CYS A CA  
1494 C C   . CYS A 196 ? 0.3246 0.2268 0.2140 -0.0382 -0.0266 0.0221  193 CYS A C   
1495 O O   . CYS A 196 ? 0.3097 0.2103 0.2012 -0.0395 -0.0265 0.0202  193 CYS A O   
1496 C CB  . CYS A 196 ? 0.3226 0.2367 0.2145 -0.0372 -0.0270 0.0182  193 CYS A CB  
1497 S SG  . CYS A 196 ? 0.3487 0.2640 0.2418 -0.0330 -0.0289 0.0181  193 CYS A SG  
1498 N N   . HIS A 197 ? 0.3310 0.2279 0.2171 -0.0366 -0.0274 0.0249  194 HIS A N   
1499 C CA  . HIS A 197 ? 0.3316 0.2196 0.2167 -0.0365 -0.0280 0.0257  194 HIS A CA  
1500 C C   . HIS A 197 ? 0.3496 0.2325 0.2305 -0.0328 -0.0294 0.0286  194 HIS A C   
1501 O O   . HIS A 197 ? 0.3485 0.2357 0.2274 -0.0311 -0.0300 0.0300  194 HIS A O   
1502 C CB  . HIS A 197 ? 0.3309 0.2152 0.2168 -0.0413 -0.0269 0.0271  194 HIS A CB  
1503 C CG  . HIS A 197 ? 0.3336 0.2202 0.2183 -0.0436 -0.0250 0.0303  194 HIS A CG  
1504 N ND1 . HIS A 197 ? 0.3472 0.2289 0.2263 -0.0426 -0.0247 0.0344  194 HIS A ND1 
1505 C CD2 . HIS A 197 ? 0.3271 0.2209 0.2143 -0.0458 -0.0229 0.0301  194 HIS A CD2 
1506 C CE1 . HIS A 197 ? 0.3561 0.2415 0.2342 -0.0451 -0.0221 0.0365  194 HIS A CE1 
1507 N NE2 . HIS A 197 ? 0.3329 0.2263 0.2163 -0.0467 -0.0208 0.0336  194 HIS A NE2 
1508 N N   . PRO A 198 ? 0.3626 0.2357 0.2413 -0.0312 -0.0303 0.0293  195 PRO A N   
1509 C CA  . PRO A 198 ? 0.3837 0.2512 0.2581 -0.0267 -0.0321 0.0321  195 PRO A CA  
1510 C C   . PRO A 198 ? 0.4038 0.2682 0.2724 -0.0278 -0.0320 0.0372  195 PRO A C   
1511 O O   . PRO A 198 ? 0.4207 0.2823 0.2854 -0.0232 -0.0342 0.0395  195 PRO A O   
1512 C CB  . PRO A 198 ? 0.4001 0.2550 0.2723 -0.0257 -0.0327 0.0318  195 PRO A CB  
1513 C CG  . PRO A 198 ? 0.3847 0.2428 0.2609 -0.0273 -0.0318 0.0270  195 PRO A CG  
1514 C CD  . PRO A 198 ? 0.3674 0.2343 0.2470 -0.0326 -0.0303 0.0267  195 PRO A CD  
1515 N N   . TYR A 199 ? 0.4012 0.2663 0.2694 -0.0335 -0.0295 0.0389  196 TYR A N   
1516 C CA  . TYR A 199 ? 0.4111 0.2739 0.2728 -0.0348 -0.0283 0.0439  196 TYR A CA  
1517 C C   . TYR A 199 ? 0.4069 0.2807 0.2678 -0.0340 -0.0279 0.0429  196 TYR A C   
1518 O O   . TYR A 199 ? 0.4141 0.2865 0.2676 -0.0340 -0.0271 0.0466  196 TYR A O   
1519 C CB  . TYR A 199 ? 0.4178 0.2761 0.2798 -0.0413 -0.0250 0.0465  196 TYR A CB  
1520 C CG  . TYR A 199 ? 0.4366 0.2817 0.2973 -0.0430 -0.0257 0.0482  196 TYR A CG  
1521 C CD1 . TYR A 199 ? 0.4587 0.2938 0.3150 -0.0379 -0.0287 0.0487  196 TYR A CD1 
1522 C CD2 . TYR A 199 ? 0.4453 0.2877 0.3090 -0.0499 -0.0233 0.0495  196 TYR A CD2 
1523 C CE1 . TYR A 199 ? 0.4775 0.2982 0.3311 -0.0397 -0.0293 0.0503  196 TYR A CE1 
1524 C CE2 . TYR A 199 ? 0.4689 0.2979 0.3309 -0.0526 -0.0242 0.0511  196 TYR A CE2 
1525 C CZ  . TYR A 199 ? 0.4833 0.3005 0.3395 -0.0475 -0.0272 0.0514  196 TYR A CZ  
1526 O OH  . TYR A 199 ? 0.5203 0.3222 0.3737 -0.0501 -0.0282 0.0526  196 TYR A OH  
1527 N N   . PHE A 200 ? 0.3897 0.2727 0.2567 -0.0332 -0.0285 0.0381  197 PHE A N   
1528 C CA  . PHE A 200 ? 0.3858 0.2782 0.2525 -0.0327 -0.0287 0.0361  197 PHE A CA  
1529 C C   . PHE A 200 ? 0.3801 0.2793 0.2531 -0.0306 -0.0307 0.0315  197 PHE A C   
1530 O O   . PHE A 200 ? 0.3679 0.2715 0.2458 -0.0330 -0.0292 0.0283  197 PHE A O   
1531 C CB  . PHE A 200 ? 0.3912 0.2867 0.2587 -0.0372 -0.0248 0.0359  197 PHE A CB  
1532 C CG  . PHE A 200 ? 0.3949 0.2973 0.2597 -0.0371 -0.0241 0.0342  197 PHE A CG  
1533 C CD1 . PHE A 200 ? 0.4146 0.3178 0.2726 -0.0341 -0.0267 0.0349  197 PHE A CD1 
1534 C CD2 . PHE A 200 ? 0.4031 0.3104 0.2716 -0.0396 -0.0212 0.0316  197 PHE A CD2 
1535 C CE1 . PHE A 200 ? 0.4200 0.3279 0.2740 -0.0342 -0.0264 0.0328  197 PHE A CE1 
1536 C CE2 . PHE A 200 ? 0.4108 0.3224 0.2755 -0.0392 -0.0203 0.0298  197 PHE A CE2 
1537 C CZ  . PHE A 200 ? 0.4198 0.3313 0.2767 -0.0368 -0.0229 0.0302  197 PHE A CZ  
1538 N N   . ASN A 201 ? 0.3775 0.2775 0.2509 -0.0261 -0.0340 0.0314  198 ASN A N   
1539 C CA  . ASN A 201 ? 0.3646 0.2700 0.2454 -0.0241 -0.0349 0.0276  198 ASN A CA  
1540 C C   . ASN A 201 ? 0.3593 0.2751 0.2432 -0.0247 -0.0361 0.0246  198 ASN A C   
1541 O O   . ASN A 201 ? 0.3473 0.2689 0.2380 -0.0246 -0.0358 0.0213  198 ASN A O   
1542 C CB  . ASN A 201 ? 0.3813 0.2824 0.2625 -0.0187 -0.0371 0.0286  198 ASN A CB  
1543 C CG  . ASN A 201 ? 0.4016 0.3064 0.2815 -0.0139 -0.0411 0.0301  198 ASN A CG  
1544 O OD1 . ASN A 201 ? 0.4063 0.3194 0.2867 -0.0145 -0.0429 0.0291  198 ASN A OD1 
1545 N ND2 . ASN A 201 ? 0.4228 0.3207 0.3007 -0.0088 -0.0431 0.0325  198 ASN A ND2 
1546 N N   . ARG A 202 ? 0.3602 0.2776 0.2388 -0.0257 -0.0369 0.0256  199 ARG A N   
1547 C CA  . ARG A 202 ? 0.3663 0.2917 0.2464 -0.0272 -0.0382 0.0224  199 ARG A CA  
1548 C C   . ARG A 202 ? 0.3637 0.2969 0.2505 -0.0246 -0.0417 0.0203  199 ARG A C   
1549 O O   . ARG A 202 ? 0.3633 0.3030 0.2559 -0.0270 -0.0414 0.0167  199 ARG A O   
1550 C CB  . ARG A 202 ? 0.3582 0.2846 0.2414 -0.0314 -0.0348 0.0195  199 ARG A CB  
1551 C CG  . ARG A 202 ? 0.3558 0.2761 0.2369 -0.0335 -0.0312 0.0213  199 ARG A CG  
1552 C CD  . ARG A 202 ? 0.3664 0.2842 0.2401 -0.0342 -0.0300 0.0237  199 ARG A CD  
1553 N NE  . ARG A 202 ? 0.3681 0.2899 0.2390 -0.0351 -0.0302 0.0211  199 ARG A NE  
1554 C CZ  . ARG A 202 ? 0.3673 0.2895 0.2382 -0.0372 -0.0272 0.0193  199 ARG A CZ  
1555 N NH1 . ARG A 202 ? 0.3586 0.2790 0.2333 -0.0388 -0.0241 0.0201  199 ARG A NH1 
1556 N NH2 . ARG A 202 ? 0.3612 0.2853 0.2283 -0.0376 -0.0277 0.0166  199 ARG A NH2 
1557 N N   . SER A 203 ? 0.3719 0.3046 0.2584 -0.0198 -0.0448 0.0225  200 SER A N   
1558 C CA  . SER A 203 ? 0.3893 0.3316 0.2844 -0.0165 -0.0482 0.0206  200 SER A CA  
1559 C C   . SER A 203 ? 0.3831 0.3346 0.2797 -0.0187 -0.0517 0.0179  200 SER A C   
1560 O O   . SER A 203 ? 0.3614 0.3222 0.2677 -0.0201 -0.0520 0.0147  200 SER A O   
1561 C CB  . SER A 203 ? 0.4176 0.3575 0.3118 -0.0100 -0.0516 0.0236  200 SER A CB  
1562 O OG  . SER A 203 ? 0.4637 0.3991 0.3477 -0.0086 -0.0551 0.0270  200 SER A OG  
1563 N N   . LYS A 204 ? 0.3981 0.3471 0.2855 -0.0193 -0.0543 0.0191  201 LYS A N   
1564 C CA  . LYS A 204 ? 0.4112 0.3683 0.2993 -0.0214 -0.0586 0.0159  201 LYS A CA  
1565 C C   . LYS A 204 ? 0.3830 0.3419 0.2745 -0.0274 -0.0553 0.0118  201 LYS A C   
1566 O O   . LYS A 204 ? 0.3694 0.3371 0.2685 -0.0299 -0.0577 0.0083  201 LYS A O   
1567 C CB  . LYS A 204 ? 0.4565 0.4088 0.3311 -0.0205 -0.0618 0.0178  201 LYS A CB  
1568 C CG  . LYS A 204 ? 0.5096 0.4608 0.3803 -0.0144 -0.0669 0.0217  201 LYS A CG  
1569 C CD  . LYS A 204 ? 0.5563 0.5030 0.4122 -0.0136 -0.0706 0.0235  201 LYS A CD  
1570 C CE  . LYS A 204 ? 0.6161 0.5597 0.4663 -0.0072 -0.0756 0.0284  201 LYS A CE  
1571 N NZ  . LYS A 204 ? 0.6525 0.5922 0.4869 -0.0063 -0.0801 0.0299  201 LYS A NZ  
1572 N N   . LEU A 205 ? 0.3641 0.3151 0.2503 -0.0298 -0.0503 0.0123  202 LEU A N   
1573 C CA  . LEU A 205 ? 0.3565 0.3072 0.2448 -0.0346 -0.0471 0.0089  202 LEU A CA  
1574 C C   . LEU A 205 ? 0.3481 0.3036 0.2475 -0.0360 -0.0451 0.0074  202 LEU A C   
1575 O O   . LEU A 205 ? 0.3474 0.3063 0.2511 -0.0399 -0.0448 0.0042  202 LEU A O   
1576 C CB  . LEU A 205 ? 0.3432 0.2854 0.2250 -0.0356 -0.0423 0.0103  202 LEU A CB  
1577 C CG  . LEU A 205 ? 0.3319 0.2724 0.2153 -0.0394 -0.0392 0.0074  202 LEU A CG  
1578 C CD1 . LEU A 205 ? 0.3449 0.2866 0.2246 -0.0417 -0.0416 0.0038  202 LEU A CD1 
1579 C CD2 . LEU A 205 ? 0.3265 0.2605 0.2057 -0.0395 -0.0348 0.0090  202 LEU A CD2 
1580 N N   . LEU A 206 ? 0.3465 0.3013 0.2496 -0.0328 -0.0435 0.0096  203 LEU A N   
1581 C CA  . LEU A 206 ? 0.3416 0.3008 0.2540 -0.0333 -0.0410 0.0082  203 LEU A CA  
1582 C C   . LEU A 206 ? 0.3475 0.3184 0.2690 -0.0340 -0.0440 0.0058  203 LEU A C   
1583 O O   . LEU A 206 ? 0.3324 0.3074 0.2597 -0.0380 -0.0420 0.0035  203 LEU A O   
1584 C CB  . LEU A 206 ? 0.3425 0.2982 0.2557 -0.0288 -0.0395 0.0105  203 LEU A CB  
1585 C CG  . LEU A 206 ? 0.3362 0.2964 0.2577 -0.0283 -0.0365 0.0089  203 LEU A CG  
1586 C CD1 . LEU A 206 ? 0.3270 0.2845 0.2480 -0.0333 -0.0325 0.0073  203 LEU A CD1 
1587 C CD2 . LEU A 206 ? 0.3426 0.2970 0.2628 -0.0235 -0.0351 0.0107  203 LEU A CD2 
1588 N N   . ASP A 207 ? 0.3698 0.3463 0.2930 -0.0302 -0.0489 0.0067  204 ASP A N   
1589 C CA  . ASP A 207 ? 0.3950 0.3848 0.3285 -0.0307 -0.0529 0.0044  204 ASP A CA  
1590 C C   . ASP A 207 ? 0.3865 0.3784 0.3196 -0.0374 -0.0544 0.0011  204 ASP A C   
1591 O O   . ASP A 207 ? 0.3778 0.3790 0.3214 -0.0410 -0.0542 -0.0014 204 ASP A O   
1592 C CB  . ASP A 207 ? 0.4431 0.4371 0.3760 -0.0250 -0.0594 0.0061  204 ASP A CB  
1593 C CG  . ASP A 207 ? 0.4899 0.4837 0.4267 -0.0182 -0.0582 0.0086  204 ASP A CG  
1594 O OD1 . ASP A 207 ? 0.5170 0.5109 0.4594 -0.0184 -0.0526 0.0078  204 ASP A OD1 
1595 O OD2 . ASP A 207 ? 0.5338 0.5269 0.4675 -0.0124 -0.0629 0.0111  204 ASP A OD2 
1596 N N   . PHE A 208 ? 0.3823 0.3660 0.3038 -0.0388 -0.0558 0.0010  205 PHE A N   
1597 C CA  . PHE A 208 ? 0.3810 0.3634 0.2995 -0.0446 -0.0570 -0.0025 205 PHE A CA  
1598 C C   . PHE A 208 ? 0.3708 0.3505 0.2934 -0.0495 -0.0514 -0.0039 205 PHE A C   
1599 O O   . PHE A 208 ? 0.3576 0.3424 0.2867 -0.0547 -0.0521 -0.0068 205 PHE A O   
1600 C CB  . PHE A 208 ? 0.3933 0.3656 0.2972 -0.0440 -0.0577 -0.0021 205 PHE A CB  
1601 C CG  . PHE A 208 ? 0.4069 0.3759 0.3066 -0.0494 -0.0585 -0.0062 205 PHE A CG  
1602 C CD1 . PHE A 208 ? 0.4273 0.4020 0.3277 -0.0517 -0.0649 -0.0094 205 PHE A CD1 
1603 C CD2 . PHE A 208 ? 0.4083 0.3685 0.3040 -0.0519 -0.0534 -0.0071 205 PHE A CD2 
1604 C CE1 . PHE A 208 ? 0.4384 0.4088 0.3349 -0.0570 -0.0659 -0.0137 205 PHE A CE1 
1605 C CE2 . PHE A 208 ? 0.4239 0.3795 0.3154 -0.0563 -0.0542 -0.0110 205 PHE A CE2 
1606 C CZ  . PHE A 208 ? 0.4396 0.3996 0.3309 -0.0590 -0.0604 -0.0144 205 PHE A CZ  
1607 N N   . CYS A 209 ? 0.3531 0.3247 0.2718 -0.0481 -0.0461 -0.0018 206 CYS A N   
1608 C CA  . CYS A 209 ? 0.3594 0.3271 0.2803 -0.0521 -0.0411 -0.0026 206 CYS A CA  
1609 C C   . CYS A 209 ? 0.3498 0.3270 0.2824 -0.0538 -0.0396 -0.0032 206 CYS A C   
1610 O O   . CYS A 209 ? 0.3549 0.3330 0.2910 -0.0591 -0.0381 -0.0050 206 CYS A O   
1611 C CB  . CYS A 209 ? 0.3526 0.3114 0.2680 -0.0498 -0.0368 -0.0002 206 CYS A CB  
1612 S SG  . CYS A 209 ? 0.3796 0.3283 0.2832 -0.0492 -0.0368 0.0000  206 CYS A SG  
1613 N N   . LYS A 210 ? 0.3650 0.3494 0.3039 -0.0493 -0.0397 -0.0018 207 LYS A N   
1614 C CA  . LYS A 210 ? 0.3682 0.3635 0.3195 -0.0502 -0.0375 -0.0025 207 LYS A CA  
1615 C C   . LYS A 210 ? 0.3793 0.3846 0.3388 -0.0554 -0.0410 -0.0053 207 LYS A C   
1616 O O   . LYS A 210 ? 0.3716 0.3807 0.3377 -0.0606 -0.0375 -0.0064 207 LYS A O   
1617 C CB  . LYS A 210 ? 0.3927 0.3941 0.3490 -0.0431 -0.0382 -0.0010 207 LYS A CB  
1618 C CG  . LYS A 210 ? 0.4080 0.3999 0.3583 -0.0394 -0.0337 0.0010  207 LYS A CG  
1619 C CD  . LYS A 210 ? 0.4337 0.4289 0.3875 -0.0320 -0.0343 0.0023  207 LYS A CD  
1620 C CE  . LYS A 210 ? 0.4561 0.4404 0.4031 -0.0298 -0.0298 0.0036  207 LYS A CE  
1621 N NZ  . LYS A 210 ? 0.4969 0.4815 0.4458 -0.0225 -0.0300 0.0045  207 LYS A NZ  
1622 N N   . SER A 211 ? 0.3878 0.3963 0.3458 -0.0546 -0.0478 -0.0063 208 SER A N   
1623 C CA  . SER A 211 ? 0.4152 0.4345 0.3819 -0.0597 -0.0526 -0.0094 208 SER A CA  
1624 C C   . SER A 211 ? 0.4204 0.4326 0.3837 -0.0680 -0.0508 -0.0118 208 SER A C   
1625 O O   . SER A 211 ? 0.4308 0.4517 0.4035 -0.0739 -0.0529 -0.0143 208 SER A O   
1626 C CB  . SER A 211 ? 0.4291 0.4516 0.3923 -0.0568 -0.0611 -0.0101 208 SER A CB  
1627 O OG  . SER A 211 ? 0.4331 0.4421 0.3807 -0.0574 -0.0622 -0.0105 208 SER A OG  
1628 N N   . LYS A 212 ? 0.4139 0.4112 0.3649 -0.0683 -0.0475 -0.0111 209 LYS A N   
1629 C CA  . LYS A 212 ? 0.4371 0.4241 0.3823 -0.0748 -0.0459 -0.0131 209 LYS A CA  
1630 C C   . LYS A 212 ? 0.4230 0.4046 0.3690 -0.0771 -0.0386 -0.0113 209 LYS A C   
1631 O O   . LYS A 212 ? 0.4192 0.3900 0.3589 -0.0813 -0.0369 -0.0121 209 LYS A O   
1632 C CB  . LYS A 212 ? 0.4407 0.4148 0.3712 -0.0725 -0.0476 -0.0136 209 LYS A CB  
1633 C CG  . LYS A 212 ? 0.4726 0.4499 0.3988 -0.0702 -0.0544 -0.0152 209 LYS A CG  
1634 C CD  . LYS A 212 ? 0.5073 0.4920 0.4397 -0.0762 -0.0601 -0.0191 209 LYS A CD  
1635 C CE  . LYS A 212 ? 0.5341 0.5201 0.4593 -0.0737 -0.0676 -0.0209 209 LYS A CE  
1636 N NZ  . LYS A 212 ? 0.5731 0.5666 0.5044 -0.0798 -0.0741 -0.0252 209 LYS A NZ  
1637 N N   . ASP A 213 ? 0.4301 0.4176 0.3820 -0.0737 -0.0347 -0.0089 210 ASP A N   
1638 C CA  . ASP A 213 ? 0.4344 0.4167 0.3852 -0.0747 -0.0277 -0.0069 210 ASP A CA  
1639 C C   . ASP A 213 ? 0.3995 0.3660 0.3370 -0.0730 -0.0262 -0.0057 210 ASP A C   
1640 O O   . ASP A 213 ? 0.3943 0.3523 0.3277 -0.0763 -0.0225 -0.0049 210 ASP A O   
1641 C CB  . ASP A 213 ? 0.4871 0.4730 0.4451 -0.0826 -0.0246 -0.0078 210 ASP A CB  
1642 C CG  . ASP A 213 ? 0.5118 0.4949 0.4693 -0.0833 -0.0172 -0.0055 210 ASP A CG  
1643 O OD1 . ASP A 213 ? 0.5533 0.5374 0.5096 -0.0773 -0.0148 -0.0038 210 ASP A OD1 
1644 O OD2 . ASP A 213 ? 0.5892 0.5688 0.5470 -0.0901 -0.0138 -0.0053 210 ASP A OD2 
1645 N N   . ILE A 214 ? 0.3688 0.3316 0.3000 -0.0680 -0.0291 -0.0052 211 ILE A N   
1646 C CA  . ILE A 214 ? 0.3519 0.3025 0.2727 -0.0652 -0.0276 -0.0038 211 ILE A CA  
1647 C C   . ILE A 214 ? 0.3436 0.2950 0.2643 -0.0599 -0.0259 -0.0013 211 ILE A C   
1648 O O   . ILE A 214 ? 0.3336 0.2919 0.2578 -0.0564 -0.0281 -0.0010 211 ILE A O   
1649 C CB  . ILE A 214 ? 0.3553 0.3018 0.2694 -0.0637 -0.0314 -0.0051 211 ILE A CB  
1650 C CG1 . ILE A 214 ? 0.3705 0.3143 0.2832 -0.0689 -0.0335 -0.0083 211 ILE A CG1 
1651 C CG2 . ILE A 214 ? 0.3469 0.2841 0.2531 -0.0603 -0.0296 -0.0035 211 ILE A CG2 
1652 C CD1 . ILE A 214 ? 0.3808 0.3222 0.2867 -0.0672 -0.0375 -0.0102 211 ILE A CD1 
1653 N N   . VAL A 215 ? 0.3241 0.2680 0.2403 -0.0594 -0.0225 0.0001  212 VAL A N   
1654 C CA  . VAL A 215 ? 0.3184 0.2609 0.2331 -0.0549 -0.0211 0.0020  212 VAL A CA  
1655 C C   . VAL A 215 ? 0.3149 0.2530 0.2245 -0.0517 -0.0235 0.0029  212 VAL A C   
1656 O O   . VAL A 215 ? 0.3117 0.2438 0.2166 -0.0527 -0.0237 0.0027  212 VAL A O   
1657 C CB  . VAL A 215 ? 0.3148 0.2503 0.2254 -0.0558 -0.0175 0.0030  212 VAL A CB  
1658 C CG1 . VAL A 215 ? 0.3036 0.2360 0.2112 -0.0515 -0.0170 0.0044  212 VAL A CG1 
1659 C CG2 . VAL A 215 ? 0.3209 0.2612 0.2361 -0.0591 -0.0140 0.0026  212 VAL A CG2 
1660 N N   . LEU A 216 ? 0.3106 0.2511 0.2212 -0.0478 -0.0245 0.0041  213 LEU A N   
1661 C CA  . LEU A 216 ? 0.3193 0.2549 0.2249 -0.0453 -0.0256 0.0057  213 LEU A CA  
1662 C C   . LEU A 216 ? 0.3175 0.2469 0.2206 -0.0446 -0.0236 0.0068  213 LEU A C   
1663 O O   . LEU A 216 ? 0.3289 0.2587 0.2335 -0.0431 -0.0224 0.0070  213 LEU A O   
1664 C CB  . LEU A 216 ? 0.3314 0.2706 0.2380 -0.0419 -0.0280 0.0070  213 LEU A CB  
1665 C CG  . LEU A 216 ? 0.3468 0.2817 0.2479 -0.0406 -0.0290 0.0088  213 LEU A CG  
1666 C CD1 . LEU A 216 ? 0.3724 0.3105 0.2720 -0.0384 -0.0321 0.0097  213 LEU A CD1 
1667 C CD2 . LEU A 216 ? 0.3617 0.2907 0.2610 -0.0393 -0.0275 0.0108  213 LEU A CD2 
1668 N N   . VAL A 217 ? 0.2968 0.2210 0.1963 -0.0453 -0.0235 0.0073  214 VAL A N   
1669 C CA  . VAL A 217 ? 0.2832 0.2020 0.1806 -0.0447 -0.0228 0.0083  214 VAL A CA  
1670 C C   . VAL A 217 ? 0.2850 0.2024 0.1817 -0.0434 -0.0238 0.0099  214 VAL A C   
1671 O O   . VAL A 217 ? 0.2918 0.2101 0.1880 -0.0437 -0.0240 0.0102  214 VAL A O   
1672 C CB  . VAL A 217 ? 0.2836 0.1982 0.1787 -0.0464 -0.0223 0.0078  214 VAL A CB  
1673 C CG1 . VAL A 217 ? 0.2822 0.1921 0.1753 -0.0457 -0.0229 0.0087  214 VAL A CG1 
1674 C CG2 . VAL A 217 ? 0.2881 0.2026 0.1829 -0.0485 -0.0208 0.0068  214 VAL A CG2 
1675 N N   . ALA A 218 ? 0.2762 0.1912 0.1728 -0.0421 -0.0241 0.0108  215 ALA A N   
1676 C CA  . ALA A 218 ? 0.2759 0.1887 0.1719 -0.0416 -0.0248 0.0128  215 ALA A CA  
1677 C C   . ALA A 218 ? 0.2740 0.1838 0.1702 -0.0432 -0.0251 0.0133  215 ALA A C   
1678 O O   . ALA A 218 ? 0.2843 0.1905 0.1796 -0.0436 -0.0258 0.0124  215 ALA A O   
1679 C CB  . ALA A 218 ? 0.2842 0.1942 0.1796 -0.0395 -0.0253 0.0134  215 ALA A CB  
1680 N N   . TYR A 219 ? 0.2695 0.1811 0.1668 -0.0440 -0.0246 0.0145  216 TYR A N   
1681 C CA  . TYR A 219 ? 0.2794 0.1902 0.1793 -0.0456 -0.0250 0.0154  216 TYR A CA  
1682 C C   . TYR A 219 ? 0.2902 0.1992 0.1904 -0.0466 -0.0247 0.0179  216 TYR A C   
1683 O O   . TYR A 219 ? 0.3014 0.2103 0.1990 -0.0455 -0.0239 0.0192  216 TYR A O   
1684 C CB  . TYR A 219 ? 0.2771 0.1918 0.1795 -0.0457 -0.0241 0.0148  216 TYR A CB  
1685 C CG  . TYR A 219 ? 0.2721 0.1905 0.1746 -0.0453 -0.0218 0.0157  216 TYR A CG  
1686 C CD1 . TYR A 219 ? 0.2826 0.2025 0.1870 -0.0465 -0.0202 0.0180  216 TYR A CD1 
1687 C CD2 . TYR A 219 ? 0.2867 0.2065 0.1869 -0.0441 -0.0209 0.0140  216 TYR A CD2 
1688 C CE1 . TYR A 219 ? 0.2900 0.2132 0.1930 -0.0461 -0.0173 0.0188  216 TYR A CE1 
1689 C CE2 . TYR A 219 ? 0.2879 0.2104 0.1864 -0.0434 -0.0186 0.0142  216 TYR A CE2 
1690 C CZ  . TYR A 219 ? 0.2963 0.2208 0.1961 -0.0442 -0.0165 0.0167  216 TYR A CZ  
1691 O OH  . TYR A 219 ? 0.3001 0.2268 0.1968 -0.0434 -0.0136 0.0169  216 TYR A OH  
1692 N N   . SER A 220 ? 0.2929 0.2006 0.1963 -0.0488 -0.0255 0.0186  217 SER A N   
1693 C CA  . SER A 220 ? 0.3047 0.2090 0.2086 -0.0510 -0.0253 0.0211  217 SER A CA  
1694 C C   . SER A 220 ? 0.3043 0.2016 0.2031 -0.0492 -0.0263 0.0213  217 SER A C   
1695 O O   . SER A 220 ? 0.3086 0.2019 0.2053 -0.0496 -0.0257 0.0240  217 SER A O   
1696 C CB  . SER A 220 ? 0.3150 0.2235 0.2203 -0.0521 -0.0222 0.0237  217 SER A CB  
1697 O OG  . SER A 220 ? 0.3088 0.2243 0.2197 -0.0528 -0.0210 0.0229  217 SER A OG  
1698 N N   . ALA A 221 ? 0.2978 0.1929 0.1945 -0.0473 -0.0277 0.0187  218 ALA A N   
1699 C CA  . ALA A 221 ? 0.3032 0.1928 0.1960 -0.0444 -0.0282 0.0182  218 ALA A CA  
1700 C C   . ALA A 221 ? 0.3178 0.1983 0.2089 -0.0459 -0.0296 0.0188  218 ALA A C   
1701 O O   . ALA A 221 ? 0.3296 0.2044 0.2173 -0.0432 -0.0299 0.0191  218 ALA A O   
1702 C CB  . ALA A 221 ? 0.2973 0.1877 0.1887 -0.0424 -0.0282 0.0152  218 ALA A CB  
1703 N N   . LEU A 222 ? 0.3248 0.2042 0.2184 -0.0499 -0.0308 0.0189  219 LEU A N   
1704 C CA  . LEU A 222 ? 0.3504 0.2206 0.2428 -0.0527 -0.0327 0.0193  219 LEU A CA  
1705 C C   . LEU A 222 ? 0.3559 0.2272 0.2520 -0.0568 -0.0314 0.0231  219 LEU A C   
1706 O O   . LEU A 222 ? 0.3690 0.2335 0.2656 -0.0607 -0.0328 0.0238  219 LEU A O   
1707 C CB  . LEU A 222 ? 0.3567 0.2248 0.2496 -0.0551 -0.0357 0.0163  219 LEU A CB  
1708 C CG  . LEU A 222 ? 0.3622 0.2287 0.2500 -0.0516 -0.0364 0.0128  219 LEU A CG  
1709 C CD1 . LEU A 222 ? 0.3707 0.2341 0.2571 -0.0541 -0.0401 0.0101  219 LEU A CD1 
1710 C CD2 . LEU A 222 ? 0.3766 0.2352 0.2584 -0.0476 -0.0355 0.0117  219 LEU A CD2 
1711 N N   . GLY A 223 ? 0.3520 0.2310 0.2499 -0.0561 -0.0286 0.0253  220 GLY A N   
1712 C CA  . GLY A 223 ? 0.3551 0.2341 0.2542 -0.0593 -0.0261 0.0295  220 GLY A CA  
1713 C C   . GLY A 223 ? 0.3515 0.2397 0.2585 -0.0632 -0.0245 0.0300  220 GLY A C   
1714 O O   . GLY A 223 ? 0.3618 0.2510 0.2711 -0.0668 -0.0218 0.0335  220 GLY A O   
1715 N N   . SER A 224 ? 0.3412 0.2363 0.2523 -0.0621 -0.0258 0.0269  221 SER A N   
1716 C CA  . SER A 224 ? 0.3379 0.2433 0.2577 -0.0642 -0.0247 0.0268  221 SER A CA  
1717 C C   . SER A 224 ? 0.3470 0.2522 0.2739 -0.0696 -0.0270 0.0269  221 SER A C   
1718 O O   . SER A 224 ? 0.3602 0.2560 0.2843 -0.0724 -0.0290 0.0274  221 SER A O   
1719 C CB  . SER A 224 ? 0.3425 0.2541 0.2635 -0.0644 -0.0197 0.0297  221 SER A CB  
1720 O OG  . SER A 224 ? 0.3600 0.2700 0.2835 -0.0693 -0.0175 0.0332  221 SER A OG  
1721 N N   . GLN A 225 ? 0.3509 0.2664 0.2869 -0.0705 -0.0272 0.0261  222 GLN A N   
1722 C CA  . GLN A 225 ? 0.3610 0.2809 0.3071 -0.0756 -0.0300 0.0257  222 GLN A CA  
1723 C C   . GLN A 225 ? 0.3879 0.3115 0.3403 -0.0809 -0.0256 0.0296  222 GLN A C   
1724 O O   . GLN A 225 ? 0.3822 0.3098 0.3443 -0.0863 -0.0274 0.0298  222 GLN A O   
1725 C CB  . GLN A 225 ? 0.3476 0.2780 0.3011 -0.0730 -0.0318 0.0235  222 GLN A CB  
1726 C CG  . GLN A 225 ? 0.3449 0.2704 0.2905 -0.0682 -0.0355 0.0204  222 GLN A CG  
1727 C CD  . GLN A 225 ? 0.3446 0.2768 0.2959 -0.0661 -0.0394 0.0183  222 GLN A CD  
1728 O OE1 . GLN A 225 ? 0.3617 0.2995 0.3223 -0.0693 -0.0429 0.0180  222 GLN A OE1 
1729 N NE2 . GLN A 225 ? 0.3156 0.2463 0.2608 -0.0610 -0.0395 0.0169  222 GLN A NE2 
1730 N N   . ARG A 226 ? 0.4095 0.3324 0.3567 -0.0795 -0.0200 0.0325  223 ARG A N   
1731 C CA  . ARG A 226 ? 0.4470 0.3717 0.3974 -0.0845 -0.0148 0.0370  223 ARG A CA  
1732 C C   . ARG A 226 ? 0.4659 0.4055 0.4313 -0.0878 -0.0125 0.0372  223 ARG A C   
1733 O O   . ARG A 226 ? 0.4845 0.4264 0.4573 -0.0946 -0.0104 0.0400  223 ARG A O   
1734 C CB  . ARG A 226 ? 0.4750 0.3866 0.4214 -0.0896 -0.0168 0.0389  223 ARG A CB  
1735 C CG  . ARG A 226 ? 0.4704 0.3681 0.4029 -0.0851 -0.0189 0.0385  223 ARG A CG  
1736 C CD  . ARG A 226 ? 0.4880 0.3715 0.4163 -0.0896 -0.0207 0.0404  223 ARG A CD  
1737 N NE  . ARG A 226 ? 0.5008 0.3833 0.4298 -0.0946 -0.0155 0.0459  223 ARG A NE  
1738 C CZ  . ARG A 226 ? 0.4975 0.3755 0.4172 -0.0921 -0.0114 0.0499  223 ARG A CZ  
1739 N NH1 . ARG A 226 ? 0.4778 0.3525 0.3881 -0.0847 -0.0125 0.0488  223 ARG A NH1 
1740 N NH2 . ARG A 226 ? 0.5187 0.3958 0.4386 -0.0973 -0.0063 0.0552  223 ARG A NH2 
1741 N N   . ASP A 227 ? 0.4741 0.4241 0.4442 -0.0830 -0.0122 0.0347  224 ASP A N   
1742 C CA  A ASP A 227 ? 0.4904 0.4565 0.4756 -0.0843 -0.0092 0.0348  224 ASP A CA  
1743 C CA  B ASP A 227 ? 0.4938 0.4599 0.4791 -0.0844 -0.0092 0.0348  224 ASP A CA  
1744 C C   . ASP A 227 ? 0.5054 0.4761 0.4904 -0.0861 -0.0002 0.0387  224 ASP A C   
1745 O O   . ASP A 227 ? 0.5028 0.4697 0.4766 -0.0814 0.0035  0.0392  224 ASP A O   
1746 C CB  A ASP A 227 ? 0.4796 0.4532 0.4677 -0.0774 -0.0110 0.0311  224 ASP A CB  
1747 C CB  B ASP A 227 ? 0.4882 0.4623 0.4770 -0.0776 -0.0110 0.0311  224 ASP A CB  
1748 C CG  A ASP A 227 ? 0.4932 0.4837 0.4980 -0.0777 -0.0087 0.0308  224 ASP A CG  
1749 C CG  B ASP A 227 ? 0.5053 0.4965 0.5100 -0.0778 -0.0074 0.0312  224 ASP A CG  
1750 O OD1 A ASP A 227 ? 0.4903 0.4887 0.4991 -0.0786 -0.0009 0.0331  224 ASP A OD1 
1751 O OD1 B ASP A 227 ? 0.5213 0.5196 0.5384 -0.0843 -0.0071 0.0329  224 ASP A OD1 
1752 O OD2 A ASP A 227 ? 0.4824 0.4784 0.4960 -0.0769 -0.0147 0.0284  224 ASP A OD2 
1753 O OD2 B ASP A 227 ? 0.4990 0.4963 0.5040 -0.0715 -0.0045 0.0296  224 ASP A OD2 
1754 N N   . LYS A 228 ? 0.5534 0.5322 0.5504 -0.0928 0.0032  0.0414  225 LYS A N   
1755 C CA  . LYS A 228 ? 0.6133 0.5981 0.6121 -0.0960 0.0128  0.0457  225 LYS A CA  
1756 C C   . LYS A 228 ? 0.5848 0.5769 0.5798 -0.0890 0.0192  0.0449  225 LYS A C   
1757 O O   . LYS A 228 ? 0.5915 0.5811 0.5780 -0.0898 0.0265  0.0485  225 LYS A O   
1758 C CB  . LYS A 228 ? 0.6890 0.6898 0.7083 -0.1022 0.0152  0.0467  225 LYS A CB  
1759 C CG  . LYS A 228 ? 0.7466 0.7435 0.7736 -0.1113 0.0102  0.0478  225 LYS A CG  
1760 C CD  . LYS A 228 ? 0.8085 0.8182 0.8515 -0.1198 0.0164  0.0514  225 LYS A CD  
1761 C CE  . LYS A 228 ? 0.8447 0.8772 0.9054 -0.1167 0.0205  0.0496  225 LYS A CE  
1762 N NZ  . LYS A 228 ? 0.8977 0.9445 0.9759 -0.1257 0.0272  0.0532  225 LYS A NZ  
1763 N N   . ARG A 229 ? 0.5476 0.5485 0.5490 -0.0830 0.0170  0.0406  226 ARG A N   
1764 C CA  . ARG A 229 ? 0.5572 0.5654 0.5566 -0.0762 0.0230  0.0390  226 ARG A CA  
1765 C C   . ARG A 229 ? 0.5389 0.5340 0.5184 -0.0713 0.0231  0.0384  226 ARG A C   
1766 O O   . ARG A 229 ? 0.5223 0.5201 0.4958 -0.0671 0.0291  0.0378  226 ARG A O   
1767 C CB  . ARG A 229 ? 0.5675 0.5860 0.5785 -0.0707 0.0194  0.0345  226 ARG A CB  
1768 C CG  . ARG A 229 ? 0.5980 0.6327 0.6306 -0.0747 0.0196  0.0350  226 ARG A CG  
1769 C CD  . ARG A 229 ? 0.6187 0.6603 0.6620 -0.0701 0.0122  0.0310  226 ARG A CD  
1770 N NE  . ARG A 229 ? 0.6195 0.6505 0.6584 -0.0717 0.0021  0.0296  226 ARG A NE  
1771 C CZ  . ARG A 229 ? 0.6117 0.6481 0.6609 -0.0707 -0.0057 0.0273  226 ARG A CZ  
1772 N NH1 . ARG A 229 ? 0.6352 0.6883 0.7013 -0.0679 -0.0051 0.0261  226 ARG A NH1 
1773 N NH2 . ARG A 229 ? 0.5880 0.6135 0.6305 -0.0721 -0.0142 0.0261  226 ARG A NH2 
1774 N N   . TRP A 230 ? 0.5208 0.5031 0.4911 -0.0714 0.0163  0.0379  227 TRP A N   
1775 C CA  . TRP A 230 ? 0.5269 0.4984 0.4805 -0.0666 0.0150  0.0367  227 TRP A CA  
1776 C C   . TRP A 230 ? 0.5260 0.4852 0.4678 -0.0697 0.0146  0.0405  227 TRP A C   
1777 O O   . TRP A 230 ? 0.5601 0.5134 0.4889 -0.0664 0.0159  0.0408  227 TRP A O   
1778 C CB  . TRP A 230 ? 0.5208 0.4888 0.4737 -0.0625 0.0078  0.0324  227 TRP A CB  
1779 C CG  . TRP A 230 ? 0.5288 0.5066 0.4903 -0.0581 0.0084  0.0291  227 TRP A CG  
1780 C CD1 . TRP A 230 ? 0.5412 0.5265 0.5159 -0.0583 0.0048  0.0275  227 TRP A CD1 
1781 C CD2 . TRP A 230 ? 0.5533 0.5339 0.5105 -0.0526 0.0126  0.0269  227 TRP A CD2 
1782 N NE1 . TRP A 230 ? 0.5682 0.5608 0.5475 -0.0527 0.0066  0.0248  227 TRP A NE1 
1783 C CE2 . TRP A 230 ? 0.5661 0.5555 0.5346 -0.0491 0.0116  0.0241  227 TRP A CE2 
1784 C CE3 . TRP A 230 ? 0.5751 0.5508 0.5190 -0.0500 0.0166  0.0267  227 TRP A CE3 
1785 C CZ2 . TRP A 230 ? 0.5720 0.5646 0.5392 -0.0430 0.0149  0.0211  227 TRP A CZ2 
1786 C CZ3 . TRP A 230 ? 0.5899 0.5687 0.5319 -0.0444 0.0196  0.0233  227 TRP A CZ3 
1787 C CH2 . TRP A 230 ? 0.5874 0.5741 0.5409 -0.0409 0.0190  0.0205  227 TRP A CH2 
1788 N N   . VAL A 231 ? 0.5222 0.4774 0.4684 -0.0755 0.0123  0.0429  228 VAL A N   
1789 C CA  . VAL A 231 ? 0.5231 0.4640 0.4585 -0.0776 0.0098  0.0458  228 VAL A CA  
1790 C C   . VAL A 231 ? 0.5387 0.4780 0.4760 -0.0847 0.0146  0.0513  228 VAL A C   
1791 O O   . VAL A 231 ? 0.5719 0.5180 0.5226 -0.0903 0.0150  0.0517  228 VAL A O   
1792 C CB  . VAL A 231 ? 0.4967 0.4304 0.4332 -0.0777 0.0018  0.0432  228 VAL A CB  
1793 C CG1 . VAL A 231 ? 0.4953 0.4141 0.4207 -0.0785 -0.0005 0.0457  228 VAL A CG1 
1794 C CG2 . VAL A 231 ? 0.4763 0.4119 0.4115 -0.0716 -0.0022 0.0382  228 VAL A CG2 
1795 N N   . ASP A 232 ? 0.5411 0.4713 0.4651 -0.0846 0.0177  0.0554  229 ASP A N   
1796 C CA  . ASP A 232 ? 0.5661 0.4910 0.4880 -0.0912 0.0224  0.0616  229 ASP A CA  
1797 C C   . ASP A 232 ? 0.5671 0.4825 0.4929 -0.0964 0.0169  0.0622  229 ASP A C   
1798 O O   . ASP A 232 ? 0.5386 0.4422 0.4563 -0.0933 0.0111  0.0610  229 ASP A O   
1799 C CB  . ASP A 232 ? 0.5800 0.4956 0.4838 -0.0882 0.0254  0.0655  229 ASP A CB  
1800 C CG  . ASP A 232 ? 0.6276 0.5354 0.5258 -0.0945 0.0307  0.0727  229 ASP A CG  
1801 O OD1 . ASP A 232 ? 0.6374 0.5478 0.5469 -0.1020 0.0327  0.0747  229 ASP A OD1 
1802 O OD2 . ASP A 232 ? 0.6687 0.5667 0.5506 -0.0919 0.0320  0.0764  229 ASP A OD2 
1803 N N   . PRO A 233 ? 0.5957 0.5156 0.5342 -0.1045 0.0187  0.0639  230 PRO A N   
1804 C CA  . PRO A 233 ? 0.6052 0.5142 0.5463 -0.1102 0.0133  0.0643  230 PRO A CA  
1805 C C   . PRO A 233 ? 0.6167 0.5061 0.5424 -0.1113 0.0132  0.0692  230 PRO A C   
1806 O O   . PRO A 233 ? 0.6286 0.5055 0.5523 -0.1133 0.0078  0.0685  230 PRO A O   
1807 C CB  . PRO A 233 ? 0.6233 0.5424 0.5808 -0.1198 0.0168  0.0662  230 PRO A CB  
1808 C CG  . PRO A 233 ? 0.6234 0.5618 0.5896 -0.1177 0.0237  0.0657  230 PRO A CG  
1809 C CD  . PRO A 233 ? 0.6112 0.5466 0.5619 -0.1091 0.0263  0.0658  230 PRO A CD  
1810 N N   . ASN A 234 ? 0.6178 0.5040 0.5319 -0.1095 0.0191  0.0740  231 ASN A N   
1811 C CA  . ASN A 234 ? 0.6392 0.5061 0.5369 -0.1091 0.0187  0.0793  231 ASN A CA  
1812 C C   . ASN A 234 ? 0.6145 0.4730 0.5010 -0.0997 0.0121  0.0762  231 ASN A C   
1813 O O   . ASN A 234 ? 0.6217 0.4636 0.4966 -0.0983 0.0096  0.0794  231 ASN A O   
1814 C CB  . ASN A 234 ? 0.6753 0.5414 0.5630 -0.1104 0.0270  0.0859  231 ASN A CB  
1815 C CG  . ASN A 234 ? 0.7005 0.5746 0.5989 -0.1203 0.0348  0.0899  231 ASN A CG  
1816 O OD1 . ASN A 234 ? 0.7027 0.5739 0.6111 -0.1282 0.0333  0.0905  231 ASN A OD1 
1817 N ND2 . ASN A 234 ? 0.6971 0.5823 0.5944 -0.1201 0.0432  0.0921  231 ASN A ND2 
1818 N N   . SER A 235 ? 0.5691 0.4382 0.4594 -0.0935 0.0093  0.0703  232 SER A N   
1819 C CA  . SER A 235 ? 0.5456 0.4090 0.4271 -0.0851 0.0037  0.0673  232 SER A CA  
1820 C C   . SER A 235 ? 0.5500 0.4009 0.4314 -0.0854 -0.0024 0.0656  232 SER A C   
1821 O O   . SER A 235 ? 0.5528 0.4037 0.4435 -0.0908 -0.0039 0.0639  232 SER A O   
1822 C CB  . SER A 235 ? 0.5231 0.3998 0.4099 -0.0801 0.0023  0.0615  232 SER A CB  
1823 O OG  . SER A 235 ? 0.4891 0.3720 0.3886 -0.0825 -0.0004 0.0571  232 SER A OG  
1824 N N   . PRO A 236 ? 0.5634 0.4029 0.4341 -0.0793 -0.0062 0.0661  233 PRO A N   
1825 C CA  . PRO A 236 ? 0.5544 0.3813 0.4239 -0.0783 -0.0115 0.0640  233 PRO A CA  
1826 C C   . PRO A 236 ? 0.5162 0.3506 0.3948 -0.0772 -0.0152 0.0570  233 PRO A C   
1827 O O   . PRO A 236 ? 0.4751 0.3207 0.3562 -0.0730 -0.0155 0.0536  233 PRO A O   
1828 C CB  . PRO A 236 ? 0.5768 0.3955 0.4347 -0.0698 -0.0143 0.0650  233 PRO A CB  
1829 C CG  . PRO A 236 ? 0.5702 0.4008 0.4252 -0.0661 -0.0119 0.0656  233 PRO A CG  
1830 C CD  . PRO A 236 ? 0.5764 0.4145 0.4354 -0.0730 -0.0057 0.0685  233 PRO A CD  
1831 N N   . VAL A 237 ? 0.5169 0.3430 0.3985 -0.0809 -0.0183 0.0550  234 VAL A N   
1832 C CA  . VAL A 237 ? 0.4984 0.3297 0.3873 -0.0808 -0.0221 0.0486  234 VAL A CA  
1833 C C   . VAL A 237 ? 0.4844 0.3096 0.3666 -0.0728 -0.0257 0.0450  234 VAL A C   
1834 O O   . VAL A 237 ? 0.5079 0.3182 0.3838 -0.0716 -0.0279 0.0452  234 VAL A O   
1835 C CB  . VAL A 237 ? 0.5248 0.3490 0.4187 -0.0886 -0.0243 0.0477  234 VAL A CB  
1836 C CG1 . VAL A 237 ? 0.5178 0.3461 0.4166 -0.0878 -0.0290 0.0412  234 VAL A CG1 
1837 C CG2 . VAL A 237 ? 0.5387 0.3698 0.4409 -0.0973 -0.0202 0.0519  234 VAL A CG2 
1838 N N   . LEU A 238 ? 0.4442 0.2804 0.3283 -0.0677 -0.0261 0.0415  235 LEU A N   
1839 C CA  . LEU A 238 ? 0.4400 0.2727 0.3189 -0.0602 -0.0285 0.0385  235 LEU A CA  
1840 C C   . LEU A 238 ? 0.4525 0.2730 0.3290 -0.0602 -0.0319 0.0351  235 LEU A C   
1841 O O   . LEU A 238 ? 0.4605 0.2707 0.3303 -0.0552 -0.0330 0.0352  235 LEU A O   
1842 C CB  . LEU A 238 ? 0.4136 0.2598 0.2963 -0.0567 -0.0284 0.0348  235 LEU A CB  
1843 C CG  . LEU A 238 ? 0.4131 0.2583 0.2921 -0.0495 -0.0299 0.0319  235 LEU A CG  
1844 C CD1 . LEU A 238 ? 0.4239 0.2674 0.2979 -0.0447 -0.0295 0.0352  235 LEU A CD1 
1845 C CD2 . LEU A 238 ? 0.3911 0.2479 0.2744 -0.0483 -0.0298 0.0282  235 LEU A CD2 
1846 N N   . LEU A 239 ? 0.4598 0.2813 0.3409 -0.0648 -0.0338 0.0318  236 LEU A N   
1847 C CA  . LEU A 239 ? 0.4809 0.2915 0.3580 -0.0639 -0.0373 0.0272  236 LEU A CA  
1848 C C   . LEU A 239 ? 0.5103 0.3032 0.3823 -0.0670 -0.0386 0.0290  236 LEU A C   
1849 O O   . LEU A 239 ? 0.5208 0.3017 0.3877 -0.0661 -0.0416 0.0250  236 LEU A O   
1850 C CB  . LEU A 239 ? 0.4767 0.2942 0.3593 -0.0680 -0.0397 0.0233  236 LEU A CB  
1851 C CG  . LEU A 239 ? 0.4556 0.2876 0.3415 -0.0644 -0.0388 0.0213  236 LEU A CG  
1852 C CD1 . LEU A 239 ? 0.4579 0.2944 0.3477 -0.0678 -0.0421 0.0177  236 LEU A CD1 
1853 C CD2 . LEU A 239 ? 0.4530 0.2837 0.3328 -0.0566 -0.0379 0.0191  236 LEU A CD2 
1854 N N   . GLU A 240 ? 0.5212 0.3109 0.3931 -0.0705 -0.0364 0.0347  237 GLU A N   
1855 C CA  . GLU A 240 ? 0.5605 0.3310 0.4260 -0.0731 -0.0372 0.0375  237 GLU A CA  
1856 C C   . GLU A 240 ? 0.5565 0.3193 0.4136 -0.0654 -0.0361 0.0409  237 GLU A C   
1857 O O   . GLU A 240 ? 0.5723 0.3184 0.4227 -0.0663 -0.0364 0.0443  237 GLU A O   
1858 C CB  . GLU A 240 ? 0.5949 0.3656 0.4653 -0.0828 -0.0351 0.0424  237 GLU A CB  
1859 C CG  . GLU A 240 ? 0.6198 0.3982 0.5001 -0.0909 -0.0370 0.0393  237 GLU A CG  
1860 C CD  . GLU A 240 ? 0.6594 0.4423 0.5477 -0.1008 -0.0341 0.0441  237 GLU A CD  
1861 O OE1 . GLU A 240 ? 0.7091 0.4875 0.5935 -0.1019 -0.0300 0.0504  237 GLU A OE1 
1862 O OE2 . GLU A 240 ? 0.6952 0.4868 0.5935 -0.1072 -0.0359 0.0417  237 GLU A OE2 
1863 N N   . ASP A 241 ? 0.5313 0.3057 0.3888 -0.0582 -0.0350 0.0404  238 ASP A N   
1864 C CA  . ASP A 241 ? 0.5507 0.3195 0.4012 -0.0502 -0.0349 0.0434  238 ASP A CA  
1865 C C   . ASP A 241 ? 0.5656 0.3163 0.4090 -0.0453 -0.0375 0.0414  238 ASP A C   
1866 O O   . ASP A 241 ? 0.5463 0.2962 0.3903 -0.0425 -0.0390 0.0355  238 ASP A O   
1867 C CB  . ASP A 241 ? 0.5354 0.3204 0.3890 -0.0437 -0.0343 0.0416  238 ASP A CB  
1868 C CG  . ASP A 241 ? 0.5618 0.3425 0.4093 -0.0361 -0.0350 0.0450  238 ASP A CG  
1869 O OD1 . ASP A 241 ? 0.5813 0.3546 0.4261 -0.0294 -0.0370 0.0425  238 ASP A OD1 
1870 O OD2 . ASP A 241 ? 0.5784 0.3627 0.4236 -0.0368 -0.0337 0.0501  238 ASP A OD2 
1871 N N   . PRO A 242 ? 0.6015 0.3364 0.4371 -0.0432 -0.0381 0.0462  239 PRO A N   
1872 C CA  . PRO A 242 ? 0.6233 0.3389 0.4517 -0.0382 -0.0405 0.0440  239 PRO A CA  
1873 C C   . PRO A 242 ? 0.6099 0.3306 0.4386 -0.0270 -0.0415 0.0391  239 PRO A C   
1874 O O   . PRO A 242 ? 0.6189 0.3305 0.4452 -0.0244 -0.0427 0.0337  239 PRO A O   
1875 C CB  . PRO A 242 ? 0.6608 0.3603 0.4808 -0.0380 -0.0406 0.0515  239 PRO A CB  
1876 C CG  . PRO A 242 ? 0.6479 0.3627 0.4699 -0.0384 -0.0383 0.0568  239 PRO A CG  
1877 C CD  . PRO A 242 ? 0.6138 0.3472 0.4458 -0.0457 -0.0361 0.0539  239 PRO A CD  
1878 N N   . VAL A 243 ? 0.5841 0.3203 0.4163 -0.0212 -0.0408 0.0404  240 VAL A N   
1879 C CA  . VAL A 243 ? 0.5744 0.3188 0.4093 -0.0112 -0.0412 0.0361  240 VAL A CA  
1880 C C   . VAL A 243 ? 0.5544 0.3087 0.3946 -0.0134 -0.0399 0.0293  240 VAL A C   
1881 O O   . VAL A 243 ? 0.5563 0.3069 0.3953 -0.0074 -0.0399 0.0241  240 VAL A O   
1882 C CB  . VAL A 243 ? 0.5634 0.3229 0.4016 -0.0064 -0.0413 0.0394  240 VAL A CB  
1883 C CG1 . VAL A 243 ? 0.5539 0.3291 0.3992 0.0006  -0.0409 0.0344  240 VAL A CG1 
1884 C CG2 . VAL A 243 ? 0.5903 0.3384 0.4214 -0.0010 -0.0435 0.0453  240 VAL A CG2 
1885 N N   . LEU A 244 ? 0.5354 0.3016 0.3808 -0.0212 -0.0388 0.0292  241 LEU A N   
1886 C CA  . LEU A 244 ? 0.5207 0.2948 0.3698 -0.0237 -0.0381 0.0233  241 LEU A CA  
1887 C C   . LEU A 244 ? 0.5480 0.3056 0.3914 -0.0260 -0.0397 0.0195  241 LEU A C   
1888 O O   . LEU A 244 ? 0.5555 0.3125 0.3970 -0.0224 -0.0395 0.0139  241 LEU A O   
1889 C CB  . LEU A 244 ? 0.5017 0.2896 0.3570 -0.0313 -0.0371 0.0245  241 LEU A CB  
1890 C CG  . LEU A 244 ? 0.4778 0.2816 0.3377 -0.0292 -0.0356 0.0272  241 LEU A CG  
1891 C CD1 . LEU A 244 ? 0.4544 0.2701 0.3198 -0.0360 -0.0344 0.0277  241 LEU A CD1 
1892 C CD2 . LEU A 244 ? 0.4703 0.2834 0.3326 -0.0219 -0.0350 0.0238  241 LEU A CD2 
1893 N N   . CYS A 245 ? 0.5646 0.3087 0.4046 -0.0320 -0.0412 0.0223  242 CYS A N   
1894 C CA  A CYS A 245 ? 0.5820 0.3086 0.4162 -0.0355 -0.0435 0.0186  242 CYS A CA  
1895 C CA  B CYS A 245 ? 0.5947 0.3209 0.4288 -0.0356 -0.0436 0.0188  242 CYS A CA  
1896 C C   . CYS A 245 ? 0.6051 0.3171 0.4314 -0.0262 -0.0440 0.0153  242 CYS A C   
1897 O O   . CYS A 245 ? 0.6070 0.3113 0.4287 -0.0254 -0.0449 0.0092  242 CYS A O   
1898 C CB  A CYS A 245 ? 0.6007 0.3168 0.4343 -0.0446 -0.0447 0.0232  242 CYS A CB  
1899 C CB  B CYS A 245 ? 0.6285 0.3430 0.4614 -0.0441 -0.0447 0.0236  242 CYS A CB  
1900 S SG  A CYS A 245 ? 0.5710 0.3056 0.4153 -0.0554 -0.0440 0.0247  242 CYS A SG  
1901 S SG  B CYS A 245 ? 0.7017 0.3893 0.5256 -0.0478 -0.0482 0.0199  242 CYS A SG  
1902 N N   . ALA A 246 ? 0.5997 0.3085 0.4243 -0.0187 -0.0434 0.0190  243 ALA A N   
1903 C CA  . ALA A 246 ? 0.6163 0.3113 0.4344 -0.0085 -0.0437 0.0159  243 ALA A CA  
1904 C C   . ALA A 246 ? 0.5961 0.3053 0.4177 -0.0013 -0.0413 0.0102  243 ALA A C   
1905 O O   . ALA A 246 ? 0.6079 0.3078 0.4241 0.0031  -0.0409 0.0043  243 ALA A O   
1906 C CB  . ALA A 246 ? 0.6295 0.3178 0.4452 -0.0022 -0.0444 0.0219  243 ALA A CB  
1907 N N   . LEU A 247 ? 0.5654 0.2965 0.3956 -0.0012 -0.0395 0.0115  244 LEU A N   
1908 C CA  . LEU A 247 ? 0.5569 0.3021 0.3911 0.0041  -0.0367 0.0065  244 LEU A CA  
1909 C C   . LEU A 247 ? 0.5528 0.2957 0.3832 -0.0011 -0.0363 0.0009  244 LEU A C   
1910 O O   . LEU A 247 ? 0.5494 0.2919 0.3768 0.0046  -0.0341 -0.0044 244 LEU A O   
1911 C CB  . LEU A 247 ? 0.5342 0.3018 0.3780 0.0035  -0.0353 0.0095  244 LEU A CB  
1912 C CG  . LEU A 247 ? 0.5421 0.3158 0.3899 0.0107  -0.0358 0.0134  244 LEU A CG  
1913 C CD1 . LEU A 247 ? 0.5182 0.3120 0.3742 0.0080  -0.0353 0.0160  244 LEU A CD1 
1914 C CD2 . LEU A 247 ? 0.5670 0.3418 0.4162 0.0218  -0.0343 0.0097  244 LEU A CD2 
1915 N N   . ALA A 248 ? 0.5525 0.2940 0.3828 -0.0111 -0.0385 0.0020  245 ALA A N   
1916 C CA  . ALA A 248 ? 0.5674 0.3060 0.3934 -0.0160 -0.0395 -0.0031 245 ALA A CA  
1917 C C   . ALA A 248 ? 0.6104 0.3283 0.4255 -0.0124 -0.0405 -0.0083 245 ALA A C   
1918 O O   . ALA A 248 ? 0.6117 0.3286 0.4212 -0.0092 -0.0391 -0.0142 245 ALA A O   
1919 C CB  . ALA A 248 ? 0.5664 0.3063 0.3953 -0.0268 -0.0424 -0.0009 245 ALA A CB  
1920 N N   . LYS A 249 ? 0.6580 0.3584 0.4688 -0.0127 -0.0428 -0.0063 246 LYS A N   
1921 C CA  . LYS A 249 ? 0.7189 0.3966 0.5182 -0.0093 -0.0441 -0.0116 246 LYS A CA  
1922 C C   . LYS A 249 ? 0.7147 0.3923 0.5110 0.0035  -0.0403 -0.0155 246 LYS A C   
1923 O O   . LYS A 249 ? 0.7205 0.3878 0.5077 0.0068  -0.0397 -0.0223 246 LYS A O   
1924 C CB  . LYS A 249 ? 0.7908 0.4491 0.5864 -0.0122 -0.0471 -0.0078 246 LYS A CB  
1925 C CG  . LYS A 249 ? 0.8536 0.5068 0.6498 -0.0254 -0.0509 -0.0065 246 LYS A CG  
1926 C CD  . LYS A 249 ? 0.9388 0.5720 0.7313 -0.0300 -0.0533 -0.0023 246 LYS A CD  
1927 C CE  . LYS A 249 ? 1.0023 0.6159 0.7859 -0.0198 -0.0529 -0.0031 246 LYS A CE  
1928 N NZ  . LYS A 249 ? 1.0792 0.6662 0.8545 -0.0255 -0.0563 -0.0026 246 LYS A NZ  
1929 N N   . LYS A 250 ? 0.6917 0.3809 0.4955 0.0104  -0.0380 -0.0115 247 LYS A N   
1930 C CA  . LYS A 250 ? 0.7036 0.3967 0.5079 0.0228  -0.0341 -0.0148 247 LYS A CA  
1931 C C   . LYS A 250 ? 0.6733 0.3780 0.4770 0.0236  -0.0302 -0.0205 247 LYS A C   
1932 O O   . LYS A 250 ? 0.6739 0.3703 0.4707 0.0312  -0.0275 -0.0263 247 LYS A O   
1933 C CB  . LYS A 250 ? 0.7087 0.4173 0.5238 0.0279  -0.0332 -0.0090 247 LYS A CB  
1934 C CG  . LYS A 250 ? 0.7399 0.4588 0.5599 0.0399  -0.0292 -0.0118 247 LYS A CG  
1935 C CD  . LYS A 250 ? 0.7395 0.4744 0.5705 0.0437  -0.0298 -0.0061 247 LYS A CD  
1936 C CE  . LYS A 250 ? 0.7733 0.5181 0.6109 0.0563  -0.0267 -0.0085 247 LYS A CE  
1937 N NZ  . LYS A 250 ? 0.7605 0.5265 0.6107 0.0578  -0.0275 -0.0038 247 LYS A NZ  
1938 N N   . HIS A 251 ? 0.6362 0.3592 0.4467 0.0170  -0.0296 -0.0186 248 HIS A N   
1939 C CA  . HIS A 251 ? 0.6220 0.3575 0.4322 0.0170  -0.0257 -0.0227 248 HIS A CA  
1940 C C   . HIS A 251 ? 0.6279 0.3521 0.4269 0.0102  -0.0281 -0.0271 248 HIS A C   
1941 O O   . HIS A 251 ? 0.6105 0.3413 0.4056 0.0105  -0.0250 -0.0308 248 HIS A O   
1942 C CB  . HIS A 251 ? 0.5989 0.3574 0.4211 0.0134  -0.0244 -0.0181 248 HIS A CB  
1943 C CG  . HIS A 251 ? 0.5949 0.3672 0.4273 0.0209  -0.0216 -0.0156 248 HIS A CG  
1944 N ND1 . HIS A 251 ? 0.6123 0.3950 0.4478 0.0279  -0.0162 -0.0189 248 HIS A ND1 
1945 C CD2 . HIS A 251 ? 0.5955 0.3733 0.4358 0.0224  -0.0236 -0.0103 248 HIS A CD2 
1946 C CE1 . HIS A 251 ? 0.6127 0.4077 0.4590 0.0334  -0.0155 -0.0159 248 HIS A CE1 
1947 N NE2 . HIS A 251 ? 0.6041 0.3957 0.4526 0.0303  -0.0203 -0.0107 248 HIS A NE2 
1948 N N   . LYS A 252 ? 0.6412 0.3488 0.4347 0.0042  -0.0334 -0.0269 249 LYS A N   
1949 C CA  . LYS A 252 ? 0.6619 0.3603 0.4469 -0.0039 -0.0375 -0.0304 249 LYS A CA  
1950 C C   . LYS A 252 ? 0.6319 0.3486 0.4229 -0.0102 -0.0376 -0.0284 249 LYS A C   
1951 O O   . LYS A 252 ? 0.6384 0.3548 0.4217 -0.0117 -0.0378 -0.0327 249 LYS A O   
1952 C CB  . LYS A 252 ? 0.6969 0.3806 0.4673 0.0012  -0.0362 -0.0384 249 LYS A CB  
1953 C CG  . LYS A 252 ? 0.7464 0.4103 0.5104 0.0083  -0.0360 -0.0407 249 LYS A CG  
1954 C CD  . LYS A 252 ? 0.7953 0.4398 0.5426 0.0116  -0.0361 -0.0491 249 LYS A CD  
1955 C CE  . LYS A 252 ? 0.8395 0.4639 0.5806 0.0198  -0.0356 -0.0515 249 LYS A CE  
1956 N NZ  . LYS A 252 ? 0.8893 0.4968 0.6137 0.0256  -0.0339 -0.0606 249 LYS A NZ  
1957 N N   . ARG A 253 ? 0.5968 0.3278 0.4001 -0.0133 -0.0376 -0.0222 250 ARG A N   
1958 C CA  . ARG A 253 ? 0.5695 0.3164 0.3797 -0.0197 -0.0384 -0.0195 250 ARG A CA  
1959 C C   . ARG A 253 ? 0.5590 0.3049 0.3755 -0.0278 -0.0428 -0.0151 250 ARG A C   
1960 O O   . ARG A 253 ? 0.6059 0.3365 0.4180 -0.0305 -0.0460 -0.0159 250 ARG A O   
1961 C CB  . ARG A 253 ? 0.5450 0.3104 0.3635 -0.0153 -0.0335 -0.0169 250 ARG A CB  
1962 C CG  . ARG A 253 ? 0.5532 0.3207 0.3669 -0.0076 -0.0282 -0.0211 250 ARG A CG  
1963 C CD  . ARG A 253 ? 0.5531 0.3212 0.3587 -0.0101 -0.0277 -0.0248 250 ARG A CD  
1964 N NE  . ARG A 253 ? 0.5583 0.3263 0.3572 -0.0030 -0.0219 -0.0290 250 ARG A NE  
1965 C CZ  . ARG A 253 ? 0.5729 0.3421 0.3634 -0.0036 -0.0197 -0.0319 250 ARG A CZ  
1966 N NH1 . ARG A 253 ? 0.5635 0.3342 0.3513 -0.0105 -0.0237 -0.0309 250 ARG A NH1 
1967 N NH2 . ARG A 253 ? 0.5935 0.3632 0.3786 0.0031  -0.0133 -0.0354 250 ARG A NH2 
1968 N N   . THR A 254 ? 0.5285 0.2899 0.3546 -0.0320 -0.0427 -0.0108 251 THR A N   
1969 C CA  . THR A 254 ? 0.5131 0.2767 0.3465 -0.0398 -0.0456 -0.0064 251 THR A CA  
1970 C C   . THR A 254 ? 0.4928 0.2691 0.3350 -0.0379 -0.0425 -0.0009 251 THR A C   
1971 O O   . THR A 254 ? 0.4810 0.2675 0.3251 -0.0326 -0.0392 -0.0011 251 THR A O   
1972 C CB  . THR A 254 ? 0.5004 0.2718 0.3368 -0.0465 -0.0487 -0.0072 251 THR A CB  
1973 O OG1 . THR A 254 ? 0.4661 0.2527 0.3061 -0.0435 -0.0456 -0.0063 251 THR A OG1 
1974 C CG2 . THR A 254 ? 0.5190 0.2793 0.3457 -0.0484 -0.0527 -0.0129 251 THR A CG2 
1975 N N   . PRO A 255 ? 0.4857 0.2618 0.3330 -0.0427 -0.0434 0.0038  252 PRO A N   
1976 C CA  . PRO A 255 ? 0.4663 0.2536 0.3201 -0.0410 -0.0407 0.0089  252 PRO A CA  
1977 C C   . PRO A 255 ? 0.4337 0.2389 0.2934 -0.0410 -0.0390 0.0089  252 PRO A C   
1978 O O   . PRO A 255 ? 0.4172 0.2312 0.2797 -0.0366 -0.0365 0.0105  252 PRO A O   
1979 C CB  . PRO A 255 ? 0.4791 0.2624 0.3358 -0.0478 -0.0419 0.0135  252 PRO A CB  
1980 C CG  . PRO A 255 ? 0.5099 0.2750 0.3605 -0.0511 -0.0450 0.0111  252 PRO A CG  
1981 C CD  . PRO A 255 ? 0.5104 0.2740 0.3564 -0.0496 -0.0468 0.0046  252 PRO A CD  
1982 N N   . ALA A 256 ? 0.4299 0.2394 0.2913 -0.0458 -0.0408 0.0070  253 ALA A N   
1983 C CA  . ALA A 256 ? 0.4066 0.2306 0.2726 -0.0459 -0.0396 0.0069  253 ALA A CA  
1984 C C   . ALA A 256 ? 0.4081 0.2349 0.2705 -0.0395 -0.0369 0.0043  253 ALA A C   
1985 O O   . ALA A 256 ? 0.3777 0.2158 0.2446 -0.0374 -0.0343 0.0059  253 ALA A O   
1986 C CB  . ALA A 256 ? 0.4131 0.2382 0.2800 -0.0512 -0.0430 0.0051  253 ALA A CB  
1987 N N   . LEU A 257 ? 0.4161 0.2330 0.2707 -0.0365 -0.0371 0.0004  254 LEU A N   
1988 C CA  . LEU A 257 ? 0.4137 0.2342 0.2653 -0.0307 -0.0335 -0.0022 254 LEU A CA  
1989 C C   . LEU A 257 ? 0.4112 0.2362 0.2671 -0.0251 -0.0307 -0.0003 254 LEU A C   
1990 O O   . LEU A 257 ? 0.3902 0.2260 0.2496 -0.0224 -0.0277 -0.0003 254 LEU A O   
1991 C CB  . LEU A 257 ? 0.4350 0.2434 0.2763 -0.0284 -0.0339 -0.0072 254 LEU A CB  
1992 C CG  . LEU A 257 ? 0.4367 0.2442 0.2728 -0.0325 -0.0363 -0.0096 254 LEU A CG  
1993 C CD1 . LEU A 257 ? 0.4626 0.2549 0.2866 -0.0310 -0.0378 -0.0147 254 LEU A CD1 
1994 C CD2 . LEU A 257 ? 0.4220 0.2409 0.2592 -0.0313 -0.0330 -0.0093 254 LEU A CD2 
1995 N N   . ILE A 258 ? 0.4223 0.2400 0.2784 -0.0240 -0.0320 0.0019  255 ILE A N   
1996 C CA  . ILE A 258 ? 0.4246 0.2470 0.2847 -0.0182 -0.0303 0.0042  255 ILE A CA  
1997 C C   . ILE A 258 ? 0.3959 0.2331 0.2635 -0.0207 -0.0297 0.0075  255 ILE A C   
1998 O O   . ILE A 258 ? 0.3812 0.2287 0.2533 -0.0167 -0.0279 0.0077  255 ILE A O   
1999 C CB  . ILE A 258 ? 0.4588 0.2683 0.3159 -0.0166 -0.0323 0.0067  255 ILE A CB  
2000 C CG1 . ILE A 258 ? 0.4866 0.2789 0.3353 -0.0147 -0.0333 0.0029  255 ILE A CG1 
2001 C CG2 . ILE A 258 ? 0.4645 0.2800 0.3256 -0.0102 -0.0315 0.0093  255 ILE A CG2 
2002 C CD1 . ILE A 258 ? 0.5026 0.2951 0.3487 -0.0070 -0.0303 -0.0017 255 ILE A CD1 
2003 N N   . ALA A 259 ? 0.3846 0.2230 0.2538 -0.0269 -0.0313 0.0100  256 ALA A N   
2004 C CA  . ALA A 259 ? 0.3661 0.2164 0.2410 -0.0290 -0.0307 0.0131  256 ALA A CA  
2005 C C   . ALA A 259 ? 0.3525 0.2138 0.2303 -0.0287 -0.0289 0.0109  256 ALA A C   
2006 O O   . ALA A 259 ? 0.3357 0.2073 0.2180 -0.0277 -0.0279 0.0122  256 ALA A O   
2007 C CB  . ALA A 259 ? 0.3653 0.2144 0.2416 -0.0354 -0.0320 0.0157  256 ALA A CB  
2008 N N   . LEU A 260 ? 0.3556 0.2145 0.2304 -0.0300 -0.0287 0.0078  257 LEU A N   
2009 C CA  . LEU A 260 ? 0.3484 0.2156 0.2243 -0.0303 -0.0267 0.0061  257 LEU A CA  
2010 C C   . LEU A 260 ? 0.3522 0.2237 0.2293 -0.0251 -0.0237 0.0045  257 LEU A C   
2011 O O   . LEU A 260 ? 0.3572 0.2391 0.2390 -0.0251 -0.0218 0.0048  257 LEU A O   
2012 C CB  . LEU A 260 ? 0.3544 0.2163 0.2247 -0.0327 -0.0276 0.0036  257 LEU A CB  
2013 C CG  . LEU A 260 ? 0.3527 0.2129 0.2238 -0.0379 -0.0310 0.0047  257 LEU A CG  
2014 C CD1 . LEU A 260 ? 0.3709 0.2258 0.2355 -0.0395 -0.0328 0.0019  257 LEU A CD1 
2015 C CD2 . LEU A 260 ? 0.3328 0.2029 0.2103 -0.0402 -0.0307 0.0072  257 LEU A CD2 
2016 N N   . ARG A 261 ? 0.3604 0.2242 0.2337 -0.0208 -0.0231 0.0026  258 ARG A N   
2017 C CA  . ARG A 261 ? 0.3594 0.2287 0.2350 -0.0152 -0.0196 0.0007  258 ARG A CA  
2018 C C   . ARG A 261 ? 0.3507 0.2297 0.2346 -0.0125 -0.0200 0.0031  258 ARG A C   
2019 O O   . ARG A 261 ? 0.3454 0.2352 0.2351 -0.0102 -0.0174 0.0022  258 ARG A O   
2020 C CB  . ARG A 261 ? 0.3778 0.2358 0.2472 -0.0103 -0.0189 -0.0022 258 ARG A CB  
2021 C CG  . ARG A 261 ? 0.3832 0.2475 0.2556 -0.0039 -0.0144 -0.0046 258 ARG A CG  
2022 C CD  . ARG A 261 ? 0.3901 0.2595 0.2602 -0.0054 -0.0101 -0.0071 258 ARG A CD  
2023 N NE  . ARG A 261 ? 0.3910 0.2715 0.2680 -0.0005 -0.0052 -0.0084 258 ARG A NE  
2024 C CZ  . ARG A 261 ? 0.3961 0.2835 0.2730 -0.0014 -0.0001 -0.0100 258 ARG A CZ  
2025 N NH1 . ARG A 261 ? 0.4052 0.2878 0.2738 -0.0065 0.0003  -0.0103 258 ARG A NH1 
2026 N NH2 . ARG A 261 ? 0.4017 0.3008 0.2868 0.0027  0.0047  -0.0110 258 ARG A NH2 
2027 N N   . TYR A 262 ? 0.3520 0.2272 0.2361 -0.0129 -0.0232 0.0062  259 TYR A N   
2028 C CA  . TYR A 262 ? 0.3518 0.2350 0.2416 -0.0106 -0.0247 0.0090  259 TYR A CA  
2029 C C   . TYR A 262 ? 0.3361 0.2327 0.2316 -0.0139 -0.0238 0.0090  259 TYR A C   
2030 O O   . TYR A 262 ? 0.3342 0.2411 0.2361 -0.0111 -0.0234 0.0087  259 TYR A O   
2031 C CB  . TYR A 262 ? 0.3614 0.2367 0.2477 -0.0126 -0.0278 0.0127  259 TYR A CB  
2032 C CG  . TYR A 262 ? 0.3621 0.2443 0.2515 -0.0114 -0.0297 0.0159  259 TYR A CG  
2033 C CD1 . TYR A 262 ? 0.3775 0.2625 0.2695 -0.0048 -0.0311 0.0166  259 TYR A CD1 
2034 C CD2 . TYR A 262 ? 0.3573 0.2434 0.2465 -0.0163 -0.0304 0.0181  259 TYR A CD2 
2035 C CE1 . TYR A 262 ? 0.3766 0.2676 0.2702 -0.0035 -0.0339 0.0195  259 TYR A CE1 
2036 C CE2 . TYR A 262 ? 0.3550 0.2465 0.2450 -0.0151 -0.0324 0.0207  259 TYR A CE2 
2037 C CZ  . TYR A 262 ? 0.3764 0.2701 0.2682 -0.0089 -0.0345 0.0215  259 TYR A CZ  
2038 O OH  . TYR A 262 ? 0.3837 0.2825 0.2751 -0.0075 -0.0374 0.0240  259 TYR A OH  
2039 N N   . GLN A 263 ? 0.3272 0.2233 0.2207 -0.0197 -0.0237 0.0093  260 GLN A N   
2040 C CA  . GLN A 263 ? 0.3104 0.2164 0.2078 -0.0233 -0.0230 0.0092  260 GLN A CA  
2041 C C   . GLN A 263 ? 0.3164 0.2288 0.2169 -0.0224 -0.0197 0.0066  260 GLN A C   
2042 O O   . GLN A 263 ? 0.3054 0.2282 0.2123 -0.0224 -0.0193 0.0064  260 GLN A O   
2043 C CB  . GLN A 263 ? 0.2997 0.2026 0.1941 -0.0284 -0.0236 0.0098  260 GLN A CB  
2044 C CG  . GLN A 263 ? 0.2966 0.1949 0.1892 -0.0298 -0.0258 0.0126  260 GLN A CG  
2045 C CD  . GLN A 263 ? 0.2971 0.2006 0.1916 -0.0290 -0.0271 0.0148  260 GLN A CD  
2046 O OE1 . GLN A 263 ? 0.2983 0.2094 0.1962 -0.0272 -0.0272 0.0141  260 GLN A OE1 
2047 N NE2 . GLN A 263 ? 0.3023 0.2014 0.1940 -0.0303 -0.0281 0.0176  260 GLN A NE2 
2048 N N   . LEU A 264 ? 0.3317 0.2384 0.2278 -0.0216 -0.0173 0.0045  261 LEU A N   
2049 C CA  . LEU A 264 ? 0.3488 0.2621 0.2473 -0.0212 -0.0130 0.0024  261 LEU A CA  
2050 C C   . LEU A 264 ? 0.3596 0.2830 0.2667 -0.0166 -0.0118 0.0018  261 LEU A C   
2051 O O   . LEU A 264 ? 0.3696 0.3036 0.2832 -0.0183 -0.0095 0.0013  261 LEU A O   
2052 C CB  . LEU A 264 ? 0.3732 0.2774 0.2633 -0.0203 -0.0106 0.0002  261 LEU A CB  
2053 C CG  . LEU A 264 ? 0.3778 0.2745 0.2605 -0.0251 -0.0122 0.0006  261 LEU A CG  
2054 C CD1 . LEU A 264 ? 0.3996 0.2892 0.2735 -0.0243 -0.0095 -0.0019 261 LEU A CD1 
2055 C CD2 . LEU A 264 ? 0.3744 0.2774 0.2601 -0.0297 -0.0122 0.0021  261 LEU A CD2 
2056 N N   . GLN A 265 ? 0.3771 0.2974 0.2849 -0.0111 -0.0136 0.0021  262 GLN A N   
2057 C CA  . GLN A 265 ? 0.3849 0.3149 0.3013 -0.0052 -0.0123 0.0011  262 GLN A CA  
2058 C C   . GLN A 265 ? 0.3822 0.3232 0.3067 -0.0063 -0.0159 0.0030  262 GLN A C   
2059 O O   . GLN A 265 ? 0.4102 0.3630 0.3443 -0.0028 -0.0156 0.0023  262 GLN A O   
2060 C CB  . GLN A 265 ? 0.3979 0.3184 0.3106 0.0019  -0.0129 0.0004  262 GLN A CB  
2061 C CG  . GLN A 265 ? 0.4106 0.3213 0.3152 0.0033  -0.0089 -0.0027 262 GLN A CG  
2062 C CD  . GLN A 265 ? 0.4298 0.3318 0.3317 0.0112  -0.0088 -0.0043 262 GLN A CD  
2063 O OE1 . GLN A 265 ? 0.4432 0.3322 0.3354 0.0119  -0.0076 -0.0065 262 GLN A OE1 
2064 N NE2 . GLN A 265 ? 0.4302 0.3388 0.3401 0.0175  -0.0103 -0.0034 262 GLN A NE2 
2065 N N   . ARG A 266 ? 0.3730 0.3108 0.2939 -0.0107 -0.0193 0.0052  263 ARG A N   
2066 C CA  . ARG A 266 ? 0.3687 0.3162 0.2956 -0.0117 -0.0230 0.0066  263 ARG A CA  
2067 C C   . ARG A 266 ? 0.3653 0.3194 0.2947 -0.0183 -0.0216 0.0056  263 ARG A C   
2068 O O   . ARG A 266 ? 0.3629 0.3233 0.2955 -0.0202 -0.0249 0.0062  263 ARG A O   
2069 C CB  . ARG A 266 ? 0.3659 0.3062 0.2868 -0.0112 -0.0276 0.0096  263 ARG A CB  
2070 C CG  . ARG A 266 ? 0.3610 0.2913 0.2736 -0.0162 -0.0273 0.0108  263 ARG A CG  
2071 C CD  . ARG A 266 ? 0.3574 0.2777 0.2636 -0.0146 -0.0299 0.0139  263 ARG A CD  
2072 N NE  . ARG A 266 ? 0.3605 0.2851 0.2670 -0.0134 -0.0335 0.0162  263 ARG A NE  
2073 C CZ  . ARG A 266 ? 0.3466 0.2706 0.2490 -0.0171 -0.0347 0.0178  263 ARG A CZ  
2074 N NH1 . ARG A 266 ? 0.3423 0.2626 0.2417 -0.0221 -0.0326 0.0176  263 ARG A NH1 
2075 N NH2 . ARG A 266 ? 0.3561 0.2835 0.2573 -0.0154 -0.0382 0.0196  263 ARG A NH2 
2076 N N   . GLY A 267 ? 0.3561 0.3087 0.2839 -0.0214 -0.0171 0.0041  264 GLY A N   
2077 C CA  . GLY A 267 ? 0.3453 0.3027 0.2751 -0.0276 -0.0155 0.0034  264 GLY A CA  
2078 C C   . GLY A 267 ? 0.3386 0.2884 0.2614 -0.0320 -0.0176 0.0046  264 GLY A C   
2079 O O   . GLY A 267 ? 0.3335 0.2863 0.2577 -0.0365 -0.0179 0.0042  264 GLY A O   
2080 N N   . VAL A 268 ? 0.3276 0.2676 0.2434 -0.0307 -0.0191 0.0059  265 VAL A N   
2081 C CA  . VAL A 268 ? 0.3141 0.2475 0.2242 -0.0342 -0.0205 0.0069  265 VAL A CA  
2082 C C   . VAL A 268 ? 0.3130 0.2394 0.2178 -0.0361 -0.0181 0.0064  265 VAL A C   
2083 O O   . VAL A 268 ? 0.3473 0.2693 0.2493 -0.0337 -0.0167 0.0057  265 VAL A O   
2084 C CB  . VAL A 268 ? 0.3086 0.2371 0.2154 -0.0323 -0.0233 0.0089  265 VAL A CB  
2085 C CG1 . VAL A 268 ? 0.3130 0.2349 0.2149 -0.0352 -0.0237 0.0099  265 VAL A CG1 
2086 C CG2 . VAL A 268 ? 0.3175 0.2526 0.2274 -0.0312 -0.0262 0.0097  265 VAL A CG2 
2087 N N   . VAL A 269 ? 0.2965 0.2210 0.1990 -0.0398 -0.0180 0.0065  266 VAL A N   
2088 C CA  . VAL A 269 ? 0.2912 0.2080 0.1875 -0.0413 -0.0172 0.0065  266 VAL A CA  
2089 C C   . VAL A 269 ? 0.2841 0.1954 0.1777 -0.0408 -0.0199 0.0076  266 VAL A C   
2090 O O   . VAL A 269 ? 0.2666 0.1798 0.1621 -0.0413 -0.0216 0.0086  266 VAL A O   
2091 C CB  . VAL A 269 ? 0.3002 0.2165 0.1951 -0.0449 -0.0161 0.0064  266 VAL A CB  
2092 C CG1 . VAL A 269 ? 0.3028 0.2110 0.1911 -0.0458 -0.0166 0.0069  266 VAL A CG1 
2093 C CG2 . VAL A 269 ? 0.3057 0.2270 0.2035 -0.0462 -0.0126 0.0055  266 VAL A CG2 
2094 N N   . VAL A 270 ? 0.2776 0.1824 0.1669 -0.0399 -0.0203 0.0073  267 VAL A N   
2095 C CA  . VAL A 270 ? 0.2817 0.1822 0.1702 -0.0400 -0.0230 0.0083  267 VAL A CA  
2096 C C   . VAL A 270 ? 0.2807 0.1764 0.1657 -0.0419 -0.0247 0.0082  267 VAL A C   
2097 O O   . VAL A 270 ? 0.2935 0.1850 0.1732 -0.0419 -0.0243 0.0070  267 VAL A O   
2098 C CB  . VAL A 270 ? 0.2964 0.1926 0.1834 -0.0374 -0.0233 0.0080  267 VAL A CB  
2099 C CG1 . VAL A 270 ? 0.3145 0.2047 0.1959 -0.0362 -0.0223 0.0059  267 VAL A CG1 
2100 C CG2 . VAL A 270 ? 0.3050 0.1976 0.1925 -0.0383 -0.0256 0.0097  267 VAL A CG2 
2101 N N   . LEU A 271 ? 0.2704 0.1671 0.1582 -0.0433 -0.0266 0.0095  268 LEU A N   
2102 C CA  . LEU A 271 ? 0.2781 0.1721 0.1652 -0.0447 -0.0292 0.0096  268 LEU A CA  
2103 C C   . LEU A 271 ? 0.2910 0.1808 0.1780 -0.0455 -0.0313 0.0096  268 LEU A C   
2104 O O   . LEU A 271 ? 0.3012 0.1907 0.1897 -0.0450 -0.0305 0.0104  268 LEU A O   
2105 C CB  . LEU A 271 ? 0.2731 0.1721 0.1651 -0.0455 -0.0293 0.0107  268 LEU A CB  
2106 C CG  . LEU A 271 ? 0.2741 0.1756 0.1657 -0.0451 -0.0276 0.0104  268 LEU A CG  
2107 C CD1 . LEU A 271 ? 0.2751 0.1797 0.1704 -0.0451 -0.0280 0.0110  268 LEU A CD1 
2108 C CD2 . LEU A 271 ? 0.2814 0.1786 0.1677 -0.0451 -0.0275 0.0096  268 LEU A CD2 
2109 N N   . ALA A 272 ? 0.3069 0.1929 0.1917 -0.0467 -0.0343 0.0088  269 ALA A N   
2110 C CA  . ALA A 272 ? 0.3165 0.1981 0.2018 -0.0486 -0.0373 0.0085  269 ALA A CA  
2111 C C   . ALA A 272 ? 0.3210 0.2040 0.2087 -0.0507 -0.0413 0.0083  269 ALA A C   
2112 O O   . ALA A 272 ? 0.3265 0.2067 0.2088 -0.0498 -0.0432 0.0071  269 ALA A O   
2113 C CB  . ALA A 272 ? 0.3269 0.1999 0.2044 -0.0474 -0.0375 0.0062  269 ALA A CB  
2114 N N   . LYS A 273 ? 0.3166 0.2048 0.2126 -0.0530 -0.0422 0.0098  270 LYS A N   
2115 C CA  . LYS A 273 ? 0.3302 0.2223 0.2317 -0.0547 -0.0463 0.0098  270 LYS A CA  
2116 C C   . LYS A 273 ? 0.3470 0.2332 0.2471 -0.0579 -0.0503 0.0084  270 LYS A C   
2117 O O   . LYS A 273 ? 0.3402 0.2233 0.2415 -0.0600 -0.0490 0.0091  270 LYS A O   
2118 C CB  . LYS A 273 ? 0.3325 0.2345 0.2448 -0.0557 -0.0448 0.0118  270 LYS A CB  
2119 C CG  . LYS A 273 ? 0.3386 0.2468 0.2598 -0.0578 -0.0489 0.0118  270 LYS A CG  
2120 C CD  . LYS A 273 ? 0.3459 0.2543 0.2729 -0.0629 -0.0507 0.0122  270 LYS A CD  
2121 C CE  . LYS A 273 ? 0.3497 0.2666 0.2879 -0.0653 -0.0551 0.0121  270 LYS A CE  
2122 N NZ  . LYS A 273 ? 0.3653 0.2824 0.3099 -0.0714 -0.0564 0.0126  270 LYS A NZ  
2123 N N   . SER A 274 ? 0.3592 0.2428 0.2562 -0.0583 -0.0555 0.0066  271 SER A N   
2124 C CA  . SER A 274 ? 0.3737 0.2535 0.2718 -0.0624 -0.0609 0.0050  271 SER A CA  
2125 C C   . SER A 274 ? 0.3840 0.2678 0.2844 -0.0626 -0.0672 0.0041  271 SER A C   
2126 O O   . SER A 274 ? 0.3917 0.2733 0.2844 -0.0590 -0.0678 0.0037  271 SER A O   
2127 C CB  . SER A 274 ? 0.3902 0.2572 0.2765 -0.0623 -0.0617 0.0023  271 SER A CB  
2128 O OG  . SER A 274 ? 0.4146 0.2771 0.3018 -0.0668 -0.0676 0.0004  271 SER A OG  
2129 N N   . TYR A 275 ? 0.3903 0.2801 0.3013 -0.0667 -0.0715 0.0041  272 TYR A N   
2130 C CA  . TYR A 275 ? 0.4097 0.3042 0.3246 -0.0671 -0.0791 0.0031  272 TYR A CA  
2131 C C   . TYR A 275 ? 0.4356 0.3210 0.3442 -0.0711 -0.0858 -0.0002 272 TYR A C   
2132 O O   . TYR A 275 ? 0.4490 0.3389 0.3629 -0.0732 -0.0931 -0.0013 272 TYR A O   
2133 C CB  . TYR A 275 ? 0.4041 0.3140 0.3370 -0.0685 -0.0793 0.0051  272 TYR A CB  
2134 C CG  . TYR A 275 ? 0.3921 0.3090 0.3276 -0.0629 -0.0760 0.0070  272 TYR A CG  
2135 C CD1 . TYR A 275 ? 0.3765 0.2887 0.3037 -0.0593 -0.0695 0.0079  272 TYR A CD1 
2136 C CD2 . TYR A 275 ? 0.3938 0.3214 0.3398 -0.0610 -0.0799 0.0075  272 TYR A CD2 
2137 C CE1 . TYR A 275 ? 0.3643 0.2805 0.2923 -0.0546 -0.0671 0.0091  272 TYR A CE1 
2138 C CE2 . TYR A 275 ? 0.3891 0.3210 0.3362 -0.0554 -0.0771 0.0088  272 TYR A CE2 
2139 C CZ  . TYR A 275 ? 0.3661 0.2915 0.3037 -0.0525 -0.0707 0.0096  272 TYR A CZ  
2140 O OH  . TYR A 275 ? 0.3706 0.2990 0.3093 -0.0475 -0.0680 0.0106  272 TYR A OH  
2141 N N   . ASN A 276 ? 0.4435 0.3165 0.3413 -0.0719 -0.0835 -0.0018 273 ASN A N   
2142 C CA  . ASN A 276 ? 0.4707 0.3330 0.3618 -0.0759 -0.0894 -0.0055 273 ASN A CA  
2143 C C   . ASN A 276 ? 0.4855 0.3348 0.3572 -0.0719 -0.0901 -0.0085 273 ASN A C   
2144 O O   . ASN A 276 ? 0.4718 0.3165 0.3360 -0.0679 -0.0831 -0.0079 273 ASN A O   
2145 C CB  . ASN A 276 ? 0.4738 0.3302 0.3674 -0.0801 -0.0862 -0.0053 273 ASN A CB  
2146 C CG  . ASN A 276 ? 0.5085 0.3511 0.3932 -0.0839 -0.0921 -0.0096 273 ASN A CG  
2147 O OD1 . ASN A 276 ? 0.5117 0.3410 0.3812 -0.0808 -0.0906 -0.0123 273 ASN A OD1 
2148 N ND2 . ASN A 276 ? 0.5153 0.3612 0.4098 -0.0908 -0.0983 -0.0104 273 ASN A ND2 
2149 N N   . GLU A 277 ? 0.5187 0.3627 0.3825 -0.0729 -0.0981 -0.0116 274 GLU A N   
2150 C CA  . GLU A 277 ? 0.5462 0.3786 0.3901 -0.0685 -0.0982 -0.0141 274 GLU A CA  
2151 C C   . GLU A 277 ? 0.5344 0.3543 0.3676 -0.0673 -0.0925 -0.0164 274 GLU A C   
2152 O O   . GLU A 277 ? 0.5188 0.3349 0.3416 -0.0623 -0.0866 -0.0162 274 GLU A O   
2153 C CB  . GLU A 277 ? 0.5906 0.4171 0.4245 -0.0696 -0.1081 -0.0175 274 GLU A CB  
2154 C CG  . GLU A 277 ? 0.6307 0.4428 0.4419 -0.0654 -0.1061 -0.0203 274 GLU A CG  
2155 C CD  . GLU A 277 ? 0.6764 0.4824 0.4731 -0.0644 -0.1146 -0.0226 274 GLU A CD  
2156 O OE1 . GLU A 277 ? 0.6789 0.4910 0.4838 -0.0676 -0.1237 -0.0229 274 GLU A OE1 
2157 O OE2 . GLU A 277 ? 0.7027 0.4980 0.4798 -0.0604 -0.1118 -0.0240 274 GLU A OE2 
2158 N N   . GLN A 278 ? 0.5418 0.3555 0.3776 -0.0716 -0.0940 -0.0183 275 GLN A N   
2159 C CA  . GLN A 278 ? 0.5620 0.3621 0.3868 -0.0695 -0.0893 -0.0209 275 GLN A CA  
2160 C C   . GLN A 278 ? 0.5176 0.3228 0.3472 -0.0654 -0.0798 -0.0174 275 GLN A C   
2161 O O   . GLN A 278 ? 0.5125 0.3107 0.3313 -0.0605 -0.0746 -0.0189 275 GLN A O   
2162 C CB  . GLN A 278 ? 0.6224 0.4131 0.4489 -0.0751 -0.0933 -0.0235 275 GLN A CB  
2163 C CG  . GLN A 278 ? 0.6714 0.4490 0.4890 -0.0719 -0.0876 -0.0253 275 GLN A CG  
2164 C CD  . GLN A 278 ? 0.7515 0.5192 0.5723 -0.0772 -0.0899 -0.0265 275 GLN A CD  
2165 O OE1 . GLN A 278 ? 0.8284 0.5798 0.6367 -0.0759 -0.0903 -0.0308 275 GLN A OE1 
2166 N NE2 . GLN A 278 ? 0.7708 0.5478 0.6081 -0.0830 -0.0907 -0.0225 275 GLN A NE2 
2167 N N   . ARG A 279 ? 0.4829 0.3000 0.3280 -0.0673 -0.0775 -0.0131 276 ARG A N   
2168 C CA  . ARG A 279 ? 0.4654 0.2873 0.3154 -0.0640 -0.0693 -0.0098 276 ARG A CA  
2169 C C   . ARG A 279 ? 0.4392 0.2674 0.2860 -0.0590 -0.0652 -0.0085 276 ARG A C   
2170 O O   . ARG A 279 ? 0.4103 0.2371 0.2535 -0.0551 -0.0593 -0.0082 276 ARG A O   
2171 C CB  . ARG A 279 ? 0.4622 0.2930 0.3275 -0.0680 -0.0684 -0.0059 276 ARG A CB  
2172 C CG  . ARG A 279 ? 0.4818 0.3030 0.3480 -0.0726 -0.0705 -0.0068 276 ARG A CG  
2173 C CD  . ARG A 279 ? 0.4806 0.3097 0.3601 -0.0762 -0.0677 -0.0023 276 ARG A CD  
2174 N NE  . ARG A 279 ? 0.4898 0.3311 0.3820 -0.0811 -0.0712 -0.0008 276 ARG A NE  
2175 C CZ  . ARG A 279 ? 0.5183 0.3586 0.4161 -0.0879 -0.0770 -0.0021 276 ARG A CZ  
2176 N NH1 . ARG A 279 ? 0.5347 0.3602 0.4248 -0.0910 -0.0806 -0.0052 276 ARG A NH1 
2177 N NH2 . ARG A 279 ? 0.5109 0.3654 0.4226 -0.0915 -0.0793 -0.0004 276 ARG A NH2 
2178 N N   . ILE A 280 ? 0.4482 0.2817 0.2951 -0.0592 -0.0689 -0.0081 277 ILE A N   
2179 C CA  . ILE A 280 ? 0.4420 0.2792 0.2841 -0.0551 -0.0653 -0.0067 277 ILE A CA  
2180 C C   . ILE A 280 ? 0.4571 0.2840 0.2839 -0.0517 -0.0620 -0.0095 277 ILE A C   
2181 O O   . ILE A 280 ? 0.4459 0.2752 0.2714 -0.0484 -0.0554 -0.0084 277 ILE A O   
2182 C CB  . ILE A 280 ? 0.4432 0.2849 0.2861 -0.0556 -0.0709 -0.0059 277 ILE A CB  
2183 C CG1 . ILE A 280 ? 0.4261 0.2804 0.2858 -0.0577 -0.0720 -0.0030 277 ILE A CG1 
2184 C CG2 . ILE A 280 ? 0.4571 0.2969 0.2896 -0.0517 -0.0681 -0.0052 277 ILE A CG2 
2185 C CD1 . ILE A 280 ? 0.4340 0.2933 0.2969 -0.0580 -0.0790 -0.0026 277 ILE A CD1 
2186 N N   . ARG A 281 ? 0.4783 0.2944 0.2938 -0.0524 -0.0665 -0.0134 278 ARG A N   
2187 C CA  . ARG A 281 ? 0.5141 0.3198 0.3135 -0.0487 -0.0628 -0.0166 278 ARG A CA  
2188 C C   . ARG A 281 ? 0.5053 0.3077 0.3063 -0.0464 -0.0570 -0.0176 278 ARG A C   
2189 O O   . ARG A 281 ? 0.5232 0.3236 0.3171 -0.0421 -0.0507 -0.0186 278 ARG A O   
2190 C CB  . ARG A 281 ? 0.5623 0.3560 0.3477 -0.0499 -0.0695 -0.0210 278 ARG A CB  
2191 C CG  . ARG A 281 ? 0.5886 0.3850 0.3703 -0.0510 -0.0755 -0.0199 278 ARG A CG  
2192 C CD  . ARG A 281 ? 0.6561 0.4400 0.4225 -0.0521 -0.0825 -0.0246 278 ARG A CD  
2193 N NE  . ARG A 281 ? 0.6973 0.4830 0.4588 -0.0525 -0.0894 -0.0235 278 ARG A NE  
2194 C CZ  . ARG A 281 ? 0.7378 0.5210 0.4865 -0.0491 -0.0872 -0.0221 278 ARG A CZ  
2195 N NH1 . ARG A 281 ? 0.7492 0.5299 0.4904 -0.0456 -0.0775 -0.0216 278 ARG A NH1 
2196 N NH2 . ARG A 281 ? 0.7542 0.5382 0.4986 -0.0494 -0.0947 -0.0208 278 ARG A NH2 
2197 N N   . GLN A 282 ? 0.4828 0.2845 0.2928 -0.0490 -0.0588 -0.0172 279 GLN A N   
2198 C CA  . GLN A 282 ? 0.4905 0.2885 0.3023 -0.0462 -0.0539 -0.0175 279 GLN A CA  
2199 C C   . GLN A 282 ? 0.4663 0.2755 0.2856 -0.0428 -0.0470 -0.0141 279 GLN A C   
2200 O O   . GLN A 282 ? 0.4634 0.2703 0.2794 -0.0381 -0.0417 -0.0153 279 GLN A O   
2201 C CB  . GLN A 282 ? 0.4978 0.2927 0.3176 -0.0504 -0.0573 -0.0167 279 GLN A CB  
2202 C CG  . GLN A 282 ? 0.5085 0.2970 0.3284 -0.0471 -0.0531 -0.0168 279 GLN A CG  
2203 C CD  . GLN A 282 ? 0.5166 0.3047 0.3462 -0.0518 -0.0555 -0.0140 279 GLN A CD  
2204 O OE1 . GLN A 282 ? 0.5039 0.2986 0.3418 -0.0508 -0.0520 -0.0100 279 GLN A OE1 
2205 N NE2 . GLN A 282 ? 0.5364 0.3172 0.3651 -0.0576 -0.0616 -0.0157 279 GLN A NE2 
2206 N N   . ASN A 283 ? 0.4366 0.2574 0.2653 -0.0447 -0.0470 -0.0104 280 ASN A N   
2207 C CA  . ASN A 283 ? 0.4189 0.2496 0.2562 -0.0425 -0.0416 -0.0073 280 ASN A CA  
2208 C C   . ASN A 283 ? 0.4227 0.2552 0.2542 -0.0385 -0.0361 -0.0081 280 ASN A C   
2209 O O   . ASN A 283 ? 0.4200 0.2586 0.2572 -0.0359 -0.0315 -0.0069 280 ASN A O   
2210 C CB  . ASN A 283 ? 0.3997 0.2412 0.2481 -0.0454 -0.0428 -0.0035 280 ASN A CB  
2211 C CG  . ASN A 283 ? 0.3947 0.2362 0.2509 -0.0490 -0.0458 -0.0020 280 ASN A CG  
2212 O OD1 . ASN A 283 ? 0.4000 0.2337 0.2543 -0.0491 -0.0462 -0.0030 280 ASN A OD1 
2213 N ND2 . ASN A 283 ? 0.3814 0.2310 0.2460 -0.0520 -0.0479 0.0003  280 ASN A ND2 
2214 N N   . VAL A 284 ? 0.4394 0.2675 0.2602 -0.0381 -0.0364 -0.0101 281 VAL A N   
2215 C CA  . VAL A 284 ? 0.4461 0.2761 0.2611 -0.0349 -0.0301 -0.0105 281 VAL A CA  
2216 C C   . VAL A 284 ? 0.4562 0.2810 0.2670 -0.0305 -0.0258 -0.0137 281 VAL A C   
2217 O O   . VAL A 284 ? 0.4480 0.2768 0.2571 -0.0275 -0.0194 -0.0141 281 VAL A O   
2218 C CB  . VAL A 284 ? 0.4755 0.3013 0.2786 -0.0359 -0.0312 -0.0110 281 VAL A CB  
2219 C CG1 . VAL A 284 ? 0.4687 0.2997 0.2773 -0.0391 -0.0356 -0.0078 281 VAL A CG1 
2220 C CG2 . VAL A 284 ? 0.5103 0.3234 0.2995 -0.0357 -0.0352 -0.0150 281 VAL A CG2 
2221 N N   . GLN A 285 ? 0.4604 0.2768 0.2701 -0.0301 -0.0290 -0.0158 282 GLN A N   
2222 C CA  . GLN A 285 ? 0.4890 0.2991 0.2953 -0.0249 -0.0253 -0.0189 282 GLN A CA  
2223 C C   . GLN A 285 ? 0.4665 0.2870 0.2849 -0.0216 -0.0209 -0.0164 282 GLN A C   
2224 O O   . GLN A 285 ? 0.4815 0.2994 0.2987 -0.0161 -0.0171 -0.0186 282 GLN A O   
2225 C CB  . GLN A 285 ? 0.5098 0.3068 0.3122 -0.0257 -0.0303 -0.0213 282 GLN A CB  
2226 C CG  . GLN A 285 ? 0.5582 0.3424 0.3454 -0.0269 -0.0339 -0.0258 282 GLN A CG  
2227 C CD  . GLN A 285 ? 0.5862 0.3572 0.3709 -0.0287 -0.0393 -0.0282 282 GLN A CD  
2228 O OE1 . GLN A 285 ? 0.6166 0.3837 0.4056 -0.0261 -0.0378 -0.0280 282 GLN A OE1 
2229 N NE2 . GLN A 285 ? 0.5985 0.3635 0.3777 -0.0339 -0.0462 -0.0297 282 GLN A NE2 
2230 N N   . VAL A 286 ? 0.4437 0.2754 0.2729 -0.0244 -0.0214 -0.0123 283 VAL A N   
2231 C CA  . VAL A 286 ? 0.4360 0.2781 0.2763 -0.0217 -0.0182 -0.0101 283 VAL A CA  
2232 C C   . VAL A 286 ? 0.4416 0.2899 0.2817 -0.0173 -0.0115 -0.0117 283 VAL A C   
2233 O O   . VAL A 286 ? 0.4275 0.2817 0.2751 -0.0132 -0.0092 -0.0113 283 VAL A O   
2234 C CB  . VAL A 286 ? 0.4203 0.2729 0.2701 -0.0257 -0.0198 -0.0060 283 VAL A CB  
2235 C CG1 . VAL A 286 ? 0.4194 0.2781 0.2681 -0.0281 -0.0178 -0.0053 283 VAL A CG1 
2236 C CG2 . VAL A 286 ? 0.4144 0.2755 0.2743 -0.0231 -0.0184 -0.0038 283 VAL A CG2 
2237 N N   . PHE A 287 ? 0.4472 0.2951 0.2796 -0.0182 -0.0084 -0.0131 284 PHE A N   
2238 C CA  . PHE A 287 ? 0.4550 0.3101 0.2880 -0.0148 -0.0009 -0.0143 284 PHE A CA  
2239 C C   . PHE A 287 ? 0.4745 0.3219 0.3004 -0.0087 0.0023  -0.0186 284 PHE A C   
2240 O O   . PHE A 287 ? 0.4750 0.3289 0.3020 -0.0053 0.0092  -0.0199 284 PHE A O   
2241 C CB  . PHE A 287 ? 0.4717 0.3285 0.2982 -0.0184 0.0020  -0.0134 284 PHE A CB  
2242 C CG  . PHE A 287 ? 0.4601 0.3244 0.2941 -0.0236 -0.0006 -0.0094 284 PHE A CG  
2243 C CD1 . PHE A 287 ? 0.4515 0.3285 0.2983 -0.0239 0.0019  -0.0074 284 PHE A CD1 
2244 C CD2 . PHE A 287 ? 0.4617 0.3203 0.2905 -0.0277 -0.0059 -0.0080 284 PHE A CD2 
2245 C CE1 . PHE A 287 ? 0.4305 0.3131 0.2832 -0.0284 -0.0004 -0.0044 284 PHE A CE1 
2246 C CE2 . PHE A 287 ? 0.4448 0.3097 0.2806 -0.0315 -0.0079 -0.0047 284 PHE A CE2 
2247 C CZ  . PHE A 287 ? 0.4276 0.3037 0.2746 -0.0318 -0.0051 -0.0031 284 PHE A CZ  
2248 N N   . GLU A 288 ? 0.4882 0.3221 0.3071 -0.0075 -0.0021 -0.0208 285 GLU A N   
2249 C CA  . GLU A 288 ? 0.5224 0.3446 0.3298 -0.0020 0.0006  -0.0259 285 GLU A CA  
2250 C C   . GLU A 288 ? 0.5210 0.3428 0.3352 0.0048  0.0019  -0.0271 285 GLU A C   
2251 O O   . GLU A 288 ? 0.5342 0.3479 0.3408 0.0108  0.0052  -0.0315 285 GLU A O   
2252 C CB  . GLU A 288 ? 0.5485 0.3539 0.3426 -0.0048 -0.0056 -0.0285 285 GLU A CB  
2253 C CG  . GLU A 288 ? 0.5595 0.3626 0.3434 -0.0097 -0.0072 -0.0284 285 GLU A CG  
2254 C CD  . GLU A 288 ? 0.5949 0.3826 0.3667 -0.0127 -0.0144 -0.0312 285 GLU A CD  
2255 O OE1 . GLU A 288 ? 0.6090 0.3854 0.3778 -0.0107 -0.0171 -0.0342 285 GLU A OE1 
2256 O OE2 . GLU A 288 ? 0.6249 0.4118 0.3903 -0.0171 -0.0178 -0.0302 285 GLU A OE2 
2257 N N   . PHE A 289 ? 0.4961 0.3257 0.3235 0.0046  -0.0007 -0.0234 286 PHE A N   
2258 C CA  . PHE A 289 ? 0.5114 0.3389 0.3444 0.0115  -0.0008 -0.0239 286 PHE A CA  
2259 C C   . PHE A 289 ? 0.5012 0.3451 0.3500 0.0121  -0.0007 -0.0197 286 PHE A C   
2260 O O   . PHE A 289 ? 0.4823 0.3365 0.3364 0.0064  -0.0012 -0.0167 286 PHE A O   
2261 C CB  . PHE A 289 ? 0.5230 0.3333 0.3494 0.0100  -0.0072 -0.0242 286 PHE A CB  
2262 C CG  . PHE A 289 ? 0.4992 0.3119 0.3321 0.0035  -0.0130 -0.0192 286 PHE A CG  
2263 C CD1 . PHE A 289 ? 0.4827 0.2953 0.3129 -0.0044 -0.0163 -0.0179 286 PHE A CD1 
2264 C CD2 . PHE A 289 ? 0.4929 0.3074 0.3339 0.0058  -0.0150 -0.0158 286 PHE A CD2 
2265 C CE1 . PHE A 289 ? 0.4639 0.2803 0.3011 -0.0097 -0.0204 -0.0135 286 PHE A CE1 
2266 C CE2 . PHE A 289 ? 0.4720 0.2890 0.3181 0.0000  -0.0193 -0.0112 286 PHE A CE2 
2267 C CZ  . PHE A 289 ? 0.4587 0.2767 0.3032 -0.0077 -0.0217 -0.0103 286 PHE A CZ  
2268 N N   . GLN A 290 ? 0.5194 0.3648 0.3746 0.0193  -0.0003 -0.0197 287 GLN A N   
2269 C CA  . GLN A 290 ? 0.5304 0.3910 0.4002 0.0210  -0.0011 -0.0161 287 GLN A CA  
2270 C C   . GLN A 290 ? 0.5320 0.3841 0.4030 0.0245  -0.0064 -0.0137 287 GLN A C   
2271 O O   . GLN A 290 ? 0.5377 0.3758 0.4016 0.0299  -0.0065 -0.0163 287 GLN A O   
2272 C CB  . GLN A 290 ? 0.5696 0.4431 0.4479 0.0284  0.0049  -0.0183 287 GLN A CB  
2273 C CG  . GLN A 290 ? 0.6051 0.4938 0.4884 0.0243  0.0103  -0.0185 287 GLN A CG  
2274 C CD  . GLN A 290 ? 0.6485 0.5513 0.5429 0.0318  0.0160  -0.0204 287 GLN A CD  
2275 O OE1 . GLN A 290 ? 0.6837 0.5984 0.5914 0.0350  0.0139  -0.0184 287 GLN A OE1 
2276 N NE2 . GLN A 290 ? 0.6773 0.5781 0.5658 0.0354  0.0231  -0.0244 287 GLN A NE2 
2277 N N   . LEU A 291 ? 0.5032 0.3630 0.3819 0.0219  -0.0102 -0.0092 288 LEU A N   
2278 C CA  . LEU A 291 ? 0.5108 0.3654 0.3916 0.0262  -0.0146 -0.0061 288 LEU A CA  
2279 C C   . LEU A 291 ? 0.5077 0.3746 0.3990 0.0352  -0.0130 -0.0065 288 LEU A C   
2280 O O   . LEU A 291 ? 0.4832 0.3674 0.3838 0.0344  -0.0101 -0.0071 288 LEU A O   
2281 C CB  . LEU A 291 ? 0.4934 0.3513 0.3764 0.0193  -0.0190 -0.0011 288 LEU A CB  
2282 C CG  . LEU A 291 ? 0.4828 0.3311 0.3578 0.0106  -0.0206 -0.0007 288 LEU A CG  
2283 C CD1 . LEU A 291 ? 0.4668 0.3230 0.3458 0.0041  -0.0230 0.0034  288 LEU A CD1 
2284 C CD2 . LEU A 291 ? 0.5030 0.3313 0.3686 0.0109  -0.0232 -0.0008 288 LEU A CD2 
2285 N N   . THR A 292 ? 0.5301 0.3883 0.4205 0.0431  -0.0154 -0.0059 289 THR A N   
2286 C CA  . THR A 292 ? 0.5527 0.4233 0.4546 0.0524  -0.0156 -0.0054 289 THR A CA  
2287 C C   . THR A 292 ? 0.5392 0.4227 0.4493 0.0494  -0.0203 -0.0005 289 THR A C   
2288 O O   . THR A 292 ? 0.5185 0.3970 0.4232 0.0415  -0.0234 0.0027  289 THR A O   
2289 C CB  . THR A 292 ? 0.5869 0.4420 0.4839 0.0622  -0.0176 -0.0057 289 THR A CB  
2290 O OG1 . THR A 292 ? 0.5958 0.4371 0.4857 0.0591  -0.0236 -0.0007 289 THR A OG1 
2291 C CG2 . THR A 292 ? 0.6054 0.4460 0.4926 0.0650  -0.0132 -0.0111 289 THR A CG2 
2292 N N   . ALA A 293 ? 0.5575 0.4575 0.4802 0.0556  -0.0209 -0.0003 290 ALA A N   
2293 C CA  . ALA A 293 ? 0.5558 0.4670 0.4855 0.0548  -0.0267 0.0040  290 ALA A CA  
2294 C C   . ALA A 293 ? 0.5625 0.4566 0.4821 0.0559  -0.0327 0.0087  290 ALA A C   
2295 O O   . ALA A 293 ? 0.5587 0.4546 0.4764 0.0506  -0.0367 0.0126  290 ALA A O   
2296 C CB  . ALA A 293 ? 0.5697 0.4994 0.5146 0.0632  -0.0271 0.0029  290 ALA A CB  
2297 N N   . GLU A 294 ? 0.5932 0.4709 0.5062 0.0632  -0.0331 0.0085  291 GLU A N   
2298 C CA  . GLU A 294 ? 0.6108 0.4691 0.5127 0.0643  -0.0382 0.0133  291 GLU A CA  
2299 C C   . GLU A 294 ? 0.5784 0.4239 0.4693 0.0531  -0.0377 0.0149  291 GLU A C   
2300 O O   . GLU A 294 ? 0.5688 0.4071 0.4537 0.0494  -0.0415 0.0200  291 GLU A O   
2301 C CB  . GLU A 294 ? 0.6630 0.5039 0.5593 0.0742  -0.0381 0.0119  291 GLU A CB  
2302 C CG  . GLU A 294 ? 0.7097 0.5617 0.6171 0.0871  -0.0383 0.0100  291 GLU A CG  
2303 C CD  . GLU A 294 ? 0.7369 0.6085 0.6570 0.0901  -0.0322 0.0041  291 GLU A CD  
2304 O OE1 . GLU A 294 ? 0.7121 0.5855 0.6302 0.0829  -0.0266 0.0005  291 GLU A OE1 
2305 O OE2 . GLU A 294 ? 0.7907 0.6768 0.7234 0.0997  -0.0330 0.0034  291 GLU A OE2 
2306 N N   . ASP A 295 ? 0.5472 0.3893 0.4352 0.0481  -0.0332 0.0107  292 ASP A N   
2307 C CA  . ASP A 295 ? 0.5301 0.3636 0.4102 0.0372  -0.0330 0.0117  292 ASP A CA  
2308 C C   . ASP A 295 ? 0.4935 0.3420 0.3787 0.0302  -0.0341 0.0146  292 ASP A C   
2309 O O   . ASP A 295 ? 0.4673 0.3096 0.3472 0.0241  -0.0363 0.0185  292 ASP A O   
2310 C CB  . ASP A 295 ? 0.5293 0.3597 0.4063 0.0339  -0.0286 0.0064  292 ASP A CB  
2311 C CG  . ASP A 295 ? 0.5628 0.3759 0.4321 0.0396  -0.0273 0.0027  292 ASP A CG  
2312 O OD1 . ASP A 295 ? 0.5836 0.3837 0.4490 0.0455  -0.0300 0.0046  292 ASP A OD1 
2313 O OD2 . ASP A 295 ? 0.5834 0.3959 0.4501 0.0386  -0.0234 -0.0024 292 ASP A OD2 
2314 N N   . MET A 296 ? 0.4914 0.3589 0.3867 0.0310  -0.0326 0.0127  293 MET A N   
2315 C CA  . MET A 296 ? 0.4789 0.3598 0.3785 0.0243  -0.0336 0.0145  293 MET A CA  
2316 C C   . MET A 296 ? 0.4862 0.3660 0.3838 0.0257  -0.0388 0.0197  293 MET A C   
2317 O O   . MET A 296 ? 0.4828 0.3616 0.3762 0.0189  -0.0398 0.0224  293 MET A O   
2318 C CB  . MET A 296 ? 0.4651 0.3657 0.3762 0.0248  -0.0312 0.0114  293 MET A CB  
2319 C CG  . MET A 296 ? 0.4605 0.3617 0.3711 0.0216  -0.0256 0.0072  293 MET A CG  
2320 S SD  . MET A 296 ? 0.4338 0.3291 0.3369 0.0103  -0.0249 0.0078  293 MET A SD  
2321 C CE  . MET A 296 ? 0.4134 0.3251 0.3239 0.0053  -0.0265 0.0095  293 MET A CE  
2322 N N   . LYS A 297 ? 0.5161 0.3952 0.4156 0.0346  -0.0418 0.0210  294 LYS A N   
2323 C CA  . LYS A 297 ? 0.5380 0.4151 0.4341 0.0374  -0.0474 0.0263  294 LYS A CA  
2324 C C   . LYS A 297 ? 0.5291 0.3865 0.4121 0.0332  -0.0480 0.0306  294 LYS A C   
2325 O O   . LYS A 297 ? 0.5134 0.3708 0.3917 0.0287  -0.0499 0.0344  294 LYS A O   
2326 C CB  . LYS A 297 ? 0.5937 0.4741 0.4956 0.0490  -0.0504 0.0262  294 LYS A CB  
2327 C CG  . LYS A 297 ? 0.6328 0.5134 0.5322 0.0540  -0.0571 0.0313  294 LYS A CG  
2328 C CD  . LYS A 297 ? 0.6869 0.5764 0.5962 0.0660  -0.0602 0.0302  294 LYS A CD  
2329 C CE  . LYS A 297 ? 0.7246 0.6193 0.6338 0.0714  -0.0681 0.0347  294 LYS A CE  
2330 N NZ  . LYS A 297 ? 0.7405 0.6205 0.6341 0.0664  -0.0709 0.0406  294 LYS A NZ  
2331 N N   . ALA A 298 ? 0.5393 0.3805 0.4165 0.0337  -0.0460 0.0296  295 ALA A N   
2332 C CA  . ALA A 298 ? 0.5502 0.3726 0.4160 0.0285  -0.0464 0.0335  295 ALA A CA  
2333 C C   . ALA A 298 ? 0.5226 0.3497 0.3877 0.0176  -0.0441 0.0339  295 ALA A C   
2334 O O   . ALA A 298 ? 0.5188 0.3384 0.3771 0.0130  -0.0449 0.0387  295 ALA A O   
2335 C CB  . ALA A 298 ? 0.5686 0.3736 0.4293 0.0302  -0.0448 0.0312  295 ALA A CB  
2336 N N   . ILE A 299 ? 0.4861 0.3247 0.3576 0.0137  -0.0412 0.0293  296 ILE A N   
2337 C CA  . ILE A 299 ? 0.4648 0.3070 0.3357 0.0041  -0.0393 0.0297  296 ILE A CA  
2338 C C   . ILE A 299 ? 0.4597 0.3137 0.3322 0.0030  -0.0409 0.0325  296 ILE A C   
2339 O O   . ILE A 299 ? 0.4594 0.3112 0.3276 -0.0029 -0.0405 0.0356  296 ILE A O   
2340 C CB  . ILE A 299 ? 0.4380 0.2867 0.3135 0.0005  -0.0362 0.0244  296 ILE A CB  
2341 C CG1 . ILE A 299 ? 0.4483 0.2836 0.3197 0.0014  -0.0350 0.0215  296 ILE A CG1 
2342 C CG2 . ILE A 299 ? 0.4093 0.2633 0.2853 -0.0079 -0.0349 0.0250  296 ILE A CG2 
2343 C CD1 . ILE A 299 ? 0.4364 0.2783 0.3112 0.0012  -0.0322 0.0161  296 ILE A CD1 
2344 N N   . ASP A 300 ? 0.4615 0.3275 0.3400 0.0084  -0.0428 0.0312  297 ASP A N   
2345 C CA  . ASP A 300 ? 0.4675 0.3440 0.3467 0.0077  -0.0454 0.0333  297 ASP A CA  
2346 C C   . ASP A 300 ? 0.4785 0.3441 0.3472 0.0077  -0.0477 0.0393  297 ASP A C   
2347 O O   . ASP A 300 ? 0.4665 0.3358 0.3314 0.0036  -0.0480 0.0414  297 ASP A O   
2348 C CB  . ASP A 300 ? 0.4785 0.3679 0.3655 0.0144  -0.0485 0.0318  297 ASP A CB  
2349 C CG  . ASP A 300 ? 0.4642 0.3679 0.3620 0.0131  -0.0460 0.0266  297 ASP A CG  
2350 O OD1 . ASP A 300 ? 0.4624 0.3676 0.3604 0.0063  -0.0425 0.0245  297 ASP A OD1 
2351 O OD2 . ASP A 300 ? 0.4866 0.3999 0.3927 0.0191  -0.0476 0.0248  297 ASP A OD2 
2352 N N   . GLY A 301 ? 0.5041 0.3559 0.3676 0.0125  -0.0492 0.0421  298 GLY A N   
2353 C CA  . GLY A 301 ? 0.5185 0.3574 0.3707 0.0132  -0.0514 0.0486  298 GLY A CA  
2354 C C   . GLY A 301 ? 0.5167 0.3473 0.3624 0.0042  -0.0477 0.0513  298 GLY A C   
2355 O O   . GLY A 301 ? 0.5368 0.3588 0.3728 0.0032  -0.0484 0.0570  298 GLY A O   
2356 N N   . LEU A 302 ? 0.4949 0.3272 0.3453 -0.0021 -0.0439 0.0477  299 LEU A N   
2357 C CA  . LEU A 302 ? 0.4830 0.3094 0.3296 -0.0107 -0.0404 0.0500  299 LEU A CA  
2358 C C   . LEU A 302 ? 0.4713 0.3093 0.3177 -0.0147 -0.0391 0.0509  299 LEU A C   
2359 O O   . LEU A 302 ? 0.4647 0.2998 0.3084 -0.0211 -0.0359 0.0533  299 LEU A O   
2360 C CB  . LEU A 302 ? 0.4653 0.2911 0.3177 -0.0152 -0.0380 0.0455  299 LEU A CB  
2361 C CG  . LEU A 302 ? 0.4864 0.2988 0.3374 -0.0119 -0.0390 0.0439  299 LEU A CG  
2362 C CD1 . LEU A 302 ? 0.4720 0.2848 0.3275 -0.0159 -0.0372 0.0387  299 LEU A CD1 
2363 C CD2 . LEU A 302 ? 0.5143 0.3083 0.3563 -0.0131 -0.0396 0.0494  299 LEU A CD2 
2364 N N   . ASP A 303 ? 0.4814 0.3322 0.3310 -0.0113 -0.0412 0.0487  300 ASP A N   
2365 C CA  . ASP A 303 ? 0.4846 0.3461 0.3341 -0.0153 -0.0397 0.0480  300 ASP A CA  
2366 C C   . ASP A 303 ? 0.5092 0.3640 0.3480 -0.0177 -0.0385 0.0537  300 ASP A C   
2367 O O   . ASP A 303 ? 0.5261 0.3723 0.3566 -0.0135 -0.0413 0.0583  300 ASP A O   
2368 C CB  . ASP A 303 ? 0.4969 0.3717 0.3509 -0.0117 -0.0429 0.0447  300 ASP A CB  
2369 C CG  . ASP A 303 ? 0.5080 0.3926 0.3621 -0.0158 -0.0414 0.0427  300 ASP A CG  
2370 O OD1 . ASP A 303 ? 0.4845 0.3694 0.3397 -0.0212 -0.0373 0.0418  300 ASP A OD1 
2371 O OD2 . ASP A 303 ? 0.5715 0.4635 0.4246 -0.0132 -0.0449 0.0418  300 ASP A OD2 
2372 N N   . ARG A 304 ? 0.5094 0.3674 0.3479 -0.0239 -0.0341 0.0538  301 ARG A N   
2373 C CA  . ARG A 304 ? 0.5362 0.3900 0.3642 -0.0263 -0.0318 0.0589  301 ARG A CA  
2374 C C   . ARG A 304 ? 0.5237 0.3879 0.3519 -0.0296 -0.0286 0.0567  301 ARG A C   
2375 O O   . ARG A 304 ? 0.5141 0.3750 0.3343 -0.0327 -0.0248 0.0607  301 ARG A O   
2376 C CB  . ARG A 304 ? 0.5682 0.4096 0.3928 -0.0309 -0.0282 0.0637  301 ARG A CB  
2377 C CG  . ARG A 304 ? 0.5674 0.4113 0.4019 -0.0371 -0.0245 0.0610  301 ARG A CG  
2378 C CD  . ARG A 304 ? 0.6174 0.4467 0.4495 -0.0398 -0.0238 0.0648  301 ARG A CD  
2379 N NE  . ARG A 304 ? 0.6497 0.4713 0.4825 -0.0344 -0.0284 0.0632  301 ARG A NE  
2380 C CZ  . ARG A 304 ? 0.6529 0.4599 0.4836 -0.0353 -0.0290 0.0652  301 ARG A CZ  
2381 N NH1 . ARG A 304 ? 0.6664 0.4649 0.4942 -0.0422 -0.0256 0.0695  301 ARG A NH1 
2382 N NH2 . ARG A 304 ? 0.6347 0.4359 0.4663 -0.0295 -0.0327 0.0627  301 ARG A NH2 
2383 N N   . ASN A 305 ? 0.5128 0.3880 0.3484 -0.0289 -0.0299 0.0510  302 ASN A N   
2384 C CA  . ASN A 305 ? 0.5371 0.4207 0.3716 -0.0311 -0.0274 0.0485  302 ASN A CA  
2385 C C   . ASN A 305 ? 0.5259 0.4090 0.3624 -0.0367 -0.0210 0.0497  302 ASN A C   
2386 O O   . ASN A 305 ? 0.5113 0.3967 0.3419 -0.0382 -0.0174 0.0506  302 ASN A O   
2387 C CB  . ASN A 305 ? 0.6055 0.4879 0.4272 -0.0285 -0.0293 0.0510  302 ASN A CB  
2388 C CG  . ASN A 305 ? 0.6469 0.5368 0.4656 -0.0298 -0.0275 0.0475  302 ASN A CG  
2389 O OD1 . ASN A 305 ? 0.6875 0.5751 0.4967 -0.0313 -0.0236 0.0500  302 ASN A OD1 
2390 N ND2 . ASN A 305 ? 0.6873 0.5852 0.5132 -0.0291 -0.0302 0.0419  302 ASN A ND2 
2391 N N   . LEU A 306 ? 0.5067 0.3871 0.3510 -0.0395 -0.0196 0.0497  303 LEU A N   
2392 C CA  . LEU A 306 ? 0.5164 0.3973 0.3648 -0.0451 -0.0143 0.0511  303 LEU A CA  
2393 C C   . LEU A 306 ? 0.4812 0.3717 0.3395 -0.0463 -0.0134 0.0457  303 LEU A C   
2394 O O   . LEU A 306 ? 0.4337 0.3241 0.2989 -0.0460 -0.0160 0.0429  303 LEU A O   
2395 C CB  . LEU A 306 ? 0.5471 0.4186 0.3981 -0.0478 -0.0144 0.0538  303 LEU A CB  
2396 C CG  . LEU A 306 ? 0.5708 0.4447 0.4299 -0.0542 -0.0103 0.0541  303 LEU A CG  
2397 C CD1 . LEU A 306 ? 0.6023 0.4764 0.4568 -0.0579 -0.0045 0.0588  303 LEU A CD1 
2398 C CD2 . LEU A 306 ? 0.5806 0.4455 0.4437 -0.0567 -0.0123 0.0547  303 LEU A CD2 
2399 N N   . HIS A 307 ? 0.4774 0.3752 0.3356 -0.0469 -0.0102 0.0441  304 HIS A N   
2400 C CA  . HIS A 307 ? 0.4850 0.3903 0.3533 -0.0485 -0.0086 0.0400  304 HIS A CA  
2401 C C   . HIS A 307 ? 0.4733 0.3797 0.3482 -0.0533 -0.0045 0.0423  304 HIS A C   
2402 O O   . HIS A 307 ? 0.5275 0.4338 0.3987 -0.0554 0.0001  0.0460  304 HIS A O   
2403 C CB  . HIS A 307 ? 0.5128 0.4249 0.3798 -0.0465 -0.0076 0.0362  304 HIS A CB  
2404 C CG  . HIS A 307 ? 0.5412 0.4535 0.3984 -0.0457 -0.0042 0.0378  304 HIS A CG  
2405 N ND1 . HIS A 307 ? 0.5802 0.4966 0.4383 -0.0476 0.0020  0.0388  304 HIS A ND1 
2406 C CD2 . HIS A 307 ? 0.5695 0.4794 0.4157 -0.0429 -0.0063 0.0380  304 HIS A CD2 
2407 C CE1 . HIS A 307 ? 0.6063 0.5216 0.4527 -0.0460 0.0043  0.0397  304 HIS A CE1 
2408 N NE2 . HIS A 307 ? 0.6101 0.5211 0.4487 -0.0432 -0.0012 0.0392  304 HIS A NE2 
2409 N N   . TYR A 308 ? 0.4387 0.3468 0.3234 -0.0551 -0.0063 0.0401  305 TYR A N   
2410 C CA  . TYR A 308 ? 0.4246 0.3350 0.3181 -0.0601 -0.0039 0.0416  305 TYR A CA  
2411 C C   . TYR A 308 ? 0.4276 0.3486 0.3266 -0.0607 0.0009  0.0406  305 TYR A C   
2412 O O   . TYR A 308 ? 0.4370 0.3614 0.3405 -0.0646 0.0054  0.0435  305 TYR A O   
2413 C CB  . TYR A 308 ? 0.3985 0.3072 0.2991 -0.0611 -0.0085 0.0388  305 TYR A CB  
2414 C CG  . TYR A 308 ? 0.3938 0.2914 0.2906 -0.0621 -0.0114 0.0407  305 TYR A CG  
2415 C CD1 . TYR A 308 ? 0.3983 0.2904 0.2953 -0.0669 -0.0096 0.0448  305 TYR A CD1 
2416 C CD2 . TYR A 308 ? 0.3775 0.2696 0.2702 -0.0582 -0.0155 0.0385  305 TYR A CD2 
2417 C CE1 . TYR A 308 ? 0.4075 0.2873 0.3000 -0.0675 -0.0123 0.0464  305 TYR A CE1 
2418 C CE2 . TYR A 308 ? 0.3810 0.2624 0.2701 -0.0582 -0.0179 0.0398  305 TYR A CE2 
2419 C CZ  . TYR A 308 ? 0.3998 0.2742 0.2883 -0.0627 -0.0166 0.0436  305 TYR A CZ  
2420 O OH  . TYR A 308 ? 0.4135 0.2752 0.2974 -0.0626 -0.0190 0.0449  305 TYR A OH  
2421 N N   . PHE A 309 ? 0.4187 0.3448 0.3181 -0.0568 0.0002  0.0365  306 PHE A N   
2422 C CA  . PHE A 309 ? 0.4369 0.3724 0.3416 -0.0559 0.0044  0.0347  306 PHE A CA  
2423 C C   . PHE A 309 ? 0.4773 0.4132 0.3722 -0.0543 0.0094  0.0360  306 PHE A C   
2424 O O   . PHE A 309 ? 0.5172 0.4480 0.4010 -0.0514 0.0075  0.0354  306 PHE A O   
2425 C CB  . PHE A 309 ? 0.4246 0.3626 0.3321 -0.0523 0.0011  0.0297  306 PHE A CB  
2426 C CG  . PHE A 309 ? 0.4092 0.3462 0.3243 -0.0536 -0.0037 0.0284  306 PHE A CG  
2427 C CD1 . PHE A 309 ? 0.4253 0.3669 0.3509 -0.0570 -0.0035 0.0294  306 PHE A CD1 
2428 C CD2 . PHE A 309 ? 0.4171 0.3485 0.3283 -0.0519 -0.0084 0.0264  306 PHE A CD2 
2429 C CE1 . PHE A 309 ? 0.4175 0.3571 0.3481 -0.0582 -0.0087 0.0279  306 PHE A CE1 
2430 C CE2 . PHE A 309 ? 0.4181 0.3478 0.3342 -0.0529 -0.0125 0.0251  306 PHE A CE2 
2431 C CZ  . PHE A 309 ? 0.4028 0.3358 0.3276 -0.0559 -0.0129 0.0258  306 PHE A CZ  
2432 N N   . ASN A 310 ? 0.6981 0.6543 0.6948 -0.1564 0.0038  0.0269  307 ASN A N   
2433 C CA  A ASN A 310 ? 0.7188 0.6828 0.7059 -0.1585 0.0253  0.0492  307 ASN A CA  
2434 C CA  B ASN A 310 ? 0.7047 0.6687 0.6926 -0.1589 0.0255  0.0493  307 ASN A CA  
2435 C C   . ASN A 310 ? 0.7079 0.7184 0.7148 -0.1575 0.0308  0.0448  307 ASN A C   
2436 O O   . ASN A 310 ? 0.7205 0.7544 0.7630 -0.1648 0.0221  0.0285  307 ASN A O   
2437 C CB  A ASN A 310 ? 0.7905 0.7312 0.7933 -0.1761 0.0395  0.0678  307 ASN A CB  
2438 C CB  B ASN A 310 ? 0.7589 0.6996 0.7612 -0.1761 0.0405  0.0689  307 ASN A CB  
2439 C CG  A ASN A 310 ? 0.8425 0.7897 0.9005 -0.1979 0.0327  0.0557  307 ASN A CG  
2440 C CG  B ASN A 310 ? 0.7549 0.6527 0.7161 -0.1661 0.0411  0.0805  307 ASN A CG  
2441 O OD1 A ASN A 310 ? 0.8518 0.8407 0.9466 -0.2056 0.0356  0.0486  307 ASN A OD1 
2442 O OD1 B ASN A 310 ? 0.7241 0.6227 0.6500 -0.1498 0.0479  0.0901  307 ASN A OD1 
2443 N ND2 A ASN A 310 ? 0.8883 0.7969 0.9540 -0.2052 0.0198  0.0486  307 ASN A ND2 
2444 N ND2 B ASN A 310 ? 0.7768 0.6383 0.7429 -0.1728 0.0312  0.0763  307 ASN A ND2 
2445 N N   . SER A 311 ? 0.7168 0.7404 0.6996 -0.1450 0.0418  0.0556  308 SER A N   
2446 C CA  . SER A 311 ? 0.7456 0.8140 0.7417 -0.1396 0.0483  0.0528  308 SER A CA  
2447 C C   . SER A 311 ? 0.7768 0.8509 0.7468 -0.1276 0.0654  0.0716  308 SER A C   
2448 O O   . SER A 311 ? 0.7543 0.8108 0.6867 -0.1098 0.0581  0.0698  308 SER A O   
2449 C CB  . SER A 311 ? 0.7075 0.7860 0.6890 -0.1224 0.0318  0.0341  308 SER A CB  
2450 O OG  . SER A 311 ? 0.7132 0.8274 0.6936 -0.1102 0.0370  0.0325  308 SER A OG  
2451 N N   . ASP A 312 ? 0.8545 0.9538 0.8452 -0.1353 0.0870  0.0886  309 ASP A N   
2452 C CA  . ASP A 312 ? 0.9038 1.0119 0.8621 -0.1160 0.1044  0.1074  309 ASP A CA  
2453 C C   . ASP A 312 ? 0.8707 1.0076 0.8097 -0.0915 0.0941  0.0916  309 ASP A C   
2454 O O   . ASP A 312 ? 0.8826 1.0104 0.7804 -0.0670 0.0912  0.0927  309 ASP A O   
2455 C CB  . ASP A 312 ? 0.9959 1.1221 0.9789 -0.1283 0.1352  0.1356  309 ASP A CB  
2456 C CG  . ASP A 312 ? 1.0261 1.2025 1.0690 -0.1467 0.1443  0.1325  309 ASP A CG  
2457 O OD1 . ASP A 312 ? 0.9755 1.1677 1.0382 -0.1496 0.1232  0.1054  309 ASP A OD1 
2458 O OD2 . ASP A 312 ? 1.1073 1.3090 1.1780 -0.1566 0.1736  0.1579  309 ASP A OD2 
2459 N N   . SER A 313 ? 0.8594 1.0261 0.8263 -0.0956 0.0851  0.0744  310 SER A N   
2460 C CA  . SER A 313 ? 0.8269 1.0103 0.7759 -0.0729 0.0698  0.0554  310 SER A CA  
2461 C C   . SER A 313 ? 0.7675 0.9082 0.6775 -0.0585 0.0519  0.0472  310 SER A C   
2462 O O   . SER A 313 ? 0.8041 0.9470 0.6858 -0.0348 0.0473  0.0434  310 SER A O   
2463 C CB  . SER A 313 ? 0.8422 1.0479 0.8224 -0.0801 0.0583  0.0368  310 SER A CB  
2464 O OG  . SER A 313 ? 0.8624 1.0627 0.8164 -0.0579 0.0404  0.0200  310 SER A OG  
2465 N N   . PHE A 314 ? 0.6889 0.7941 0.5998 -0.0706 0.0418  0.0438  311 PHE A N   
2466 C CA  . PHE A 314 ? 0.6483 0.7188 0.5338 -0.0601 0.0266  0.0367  311 PHE A CA  
2467 C C   . PHE A 314 ? 0.6417 0.6887 0.5061 -0.0558 0.0295  0.0461  311 PHE A C   
2468 O O   . PHE A 314 ? 0.6051 0.6345 0.4526 -0.0429 0.0175  0.0386  311 PHE A O   
2469 C CB  . PHE A 314 ? 0.6270 0.6783 0.5217 -0.0693 0.0162  0.0293  311 PHE A CB  
2470 C CG  . PHE A 314 ? 0.6162 0.6859 0.5166 -0.0603 0.0086  0.0167  311 PHE A CG  
2471 C CD1 . PHE A 314 ? 0.6277 0.6925 0.5103 -0.0421 0.0008  0.0107  311 PHE A CD1 
2472 C CD2 . PHE A 314 ? 0.6307 0.7250 0.5556 -0.0676 0.0081  0.0092  311 PHE A CD2 
2473 C CE1 . PHE A 314 ? 0.6488 0.7280 0.5308 -0.0294 -0.0059 0.0001  311 PHE A CE1 
2474 C CE2 . PHE A 314 ? 0.6555 0.7706 0.5817 -0.0537 0.0000  -0.0042 311 PHE A CE2 
2475 C CZ  . PHE A 314 ? 0.6569 0.7629 0.5582 -0.0336 -0.0061 -0.0072 311 PHE A CZ  
2476 N N   . ALA A 315 ? 0.6599 0.7066 0.5269 -0.0648 0.0446  0.0618  312 ALA A N   
2477 C CA  . ALA A 315 ? 0.6875 0.7121 0.5282 -0.0556 0.0483  0.0719  312 ALA A CA  
2478 C C   . ALA A 315 ? 0.6867 0.7198 0.4992 -0.0268 0.0416  0.0648  312 ALA A C   
2479 O O   . ALA A 315 ? 0.6826 0.6953 0.4733 -0.0137 0.0331  0.0616  312 ALA A O   
2480 C CB  . ALA A 315 ? 0.7385 0.7647 0.5839 -0.0652 0.0703  0.0942  312 ALA A CB  
2481 N N   . SER A 316 ? 0.7002 0.7645 0.5129 -0.0145 0.0440  0.0606  313 SER A N   
2482 C CA  . SER A 316 ? 0.7172 0.7929 0.5004 0.0185  0.0366  0.0520  313 SER A CA  
2483 C C   . SER A 316 ? 0.6593 0.7200 0.4438 0.0268  0.0105  0.0276  313 SER A C   
2484 O O   . SER A 316 ? 0.6795 0.7401 0.4428 0.0542  -0.0036 0.0138  313 SER A O   
2485 C CB  . SER A 316 ? 0.7768 0.8952 0.5571 0.0318  0.0532  0.0605  313 SER A CB  
2486 O OG  . SER A 316 ? 0.7675 0.9065 0.5755 0.0197  0.0509  0.0522  313 SER A OG  
2487 N N   . HIS A 317 ? 0.5891 0.6350 0.3970 0.0065  0.0035  0.0223  314 HIS A N   
2488 C CA  . HIS A 317 ? 0.5591 0.5864 0.3714 0.0129  -0.0170 0.0048  314 HIS A CA  
2489 C C   . HIS A 317 ? 0.5612 0.5636 0.3690 0.0206  -0.0322 -0.0049 314 HIS A C   
2490 O O   . HIS A 317 ? 0.5392 0.5297 0.3501 0.0096  -0.0284 0.0022  314 HIS A O   
2491 C CB  . HIS A 317 ? 0.5079 0.5237 0.3410 -0.0070 -0.0167 0.0068  314 HIS A CB  
2492 C CG  . HIS A 317 ? 0.5048 0.5047 0.3413 0.0009  -0.0307 -0.0047 314 HIS A CG  
2493 N ND1 . HIS A 317 ? 0.5111 0.4821 0.3534 0.0044  -0.0454 -0.0131 314 HIS A ND1 
2494 C CD2 . HIS A 317 ? 0.5026 0.5089 0.3397 0.0060  -0.0323 -0.0084 314 HIS A CD2 
2495 C CE1 . HIS A 317 ? 0.5248 0.4801 0.3721 0.0089  -0.0531 -0.0182 314 HIS A CE1 
2496 N NE2 . HIS A 317 ? 0.5180 0.4942 0.3570 0.0127  -0.0457 -0.0156 314 HIS A NE2 
2497 N N   . PRO A 318 ? 0.5895 0.5822 0.3946 0.0392  -0.0526 -0.0240 315 PRO A N   
2498 C CA  . PRO A 318 ? 0.6068 0.5781 0.4210 0.0432  -0.0706 -0.0376 315 PRO A CA  
2499 C C   . PRO A 318 ? 0.5683 0.5198 0.4116 0.0167  -0.0682 -0.0307 315 PRO A C   
2500 O O   . PRO A 318 ? 0.5604 0.5055 0.4111 0.0165  -0.0752 -0.0359 315 PRO A O   
2501 C CB  . PRO A 318 ? 0.6499 0.6079 0.4713 0.0595  -0.0945 -0.0605 315 PRO A CB  
2502 C CG  . PRO A 318 ? 0.6681 0.6476 0.4665 0.0766  -0.0891 -0.0600 315 PRO A CG  
2503 C CD  . PRO A 318 ? 0.6197 0.6206 0.4174 0.0575  -0.0619 -0.0361 315 PRO A CD  
2504 N N   . ASN A 319 ? 0.5413 0.4869 0.3989 -0.0013 -0.0586 -0.0198 316 ASN A N   
2505 C CA  . ASN A 319 ? 0.5272 0.4578 0.4092 -0.0215 -0.0538 -0.0109 316 ASN A CA  
2506 C C   . ASN A 319 ? 0.5009 0.4406 0.3741 -0.0338 -0.0370 0.0049  316 ASN A C   
2507 O O   . ASN A 319 ? 0.4835 0.4156 0.3699 -0.0464 -0.0307 0.0136  316 ASN A O   
2508 C CB  . ASN A 319 ? 0.5509 0.4651 0.4497 -0.0272 -0.0543 -0.0080 316 ASN A CB  
2509 C CG  . ASN A 319 ? 0.6113 0.5038 0.5373 -0.0254 -0.0708 -0.0206 316 ASN A CG  
2510 O OD1 . ASN A 319 ? 0.6671 0.5600 0.6077 -0.0237 -0.0826 -0.0327 316 ASN A OD1 
2511 N ND2 . ASN A 319 ? 0.6461 0.5186 0.5812 -0.0247 -0.0731 -0.0190 316 ASN A ND2 
2512 N N   . TYR A 320 ? 0.4981 0.4530 0.3510 -0.0292 -0.0289 0.0095  317 TYR A N   
2513 C CA  . TYR A 320 ? 0.4750 0.4316 0.3243 -0.0418 -0.0158 0.0226  317 TYR A CA  
2514 C C   . TYR A 320 ? 0.4624 0.4042 0.3182 -0.0461 -0.0200 0.0227  317 TYR A C   
2515 O O   . TYR A 320 ? 0.4680 0.4068 0.3204 -0.0354 -0.0292 0.0146  317 TYR A O   
2516 C CB  . TYR A 320 ? 0.5029 0.4720 0.3335 -0.0358 -0.0055 0.0304  317 TYR A CB  
2517 C CG  . TYR A 320 ? 0.4983 0.4637 0.3318 -0.0515 0.0073  0.0438  317 TYR A CG  
2518 C CD1 . TYR A 320 ? 0.4847 0.4552 0.3358 -0.0658 0.0104  0.0446  317 TYR A CD1 
2519 C CD2 . TYR A 320 ? 0.5353 0.4904 0.3532 -0.0493 0.0148  0.0542  317 TYR A CD2 
2520 C CE1 . TYR A 320 ? 0.4956 0.4593 0.3548 -0.0800 0.0170  0.0518  317 TYR A CE1 
2521 C CE2 . TYR A 320 ? 0.5435 0.4877 0.3673 -0.0646 0.0245  0.0657  317 TYR A CE2 
2522 C CZ  . TYR A 320 ? 0.5377 0.4862 0.3851 -0.0811 0.0244  0.0630  317 TYR A CZ  
2523 O OH  . TYR A 320 ? 0.5712 0.5067 0.4291 -0.0957 0.0296  0.0697  317 TYR A OH  
2524 N N   . PRO A 321 ? 0.4430 0.3786 0.3091 -0.0577 -0.0155 0.0290  318 PRO A N   
2525 C CA  . PRO A 321 ? 0.4467 0.3747 0.3217 -0.0594 -0.0186 0.0288  318 PRO A CA  
2526 C C   . PRO A 321 ? 0.4774 0.3999 0.3346 -0.0561 -0.0171 0.0318  318 PRO A C   
2527 O O   . PRO A 321 ? 0.4735 0.3937 0.3357 -0.0529 -0.0220 0.0285  318 PRO A O   
2528 C CB  . PRO A 321 ? 0.4262 0.3528 0.3100 -0.0668 -0.0122 0.0362  318 PRO A CB  
2529 C CG  . PRO A 321 ? 0.4165 0.3478 0.2904 -0.0695 -0.0073 0.0385  318 PRO A CG  
2530 C CD  . PRO A 321 ? 0.4320 0.3717 0.3010 -0.0652 -0.0088 0.0341  318 PRO A CD  
2531 N N   . TYR A 322 ? 0.5118 0.4321 0.3517 -0.0577 -0.0090 0.0394  319 TYR A N   
2532 C CA  . TYR A 322 ? 0.5691 0.4755 0.3894 -0.0539 -0.0056 0.0460  319 TYR A CA  
2533 C C   . TYR A 322 ? 0.6473 0.5561 0.4459 -0.0364 -0.0062 0.0456  319 TYR A C   
2534 O O   . TYR A 322 ? 0.7238 0.6190 0.5007 -0.0271 -0.0042 0.0512  319 TYR A O   
2535 C CB  . TYR A 322 ? 0.5670 0.4637 0.3872 -0.0669 0.0034  0.0558  319 TYR A CB  
2536 C CG  . TYR A 322 ? 0.5407 0.4376 0.3767 -0.0757 -0.0002 0.0515  319 TYR A CG  
2537 C CD1 . TYR A 322 ? 0.5293 0.4226 0.3666 -0.0707 -0.0062 0.0475  319 TYR A CD1 
2538 C CD2 . TYR A 322 ? 0.5322 0.4370 0.3814 -0.0856 0.0026  0.0508  319 TYR A CD2 
2539 C CE1 . TYR A 322 ? 0.5153 0.4114 0.3601 -0.0720 -0.0080 0.0451  319 TYR A CE1 
2540 C CE2 . TYR A 322 ? 0.5197 0.4258 0.3771 -0.0867 -0.0028 0.0446  319 TYR A CE2 
2541 C CZ  . TYR A 322 ? 0.5147 0.4155 0.3665 -0.0782 -0.0074 0.0427  319 TYR A CZ  
2542 O OH  . TYR A 322 ? 0.5140 0.4182 0.3674 -0.0730 -0.0117 0.0375  319 TYR A OH  
2543 N N   . SER A 323 ? 0.7125 0.6358 0.5157 -0.0274 -0.0131 0.0355  320 SER A N   
2544 C CA  . SER A 323 ? 0.8208 0.7548 0.6024 -0.0071 -0.0128 0.0338  320 SER A CA  
2545 C C   . SER A 323 ? 0.9336 0.8611 0.6839 0.0172  -0.0162 0.0330  320 SER A C   
2546 O O   . SER A 323 ? 1.0616 0.9967 0.7840 0.0364  -0.0083 0.0402  320 SER A O   
2547 C CB  . SER A 323 ? 0.8122 0.7575 0.6080 0.0005  -0.0274 0.0160  320 SER A CB  
2548 O OG  . SER A 323 ? 0.8386 0.7944 0.6098 0.0275  -0.0327 0.0088  320 SER A OG  
2549 N N   . ASP A 324 ? 0.9898 0.9076 0.7423 0.0211  -0.0273 0.0245  321 ASP A N   
2550 C CA  . ASP A 324 ? 1.0653 0.9789 0.7852 0.0511  -0.0352 0.0187  321 ASP A CA  
2551 C C   . ASP A 324 ? 1.0947 0.9866 0.7986 0.0485  -0.0278 0.0315  321 ASP A C   
2552 O O   . ASP A 324 ? 1.0955 0.9845 0.7849 0.0694  -0.0407 0.0201  321 ASP A O   
2553 C CB  . ASP A 324 ? 1.1010 1.0286 0.8406 0.0661  -0.0619 -0.0115 321 ASP A CB  
2554 C CG  . ASP A 324 ? 1.1157 1.0569 0.8671 0.0727  -0.0724 -0.0261 321 ASP A CG  
2555 O OD1 . ASP A 324 ? 1.1563 1.1053 0.8769 0.1052  -0.0805 -0.0356 321 ASP A OD1 
2556 O OD2 . ASP A 324 ? 1.0879 1.0307 0.8758 0.0492  -0.0732 -0.0283 321 ASP A OD2 
2557 N N   . GLU A 325 ? 1.0922 0.9693 0.7990 0.0260  -0.0099 0.0521  322 GLU A N   
2558 C CA  . GLU A 325 ? 1.0824 0.9311 0.7751 0.0208  -0.0026 0.0656  322 GLU A CA  
2559 C C   . GLU A 325 ? 1.1398 0.9685 0.7845 0.0477  0.0059  0.0799  322 GLU A C   
2560 O O   . GLU A 325 ? 1.2208 1.0276 0.8437 0.0604  0.0009  0.0803  322 GLU A O   
2561 C CB  . GLU A 325 ? 1.0882 0.9275 0.8010 -0.0084 0.0116  0.0803  322 GLU A CB  
2562 C CG  . GLU A 325 ? 1.1516 0.9554 0.8525 -0.0147 0.0180  0.0937  322 GLU A CG  
2563 C CD  . GLU A 325 ? 1.2155 1.0000 0.9185 -0.0303 0.0383  0.1172  322 GLU A CD  
2564 O OE1 . GLU A 325 ? 1.1912 0.9749 0.9266 -0.0554 0.0396  0.1165  322 GLU A OE1 
2565 O OE2 . GLU A 325 ? 1.2835 1.0523 0.9564 -0.0158 0.0530  0.1368  322 GLU A OE2 
2566 N N   . TYR A 326 ? 1.1134 0.9491 0.7388 0.0589  0.0202  0.0937  323 TYR A N   
2567 C CA  . TYR A 326 ? 1.1586 0.9771 0.7320 0.0899  0.0338  0.1133  323 TYR A CA  
2568 C C   . TYR A 326 ? 1.1622 1.0092 0.7128 0.1211  0.0325  0.1073  323 TYR A C   
2569 O O   . TYR A 326 ? 1.0564 0.9317 0.6389 0.1097  0.0229  0.0903  323 TYR A O   
2570 C CB  . TYR A 326 ? 1.1945 0.9858 0.7660 0.0704  0.0630  0.1484  323 TYR A CB  
2571 C CG  . TYR A 326 ? 1.2077 1.0230 0.7932 0.0605  0.0846  0.1653  323 TYR A CG  
2572 C CD1 . TYR A 326 ? 1.2819 1.1022 0.8282 0.0892  0.1057  0.1883  323 TYR A CD1 
2573 C CD2 . TYR A 326 ? 1.1352 0.9737 0.7702 0.0282  0.0832  0.1568  323 TYR A CD2 
2574 C CE1 . TYR A 326 ? 1.3131 1.1634 0.8735 0.0832  0.1271  0.2042  323 TYR A CE1 
2575 C CE2 . TYR A 326 ? 1.1622 1.0292 0.8117 0.0220  0.1016  0.1696  323 TYR A CE2 
2576 C CZ  . TYR A 326 ? 1.2606 1.1354 0.8749 0.0485  0.1241  0.1934  323 TYR A CZ  
2577 O OH  . TYR A 326 ? 1.3196 1.2288 0.9500 0.0441  0.1442  0.2070  323 TYR A OH  
2578 O OXT . TYR A 326 ? 1.1645 1.0053 0.6628 0.1600  0.0403  0.1189  323 TYR A OXT 
2579 N N   . GLN B 9   ? 0.7326 0.6536 0.6644 -0.1335 -0.0876 0.0724  6   GLN B N   
2580 C CA  . GLN B 9   ? 0.7151 0.6544 0.6567 -0.1295 -0.0848 0.0684  6   GLN B CA  
2581 C C   . GLN B 9   ? 0.6412 0.5884 0.5768 -0.1168 -0.0747 0.0625  6   GLN B C   
2582 O O   . GLN B 9   ? 0.5787 0.5120 0.5037 -0.1079 -0.0754 0.0550  6   GLN B O   
2583 C CB  . GLN B 9   ? 0.7671 0.6960 0.7106 -0.1292 -0.0959 0.0618  6   GLN B CB  
2584 C CG  . GLN B 9   ? 0.8030 0.7534 0.7595 -0.1289 -0.0946 0.0609  6   GLN B CG  
2585 C CD  . GLN B 9   ? 0.8423 0.7860 0.7965 -0.1214 -0.1012 0.0514  6   GLN B CD  
2586 O OE1 . GLN B 9   ? 0.8980 0.8211 0.8456 -0.1218 -0.1118 0.0469  6   GLN B OE1 
2587 N NE2 . GLN B 9   ? 0.8231 0.7840 0.7822 -0.1142 -0.0955 0.0483  6   GLN B NE2 
2588 N N   . CYS B 10  ? 0.6254 0.5952 0.5683 -0.1160 -0.0657 0.0660  7   CYS B N   
2589 C CA  . CYS B 10  ? 0.6056 0.5842 0.5432 -0.1055 -0.0554 0.0624  7   CYS B CA  
2590 C C   . CYS B 10  ? 0.5703 0.5681 0.5176 -0.1014 -0.0520 0.0605  7   CYS B C   
2591 O O   . CYS B 10  ? 0.5841 0.5924 0.5433 -0.1084 -0.0562 0.0644  7   CYS B O   
2592 C CB  . CYS B 10  ? 0.6423 0.6288 0.5768 -0.1078 -0.0476 0.0692  7   CYS B CB  
2593 S SG  . CYS B 10  ? 0.6938 0.6577 0.6131 -0.1076 -0.0496 0.0691  7   CYS B SG  
2594 N N   . VAL B 11  ? 0.5350 0.5367 0.4772 -0.0907 -0.0453 0.0551  8   VAL B N   
2595 C CA  . VAL B 11  ? 0.5260 0.5469 0.4757 -0.0849 -0.0404 0.0541  8   VAL B CA  
2596 C C   . VAL B 11  ? 0.5131 0.5449 0.4585 -0.0795 -0.0300 0.0558  8   VAL B C   
2597 O O   . VAL B 11  ? 0.5154 0.5347 0.4492 -0.0769 -0.0274 0.0539  8   VAL B O   
2598 C CB  . VAL B 11  ? 0.5235 0.5370 0.4697 -0.0761 -0.0429 0.0459  8   VAL B CB  
2599 C CG1 . VAL B 11  ? 0.5449 0.5487 0.4943 -0.0808 -0.0536 0.0440  8   VAL B CG1 
2600 C CG2 . VAL B 11  ? 0.5042 0.5024 0.4369 -0.0684 -0.0397 0.0402  8   VAL B CG2 
2601 N N   . LYS B 12  ? 0.5097 0.5639 0.4638 -0.0773 -0.0247 0.0587  9   LYS B N   
2602 C CA  . LYS B 12  ? 0.5229 0.5893 0.4725 -0.0706 -0.0148 0.0600  9   LYS B CA  
2603 C C   . LYS B 12  ? 0.4958 0.5555 0.4370 -0.0580 -0.0120 0.0516  9   LYS B C   
2604 O O   . LYS B 12  ? 0.5055 0.5703 0.4522 -0.0536 -0.0139 0.0487  9   LYS B O   
2605 C CB  . LYS B 12  ? 0.5500 0.6450 0.5127 -0.0732 -0.0102 0.0673  9   LYS B CB  
2606 C CG  . LYS B 12  ? 0.5781 0.6857 0.5346 -0.0668 0.0000  0.0695  9   LYS B CG  
2607 C CD  . LYS B 12  ? 0.6069 0.7455 0.5759 -0.0649 0.0056  0.0748  9   LYS B CD  
2608 C CE  . LYS B 12  ? 0.6481 0.7993 0.6100 -0.0597 0.0155  0.0783  9   LYS B CE  
2609 N NZ  . LYS B 12  ? 0.6876 0.8724 0.6643 -0.0624 0.0208  0.0871  9   LYS B NZ  
2610 N N   . LEU B 13  ? 0.4786 0.5253 0.4064 -0.0528 -0.0085 0.0479  10  LEU B N   
2611 C CA  . LEU B 13  ? 0.4485 0.4867 0.3677 -0.0419 -0.0062 0.0405  10  LEU B CA  
2612 C C   . LEU B 13  ? 0.4509 0.5062 0.3708 -0.0331 0.0009  0.0406  10  LEU B C   
2613 O O   . LEU B 13  ? 0.4545 0.5282 0.3794 -0.0350 0.0053  0.0463  10  LEU B O   
2614 C CB  . LEU B 13  ? 0.4423 0.4614 0.3481 -0.0407 -0.0059 0.0368  10  LEU B CB  
2615 C CG  . LEU B 13  ? 0.4329 0.4364 0.3373 -0.0479 -0.0124 0.0367  10  LEU B CG  
2616 C CD1 . LEU B 13  ? 0.4296 0.4187 0.3221 -0.0466 -0.0116 0.0338  10  LEU B CD1 
2617 C CD2 . LEU B 13  ? 0.4277 0.4228 0.3348 -0.0470 -0.0179 0.0328  10  LEU B CD2 
2618 N N   . ASN B 14  ? 0.4454 0.4945 0.3594 -0.0231 0.0021  0.0346  11  ASN B N   
2619 C CA  . ASN B 14  ? 0.4635 0.5267 0.3768 -0.0124 0.0080  0.0336  11  ASN B CA  
2620 C C   . ASN B 14  ? 0.4775 0.5409 0.3796 -0.0076 0.0142  0.0329  11  ASN B C   
2621 O O   . ASN B 14  ? 0.4948 0.5706 0.3954 0.0021  0.0192  0.0320  11  ASN B O   
2622 C CB  . ASN B 14  ? 0.4604 0.5140 0.3697 -0.0032 0.0064  0.0277  11  ASN B CB  
2623 C CG  . ASN B 14  ? 0.4558 0.4838 0.3512 -0.0008 0.0051  0.0221  11  ASN B CG  
2624 O OD1 . ASN B 14  ? 0.4636 0.4836 0.3496 -0.0006 0.0075  0.0207  11  ASN B OD1 
2625 N ND2 . ASN B 14  ? 0.4467 0.4626 0.3406 0.0014  0.0015  0.0190  11  ASN B ND2 
2626 N N   . ASP B 15  ? 0.4742 0.5250 0.3684 -0.0131 0.0135  0.0332  12  ASP B N   
2627 C CA  . ASP B 15  ? 0.4893 0.5412 0.3723 -0.0094 0.0187  0.0331  12  ASP B CA  
2628 C C   . ASP B 15  ? 0.4994 0.5657 0.3876 -0.0180 0.0209  0.0415  12  ASP B C   
2629 O O   . ASP B 15  ? 0.5025 0.5684 0.3804 -0.0162 0.0245  0.0421  12  ASP B O   
2630 C CB  . ASP B 15  ? 0.4897 0.5171 0.3586 -0.0087 0.0161  0.0272  12  ASP B CB  
2631 C CG  . ASP B 15  ? 0.4858 0.5014 0.3560 -0.0194 0.0109  0.0292  12  ASP B CG  
2632 O OD1 . ASP B 15  ? 0.4825 0.5060 0.3638 -0.0277 0.0085  0.0348  12  ASP B OD1 
2633 O OD2 . ASP B 15  ? 0.4896 0.4880 0.3497 -0.0194 0.0086  0.0250  12  ASP B OD2 
2634 N N   . GLY B 16  ? 0.4917 0.5690 0.3944 -0.0275 0.0181  0.0479  13  GLY B N   
2635 C CA  . GLY B 16  ? 0.5048 0.5974 0.4139 -0.0364 0.0203  0.0574  13  GLY B CA  
2636 C C   . GLY B 16  ? 0.5028 0.5787 0.4092 -0.0472 0.0147  0.0600  13  GLY B C   
2637 O O   . GLY B 16  ? 0.5250 0.6102 0.4381 -0.0566 0.0146  0.0685  13  GLY B O   
2638 N N   . HIS B 17  ? 0.4968 0.5491 0.3934 -0.0458 0.0103  0.0534  14  HIS B N   
2639 C CA  . HIS B 17  ? 0.5020 0.5374 0.3959 -0.0544 0.0042  0.0549  14  HIS B CA  
2640 C C   . HIS B 17  ? 0.4904 0.5218 0.3956 -0.0618 -0.0031 0.0560  14  HIS B C   
2641 O O   . HIS B 17  ? 0.4778 0.5167 0.3914 -0.0592 -0.0039 0.0540  14  HIS B O   
2642 C CB  . HIS B 17  ? 0.5073 0.5221 0.3879 -0.0495 0.0023  0.0473  14  HIS B CB  
2643 C CG  . HIS B 17  ? 0.5312 0.5470 0.3993 -0.0437 0.0075  0.0461  14  HIS B CG  
2644 N ND1 . HIS B 17  ? 0.5400 0.5513 0.3992 -0.0336 0.0102  0.0387  14  HIS B ND1 
2645 C CD2 . HIS B 17  ? 0.5477 0.5676 0.4095 -0.0461 0.0101  0.0513  14  HIS B CD2 
2646 C CE1 . HIS B 17  ? 0.5475 0.5600 0.3951 -0.0299 0.0139  0.0387  14  HIS B CE1 
2647 N NE2 . HIS B 17  ? 0.5603 0.5792 0.4093 -0.0371 0.0143  0.0466  14  HIS B NE2 
2648 N N   . PHE B 18  ? 0.4996 0.5181 0.4035 -0.0697 -0.0089 0.0585  15  PHE B N   
2649 C CA  . PHE B 18  ? 0.4948 0.5071 0.4072 -0.0777 -0.0170 0.0603  15  PHE B CA  
2650 C C   . PHE B 18  ? 0.4809 0.4709 0.3857 -0.0761 -0.0231 0.0540  15  PHE B C   
2651 O O   . PHE B 18  ? 0.4725 0.4517 0.3672 -0.0749 -0.0229 0.0529  15  PHE B O   
2652 C CB  . PHE B 18  ? 0.5290 0.5464 0.4469 -0.0888 -0.0190 0.0701  15  PHE B CB  
2653 C CG  . PHE B 18  ? 0.5580 0.6010 0.4869 -0.0914 -0.0134 0.0771  15  PHE B CG  
2654 C CD1 . PHE B 18  ? 0.5648 0.6195 0.5078 -0.0946 -0.0164 0.0781  15  PHE B CD1 
2655 C CD2 . PHE B 18  ? 0.5939 0.6509 0.5189 -0.0896 -0.0049 0.0822  15  PHE B CD2 
2656 C CE1 . PHE B 18  ? 0.5917 0.6732 0.5465 -0.0968 -0.0111 0.0848  15  PHE B CE1 
2657 C CE2 . PHE B 18  ? 0.6128 0.6964 0.5484 -0.0910 0.0010  0.0890  15  PHE B CE2 
2658 C CZ  . PHE B 18  ? 0.6046 0.7013 0.5560 -0.0946 -0.0020 0.0903  15  PHE B CZ  
2659 N N   . MET B 19  ? 0.4555 0.4404 0.3651 -0.0755 -0.0284 0.0500  16  MET B N   
2660 C CA  . MET B 19  ? 0.4408 0.4073 0.3443 -0.0731 -0.0340 0.0441  16  MET B CA  
2661 C C   . MET B 19  ? 0.4291 0.3879 0.3373 -0.0797 -0.0428 0.0457  16  MET B C   
2662 O O   . MET B 19  ? 0.4332 0.3997 0.3504 -0.0820 -0.0455 0.0466  16  MET B O   
2663 C CB  . MET B 19  ? 0.4349 0.4012 0.3374 -0.0647 -0.0322 0.0373  16  MET B CB  
2664 C CG  . MET B 19  ? 0.4425 0.3936 0.3401 -0.0620 -0.0371 0.0320  16  MET B CG  
2665 S SD  . MET B 19  ? 0.4553 0.4073 0.3533 -0.0538 -0.0358 0.0261  16  MET B SD  
2666 C CE  . MET B 19  ? 0.4347 0.3846 0.3245 -0.0485 -0.0288 0.0236  16  MET B CE  
2667 N N   . PRO B 20  ? 0.4313 0.3743 0.3333 -0.0825 -0.0484 0.0459  17  PRO B N   
2668 C CA  . PRO B 20  ? 0.4389 0.3707 0.3432 -0.0870 -0.0580 0.0458  17  PRO B CA  
2669 C C   . PRO B 20  ? 0.4245 0.3529 0.3295 -0.0809 -0.0614 0.0385  17  PRO B C   
2670 O O   . PRO B 20  ? 0.4019 0.3284 0.3016 -0.0731 -0.0580 0.0332  17  PRO B O   
2671 C CB  . PRO B 20  ? 0.4489 0.3635 0.3434 -0.0871 -0.0620 0.0454  17  PRO B CB  
2672 C CG  . PRO B 20  ? 0.4465 0.3672 0.3366 -0.0869 -0.0547 0.0491  17  PRO B CG  
2673 C CD  . PRO B 20  ? 0.4284 0.3630 0.3206 -0.0808 -0.0466 0.0460  17  PRO B CD  
2674 N N   . VAL B 21  ? 0.4325 0.3606 0.3438 -0.0847 -0.0682 0.0386  18  VAL B N   
2675 C CA  . VAL B 21  ? 0.4304 0.3581 0.3424 -0.0786 -0.0711 0.0322  18  VAL B CA  
2676 C C   . VAL B 21  ? 0.4298 0.3397 0.3321 -0.0730 -0.0770 0.0261  18  VAL B C   
2677 O O   . VAL B 21  ? 0.4297 0.3397 0.3297 -0.0656 -0.0771 0.0206  18  VAL B O   
2678 C CB  . VAL B 21  ? 0.4555 0.3909 0.3778 -0.0842 -0.0768 0.0342  18  VAL B CB  
2679 C CG1 . VAL B 21  ? 0.4629 0.4200 0.3957 -0.0878 -0.0698 0.0400  18  VAL B CG1 
2680 C CG2 . VAL B 21  ? 0.4814 0.4037 0.4043 -0.0928 -0.0875 0.0363  18  VAL B CG2 
2681 N N   . LEU B 22  ? 0.4434 0.3393 0.3397 -0.0756 -0.0816 0.0271  19  LEU B N   
2682 C CA  . LEU B 22  ? 0.4517 0.3328 0.3379 -0.0683 -0.0856 0.0212  19  LEU B CA  
2683 C C   . LEU B 22  ? 0.4542 0.3347 0.3347 -0.0646 -0.0796 0.0213  19  LEU B C   
2684 O O   . LEU B 22  ? 0.4812 0.3601 0.3609 -0.0697 -0.0785 0.0263  19  LEU B O   
2685 C CB  . LEU B 22  ? 0.4779 0.3417 0.3603 -0.0721 -0.0966 0.0213  19  LEU B CB  
2686 C CG  . LEU B 22  ? 0.4824 0.3309 0.3537 -0.0636 -0.1012 0.0154  19  LEU B CG  
2687 C CD1 . LEU B 22  ? 0.4824 0.3318 0.3506 -0.0543 -0.1023 0.0081  19  LEU B CD1 
2688 C CD2 . LEU B 22  ? 0.5201 0.3494 0.3864 -0.0679 -0.1121 0.0165  19  LEU B CD2 
2689 N N   . GLY B 23  ? 0.4381 0.3196 0.3145 -0.0563 -0.0762 0.0162  20  GLY B N   
2690 C CA  . GLY B 23  ? 0.4246 0.3066 0.2967 -0.0531 -0.0711 0.0159  20  GLY B CA  
2691 C C   . GLY B 23  ? 0.4242 0.2969 0.2893 -0.0461 -0.0751 0.0113  20  GLY B C   
2692 O O   . GLY B 23  ? 0.4047 0.2740 0.2676 -0.0407 -0.0787 0.0069  20  GLY B O   
2693 N N   . PHE B 24  ? 0.4141 0.2844 0.2754 -0.0451 -0.0740 0.0120  21  PHE B N   
2694 C CA  . PHE B 24  ? 0.4177 0.2820 0.2731 -0.0376 -0.0772 0.0079  21  PHE B CA  
2695 C C   . PHE B 24  ? 0.4014 0.2766 0.2584 -0.0325 -0.0704 0.0053  21  PHE B C   
2696 O O   . PHE B 24  ? 0.3851 0.2675 0.2444 -0.0352 -0.0646 0.0072  21  PHE B O   
2697 C CB  . PHE B 24  ? 0.4299 0.2860 0.2806 -0.0387 -0.0808 0.0101  21  PHE B CB  
2698 C CG  . PHE B 24  ? 0.4381 0.2887 0.2830 -0.0301 -0.0849 0.0058  21  PHE B CG  
2699 C CD1 . PHE B 24  ? 0.4521 0.2932 0.2924 -0.0243 -0.0916 0.0018  21  PHE B CD1 
2700 C CD2 . PHE B 24  ? 0.4253 0.2812 0.2692 -0.0268 -0.0823 0.0054  21  PHE B CD2 
2701 C CE1 . PHE B 24  ? 0.4575 0.2952 0.2921 -0.0147 -0.0950 -0.0024 21  PHE B CE1 
2702 C CE2 . PHE B 24  ? 0.4335 0.2879 0.2735 -0.0180 -0.0855 0.0015  21  PHE B CE2 
2703 C CZ  . PHE B 24  ? 0.4488 0.2938 0.2837 -0.0115 -0.0919 -0.0022 21  PHE B CZ  
2704 N N   . GLY B 25  ? 0.3989 0.2752 0.2542 -0.0254 -0.0712 0.0012  22  GLY B N   
2705 C CA  . GLY B 25  ? 0.3958 0.2827 0.2530 -0.0212 -0.0650 -0.0002 22  GLY B CA  
2706 C C   . GLY B 25  ? 0.3975 0.2859 0.2528 -0.0170 -0.0658 -0.0014 22  GLY B C   
2707 O O   . GLY B 25  ? 0.4188 0.3008 0.2693 -0.0113 -0.0715 -0.0039 22  GLY B O   
2708 N N   . THR B 26  ? 0.3803 0.2766 0.2390 -0.0193 -0.0610 0.0000  23  THR B N   
2709 C CA  . THR B 26  ? 0.3827 0.2817 0.2407 -0.0164 -0.0626 -0.0007 23  THR B CA  
2710 C C   . THR B 26  ? 0.3844 0.2956 0.2460 -0.0115 -0.0589 -0.0022 23  THR B C   
2711 O O   . THR B 26  ? 0.3970 0.3130 0.2592 -0.0079 -0.0606 -0.0031 23  THR B O   
2712 C CB  . THR B 26  ? 0.3698 0.2690 0.2284 -0.0221 -0.0617 0.0017  23  THR B CB  
2713 O OG1 . THR B 26  ? 0.3597 0.2657 0.2224 -0.0268 -0.0556 0.0028  23  THR B OG1 
2714 C CG2 . THR B 26  ? 0.3744 0.2631 0.2291 -0.0267 -0.0651 0.0043  23  THR B CG2 
2715 N N   . TYR B 27  ? 0.3848 0.3019 0.2490 -0.0112 -0.0542 -0.0020 24  TYR B N   
2716 C CA  . TYR B 27  ? 0.3881 0.3183 0.2564 -0.0079 -0.0499 -0.0020 24  TYR B CA  
2717 C C   . TYR B 27  ? 0.4092 0.3423 0.2744 0.0019  -0.0532 -0.0047 24  TYR B C   
2718 O O   . TYR B 27  ? 0.4258 0.3518 0.2851 0.0071  -0.0562 -0.0070 24  TYR B O   
2719 C CB  . TYR B 27  ? 0.3861 0.3211 0.2563 -0.0086 -0.0443 -0.0005 24  TYR B CB  
2720 C CG  . TYR B 27  ? 0.3881 0.3373 0.2631 -0.0063 -0.0398 0.0009  24  TYR B CG  
2721 C CD1 . TYR B 27  ? 0.3910 0.3473 0.2725 -0.0125 -0.0369 0.0033  24  TYR B CD1 
2722 C CD2 . TYR B 27  ? 0.3952 0.3512 0.2679 0.0020  -0.0389 0.0000  24  TYR B CD2 
2723 C CE1 . TYR B 27  ? 0.4019 0.3727 0.2894 -0.0118 -0.0330 0.0056  24  TYR B CE1 
2724 C CE2 . TYR B 27  ? 0.4097 0.3814 0.2876 0.0040  -0.0342 0.0024  24  TYR B CE2 
2725 C CZ  . TYR B 27  ? 0.4179 0.3974 0.3040 -0.0038 -0.0311 0.0056  24  TYR B CZ  
2726 O OH  . TYR B 27  ? 0.4560 0.4524 0.3490 -0.0034 -0.0266 0.0089  24  TYR B OH  
2727 N N   . ALA B 28  ? 0.4172 0.3618 0.2863 0.0050  -0.0524 -0.0047 25  ALA B N   
2728 C CA  . ALA B 28  ? 0.4338 0.3865 0.3010 0.0159  -0.0534 -0.0070 25  ALA B CA  
2729 C C   . ALA B 28  ? 0.4390 0.4119 0.3150 0.0156  -0.0472 -0.0043 25  ALA B C   
2730 O O   . ALA B 28  ? 0.4207 0.3986 0.3038 0.0071  -0.0448 -0.0016 25  ALA B O   
2731 C CB  . ALA B 28  ? 0.4473 0.3940 0.3100 0.0219  -0.0605 -0.0098 25  ALA B CB  
2732 N N   . PRO B 29  ? 0.4599 0.4443 0.3353 0.0243  -0.0444 -0.0048 26  PRO B N   
2733 C CA  . PRO B 29  ? 0.4918 0.4974 0.3763 0.0234  -0.0378 -0.0010 26  PRO B CA  
2734 C C   . PRO B 29  ? 0.5187 0.5364 0.4119 0.0216  -0.0393 -0.0003 26  PRO B C   
2735 O O   . PRO B 29  ? 0.5149 0.5270 0.4047 0.0263  -0.0455 -0.0035 26  PRO B O   
2736 C CB  . PRO B 29  ? 0.5010 0.5169 0.3811 0.0358  -0.0356 -0.0022 26  PRO B CB  
2737 C CG  . PRO B 29  ? 0.5093 0.5055 0.3765 0.0420  -0.0411 -0.0071 26  PRO B CG  
2738 C CD  . PRO B 29  ? 0.4916 0.4693 0.3569 0.0352  -0.0475 -0.0088 26  PRO B CD  
2739 N N   . PRO B 30  ? 0.5600 0.5946 0.4644 0.0150  -0.0342 0.0042  27  PRO B N   
2740 C CA  . PRO B 30  ? 0.5827 0.6309 0.4966 0.0126  -0.0361 0.0050  27  PRO B CA  
2741 C C   . PRO B 30  ? 0.5941 0.6538 0.5074 0.0257  -0.0394 0.0020  27  PRO B C   
2742 O O   . PRO B 30  ? 0.6030 0.6671 0.5205 0.0254  -0.0437 0.0009  27  PRO B O   
2743 C CB  . PRO B 30  ? 0.5979 0.6648 0.5241 0.0046  -0.0295 0.0109  27  PRO B CB  
2744 C CG  . PRO B 30  ? 0.6038 0.6588 0.5252 -0.0007 -0.0251 0.0133  27  PRO B CG  
2745 C CD  . PRO B 30  ? 0.5798 0.6215 0.4883 0.0095  -0.0269 0.0092  27  PRO B CD  
2746 N N   . GLU B 31  ? 0.6097 0.6737 0.5169 0.0376  -0.0377 0.0003  28  GLU B N   
2747 C CA  . GLU B 31  ? 0.6240 0.6995 0.5295 0.0523  -0.0406 -0.0031 28  GLU B CA  
2748 C C   . GLU B 31  ? 0.6025 0.6573 0.4983 0.0568  -0.0500 -0.0083 28  GLU B C   
2749 O O   . GLU B 31  ? 0.6338 0.6969 0.5303 0.0661  -0.0540 -0.0106 28  GLU B O   
2750 C CB  . GLU B 31  ? 0.6519 0.7332 0.5499 0.0649  -0.0371 -0.0045 28  GLU B CB  
2751 C CG  . GLU B 31  ? 0.6668 0.7725 0.5741 0.0625  -0.0272 0.0017  28  GLU B CG  
2752 C CD  . GLU B 31  ? 0.6662 0.7660 0.5771 0.0478  -0.0221 0.0071  28  GLU B CD  
2753 O OE1 . GLU B 31  ? 0.6348 0.7109 0.5367 0.0440  -0.0248 0.0049  28  GLU B OE1 
2754 O OE2 . GLU B 31  ? 0.6713 0.7902 0.5943 0.0400  -0.0157 0.0137  28  GLU B OE2 
2755 N N   . VAL B 32  ? 0.5528 0.5822 0.4403 0.0505  -0.0535 -0.0096 29  VAL B N   
2756 C CA  . VAL B 32  ? 0.5281 0.5350 0.4051 0.0535  -0.0623 -0.0134 29  VAL B CA  
2757 C C   . VAL B 32  ? 0.5112 0.5189 0.3939 0.0462  -0.0654 -0.0118 29  VAL B C   
2758 O O   . VAL B 32  ? 0.4956 0.5045 0.3846 0.0341  -0.0624 -0.0086 29  VAL B O   
2759 C CB  . VAL B 32  ? 0.5162 0.4993 0.3841 0.0484  -0.0640 -0.0142 29  VAL B CB  
2760 C CG1 . VAL B 32  ? 0.5193 0.4794 0.3780 0.0479  -0.0725 -0.0162 29  VAL B CG1 
2761 C CG2 . VAL B 32  ? 0.5176 0.4991 0.3784 0.0569  -0.0625 -0.0166 29  VAL B CG2 
2762 N N   . PRO B 33  ? 0.5244 0.5317 0.4043 0.0543  -0.0717 -0.0141 30  PRO B N   
2763 C CA  . PRO B 33  ? 0.5181 0.5265 0.4023 0.0482  -0.0753 -0.0126 30  PRO B CA  
2764 C C   . PRO B 33  ? 0.4980 0.4858 0.3771 0.0363  -0.0767 -0.0110 30  PRO B C   
2765 O O   . PRO B 33  ? 0.4802 0.4485 0.3497 0.0365  -0.0789 -0.0119 30  PRO B O   
2766 C CB  . PRO B 33  ? 0.5492 0.5517 0.4255 0.0611  -0.0833 -0.0160 30  PRO B CB  
2767 C CG  . PRO B 33  ? 0.5696 0.5821 0.4440 0.0750  -0.0816 -0.0189 30  PRO B CG  
2768 C CD  . PRO B 33  ? 0.5455 0.5496 0.4165 0.0704  -0.0767 -0.0185 30  PRO B CD  
2769 N N   . ARG B 34  ? 0.4932 0.4867 0.3790 0.0266  -0.0758 -0.0087 31  ARG B N   
2770 C CA  . ARG B 34  ? 0.4873 0.4644 0.3685 0.0157  -0.0762 -0.0070 31  ARG B CA  
2771 C C   . ARG B 34  ? 0.4919 0.4487 0.3610 0.0189  -0.0832 -0.0076 31  ARG B C   
2772 O O   . ARG B 34  ? 0.4853 0.4260 0.3483 0.0122  -0.0830 -0.0060 31  ARG B O   
2773 C CB  . ARG B 34  ? 0.4979 0.4861 0.3876 0.0068  -0.0749 -0.0054 31  ARG B CB  
2774 C CG  . ARG B 34  ? 0.4984 0.5050 0.4003 0.0019  -0.0685 -0.0039 31  ARG B CG  
2775 C CD  . ARG B 34  ? 0.4821 0.4813 0.3826 -0.0032 -0.0626 -0.0025 31  ARG B CD  
2776 N NE  . ARG B 34  ? 0.4866 0.4873 0.3848 0.0047  -0.0600 -0.0032 31  ARG B NE  
2777 C CZ  . ARG B 34  ? 0.4755 0.4696 0.3713 0.0022  -0.0556 -0.0022 31  ARG B CZ  
2778 N NH1 . ARG B 34  ? 0.4626 0.4480 0.3581 -0.0075 -0.0534 -0.0007 31  ARG B NH1 
2779 N NH2 . ARG B 34  ? 0.4730 0.4681 0.3654 0.0101  -0.0539 -0.0032 31  ARG B NH2 
2780 N N   . SER B 35  ? 0.5059 0.4631 0.3714 0.0290  -0.0892 -0.0094 32  SER B N   
2781 C CA  . SER B 35  ? 0.5279 0.4639 0.3807 0.0329  -0.0967 -0.0093 32  SER B CA  
2782 C C   . SER B 35  ? 0.5281 0.4442 0.3723 0.0325  -0.0974 -0.0095 32  SER B C   
2783 O O   . SER B 35  ? 0.5343 0.4307 0.3694 0.0290  -0.1018 -0.0074 32  SER B O   
2784 C CB  . SER B 35  ? 0.5538 0.4940 0.4041 0.0460  -0.1028 -0.0118 32  SER B CB  
2785 O OG  . SER B 35  ? 0.5666 0.5175 0.4197 0.0559  -0.1008 -0.0149 32  SER B OG  
2786 N N   . LYS B 36  ? 0.5246 0.4459 0.3714 0.0358  -0.0937 -0.0116 33  LYS B N   
2787 C CA  . LYS B 36  ? 0.5461 0.4495 0.3848 0.0367  -0.0957 -0.0128 33  LYS B CA  
2788 C C   . LYS B 36  ? 0.5146 0.4083 0.3534 0.0236  -0.0928 -0.0092 33  LYS B C   
2789 O O   . LYS B 36  ? 0.5189 0.3940 0.3500 0.0214  -0.0975 -0.0081 33  LYS B O   
2790 C CB  . LYS B 36  ? 0.5820 0.4957 0.4228 0.0445  -0.0923 -0.0161 33  LYS B CB  
2791 C CG  . LYS B 36  ? 0.6347 0.5469 0.4687 0.0600  -0.0980 -0.0205 33  LYS B CG  
2792 C CD  . LYS B 36  ? 0.6830 0.5678 0.5035 0.0631  -0.1064 -0.0225 33  LYS B CD  
2793 C CE  . LYS B 36  ? 0.7355 0.6144 0.5466 0.0797  -0.1134 -0.0278 33  LYS B CE  
2794 N NZ  . LYS B 36  ? 0.7670 0.6162 0.5646 0.0810  -0.1222 -0.0298 33  LYS B NZ  
2795 N N   . ALA B 37  ? 0.4813 0.3872 0.3285 0.0152  -0.0859 -0.0072 34  ALA B N   
2796 C CA  . ALA B 37  ? 0.4704 0.3688 0.3174 0.0042  -0.0829 -0.0040 34  ALA B CA  
2797 C C   . ALA B 37  ? 0.4756 0.3599 0.3155 0.0002  -0.0877 -0.0009 34  ALA B C   
2798 O O   . ALA B 37  ? 0.4726 0.3454 0.3091 -0.0059 -0.0880 0.0016  34  ALA B O   
2799 C CB  . ALA B 37  ? 0.4460 0.3585 0.3016 -0.0025 -0.0759 -0.0028 34  ALA B CB  
2800 N N   . LEU B 38  ? 0.4830 0.3694 0.3210 0.0033  -0.0912 -0.0007 35  LEU B N   
2801 C CA  . LEU B 38  ? 0.5031 0.3758 0.3327 0.0004  -0.0959 0.0029  35  LEU B CA  
2802 C C   . LEU B 38  ? 0.5207 0.3740 0.3415 0.0039  -0.1027 0.0033  35  LEU B C   
2803 O O   . LEU B 38  ? 0.5443 0.3845 0.3606 -0.0031 -0.1037 0.0075  35  LEU B O   
2804 C CB  . LEU B 38  ? 0.5088 0.3887 0.3378 0.0045  -0.0990 0.0025  35  LEU B CB  
2805 C CG  . LEU B 38  ? 0.5292 0.3942 0.3476 0.0044  -0.1052 0.0062  35  LEU B CG  
2806 C CD1 . LEU B 38  ? 0.5228 0.3800 0.3374 -0.0060 -0.1021 0.0112  35  LEU B CD1 
2807 C CD2 . LEU B 38  ? 0.5423 0.4164 0.3605 0.0092  -0.1084 0.0054  35  LEU B CD2 
2808 N N   . GLU B 39  ? 0.5353 0.3868 0.3538 0.0145  -0.1070 -0.0007 36  GLU B N   
2809 C CA  . GLU B 39  ? 0.5703 0.4004 0.3787 0.0191  -0.1152 -0.0013 36  GLU B CA  
2810 C C   . GLU B 39  ? 0.5481 0.3683 0.3564 0.0119  -0.1143 -0.0002 36  GLU B C   
2811 O O   . GLU B 39  ? 0.5588 0.3603 0.3606 0.0063  -0.1194 0.0037  36  GLU B O   
2812 C CB  . GLU B 39  ? 0.6099 0.4429 0.4161 0.0335  -0.1190 -0.0071 36  GLU B CB  
2813 C CG  . GLU B 39  ? 0.6638 0.4729 0.4583 0.0394  -0.1281 -0.0090 36  GLU B CG  
2814 C CD  . GLU B 39  ? 0.7176 0.5313 0.5097 0.0546  -0.1305 -0.0159 36  GLU B CD  
2815 O OE1 . GLU B 39  ? 0.7756 0.5815 0.5643 0.0573  -0.1321 -0.0195 36  GLU B OE1 
2816 O OE2 . GLU B 39  ? 0.7579 0.5848 0.5518 0.0639  -0.1305 -0.0178 36  GLU B OE2 
2817 N N   . VAL B 40  ? 0.5099 0.3421 0.3253 0.0119  -0.1086 -0.0031 37  VAL B N   
2818 C CA  . VAL B 40  ? 0.5133 0.3376 0.3287 0.0074  -0.1088 -0.0033 37  VAL B CA  
2819 C C   . VAL B 40  ? 0.4986 0.3233 0.3182 -0.0058 -0.1045 0.0023  37  VAL B C   
2820 O O   . VAL B 40  ? 0.5032 0.3163 0.3212 -0.0113 -0.1076 0.0041  37  VAL B O   
2821 C CB  . VAL B 40  ? 0.5013 0.3382 0.3213 0.0130  -0.1043 -0.0081 37  VAL B CB  
2822 C CG1 . VAL B 40  ? 0.5240 0.3627 0.3394 0.0271  -0.1080 -0.0134 37  VAL B CG1 
2823 C CG2 . VAL B 40  ? 0.4740 0.3310 0.3042 0.0077  -0.0944 -0.0065 37  VAL B CG2 
2824 N N   . THR B 41  ? 0.4745 0.3116 0.2990 -0.0105 -0.0982 0.0049  38  THR B N   
2825 C CA  . THR B 41  ? 0.4703 0.3090 0.2978 -0.0214 -0.0937 0.0100  38  THR B CA  
2826 C C   . THR B 41  ? 0.4942 0.3170 0.3146 -0.0262 -0.0993 0.0154  38  THR B C   
2827 O O   . THR B 41  ? 0.5016 0.3203 0.3233 -0.0342 -0.0987 0.0196  38  THR B O   
2828 C CB  . THR B 41  ? 0.4558 0.3102 0.2884 -0.0237 -0.0863 0.0103  38  THR B CB  
2829 O OG1 . THR B 41  ? 0.4321 0.2991 0.2714 -0.0204 -0.0816 0.0063  38  THR B OG1 
2830 C CG2 . THR B 41  ? 0.4542 0.3104 0.2883 -0.0329 -0.0816 0.0149  38  THR B CG2 
2831 N N   . LYS B 42  ? 0.5134 0.3284 0.3266 -0.0215 -0.1046 0.0160  39  LYS B N   
2832 C CA  . LYS B 42  ? 0.5448 0.3420 0.3497 -0.0255 -0.1110 0.0218  39  LYS B CA  
2833 C C   . LYS B 42  ? 0.5628 0.3429 0.3646 -0.0262 -0.1181 0.0213  39  LYS B C   
2834 O O   . LYS B 42  ? 0.5745 0.3449 0.3752 -0.0355 -0.1200 0.0275  39  LYS B O   
2835 C CB  . LYS B 42  ? 0.5653 0.3570 0.3624 -0.0179 -0.1161 0.0215  39  LYS B CB  
2836 C CG  . LYS B 42  ? 0.5635 0.3682 0.3615 -0.0191 -0.1112 0.0233  39  LYS B CG  
2837 C CD  . LYS B 42  ? 0.6001 0.3947 0.3884 -0.0136 -0.1180 0.0253  39  LYS B CD  
2838 C CE  . LYS B 42  ? 0.6175 0.4185 0.4065 -0.0013 -0.1212 0.0186  39  LYS B CE  
2839 N NZ  . LYS B 42  ? 0.6610 0.4518 0.4399 0.0052  -0.1287 0.0204  39  LYS B NZ  
2840 N N   . LEU B 43  ? 0.5695 0.3462 0.3697 -0.0167 -0.1221 0.0144  40  LEU B N   
2841 C CA  . LEU B 43  ? 0.5918 0.3515 0.3882 -0.0164 -0.1298 0.0123  40  LEU B CA  
2842 C C   . LEU B 43  ? 0.5759 0.3411 0.3804 -0.0269 -0.1259 0.0147  40  LEU B C   
2843 O O   . LEU B 43  ? 0.6019 0.3514 0.4040 -0.0332 -0.1326 0.0174  40  LEU B O   
2844 C CB  . LEU B 43  ? 0.5982 0.3584 0.3918 -0.0030 -0.1327 0.0036  40  LEU B CB  
2845 C CG  . LEU B 43  ? 0.6253 0.3782 0.4100 0.0096  -0.1386 0.0003  40  LEU B CG  
2846 C CD1 . LEU B 43  ? 0.6268 0.3836 0.4095 0.0231  -0.1402 -0.0083 40  LEU B CD1 
2847 C CD2 . LEU B 43  ? 0.6670 0.3920 0.4397 0.0091  -0.1498 0.0034  40  LEU B CD2 
2848 N N   . ALA B 44  ? 0.5349 0.3206 0.3485 -0.0280 -0.1165 0.0133  41  ALA B N   
2849 C CA  . ALA B 44  ? 0.5158 0.3091 0.3375 -0.0364 -0.1123 0.0153  41  ALA B CA  
2850 C C   . ALA B 44  ? 0.5277 0.3177 0.3508 -0.0484 -0.1118 0.0240  41  ALA B C   
2851 O O   . ALA B 44  ? 0.5335 0.3168 0.3591 -0.0561 -0.1157 0.0271  41  ALA B O   
2852 C CB  . ALA B 44  ? 0.4828 0.2967 0.3121 -0.0345 -0.1026 0.0126  41  ALA B CB  
2853 N N   . ILE B 45  ? 0.5240 0.3188 0.3453 -0.0501 -0.1078 0.0283  42  ILE B N   
2854 C CA  . ILE B 45  ? 0.5392 0.3338 0.3611 -0.0607 -0.1058 0.0374  42  ILE B CA  
2855 C C   . ILE B 45  ? 0.5872 0.3602 0.4029 -0.0653 -0.1158 0.0419  42  ILE B C   
2856 O O   . ILE B 45  ? 0.5968 0.3684 0.4166 -0.0758 -0.1163 0.0484  42  ILE B O   
2857 C CB  . ILE B 45  ? 0.5288 0.3324 0.3477 -0.0596 -0.1000 0.0399  42  ILE B CB  
2858 C CG1 . ILE B 45  ? 0.5018 0.3249 0.3278 -0.0571 -0.0910 0.0355  42  ILE B CG1 
2859 C CG2 . ILE B 45  ? 0.5458 0.3478 0.3624 -0.0690 -0.0985 0.0497  42  ILE B CG2 
2860 C CD1 . ILE B 45  ? 0.4922 0.3234 0.3150 -0.0539 -0.0867 0.0351  42  ILE B CD1 
2861 N N   . GLU B 46  ? 0.6261 0.3825 0.4324 -0.0575 -0.1238 0.0386  43  GLU B N   
2862 C CA  . GLU B 46  ? 0.6748 0.4065 0.4732 -0.0613 -0.1346 0.0428  43  GLU B CA  
2863 C C   . GLU B 46  ? 0.6843 0.4080 0.4869 -0.0664 -0.1404 0.0411  43  GLU B C   
2864 O O   . GLU B 46  ? 0.7104 0.4200 0.5117 -0.0764 -0.1464 0.0481  43  GLU B O   
2865 C CB  . GLU B 46  ? 0.7229 0.4388 0.5096 -0.0493 -0.1422 0.0380  43  GLU B CB  
2866 C CG  . GLU B 46  ? 0.7363 0.4556 0.5177 -0.0474 -0.1392 0.0424  43  GLU B CG  
2867 C CD  . GLU B 46  ? 0.7705 0.4863 0.5442 -0.0332 -0.1429 0.0364  43  GLU B CD  
2868 O OE1 . GLU B 46  ? 0.7988 0.5055 0.5690 -0.0238 -0.1492 0.0290  43  GLU B OE1 
2869 O OE2 . GLU B 46  ? 0.7734 0.4962 0.5441 -0.0311 -0.1398 0.0390  43  GLU B OE2 
2870 N N   . ALA B 47  ? 0.6479 0.3799 0.4549 -0.0599 -0.1390 0.0327  44  ALA B N   
2871 C CA  . ALA B 47  ? 0.6582 0.3837 0.4687 -0.0637 -0.1450 0.0299  44  ALA B CA  
2872 C C   . ALA B 47  ? 0.6470 0.3875 0.4699 -0.0769 -0.1392 0.0367  44  ALA B C   
2873 O O   . ALA B 47  ? 0.6662 0.3992 0.4926 -0.0841 -0.1458 0.0378  44  ALA B O   
2874 C CB  . ALA B 47  ? 0.6370 0.3682 0.4470 -0.0519 -0.1445 0.0195  44  ALA B CB  
2875 N N   . GLY B 48  ? 0.6195 0.3810 0.4488 -0.0794 -0.1278 0.0406  45  GLY B N   
2876 C CA  . GLY B 48  ? 0.6108 0.3883 0.4514 -0.0907 -0.1216 0.0475  45  GLY B CA  
2877 C C   . GLY B 48  ? 0.5655 0.3664 0.4142 -0.0868 -0.1113 0.0436  45  GLY B C   
2878 O O   . GLY B 48  ? 0.5566 0.3725 0.4149 -0.0943 -0.1059 0.0482  45  GLY B O   
2879 N N   . PHE B 49  ? 0.5392 0.3441 0.3844 -0.0758 -0.1080 0.0361  46  PHE B N   
2880 C CA  . PHE B 49  ? 0.5021 0.3275 0.3537 -0.0724 -0.0978 0.0333  46  PHE B CA  
2881 C C   . PHE B 49  ? 0.4967 0.3332 0.3491 -0.0761 -0.0896 0.0391  46  PHE B C   
2882 O O   . PHE B 49  ? 0.4990 0.3282 0.3440 -0.0750 -0.0909 0.0413  46  PHE B O   
2883 C CB  . PHE B 49  ? 0.4842 0.3111 0.3320 -0.0609 -0.0963 0.0252  46  PHE B CB  
2884 C CG  . PHE B 49  ? 0.4882 0.3102 0.3354 -0.0553 -0.1014 0.0186  46  PHE B CG  
2885 C CD1 . PHE B 49  ? 0.5122 0.3165 0.3514 -0.0505 -0.1110 0.0151  46  PHE B CD1 
2886 C CD2 . PHE B 49  ? 0.4687 0.3033 0.3218 -0.0533 -0.0966 0.0155  46  PHE B CD2 
2887 C CE1 . PHE B 49  ? 0.5154 0.3152 0.3523 -0.0440 -0.1157 0.0085  46  PHE B CE1 
2888 C CE2 . PHE B 49  ? 0.4753 0.3058 0.3265 -0.0473 -0.1011 0.0096  46  PHE B CE2 
2889 C CZ  . PHE B 49  ? 0.5060 0.3193 0.3488 -0.0426 -0.1107 0.0059  46  PHE B CZ  
2890 N N   . ARG B 50  ? 0.4840 0.3374 0.3441 -0.0791 -0.0819 0.0410  47  ARG B N   
2891 C CA  . ARG B 50  ? 0.4894 0.3551 0.3496 -0.0814 -0.0735 0.0456  47  ARG B CA  
2892 C C   . ARG B 50  ? 0.4618 0.3406 0.3242 -0.0753 -0.0657 0.0404  47  ARG B C   
2893 O O   . ARG B 50  ? 0.4677 0.3517 0.3263 -0.0736 -0.0605 0.0411  47  ARG B O   
2894 C CB  . ARG B 50  ? 0.5090 0.3822 0.3755 -0.0913 -0.0719 0.0541  47  ARG B CB  
2895 C CG  . ARG B 50  ? 0.5429 0.4012 0.4054 -0.0984 -0.0793 0.0608  47  ARG B CG  
2896 C CD  . ARG B 50  ? 0.5596 0.4118 0.4119 -0.0974 -0.0783 0.0646  47  ARG B CD  
2897 N NE  . ARG B 50  ? 0.5903 0.4259 0.4381 -0.1043 -0.0861 0.0716  47  ARG B NE  
2898 C CZ  . ARG B 50  ? 0.6092 0.4237 0.4500 -0.1015 -0.0959 0.0687  47  ARG B CZ  
2899 N NH1 . ARG B 50  ? 0.5898 0.3990 0.4280 -0.0916 -0.0989 0.0589  47  ARG B NH1 
2900 N NH2 . ARG B 50  ? 0.6468 0.4453 0.4829 -0.1085 -0.1029 0.0761  47  ARG B NH2 
2901 N N   . HIS B 51  ? 0.4454 0.3273 0.3125 -0.0718 -0.0659 0.0354  48  HIS B N   
2902 C CA  . HIS B 51  ? 0.4173 0.3090 0.2862 -0.0660 -0.0594 0.0305  48  HIS B CA  
2903 C C   . HIS B 51  ? 0.4040 0.2887 0.2681 -0.0591 -0.0618 0.0247  48  HIS B C   
2904 O O   . HIS B 51  ? 0.4071 0.2836 0.2701 -0.0567 -0.0678 0.0220  48  HIS B O   
2905 C CB  . HIS B 51  ? 0.4234 0.3225 0.3000 -0.0668 -0.0588 0.0298  48  HIS B CB  
2906 C CG  . HIS B 51  ? 0.4027 0.3092 0.2808 -0.0609 -0.0536 0.0253  48  HIS B CG  
2907 N ND1 . HIS B 51  ? 0.3967 0.3114 0.2809 -0.0605 -0.0521 0.0249  48  HIS B ND1 
2908 C CD2 . HIS B 51  ? 0.3870 0.2934 0.2613 -0.0555 -0.0501 0.0214  48  HIS B CD2 
2909 C CE1 . HIS B 51  ? 0.3829 0.3009 0.2659 -0.0548 -0.0476 0.0212  48  HIS B CE1 
2910 N NE2 . HIS B 51  ? 0.3816 0.2945 0.2590 -0.0522 -0.0464 0.0192  48  HIS B NE2 
2911 N N   A ILE B 52  ? 0.3878 0.2759 0.2488 -0.0560 -0.0576 0.0230  49  ILE B N   
2912 N N   B ILE B 52  ? 0.3884 0.2766 0.2494 -0.0561 -0.0575 0.0231  49  ILE B N   
2913 C CA  A ILE B 52  ? 0.3810 0.2660 0.2390 -0.0500 -0.0592 0.0183  49  ILE B CA  
2914 C CA  B ILE B 52  ? 0.3853 0.2704 0.2433 -0.0501 -0.0590 0.0184  49  ILE B CA  
2915 C C   A ILE B 52  ? 0.3624 0.2558 0.2229 -0.0471 -0.0532 0.0151  49  ILE B C   
2916 C C   B ILE B 52  ? 0.3640 0.2576 0.2247 -0.0471 -0.0531 0.0152  49  ILE B C   
2917 O O   A ILE B 52  ? 0.3584 0.2569 0.2185 -0.0488 -0.0485 0.0162  49  ILE B O   
2918 O O   B ILE B 52  ? 0.3613 0.2600 0.2215 -0.0487 -0.0483 0.0161  49  ILE B O   
2919 C CB  A ILE B 52  ? 0.3892 0.2692 0.2414 -0.0497 -0.0617 0.0196  49  ILE B CB  
2920 C CB  B ILE B 52  ? 0.3965 0.2770 0.2486 -0.0501 -0.0612 0.0199  49  ILE B CB  
2921 C CG1 A ILE B 52  ? 0.4075 0.2756 0.2559 -0.0517 -0.0689 0.0225  49  ILE B CG1 
2922 C CG1 B ILE B 52  ? 0.4173 0.2884 0.2660 -0.0544 -0.0664 0.0248  49  ILE B CG1 
2923 C CG2 A ILE B 52  ? 0.3835 0.2657 0.2348 -0.0439 -0.0618 0.0151  49  ILE B CG2 
2924 C CG2 B ILE B 52  ? 0.3972 0.2766 0.2477 -0.0438 -0.0636 0.0154  49  ILE B CG2 
2925 C CD1 A ILE B 52  ? 0.4194 0.2816 0.2610 -0.0518 -0.0716 0.0251  49  ILE B CD1 
2926 C CD1 B ILE B 52  ? 0.4263 0.2858 0.2735 -0.0525 -0.0742 0.0234  49  ILE B CD1 
2927 N N   . ASP B 53  ? 0.3531 0.2473 0.2153 -0.0426 -0.0537 0.0116  50  ASP B N   
2928 C CA  . ASP B 53  ? 0.3456 0.2465 0.2104 -0.0404 -0.0484 0.0094  50  ASP B CA  
2929 C C   . ASP B 53  ? 0.3464 0.2493 0.2106 -0.0374 -0.0482 0.0072  50  ASP B C   
2930 O O   . ASP B 53  ? 0.3482 0.2504 0.2120 -0.0331 -0.0512 0.0054  50  ASP B O   
2931 C CB  . ASP B 53  ? 0.3443 0.2467 0.2116 -0.0379 -0.0481 0.0082  50  ASP B CB  
2932 C CG  . ASP B 53  ? 0.3380 0.2457 0.2070 -0.0362 -0.0425 0.0072  50  ASP B CG  
2933 O OD1 . ASP B 53  ? 0.3422 0.2524 0.2122 -0.0380 -0.0389 0.0085  50  ASP B OD1 
2934 O OD2 . ASP B 53  ? 0.3291 0.2385 0.1980 -0.0327 -0.0418 0.0056  50  ASP B OD2 
2935 N N   . SER B 54  ? 0.3545 0.2606 0.2186 -0.0393 -0.0448 0.0071  51  SER B N   
2936 C CA  . SER B 54  ? 0.3559 0.2662 0.2215 -0.0381 -0.0442 0.0054  51  SER B CA  
2937 C C   . SER B 54  ? 0.3521 0.2649 0.2193 -0.0401 -0.0395 0.0050  51  SER B C   
2938 O O   . SER B 54  ? 0.3408 0.2522 0.2077 -0.0406 -0.0365 0.0056  51  SER B O   
2939 C CB  . SER B 54  ? 0.3706 0.2797 0.2334 -0.0390 -0.0475 0.0055  51  SER B CB  
2940 O OG  . SER B 54  ? 0.3717 0.2865 0.2372 -0.0380 -0.0482 0.0039  51  SER B OG  
2941 N N   . ALA B 55  ? 0.3476 0.2638 0.2167 -0.0411 -0.0394 0.0040  52  ALA B N   
2942 C CA  . ALA B 55  ? 0.3516 0.2685 0.2224 -0.0437 -0.0362 0.0036  52  ALA B CA  
2943 C C   . ALA B 55  ? 0.3536 0.2752 0.2275 -0.0460 -0.0383 0.0027  52  ALA B C   
2944 O O   . ALA B 55  ? 0.3589 0.2864 0.2356 -0.0438 -0.0409 0.0027  52  ALA B O   
2945 C CB  . ALA B 55  ? 0.3500 0.2690 0.2237 -0.0418 -0.0332 0.0047  52  ALA B CB  
2946 N N   . HIS B 56  ? 0.3614 0.2805 0.2351 -0.0500 -0.0375 0.0019  53  HIS B N   
2947 C CA  . HIS B 56  ? 0.3684 0.2927 0.2467 -0.0535 -0.0398 0.0014  53  HIS B CA  
2948 C C   . HIS B 56  ? 0.3745 0.3096 0.2610 -0.0525 -0.0384 0.0035  53  HIS B C   
2949 O O   . HIS B 56  ? 0.3817 0.3264 0.2733 -0.0522 -0.0411 0.0035  53  HIS B O   
2950 C CB  . HIS B 56  ? 0.3823 0.2994 0.2585 -0.0584 -0.0395 0.0002  53  HIS B CB  
2951 C CG  . HIS B 56  ? 0.3949 0.3172 0.2770 -0.0636 -0.0426 -0.0002 53  HIS B CG  
2952 N ND1 . HIS B 56  ? 0.4067 0.3322 0.2884 -0.0644 -0.0475 -0.0023 53  HIS B ND1 
2953 C CD2 . HIS B 56  ? 0.4110 0.3365 0.2998 -0.0685 -0.0420 0.0017  53  HIS B CD2 
2954 C CE1 . HIS B 56  ? 0.4211 0.3527 0.3099 -0.0697 -0.0502 -0.0022 53  HIS B CE1 
2955 N NE2 . HIS B 56  ? 0.4283 0.3598 0.3219 -0.0730 -0.0468 0.0005  53  HIS B NE2 
2956 N N   . LEU B 57  ? 0.3783 0.3128 0.2654 -0.0509 -0.0344 0.0055  54  LEU B N   
2957 C CA  . LEU B 57  ? 0.3804 0.3257 0.2740 -0.0495 -0.0320 0.0082  54  LEU B CA  
2958 C C   . LEU B 57  ? 0.3681 0.3225 0.2635 -0.0434 -0.0341 0.0074  54  LEU B C   
2959 O O   . LEU B 57  ? 0.3647 0.3315 0.2664 -0.0423 -0.0329 0.0091  54  LEU B O   
2960 C CB  . LEU B 57  ? 0.3912 0.3324 0.2822 -0.0474 -0.0277 0.0102  54  LEU B CB  
2961 C CG  . LEU B 57  ? 0.4089 0.3607 0.3051 -0.0461 -0.0242 0.0138  54  LEU B CG  
2962 C CD1 . LEU B 57  ? 0.4231 0.3787 0.3256 -0.0539 -0.0232 0.0167  54  LEU B CD1 
2963 C CD2 . LEU B 57  ? 0.4146 0.3619 0.3062 -0.0422 -0.0207 0.0154  54  LEU B CD2 
2964 N N   . TYR B 58  ? 0.3625 0.3110 0.2524 -0.0395 -0.0370 0.0053  55  TYR B N   
2965 C CA  . TYR B 58  ? 0.3645 0.3175 0.2537 -0.0323 -0.0395 0.0043  55  TYR B CA  
2966 C C   . TYR B 58  ? 0.3736 0.3351 0.2666 -0.0314 -0.0433 0.0034  55  TYR B C   
2967 O O   . TYR B 58  ? 0.3717 0.3381 0.2645 -0.0244 -0.0455 0.0024  55  TYR B O   
2968 C CB  . TYR B 58  ? 0.3621 0.3035 0.2440 -0.0298 -0.0423 0.0030  55  TYR B CB  
2969 C CG  . TYR B 58  ? 0.3495 0.2845 0.2285 -0.0298 -0.0396 0.0036  55  TYR B CG  
2970 C CD1 . TYR B 58  ? 0.3547 0.2927 0.2358 -0.0305 -0.0350 0.0051  55  TYR B CD1 
2971 C CD2 . TYR B 58  ? 0.3562 0.2822 0.2303 -0.0294 -0.0419 0.0031  55  TYR B CD2 
2972 C CE1 . TYR B 58  ? 0.3501 0.2826 0.2282 -0.0295 -0.0332 0.0056  55  TYR B CE1 
2973 C CE2 . TYR B 58  ? 0.3477 0.2694 0.2202 -0.0295 -0.0400 0.0037  55  TYR B CE2 
2974 C CZ  . TYR B 58  ? 0.3503 0.2755 0.2246 -0.0289 -0.0358 0.0046  55  TYR B CZ  
2975 O OH  . TYR B 58  ? 0.3649 0.2865 0.2375 -0.0283 -0.0344 0.0050  55  TYR B OH  
2976 N N   . ASN B 59  ? 0.3723 0.3349 0.2679 -0.0375 -0.0446 0.0033  56  ASN B N   
2977 C CA  . ASN B 59  ? 0.3866 0.3580 0.2861 -0.0368 -0.0490 0.0023  56  ASN B CA  
2978 C C   . ASN B 59  ? 0.3855 0.3508 0.2781 -0.0302 -0.0535 0.0007  56  ASN B C   
2979 O O   . ASN B 59  ? 0.3979 0.3720 0.2929 -0.0241 -0.0561 0.0000  56  ASN B O   
2980 C CB  . ASN B 59  ? 0.3972 0.3872 0.3070 -0.0352 -0.0475 0.0039  56  ASN B CB  
2981 C CG  . ASN B 59  ? 0.4121 0.4134 0.3274 -0.0349 -0.0523 0.0029  56  ASN B CG  
2982 O OD1 . ASN B 59  ? 0.4107 0.4061 0.3235 -0.0393 -0.0561 0.0015  56  ASN B OD1 
2983 N ND2 . ASN B 59  ? 0.4191 0.4371 0.3413 -0.0291 -0.0522 0.0036  56  ASN B ND2 
2984 N N   . ASN B 60  ? 0.3773 0.3283 0.2615 -0.0312 -0.0543 0.0004  57  ASN B N   
2985 C CA  . ASN B 60  ? 0.3863 0.3296 0.2636 -0.0265 -0.0592 -0.0001 57  ASN B CA  
2986 C C   . ASN B 60  ? 0.3862 0.3182 0.2562 -0.0308 -0.0606 0.0006  57  ASN B C   
2987 O O   . ASN B 60  ? 0.3817 0.3053 0.2452 -0.0283 -0.0640 0.0014  57  ASN B O   
2988 C CB  . ASN B 60  ? 0.3867 0.3249 0.2609 -0.0208 -0.0593 -0.0003 57  ASN B CB  
2989 C CG  . ASN B 60  ? 0.3745 0.3038 0.2458 -0.0243 -0.0562 0.0007  57  ASN B CG  
2990 O OD1 . ASN B 60  ? 0.3738 0.3003 0.2445 -0.0301 -0.0538 0.0016  57  ASN B OD1 
2991 N ND2 . ASN B 60  ? 0.3703 0.2960 0.2397 -0.0202 -0.0563 0.0002  57  ASN B ND2 
2992 N N   . GLU B 61  ? 0.3836 0.3146 0.2534 -0.0367 -0.0579 0.0006  58  GLU B N   
2993 C CA  . GLU B 61  ? 0.3954 0.3167 0.2571 -0.0394 -0.0581 0.0016  58  GLU B CA  
2994 C C   . GLU B 61  ? 0.4021 0.3219 0.2586 -0.0379 -0.0634 0.0017  58  GLU B C   
2995 O O   . GLU B 61  ? 0.4006 0.3123 0.2493 -0.0384 -0.0643 0.0038  58  GLU B O   
2996 C CB  . GLU B 61  ? 0.3946 0.3143 0.2553 -0.0443 -0.0546 0.0008  58  GLU B CB  
2997 C CG  . GLU B 61  ? 0.3913 0.3093 0.2542 -0.0450 -0.0495 0.0014  58  GLU B CG  
2998 C CD  . GLU B 61  ? 0.3972 0.3111 0.2573 -0.0483 -0.0462 0.0005  58  GLU B CD  
2999 O OE1 . GLU B 61  ? 0.4042 0.3197 0.2670 -0.0508 -0.0462 -0.0011 58  GLU B OE1 
3000 O OE2 . GLU B 61  ? 0.3991 0.3084 0.2543 -0.0480 -0.0440 0.0015  58  GLU B OE2 
3001 N N   . GLU B 62  ? 0.4222 0.3504 0.2829 -0.0363 -0.0669 0.0001  59  GLU B N   
3002 C CA  . GLU B 62  ? 0.4424 0.3697 0.2979 -0.0337 -0.0728 0.0001  59  GLU B CA  
3003 C C   . GLU B 62  ? 0.4408 0.3602 0.2908 -0.0284 -0.0759 0.0022  59  GLU B C   
3004 O O   . GLU B 62  ? 0.4437 0.3538 0.2846 -0.0284 -0.0784 0.0046  59  GLU B O   
3005 C CB  . GLU B 62  ? 0.4693 0.4098 0.3326 -0.0320 -0.0763 -0.0020 59  GLU B CB  
3006 C CG  . GLU B 62  ? 0.4968 0.4368 0.3544 -0.0284 -0.0830 -0.0021 59  GLU B CG  
3007 C CD  . GLU B 62  ? 0.5323 0.4875 0.3983 -0.0259 -0.0874 -0.0041 59  GLU B CD  
3008 O OE1 . GLU B 62  ? 0.5375 0.5053 0.4149 -0.0284 -0.0851 -0.0051 59  GLU B OE1 
3009 O OE2 . GLU B 62  ? 0.5701 0.5252 0.4314 -0.0215 -0.0933 -0.0042 59  GLU B OE2 
3010 N N   . GLN B 63  ? 0.4275 0.3492 0.2820 -0.0242 -0.0756 0.0016  60  GLN B N   
3011 C CA  . GLN B 63  ? 0.4435 0.3563 0.2928 -0.0183 -0.0797 0.0026  60  GLN B CA  
3012 C C   . GLN B 63  ? 0.4373 0.3367 0.2807 -0.0219 -0.0782 0.0054  60  GLN B C   
3013 O O   . GLN B 63  ? 0.4473 0.3353 0.2832 -0.0203 -0.0828 0.0077  60  GLN B O   
3014 C CB  . GLN B 63  ? 0.4460 0.3667 0.3013 -0.0116 -0.0798 0.0001  60  GLN B CB  
3015 C CG  . GLN B 63  ? 0.4550 0.3906 0.3164 -0.0073 -0.0821 -0.0018 60  GLN B CG  
3016 C CD  . GLN B 63  ? 0.4366 0.3874 0.3084 -0.0126 -0.0775 -0.0025 60  GLN B CD  
3017 O OE1 . GLN B 63  ? 0.4265 0.3764 0.3008 -0.0183 -0.0723 -0.0019 60  GLN B OE1 
3018 N NE2 . GLN B 63  ? 0.4494 0.4144 0.3278 -0.0105 -0.0801 -0.0035 60  GLN B NE2 
3019 N N   . VAL B 64  ? 0.4111 0.3121 0.2584 -0.0262 -0.0726 0.0055  61  VAL B N   
3020 C CA  . VAL B 64  ? 0.4016 0.2930 0.2453 -0.0300 -0.0711 0.0083  61  VAL B CA  
3021 C C   . VAL B 64  ? 0.4098 0.2963 0.2469 -0.0345 -0.0711 0.0119  61  VAL B C   
3022 O O   . VAL B 64  ? 0.4101 0.2872 0.2419 -0.0364 -0.0733 0.0158  61  VAL B O   
3023 C CB  . VAL B 64  ? 0.3852 0.2812 0.2346 -0.0326 -0.0653 0.0074  61  VAL B CB  
3024 C CG1 . VAL B 64  ? 0.3764 0.2657 0.2238 -0.0368 -0.0639 0.0104  61  VAL B CG1 
3025 C CG2 . VAL B 64  ? 0.3848 0.2857 0.2391 -0.0275 -0.0653 0.0046  61  VAL B CG2 
3026 N N   . GLY B 65  ? 0.4083 0.3010 0.2451 -0.0364 -0.0690 0.0108  62  GLY B N   
3027 C CA  . GLY B 65  ? 0.4172 0.3068 0.2463 -0.0396 -0.0683 0.0137  62  GLY B CA  
3028 C C   . GLY B 65  ? 0.4338 0.3161 0.2551 -0.0374 -0.0742 0.0167  62  GLY B C   
3029 O O   . GLY B 65  ? 0.4390 0.3145 0.2535 -0.0401 -0.0741 0.0217  62  GLY B O   
3030 N N   . LEU B 66  ? 0.4395 0.3237 0.2620 -0.0322 -0.0791 0.0141  63  LEU B N   
3031 C CA  . LEU B 66  ? 0.4676 0.3444 0.2823 -0.0283 -0.0858 0.0164  63  LEU B CA  
3032 C C   . LEU B 66  ? 0.4728 0.3363 0.2837 -0.0283 -0.0884 0.0203  63  LEU B C   
3033 O O   . LEU B 66  ? 0.4802 0.3334 0.2818 -0.0293 -0.0917 0.0253  63  LEU B O   
3034 C CB  . LEU B 66  ? 0.4852 0.3706 0.3055 -0.0219 -0.0896 0.0118  63  LEU B CB  
3035 C CG  . LEU B 66  ? 0.5175 0.4018 0.3323 -0.0162 -0.0965 0.0119  63  LEU B CG  
3036 C CD1 . LEU B 66  ? 0.5410 0.4212 0.3456 -0.0191 -0.0975 0.0151  63  LEU B CD1 
3037 C CD2 . LEU B 66  ? 0.5141 0.4149 0.3388 -0.0126 -0.0975 0.0069  63  LEU B CD2 
3038 N N   . ALA B 67  ? 0.4638 0.3265 0.2807 -0.0277 -0.0874 0.0184  64  ALA B N   
3039 C CA  . ALA B 67  ? 0.4784 0.3269 0.2916 -0.0284 -0.0910 0.0215  64  ALA B CA  
3040 C C   . ALA B 67  ? 0.4850 0.3292 0.2952 -0.0370 -0.0878 0.0279  64  ALA B C   
3041 O O   . ALA B 67  ? 0.4975 0.3292 0.3007 -0.0391 -0.0920 0.0332  64  ALA B O   
3042 C CB  . ALA B 67  ? 0.4718 0.3214 0.2916 -0.0265 -0.0903 0.0178  64  ALA B CB  
3043 N N   . ILE B 68  ? 0.4721 0.3268 0.2869 -0.0414 -0.0806 0.0276  65  ILE B N   
3044 C CA  . ILE B 68  ? 0.4844 0.3395 0.2974 -0.0486 -0.0761 0.0335  65  ILE B CA  
3045 C C   . ILE B 68  ? 0.5102 0.3619 0.3131 -0.0495 -0.0773 0.0385  65  ILE B C   
3046 O O   . ILE B 68  ? 0.5266 0.3710 0.3250 -0.0543 -0.0782 0.0458  65  ILE B O   
3047 C CB  . ILE B 68  ? 0.4610 0.3283 0.2804 -0.0508 -0.0684 0.0311  65  ILE B CB  
3048 C CG1 . ILE B 68  ? 0.4435 0.3121 0.2714 -0.0501 -0.0680 0.0277  65  ILE B CG1 
3049 C CG2 . ILE B 68  ? 0.4670 0.3378 0.2838 -0.0563 -0.0634 0.0370  65  ILE B CG2 
3050 C CD1 . ILE B 68  ? 0.4243 0.3034 0.2583 -0.0506 -0.0614 0.0245  65  ILE B CD1 
3051 N N   . ARG B 69  ? 0.5288 0.3858 0.3285 -0.0456 -0.0775 0.0351  66  ARG B N   
3052 C CA  . ARG B 69  ? 0.5660 0.4206 0.3547 -0.0454 -0.0789 0.0392  66  ARG B CA  
3053 C C   . ARG B 69  ? 0.5699 0.4102 0.3514 -0.0441 -0.0861 0.0441  66  ARG B C   
3054 O O   . ARG B 69  ? 0.5947 0.4295 0.3676 -0.0472 -0.0862 0.0512  66  ARG B O   
3055 C CB  . ARG B 69  ? 0.5886 0.4508 0.3760 -0.0407 -0.0800 0.0333  66  ARG B CB  
3056 C CG  . ARG B 69  ? 0.6175 0.4895 0.4052 -0.0427 -0.0737 0.0307  66  ARG B CG  
3057 C CD  . ARG B 69  ? 0.6742 0.5491 0.4545 -0.0395 -0.0767 0.0278  66  ARG B CD  
3058 N NE  . ARG B 69  ? 0.7020 0.5812 0.4887 -0.0356 -0.0816 0.0217  66  ARG B NE  
3059 C CZ  . ARG B 69  ? 0.7344 0.6145 0.5163 -0.0317 -0.0877 0.0201  66  ARG B CZ  
3060 N NH1 . ARG B 69  ? 0.7098 0.5972 0.5001 -0.0287 -0.0915 0.0148  66  ARG B NH1 
3061 N NH2 . ARG B 69  ? 0.7728 0.6478 0.5418 -0.0306 -0.0899 0.0242  66  ARG B NH2 
3062 N N   . SER B 70  ? 0.5609 0.3955 0.3457 -0.0392 -0.0918 0.0404  67  SER B N   
3063 C CA  . SER B 70  ? 0.5933 0.4118 0.3707 -0.0361 -0.1000 0.0436  67  SER B CA  
3064 C C   . SER B 70  ? 0.6003 0.4062 0.3755 -0.0434 -0.1008 0.0511  67  SER B C   
3065 O O   . SER B 70  ? 0.6182 0.4118 0.3834 -0.0452 -0.1047 0.0583  67  SER B O   
3066 C CB  . SER B 70  ? 0.5967 0.4144 0.3783 -0.0278 -0.1051 0.0368  67  SER B CB  
3067 O OG  . SER B 70  ? 0.6547 0.4578 0.4271 -0.0222 -0.1135 0.0388  67  SER B OG  
3068 N N   . LYS B 71  ? 0.5801 0.3901 0.3643 -0.0483 -0.0968 0.0503  68  LYS B N   
3069 C CA  . LYS B 71  ? 0.5997 0.3995 0.3843 -0.0564 -0.0981 0.0572  68  LYS B CA  
3070 C C   . LYS B 71  ? 0.6014 0.4070 0.3831 -0.0645 -0.0922 0.0660  68  LYS B C   
3071 O O   . LYS B 71  ? 0.6396 0.4357 0.4191 -0.0717 -0.0944 0.0743  68  LYS B O   
3072 C CB  . LYS B 71  ? 0.5847 0.3880 0.3800 -0.0579 -0.0969 0.0526  68  LYS B CB  
3073 C CG  . LYS B 71  ? 0.5951 0.3900 0.3907 -0.0498 -0.1036 0.0454  68  LYS B CG  
3074 C CD  . LYS B 71  ? 0.6358 0.4091 0.4216 -0.0470 -0.1137 0.0478  68  LYS B CD  
3075 C CE  . LYS B 71  ? 0.6724 0.4313 0.4565 -0.0566 -0.1175 0.0555  68  LYS B CE  
3076 N NZ  . LYS B 71  ? 0.7183 0.4529 0.4911 -0.0536 -0.1283 0.0579  68  LYS B NZ  
3077 N N   . ILE B 72  ? 0.5788 0.3997 0.3607 -0.0634 -0.0850 0.0644  69  ILE B N   
3078 C CA  . ILE B 72  ? 0.5889 0.4166 0.3657 -0.0688 -0.0790 0.0724  69  ILE B CA  
3079 C C   . ILE B 72  ? 0.6164 0.4339 0.3793 -0.0668 -0.0835 0.0779  69  ILE B C   
3080 O O   . ILE B 72  ? 0.6495 0.4607 0.4065 -0.0732 -0.0835 0.0885  69  ILE B O   
3081 C CB  . ILE B 72  ? 0.5666 0.4122 0.3464 -0.0669 -0.0706 0.0676  69  ILE B CB  
3082 C CG1 . ILE B 72  ? 0.5469 0.4015 0.3396 -0.0687 -0.0663 0.0633  69  ILE B CG1 
3083 C CG2 . ILE B 72  ? 0.5865 0.4390 0.3582 -0.0700 -0.0648 0.0753  69  ILE B CG2 
3084 C CD1 . ILE B 72  ? 0.5292 0.3968 0.3249 -0.0646 -0.0604 0.0558  69  ILE B CD1 
3085 N N   . ALA B 73  ? 0.6167 0.4322 0.3746 -0.0584 -0.0878 0.0718  70  ALA B N   
3086 C CA  . ALA B 73  ? 0.6558 0.4626 0.3996 -0.0551 -0.0924 0.0764  70  ALA B CA  
3087 C C   . ALA B 73  ? 0.6961 0.4821 0.4342 -0.0569 -0.1005 0.0831  70  ALA B C   
3088 O O   . ALA B 73  ? 0.7315 0.5083 0.4572 -0.0582 -0.1027 0.0918  70  ALA B O   
3089 C CB  . ALA B 73  ? 0.6475 0.4593 0.3891 -0.0460 -0.0956 0.0680  70  ALA B CB  
3090 N N   . ASP B 74  ? 0.7042 0.4811 0.4495 -0.0568 -0.1052 0.0797  71  ASP B N   
3091 C CA  . ASP B 74  ? 0.7520 0.5056 0.4908 -0.0579 -0.1144 0.0849  71  ASP B CA  
3092 C C   . ASP B 74  ? 0.7588 0.5065 0.4985 -0.0705 -0.1125 0.0960  71  ASP B C   
3093 O O   . ASP B 74  ? 0.7898 0.5164 0.5230 -0.0733 -0.1203 0.1020  71  ASP B O   
3094 C CB  . ASP B 74  ? 0.7658 0.5108 0.5092 -0.0507 -0.1214 0.0760  71  ASP B CB  
3095 C CG  . ASP B 74  ? 0.7735 0.5191 0.5282 -0.0552 -0.1205 0.0727  71  ASP B CG  
3096 O OD1 . ASP B 74  ? 0.7798 0.5284 0.5394 -0.0656 -0.1163 0.0788  71  ASP B OD1 
3097 O OD2 . ASP B 74  ? 0.8077 0.5501 0.5656 -0.0477 -0.1248 0.0643  71  ASP B OD2 
3098 N N   . GLY B 75  ? 0.7440 0.5095 0.4903 -0.0775 -0.1028 0.0994  72  GLY B N   
3099 C CA  . GLY B 75  ? 0.7629 0.5286 0.5123 -0.0901 -0.0996 0.1106  72  GLY B CA  
3100 C C   . GLY B 75  ? 0.7600 0.5247 0.5227 -0.0957 -0.1012 0.1079  72  GLY B C   
3101 O O   . GLY B 75  ? 0.7686 0.5333 0.5362 -0.1068 -0.1001 0.1168  72  GLY B O   
3102 N N   . SER B 76  ? 0.7431 0.5076 0.5118 -0.0885 -0.1040 0.0963  73  SER B N   
3103 C CA  . SER B 76  ? 0.7506 0.5123 0.5302 -0.0925 -0.1069 0.0929  73  SER B CA  
3104 C C   . SER B 76  ? 0.7266 0.5104 0.5187 -0.0993 -0.0973 0.0944  73  SER B C   
3105 O O   . SER B 76  ? 0.7506 0.5330 0.5501 -0.1084 -0.0988 0.0991  73  SER B O   
3106 C CB  . SER B 76  ? 0.7276 0.4852 0.5091 -0.0821 -0.1115 0.0806  73  SER B CB  
3107 O OG  . SER B 76  ? 0.7601 0.4955 0.5311 -0.0764 -0.1218 0.0798  73  SER B OG  
3108 N N   . VAL B 77  ? 0.6991 0.5021 0.4931 -0.0947 -0.0884 0.0904  74  VAL B N   
3109 C CA  . VAL B 77  ? 0.6801 0.5045 0.4851 -0.0984 -0.0792 0.0901  74  VAL B CA  
3110 C C   . VAL B 77  ? 0.6661 0.5057 0.4658 -0.0958 -0.0703 0.0920  74  VAL B C   
3111 O O   . VAL B 77  ? 0.6570 0.4916 0.4463 -0.0894 -0.0719 0.0898  74  VAL B O   
3112 C CB  . VAL B 77  ? 0.6502 0.4808 0.4639 -0.0925 -0.0785 0.0789  74  VAL B CB  
3113 C CG1 . VAL B 77  ? 0.6628 0.4809 0.4817 -0.0950 -0.0865 0.0768  74  VAL B CG1 
3114 C CG2 . VAL B 77  ? 0.6370 0.4677 0.4456 -0.0818 -0.0787 0.0698  74  VAL B CG2 
3115 N N   . LYS B 78  ? 0.6643 0.5221 0.4708 -0.0997 -0.0619 0.0950  75  LYS B N   
3116 C CA  . LYS B 78  ? 0.6750 0.5482 0.4764 -0.0953 -0.0531 0.0944  75  LYS B CA  
3117 C C   . LYS B 78  ? 0.6233 0.5061 0.4313 -0.0888 -0.0497 0.0833  75  LYS B C   
3118 O O   . LYS B 78  ? 0.5841 0.4652 0.4022 -0.0895 -0.0524 0.0787  75  LYS B O   
3119 C CB  . LYS B 78  ? 0.7316 0.6183 0.5332 -0.1023 -0.0460 0.1058  75  LYS B CB  
3120 C CG  . LYS B 78  ? 0.7615 0.6632 0.5776 -0.1087 -0.0414 0.1089  75  LYS B CG  
3121 C CD  . LYS B 78  ? 0.8035 0.7170 0.6203 -0.1176 -0.0360 0.1230  75  LYS B CD  
3122 C CE  . LYS B 78  ? 0.8190 0.7558 0.6497 -0.1215 -0.0285 0.1260  75  LYS B CE  
3123 N NZ  . LYS B 78  ? 0.8295 0.7637 0.6752 -0.1294 -0.0342 0.1265  75  LYS B NZ  
3124 N N   . ARG B 79  ? 0.5951 0.4852 0.3965 -0.0822 -0.0451 0.0788  76  ARG B N   
3125 C CA  . ARG B 79  ? 0.5685 0.4660 0.3745 -0.0762 -0.0419 0.0687  76  ARG B CA  
3126 C C   . ARG B 79  ? 0.5613 0.4706 0.3790 -0.0793 -0.0370 0.0694  76  ARG B C   
3127 O O   . ARG B 79  ? 0.5400 0.4496 0.3649 -0.0766 -0.0378 0.0624  76  ARG B O   
3128 C CB  . ARG B 79  ? 0.5589 0.4627 0.3553 -0.0700 -0.0375 0.0649  76  ARG B CB  
3129 C CG  . ARG B 79  ? 0.5304 0.4402 0.3311 -0.0649 -0.0344 0.0555  76  ARG B CG  
3130 C CD  . ARG B 79  ? 0.5136 0.4148 0.3191 -0.0624 -0.0403 0.0479  76  ARG B CD  
3131 N NE  . ARG B 79  ? 0.4858 0.3917 0.2964 -0.0588 -0.0375 0.0402  76  ARG B NE  
3132 C CZ  . ARG B 79  ? 0.4663 0.3765 0.2865 -0.0597 -0.0353 0.0389  76  ARG B CZ  
3133 N NH1 . ARG B 79  ? 0.4615 0.3728 0.2885 -0.0643 -0.0358 0.0440  76  ARG B NH1 
3134 N NH2 . ARG B 79  ? 0.4479 0.3604 0.2709 -0.0561 -0.0331 0.0324  76  ARG B NH2 
3135 N N   . GLU B 80  ? 0.5925 0.5126 0.4123 -0.0845 -0.0321 0.0780  77  GLU B N   
3136 C CA  . GLU B 80  ? 0.6043 0.5397 0.4355 -0.0861 -0.0266 0.0785  77  GLU B CA  
3137 C C   . GLU B 80  ? 0.5934 0.5236 0.4363 -0.0921 -0.0324 0.0794  77  GLU B C   
3138 O O   . GLU B 80  ? 0.5742 0.5154 0.4273 -0.0925 -0.0296 0.0778  77  GLU B O   
3139 C CB  . GLU B 80  ? 0.6623 0.6146 0.4931 -0.0892 -0.0189 0.0877  77  GLU B CB  
3140 C CG  . GLU B 80  ? 0.7059 0.6635 0.5234 -0.0820 -0.0133 0.0861  77  GLU B CG  
3141 C CD  . GLU B 80  ? 0.7754 0.7264 0.5813 -0.0850 -0.0148 0.0941  77  GLU B CD  
3142 O OE1 . GLU B 80  ? 0.8555 0.8194 0.6569 -0.0859 -0.0082 0.1019  77  GLU B OE1 
3143 O OE2 . GLU B 80  ? 0.8019 0.7355 0.6031 -0.0858 -0.0225 0.0928  77  GLU B OE2 
3144 N N   . ASP B 81  ? 0.5865 0.5000 0.4271 -0.0958 -0.0406 0.0813  78  ASP B N   
3145 C CA  . ASP B 81  ? 0.5766 0.4815 0.4259 -0.1002 -0.0477 0.0803  78  ASP B CA  
3146 C C   . ASP B 81  ? 0.5398 0.4391 0.3905 -0.0926 -0.0505 0.0691  78  ASP B C   
3147 O O   . ASP B 81  ? 0.5415 0.4373 0.3994 -0.0944 -0.0549 0.0669  78  ASP B O   
3148 C CB  . ASP B 81  ? 0.6073 0.4932 0.4516 -0.1054 -0.0566 0.0853  78  ASP B CB  
3149 C CG  . ASP B 81  ? 0.6574 0.5452 0.5009 -0.1152 -0.0557 0.0980  78  ASP B CG  
3150 O OD1 . ASP B 81  ? 0.6617 0.5669 0.5144 -0.1206 -0.0500 0.1035  78  ASP B OD1 
3151 O OD2 . ASP B 81  ? 0.6956 0.5675 0.5293 -0.1170 -0.0610 0.1028  78  ASP B OD2 
3152 N N   . ILE B 82  ? 0.5084 0.4057 0.3520 -0.0849 -0.0489 0.0628  79  ILE B N   
3153 C CA  . ILE B 82  ? 0.4854 0.3782 0.3304 -0.0782 -0.0512 0.0532  79  ILE B CA  
3154 C C   . ILE B 82  ? 0.4619 0.3678 0.3116 -0.0744 -0.0444 0.0486  79  ILE B C   
3155 O O   . ILE B 82  ? 0.4759 0.3908 0.3222 -0.0727 -0.0381 0.0494  79  ILE B O   
3156 C CB  . ILE B 82  ? 0.4748 0.3588 0.3110 -0.0728 -0.0543 0.0492  79  ILE B CB  
3157 C CG1 . ILE B 82  ? 0.4983 0.3674 0.3292 -0.0748 -0.0621 0.0530  79  ILE B CG1 
3158 C CG2 . ILE B 82  ? 0.4588 0.3424 0.2977 -0.0664 -0.0551 0.0405  79  ILE B CG2 
3159 C CD1 . ILE B 82  ? 0.5005 0.3594 0.3350 -0.0741 -0.0690 0.0498  79  ILE B CD1 
3160 N N   . PHE B 83  ? 0.4397 0.3454 0.2957 -0.0722 -0.0458 0.0436  80  PHE B N   
3161 C CA  . PHE B 83  ? 0.4159 0.3314 0.2759 -0.0680 -0.0402 0.0391  80  PHE B CA  
3162 C C   . PHE B 83  ? 0.4065 0.3157 0.2642 -0.0624 -0.0419 0.0320  80  PHE B C   
3163 O O   . PHE B 83  ? 0.4064 0.3098 0.2669 -0.0614 -0.0465 0.0295  80  PHE B O   
3164 C CB  . PHE B 83  ? 0.4159 0.3377 0.2854 -0.0702 -0.0403 0.0399  80  PHE B CB  
3165 C CG  . PHE B 83  ? 0.3935 0.3248 0.2661 -0.0654 -0.0347 0.0362  80  PHE B CG  
3166 C CD1 . PHE B 83  ? 0.3717 0.2988 0.2438 -0.0601 -0.0351 0.0299  80  PHE B CD1 
3167 C CD2 . PHE B 83  ? 0.3936 0.3385 0.2694 -0.0659 -0.0289 0.0396  80  PHE B CD2 
3168 C CE1 . PHE B 83  ? 0.3645 0.2984 0.2386 -0.0558 -0.0304 0.0271  80  PHE B CE1 
3169 C CE2 . PHE B 83  ? 0.3810 0.3333 0.2586 -0.0604 -0.0243 0.0359  80  PHE B CE2 
3170 C CZ  . PHE B 83  ? 0.3658 0.3114 0.2424 -0.0556 -0.0254 0.0299  80  PHE B CZ  
3171 N N   . TYR B 84  ? 0.3988 0.3086 0.2510 -0.0591 -0.0392 0.0291  81  TYR B N   
3172 C CA  . TYR B 84  ? 0.3874 0.2930 0.2383 -0.0549 -0.0408 0.0233  81  TYR B CA  
3173 C C   . TYR B 84  ? 0.3696 0.2799 0.2227 -0.0520 -0.0361 0.0194  81  TYR B C   
3174 O O   . TYR B 84  ? 0.3618 0.2766 0.2122 -0.0512 -0.0317 0.0195  81  TYR B O   
3175 C CB  . TYR B 84  ? 0.4004 0.3028 0.2439 -0.0541 -0.0422 0.0228  81  TYR B CB  
3176 C CG  . TYR B 84  ? 0.3996 0.3004 0.2436 -0.0508 -0.0441 0.0175  81  TYR B CG  
3177 C CD1 . TYR B 84  ? 0.4085 0.3059 0.2552 -0.0489 -0.0485 0.0160  81  TYR B CD1 
3178 C CD2 . TYR B 84  ? 0.4124 0.3155 0.2543 -0.0495 -0.0415 0.0141  81  TYR B CD2 
3179 C CE1 . TYR B 84  ? 0.4078 0.3070 0.2563 -0.0462 -0.0496 0.0120  81  TYR B CE1 
3180 C CE2 . TYR B 84  ? 0.4050 0.3081 0.2491 -0.0480 -0.0432 0.0101  81  TYR B CE2 
3181 C CZ  . TYR B 84  ? 0.3993 0.3020 0.2475 -0.0465 -0.0468 0.0095  81  TYR B CZ  
3182 O OH  . TYR B 84  ? 0.4128 0.3184 0.2641 -0.0452 -0.0480 0.0064  81  TYR B OH  
3183 N N   . THR B 85  ? 0.3628 0.2715 0.2197 -0.0497 -0.0374 0.0162  82  THR B N   
3184 C CA  . THR B 85  ? 0.3557 0.2666 0.2146 -0.0471 -0.0339 0.0130  82  THR B CA  
3185 C C   . THR B 85  ? 0.3544 0.2628 0.2121 -0.0458 -0.0349 0.0097  82  THR B C   
3186 O O   . THR B 85  ? 0.3604 0.2673 0.2194 -0.0452 -0.0386 0.0091  82  THR B O   
3187 C CB  . THR B 85  ? 0.3533 0.2656 0.2175 -0.0457 -0.0342 0.0128  82  THR B CB  
3188 O OG1 . THR B 85  ? 0.3466 0.2630 0.2135 -0.0477 -0.0337 0.0160  82  THR B OG1 
3189 C CG2 . THR B 85  ? 0.3523 0.2655 0.2173 -0.0428 -0.0307 0.0103  82  THR B CG2 
3190 N N   . SER B 86  ? 0.3595 0.2674 0.2146 -0.0453 -0.0322 0.0076  83  SER B N   
3191 C CA  . SER B 86  ? 0.3680 0.2744 0.2241 -0.0453 -0.0329 0.0049  83  SER B CA  
3192 C C   . SER B 86  ? 0.3579 0.2629 0.2151 -0.0441 -0.0294 0.0039  83  SER B C   
3193 O O   . SER B 86  ? 0.3816 0.2871 0.2378 -0.0424 -0.0267 0.0046  83  SER B O   
3194 C CB  . SER B 86  ? 0.3846 0.2891 0.2363 -0.0468 -0.0348 0.0031  83  SER B CB  
3195 O OG  . SER B 86  ? 0.4061 0.3111 0.2614 -0.0480 -0.0362 0.0013  83  SER B OG  
3196 N N   . LYS B 87  ? 0.3499 0.2538 0.2094 -0.0450 -0.0296 0.0027  84  LYS B N   
3197 C CA  . LYS B 87  ? 0.3577 0.2586 0.2179 -0.0442 -0.0268 0.0026  84  LYS B CA  
3198 C C   . LYS B 87  ? 0.3636 0.2598 0.2227 -0.0474 -0.0277 0.0010  84  LYS B C   
3199 O O   . LYS B 87  ? 0.3704 0.2702 0.2328 -0.0503 -0.0305 0.0008  84  LYS B O   
3200 C CB  . LYS B 87  ? 0.3509 0.2556 0.2159 -0.0424 -0.0261 0.0045  84  LYS B CB  
3201 C CG  . LYS B 87  ? 0.3475 0.2558 0.2138 -0.0401 -0.0272 0.0055  84  LYS B CG  
3202 C CD  . LYS B 87  ? 0.3515 0.2622 0.2204 -0.0372 -0.0267 0.0064  84  LYS B CD  
3203 C CE  . LYS B 87  ? 0.3618 0.2743 0.2315 -0.0352 -0.0293 0.0067  84  LYS B CE  
3204 N NZ  . LYS B 87  ? 0.3709 0.2845 0.2412 -0.0350 -0.0330 0.0061  84  LYS B NZ  
3205 N N   . LEU B 88  ? 0.3652 0.2537 0.2199 -0.0467 -0.0261 -0.0001 85  LEU B N   
3206 C CA  . LEU B 88  ? 0.3799 0.2602 0.2327 -0.0501 -0.0274 -0.0015 85  LEU B CA  
3207 C C   . LEU B 88  ? 0.3783 0.2606 0.2374 -0.0527 -0.0264 0.0017  85  LEU B C   
3208 O O   . LEU B 88  ? 0.3757 0.2567 0.2346 -0.0495 -0.0233 0.0038  85  LEU B O   
3209 C CB  . LEU B 88  ? 0.3894 0.2592 0.2340 -0.0468 -0.0260 -0.0036 85  LEU B CB  
3210 C CG  . LEU B 88  ? 0.4106 0.2678 0.2513 -0.0500 -0.0283 -0.0055 85  LEU B CG  
3211 C CD1 . LEU B 88  ? 0.4254 0.2797 0.2621 -0.0529 -0.0327 -0.0094 85  LEU B CD1 
3212 C CD2 . LEU B 88  ? 0.4190 0.2649 0.2517 -0.0447 -0.0265 -0.0069 85  LEU B CD2 
3213 N N   . TRP B 89  ? 0.3900 0.2761 0.2544 -0.0578 -0.0287 0.0024  86  TRP B N   
3214 C CA  . TRP B 89  ? 0.3967 0.2869 0.2677 -0.0607 -0.0269 0.0065  86  TRP B CA  
3215 C C   . TRP B 89  ? 0.4265 0.3038 0.2939 -0.0636 -0.0263 0.0076  86  TRP B C   
3216 O O   . TRP B 89  ? 0.4435 0.3086 0.3042 -0.0645 -0.0288 0.0042  86  TRP B O   
3217 C CB  . TRP B 89  ? 0.4004 0.3025 0.2799 -0.0649 -0.0291 0.0076  86  TRP B CB  
3218 C CG  . TRP B 89  ? 0.4027 0.3131 0.2892 -0.0666 -0.0262 0.0125  86  TRP B CG  
3219 C CD1 . TRP B 89  ? 0.4195 0.3342 0.3129 -0.0737 -0.0269 0.0155  86  TRP B CD1 
3220 C CD2 . TRP B 89  ? 0.3964 0.3103 0.2826 -0.0616 -0.0220 0.0156  86  TRP B CD2 
3221 N NE1 . TRP B 89  ? 0.4207 0.3430 0.3184 -0.0731 -0.0226 0.0208  86  TRP B NE1 
3222 C CE2 . TRP B 89  ? 0.4080 0.3295 0.3006 -0.0653 -0.0196 0.0206  86  TRP B CE2 
3223 C CE3 . TRP B 89  ? 0.3786 0.2914 0.2602 -0.0545 -0.0203 0.0147  86  TRP B CE3 
3224 C CZ2 . TRP B 89  ? 0.4107 0.3378 0.3034 -0.0612 -0.0153 0.0246  86  TRP B CZ2 
3225 C CZ3 . TRP B 89  ? 0.3876 0.3055 0.2698 -0.0507 -0.0170 0.0178  86  TRP B CZ3 
3226 C CH2 . TRP B 89  ? 0.4024 0.3269 0.2892 -0.0535 -0.0144 0.0227  86  TRP B CH2 
3227 N N   . SER B 90  ? 0.4250 0.3045 0.2960 -0.0647 -0.0234 0.0125  87  SER B N   
3228 C CA  . SER B 90  ? 0.4445 0.3112 0.3115 -0.0664 -0.0221 0.0153  87  SER B CA  
3229 C C   . SER B 90  ? 0.4675 0.3249 0.3354 -0.0753 -0.0259 0.0156  87  SER B C   
3230 O O   . SER B 90  ? 0.4792 0.3210 0.3416 -0.0770 -0.0262 0.0171  87  SER B O   
3231 C CB  . SER B 90  ? 0.4438 0.3181 0.3144 -0.0647 -0.0177 0.0212  87  SER B CB  
3232 O OG  . SER B 90  ? 0.4353 0.3166 0.3044 -0.0567 -0.0157 0.0200  87  SER B OG  
3233 N N   . THR B 91  ? 0.4675 0.3333 0.3420 -0.0808 -0.0292 0.0143  88  THR B N   
3234 C CA  . THR B 91  ? 0.4912 0.3489 0.3672 -0.0900 -0.0346 0.0134  88  THR B CA  
3235 C C   . THR B 91  ? 0.4988 0.3416 0.3643 -0.0882 -0.0395 0.0060  88  THR B C   
3236 O O   . THR B 91  ? 0.5301 0.3623 0.3945 -0.0953 -0.0450 0.0042  88  THR B O   
3237 C CB  . THR B 91  ? 0.4887 0.3648 0.3773 -0.0962 -0.0363 0.0154  88  THR B CB  
3238 O OG1 . THR B 91  ? 0.4592 0.3456 0.3477 -0.0903 -0.0370 0.0113  88  THR B OG1 
3239 C CG2 . THR B 91  ? 0.4895 0.3801 0.3877 -0.0982 -0.0313 0.0231  88  THR B CG2 
3240 N N   . PHE B 92  ? 0.4828 0.3244 0.3407 -0.0793 -0.0377 0.0021  89  PHE B N   
3241 C CA  . PHE B 92  ? 0.4940 0.3251 0.3411 -0.0755 -0.0411 -0.0047 89  PHE B CA  
3242 C C   . PHE B 92  ? 0.5026 0.3220 0.3390 -0.0671 -0.0382 -0.0064 89  PHE B C   
3243 O O   . PHE B 92  ? 0.5204 0.3368 0.3484 -0.0610 -0.0385 -0.0112 89  PHE B O   
3244 C CB  . PHE B 92  ? 0.4738 0.3186 0.3225 -0.0723 -0.0412 -0.0070 89  PHE B CB  
3245 C CG  . PHE B 92  ? 0.4727 0.3309 0.3316 -0.0784 -0.0442 -0.0056 89  PHE B CG  
3246 C CD1 . PHE B 92  ? 0.5019 0.3563 0.3620 -0.0854 -0.0505 -0.0081 89  PHE B CD1 
3247 C CD2 . PHE B 92  ? 0.4582 0.3330 0.3257 -0.0766 -0.0412 -0.0022 89  PHE B CD2 
3248 C CE1 . PHE B 92  ? 0.4984 0.3676 0.3689 -0.0903 -0.0534 -0.0067 89  PHE B CE1 
3249 C CE2 . PHE B 92  ? 0.4585 0.3468 0.3353 -0.0807 -0.0439 -0.0011 89  PHE B CE2 
3250 C CZ  . PHE B 92  ? 0.4726 0.3593 0.3516 -0.0875 -0.0498 -0.0031 89  PHE B CZ  
3251 N N   . HIS B 93  ? 0.4977 0.3112 0.3341 -0.0663 -0.0353 -0.0024 90  HIS B N   
3252 C CA  . HIS B 93  ? 0.5092 0.3110 0.3357 -0.0579 -0.0330 -0.0038 90  HIS B CA  
3253 C C   . HIS B 93  ? 0.5404 0.3207 0.3547 -0.0570 -0.0379 -0.0092 90  HIS B C   
3254 O O   . HIS B 93  ? 0.5461 0.3192 0.3502 -0.0476 -0.0368 -0.0130 90  HIS B O   
3255 C CB  . HIS B 93  ? 0.5089 0.3094 0.3383 -0.0578 -0.0295 0.0025  90  HIS B CB  
3256 C CG  . HIS B 93  ? 0.4880 0.3065 0.3248 -0.0545 -0.0247 0.0061  90  HIS B CG  
3257 N ND1 . HIS B 93  ? 0.4954 0.3144 0.3332 -0.0521 -0.0213 0.0113  90  HIS B ND1 
3258 C CD2 . HIS B 93  ? 0.4668 0.3014 0.3087 -0.0522 -0.0234 0.0051  90  HIS B CD2 
3259 C CE1 . HIS B 93  ? 0.4696 0.3045 0.3127 -0.0485 -0.0184 0.0125  90  HIS B CE1 
3260 N NE2 . HIS B 93  ? 0.4523 0.2963 0.2983 -0.0489 -0.0197 0.0089  90  HIS B NE2 
3261 N N   . ARG B 94  ? 0.5667 0.3364 0.3812 -0.0658 -0.0435 -0.0099 91  ARG B N   
3262 C CA  . ARG B 94  ? 0.6177 0.3636 0.4183 -0.0639 -0.0492 -0.0160 91  ARG B CA  
3263 C C   . ARG B 94  ? 0.6162 0.3657 0.4087 -0.0564 -0.0499 -0.0231 91  ARG B C   
3264 O O   . ARG B 94  ? 0.5961 0.3620 0.3953 -0.0589 -0.0496 -0.0232 91  ARG B O   
3265 C CB  . ARG B 94  ? 0.6560 0.3892 0.4585 -0.0758 -0.0565 -0.0159 91  ARG B CB  
3266 C CG  . ARG B 94  ? 0.6764 0.4039 0.4851 -0.0832 -0.0554 -0.0079 91  ARG B CG  
3267 C CD  . ARG B 94  ? 0.7167 0.4344 0.5299 -0.0968 -0.0625 -0.0063 91  ARG B CD  
3268 N NE  . ARG B 94  ? 0.7380 0.4503 0.5557 -0.1024 -0.0600 0.0026  91  ARG B NE  
3269 C CZ  . ARG B 94  ? 0.7942 0.4797 0.6023 -0.1043 -0.0638 0.0036  91  ARG B CZ  
3270 N NH1 . ARG B 94  ? 0.8263 0.4875 0.6197 -0.1008 -0.0709 -0.0047 91  ARG B NH1 
3271 N NH2 . ARG B 94  ? 0.8017 0.4837 0.6138 -0.1094 -0.0610 0.0129  91  ARG B NH2 
3272 N N   . PRO B 95  ? 0.6322 0.3692 0.4106 -0.0458 -0.0497 -0.0283 92  PRO B N   
3273 C CA  . PRO B 95  ? 0.6286 0.3740 0.3998 -0.0364 -0.0475 -0.0332 92  PRO B CA  
3274 C C   . PRO B 95  ? 0.6320 0.3801 0.4006 -0.0399 -0.0523 -0.0379 92  PRO B C   
3275 O O   . PRO B 95  ? 0.6074 0.3714 0.3772 -0.0365 -0.0492 -0.0380 92  PRO B O   
3276 C CB  . PRO B 95  ? 0.6647 0.3931 0.4201 -0.0248 -0.0476 -0.0382 92  PRO B CB  
3277 C CG  . PRO B 95  ? 0.6878 0.3948 0.4410 -0.0286 -0.0511 -0.0362 92  PRO B CG  
3278 C CD  . PRO B 95  ? 0.6619 0.3782 0.4311 -0.0412 -0.0504 -0.0284 92  PRO B CD  
3279 N N   . GLU B 96  ? 0.6619 0.3948 0.4276 -0.0476 -0.0602 -0.0409 93  GLU B N   
3280 C CA  . GLU B 96  ? 0.6766 0.4097 0.4386 -0.0511 -0.0665 -0.0461 93  GLU B CA  
3281 C C   . GLU B 96  ? 0.6370 0.3925 0.4148 -0.0588 -0.0652 -0.0411 93  GLU B C   
3282 O O   . GLU B 96  ? 0.6325 0.3933 0.4082 -0.0601 -0.0691 -0.0445 93  GLU B O   
3283 C CB  . GLU B 96  ? 0.7243 0.4340 0.4797 -0.0580 -0.0764 -0.0507 93  GLU B CB  
3284 C CG  . GLU B 96  ? 0.7350 0.4452 0.5055 -0.0720 -0.0790 -0.0442 93  GLU B CG  
3285 C CD  . GLU B 96  ? 0.7600 0.4578 0.5323 -0.0739 -0.0768 -0.0389 93  GLU B CD  
3286 O OE1 . GLU B 96  ? 0.7752 0.4658 0.5384 -0.0631 -0.0723 -0.0397 93  GLU B OE1 
3287 O OE2 . GLU B 96  ? 0.7864 0.4823 0.5693 -0.0861 -0.0796 -0.0336 93  GLU B OE2 
3288 N N   . LEU B 97  ? 0.6014 0.3697 0.3931 -0.0624 -0.0599 -0.0336 94  LEU B N   
3289 C CA  . LEU B 97  ? 0.5718 0.3607 0.3779 -0.0685 -0.0589 -0.0291 94  LEU B CA  
3290 C C   . LEU B 97  ? 0.5399 0.3457 0.3479 -0.0613 -0.0522 -0.0270 94  LEU B C   
3291 O O   . LEU B 97  ? 0.5174 0.3389 0.3343 -0.0640 -0.0518 -0.0244 94  LEU B O   
3292 C CB  . LEU B 97  ? 0.5689 0.3612 0.3881 -0.0767 -0.0576 -0.0224 94  LEU B CB  
3293 C CG  . LEU B 97  ? 0.6009 0.3781 0.4209 -0.0863 -0.0642 -0.0226 94  LEU B CG  
3294 C CD1 . LEU B 97  ? 0.5956 0.3811 0.4299 -0.0945 -0.0616 -0.0143 94  LEU B CD1 
3295 C CD2 . LEU B 97  ? 0.6183 0.3954 0.4387 -0.0927 -0.0725 -0.0272 94  LEU B CD2 
3296 N N   . VAL B 98  ? 0.5337 0.3367 0.3338 -0.0524 -0.0477 -0.0279 95  VAL B N   
3297 C CA  . VAL B 98  ? 0.5013 0.3205 0.3059 -0.0472 -0.0413 -0.0244 95  VAL B CA  
3298 C C   . VAL B 98  ? 0.5011 0.3296 0.3023 -0.0455 -0.0422 -0.0261 95  VAL B C   
3299 O O   . VAL B 98  ? 0.4743 0.3165 0.2840 -0.0478 -0.0409 -0.0224 95  VAL B O   
3300 C CB  . VAL B 98  ? 0.5023 0.3178 0.3009 -0.0386 -0.0364 -0.0244 95  VAL B CB  
3301 C CG1 . VAL B 98  ? 0.4801 0.3118 0.2821 -0.0338 -0.0310 -0.0215 95  VAL B CG1 
3302 C CG2 . VAL B 98  ? 0.5044 0.3130 0.3073 -0.0402 -0.0352 -0.0211 95  VAL B CG2 
3303 N N   . ARG B 99  ? 0.5177 0.3383 0.3057 -0.0407 -0.0441 -0.0314 96  ARG B N   
3304 C CA  . ARG B 99  ? 0.5220 0.3510 0.3047 -0.0382 -0.0445 -0.0325 96  ARG B CA  
3305 C C   . ARG B 99  ? 0.5177 0.3517 0.3070 -0.0457 -0.0498 -0.0319 96  ARG B C   
3306 O O   . ARG B 99  ? 0.5049 0.3511 0.2979 -0.0459 -0.0487 -0.0288 96  ARG B O   
3307 C CB  . ARG B 99  ? 0.5543 0.3742 0.3200 -0.0308 -0.0457 -0.0385 96  ARG B CB  
3308 C CG  . ARG B 99  ? 0.5565 0.3860 0.3166 -0.0288 -0.0457 -0.0384 96  ARG B CG  
3309 C CD  . ARG B 99  ? 0.5847 0.4095 0.3274 -0.0197 -0.0450 -0.0433 96  ARG B CD  
3310 N NE  . ARG B 99  ? 0.5904 0.4228 0.3277 -0.0195 -0.0466 -0.0429 96  ARG B NE  
3311 C CZ  . ARG B 99  ? 0.6110 0.4476 0.3351 -0.0116 -0.0435 -0.0438 96  ARG B CZ  
3312 N NH1 . ARG B 99  ? 0.6291 0.4652 0.3456 -0.0029 -0.0382 -0.0453 96  ARG B NH1 
3313 N NH2 . ARG B 99  ? 0.6106 0.4528 0.3289 -0.0119 -0.0455 -0.0429 96  ARG B NH2 
3314 N N   . PRO B 100 ? 0.5313 0.3567 0.3226 -0.0522 -0.0562 -0.0346 97  PRO B N   
3315 C CA  . PRO B 100 ? 0.5296 0.3633 0.3287 -0.0587 -0.0612 -0.0338 97  PRO B CA  
3316 C C   . PRO B 100 ? 0.4962 0.3451 0.3104 -0.0617 -0.0577 -0.0273 97  PRO B C   
3317 O O   . PRO B 100 ? 0.4787 0.3379 0.2969 -0.0629 -0.0600 -0.0261 97  PRO B O   
3318 C CB  . PRO B 100 ? 0.5541 0.3760 0.3540 -0.0657 -0.0683 -0.0372 97  PRO B CB  
3319 C CG  . PRO B 100 ? 0.5831 0.3866 0.3673 -0.0600 -0.0689 -0.0428 97  PRO B CG  
3320 C CD  . PRO B 100 ? 0.5653 0.3724 0.3498 -0.0532 -0.0601 -0.0391 97  PRO B CD  
3321 N N   . ALA B 101 ? 0.4871 0.3367 0.3078 -0.0616 -0.0527 -0.0236 98  ALA B N   
3322 C CA  . ALA B 101 ? 0.4608 0.3237 0.2937 -0.0628 -0.0493 -0.0180 98  ALA B CA  
3323 C C   . ALA B 101 ? 0.4449 0.3157 0.2753 -0.0575 -0.0462 -0.0163 98  ALA B C   
3324 O O   . ALA B 101 ? 0.4438 0.3244 0.2801 -0.0583 -0.0472 -0.0140 98  ALA B O   
3325 C CB  . ALA B 101 ? 0.4517 0.3126 0.2901 -0.0632 -0.0450 -0.0147 98  ALA B CB  
3326 N N   . LEU B 102 ? 0.4496 0.3164 0.2710 -0.0520 -0.0429 -0.0173 99  LEU B N   
3327 C CA  . LEU B 102 ? 0.4383 0.3130 0.2577 -0.0483 -0.0401 -0.0147 99  LEU B CA  
3328 C C   . LEU B 102 ? 0.4528 0.3299 0.2674 -0.0491 -0.0445 -0.0159 99  LEU B C   
3329 O O   . LEU B 102 ? 0.4272 0.3117 0.2452 -0.0492 -0.0447 -0.0125 99  LEU B O   
3330 C CB  . LEU B 102 ? 0.4436 0.3159 0.2551 -0.0425 -0.0355 -0.0152 99  LEU B CB  
3331 C CG  . LEU B 102 ? 0.4392 0.3202 0.2485 -0.0395 -0.0321 -0.0117 99  LEU B CG  
3332 C CD1 . LEU B 102 ? 0.4115 0.3008 0.2311 -0.0422 -0.0315 -0.0067 99  LEU B CD1 
3333 C CD2 . LEU B 102 ? 0.4443 0.3258 0.2482 -0.0336 -0.0270 -0.0120 99  LEU B CD2 
3334 N N   . GLU B 103 ? 0.4797 0.3496 0.2857 -0.0492 -0.0487 -0.0207 100 GLU B N   
3335 C CA  . GLU B 103 ? 0.5125 0.3846 0.3123 -0.0490 -0.0532 -0.0219 100 GLU B CA  
3336 C C   . GLU B 103 ? 0.4949 0.3743 0.3053 -0.0535 -0.0576 -0.0202 100 GLU B C   
3337 O O   . GLU B 103 ? 0.4950 0.3796 0.3035 -0.0524 -0.0598 -0.0186 100 GLU B O   
3338 C CB  . GLU B 103 ? 0.5524 0.4144 0.3403 -0.0480 -0.0580 -0.0285 100 GLU B CB  
3339 C CG  . GLU B 103 ? 0.5875 0.4433 0.3624 -0.0413 -0.0539 -0.0307 100 GLU B CG  
3340 C CD  . GLU B 103 ? 0.6297 0.4724 0.3916 -0.0394 -0.0590 -0.0383 100 GLU B CD  
3341 O OE1 . GLU B 103 ? 0.6983 0.5330 0.4640 -0.0449 -0.0651 -0.0417 100 GLU B OE1 
3342 O OE2 . GLU B 103 ? 0.6509 0.4910 0.3989 -0.0323 -0.0569 -0.0406 100 GLU B OE2 
3343 N N   . ASN B 104 ? 0.5043 0.3847 0.3254 -0.0580 -0.0587 -0.0202 101 ASN B N   
3344 C CA  . ASN B 104 ? 0.4997 0.3901 0.3324 -0.0615 -0.0619 -0.0182 101 ASN B CA  
3345 C C   . ASN B 104 ? 0.4700 0.3681 0.3070 -0.0582 -0.0584 -0.0135 101 ASN B C   
3346 O O   . ASN B 104 ? 0.4639 0.3680 0.3021 -0.0571 -0.0617 -0.0124 101 ASN B O   
3347 C CB  . ASN B 104 ? 0.5305 0.4220 0.3739 -0.0670 -0.0624 -0.0180 101 ASN B CB  
3348 C CG  . ASN B 104 ? 0.5530 0.4581 0.4087 -0.0695 -0.0651 -0.0158 101 ASN B CG  
3349 O OD1 . ASN B 104 ? 0.6169 0.5299 0.4807 -0.0683 -0.0616 -0.0121 101 ASN B OD1 
3350 N ND2 . ASN B 104 ? 0.5657 0.4742 0.4216 -0.0718 -0.0717 -0.0183 101 ASN B ND2 
3351 N N   . SER B 105 ? 0.4428 0.3395 0.2809 -0.0564 -0.0527 -0.0111 102 SER B N   
3352 C CA  . SER B 105 ? 0.4217 0.3235 0.2631 -0.0537 -0.0504 -0.0070 102 SER B CA  
3353 C C   . SER B 105 ? 0.4256 0.3266 0.2587 -0.0512 -0.0518 -0.0057 102 SER B C   
3354 O O   . SER B 105 ? 0.4093 0.3139 0.2449 -0.0501 -0.0539 -0.0033 102 SER B O   
3355 C CB  . SER B 105 ? 0.4081 0.3085 0.2518 -0.0524 -0.0449 -0.0051 102 SER B CB  
3356 O OG  . SER B 105 ? 0.4121 0.3150 0.2643 -0.0541 -0.0439 -0.0047 102 SER B OG  
3357 N N   . LEU B 106 ? 0.4411 0.3375 0.2642 -0.0499 -0.0501 -0.0066 103 LEU B N   
3358 C CA  . LEU B 106 ? 0.4640 0.3602 0.2778 -0.0477 -0.0508 -0.0043 103 LEU B CA  
3359 C C   . LEU B 106 ? 0.4860 0.3835 0.2978 -0.0479 -0.0572 -0.0054 103 LEU B C   
3360 O O   . LEU B 106 ? 0.4803 0.3789 0.2898 -0.0466 -0.0588 -0.0018 103 LEU B O   
3361 C CB  . LEU B 106 ? 0.4892 0.3818 0.2920 -0.0454 -0.0477 -0.0060 103 LEU B CB  
3362 C CG  . LEU B 106 ? 0.4943 0.3879 0.2985 -0.0438 -0.0411 -0.0042 103 LEU B CG  
3363 C CD1 . LEU B 106 ? 0.5238 0.4148 0.3163 -0.0399 -0.0383 -0.0067 103 LEU B CD1 
3364 C CD2 . LEU B 106 ? 0.4854 0.3841 0.2936 -0.0444 -0.0386 0.0021  103 LEU B CD2 
3365 N N   . LYS B 107 ? 0.5040 0.4010 0.3164 -0.0496 -0.0614 -0.0100 104 LYS B N   
3366 C CA  . LYS B 107 ? 0.5280 0.4284 0.3403 -0.0498 -0.0684 -0.0114 104 LYS B CA  
3367 C C   . LYS B 107 ? 0.5036 0.4110 0.3262 -0.0493 -0.0701 -0.0085 104 LYS B C   
3368 O O   . LYS B 107 ? 0.4864 0.3950 0.3051 -0.0466 -0.0739 -0.0066 104 LYS B O   
3369 C CB  . LYS B 107 ? 0.5664 0.4658 0.3802 -0.0531 -0.0729 -0.0170 104 LYS B CB  
3370 C CG  . LYS B 107 ? 0.6104 0.5140 0.4230 -0.0532 -0.0808 -0.0190 104 LYS B CG  
3371 C CD  . LYS B 107 ? 0.6622 0.5664 0.4789 -0.0579 -0.0868 -0.0241 104 LYS B CD  
3372 C CE  . LYS B 107 ? 0.7064 0.6219 0.5310 -0.0583 -0.0936 -0.0239 104 LYS B CE  
3373 N NZ  . LYS B 107 ? 0.7704 0.6881 0.5980 -0.0631 -0.1014 -0.0288 104 LYS B NZ  
3374 N N   . LYS B 108 ? 0.4840 0.3956 0.3180 -0.0508 -0.0676 -0.0080 105 LYS B N   
3375 C CA  . LYS B 108 ? 0.4887 0.4075 0.3317 -0.0489 -0.0691 -0.0059 105 LYS B CA  
3376 C C   . LYS B 108 ? 0.4565 0.3712 0.2946 -0.0452 -0.0683 -0.0021 105 LYS B C   
3377 O O   . LYS B 108 ? 0.4502 0.3669 0.2881 -0.0419 -0.0728 -0.0009 105 LYS B O   
3378 C CB  . LYS B 108 ? 0.5054 0.4285 0.3589 -0.0501 -0.0650 -0.0054 105 LYS B CB  
3379 C CG  . LYS B 108 ? 0.5634 0.4903 0.4240 -0.0549 -0.0649 -0.0076 105 LYS B CG  
3380 C CD  . LYS B 108 ? 0.6187 0.5537 0.4839 -0.0567 -0.0710 -0.0095 105 LYS B CD  
3381 C CE  . LYS B 108 ? 0.6480 0.5953 0.5220 -0.0531 -0.0727 -0.0078 105 LYS B CE  
3382 N NZ  . LYS B 108 ? 0.6579 0.6180 0.5443 -0.0573 -0.0745 -0.0084 105 LYS B NZ  
3383 N N   . ALA B 109 ? 0.4327 0.3416 0.2669 -0.0458 -0.0634 0.0000  106 ALA B N   
3384 C CA  . ALA B 109 ? 0.4394 0.3439 0.2705 -0.0442 -0.0626 0.0044  106 ALA B CA  
3385 C C   . ALA B 109 ? 0.4589 0.3587 0.2788 -0.0436 -0.0646 0.0071  106 ALA B C   
3386 O O   . ALA B 109 ? 0.4608 0.3559 0.2776 -0.0431 -0.0650 0.0116  106 ALA B O   
3387 C CB  . ALA B 109 ? 0.4180 0.3207 0.2510 -0.0458 -0.0569 0.0058  106 ALA B CB  
3388 N N   . GLN B 110 ? 0.4823 0.3825 0.2957 -0.0439 -0.0658 0.0047  107 GLN B N   
3389 C CA  . GLN B 110 ? 0.5276 0.4241 0.3282 -0.0428 -0.0668 0.0071  107 GLN B CA  
3390 C C   . GLN B 110 ? 0.5199 0.4136 0.3164 -0.0440 -0.0613 0.0125  107 GLN B C   
3391 O O   . GLN B 110 ? 0.5333 0.4236 0.3230 -0.0438 -0.0625 0.0179  107 GLN B O   
3392 C CB  . GLN B 110 ? 0.5645 0.4599 0.3611 -0.0401 -0.0736 0.0085  107 GLN B CB  
3393 C CG  . GLN B 110 ? 0.5928 0.4929 0.3900 -0.0392 -0.0789 0.0032  107 GLN B CG  
3394 C CD  . GLN B 110 ? 0.6157 0.5143 0.4031 -0.0398 -0.0782 0.0002  107 GLN B CD  
3395 O OE1 . GLN B 110 ? 0.6538 0.5484 0.4285 -0.0382 -0.0773 0.0032  107 GLN B OE1 
3396 N NE2 . GLN B 110 ? 0.5747 0.4757 0.3670 -0.0421 -0.0788 -0.0055 107 GLN B NE2 
3397 N N   . LEU B 111 ? 0.5040 0.3997 0.3039 -0.0454 -0.0557 0.0113  108 LEU B N   
3398 C CA  . LEU B 111 ? 0.5124 0.4091 0.3093 -0.0464 -0.0498 0.0159  108 LEU B CA  
3399 C C   . LEU B 111 ? 0.5290 0.4274 0.3180 -0.0445 -0.0461 0.0128  108 LEU B C   
3400 O O   . LEU B 111 ? 0.5285 0.4254 0.3174 -0.0435 -0.0481 0.0065  108 LEU B O   
3401 C CB  . LEU B 111 ? 0.5150 0.4132 0.3229 -0.0481 -0.0470 0.0167  108 LEU B CB  
3402 C CG  . LEU B 111 ? 0.5112 0.4063 0.3252 -0.0489 -0.0512 0.0188  108 LEU B CG  
3403 C CD1 . LEU B 111 ? 0.5066 0.4033 0.3305 -0.0497 -0.0490 0.0179  108 LEU B CD1 
3404 C CD2 . LEU B 111 ? 0.5326 0.4235 0.3414 -0.0505 -0.0529 0.0256  108 LEU B CD2 
3405 N N   . ASP B 112 ? 0.5443 0.4457 0.3264 -0.0438 -0.0413 0.0171  109 ASP B N   
3406 C CA  . ASP B 112 ? 0.5633 0.4670 0.3362 -0.0401 -0.0372 0.0141  109 ASP B CA  
3407 C C   . ASP B 112 ? 0.5277 0.4342 0.3074 -0.0393 -0.0321 0.0118  109 ASP B C   
3408 O O   . ASP B 112 ? 0.5436 0.4485 0.3172 -0.0355 -0.0305 0.0065  109 ASP B O   
3409 C CB  . ASP B 112 ? 0.6113 0.5195 0.3738 -0.0389 -0.0335 0.0205  109 ASP B CB  
3410 C CG  . ASP B 112 ? 0.6535 0.5576 0.4070 -0.0388 -0.0388 0.0228  109 ASP B CG  
3411 O OD1 . ASP B 112 ? 0.6765 0.5757 0.4270 -0.0372 -0.0446 0.0167  109 ASP B OD1 
3412 O OD2 . ASP B 112 ? 0.6828 0.5883 0.4334 -0.0408 -0.0377 0.0310  109 ASP B OD2 
3413 N N   . TYR B 113 ? 0.4951 0.4046 0.2861 -0.0423 -0.0303 0.0155  110 TYR B N   
3414 C CA  . TYR B 113 ? 0.4772 0.3899 0.2752 -0.0412 -0.0260 0.0137  110 TYR B CA  
3415 C C   . TYR B 113 ? 0.4536 0.3657 0.2642 -0.0448 -0.0279 0.0152  110 TYR B C   
3416 O O   . TYR B 113 ? 0.4495 0.3598 0.2623 -0.0478 -0.0315 0.0187  110 TYR B O   
3417 C CB  . TYR B 113 ? 0.4851 0.4072 0.2804 -0.0393 -0.0194 0.0181  110 TYR B CB  
3418 C CG  . TYR B 113 ? 0.4952 0.4232 0.2952 -0.0441 -0.0185 0.0268  110 TYR B CG  
3419 C CD1 . TYR B 113 ? 0.4772 0.4087 0.2894 -0.0476 -0.0180 0.0299  110 TYR B CD1 
3420 C CD2 . TYR B 113 ? 0.5217 0.4514 0.3134 -0.0452 -0.0184 0.0323  110 TYR B CD2 
3421 C CE1 . TYR B 113 ? 0.4912 0.4270 0.3078 -0.0529 -0.0180 0.0379  110 TYR B CE1 
3422 C CE2 . TYR B 113 ? 0.5272 0.4612 0.3232 -0.0506 -0.0178 0.0412  110 TYR B CE2 
3423 C CZ  . TYR B 113 ? 0.5117 0.4480 0.3207 -0.0550 -0.0181 0.0438  110 TYR B CZ  
3424 O OH  . TYR B 113 ? 0.5277 0.4662 0.3409 -0.0614 -0.0188 0.0525  110 TYR B OH  
3425 N N   . VAL B 114 ? 0.4349 0.3472 0.2519 -0.0438 -0.0261 0.0123  111 VAL B N   
3426 C CA  . VAL B 114 ? 0.4162 0.3300 0.2440 -0.0462 -0.0267 0.0146  111 VAL B CA  
3427 C C   . VAL B 114 ? 0.4206 0.3427 0.2519 -0.0461 -0.0220 0.0185  111 VAL B C   
3428 O O   . VAL B 114 ? 0.4299 0.3565 0.2574 -0.0425 -0.0175 0.0175  111 VAL B O   
3429 C CB  . VAL B 114 ? 0.4007 0.3105 0.2338 -0.0454 -0.0279 0.0100  111 VAL B CB  
3430 C CG1 . VAL B 114 ? 0.3975 0.3024 0.2293 -0.0462 -0.0324 0.0068  111 VAL B CG1 
3431 C CG2 . VAL B 114 ? 0.4007 0.3104 0.2324 -0.0420 -0.0241 0.0069  111 VAL B CG2 
3432 N N   . ASP B 115 ? 0.4113 0.3357 0.2504 -0.0495 -0.0234 0.0225  112 ASP B N   
3433 C CA  . ASP B 115 ? 0.4099 0.3440 0.2552 -0.0502 -0.0198 0.0262  112 ASP B CA  
3434 C C   . ASP B 115 ? 0.3952 0.3306 0.2444 -0.0461 -0.0177 0.0219  112 ASP B C   
3435 O O   . ASP B 115 ? 0.3961 0.3404 0.2474 -0.0436 -0.0134 0.0230  112 ASP B O   
3436 C CB  . ASP B 115 ? 0.4067 0.3408 0.2585 -0.0559 -0.0236 0.0313  112 ASP B CB  
3437 C CG  . ASP B 115 ? 0.4216 0.3532 0.2677 -0.0595 -0.0253 0.0363  112 ASP B CG  
3438 O OD1 . ASP B 115 ? 0.4159 0.3380 0.2578 -0.0596 -0.0298 0.0348  112 ASP B OD1 
3439 O OD2 . ASP B 115 ? 0.4410 0.3811 0.2867 -0.0619 -0.0218 0.0421  112 ASP B OD2 
3440 N N   . LEU B 116 ? 0.3818 0.3092 0.2319 -0.0451 -0.0204 0.0176  113 LEU B N   
3441 C CA  . LEU B 116 ? 0.3683 0.2953 0.2218 -0.0417 -0.0189 0.0146  113 LEU B CA  
3442 C C   . LEU B 116 ? 0.3652 0.2832 0.2154 -0.0405 -0.0204 0.0101  113 LEU B C   
3443 O O   . LEU B 116 ? 0.3618 0.2758 0.2126 -0.0429 -0.0241 0.0097  113 LEU B O   
3444 C CB  . LEU B 116 ? 0.3551 0.2840 0.2168 -0.0435 -0.0214 0.0164  113 LEU B CB  
3445 C CG  . LEU B 116 ? 0.3519 0.2815 0.2170 -0.0397 -0.0200 0.0142  113 LEU B CG  
3446 C CD1 . LEU B 116 ? 0.3597 0.2960 0.2239 -0.0355 -0.0153 0.0142  113 LEU B CD1 
3447 C CD2 . LEU B 116 ? 0.3426 0.2740 0.2144 -0.0413 -0.0234 0.0156  113 LEU B CD2 
3448 N N   . TYR B 117 ? 0.3745 0.2896 0.2213 -0.0367 -0.0179 0.0070  114 TYR B N   
3449 C CA  . TYR B 117 ? 0.3744 0.2807 0.2194 -0.0367 -0.0195 0.0034  114 TYR B CA  
3450 C C   . TYR B 117 ? 0.3796 0.2843 0.2275 -0.0339 -0.0179 0.0030  114 TYR B C   
3451 O O   . TYR B 117 ? 0.3900 0.2965 0.2357 -0.0296 -0.0149 0.0027  114 TYR B O   
3452 C CB  . TYR B 117 ? 0.3849 0.2848 0.2209 -0.0355 -0.0197 -0.0001 114 TYR B CB  
3453 C CG  . TYR B 117 ? 0.3810 0.2731 0.2164 -0.0385 -0.0232 -0.0028 114 TYR B CG  
3454 C CD1 . TYR B 117 ? 0.3723 0.2664 0.2128 -0.0424 -0.0264 -0.0017 114 TYR B CD1 
3455 C CD2 . TYR B 117 ? 0.3947 0.2773 0.2242 -0.0373 -0.0237 -0.0066 114 TYR B CD2 
3456 C CE1 . TYR B 117 ? 0.3721 0.2623 0.2138 -0.0455 -0.0294 -0.0036 114 TYR B CE1 
3457 C CE2 . TYR B 117 ? 0.3949 0.2711 0.2251 -0.0415 -0.0274 -0.0085 114 TYR B CE2 
3458 C CZ  . TYR B 117 ? 0.3905 0.2721 0.2275 -0.0458 -0.0301 -0.0068 114 TYR B CZ  
3459 O OH  . TYR B 117 ? 0.3955 0.2740 0.2349 -0.0503 -0.0337 -0.0082 114 TYR B OH  
3460 N N   . LEU B 118 ? 0.3676 0.2697 0.2197 -0.0356 -0.0196 0.0032  115 LEU B N   
3461 C CA  . LEU B 118 ? 0.3648 0.2647 0.2187 -0.0330 -0.0181 0.0035  115 LEU B CA  
3462 C C   . LEU B 118 ? 0.3707 0.2614 0.2218 -0.0341 -0.0184 0.0020  115 LEU B C   
3463 O O   . LEU B 118 ? 0.3674 0.2568 0.2193 -0.0381 -0.0206 0.0015  115 LEU B O   
3464 C CB  . LEU B 118 ? 0.3505 0.2553 0.2105 -0.0338 -0.0197 0.0055  115 LEU B CB  
3465 C CG  . LEU B 118 ? 0.3421 0.2540 0.2055 -0.0344 -0.0210 0.0072  115 LEU B CG  
3466 C CD1 . LEU B 118 ? 0.3387 0.2527 0.2064 -0.0339 -0.0234 0.0081  115 LEU B CD1 
3467 C CD2 . LEU B 118 ? 0.3477 0.2650 0.2114 -0.0319 -0.0186 0.0081  115 LEU B CD2 
3468 N N   . ILE B 119 ? 0.3803 0.2651 0.2286 -0.0308 -0.0166 0.0018  116 ILE B N   
3469 C CA  . ILE B 119 ? 0.3891 0.2661 0.2371 -0.0327 -0.0169 0.0027  116 ILE B CA  
3470 C C   . ILE B 119 ? 0.3737 0.2583 0.2283 -0.0340 -0.0170 0.0056  116 ILE B C   
3471 O O   . ILE B 119 ? 0.3710 0.2601 0.2271 -0.0302 -0.0160 0.0069  116 ILE B O   
3472 C CB  . ILE B 119 ? 0.4053 0.2728 0.2477 -0.0282 -0.0154 0.0025  116 ILE B CB  
3473 C CG1 . ILE B 119 ? 0.4325 0.2925 0.2668 -0.0250 -0.0155 -0.0013 116 ILE B CG1 
3474 C CG2 . ILE B 119 ? 0.4125 0.2718 0.2550 -0.0317 -0.0158 0.0048  116 ILE B CG2 
3475 C CD1 . ILE B 119 ? 0.4510 0.2990 0.2780 -0.0192 -0.0147 -0.0023 116 ILE B CD1 
3476 N N   . HIS B 120 ? 0.3668 0.2534 0.2249 -0.0384 -0.0184 0.0064  117 HIS B N   
3477 C CA  . HIS B 120 ? 0.3544 0.2492 0.2177 -0.0384 -0.0185 0.0085  117 HIS B CA  
3478 C C   . HIS B 120 ? 0.3629 0.2567 0.2256 -0.0355 -0.0162 0.0113  117 HIS B C   
3479 O O   . HIS B 120 ? 0.3478 0.2476 0.2121 -0.0321 -0.0161 0.0123  117 HIS B O   
3480 C CB  . HIS B 120 ? 0.3558 0.2547 0.2233 -0.0429 -0.0200 0.0090  117 HIS B CB  
3481 C CG  . HIS B 120 ? 0.3459 0.2544 0.2175 -0.0411 -0.0211 0.0095  117 HIS B CG  
3482 N ND1 . HIS B 120 ? 0.3404 0.2546 0.2153 -0.0431 -0.0236 0.0087  117 HIS B ND1 
3483 C CD2 . HIS B 120 ? 0.3402 0.2528 0.2120 -0.0366 -0.0207 0.0103  117 HIS B CD2 
3484 C CE1 . HIS B 120 ? 0.3361 0.2568 0.2128 -0.0394 -0.0245 0.0090  117 HIS B CE1 
3485 N NE2 . HIS B 120 ? 0.3428 0.2621 0.2174 -0.0355 -0.0230 0.0097  117 HIS B NE2 
3486 N N   . SER B 121 ? 0.3767 0.2617 0.2363 -0.0366 -0.0148 0.0127  118 SER B N   
3487 C CA  . SER B 121 ? 0.3897 0.2723 0.2476 -0.0345 -0.0124 0.0164  118 SER B CA  
3488 C C   . SER B 121 ? 0.4092 0.2778 0.2611 -0.0348 -0.0119 0.0169  118 SER B C   
3489 O O   . SER B 121 ? 0.4132 0.2745 0.2636 -0.0387 -0.0136 0.0148  118 SER B O   
3490 C CB  . SER B 121 ? 0.3948 0.2839 0.2572 -0.0380 -0.0114 0.0199  118 SER B CB  
3491 O OG  . SER B 121 ? 0.4085 0.2926 0.2684 -0.0382 -0.0089 0.0245  118 SER B OG  
3492 N N   . PRO B 122 ? 0.4198 0.2832 0.2673 -0.0299 -0.0104 0.0191  119 PRO B N   
3493 C CA  . PRO B 122 ? 0.4453 0.2929 0.2859 -0.0294 -0.0105 0.0197  119 PRO B CA  
3494 C C   . PRO B 122 ? 0.4679 0.3076 0.3084 -0.0364 -0.0102 0.0243  119 PRO B C   
3495 O O   . PRO B 122 ? 0.4992 0.3225 0.3333 -0.0373 -0.0114 0.0247  119 PRO B O   
3496 C CB  . PRO B 122 ? 0.4494 0.2964 0.2857 -0.0211 -0.0092 0.0209  119 PRO B CB  
3497 C CG  . PRO B 122 ? 0.4321 0.2925 0.2730 -0.0198 -0.0080 0.0233  119 PRO B CG  
3498 C CD  . PRO B 122 ? 0.4160 0.2871 0.2637 -0.0240 -0.0092 0.0207  119 PRO B CD  
3499 N N   . MET B 123 ? 0.4546 0.3056 0.3020 -0.0411 -0.0089 0.0277  120 MET B N   
3500 C CA  . MET B 123 ? 0.4783 0.3260 0.3274 -0.0481 -0.0077 0.0340  120 MET B CA  
3501 C C   . MET B 123 ? 0.4802 0.3248 0.3337 -0.0573 -0.0107 0.0326  120 MET B C   
3502 O O   . MET B 123 ? 0.4640 0.3225 0.3256 -0.0613 -0.0108 0.0328  120 MET B O   
3503 C CB  . MET B 123 ? 0.4818 0.3460 0.3361 -0.0472 -0.0043 0.0385  120 MET B CB  
3504 C CG  . MET B 123 ? 0.4911 0.3553 0.3395 -0.0387 -0.0022 0.0403  120 MET B CG  
3505 S SD  . MET B 123 ? 0.5053 0.3877 0.3565 -0.0353 0.0015  0.0447  120 MET B SD  
3506 C CE  . MET B 123 ? 0.4812 0.3774 0.3386 -0.0330 -0.0011 0.0377  120 MET B CE  
3507 N N   . SER B 124 ? 0.4967 0.3233 0.3439 -0.0594 -0.0139 0.0302  121 SER B N   
3508 C CA  . SER B 124 ? 0.5171 0.3372 0.3662 -0.0677 -0.0183 0.0276  121 SER B CA  
3509 C C   . SER B 124 ? 0.5323 0.3606 0.3911 -0.0781 -0.0180 0.0338  121 SER B C   
3510 O O   . SER B 124 ? 0.5466 0.3735 0.4057 -0.0802 -0.0149 0.0412  121 SER B O   
3511 C CB  . SER B 124 ? 0.5419 0.3382 0.3804 -0.0672 -0.0217 0.0250  121 SER B CB  
3512 O OG  . SER B 124 ? 0.5393 0.3320 0.3700 -0.0564 -0.0211 0.0201  121 SER B OG  
3513 N N   . LEU B 125 ? 0.5248 0.3620 0.3912 -0.0843 -0.0210 0.0315  122 LEU B N   
3514 C CA  . LEU B 125 ? 0.5444 0.3924 0.4219 -0.0947 -0.0211 0.0372  122 LEU B CA  
3515 C C   . LEU B 125 ? 0.5831 0.4196 0.4613 -0.1039 -0.0280 0.0340  122 LEU B C   
3516 O O   . LEU B 125 ? 0.5942 0.4190 0.4645 -0.1005 -0.0322 0.0263  122 LEU B O   
3517 C CB  . LEU B 125 ? 0.5180 0.3914 0.4056 -0.0928 -0.0188 0.0374  122 LEU B CB  
3518 C CG  . LEU B 125 ? 0.5029 0.3872 0.3889 -0.0830 -0.0133 0.0390  122 LEU B CG  
3519 C CD1 . LEU B 125 ? 0.4831 0.3899 0.3779 -0.0809 -0.0122 0.0385  122 LEU B CD1 
3520 C CD2 . LEU B 125 ? 0.5231 0.4050 0.4071 -0.0833 -0.0087 0.0470  122 LEU B CD2 
3521 N N   . LYS B 126 ? 0.6125 0.4519 0.4992 -0.1151 -0.0291 0.0403  123 LYS B N   
3522 C CA  . LYS B 126 ? 0.6533 0.4816 0.5421 -0.1262 -0.0365 0.0386  123 LYS B CA  
3523 C C   . LYS B 126 ? 0.6417 0.4768 0.5317 -0.1242 -0.0412 0.0300  123 LYS B C   
3524 O O   . LYS B 126 ? 0.5907 0.4481 0.4892 -0.1217 -0.0389 0.0300  123 LYS B O   
3525 C CB  . LYS B 126 ? 0.6859 0.5276 0.5889 -0.1387 -0.0357 0.0479  123 LYS B CB  
3526 C CG  . LYS B 126 ? 0.7361 0.5690 0.6441 -0.1521 -0.0442 0.0470  123 LYS B CG  
3527 C CD  . LYS B 126 ? 0.7526 0.6129 0.6795 -0.1617 -0.0440 0.0524  123 LYS B CD  
3528 C CE  . LYS B 126 ? 0.7894 0.6463 0.7217 -0.1720 -0.0539 0.0477  123 LYS B CE  
3529 N NZ  . LYS B 126 ? 0.8296 0.6744 0.7668 -0.1875 -0.0582 0.0548  123 LYS B NZ  
3530 N N   . PRO B 127 ? 0.6754 0.4906 0.5560 -0.1250 -0.0481 0.0228  124 PRO B N   
3531 C CA  . PRO B 127 ? 0.6957 0.5157 0.5756 -0.1235 -0.0531 0.0149  124 PRO B CA  
3532 C C   . PRO B 127 ? 0.7407 0.5745 0.6349 -0.1354 -0.0578 0.0173  124 PRO B C   
3533 O O   . PRO B 127 ? 0.7557 0.5852 0.6560 -0.1462 -0.0597 0.0229  124 PRO B O   
3534 C CB  . PRO B 127 ? 0.7146 0.5078 0.5788 -0.1209 -0.0592 0.0072  124 PRO B CB  
3535 C CG  . PRO B 127 ? 0.7365 0.5094 0.5925 -0.1199 -0.0572 0.0108  124 PRO B CG  
3536 C CD  . PRO B 127 ? 0.7165 0.5025 0.5845 -0.1260 -0.0516 0.0215  124 PRO B CD  
3537 N N   . GLY B 128 ? 0.6447 0.6294 0.5211 -0.1155 -0.0552 0.0236  125 GLY B N   
3538 C CA  . GLY B 128 ? 0.7144 0.7461 0.6009 -0.1240 -0.0575 0.0329  125 GLY B CA  
3539 C C   . GLY B 128 ? 0.7423 0.8057 0.6419 -0.1042 -0.0548 0.0465  125 GLY B C   
3540 O O   . GLY B 128 ? 0.7580 0.8040 0.6576 -0.0871 -0.0512 0.0465  125 GLY B O   
3541 N N   . GLU B 129 ? 0.7968 0.9052 0.7086 -0.1060 -0.0551 0.0585  126 GLU B N   
3542 C CA  . GLU B 129 ? 0.8353 0.9787 0.7617 -0.0858 -0.0510 0.0744  126 GLU B CA  
3543 C C   . GLU B 129 ? 0.7897 0.9103 0.7242 -0.0651 -0.0409 0.0785  126 GLU B C   
3544 O O   . GLU B 129 ? 0.8088 0.9195 0.7486 -0.0466 -0.0348 0.0829  126 GLU B O   
3545 C CB  . GLU B 129 ? 0.9074 1.1133 0.8451 -0.0935 -0.0547 0.0866  126 GLU B CB  
3546 C CG  . GLU B 129 ? 0.9519 1.1993 0.9039 -0.0718 -0.0512 0.1060  126 GLU B CG  
3547 C CD  . GLU B 129 ? 0.9876 1.2187 0.9349 -0.0582 -0.0495 0.1076  126 GLU B CD  
3548 O OE1 . GLU B 129 ? 0.9906 1.2542 0.9323 -0.0658 -0.0565 0.1093  126 GLU B OE1 
3549 O OE2 . GLU B 129 ? 1.0035 1.1937 0.9532 -0.0407 -0.0406 0.1073  126 GLU B OE2 
3550 N N   . GLU B 130 ? 0.7417 0.8530 0.6761 -0.0695 -0.0384 0.0762  127 GLU B N   
3551 C CA  . GLU B 130 ? 0.7115 0.8099 0.6524 -0.0520 -0.0283 0.0775  127 GLU B CA  
3552 C C   . GLU B 130 ? 0.6741 0.7260 0.6051 -0.0460 -0.0262 0.0648  127 GLU B C   
3553 O O   . GLU B 130 ? 0.6311 0.6576 0.5486 -0.0579 -0.0320 0.0556  127 GLU B O   
3554 C CB  . GLU B 130 ? 0.7392 0.8502 0.6813 -0.0595 -0.0265 0.0796  127 GLU B CB  
3555 C CG  . GLU B 130 ? 0.7771 0.9407 0.7321 -0.0649 -0.0271 0.0927  127 GLU B CG  
3556 C CD  . GLU B 130 ? 0.8218 1.0200 0.7952 -0.0426 -0.0191 0.1061  127 GLU B CD  
3557 O OE1 . GLU B 130 ? 0.7964 1.0448 0.7809 -0.0462 -0.0222 0.1187  127 GLU B OE1 
3558 O OE2 . GLU B 130 ? 0.8443 1.0205 0.8220 -0.0217 -0.0088 0.1042  127 GLU B OE2 
3559 N N   . LEU B 131 ? 0.6199 0.6610 0.5586 -0.0281 -0.0168 0.0644  128 LEU B N   
3560 C CA  . LEU B 131 ? 0.5917 0.5961 0.5240 -0.0235 -0.0134 0.0513  128 LEU B CA  
3561 C C   . LEU B 131 ? 0.5675 0.5651 0.4926 -0.0274 -0.0124 0.0435  128 LEU B C   
3562 O O   . LEU B 131 ? 0.5144 0.4896 0.4297 -0.0302 -0.0149 0.0336  128 LEU B O   
3563 C CB  . LEU B 131 ? 0.5891 0.5836 0.5333 -0.0068 -0.0015 0.0517  128 LEU B CB  
3564 C CG  . LEU B 131 ? 0.5902 0.5927 0.5422 -0.0002 -0.0007 0.0638  128 LEU B CG  
3565 C CD1 . LEU B 131 ? 0.6063 0.5908 0.5713 0.0160  0.0139  0.0658  128 LEU B CD1 
3566 C CD2 . LEU B 131 ? 0.5818 0.5747 0.5214 -0.0110 -0.0108 0.0593  128 LEU B CD2 
3567 N N   . SER B 132 ? 0.6067 0.6277 0.5368 -0.0265 -0.0086 0.0491  129 SER B N   
3568 C CA  . SER B 132 ? 0.6443 0.6675 0.5661 -0.0316 -0.0082 0.0454  129 SER B CA  
3569 C C   . SER B 132 ? 0.6512 0.6950 0.5716 -0.0459 -0.0142 0.0565  129 SER B C   
3570 O O   . SER B 132 ? 0.6770 0.7516 0.6064 -0.0446 -0.0099 0.0646  129 SER B O   
3571 C CB  . SER B 132 ? 0.6892 0.7236 0.6168 -0.0196 0.0037  0.0403  129 SER B CB  
3572 O OG  . SER B 132 ? 0.7203 0.7333 0.6515 -0.0090 0.0115  0.0282  129 SER B OG  
3573 N N   . PRO B 133 ? 0.6293 0.6566 0.5399 -0.0603 -0.0228 0.0567  130 PRO B N   
3574 C CA  . PRO B 133 ? 0.6335 0.6749 0.5437 -0.0781 -0.0271 0.0653  130 PRO B CA  
3575 C C   . PRO B 133 ? 0.6384 0.6858 0.5444 -0.0806 -0.0232 0.0705  130 PRO B C   
3576 O O   . PRO B 133 ? 0.6259 0.6525 0.5219 -0.0760 -0.0227 0.0666  130 PRO B O   
3577 C CB  . PRO B 133 ? 0.6389 0.6495 0.5387 -0.0901 -0.0341 0.0598  130 PRO B CB  
3578 C CG  . PRO B 133 ? 0.6264 0.6071 0.5184 -0.0774 -0.0333 0.0511  130 PRO B CG  
3579 C CD  . PRO B 133 ? 0.6135 0.6071 0.5139 -0.0607 -0.0272 0.0480  130 PRO B CD  
3580 N N   . THR B 134 ? 0.6390 0.7205 0.5533 -0.0866 -0.0203 0.0804  131 THR B N   
3581 C CA  . THR B 134 ? 0.6568 0.7541 0.5684 -0.0882 -0.0150 0.0878  131 THR B CA  
3582 C C   . THR B 134 ? 0.6842 0.7965 0.5990 -0.1104 -0.0168 0.1003  131 THR B C   
3583 O O   . THR B 134 ? 0.6829 0.8160 0.6077 -0.1204 -0.0198 0.1025  131 THR B O   
3584 C CB  . THR B 134 ? 0.6661 0.7931 0.5857 -0.0708 -0.0057 0.0859  131 THR B CB  
3585 O OG1 . THR B 134 ? 0.6740 0.8355 0.6097 -0.0704 -0.0040 0.0930  131 THR B OG1 
3586 C CG2 . THR B 134 ? 0.6606 0.7660 0.5774 -0.0532 -0.0024 0.0711  131 THR B CG2 
3587 N N   . ASP B 135 ? 0.7186 0.8216 0.6252 -0.1187 -0.0148 0.1088  132 ASP B N   
3588 C CA  . ASP B 135 ? 0.7711 0.8855 0.6812 -0.1416 -0.0135 0.1227  132 ASP B CA  
3589 C C   . ASP B 135 ? 0.7758 0.9451 0.6978 -0.1403 -0.0073 0.1318  132 ASP B C   
3590 O O   . ASP B 135 ? 0.7305 0.9231 0.6576 -0.1204 -0.0036 0.1260  132 ASP B O   
3591 C CB  . ASP B 135 ? 0.7988 0.8808 0.6966 -0.1468 -0.0113 0.1323  132 ASP B CB  
3592 C CG  . ASP B 135 ? 0.8105 0.9097 0.7007 -0.1315 -0.0056 0.1397  132 ASP B CG  
3593 O OD1 . ASP B 135 ? 0.8017 0.9404 0.6968 -0.1208 -0.0014 0.1371  132 ASP B OD1 
3594 O OD2 . ASP B 135 ? 0.8606 0.9358 0.7398 -0.1297 -0.0046 0.1482  132 ASP B OD2 
3595 N N   . GLU B 136 ? 0.8512 1.0385 0.7778 -0.1609 -0.0046 0.1459  133 GLU B N   
3596 C CA  . GLU B 136 ? 0.8930 1.1363 0.8310 -0.1629 0.0025  0.1579  133 GLU B CA  
3597 C C   . GLU B 136 ? 0.8730 1.1347 0.8048 -0.1389 0.0104  0.1575  133 GLU B C   
3598 O O   . GLU B 136 ? 0.8699 1.1801 0.8125 -0.1305 0.0172  0.1605  133 GLU B O   
3599 C CB  . GLU B 136 ? 0.9903 1.2363 0.9301 -0.1910 0.0053  0.1746  133 GLU B CB  
3600 C CG  . GLU B 136 ? 1.0654 1.2761 1.0060 -0.2180 -0.0005 0.1709  133 GLU B CG  
3601 C CD  . GLU B 136 ? 1.1211 1.2647 1.0462 -0.2194 -0.0013 0.1690  133 GLU B CD  
3602 O OE1 . GLU B 136 ? 1.1900 1.3137 1.1110 -0.2316 0.0051  0.1847  133 GLU B OE1 
3603 O OE2 . GLU B 136 ? 1.1215 1.2341 1.0397 -0.2073 -0.0073 0.1537  133 GLU B OE2 
3604 N N   . ASN B 137 ? 0.8546 1.0840 0.7698 -0.1283 0.0103  0.1534  134 ASN B N   
3605 C CA  . ASN B 137 ? 0.8537 1.1047 0.7597 -0.1103 0.0177  0.1516  134 ASN B CA  
3606 C C   . ASN B 137 ? 0.8044 1.0427 0.7071 -0.0882 0.0178  0.1296  134 ASN B C   
3607 O O   . ASN B 137 ? 0.8218 1.0692 0.7138 -0.0752 0.0228  0.1219  134 ASN B O   
3608 C CB  . ASN B 137 ? 0.8865 1.1239 0.7770 -0.1155 0.0185  0.1654  134 ASN B CB  
3609 C CG  . ASN B 137 ? 0.9371 1.1835 0.8336 -0.1389 0.0212  0.1883  134 ASN B CG  
3610 O OD1 . ASN B 137 ? 0.9833 1.1902 0.8776 -0.1537 0.0179  0.1969  134 ASN B OD1 
3611 N ND2 . ASN B 137 ? 0.9327 1.2296 0.8383 -0.1429 0.0286  0.1974  134 ASN B ND2 
3612 N N   . GLY B 138 ? 0.7597 0.9807 0.6715 -0.0855 0.0131  0.1201  135 GLY B N   
3613 C CA  . GLY B 138 ? 0.7327 0.9342 0.6436 -0.0672 0.0138  0.1011  135 GLY B CA  
3614 C C   . GLY B 138 ? 0.7095 0.8746 0.6043 -0.0651 0.0087  0.0930  135 GLY B C   
3615 O O   . GLY B 138 ? 0.6682 0.8221 0.5601 -0.0514 0.0112  0.0759  135 GLY B O   
3616 N N   . LYS B 139 ? 0.7216 0.8691 0.6077 -0.0780 0.0031  0.1051  136 LYS B N   
3617 C CA  . LYS B 139 ? 0.7216 0.8355 0.5949 -0.0748 -0.0023 0.1010  136 LYS B CA  
3618 C C   . LYS B 139 ? 0.6743 0.7537 0.5522 -0.0763 -0.0090 0.0919  136 LYS B C   
3619 O O   . LYS B 139 ? 0.6418 0.7122 0.5259 -0.0895 -0.0123 0.0981  136 LYS B O   
3620 C CB  . LYS B 139 ? 0.7865 0.8945 0.6505 -0.0838 -0.0030 0.1206  136 LYS B CB  
3621 C CG  . LYS B 139 ? 0.8485 0.9964 0.7056 -0.0804 0.0038  0.1304  136 LYS B CG  
3622 C CD  . LYS B 139 ? 0.8577 1.0274 0.7073 -0.0642 0.0068  0.1114  136 LYS B CD  
3623 C CE  . LYS B 139 ? 0.9099 1.1240 0.7492 -0.0605 0.0136  0.1177  136 LYS B CE  
3624 N NZ  . LYS B 139 ? 0.9124 1.1612 0.7601 -0.0581 0.0227  0.1112  136 LYS B NZ  
3625 N N   . VAL B 140 ? 0.6464 0.7115 0.5208 -0.0642 -0.0102 0.0766  137 VAL B N   
3626 C CA  . VAL B 140 ? 0.6244 0.6580 0.5006 -0.0627 -0.0158 0.0671  137 VAL B CA  
3627 C C   . VAL B 140 ? 0.6128 0.6170 0.4820 -0.0717 -0.0215 0.0756  137 VAL B C   
3628 O O   . VAL B 140 ? 0.6086 0.6100 0.4687 -0.0698 -0.0212 0.0836  137 VAL B O   
3629 C CB  . VAL B 140 ? 0.6346 0.6624 0.5079 -0.0500 -0.0144 0.0506  137 VAL B CB  
3630 C CG1 . VAL B 140 ? 0.6339 0.6325 0.5089 -0.0488 -0.0194 0.0430  137 VAL B CG1 
3631 C CG2 . VAL B 140 ? 0.6488 0.6976 0.5297 -0.0410 -0.0054 0.0401  137 VAL B CG2 
3632 N N   . ILE B 141 ? 0.5870 0.5714 0.4601 -0.0801 -0.0255 0.0735  138 ILE B N   
3633 C CA  . ILE B 141 ? 0.6090 0.5600 0.4764 -0.0898 -0.0284 0.0783  138 ILE B CA  
3634 C C   . ILE B 141 ? 0.5808 0.5061 0.4433 -0.0796 -0.0316 0.0675  138 ILE B C   
3635 O O   . ILE B 141 ? 0.5658 0.4913 0.4326 -0.0760 -0.0338 0.0558  138 ILE B O   
3636 C CB  . ILE B 141 ? 0.6408 0.5900 0.5141 -0.1086 -0.0299 0.0791  138 ILE B CB  
3637 C CG1 . ILE B 141 ? 0.6682 0.6502 0.5487 -0.1196 -0.0265 0.0905  138 ILE B CG1 
3638 C CG2 . ILE B 141 ? 0.6850 0.5933 0.5518 -0.1196 -0.0302 0.0798  138 ILE B CG2 
3639 C CD1 . ILE B 141 ? 0.6846 0.6836 0.5744 -0.1365 -0.0292 0.0881  138 ILE B CD1 
3640 N N   . PHE B 142 ? 0.5836 0.4914 0.4384 -0.0737 -0.0312 0.0737  139 PHE B N   
3641 C CA  . PHE B 142 ? 0.5706 0.4591 0.4213 -0.0623 -0.0335 0.0661  139 PHE B CA  
3642 C C   . PHE B 142 ? 0.5929 0.4465 0.4425 -0.0699 -0.0340 0.0624  139 PHE B C   
3643 O O   . PHE B 142 ? 0.6210 0.4637 0.4715 -0.0854 -0.0322 0.0667  139 PHE B O   
3644 C CB  . PHE B 142 ? 0.5947 0.4859 0.4389 -0.0513 -0.0322 0.0777  139 PHE B CB  
3645 C CG  . PHE B 142 ? 0.5837 0.5134 0.4258 -0.0456 -0.0314 0.0798  139 PHE B CG  
3646 C CD1 . PHE B 142 ? 0.5599 0.5135 0.4069 -0.0471 -0.0304 0.0675  139 PHE B CD1 
3647 C CD2 . PHE B 142 ? 0.6091 0.5529 0.4442 -0.0372 -0.0305 0.0936  139 PHE B CD2 
3648 C CE1 . PHE B 142 ? 0.5628 0.5502 0.4065 -0.0424 -0.0279 0.0653  139 PHE B CE1 
3649 C CE2 . PHE B 142 ? 0.6128 0.5975 0.4438 -0.0331 -0.0298 0.0927  139 PHE B CE2 
3650 C CZ  . PHE B 142 ? 0.5874 0.5923 0.4221 -0.0365 -0.0281 0.0763  139 PHE B CZ  
3651 N N   . ASP B 143 ? 0.5801 0.4187 0.4275 -0.0602 -0.0356 0.0537  140 ASP B N   
3652 C CA  . ASP B 143 ? 0.6063 0.4100 0.4503 -0.0632 -0.0344 0.0477  140 ASP B CA  
3653 C C   . ASP B 143 ? 0.6088 0.3991 0.4496 -0.0457 -0.0328 0.0513  140 ASP B C   
3654 O O   . ASP B 143 ? 0.5837 0.3991 0.4257 -0.0335 -0.0351 0.0524  140 ASP B O   
3655 C CB  . ASP B 143 ? 0.5932 0.4019 0.4393 -0.0684 -0.0377 0.0321  140 ASP B CB  
3656 C CG  . ASP B 143 ? 0.6328 0.4122 0.4737 -0.0767 -0.0361 0.0219  140 ASP B CG  
3657 O OD1 . ASP B 143 ? 0.6962 0.4458 0.5335 -0.0838 -0.0312 0.0259  140 ASP B OD1 
3658 O OD2 . ASP B 143 ? 0.5956 0.3817 0.4360 -0.0763 -0.0386 0.0099  140 ASP B OD2 
3659 N N   . ILE B 144 ? 0.6542 0.4080 0.4916 -0.0445 -0.0281 0.0517  141 ILE B N   
3660 C CA  . ILE B 144 ? 0.6767 0.4185 0.5128 -0.0246 -0.0252 0.0571  141 ILE B CA  
3661 C C   . ILE B 144 ? 0.6642 0.3925 0.4993 -0.0223 -0.0251 0.0390  141 ILE B C   
3662 O O   . ILE B 144 ? 0.6701 0.3682 0.5015 -0.0334 -0.0212 0.0293  141 ILE B O   
3663 C CB  . ILE B 144 ? 0.7607 0.4687 0.5949 -0.0203 -0.0165 0.0751  141 ILE B CB  
3664 C CG1 . ILE B 144 ? 0.7800 0.5066 0.6146 -0.0229 -0.0159 0.0959  141 ILE B CG1 
3665 C CG2 . ILE B 144 ? 0.7898 0.4876 0.6246 0.0035  -0.0125 0.0814  141 ILE B CG2 
3666 C CD1 . ILE B 144 ? 0.8542 0.5448 0.6885 -0.0368 -0.0073 0.1080  141 ILE B CD1 
3667 N N   . VAL B 145 ? 0.6300 0.3830 0.4680 -0.0109 -0.0290 0.0331  142 VAL B N   
3668 C CA  . VAL B 145 ? 0.6319 0.3788 0.4692 -0.0078 -0.0286 0.0175  142 VAL B CA  
3669 C C   . VAL B 145 ? 0.6235 0.3847 0.4646 0.0123  -0.0281 0.0213  142 VAL B C   
3670 O O   . VAL B 145 ? 0.5808 0.3754 0.4265 0.0170  -0.0325 0.0263  142 VAL B O   
3671 C CB  . VAL B 145 ? 0.5912 0.3609 0.4306 -0.0188 -0.0337 0.0056  142 VAL B CB  
3672 C CG1 . VAL B 145 ? 0.5974 0.3644 0.4352 -0.0155 -0.0325 -0.0077 142 VAL B CG1 
3673 C CG2 . VAL B 145 ? 0.6011 0.3687 0.4389 -0.0374 -0.0351 0.0047  142 VAL B CG2 
3674 N N   . ASP B 146 ? 0.6559 0.3950 0.4955 0.0232  -0.0222 0.0175  143 ASP B N   
3675 C CA  . ASP B 146 ? 0.6547 0.4140 0.4997 0.0421  -0.0216 0.0184  143 ASP B CA  
3676 C C   . ASP B 146 ? 0.5861 0.3775 0.4352 0.0353  -0.0272 0.0057  143 ASP B C   
3677 O O   . ASP B 146 ? 0.5615 0.3442 0.4073 0.0267  -0.0263 -0.0075 143 ASP B O   
3678 C CB  . ASP B 146 ? 0.7300 0.4564 0.5724 0.0548  -0.0121 0.0144  143 ASP B CB  
3679 C CG  . ASP B 146 ? 0.7478 0.4994 0.5973 0.0755  -0.0106 0.0158  143 ASP B CG  
3680 O OD1 . ASP B 146 ? 0.7016 0.4971 0.5583 0.0784  -0.0175 0.0212  143 ASP B OD1 
3681 O OD2 . ASP B 146 ? 0.8283 0.5564 0.6765 0.0879  -0.0017 0.0105  143 ASP B OD2 
3682 N N   . LEU B 147 ? 0.5536 0.3818 0.4095 0.0375  -0.0321 0.0092  144 LEU B N   
3683 C CA  . LEU B 147 ? 0.5092 0.3620 0.3708 0.0281  -0.0352 -0.0021 144 LEU B CA  
3684 C C   . LEU B 147 ? 0.5047 0.3658 0.3702 0.0360  -0.0323 -0.0092 144 LEU B C   
3685 O O   . LEU B 147 ? 0.4477 0.3216 0.3173 0.0277  -0.0327 -0.0171 144 LEU B O   
3686 C CB  . LEU B 147 ? 0.4855 0.3726 0.3534 0.0249  -0.0394 -0.0003 144 LEU B CB  
3687 C CG  . LEU B 147 ? 0.4856 0.3718 0.3499 0.0160  -0.0415 0.0041  144 LEU B CG  
3688 C CD1 . LEU B 147 ? 0.4699 0.3923 0.3392 0.0131  -0.0441 0.0010  144 LEU B CD1 
3689 C CD2 . LEU B 147 ? 0.4820 0.3512 0.3447 0.0028  -0.0408 -0.0013 144 LEU B CD2 
3690 N N   . CYS B 148 ? 0.5475 0.4023 0.4128 0.0527  -0.0281 -0.0047 145 CYS B N   
3691 C CA  . CYS B 148 ? 0.5740 0.4363 0.4425 0.0619  -0.0236 -0.0120 145 CYS B CA  
3692 C C   . CYS B 148 ? 0.5690 0.4065 0.4286 0.0526  -0.0202 -0.0244 145 CYS B C   
3693 O O   . CYS B 148 ? 0.5666 0.4187 0.4282 0.0535  -0.0177 -0.0321 145 CYS B O   
3694 C CB  . CYS B 148 ? 0.6246 0.4818 0.4948 0.0848  -0.0177 -0.0037 145 CYS B CB  
3695 S SG  . CYS B 148 ? 0.6463 0.5554 0.5290 0.0974  -0.0227 0.0111  145 CYS B SG  
3696 N N   . THR B 149 ? 0.5818 0.3865 0.4317 0.0442  -0.0195 -0.0259 146 THR B N   
3697 C CA  . THR B 149 ? 0.5879 0.3755 0.4278 0.0324  -0.0174 -0.0391 146 THR B CA  
3698 C C   . THR B 149 ? 0.5321 0.3443 0.3752 0.0178  -0.0232 -0.0398 146 THR B C   
3699 O O   . THR B 149 ? 0.5316 0.3543 0.3720 0.0140  -0.0218 -0.0470 146 THR B O   
3700 C CB  . THR B 149 ? 0.6241 0.3724 0.4539 0.0248  -0.0143 -0.0424 146 THR B CB  
3701 O OG1 . THR B 149 ? 0.5919 0.3407 0.4231 0.0125  -0.0200 -0.0339 146 THR B OG1 
3702 C CG2 . THR B 149 ? 0.6863 0.4040 0.5152 0.0417  -0.0054 -0.0393 146 THR B CG2 
3703 N N   . THR B 150 ? 0.4943 0.3165 0.3433 0.0118  -0.0282 -0.0314 147 THR B N   
3704 C CA  . THR B 150 ? 0.4604 0.3020 0.3150 0.0011  -0.0312 -0.0304 147 THR B CA  
3705 C C   . THR B 150 ? 0.4422 0.3062 0.3050 0.0052  -0.0287 -0.0324 147 THR B C   
3706 O O   . THR B 150 ? 0.4364 0.3093 0.2995 -0.0005 -0.0271 -0.0337 147 THR B O   
3707 C CB  . THR B 150 ? 0.4410 0.2882 0.3010 -0.0031 -0.0345 -0.0233 147 THR B CB  
3708 O OG1 . THR B 150 ? 0.4600 0.2879 0.3131 -0.0060 -0.0356 -0.0195 147 THR B OG1 
3709 C CG2 . THR B 150 ? 0.4168 0.2758 0.2826 -0.0122 -0.0348 -0.0221 147 THR B CG2 
3710 N N   . TRP B 151 ? 0.4483 0.3249 0.3180 0.0145  -0.0282 -0.0310 148 TRP B N   
3711 C CA  . TRP B 151 ? 0.4457 0.3480 0.3253 0.0169  -0.0254 -0.0331 148 TRP B CA  
3712 C C   . TRP B 151 ? 0.4645 0.3669 0.3388 0.0206  -0.0207 -0.0381 148 TRP B C   
3713 O O   . TRP B 151 ? 0.4630 0.3818 0.3430 0.0147  -0.0180 -0.0378 148 TRP B O   
3714 C CB  . TRP B 151 ? 0.4493 0.3727 0.3370 0.0263  -0.0265 -0.0307 148 TRP B CB  
3715 C CG  . TRP B 151 ? 0.4325 0.3861 0.3327 0.0225  -0.0239 -0.0337 148 TRP B CG  
3716 C CD1 . TRP B 151 ? 0.4489 0.4216 0.3538 0.0312  -0.0201 -0.0350 148 TRP B CD1 
3717 C CD2 . TRP B 151 ? 0.4092 0.3736 0.3192 0.0073  -0.0228 -0.0361 148 TRP B CD2 
3718 N NE1 . TRP B 151 ? 0.4387 0.4368 0.3563 0.0207  -0.0175 -0.0372 148 TRP B NE1 
3719 C CE2 . TRP B 151 ? 0.4160 0.4066 0.3372 0.0055  -0.0185 -0.0383 148 TRP B CE2 
3720 C CE3 . TRP B 151 ? 0.3852 0.3390 0.2968 -0.0043 -0.0233 -0.0368 148 TRP B CE3 
3721 C CZ2 . TRP B 151 ? 0.4087 0.4112 0.3428 -0.0098 -0.0144 -0.0413 148 TRP B CZ2 
3722 C CZ3 . TRP B 151 ? 0.3849 0.3479 0.3088 -0.0167 -0.0184 -0.0404 148 TRP B CZ3 
3723 C CH2 . TRP B 151 ? 0.3934 0.3780 0.3285 -0.0206 -0.0138 -0.0426 148 TRP B CH2 
3724 N N   . GLU B 152 ? 0.5019 0.3854 0.3655 0.0291  -0.0183 -0.0427 149 GLU B N   
3725 C CA  . GLU B 152 ? 0.5312 0.4166 0.3872 0.0323  -0.0127 -0.0511 149 GLU B CA  
3726 C C   . GLU B 152 ? 0.5040 0.3941 0.3540 0.0182  -0.0139 -0.0521 149 GLU B C   
3727 O O   . GLU B 152 ? 0.4913 0.4014 0.3412 0.0180  -0.0101 -0.0532 149 GLU B O   
3728 C CB  . GLU B 152 ? 0.6025 0.4596 0.4467 0.0423  -0.0078 -0.0598 149 GLU B CB  
3729 C CG  . GLU B 152 ? 0.6517 0.5105 0.5032 0.0621  -0.0034 -0.0561 149 GLU B CG  
3730 C CD  . GLU B 152 ? 0.7456 0.5671 0.5887 0.0751  0.0039  -0.0609 149 GLU B CD  
3731 O OE1 . GLU B 152 ? 0.7960 0.6219 0.6466 0.0952  0.0088  -0.0547 149 GLU B OE1 
3732 O OE2 . GLU B 152 ? 0.8052 0.5943 0.6351 0.0650  0.0057  -0.0707 149 GLU B OE2 
3733 N N   . ALA B 153 ? 0.4889 0.3661 0.3347 0.0078  -0.0186 -0.0497 150 ALA B N   
3734 C CA  . ALA B 153 ? 0.4834 0.3718 0.3250 -0.0036 -0.0203 -0.0471 150 ALA B CA  
3735 C C   . ALA B 153 ? 0.4507 0.3600 0.3063 -0.0061 -0.0189 -0.0352 150 ALA B C   
3736 O O   . ALA B 153 ? 0.4402 0.3670 0.2944 -0.0091 -0.0165 -0.0305 150 ALA B O   
3737 C CB  . ALA B 153 ? 0.4880 0.3623 0.3239 -0.0131 -0.0252 -0.0467 150 ALA B CB  
3738 N N   . MET B 154 ? 0.4312 0.3394 0.2997 -0.0051 -0.0192 -0.0309 151 MET B N   
3739 C CA  . MET B 154 ? 0.4198 0.3420 0.3035 -0.0087 -0.0149 -0.0236 151 MET B CA  
3740 C C   . MET B 154 ? 0.4344 0.3759 0.3213 -0.0056 -0.0092 -0.0239 151 MET B C   
3741 O O   . MET B 154 ? 0.4267 0.3797 0.3200 -0.0098 -0.0040 -0.0152 151 MET B O   
3742 C CB  . MET B 154 ? 0.4063 0.3267 0.3009 -0.0097 -0.0160 -0.0255 151 MET B CB  
3743 C CG  . MET B 154 ? 0.3986 0.3043 0.2909 -0.0127 -0.0203 -0.0244 151 MET B CG  
3744 S SD  . MET B 154 ? 0.3992 0.3013 0.2986 -0.0194 -0.0164 -0.0152 151 MET B SD  
3745 C CE  . MET B 154 ? 0.3913 0.2983 0.3083 -0.0247 -0.0092 -0.0187 151 MET B CE  
3746 N N   . GLU B 155 ? 0.4532 0.3991 0.3367 0.0030  -0.0090 -0.0318 152 GLU B N   
3747 C CA  . GLU B 155 ? 0.4684 0.4378 0.3559 0.0072  -0.0028 -0.0325 152 GLU B CA  
3748 C C   . GLU B 155 ? 0.4932 0.4712 0.3694 0.0056  0.0005  -0.0303 152 GLU B C   
3749 O O   . GLU B 155 ? 0.4949 0.4954 0.3779 0.0032  0.0068  -0.0229 152 GLU B O   
3750 C CB  . GLU B 155 ? 0.4867 0.4590 0.3713 0.0208  -0.0023 -0.0409 152 GLU B CB  
3751 C CG  . GLU B 155 ? 0.4809 0.4592 0.3777 0.0239  -0.0054 -0.0400 152 GLU B CG  
3752 C CD  . GLU B 155 ? 0.5101 0.4945 0.4063 0.0414  -0.0041 -0.0434 152 GLU B CD  
3753 O OE1 . GLU B 155 ? 0.5392 0.5044 0.4221 0.0513  -0.0013 -0.0492 152 GLU B OE1 
3754 O OE2 . GLU B 155 ? 0.5121 0.5224 0.4217 0.0451  -0.0049 -0.0408 152 GLU B OE2 
3755 N N   . LYS B 156 ? 0.5110 0.4752 0.3708 0.0052  -0.0033 -0.0362 153 LYS B N   
3756 C CA  . LYS B 156 ? 0.5529 0.5334 0.3994 0.0023  -0.0013 -0.0360 153 LYS B CA  
3757 C C   . LYS B 156 ? 0.5218 0.5169 0.3770 -0.0048 -0.0001 -0.0176 153 LYS B C   
3758 O O   . LYS B 156 ? 0.5283 0.5492 0.3800 -0.0051 0.0046  -0.0099 153 LYS B O   
3759 C CB  . LYS B 156 ? 0.6115 0.5760 0.4390 0.0006  -0.0052 -0.0506 153 LYS B CB  
3760 C CG  . LYS B 156 ? 0.6860 0.6408 0.5056 0.0111  -0.0003 -0.0672 153 LYS B CG  
3761 C CD  . LYS B 156 ? 0.7590 0.6776 0.5705 0.0134  -0.0016 -0.0803 153 LYS B CD  
3762 C CE  . LYS B 156 ? 0.8267 0.7344 0.6352 0.0290  0.0065  -0.0926 153 LYS B CE  
3763 N NZ  . LYS B 156 ? 0.8331 0.7285 0.6562 0.0408  0.0060  -0.0847 153 LYS B NZ  
3764 N N   . CYS B 157 ? 0.6036 0.4844 0.3806 0.0045  -0.0224 -0.0523 154 CYS B N   
3765 C CA  . CYS B 157 ? 0.5787 0.4687 0.3593 -0.0048 -0.0209 -0.0443 154 CYS B CA  
3766 C C   . CYS B 157 ? 0.5646 0.4768 0.3476 -0.0036 -0.0124 -0.0374 154 CYS B C   
3767 O O   . CYS B 157 ? 0.5564 0.4777 0.3331 -0.0062 -0.0108 -0.0336 154 CYS B O   
3768 C CB  . CYS B 157 ? 0.5617 0.4443 0.3547 -0.0148 -0.0241 -0.0388 154 CYS B CB  
3769 S SG  . CYS B 157 ? 0.5881 0.4494 0.3781 -0.0192 -0.0340 -0.0449 154 CYS B SG  
3770 N N   . LYS B 158 ? 0.5546 0.4756 0.3449 0.0007  -0.0077 -0.0361 155 LYS B N   
3771 C CA  . LYS B 158 ? 0.5513 0.4955 0.3464 0.0004  0.0001  -0.0288 155 LYS B CA  
3772 C C   . LYS B 158 ? 0.5848 0.5423 0.3667 0.0093  0.0047  -0.0333 155 LYS B C   
3773 O O   . LYS B 158 ? 0.5794 0.5522 0.3589 0.0052  0.0091  -0.0262 155 LYS B O   
3774 C CB  . LYS B 158 ? 0.5308 0.4821 0.3394 0.0017  0.0031  -0.0259 155 LYS B CB  
3775 C CG  . LYS B 158 ? 0.5350 0.5124 0.3488 0.0033  0.0110  -0.0202 155 LYS B CG  
3776 C CD  . LYS B 158 ? 0.5215 0.5046 0.3510 0.0016  0.0119  -0.0159 155 LYS B CD  
3777 C CE  . LYS B 158 ? 0.5371 0.5479 0.3741 0.0039  0.0192  -0.0113 155 LYS B CE  
3778 N NZ  . LYS B 158 ? 0.5368 0.5605 0.3766 -0.0071 0.0221  -0.0002 155 LYS B NZ  
3779 N N   . ASP B 159 ? 0.6149 0.5650 0.3876 0.0206  0.0027  -0.0445 156 ASP B N   
3780 C CA  . ASP B 159 ? 0.6696 0.6317 0.4272 0.0314  0.0066  -0.0511 156 ASP B CA  
3781 C C   . ASP B 159 ? 0.6718 0.6323 0.4166 0.0265  0.0048  -0.0493 156 ASP B C   
3782 O O   . ASP B 159 ? 0.6885 0.6683 0.4242 0.0295  0.0111  -0.0471 156 ASP B O   
3783 C CB  . ASP B 159 ? 0.7162 0.6640 0.4641 0.0450  0.0017  -0.0653 156 ASP B CB  
3784 C CG  . ASP B 159 ? 0.7409 0.6923 0.4980 0.0537  0.0034  -0.0685 156 ASP B CG  
3785 O OD1 . ASP B 159 ? 0.7440 0.7206 0.5113 0.0544  0.0117  -0.0623 156 ASP B OD1 
3786 O OD2 . ASP B 159 ? 0.7820 0.7107 0.5364 0.0592  -0.0042 -0.0769 156 ASP B OD2 
3787 N N   . ALA B 160 ? 0.6607 0.6003 0.4045 0.0192  -0.0036 -0.0501 157 ALA B N   
3788 C CA  . ALA B 160 ? 0.6662 0.6019 0.3978 0.0151  -0.0073 -0.0495 157 ALA B CA  
3789 C C   . ALA B 160 ? 0.6437 0.5927 0.3808 0.0050  -0.0034 -0.0361 157 ALA B C   
3790 O O   . ALA B 160 ? 0.6498 0.5980 0.3764 0.0021  -0.0059 -0.0341 157 ALA B O   
3791 C CB  . ALA B 160 ? 0.6642 0.5762 0.3958 0.0106  -0.0178 -0.0545 157 ALA B CB  
3792 N N   . GLY B 161 ? 0.6081 0.5673 0.3604 -0.0002 0.0014  -0.0274 158 GLY B N   
3793 C CA  . GLY B 161 ? 0.5975 0.5654 0.3555 -0.0105 0.0032  -0.0146 158 GLY B CA  
3794 C C   . GLY B 161 ? 0.5765 0.5278 0.3400 -0.0190 -0.0047 -0.0119 158 GLY B C   
3795 O O   . GLY B 161 ? 0.5779 0.5325 0.3435 -0.0267 -0.0053 -0.0023 158 GLY B O   
3796 N N   . LEU B 162 ? 0.5573 0.4920 0.3245 -0.0182 -0.0108 -0.0193 159 LEU B N   
3797 C CA  . LEU B 162 ? 0.5280 0.4508 0.3026 -0.0259 -0.0176 -0.0169 159 LEU B CA  
3798 C C   . LEU B 162 ? 0.4914 0.4163 0.2820 -0.0313 -0.0159 -0.0101 159 LEU B C   
3799 O O   . LEU B 162 ? 0.4632 0.3838 0.2596 -0.0373 -0.0200 -0.0056 159 LEU B O   
3800 C CB  . LEU B 162 ? 0.5399 0.4470 0.3136 -0.0243 -0.0241 -0.0262 159 LEU B CB  
3801 C CG  . LEU B 162 ? 0.5845 0.4861 0.3422 -0.0192 -0.0281 -0.0344 159 LEU B CG  
3802 C CD1 . LEU B 162 ? 0.5969 0.4820 0.3566 -0.0201 -0.0358 -0.0423 159 LEU B CD1 
3803 C CD2 . LEU B 162 ? 0.6026 0.5071 0.3515 -0.0220 -0.0310 -0.0309 159 LEU B CD2 
3804 N N   . ALA B 163 ? 0.4780 0.4084 0.2752 -0.0280 -0.0112 -0.0106 160 ALA B N   
3805 C CA  . ALA B 163 ? 0.4588 0.3930 0.2700 -0.0322 -0.0094 -0.0043 160 ALA B CA  
3806 C C   . ALA B 163 ? 0.4688 0.4208 0.2824 -0.0304 -0.0024 0.0004  160 ALA B C   
3807 O O   . ALA B 163 ? 0.4869 0.4451 0.2963 -0.0226 0.0014  -0.0050 160 ALA B O   
3808 C CB  . ALA B 163 ? 0.4453 0.3691 0.2635 -0.0305 -0.0115 -0.0094 160 ALA B CB  
3809 N N   . LYS B 164 ? 0.4611 0.4213 0.2815 -0.0372 -0.0013 0.0100  161 LYS B N   
3810 C CA  . LYS B 164 ? 0.4785 0.4581 0.3040 -0.0375 0.0052  0.0158  161 LYS B CA  
3811 C C   . LYS B 164 ? 0.4540 0.4357 0.2905 -0.0330 0.0068  0.0122  161 LYS B C   
3812 O O   . LYS B 164 ? 0.4650 0.4619 0.3028 -0.0268 0.0123  0.0103  161 LYS B O   
3813 C CB  . LYS B 164 ? 0.4963 0.4814 0.3273 -0.0475 0.0042  0.0276  161 LYS B CB  
3814 C CG  . LYS B 164 ? 0.5358 0.5200 0.3554 -0.0523 0.0025  0.0334  161 LYS B CG  
3815 C CD  . LYS B 164 ? 0.5870 0.5832 0.3928 -0.0470 0.0081  0.0314  161 LYS B CD  
3816 C CE  . LYS B 164 ? 0.6166 0.6133 0.4102 -0.0526 0.0066  0.0392  161 LYS B CE  
3817 N NZ  . LYS B 164 ? 0.6642 0.6796 0.4459 -0.0483 0.0143  0.0397  161 LYS B NZ  
3818 N N   . SER B 165 ? 0.4232 0.3910 0.2670 -0.0354 0.0019  0.0110  162 SER B N   
3819 C CA  . SER B 165 ? 0.4083 0.3751 0.2615 -0.0318 0.0019  0.0083  162 SER B CA  
3820 C C   . SER B 165 ? 0.3925 0.3401 0.2438 -0.0302 -0.0029 0.0021  162 SER B C   
3821 O O   . SER B 165 ? 0.3841 0.3214 0.2315 -0.0343 -0.0067 0.0019  162 SER B O   
3822 C CB  . SER B 165 ? 0.3976 0.3705 0.2630 -0.0382 0.0010  0.0159  162 SER B CB  
3823 O OG  . SER B 165 ? 0.4084 0.4006 0.2768 -0.0408 0.0055  0.0224  162 SER B OG  
3824 N N   . ILE B 166 ? 0.3963 0.3403 0.2508 -0.0246 -0.0029 -0.0021 163 ILE B N   
3825 C CA  . ILE B 166 ? 0.3884 0.3145 0.2419 -0.0243 -0.0074 -0.0063 163 ILE B CA  
3826 C C   . ILE B 166 ? 0.3758 0.3009 0.2384 -0.0242 -0.0083 -0.0041 163 ILE B C   
3827 O O   . ILE B 166 ? 0.3667 0.3034 0.2350 -0.0202 -0.0058 -0.0030 163 ILE B O   
3828 C CB  . ILE B 166 ? 0.4137 0.3304 0.2576 -0.0173 -0.0086 -0.0145 163 ILE B CB  
3829 C CG1 . ILE B 166 ? 0.4329 0.3589 0.2761 -0.0074 -0.0052 -0.0183 163 ILE B CG1 
3830 C CG2 . ILE B 166 ? 0.4203 0.3354 0.2546 -0.0187 -0.0094 -0.0168 163 ILE B CG2 
3831 C CD1 . ILE B 166 ? 0.4684 0.3829 0.3009 0.0007  -0.0077 -0.0274 163 ILE B CD1 
3832 N N   . GLY B 167 ? 0.3688 0.2817 0.2326 -0.0281 -0.0120 -0.0037 164 GLY B N   
3833 C CA  . GLY B 167 ? 0.3625 0.2726 0.2324 -0.0282 -0.0135 -0.0016 164 GLY B CA  
3834 C C   . GLY B 167 ? 0.3629 0.2585 0.2299 -0.0310 -0.0168 -0.0027 164 GLY B C   
3835 O O   . GLY B 167 ? 0.3609 0.2484 0.2220 -0.0322 -0.0182 -0.0058 164 GLY B O   
3836 N N   . VAL B 168 ? 0.3624 0.2556 0.2334 -0.0321 -0.0182 0.0000  165 VAL B N   
3837 C CA  . VAL B 168 ? 0.3708 0.2523 0.2390 -0.0353 -0.0206 0.0003  165 VAL B CA  
3838 C C   . VAL B 168 ? 0.3607 0.2463 0.2330 -0.0393 -0.0212 0.0040  165 VAL B C   
3839 O O   . VAL B 168 ? 0.3483 0.2427 0.2253 -0.0392 -0.0209 0.0058  165 VAL B O   
3840 C CB  . VAL B 168 ? 0.3896 0.2607 0.2546 -0.0309 -0.0225 -0.0007 165 VAL B CB  
3841 C CG1 . VAL B 168 ? 0.4111 0.2764 0.2706 -0.0252 -0.0231 -0.0059 165 VAL B CG1 
3842 C CG2 . VAL B 168 ? 0.3866 0.2634 0.2564 -0.0271 -0.0226 0.0016  165 VAL B CG2 
3843 N N   . SER B 169 ? 0.3730 0.2527 0.2432 -0.0429 -0.0222 0.0050  166 SER B N   
3844 C CA  . SER B 169 ? 0.3595 0.2433 0.2319 -0.0455 -0.0226 0.0074  166 SER B CA  
3845 C C   . SER B 169 ? 0.3642 0.2412 0.2329 -0.0472 -0.0231 0.0096  166 SER B C   
3846 O O   . SER B 169 ? 0.3707 0.2397 0.2359 -0.0498 -0.0235 0.0095  166 SER B O   
3847 C CB  . SER B 169 ? 0.3535 0.2427 0.2275 -0.0488 -0.0227 0.0065  166 SER B CB  
3848 O OG  . SER B 169 ? 0.3509 0.2451 0.2266 -0.0491 -0.0234 0.0075  166 SER B OG  
3849 N N   . ASN B 170 ? 0.3604 0.2400 0.2291 -0.0462 -0.0235 0.0118  167 ASN B N   
3850 C CA  . ASN B 170 ? 0.3657 0.2407 0.2294 -0.0483 -0.0236 0.0151  167 ASN B CA  
3851 C C   . ASN B 170 ? 0.3865 0.2489 0.2456 -0.0467 -0.0253 0.0166  167 ASN B C   
3852 O O   . ASN B 170 ? 0.4145 0.2696 0.2683 -0.0506 -0.0257 0.0202  167 ASN B O   
3853 C CB  . ASN B 170 ? 0.3633 0.2412 0.2265 -0.0544 -0.0219 0.0159  167 ASN B CB  
3854 C CG  . ASN B 170 ? 0.3545 0.2450 0.2215 -0.0543 -0.0208 0.0142  167 ASN B CG  
3855 O OD1 . ASN B 170 ? 0.3545 0.2496 0.2206 -0.0513 -0.0212 0.0144  167 ASN B OD1 
3856 N ND2 . ASN B 170 ? 0.3347 0.2297 0.2055 -0.0564 -0.0206 0.0117  167 ASN B ND2 
3857 N N   . PHE B 171 ? 0.3858 0.2460 0.2466 -0.0411 -0.0266 0.0143  168 PHE B N   
3858 C CA  . PHE B 171 ? 0.4058 0.2543 0.2625 -0.0367 -0.0294 0.0146  168 PHE B CA  
3859 C C   . PHE B 171 ? 0.4151 0.2652 0.2714 -0.0328 -0.0313 0.0171  168 PHE B C   
3860 O O   . PHE B 171 ? 0.3982 0.2598 0.2600 -0.0315 -0.0308 0.0166  168 PHE B O   
3861 C CB  . PHE B 171 ? 0.4083 0.2569 0.2673 -0.0309 -0.0296 0.0099  168 PHE B CB  
3862 C CG  . PHE B 171 ? 0.4241 0.2649 0.2796 -0.0327 -0.0298 0.0068  168 PHE B CG  
3863 C CD1 . PHE B 171 ? 0.4218 0.2650 0.2776 -0.0399 -0.0283 0.0071  168 PHE B CD1 
3864 C CD2 . PHE B 171 ? 0.4472 0.2785 0.2989 -0.0265 -0.0323 0.0028  168 PHE B CD2 
3865 C CE1 . PHE B 171 ? 0.4335 0.2697 0.2863 -0.0418 -0.0296 0.0038  168 PHE B CE1 
3866 C CE2 . PHE B 171 ? 0.4607 0.2834 0.3079 -0.0277 -0.0336 -0.0010 168 PHE B CE2 
3867 C CZ  . PHE B 171 ? 0.4530 0.2783 0.3009 -0.0359 -0.0324 -0.0004 168 PHE B CZ  
3868 N N   . ASN B 172 ? 0.4395 0.2771 0.2891 -0.0311 -0.0344 0.0198  169 ASN B N   
3869 C CA  . ASN B 172 ? 0.4590 0.2958 0.3073 -0.0257 -0.0377 0.0217  169 ASN B CA  
3870 C C   . ASN B 172 ? 0.4792 0.3146 0.3312 -0.0171 -0.0402 0.0179  169 ASN B C   
3871 O O   . ASN B 172 ? 0.4686 0.3031 0.3225 -0.0156 -0.0390 0.0140  169 ASN B O   
3872 C CB  . ASN B 172 ? 0.4769 0.3019 0.3147 -0.0287 -0.0400 0.0276  169 ASN B CB  
3873 C CG  . ASN B 172 ? 0.4991 0.3053 0.3296 -0.0301 -0.0429 0.0294  169 ASN B CG  
3874 O OD1 . ASN B 172 ? 0.5144 0.3145 0.3467 -0.0251 -0.0449 0.0249  169 ASN B OD1 
3875 N ND2 . ASN B 172 ? 0.5092 0.3061 0.3309 -0.0370 -0.0435 0.0358  169 ASN B ND2 
3876 N N   . ARG B 173 ? 0.5022 0.3384 0.3549 -0.0111 -0.0439 0.0188  170 ARG B N   
3877 C CA  . ARG B 173 ? 0.5255 0.3635 0.3829 -0.0014 -0.0468 0.0152  170 ARG B CA  
3878 C C   . ARG B 173 ? 0.5444 0.3656 0.3950 0.0027  -0.0493 0.0129  170 ARG B C   
3879 O O   . ARG B 173 ? 0.5281 0.3543 0.3833 0.0097  -0.0488 0.0074  170 ARG B O   
3880 C CB  . ARG B 173 ? 0.5645 0.4019 0.4211 0.0039  -0.0520 0.0175  170 ARG B CB  
3881 C CG  . ARG B 173 ? 0.5934 0.4356 0.4566 0.0149  -0.0553 0.0135  170 ARG B CG  
3882 C CD  . ARG B 173 ? 0.6435 0.4937 0.5113 0.0195  -0.0600 0.0150  170 ARG B CD  
3883 N NE  . ARG B 173 ? 0.7025 0.5536 0.5741 0.0312  -0.0642 0.0114  170 ARG B NE  
3884 C CZ  . ARG B 173 ? 0.7574 0.6199 0.6371 0.0379  -0.0686 0.0108  170 ARG B CZ  
3885 N NH1 . ARG B 173 ? 0.7778 0.6415 0.6609 0.0498  -0.0726 0.0069  170 ARG B NH1 
3886 N NH2 . ARG B 173 ? 0.7584 0.6314 0.6428 0.0334  -0.0699 0.0135  170 ARG B NH2 
3887 N N   A ARG B 174 ? 0.5585 0.3603 0.3978 -0.0010 -0.0527 0.0172  171 ARG B N   
3888 N N   B ARG B 174 ? 0.5617 0.3634 0.4009 -0.0010 -0.0527 0.0172  171 ARG B N   
3889 C CA  A ARG B 174 ? 0.5938 0.3740 0.4246 0.0024  -0.0577 0.0157  171 ARG B CA  
3890 C CA  B ARG B 174 ? 0.5990 0.3792 0.4298 0.0024  -0.0577 0.0158  171 ARG B CA  
3891 C C   A ARG B 174 ? 0.5812 0.3625 0.4139 0.0003  -0.0544 0.0105  171 ARG B C   
3892 C C   B ARG B 174 ? 0.5842 0.3654 0.4169 0.0003  -0.0544 0.0105  171 ARG B C   
3893 O O   A ARG B 174 ? 0.5876 0.3621 0.4190 0.0087  -0.0572 0.0044  171 ARG B O   
3894 O O   B ARG B 174 ? 0.5902 0.3647 0.4215 0.0087  -0.0573 0.0044  171 ARG B O   
3895 C CB  A ARG B 174 ? 0.6302 0.3903 0.4487 -0.0049 -0.0615 0.0235  171 ARG B CB  
3896 C CB  B ARG B 174 ? 0.6391 0.3996 0.4576 -0.0050 -0.0615 0.0236  171 ARG B CB  
3897 C CG  A ARG B 174 ? 0.6817 0.4151 0.4900 -0.0006 -0.0697 0.0233  171 ARG B CG  
3898 C CG  B ARG B 174 ? 0.6950 0.4320 0.5038 0.0019  -0.0704 0.0249  171 ARG B CG  
3899 C CD  A ARG B 174 ? 0.7131 0.4278 0.5120 -0.0125 -0.0714 0.0289  171 ARG B CD  
3900 C CD  B ARG B 174 ? 0.7138 0.4551 0.5237 0.0113  -0.0743 0.0256  171 ARG B CD  
3901 N NE  A ARG B 174 ? 0.7057 0.4330 0.5057 -0.0246 -0.0652 0.0356  171 ARG B NE  
3902 N NE  B ARG B 174 ? 0.7306 0.4787 0.5482 0.0250  -0.0766 0.0174  171 ARG B NE  
3903 C CZ  A ARG B 174 ? 0.6961 0.4260 0.4975 -0.0354 -0.0614 0.0370  171 ARG B CZ  
3904 C CZ  B ARG B 174 ? 0.7204 0.4922 0.5503 0.0309  -0.0738 0.0141  171 ARG B CZ  
3905 N NH1 A ARG B 174 ? 0.6797 0.4237 0.4826 -0.0444 -0.0557 0.0424  171 ARG B NH1 
3906 N NH1 B ARG B 174 ? 0.7459 0.5264 0.5834 0.0432  -0.0754 0.0070  171 ARG B NH1 
3907 N NH2 A ARG B 174 ? 0.7034 0.4230 0.5047 -0.0362 -0.0638 0.0323  171 ARG B NH2 
3908 N NH2 B ARG B 174 ? 0.6979 0.4854 0.5328 0.0244  -0.0698 0.0177  171 ARG B NH2 
3909 N N   . GLN B 175 ? 0.5563 0.3466 0.3917 -0.0096 -0.0491 0.0122  172 GLN B N   
3910 C CA  . GLN B 175 ? 0.5453 0.3352 0.3811 -0.0131 -0.0468 0.0081  172 GLN B CA  
3911 C C   . GLN B 175 ? 0.5288 0.3353 0.3724 -0.0053 -0.0434 0.0016  172 GLN B C   
3912 O O   . GLN B 175 ? 0.5492 0.3507 0.3901 -0.0006 -0.0443 -0.0044 172 GLN B O   
3913 C CB  . GLN B 175 ? 0.5172 0.3134 0.3543 -0.0248 -0.0427 0.0120  172 GLN B CB  
3914 C CG  . GLN B 175 ? 0.5388 0.3208 0.3682 -0.0333 -0.0453 0.0188  172 GLN B CG  
3915 C CD  . GLN B 175 ? 0.5163 0.3112 0.3485 -0.0427 -0.0405 0.0235  172 GLN B CD  
3916 O OE1 . GLN B 175 ? 0.4940 0.3060 0.3326 -0.0414 -0.0365 0.0223  172 GLN B OE1 
3917 N NE2 . GLN B 175 ? 0.5342 0.3213 0.3616 -0.0522 -0.0413 0.0288  172 GLN B NE2 
3918 N N   . LEU B 176 ? 0.5076 0.3332 0.3600 -0.0038 -0.0401 0.0026  173 LEU B N   
3919 C CA  . LEU B 176 ? 0.5078 0.3514 0.3684 0.0030  -0.0368 -0.0020 173 LEU B CA  
3920 C C   . LEU B 176 ? 0.5460 0.3849 0.4049 0.0153  -0.0403 -0.0072 173 LEU B C   
3921 O O   . LEU B 176 ? 0.5413 0.3858 0.4003 0.0206  -0.0381 -0.0130 173 LEU B O   
3922 C CB  . LEU B 176 ? 0.4895 0.3517 0.3601 0.0017  -0.0347 0.0011  173 LEU B CB  
3923 C CG  . LEU B 176 ? 0.4700 0.3394 0.3432 -0.0080 -0.0317 0.0046  173 LEU B CG  
3924 C CD1 . LEU B 176 ? 0.4554 0.3393 0.3374 -0.0088 -0.0318 0.0072  173 LEU B CD1 
3925 C CD2 . LEU B 176 ? 0.4609 0.3366 0.3350 -0.0108 -0.0276 0.0020  173 LEU B CD2 
3926 N N   . GLU B 177 ? 0.5815 0.4110 0.4381 0.0206  -0.0456 -0.0056 174 GLU B N   
3927 C CA  . GLU B 177 ? 0.6309 0.4548 0.4857 0.0342  -0.0503 -0.0110 174 GLU B CA  
3928 C C   . GLU B 177 ? 0.6597 0.4653 0.5044 0.0375  -0.0530 -0.0168 174 GLU B C   
3929 O O   . GLU B 177 ? 0.6493 0.4587 0.4941 0.0495  -0.0538 -0.0243 174 GLU B O   
3930 C CB  . GLU B 177 ? 0.6774 0.4859 0.5272 0.0379  -0.0577 -0.0074 174 GLU B CB  
3931 C CG  . GLU B 177 ? 0.6861 0.5099 0.5442 0.0366  -0.0572 -0.0027 174 GLU B CG  
3932 C CD  . GLU B 177 ? 0.7348 0.5784 0.6044 0.0481  -0.0579 -0.0065 174 GLU B CD  
3933 O OE1 . GLU B 177 ? 0.7587 0.6054 0.6314 0.0503  -0.0620 -0.0033 174 GLU B OE1 
3934 O OE2 . GLU B 177 ? 0.7697 0.6278 0.6453 0.0545  -0.0541 -0.0126 174 GLU B OE2 
3935 N N   . MET B 178 ? 0.6755 0.4613 0.5113 0.0276  -0.0554 -0.0133 175 MET B N   
3936 C CA  . MET B 178 ? 0.7305 0.4960 0.5563 0.0284  -0.0595 -0.0182 175 MET B CA  
3937 C C   . MET B 178 ? 0.6900 0.4716 0.5190 0.0324  -0.0541 -0.0256 175 MET B C   
3938 O O   . MET B 178 ? 0.7091 0.4807 0.5314 0.0421  -0.0579 -0.0337 175 MET B O   
3939 C CB  . MET B 178 ? 0.7921 0.5425 0.6122 0.0135  -0.0608 -0.0119 175 MET B CB  
3940 C CG  . MET B 178 ? 0.8950 0.6228 0.7053 0.0121  -0.0666 -0.0162 175 MET B CG  
3941 S SD  . MET B 178 ? 1.0176 0.7333 0.8245 -0.0072 -0.0676 -0.0075 175 MET B SD  
3942 C CE  . MET B 178 ? 0.9656 0.7134 0.7845 -0.0148 -0.0565 -0.0049 175 MET B CE  
3943 N N   . ILE B 179 ? 0.6371 0.4415 0.4746 0.0257  -0.0462 -0.0231 176 ILE B N   
3944 C CA  . ILE B 179 ? 0.6234 0.4434 0.4625 0.0286  -0.0409 -0.0287 176 ILE B CA  
3945 C C   . ILE B 179 ? 0.6231 0.4621 0.4683 0.0420  -0.0384 -0.0334 176 ILE B C   
3946 O O   . ILE B 179 ? 0.6404 0.4835 0.4816 0.0512  -0.0374 -0.0412 176 ILE B O   
3947 C CB  . ILE B 179 ? 0.5921 0.4288 0.4375 0.0174  -0.0343 -0.0240 176 ILE B CB  
3948 C CG1 . ILE B 179 ? 0.5880 0.4117 0.4300 0.0046  -0.0360 -0.0193 176 ILE B CG1 
3949 C CG2 . ILE B 179 ? 0.5942 0.4460 0.4394 0.0207  -0.0294 -0.0289 176 ILE B CG2 
3950 C CD1 . ILE B 179 ? 0.6169 0.4190 0.4486 0.0030  -0.0413 -0.0231 176 ILE B CD1 
3951 N N   . LEU B 180 ? 0.6043 0.4568 0.4594 0.0431  -0.0373 -0.0290 177 LEU B N   
3952 C CA  . LEU B 180 ? 0.6090 0.4870 0.4739 0.0537  -0.0337 -0.0320 177 LEU B CA  
3953 C C   . LEU B 180 ? 0.6543 0.5229 0.5133 0.0701  -0.0390 -0.0407 177 LEU B C   
3954 O O   . LEU B 180 ? 0.6616 0.5511 0.5252 0.0811  -0.0352 -0.0466 177 LEU B O   
3955 C CB  . LEU B 180 ? 0.5853 0.4773 0.4622 0.0506  -0.0333 -0.0255 177 LEU B CB  
3956 C CG  . LEU B 180 ? 0.5486 0.4532 0.4324 0.0368  -0.0285 -0.0183 177 LEU B CG  
3957 C CD1 . LEU B 180 ? 0.5344 0.4450 0.4267 0.0338  -0.0309 -0.0125 177 LEU B CD1 
3958 C CD2 . LEU B 180 ? 0.5302 0.4598 0.4207 0.0359  -0.0212 -0.0189 177 LEU B CD2 
3959 N N   . ASN B 181 ? 0.6863 0.5248 0.5351 0.0717  -0.0476 -0.0412 178 ASN B N   
3960 C CA  . ASN B 181 ? 0.7469 0.5705 0.5886 0.0879  -0.0552 -0.0493 178 ASN B CA  
3961 C C   . ASN B 181 ? 0.7742 0.5761 0.6017 0.0915  -0.0593 -0.0572 178 ASN B C   
3962 O O   . ASN B 181 ? 0.8082 0.5924 0.6275 0.1049  -0.0672 -0.0645 178 ASN B O   
3963 C CB  . ASN B 181 ? 0.7829 0.5839 0.6208 0.0882  -0.0641 -0.0446 178 ASN B CB  
3964 C CG  . ASN B 181 ? 0.7789 0.6010 0.6300 0.0874  -0.0618 -0.0386 178 ASN B CG  
3965 O OD1 . ASN B 181 ? 0.7944 0.6460 0.6578 0.0944  -0.0567 -0.0413 178 ASN B OD1 
3966 N ND2 . ASN B 181 ? 0.7746 0.5825 0.6230 0.0785  -0.0656 -0.0303 178 ASN B ND2 
3967 N N   . LYS B 182 ? 0.7563 0.5586 0.5807 0.0805  -0.0550 -0.0560 179 LYS B N   
3968 C CA  . LYS B 182 ? 0.7978 0.5799 0.6087 0.0825  -0.0595 -0.0636 179 LYS B CA  
3969 C C   . LYS B 182 ? 0.8202 0.6142 0.6281 0.1013  -0.0585 -0.0756 179 LYS B C   
3970 O O   . LYS B 182 ? 0.7948 0.6217 0.6115 0.1051  -0.0491 -0.0765 179 LYS B O   
3971 C CB  . LYS B 182 ? 0.7799 0.5675 0.5909 0.0676  -0.0540 -0.0597 179 LYS B CB  
3972 C CG  . LYS B 182 ? 0.8253 0.5903 0.6229 0.0663  -0.0599 -0.0661 179 LYS B CG  
3973 C CD  . LYS B 182 ? 0.8067 0.5813 0.6053 0.0537  -0.0545 -0.0632 179 LYS B CD  
3974 C CE  . LYS B 182 ? 0.8236 0.6197 0.6203 0.0621  -0.0482 -0.0703 179 LYS B CE  
3975 N NZ  . LYS B 182 ? 0.8791 0.6604 0.6627 0.0774  -0.0547 -0.0829 179 LYS B NZ  
3976 N N   . PRO B 183 ? 0.8676 0.6351 0.6624 0.1135  -0.0685 -0.0852 180 PRO B N   
3977 C CA  . PRO B 183 ? 0.8941 0.6693 0.6820 0.1316  -0.0684 -0.0986 180 PRO B CA  
3978 C C   . PRO B 183 ? 0.8617 0.6563 0.6477 0.1273  -0.0597 -0.1011 180 PRO B C   
3979 O O   . PRO B 183 ? 0.8480 0.6290 0.6290 0.1133  -0.0609 -0.0975 180 PRO B O   
3980 C CB  . PRO B 183 ? 0.9571 0.6890 0.7278 0.1381  -0.0831 -0.1064 180 PRO B CB  
3981 C CG  . PRO B 183 ? 0.9607 0.6710 0.7337 0.1309  -0.0904 -0.0970 180 PRO B CG  
3982 C CD  . PRO B 183 ? 0.8989 0.6265 0.6837 0.1106  -0.0812 -0.0834 180 PRO B CD  
3983 N N   . GLY B 184 ? 0.8481 0.6756 0.6385 0.1391  -0.0511 -0.1065 181 GLY B N   
3984 C CA  . GLY B 184 ? 0.8279 0.6765 0.6149 0.1373  -0.0425 -0.1089 181 GLY B CA  
3985 C C   . GLY B 184 ? 0.7707 0.6341 0.5673 0.1172  -0.0346 -0.0961 181 GLY B C   
3986 O O   . GLY B 184 ? 0.7622 0.6306 0.5526 0.1112  -0.0309 -0.0965 181 GLY B O   
3987 N N   . LEU B 185 ? 0.7306 0.6006 0.5411 0.1073  -0.0326 -0.0853 182 LEU B N   
3988 C CA  . LEU B 185 ? 0.6884 0.5754 0.5087 0.0903  -0.0251 -0.0739 182 LEU B CA  
3989 C C   . LEU B 185 ? 0.6882 0.6070 0.5097 0.0930  -0.0151 -0.0751 182 LEU B C   
3990 O O   . LEU B 185 ? 0.7063 0.6473 0.5315 0.1064  -0.0110 -0.0799 182 LEU B O   
3991 C CB  . LEU B 185 ? 0.6563 0.5542 0.4919 0.0851  -0.0235 -0.0649 182 LEU B CB  
3992 C CG  . LEU B 185 ? 0.6171 0.5295 0.4626 0.0685  -0.0175 -0.0536 182 LEU B CG  
3993 C CD1 . LEU B 185 ? 0.5971 0.4851 0.4365 0.0549  -0.0218 -0.0495 182 LEU B CD1 
3994 C CD2 . LEU B 185 ? 0.6027 0.5303 0.4632 0.0666  -0.0161 -0.0468 182 LEU B CD2 
3995 N N   . LYS B 186 ? 0.6715 0.5945 0.4909 0.0807  -0.0112 -0.0699 183 LYS B N   
3996 C CA  . LYS B 186 ? 0.6912 0.6449 0.5118 0.0804  -0.0014 -0.0681 183 LYS B CA  
3997 C C   . LYS B 186 ? 0.6532 0.6259 0.4889 0.0662  0.0043  -0.0549 183 LYS B C   
3998 O O   . LYS B 186 ? 0.6604 0.6641 0.5051 0.0676  0.0119  -0.0511 183 LYS B O   
3999 C CB  . LYS B 186 ? 0.7202 0.6641 0.5253 0.0781  -0.0023 -0.0722 183 LYS B CB  
4000 C CG  . LYS B 186 ? 0.7581 0.7318 0.5597 0.0813  0.0070  -0.0721 183 LYS B CG  
4001 C CD  . LYS B 186 ? 0.7944 0.7601 0.5788 0.0806  0.0060  -0.0767 183 LYS B CD  
4002 C CE  . LYS B 186 ? 0.8247 0.8229 0.6050 0.0849  0.0160  -0.0758 183 LYS B CE  
4003 N NZ  . LYS B 186 ? 0.8756 0.8658 0.6362 0.0885  0.0142  -0.0829 183 LYS B NZ  
4004 N N   . TYR B 187 ? 0.6154 0.5707 0.4532 0.0526  0.0004  -0.0483 184 TYR B N   
4005 C CA  . TYR B 187 ? 0.5800 0.5478 0.4296 0.0387  0.0039  -0.0367 184 TYR B CA  
4006 C C   . TYR B 187 ? 0.5565 0.5090 0.4136 0.0329  -0.0015 -0.0324 184 TYR B C   
4007 O O   . TYR B 187 ? 0.5403 0.4681 0.3909 0.0294  -0.0073 -0.0339 184 TYR B O   
4008 C CB  . TYR B 187 ? 0.5750 0.5381 0.4178 0.0281  0.0046  -0.0331 184 TYR B CB  
4009 C CG  . TYR B 187 ? 0.6030 0.5801 0.4361 0.0327  0.0095  -0.0363 184 TYR B CG  
4010 C CD1 . TYR B 187 ? 0.6209 0.6280 0.4588 0.0365  0.0174  -0.0338 184 TYR B CD1 
4011 C CD2 . TYR B 187 ? 0.6230 0.5842 0.4416 0.0332  0.0061  -0.0419 184 TYR B CD2 
4012 C CE1 . TYR B 187 ? 0.6458 0.6672 0.4731 0.0409  0.0225  -0.0363 184 TYR B CE1 
4013 C CE2 . TYR B 187 ? 0.6537 0.6270 0.4611 0.0383  0.0102  -0.0455 184 TYR B CE2 
4014 C CZ  . TYR B 187 ? 0.6629 0.6666 0.4739 0.0422  0.0188  -0.0424 184 TYR B CZ  
4015 O OH  . TYR B 187 ? 0.6930 0.7093 0.4911 0.0473  0.0232  -0.0456 184 TYR B OH  
4016 N N   . LYS B 188 ? 0.5440 0.5125 0.4145 0.0309  0.0005  -0.0266 185 LYS B N   
4017 C CA  . LYS B 188 ? 0.5307 0.4884 0.4083 0.0244  -0.0039 -0.0214 185 LYS B CA  
4018 C C   . LYS B 188 ? 0.4984 0.4483 0.3749 0.0110  -0.0045 -0.0154 185 LYS B C   
4019 O O   . LYS B 188 ? 0.4801 0.4399 0.3555 0.0060  -0.0009 -0.0128 185 LYS B O   
4020 C CB  . LYS B 188 ? 0.5379 0.5173 0.4302 0.0251  -0.0020 -0.0168 185 LYS B CB  
4021 C CG  . LYS B 188 ? 0.5741 0.5652 0.4701 0.0394  -0.0016 -0.0227 185 LYS B CG  
4022 C CD  . LYS B 188 ? 0.5874 0.5906 0.4975 0.0402  -0.0035 -0.0189 185 LYS B CD  
4023 C CE  . LYS B 188 ? 0.5839 0.6128 0.5077 0.0305  0.0008  -0.0106 185 LYS B CE  
4024 N NZ  . LYS B 188 ? 0.5851 0.6283 0.5233 0.0331  -0.0017 -0.0084 185 LYS B NZ  
4025 N N   . PRO B 189 ? 0.4824 0.4150 0.3587 0.0053  -0.0092 -0.0129 186 PRO B N   
4026 C CA  . PRO B 189 ? 0.4570 0.3871 0.3347 -0.0060 -0.0095 -0.0073 186 PRO B CA  
4027 C C   . PRO B 189 ? 0.4331 0.3826 0.3216 -0.0105 -0.0070 -0.0011 186 PRO B C   
4028 O O   . PRO B 189 ? 0.4309 0.3893 0.3274 -0.0074 -0.0074 0.0001  186 PRO B O   
4029 C CB  . PRO B 189 ? 0.4578 0.3708 0.3346 -0.0089 -0.0143 -0.0060 186 PRO B CB  
4030 C CG  . PRO B 189 ? 0.4906 0.3908 0.3615 -0.0003 -0.0173 -0.0114 186 PRO B CG  
4031 C CD  . PRO B 189 ? 0.5013 0.4172 0.3756 0.0096  -0.0144 -0.0149 186 PRO B CD  
4032 N N   . VAL B 190 ? 0.4136 0.3685 0.3020 -0.0180 -0.0054 0.0030  187 VAL B N   
4033 C CA  . VAL B 190 ? 0.4046 0.3748 0.3028 -0.0242 -0.0046 0.0100  187 VAL B CA  
4034 C C   . VAL B 190 ? 0.3766 0.3377 0.2795 -0.0292 -0.0098 0.0130  187 VAL B C   
4035 O O   . VAL B 190 ? 0.3604 0.3310 0.2722 -0.0333 -0.0112 0.0177  187 VAL B O   
4036 C CB  . VAL B 190 ? 0.4125 0.3891 0.3077 -0.0307 -0.0025 0.0141  187 VAL B CB  
4037 C CG1 . VAL B 190 ? 0.4308 0.4200 0.3207 -0.0253 0.0032  0.0117  187 VAL B CG1 
4038 C CG2 . VAL B 190 ? 0.4034 0.3631 0.2912 -0.0355 -0.0060 0.0137  187 VAL B CG2 
4039 N N   . CYS B 191 ? 0.3635 0.3074 0.2601 -0.0299 -0.0127 0.0106  188 CYS B N   
4040 C CA  . CYS B 191 ? 0.3566 0.2931 0.2557 -0.0340 -0.0172 0.0129  188 CYS B CA  
4041 C C   . CYS B 191 ? 0.3470 0.2686 0.2398 -0.0317 -0.0189 0.0098  188 CYS B C   
4042 O O   . CYS B 191 ? 0.3521 0.2666 0.2384 -0.0293 -0.0176 0.0063  188 CYS B O   
4043 C CB  . CYS B 191 ? 0.3566 0.2909 0.2550 -0.0409 -0.0191 0.0158  188 CYS B CB  
4044 S SG  . CYS B 191 ? 0.3803 0.3050 0.2691 -0.0422 -0.0183 0.0128  188 CYS B SG  
4045 N N   . ASN B 192 ? 0.3427 0.2595 0.2368 -0.0334 -0.0222 0.0113  189 ASN B N   
4046 C CA  . ASN B 192 ? 0.3435 0.2481 0.2314 -0.0337 -0.0237 0.0103  189 ASN B CA  
4047 C C   . ASN B 192 ? 0.3392 0.2434 0.2275 -0.0379 -0.0260 0.0117  189 ASN B C   
4048 O O   . ASN B 192 ? 0.3285 0.2359 0.2207 -0.0380 -0.0291 0.0133  189 ASN B O   
4049 C CB  . ASN B 192 ? 0.3550 0.2550 0.2421 -0.0293 -0.0256 0.0104  189 ASN B CB  
4050 C CG  . ASN B 192 ? 0.3618 0.2493 0.2412 -0.0304 -0.0266 0.0106  189 ASN B CG  
4051 O OD1 . ASN B 192 ? 0.3631 0.2463 0.2387 -0.0342 -0.0253 0.0101  189 ASN B OD1 
4052 N ND2 . ASN B 192 ? 0.3614 0.2441 0.2387 -0.0276 -0.0291 0.0121  189 ASN B ND2 
4053 N N   . GLN B 193 ? 0.3334 0.2346 0.2182 -0.0408 -0.0253 0.0107  190 GLN B N   
4054 C CA  . GLN B 193 ? 0.3278 0.2290 0.2124 -0.0430 -0.0278 0.0108  190 GLN B CA  
4055 C C   . GLN B 193 ? 0.3278 0.2251 0.2083 -0.0424 -0.0279 0.0104  190 GLN B C   
4056 O O   . GLN B 193 ? 0.3365 0.2306 0.2136 -0.0437 -0.0258 0.0101  190 GLN B O   
4057 C CB  . GLN B 193 ? 0.3257 0.2277 0.2092 -0.0455 -0.0273 0.0096  190 GLN B CB  
4058 C CG  . GLN B 193 ? 0.3351 0.2373 0.2187 -0.0459 -0.0306 0.0088  190 GLN B CG  
4059 C CD  . GLN B 193 ? 0.3318 0.2348 0.2145 -0.0473 -0.0316 0.0074  190 GLN B CD  
4060 O OE1 . GLN B 193 ? 0.3349 0.2392 0.2166 -0.0467 -0.0318 0.0053  190 GLN B OE1 
4061 N NE2 . GLN B 193 ? 0.3384 0.2421 0.2216 -0.0489 -0.0321 0.0090  190 GLN B NE2 
4062 N N   . VAL B 194 ? 0.3339 0.2317 0.2143 -0.0408 -0.0309 0.0108  191 VAL B N   
4063 C CA  . VAL B 194 ? 0.3432 0.2385 0.2181 -0.0395 -0.0307 0.0113  191 VAL B CA  
4064 C C   . VAL B 194 ? 0.3381 0.2360 0.2113 -0.0378 -0.0338 0.0095  191 VAL B C   
4065 O O   . VAL B 194 ? 0.3316 0.2301 0.2082 -0.0373 -0.0378 0.0083  191 VAL B O   
4066 C CB  . VAL B 194 ? 0.3528 0.2444 0.2264 -0.0370 -0.0316 0.0133  191 VAL B CB  
4067 C CG1 . VAL B 194 ? 0.3623 0.2502 0.2367 -0.0367 -0.0294 0.0137  191 VAL B CG1 
4068 C CG2 . VAL B 194 ? 0.3550 0.2495 0.2332 -0.0348 -0.0359 0.0132  191 VAL B CG2 
4069 N N   . GLU B 195 ? 0.3570 0.2560 0.2243 -0.0370 -0.0323 0.0096  192 GLU B N   
4070 C CA  . GLU B 195 ? 0.3681 0.2702 0.2318 -0.0333 -0.0353 0.0068  192 GLU B CA  
4071 C C   . GLU B 195 ? 0.3667 0.2648 0.2301 -0.0305 -0.0407 0.0067  192 GLU B C   
4072 O O   . GLU B 195 ? 0.3662 0.2615 0.2277 -0.0301 -0.0406 0.0095  192 GLU B O   
4073 C CB  . GLU B 195 ? 0.3898 0.2971 0.2466 -0.0328 -0.0317 0.0074  192 GLU B CB  
4074 C CG  . GLU B 195 ? 0.4118 0.3233 0.2633 -0.0271 -0.0347 0.0034  192 GLU B CG  
4075 C CD  . GLU B 195 ? 0.4250 0.3451 0.2690 -0.0262 -0.0301 0.0045  192 GLU B CD  
4076 O OE1 . GLU B 195 ? 0.4466 0.3681 0.2901 -0.0315 -0.0250 0.0094  192 GLU B OE1 
4077 O OE2 . GLU B 195 ? 0.4353 0.3607 0.2735 -0.0204 -0.0318 0.0005  192 GLU B OE2 
4078 N N   . CYS B 196 ? 0.3640 0.2610 0.2294 -0.0287 -0.0465 0.0037  193 CYS B N   
4079 C CA  . CYS B 196 ? 0.3743 0.2677 0.2415 -0.0276 -0.0530 0.0038  193 CYS B CA  
4080 C C   . CYS B 196 ? 0.3838 0.2738 0.2486 -0.0245 -0.0604 -0.0008 193 CYS B C   
4081 O O   . CYS B 196 ? 0.3826 0.2706 0.2510 -0.0260 -0.0629 -0.0020 193 CYS B O   
4082 C CB  . CYS B 196 ? 0.3738 0.2679 0.2505 -0.0315 -0.0531 0.0071  193 CYS B CB  
4083 S SG  . CYS B 196 ? 0.3981 0.2916 0.2801 -0.0314 -0.0611 0.0079  193 CYS B SG  
4084 N N   . HIS B 197 ? 0.3892 0.2774 0.2468 -0.0198 -0.0646 -0.0035 194 HIS B N   
4085 C CA  . HIS B 197 ? 0.3991 0.2818 0.2522 -0.0153 -0.0734 -0.0093 194 HIS B CA  
4086 C C   . HIS B 197 ? 0.4108 0.2911 0.2572 -0.0115 -0.0784 -0.0107 194 HIS B C   
4087 O O   . HIS B 197 ? 0.4064 0.2899 0.2513 -0.0121 -0.0743 -0.0068 194 HIS B O   
4088 C CB  . HIS B 197 ? 0.4026 0.2892 0.2493 -0.0103 -0.0707 -0.0141 194 HIS B CB  
4089 C CG  . HIS B 197 ? 0.3985 0.2946 0.2388 -0.0087 -0.0618 -0.0126 194 HIS B CG  
4090 N ND1 . HIS B 197 ? 0.4178 0.3158 0.2481 -0.0044 -0.0619 -0.0133 194 HIS B ND1 
4091 C CD2 . HIS B 197 ? 0.3880 0.2919 0.2304 -0.0119 -0.0530 -0.0095 194 HIS B CD2 
4092 C CE1 . HIS B 197 ? 0.4196 0.3265 0.2459 -0.0055 -0.0531 -0.0100 194 HIS B CE1 
4093 N NE2 . HIS B 197 ? 0.3949 0.3053 0.2294 -0.0106 -0.0478 -0.0076 194 HIS B NE2 
4094 N N   . PRO B 198 ? 0.4300 0.3034 0.2713 -0.0070 -0.0883 -0.0163 195 PRO B N   
4095 C CA  . PRO B 198 ? 0.4482 0.3186 0.2829 -0.0034 -0.0945 -0.0180 195 PRO B CA  
4096 C C   . PRO B 198 ? 0.4599 0.3364 0.2820 0.0018  -0.0885 -0.0179 195 PRO B C   
4097 O O   . PRO B 198 ? 0.4771 0.3513 0.2947 0.0036  -0.0929 -0.0175 195 PRO B O   
4098 C CB  . PRO B 198 ? 0.4667 0.3273 0.2958 0.0016  -0.1063 -0.0259 195 PRO B CB  
4099 C CG  . PRO B 198 ? 0.4665 0.3223 0.3057 -0.0036 -0.1086 -0.0249 195 PRO B CG  
4100 C CD  . PRO B 198 ? 0.4379 0.3036 0.2801 -0.0057 -0.0960 -0.0212 195 PRO B CD  
4101 N N   . TYR B 199 ? 0.4553 0.3398 0.2721 0.0036  -0.0793 -0.0178 196 TYR B N   
4102 C CA  . TYR B 199 ? 0.4717 0.3633 0.2766 0.0065  -0.0726 -0.0155 196 TYR B CA  
4103 C C   . TYR B 199 ? 0.4572 0.3507 0.2668 -0.0002 -0.0651 -0.0067 196 TYR B C   
4104 O O   . TYR B 199 ? 0.4664 0.3626 0.2666 0.0003  -0.0608 -0.0026 196 TYR B O   
4105 C CB  . TYR B 199 ? 0.4921 0.3935 0.2893 0.0116  -0.0673 -0.0196 196 TYR B CB  
4106 C CG  . TYR B 199 ? 0.5255 0.4244 0.3144 0.0210  -0.0753 -0.0295 196 TYR B CG  
4107 C CD1 . TYR B 199 ? 0.5505 0.4387 0.3343 0.0249  -0.0867 -0.0338 196 TYR B CD1 
4108 C CD2 . TYR B 199 ? 0.5439 0.4525 0.3292 0.0269  -0.0718 -0.0349 196 TYR B CD2 
4109 C CE1 . TYR B 199 ? 0.5801 0.4639 0.3543 0.0346  -0.0952 -0.0438 196 TYR B CE1 
4110 C CE2 . TYR B 199 ? 0.5765 0.4829 0.3523 0.0377  -0.0794 -0.0452 196 TYR B CE2 
4111 C CZ  . TYR B 199 ? 0.5953 0.4878 0.3650 0.0416  -0.0915 -0.0498 196 TYR B CZ  
4112 O OH  . TYR B 199 ? 0.6278 0.5157 0.3873 0.0528  -0.1003 -0.0609 196 TYR B OH  
4113 N N   . PHE B 200 ? 0.4320 0.3230 0.2548 -0.0061 -0.0643 -0.0039 197 PHE B N   
4114 C CA  . PHE B 200 ? 0.4269 0.3178 0.2549 -0.0114 -0.0585 0.0029  197 PHE B CA  
4115 C C   . PHE B 200 ? 0.4126 0.3008 0.2544 -0.0151 -0.0616 0.0037  197 PHE B C   
4116 O O   . PHE B 200 ? 0.3916 0.2816 0.2411 -0.0190 -0.0577 0.0044  197 PHE B O   
4117 C CB  . PHE B 200 ? 0.4334 0.3301 0.2605 -0.0144 -0.0495 0.0050  197 PHE B CB  
4118 C CG  . PHE B 200 ? 0.4414 0.3360 0.2702 -0.0194 -0.0441 0.0114  197 PHE B CG  
4119 C CD1 . PHE B 200 ? 0.4555 0.3438 0.2809 -0.0188 -0.0461 0.0154  197 PHE B CD1 
4120 C CD2 . PHE B 200 ? 0.4515 0.3493 0.2846 -0.0241 -0.0380 0.0129  197 PHE B CD2 
4121 C CE1 . PHE B 200 ? 0.4745 0.3581 0.3001 -0.0224 -0.0424 0.0207  197 PHE B CE1 
4122 C CE2 . PHE B 200 ? 0.4644 0.3577 0.2979 -0.0285 -0.0343 0.0182  197 PHE B CE2 
4123 C CZ  . PHE B 200 ? 0.4625 0.3479 0.2916 -0.0274 -0.0367 0.0220  197 PHE B CZ  
4124 N N   . ASN B 201 ? 0.4134 0.2989 0.2586 -0.0142 -0.0684 0.0039  198 ASN B N   
4125 C CA  . ASN B 201 ? 0.4060 0.2922 0.2649 -0.0179 -0.0727 0.0041  198 ASN B CA  
4126 C C   . ASN B 201 ? 0.4008 0.2905 0.2683 -0.0207 -0.0678 0.0087  198 ASN B C   
4127 O O   . ASN B 201 ? 0.4045 0.2984 0.2838 -0.0244 -0.0687 0.0098  198 ASN B O   
4128 C CB  . ASN B 201 ? 0.4171 0.3005 0.2771 -0.0164 -0.0834 0.0014  198 ASN B CB  
4129 C CG  . ASN B 201 ? 0.4292 0.3133 0.2888 -0.0140 -0.0871 0.0034  198 ASN B CG  
4130 O OD1 . ASN B 201 ? 0.4188 0.3059 0.2817 -0.0142 -0.0823 0.0074  198 ASN B OD1 
4131 N ND2 . ASN B 201 ? 0.4326 0.3132 0.2879 -0.0110 -0.0967 0.0000  198 ASN B ND2 
4132 N N   . ARG B 202 ? 0.4036 0.2917 0.2647 -0.0188 -0.0631 0.0113  199 ARG B N   
4133 C CA  . ARG B 202 ? 0.4048 0.2937 0.2714 -0.0197 -0.0589 0.0145  199 ARG B CA  
4134 C C   . ARG B 202 ? 0.4121 0.3065 0.2901 -0.0188 -0.0636 0.0149  199 ARG B C   
4135 O O   . ARG B 202 ? 0.3961 0.2963 0.2838 -0.0205 -0.0604 0.0158  199 ARG B O   
4136 C CB  . ARG B 202 ? 0.3971 0.2877 0.2678 -0.0236 -0.0525 0.0145  199 ARG B CB  
4137 C CG  . ARG B 202 ? 0.3977 0.2877 0.2623 -0.0252 -0.0498 0.0128  199 ARG B CG  
4138 C CD  . ARG B 202 ? 0.4074 0.2943 0.2612 -0.0248 -0.0458 0.0147  199 ARG B CD  
4139 N NE  . ARG B 202 ? 0.4193 0.3019 0.2731 -0.0263 -0.0421 0.0180  199 ARG B NE  
4140 C CZ  . ARG B 202 ? 0.4146 0.2964 0.2687 -0.0300 -0.0372 0.0187  199 ARG B CZ  
4141 N NH1 . ARG B 202 ? 0.4070 0.2941 0.2623 -0.0324 -0.0348 0.0167  199 ARG B NH1 
4142 N NH2 . ARG B 202 ? 0.4206 0.2957 0.2736 -0.0308 -0.0357 0.0210  199 ARG B NH2 
4143 N N   . SER B 203 ? 0.4182 0.3126 0.2953 -0.0160 -0.0708 0.0143  200 SER B N   
4144 C CA  . SER B 203 ? 0.4260 0.3289 0.3164 -0.0158 -0.0760 0.0149  200 SER B CA  
4145 C C   . SER B 203 ? 0.4391 0.3453 0.3338 -0.0121 -0.0727 0.0168  200 SER B C   
4146 O O   . SER B 203 ? 0.4391 0.3565 0.3472 -0.0130 -0.0720 0.0173  200 SER B O   
4147 C CB  . SER B 203 ? 0.4431 0.3453 0.3321 -0.0135 -0.0854 0.0135  200 SER B CB  
4148 O OG  . SER B 203 ? 0.4750 0.3693 0.3501 -0.0081 -0.0861 0.0140  200 SER B OG  
4149 N N   . LYS B 204 ? 0.4579 0.3550 0.3417 -0.0077 -0.0713 0.0180  201 LYS B N   
4150 C CA  . LYS B 204 ? 0.4772 0.3746 0.3642 -0.0027 -0.0701 0.0191  201 LYS B CA  
4151 C C   . LYS B 204 ? 0.4588 0.3584 0.3502 -0.0046 -0.0626 0.0185  201 LYS B C   
4152 O O   . LYS B 204 ? 0.4530 0.3613 0.3541 -0.0011 -0.0618 0.0176  201 LYS B O   
4153 C CB  . LYS B 204 ? 0.5198 0.4032 0.3920 0.0017  -0.0717 0.0213  201 LYS B CB  
4154 C CG  . LYS B 204 ? 0.5456 0.4278 0.4131 0.0053  -0.0799 0.0218  201 LYS B CG  
4155 C CD  . LYS B 204 ? 0.5900 0.4574 0.4399 0.0079  -0.0808 0.0254  201 LYS B CD  
4156 C CE  . LYS B 204 ? 0.6372 0.5026 0.4803 0.0126  -0.0894 0.0261  201 LYS B CE  
4157 N NZ  . LYS B 204 ? 0.6735 0.5241 0.5008 0.0160  -0.0909 0.0309  201 LYS B NZ  
4158 N N   . LEU B 205 ? 0.4424 0.3356 0.3268 -0.0092 -0.0576 0.0187  202 LEU B N   
4159 C CA  . LEU B 205 ? 0.4321 0.3266 0.3194 -0.0111 -0.0513 0.0177  202 LEU B CA  
4160 C C   . LEU B 205 ? 0.4175 0.3268 0.3181 -0.0138 -0.0501 0.0168  202 LEU B C   
4161 O O   . LEU B 205 ? 0.4167 0.3325 0.3230 -0.0122 -0.0465 0.0158  202 LEU B O   
4162 C CB  . LEU B 205 ? 0.4211 0.3083 0.2999 -0.0163 -0.0472 0.0181  202 LEU B CB  
4163 C CG  . LEU B 205 ? 0.4143 0.3019 0.2950 -0.0187 -0.0418 0.0168  202 LEU B CG  
4164 C CD1 . LEU B 205 ? 0.4260 0.3063 0.3040 -0.0140 -0.0413 0.0164  202 LEU B CD1 
4165 C CD2 . LEU B 205 ? 0.4111 0.2939 0.2851 -0.0239 -0.0388 0.0172  202 LEU B CD2 
4166 N N   . LEU B 206 ? 0.4068 0.3210 0.3115 -0.0177 -0.0537 0.0172  203 LEU B N   
4167 C CA  . LEU B 206 ? 0.4069 0.3342 0.3242 -0.0221 -0.0539 0.0179  203 LEU B CA  
4168 C C   . LEU B 206 ? 0.4214 0.3629 0.3507 -0.0185 -0.0548 0.0185  203 LEU B C   
4169 O O   . LEU B 206 ? 0.4189 0.3728 0.3566 -0.0200 -0.0506 0.0192  203 LEU B O   
4170 C CB  . LEU B 206 ? 0.3937 0.3198 0.3119 -0.0267 -0.0602 0.0182  203 LEU B CB  
4171 C CG  . LEU B 206 ? 0.3851 0.3227 0.3162 -0.0329 -0.0624 0.0204  203 LEU B CG  
4172 C CD1 . LEU B 206 ? 0.3707 0.3102 0.3020 -0.0369 -0.0560 0.0215  203 LEU B CD1 
4173 C CD2 . LEU B 206 ? 0.3817 0.3138 0.3123 -0.0367 -0.0711 0.0200  203 LEU B CD2 
4174 N N   . ASP B 207 ? 0.4476 0.3890 0.3775 -0.0135 -0.0604 0.0182  204 ASP B N   
4175 C CA  . ASP B 207 ? 0.4769 0.4343 0.4198 -0.0088 -0.0621 0.0182  204 ASP B CA  
4176 C C   . ASP B 207 ? 0.4654 0.4249 0.4076 -0.0020 -0.0561 0.0163  204 ASP B C   
4177 O O   . ASP B 207 ? 0.4631 0.4413 0.4176 0.0003  -0.0534 0.0159  204 ASP B O   
4178 C CB  . ASP B 207 ? 0.5164 0.4703 0.4578 -0.0035 -0.0701 0.0178  204 ASP B CB  
4179 C CG  . ASP B 207 ? 0.5510 0.5085 0.4975 -0.0091 -0.0777 0.0188  204 ASP B CG  
4180 O OD1 . ASP B 207 ? 0.5717 0.5390 0.5282 -0.0167 -0.0775 0.0205  204 ASP B OD1 
4181 O OD2 . ASP B 207 ? 0.6016 0.5519 0.5422 -0.0056 -0.0847 0.0182  204 ASP B OD2 
4182 N N   . PHE B 208 ? 0.4675 0.4086 0.3954 0.0015  -0.0547 0.0150  205 PHE B N   
4183 C CA  . PHE B 208 ? 0.4718 0.4091 0.3959 0.0079  -0.0504 0.0123  205 PHE B CA  
4184 C C   . PHE B 208 ? 0.4527 0.4007 0.3817 0.0038  -0.0435 0.0116  205 PHE B C   
4185 O O   . PHE B 208 ? 0.4484 0.4095 0.3840 0.0090  -0.0403 0.0094  205 PHE B O   
4186 C CB  . PHE B 208 ? 0.4827 0.3966 0.3905 0.0086  -0.0507 0.0123  205 PHE B CB  
4187 C CG  . PHE B 208 ? 0.5046 0.4117 0.4077 0.0139  -0.0477 0.0092  205 PHE B CG  
4188 C CD1 . PHE B 208 ? 0.5314 0.4384 0.4359 0.0248  -0.0508 0.0063  205 PHE B CD1 
4189 C CD2 . PHE B 208 ? 0.4990 0.4013 0.3973 0.0091  -0.0425 0.0082  205 PHE B CD2 
4190 C CE1 . PHE B 208 ? 0.5551 0.4544 0.4545 0.0309  -0.0492 0.0022  205 PHE B CE1 
4191 C CE2 . PHE B 208 ? 0.5190 0.4143 0.4125 0.0144  -0.0409 0.0044  205 PHE B CE2 
4192 C CZ  . PHE B 208 ? 0.5429 0.4361 0.4365 0.0254  -0.0443 0.0011  205 PHE B CZ  
4193 N N   . CYS B 209 ? 0.4392 0.3823 0.3642 -0.0048 -0.0413 0.0134  206 CYS B N   
4194 C CA  . CYS B 209 ? 0.4294 0.3804 0.3568 -0.0093 -0.0354 0.0134  206 CYS B CA  
4195 C C   . CYS B 209 ? 0.4337 0.4083 0.3758 -0.0107 -0.0341 0.0154  206 CYS B C   
4196 O O   . CYS B 209 ? 0.4242 0.4102 0.3690 -0.0080 -0.0287 0.0140  206 CYS B O   
4197 C CB  . CYS B 209 ? 0.4210 0.3631 0.3426 -0.0176 -0.0350 0.0151  206 CYS B CB  
4198 S SG  . CYS B 209 ? 0.4405 0.3615 0.3468 -0.0171 -0.0336 0.0131  206 CYS B SG  
4199 N N   . LYS B 210 ? 0.4418 0.4241 0.3928 -0.0152 -0.0390 0.0185  207 LYS B N   
4200 C CA  . LYS B 210 ? 0.4641 0.4708 0.4311 -0.0182 -0.0385 0.0216  207 LYS B CA  
4201 C C   . LYS B 210 ? 0.4858 0.5085 0.4596 -0.0080 -0.0354 0.0186  207 LYS B C   
4202 O O   . LYS B 210 ? 0.4958 0.5391 0.4779 -0.0089 -0.0299 0.0200  207 LYS B O   
4203 C CB  . LYS B 210 ? 0.4919 0.5020 0.4673 -0.0235 -0.0465 0.0246  207 LYS B CB  
4204 C CG  . LYS B 210 ? 0.5017 0.5010 0.4733 -0.0336 -0.0498 0.0274  207 LYS B CG  
4205 C CD  . LYS B 210 ? 0.5355 0.5335 0.5126 -0.0376 -0.0594 0.0288  207 LYS B CD  
4206 C CE  . LYS B 210 ? 0.5467 0.5406 0.5250 -0.0484 -0.0631 0.0324  207 LYS B CE  
4207 N NZ  . LYS B 210 ? 0.5729 0.5542 0.5482 -0.0504 -0.0733 0.0311  207 LYS B NZ  
4208 N N   . SER B 211 ? 0.4816 0.4952 0.4510 0.0018  -0.0388 0.0148  208 SER B N   
4209 C CA  . SER B 211 ? 0.5036 0.5320 0.4801 0.0135  -0.0379 0.0111  208 SER B CA  
4210 C C   . SER B 211 ? 0.5125 0.5429 0.4831 0.0191  -0.0304 0.0072  208 SER B C   
4211 O O   . SER B 211 ? 0.5263 0.5753 0.5045 0.0282  -0.0279 0.0040  208 SER B O   
4212 C CB  . SER B 211 ? 0.5146 0.5287 0.4856 0.0229  -0.0447 0.0082  208 SER B CB  
4213 O OG  . SER B 211 ? 0.5028 0.4896 0.4560 0.0257  -0.0448 0.0059  208 SER B OG  
4214 N N   . LYS B 212 ? 0.5102 0.5218 0.4672 0.0149  -0.0277 0.0067  209 LYS B N   
4215 C CA  . LYS B 212 ? 0.5189 0.5287 0.4678 0.0197  -0.0218 0.0023  209 LYS B CA  
4216 C C   . LYS B 212 ? 0.5083 0.5300 0.4590 0.0105  -0.0158 0.0059  209 LYS B C   
4217 O O   . LYS B 212 ? 0.5175 0.5360 0.4597 0.0130  -0.0114 0.0027  209 LYS B O   
4218 C CB  . LYS B 212 ? 0.5221 0.5016 0.4544 0.0214  -0.0244 -0.0007 209 LYS B CB  
4219 C CG  . LYS B 212 ? 0.5455 0.5096 0.4735 0.0292  -0.0311 -0.0026 209 LYS B CG  
4220 C CD  . LYS B 212 ? 0.5755 0.5482 0.5071 0.0435  -0.0323 -0.0082 209 LYS B CD  
4221 C CE  . LYS B 212 ? 0.5975 0.5478 0.5207 0.0508  -0.0401 -0.0097 209 LYS B CE  
4222 N NZ  . LYS B 212 ? 0.6351 0.5953 0.5640 0.0659  -0.0430 -0.0150 209 LYS B NZ  
4223 N N   . ASP B 213 ? 0.5014 0.5353 0.4621 0.0001  -0.0164 0.0124  210 ASP B N   
4224 C CA  . ASP B 213 ? 0.5100 0.5525 0.4720 -0.0105 -0.0123 0.0177  210 ASP B CA  
4225 C C   . ASP B 213 ? 0.4771 0.4966 0.4239 -0.0141 -0.0119 0.0164  210 ASP B C   
4226 O O   . ASP B 213 ? 0.4702 0.4937 0.4122 -0.0168 -0.0071 0.0171  210 ASP B O   
4227 C CB  . ASP B 213 ? 0.5427 0.6125 0.5110 -0.0083 -0.0048 0.0184  210 ASP B CB  
4228 C CG  . ASP B 213 ? 0.5707 0.6523 0.5433 -0.0214 -0.0023 0.0268  210 ASP B CG  
4229 O OD1 . ASP B 213 ? 0.5932 0.6669 0.5695 -0.0318 -0.0080 0.0322  210 ASP B OD1 
4230 O OD2 . ASP B 213 ? 0.6147 0.7128 0.5861 -0.0212 0.0048  0.0280  210 ASP B OD2 
4231 N N   . ILE B 214 ? 0.4501 0.4475 0.3895 -0.0140 -0.0167 0.0146  211 ILE B N   
4232 C CA  . ILE B 214 ? 0.4271 0.4048 0.3547 -0.0188 -0.0172 0.0142  211 ILE B CA  
4233 C C   . ILE B 214 ? 0.4155 0.3892 0.3461 -0.0278 -0.0217 0.0188  211 ILE B C   
4234 O O   . ILE B 214 ? 0.4173 0.3900 0.3527 -0.0276 -0.0266 0.0197  211 ILE B O   
4235 C CB  . ILE B 214 ? 0.4264 0.3840 0.3436 -0.0133 -0.0192 0.0096  211 ILE B CB  
4236 C CG1 . ILE B 214 ? 0.4394 0.3971 0.3524 -0.0035 -0.0168 0.0042  211 ILE B CG1 
4237 C CG2 . ILE B 214 ? 0.4160 0.3584 0.3243 -0.0193 -0.0196 0.0099  211 ILE B CG2 
4238 C CD1 . ILE B 214 ? 0.4482 0.3867 0.3536 0.0021  -0.0209 0.0010  211 ILE B CD1 
4239 N N   . VAL B 215 ? 0.3993 0.3701 0.3265 -0.0346 -0.0208 0.0211  212 VAL B N   
4240 C CA  . VAL B 215 ? 0.3823 0.3460 0.3102 -0.0420 -0.0261 0.0244  212 VAL B CA  
4241 C C   . VAL B 215 ? 0.3702 0.3161 0.2893 -0.0401 -0.0289 0.0210  212 VAL B C   
4242 O O   . VAL B 215 ? 0.3599 0.2976 0.2708 -0.0383 -0.0260 0.0181  212 VAL B O   
4243 C CB  . VAL B 215 ? 0.3884 0.3535 0.3143 -0.0489 -0.0250 0.0279  212 VAL B CB  
4244 C CG1 . VAL B 215 ? 0.3825 0.3358 0.3068 -0.0544 -0.0317 0.0296  212 VAL B CG1 
4245 C CG2 . VAL B 215 ? 0.3977 0.3827 0.3326 -0.0526 -0.0221 0.0332  212 VAL B CG2 
4246 N N   . LEU B 216 ? 0.3567 0.2976 0.2772 -0.0411 -0.0345 0.0214  213 LEU B N   
4247 C CA  . LEU B 216 ? 0.3553 0.2821 0.2669 -0.0403 -0.0367 0.0189  213 LEU B CA  
4248 C C   . LEU B 216 ? 0.3493 0.2717 0.2587 -0.0453 -0.0390 0.0197  213 LEU B C   
4249 O O   . LEU B 216 ? 0.3382 0.2630 0.2527 -0.0493 -0.0435 0.0222  213 LEU B O   
4250 C CB  . LEU B 216 ? 0.3629 0.2863 0.2744 -0.0377 -0.0416 0.0184  213 LEU B CB  
4251 C CG  . LEU B 216 ? 0.3757 0.2878 0.2770 -0.0352 -0.0417 0.0161  213 LEU B CG  
4252 C CD1 . LEU B 216 ? 0.4069 0.3166 0.3062 -0.0309 -0.0449 0.0160  213 LEU B CD1 
4253 C CD2 . LEU B 216 ? 0.3805 0.2875 0.2777 -0.0376 -0.0449 0.0149  213 LEU B CD2 
4254 N N   . VAL B 217 ? 0.3382 0.2537 0.2405 -0.0449 -0.0369 0.0174  214 VAL B N   
4255 C CA  . VAL B 217 ? 0.3440 0.2547 0.2436 -0.0478 -0.0399 0.0171  214 VAL B CA  
4256 C C   . VAL B 217 ? 0.3400 0.2440 0.2339 -0.0449 -0.0420 0.0137  214 VAL B C   
4257 O O   . VAL B 217 ? 0.3507 0.2534 0.2403 -0.0427 -0.0382 0.0121  214 VAL B O   
4258 C CB  . VAL B 217 ? 0.3498 0.2612 0.2465 -0.0492 -0.0359 0.0171  214 VAL B CB  
4259 C CG1 . VAL B 217 ? 0.3508 0.2569 0.2446 -0.0510 -0.0398 0.0165  214 VAL B CG1 
4260 C CG2 . VAL B 217 ? 0.3626 0.2830 0.2634 -0.0513 -0.0329 0.0204  214 VAL B CG2 
4261 N N   . ALA B 218 ? 0.3367 0.2366 0.2301 -0.0448 -0.0484 0.0128  215 ALA B N   
4262 C CA  . ALA B 218 ? 0.3324 0.2282 0.2198 -0.0407 -0.0508 0.0089  215 ALA B CA  
4263 C C   . ALA B 218 ? 0.3350 0.2295 0.2186 -0.0395 -0.0502 0.0060  215 ALA B C   
4264 O O   . ALA B 218 ? 0.3380 0.2292 0.2227 -0.0408 -0.0545 0.0060  215 ALA B O   
4265 C CB  . ALA B 218 ? 0.3393 0.2310 0.2273 -0.0399 -0.0589 0.0081  215 ALA B CB  
4266 N N   . TYR B 219 ? 0.3290 0.2265 0.2086 -0.0373 -0.0456 0.0041  216 TYR B N   
4267 C CA  . TYR B 219 ? 0.3325 0.2322 0.2093 -0.0346 -0.0460 0.0003  216 TYR B CA  
4268 C C   . TYR B 219 ? 0.3403 0.2416 0.2116 -0.0292 -0.0477 -0.0032 216 TYR B C   
4269 O O   . TYR B 219 ? 0.3433 0.2442 0.2119 -0.0285 -0.0470 -0.0020 216 TYR B O   
4270 C CB  . TYR B 219 ? 0.3318 0.2367 0.2093 -0.0369 -0.0399 0.0008  216 TYR B CB  
4271 C CG  . TYR B 219 ? 0.3375 0.2461 0.2126 -0.0379 -0.0343 0.0021  216 TYR B CG  
4272 C CD1 . TYR B 219 ? 0.3479 0.2626 0.2194 -0.0354 -0.0328 0.0005  216 TYR B CD1 
4273 C CD2 . TYR B 219 ? 0.3440 0.2502 0.2200 -0.0416 -0.0307 0.0051  216 TYR B CD2 
4274 C CE1 . TYR B 219 ? 0.3572 0.2751 0.2261 -0.0381 -0.0278 0.0033  216 TYR B CE1 
4275 C CE2 . TYR B 219 ? 0.3517 0.2582 0.2248 -0.0434 -0.0269 0.0071  216 TYR B CE2 
4276 C CZ  . TYR B 219 ? 0.3584 0.2706 0.2280 -0.0426 -0.0254 0.0069  216 TYR B CZ  
4277 O OH  . TYR B 219 ? 0.3702 0.2825 0.2367 -0.0461 -0.0219 0.0104  216 TYR B OH  
4278 N N   . SER B 220 ? 0.3502 0.2542 0.2195 -0.0248 -0.0500 -0.0078 217 SER B N   
4279 C CA  . SER B 220 ? 0.3756 0.2824 0.2386 -0.0176 -0.0525 -0.0129 217 SER B CA  
4280 C C   . SER B 220 ? 0.3869 0.2838 0.2472 -0.0158 -0.0600 -0.0138 217 SER B C   
4281 O O   . SER B 220 ? 0.3903 0.2888 0.2440 -0.0113 -0.0608 -0.0161 217 SER B O   
4282 C CB  . SER B 220 ? 0.3840 0.3012 0.2434 -0.0175 -0.0449 -0.0116 217 SER B CB  
4283 O OG  . SER B 220 ? 0.3610 0.2875 0.2243 -0.0204 -0.0391 -0.0106 217 SER B OG  
4284 N N   . ALA B 221 ? 0.3842 0.2721 0.2493 -0.0197 -0.0657 -0.0116 218 ALA B N   
4285 C CA  . ALA B 221 ? 0.3957 0.2745 0.2605 -0.0200 -0.0740 -0.0116 218 ALA B CA  
4286 C C   . ALA B 221 ? 0.4159 0.2885 0.2734 -0.0120 -0.0825 -0.0190 218 ALA B C   
4287 O O   . ALA B 221 ? 0.4263 0.2915 0.2812 -0.0107 -0.0900 -0.0207 218 ALA B O   
4288 C CB  . ALA B 221 ? 0.3981 0.2709 0.2702 -0.0271 -0.0779 -0.0068 218 ALA B CB  
4289 N N   . LEU B 222 ? 0.4192 0.2944 0.2737 -0.0063 -0.0824 -0.0239 219 LEU B N   
4290 C CA  . LEU B 222 ? 0.4434 0.3127 0.2900 0.0036  -0.0911 -0.0326 219 LEU B CA  
4291 C C   . LEU B 222 ? 0.4469 0.3305 0.2866 0.0117  -0.0845 -0.0375 219 LEU B C   
4292 O O   . LEU B 222 ? 0.4704 0.3538 0.3036 0.0218  -0.0896 -0.0457 219 LEU B O   
4293 C CB  . LEU B 222 ? 0.4499 0.3117 0.2978 0.0061  -0.0975 -0.0354 219 LEU B CB  
4294 C CG  . LEU B 222 ? 0.4483 0.2966 0.3021 -0.0029 -0.1038 -0.0292 219 LEU B CG  
4295 C CD1 . LEU B 222 ? 0.4636 0.3030 0.3164 0.0007  -0.1111 -0.0320 219 LEU B CD1 
4296 C CD2 . LEU B 222 ? 0.4655 0.3007 0.3185 -0.0060 -0.1135 -0.0282 219 LEU B CD2 
4297 N N   . GLY B 223 ? 0.4302 0.3255 0.2711 0.0073  -0.0739 -0.0323 220 GLY B N   
4298 C CA  . GLY B 223 ? 0.4353 0.3450 0.2692 0.0121  -0.0668 -0.0341 220 GLY B CA  
4299 C C   . GLY B 223 ? 0.4307 0.3567 0.2677 0.0132  -0.0588 -0.0347 220 GLY B C   
4300 O O   . GLY B 223 ? 0.4464 0.3870 0.2776 0.0183  -0.0534 -0.0370 220 GLY B O   
4301 N N   . SER B 224 ? 0.4264 0.3518 0.2724 0.0075  -0.0571 -0.0316 221 SER B N   
4302 C CA  . SER B 224 ? 0.4189 0.3600 0.2704 0.0065  -0.0500 -0.0312 221 SER B CA  
4303 C C   . SER B 224 ? 0.4332 0.3817 0.2839 0.0170  -0.0539 -0.0398 221 SER B C   
4304 O O   . SER B 224 ? 0.4451 0.3877 0.2889 0.0265  -0.0613 -0.0469 221 SER B O   
4305 C CB  . SER B 224 ? 0.4184 0.3743 0.2681 0.0030  -0.0401 -0.0269 221 SER B CB  
4306 O OG  . SER B 224 ? 0.4361 0.4060 0.2791 0.0116  -0.0383 -0.0321 221 SER B OG  
4307 N N   . GLN B 225 ? 0.4310 0.3931 0.2890 0.0155  -0.0491 -0.0393 222 GLN B N   
4308 C CA  . GLN B 225 ? 0.4526 0.4265 0.3129 0.0251  -0.0515 -0.0469 222 GLN B CA  
4309 C C   . GLN B 225 ? 0.4836 0.4803 0.3400 0.0321  -0.0450 -0.0507 222 GLN B C   
4310 O O   . GLN B 225 ? 0.5021 0.5137 0.3600 0.0422  -0.0459 -0.0581 222 GLN B O   
4311 C CB  . GLN B 225 ? 0.4336 0.4134 0.3043 0.0188  -0.0491 -0.0437 222 GLN B CB  
4312 C CG  . GLN B 225 ? 0.4158 0.3742 0.2882 0.0121  -0.0548 -0.0394 222 GLN B CG  
4313 C CD  . GLN B 225 ? 0.4111 0.3706 0.2903 0.0107  -0.0571 -0.0394 222 GLN B CD  
4314 O OE1 . GLN B 225 ? 0.4418 0.4118 0.3237 0.0188  -0.0598 -0.0454 222 GLN B OE1 
4315 N NE2 . GLN B 225 ? 0.4049 0.3546 0.2864 0.0010  -0.0562 -0.0329 222 GLN B NE2 
4316 N N   . ARG B 226 ? 0.4907 0.4918 0.3425 0.0266  -0.0380 -0.0452 223 ARG B N   
4317 C CA  . ARG B 226 ? 0.5252 0.5489 0.3714 0.0313  -0.0305 -0.0465 223 ARG B CA  
4318 C C   . ARG B 226 ? 0.5416 0.5927 0.3976 0.0310  -0.0233 -0.0467 223 ARG B C   
4319 O O   . ARG B 226 ? 0.5515 0.6243 0.4053 0.0402  -0.0200 -0.0521 223 ARG B O   
4320 C CB  . ARG B 226 ? 0.5487 0.5685 0.3833 0.0460  -0.0375 -0.0566 223 ARG B CB  
4321 C CG  . ARG B 226 ? 0.5425 0.5359 0.3689 0.0452  -0.0457 -0.0561 223 ARG B CG  
4322 C CD  . ARG B 226 ? 0.5751 0.5658 0.3885 0.0597  -0.0527 -0.0665 223 ARG B CD  
4323 N NE  . ARG B 226 ? 0.5964 0.6094 0.4012 0.0643  -0.0440 -0.0670 223 ARG B NE  
4324 C CZ  . ARG B 226 ? 0.5933 0.6064 0.3900 0.0588  -0.0392 -0.0605 223 ARG B CZ  
4325 N NH1 . ARG B 226 ? 0.5725 0.5652 0.3700 0.0492  -0.0425 -0.0537 223 ARG B NH1 
4326 N NH2 . ARG B 226 ? 0.6142 0.6489 0.4020 0.0631  -0.0312 -0.0605 223 ARG B NH2 
4327 N N   . ASP B 227 ? 0.5677 0.6193 0.4348 0.0207  -0.0211 -0.0411 224 ASP B N   
4328 C CA  . ASP B 227 ? 0.6027 0.6816 0.4808 0.0180  -0.0144 -0.0401 224 ASP B CA  
4329 C C   . ASP B 227 ? 0.6166 0.7168 0.4923 0.0121  -0.0036 -0.0336 224 ASP B C   
4330 O O   . ASP B 227 ? 0.5868 0.6754 0.4586 0.0012  -0.0005 -0.0247 224 ASP B O   
4331 C CB  . ASP B 227 ? 0.6192 0.6906 0.5079 0.0069  -0.0153 -0.0349 224 ASP B CB  
4332 C CG  . ASP B 227 ? 0.6677 0.7673 0.5688 0.0047  -0.0103 -0.0349 224 ASP B CG  
4333 O OD1 . ASP B 227 ? 0.7057 0.8271 0.6083 -0.0002 -0.0016 -0.0303 224 ASP B OD1 
4334 O OD2 . ASP B 227 ? 0.7140 0.8147 0.6230 0.0083  -0.0156 -0.0394 224 ASP B OD2 
4335 N N   . LYS B 228 ? 0.6548 0.7862 0.5342 0.0183  0.0019  -0.0372 225 LYS B N   
4336 C CA  . LYS B 228 ? 0.7090 0.8662 0.5852 0.0143  0.0126  -0.0313 225 LYS B CA  
4337 C C   . LYS B 228 ? 0.6810 0.8377 0.5629 -0.0050 0.0187  -0.0180 225 LYS B C   
4338 O O   . LYS B 228 ? 0.6910 0.8517 0.5648 -0.0115 0.0249  -0.0100 225 LYS B O   
4339 C CB  . LYS B 228 ? 0.7713 0.9668 0.6578 0.0208  0.0178  -0.0361 225 LYS B CB  
4340 C CG  . LYS B 228 ? 0.8364 1.0478 0.7153 0.0407  0.0167  -0.0483 225 LYS B CG  
4341 C CD  . LYS B 228 ? 0.8918 1.1446 0.7833 0.0468  0.0224  -0.0528 225 LYS B CD  
4342 C CE  . LYS B 228 ? 0.9595 1.2374 0.8415 0.0643  0.0260  -0.0620 225 LYS B CE  
4343 N NZ  . LYS B 228 ? 1.0017 1.2658 0.8640 0.0650  0.0277  -0.0593 225 LYS B NZ  
4344 N N   . ARG B 229 ? 0.6524 0.8034 0.5466 -0.0133 0.0161  -0.0158 226 ARG B N   
4345 C CA  . ARG B 229 ? 0.6454 0.7964 0.5460 -0.0312 0.0205  -0.0043 226 ARG B CA  
4346 C C   . ARG B 229 ? 0.6092 0.7302 0.4987 -0.0384 0.0188  0.0026  226 ARG B C   
4347 O O   . ARG B 229 ? 0.6015 0.7217 0.4914 -0.0518 0.0228  0.0127  226 ARG B O   
4348 C CB  . ARG B 229 ? 0.6723 0.8203 0.5867 -0.0366 0.0161  -0.0054 226 ARG B CB  
4349 C CG  . ARG B 229 ? 0.7336 0.9131 0.6614 -0.0308 0.0173  -0.0113 226 ARG B CG  
4350 C CD  . ARG B 229 ? 0.7730 0.9451 0.7122 -0.0349 0.0111  -0.0131 226 ARG B CD  
4351 N NE  . ARG B 229 ? 0.7967 0.9478 0.7318 -0.0230 0.0020  -0.0218 226 ARG B NE  
4352 C CZ  . ARG B 229 ? 0.8349 0.9972 0.7750 -0.0100 -0.0026 -0.0313 226 ARG B CZ  
4353 N NH1 . ARG B 229 ? 0.8743 1.0714 0.8248 -0.0056 0.0014  -0.0344 226 ARG B NH1 
4354 N NH2 . ARG B 229 ? 0.7969 0.9358 0.7314 -0.0011 -0.0116 -0.0374 226 ARG B NH2 
4355 N N   . TRP B 230 ? 0.5809 0.6775 0.4621 -0.0303 0.0122  -0.0026 227 TRP B N   
4356 C CA  . TRP B 230 ? 0.5710 0.6389 0.4443 -0.0362 0.0093  0.0029  227 TRP B CA  
4357 C C   . TRP B 230 ? 0.5671 0.6272 0.4262 -0.0288 0.0084  0.0017  227 TRP B C   
4358 O O   . TRP B 230 ? 0.5804 0.6247 0.4325 -0.0346 0.0083  0.0082  227 TRP B O   
4359 C CB  . TRP B 230 ? 0.5676 0.6132 0.4451 -0.0355 0.0018  -0.0007 227 TRP B CB  
4360 C CG  . TRP B 230 ? 0.5639 0.6135 0.4531 -0.0434 0.0018  0.0009  227 TRP B CG  
4361 C CD1 . TRP B 230 ? 0.5692 0.6282 0.4675 -0.0390 -0.0011 -0.0053 227 TRP B CD1 
4362 C CD2 . TRP B 230 ? 0.5801 0.6244 0.4727 -0.0568 0.0039  0.0089  227 TRP B CD2 
4363 N NE1 . TRP B 230 ? 0.5699 0.6300 0.4770 -0.0488 -0.0010 -0.0018 227 TRP B NE1 
4364 C CE2 . TRP B 230 ? 0.5838 0.6348 0.4876 -0.0600 0.0020  0.0067  227 TRP B CE2 
4365 C CE3 . TRP B 230 ? 0.6051 0.6373 0.4915 -0.0659 0.0059  0.0173  227 TRP B CE3 
4366 C CZ2 . TRP B 230 ? 0.5907 0.6371 0.4998 -0.0723 0.0019  0.0122  227 TRP B CZ2 
4367 C CZ3 . TRP B 230 ? 0.6169 0.6430 0.5082 -0.0777 0.0056  0.0228  227 TRP B CZ3 
4368 C CH2 . TRP B 230 ? 0.6046 0.6375 0.5071 -0.0810 0.0036  0.0200  227 TRP B CH2 
4369 N N   . VAL B 231 ? 0.5674 0.6372 0.4222 -0.0157 0.0067  -0.0070 228 VAL B N   
4370 C CA  . VAL B 231 ? 0.5647 0.6223 0.4060 -0.0065 0.0025  -0.0110 228 VAL B CA  
4371 C C   . VAL B 231 ? 0.5877 0.6696 0.4207 0.0014  0.0080  -0.0136 228 VAL B C   
4372 O O   . VAL B 231 ? 0.5856 0.6878 0.4231 0.0098  0.0092  -0.0208 228 VAL B O   
4373 C CB  . VAL B 231 ? 0.5506 0.5911 0.3927 0.0030  -0.0076 -0.0205 228 VAL B CB  
4374 C CG1 . VAL B 231 ? 0.5566 0.5846 0.3853 0.0116  -0.0132 -0.0247 228 VAL B CG1 
4375 C CG2 . VAL B 231 ? 0.5220 0.5419 0.3720 -0.0047 -0.0121 -0.0175 228 VAL B CG2 
4376 N N   . ASP B 232 ? 0.6125 0.6923 0.4330 -0.0009 0.0110  -0.0078 229 ASP B N   
4377 C CA  . ASP B 232 ? 0.6569 0.7564 0.4645 0.0078  0.0157  -0.0102 229 ASP B CA  
4378 C C   . ASP B 232 ? 0.6662 0.7640 0.4683 0.0255  0.0083  -0.0246 229 ASP B C   
4379 O O   . ASP B 232 ? 0.6465 0.7192 0.4432 0.0299  -0.0011 -0.0290 229 ASP B O   
4380 C CB  . ASP B 232 ? 0.6668 0.7555 0.4602 0.0025  0.0171  -0.0014 229 ASP B CB  
4381 C CG  . ASP B 232 ? 0.7078 0.8190 0.4866 0.0082  0.0238  -0.0006 229 ASP B CG  
4382 O OD1 . ASP B 232 ? 0.7244 0.8583 0.5028 0.0193  0.0263  -0.0092 229 ASP B OD1 
4383 O OD2 . ASP B 232 ? 0.7361 0.8414 0.5033 0.0022  0.0261  0.0085  229 ASP B OD2 
4384 N N   . PRO B 233 ? 0.6917 0.8163 0.4945 0.0363  0.0117  -0.0325 230 PRO B N   
4385 C CA  . PRO B 233 ? 0.7042 0.8252 0.5000 0.0545  0.0034  -0.0472 230 PRO B CA  
4386 C C   . PRO B 233 ? 0.7199 0.8310 0.4958 0.0622  0.0000  -0.0500 230 PRO B C   
4387 O O   . PRO B 233 ? 0.7294 0.8278 0.4982 0.0754  -0.0099 -0.0615 230 PRO B O   
4388 C CB  . PRO B 233 ? 0.7290 0.8856 0.5298 0.0646  0.0095  -0.0541 230 PRO B CB  
4389 C CG  . PRO B 233 ? 0.7295 0.9098 0.5431 0.0491  0.0214  -0.0419 230 PRO B CG  
4390 C CD  . PRO B 233 ? 0.7123 0.8726 0.5227 0.0322  0.0231  -0.0281 230 PRO B CD  
4391 N N   . ASN B 234 ? 0.7248 0.8410 0.4915 0.0540  0.0071  -0.0396 231 ASN B N   
4392 C CA  . ASN B 234 ? 0.7513 0.8580 0.4976 0.0608  0.0036  -0.0414 231 ASN B CA  
4393 C C   . ASN B 234 ? 0.7150 0.7856 0.4604 0.0559  -0.0071 -0.0395 231 ASN B C   
4394 O O   . ASN B 234 ? 0.7285 0.7868 0.4591 0.0633  -0.0139 -0.0440 231 ASN B O   
4395 C CB  . ASN B 234 ? 0.7869 0.9130 0.5221 0.0542  0.0149  -0.0303 231 ASN B CB  
4396 C CG  . ASN B 234 ? 0.8204 0.9867 0.5561 0.0588  0.0265  -0.0313 231 ASN B CG  
4397 O OD1 . ASN B 234 ? 0.8385 1.0190 0.5738 0.0743  0.0246  -0.0446 231 ASN B OD1 
4398 N ND2 . ASN B 234 ? 0.8346 1.0199 0.5717 0.0452  0.0380  -0.0172 231 ASN B ND2 
4399 N N   . SER B 235 ? 0.6735 0.7293 0.4343 0.0443  -0.0089 -0.0338 232 SER B N   
4400 C CA  . SER B 235 ? 0.6410 0.6662 0.4037 0.0394  -0.0182 -0.0318 232 SER B CA  
4401 C C   . SER B 235 ? 0.6470 0.6565 0.4057 0.0515  -0.0309 -0.0443 232 SER B C   
4402 O O   . SER B 235 ? 0.6501 0.6651 0.4117 0.0608  -0.0341 -0.0539 232 SER B O   
4403 C CB  . SER B 235 ? 0.6130 0.6288 0.3923 0.0268  -0.0172 -0.0248 232 SER B CB  
4404 O OG  . SER B 235 ? 0.5891 0.6040 0.3795 0.0305  -0.0213 -0.0320 232 SER B OG  
4405 N N   . PRO B 236 ? 0.6487 0.6372 0.4006 0.0516  -0.0396 -0.0444 233 PRO B N   
4406 C CA  . PRO B 236 ? 0.6528 0.6238 0.4010 0.0611  -0.0533 -0.0553 233 PRO B CA  
4407 C C   . PRO B 236 ? 0.6218 0.5826 0.3849 0.0592  -0.0589 -0.0585 233 PRO B C   
4408 O O   . PRO B 236 ? 0.5881 0.5460 0.3644 0.0479  -0.0551 -0.0505 233 PRO B O   
4409 C CB  . PRO B 236 ? 0.6510 0.6031 0.3947 0.0564  -0.0602 -0.0510 233 PRO B CB  
4410 C CG  . PRO B 236 ? 0.6333 0.5892 0.3832 0.0432  -0.0507 -0.0375 233 PRO B CG  
4411 C CD  . PRO B 236 ? 0.6415 0.6216 0.3895 0.0424  -0.0378 -0.0340 233 PRO B CD  
4412 N N   . VAL B 237 ? 0.6297 0.5845 0.3893 0.0708  -0.0683 -0.0702 234 VAL B N   
4413 C CA  . VAL B 237 ? 0.6230 0.5665 0.3941 0.0706  -0.0753 -0.0738 234 VAL B CA  
4414 C C   . VAL B 237 ? 0.6000 0.5168 0.3746 0.0647  -0.0874 -0.0723 234 VAL B C   
4415 O O   . VAL B 237 ? 0.6146 0.5174 0.3796 0.0723  -0.0991 -0.0799 234 VAL B O   
4416 C CB  . VAL B 237 ? 0.6609 0.6092 0.4261 0.0867  -0.0809 -0.0872 234 VAL B CB  
4417 C CG1 . VAL B 237 ? 0.6545 0.5876 0.4300 0.0863  -0.0898 -0.0900 234 VAL B CG1 
4418 C CG2 . VAL B 237 ? 0.6686 0.6485 0.4319 0.0931  -0.0684 -0.0889 234 VAL B CG2 
4419 N N   . LEU B 238 ? 0.5543 0.4647 0.3422 0.0519  -0.0851 -0.0631 235 LEU B N   
4420 C CA  . LEU B 238 ? 0.5391 0.4291 0.3319 0.0445  -0.0946 -0.0597 235 LEU B CA  
4421 C C   . LEU B 238 ? 0.5635 0.4350 0.3535 0.0510  -0.1100 -0.0684 235 LEU B C   
4422 O O   . LEU B 238 ? 0.5702 0.4272 0.3562 0.0506  -0.1202 -0.0700 235 LEU B O   
4423 C CB  . LEU B 238 ? 0.5050 0.3935 0.3124 0.0314  -0.0895 -0.0497 235 LEU B CB  
4424 C CG  . LEU B 238 ? 0.4943 0.3669 0.3080 0.0234  -0.0977 -0.0453 235 LEU B CG  
4425 C CD1 . LEU B 238 ? 0.4945 0.3679 0.3036 0.0216  -0.0969 -0.0420 235 LEU B CD1 
4426 C CD2 . LEU B 238 ? 0.4718 0.3438 0.2989 0.0127  -0.0935 -0.0374 235 LEU B CD2 
4427 N N   . LEU B 239 ? 0.5746 0.4452 0.3669 0.0564  -0.1127 -0.0736 236 LEU B N   
4428 C CA  . LEU B 239 ? 0.6036 0.4518 0.3949 0.0601  -0.1286 -0.0799 236 LEU B CA  
4429 C C   . LEU B 239 ? 0.6551 0.4959 0.4310 0.0749  -0.1392 -0.0926 236 LEU B C   
4430 O O   . LEU B 239 ? 0.6776 0.4970 0.4508 0.0787  -0.1543 -0.0986 236 LEU B O   
4431 C CB  . LEU B 239 ? 0.5990 0.4485 0.3976 0.0611  -0.1279 -0.0804 236 LEU B CB  
4432 C CG  . LEU B 239 ? 0.5645 0.4165 0.3768 0.0463  -0.1204 -0.0684 236 LEU B CG  
4433 C CD1 . LEU B 239 ? 0.5645 0.4130 0.3823 0.0475  -0.1231 -0.0692 236 LEU B CD1 
4434 C CD2 . LEU B 239 ? 0.5536 0.3907 0.3711 0.0343  -0.1260 -0.0607 236 LEU B CD2 
4435 N N   . GLU B 240 ? 0.6714 0.5289 0.4368 0.0828  -0.1318 -0.0964 237 GLU B N   
4436 C CA  . GLU B 240 ? 0.7273 0.5792 0.4753 0.0974  -0.1412 -0.1088 237 GLU B CA  
4437 C C   . GLU B 240 ? 0.7364 0.5834 0.4782 0.0928  -0.1436 -0.1054 237 GLU B C   
4438 O O   . GLU B 240 ? 0.7895 0.6308 0.5158 0.1042  -0.1520 -0.1153 237 GLU B O   
4439 C CB  . GLU B 240 ? 0.7496 0.6265 0.4881 0.1113  -0.1314 -0.1161 237 GLU B CB  
4440 C CG  . GLU B 240 ? 0.7675 0.6497 0.5114 0.1191  -0.1316 -0.1219 237 GLU B CG  
4441 C CD  . GLU B 240 ? 0.7932 0.7052 0.5305 0.1324  -0.1208 -0.1287 237 GLU B CD  
4442 O OE1 . GLU B 240 ? 0.8085 0.7369 0.5357 0.1351  -0.1126 -0.1282 237 GLU B OE1 
4443 O OE2 . GLU B 240 ? 0.8059 0.7260 0.5484 0.1401  -0.1206 -0.1341 237 GLU B OE2 
4444 N N   . ASP B 241 ? 0.6985 0.5469 0.4510 0.0780  -0.1374 -0.0930 238 ASP B N   
4445 C CA  . ASP B 241 ? 0.7114 0.5553 0.4594 0.0737  -0.1404 -0.0894 238 ASP B CA  
4446 C C   . ASP B 241 ? 0.7360 0.5566 0.4770 0.0783  -0.1598 -0.0980 238 ASP B C   
4447 O O   . ASP B 241 ? 0.7189 0.5216 0.4682 0.0734  -0.1708 -0.0983 238 ASP B O   
4448 C CB  . ASP B 241 ? 0.6829 0.5280 0.4465 0.0576  -0.1343 -0.0759 238 ASP B CB  
4449 C CG  . ASP B 241 ? 0.7007 0.5460 0.4599 0.0545  -0.1351 -0.0719 238 ASP B CG  
4450 O OD1 . ASP B 241 ? 0.7129 0.5731 0.4650 0.0561  -0.1241 -0.0683 238 ASP B OD1 
4451 O OD2 . ASP B 241 ? 0.7434 0.5735 0.5051 0.0512  -0.1480 -0.0727 238 ASP B OD2 
4452 N N   . PRO B 242 ? 0.7799 0.5990 0.5047 0.0873  -0.1655 -0.1050 239 PRO B N   
4453 C CA  . PRO B 242 ? 0.8127 0.6082 0.5296 0.0923  -0.1856 -0.1145 239 PRO B CA  
4454 C C   . PRO B 242 ? 0.7896 0.5683 0.5212 0.0771  -0.1961 -0.1068 239 PRO B C   
4455 O O   . PRO B 242 ? 0.8175 0.5745 0.5505 0.0765  -0.2125 -0.1118 239 PRO B O   
4456 C CB  . PRO B 242 ? 0.8527 0.6545 0.5490 0.1039  -0.1864 -0.1216 239 PRO B CB  
4457 C CG  . PRO B 242 ? 0.8288 0.6552 0.5263 0.0991  -0.1672 -0.1110 239 PRO B CG  
4458 C CD  . PRO B 242 ? 0.7856 0.6245 0.4973 0.0934  -0.1538 -0.1045 239 PRO B CD  
4459 N N   . VAL B 243 ? 0.7467 0.5363 0.4908 0.0646  -0.1864 -0.0942 240 VAL B N   
4460 C CA  . VAL B 243 ? 0.7294 0.5097 0.4903 0.0496  -0.1937 -0.0856 240 VAL B CA  
4461 C C   . VAL B 243 ? 0.7115 0.4837 0.4867 0.0411  -0.1954 -0.0813 240 VAL B C   
4462 O O   . VAL B 243 ? 0.7107 0.4652 0.4925 0.0344  -0.2100 -0.0811 240 VAL B O   
4463 C CB  . VAL B 243 ? 0.7046 0.5013 0.4734 0.0415  -0.1814 -0.0745 240 VAL B CB  
4464 C CG1 . VAL B 243 ? 0.6791 0.4734 0.4684 0.0263  -0.1845 -0.0645 240 VAL B CG1 
4465 C CG2 . VAL B 243 ? 0.7303 0.5303 0.4841 0.0489  -0.1837 -0.0782 240 VAL B CG2 
4466 N N   . LEU B 244 ? 0.6774 0.4623 0.4574 0.0407  -0.1813 -0.0773 241 LEU B N   
4467 C CA  . LEU B 244 ? 0.6788 0.4563 0.4699 0.0341  -0.1828 -0.0736 241 LEU B CA  
4468 C C   . LEU B 244 ? 0.7221 0.4781 0.5041 0.0426  -0.1990 -0.0843 241 LEU B C   
4469 O O   . LEU B 244 ? 0.7307 0.4703 0.5208 0.0342  -0.2094 -0.0809 241 LEU B O   
4470 C CB  . LEU B 244 ? 0.6463 0.4419 0.4410 0.0347  -0.1655 -0.0696 241 LEU B CB  
4471 C CG  . LEU B 244 ? 0.6107 0.4244 0.4139 0.0264  -0.1504 -0.0592 241 LEU B CG  
4472 C CD1 . LEU B 244 ? 0.5824 0.4088 0.3917 0.0244  -0.1368 -0.0548 241 LEU B CD1 
4473 C CD2 . LEU B 244 ? 0.5986 0.4086 0.4153 0.0133  -0.1539 -0.0502 241 LEU B CD2 
4474 N N   . CYS B 245 ? 0.7677 0.5239 0.5330 0.0589  -0.2012 -0.0967 242 CYS B N   
4475 C CA  . CYS B 245 ? 0.8217 0.5566 0.5758 0.0705  -0.2178 -0.1094 242 CYS B CA  
4476 C C   . CYS B 245 ? 0.8479 0.5568 0.5997 0.0665  -0.2387 -0.1124 242 CYS B C   
4477 O O   . CYS B 245 ? 0.8655 0.5512 0.6185 0.0647  -0.2535 -0.1147 242 CYS B O   
4478 C CB  . CYS B 245 ? 0.8623 0.6085 0.5989 0.0899  -0.2134 -0.1221 242 CYS B CB  
4479 S SG  . CYS B 245 ? 0.8664 0.6396 0.6089 0.0932  -0.1928 -0.1188 242 CYS B SG  
4480 N N   . ALA B 246 ? 0.8512 0.5633 0.6002 0.0642  -0.2408 -0.1118 243 ALA B N   
4481 C CA  . ALA B 246 ? 0.8798 0.5700 0.6294 0.0579  -0.2606 -0.1133 243 ALA B CA  
4482 C C   . ALA B 246 ? 0.8557 0.5388 0.6263 0.0378  -0.2642 -0.0998 243 ALA B C   
4483 O O   . ALA B 246 ? 0.8858 0.5441 0.6583 0.0323  -0.2826 -0.1010 243 ALA B O   
4484 C CB  . ALA B 246 ? 0.8845 0.5844 0.6280 0.0596  -0.2595 -0.1143 243 ALA B CB  
4485 N N   . LEU B 247 ? 0.8067 0.5107 0.5924 0.0267  -0.2478 -0.0870 244 LEU B N   
4486 C CA  . LEU B 247 ? 0.7898 0.4918 0.5954 0.0080  -0.2492 -0.0737 244 LEU B CA  
4487 C C   . LEU B 247 ? 0.8023 0.4883 0.6092 0.0060  -0.2548 -0.0729 244 LEU B C   
4488 O O   . LEU B 247 ? 0.8169 0.4880 0.6336 -0.0073 -0.2665 -0.0660 244 LEU B O   
4489 C CB  . LEU B 247 ? 0.7400 0.4690 0.5585 0.0002  -0.2292 -0.0622 244 LEU B CB  
4490 C CG  . LEU B 247 ? 0.7276 0.4695 0.5483 -0.0013 -0.2266 -0.0603 244 LEU B CG  
4491 C CD1 . LEU B 247 ? 0.6785 0.4446 0.5107 -0.0072 -0.2076 -0.0499 244 LEU B CD1 
4492 C CD2 . LEU B 247 ? 0.7477 0.4788 0.5780 -0.0122 -0.2429 -0.0573 244 LEU B CD2 
4493 N N   . ALA B 248 ? 0.8028 0.4925 0.6010 0.0180  -0.2470 -0.0788 245 ALA B N   
4494 C CA  . ALA B 248 ? 0.8319 0.5057 0.6294 0.0187  -0.2531 -0.0792 245 ALA B CA  
4495 C C   . ALA B 248 ? 0.9061 0.5468 0.6945 0.0216  -0.2779 -0.0874 245 ALA B C   
4496 O O   . ALA B 248 ? 0.9285 0.5503 0.7237 0.0102  -0.2891 -0.0806 245 ALA B O   
4497 C CB  . ALA B 248 ? 0.8141 0.5003 0.6036 0.0332  -0.2414 -0.0860 245 ALA B CB  
4498 N N   . LYS B 249 ? 0.9567 0.5897 0.7301 0.0354  -0.2871 -0.1010 246 LYS B N   
4499 C CA  . LYS B 249 ? 1.0445 0.6431 0.8072 0.0396  -0.3126 -0.1106 246 LYS B CA  
4500 C C   . LYS B 249 ? 1.0564 0.6418 0.8322 0.0193  -0.3254 -0.1001 246 LYS B C   
4501 O O   . LYS B 249 ? 1.1107 0.6700 0.8891 0.0110  -0.3416 -0.0968 246 LYS B O   
4502 C CB  . LYS B 249 ? 1.0859 0.6823 0.8294 0.0583  -0.3186 -0.1272 246 LYS B CB  
4503 C CG  . LYS B 249 ? 1.1096 0.7105 0.8369 0.0807  -0.3140 -0.1411 246 LYS B CG  
4504 C CD  . LYS B 249 ? 1.1802 0.7687 0.8867 0.0982  -0.3277 -0.1585 246 LYS B CD  
4505 C CE  . LYS B 249 ? 1.2487 0.8000 0.9524 0.0921  -0.3550 -0.1619 246 LYS B CE  
4506 N NZ  . LYS B 249 ? 1.3227 0.8545 1.0032 0.1120  -0.3723 -0.1817 246 LYS B NZ  
4507 N N   . LYS B 250 ? 1.0383 0.6427 0.8231 0.0110  -0.3181 -0.0940 247 LYS B N   
4508 C CA  . LYS B 250 ? 1.0531 0.6524 0.8533 -0.0087 -0.3283 -0.0834 247 LYS B CA  
4509 C C   . LYS B 250 ? 1.0339 0.6274 0.8493 -0.0262 -0.3289 -0.0690 247 LYS B C   
4510 O O   . LYS B 250 ? 1.0858 0.6552 0.9048 -0.0375 -0.3482 -0.0657 247 LYS B O   
4511 C CB  . LYS B 250 ? 1.0337 0.6625 0.8444 -0.0141 -0.3141 -0.0769 247 LYS B CB  
4512 C CG  . LYS B 250 ? 1.0246 0.6622 0.8582 -0.0362 -0.3148 -0.0613 247 LYS B CG  
4513 C CD  . LYS B 250 ? 1.0262 0.6823 0.8670 -0.0393 -0.3120 -0.0594 247 LYS B CD  
4514 C CE  . LYS B 250 ? 1.0101 0.6814 0.8756 -0.0599 -0.3094 -0.0437 247 LYS B CE  
4515 N NZ  . LYS B 250 ? 0.9894 0.6832 0.8625 -0.0604 -0.3037 -0.0421 247 LYS B NZ  
4516 N N   . HIS B 251 ? 0.9707 0.5848 0.7938 -0.0288 -0.3093 -0.0605 248 HIS B N   
4517 C CA  . HIS B 251 ? 0.9501 0.5647 0.7877 -0.0461 -0.3064 -0.0451 248 HIS B CA  
4518 C C   . HIS B 251 ? 0.9641 0.5559 0.7921 -0.0406 -0.3138 -0.0479 248 HIS B C   
4519 O O   . HIS B 251 ? 0.9557 0.5473 0.7930 -0.0536 -0.3108 -0.0352 248 HIS B O   
4520 C CB  . HIS B 251 ? 0.8993 0.5485 0.7494 -0.0510 -0.2816 -0.0350 248 HIS B CB  
4521 C CG  . HIS B 251 ? 0.8853 0.5561 0.7487 -0.0599 -0.2755 -0.0288 248 HIS B CG  
4522 N ND1 . HIS B 251 ? 0.8947 0.5732 0.7765 -0.0792 -0.2770 -0.0150 248 HIS B ND1 
4523 C CD2 . HIS B 251 ? 0.8537 0.5408 0.7148 -0.0520 -0.2684 -0.0342 248 HIS B CD2 
4524 C CE1 . HIS B 251 ? 0.8763 0.5752 0.7673 -0.0817 -0.2715 -0.0132 248 HIS B CE1 
4525 N NE2 . HIS B 251 ? 0.8475 0.5505 0.7254 -0.0653 -0.2665 -0.0246 248 HIS B NE2 
4526 N N   . LYS B 252 ? 0.9830 0.5585 0.7928 -0.0212 -0.3220 -0.0638 249 LYS B N   
4527 C CA  . LYS B 252 ? 1.0093 0.5649 0.8080 -0.0110 -0.3286 -0.0695 249 LYS B CA  
4528 C C   . LYS B 252 ? 0.9470 0.5250 0.7532 -0.0131 -0.3083 -0.0608 249 LYS B C   
4529 O O   . LYS B 252 ? 0.9456 0.5107 0.7540 -0.0201 -0.3126 -0.0532 249 LYS B O   
4530 C CB  . LYS B 252 ? 1.0876 0.6067 0.8856 -0.0217 -0.3518 -0.0648 249 LYS B CB  
4531 C CG  . LYS B 252 ? 1.1510 0.6501 0.9510 -0.0324 -0.3718 -0.0643 249 LYS B CG  
4532 C CD  . LYS B 252 ? 1.2055 0.6822 1.0151 -0.0547 -0.3865 -0.0491 249 LYS B CD  
4533 C CE  . LYS B 252 ? 1.1805 0.6873 1.0117 -0.0760 -0.3697 -0.0297 249 LYS B CE  
4534 N NZ  . LYS B 252 ? 1.1853 0.7107 1.0281 -0.0843 -0.3676 -0.0276 249 LYS B NZ  
4535 N N   . ARG B 253 ? 0.8993 0.5092 0.7091 -0.0083 -0.2874 -0.0611 250 ARG B N   
4536 C CA  . ARG B 253 ? 0.8509 0.4839 0.6673 -0.0095 -0.2674 -0.0540 250 ARG B CA  
4537 C C   . ARG B 253 ? 0.8294 0.4768 0.6352 0.0103  -0.2573 -0.0669 250 ARG B C   
4538 O O   . ARG B 253 ? 0.8631 0.4961 0.6554 0.0248  -0.2690 -0.0804 250 ARG B O   
4539 C CB  . ARG B 253 ? 0.8204 0.4779 0.6529 -0.0253 -0.2526 -0.0403 250 ARG B CB  
4540 C CG  . ARG B 253 ? 0.8460 0.4933 0.6901 -0.0454 -0.2616 -0.0267 250 ARG B CG  
4541 C CD  . ARG B 253 ? 0.8644 0.4970 0.7087 -0.0522 -0.2664 -0.0189 250 ARG B CD  
4542 N NE  . ARG B 253 ? 0.8996 0.5208 0.7535 -0.0720 -0.2771 -0.0057 250 ARG B NE  
4543 C CZ  . ARG B 253 ? 0.9247 0.5373 0.7817 -0.0839 -0.2798 0.0062  250 ARG B CZ  
4544 N NH1 . ARG B 253 ? 0.9044 0.5172 0.7556 -0.0774 -0.2731 0.0062  250 ARG B NH1 
4545 N NH2 . ARG B 253 ? 0.9602 0.5653 0.8266 -0.1030 -0.2892 0.0187  250 ARG B NH2 
4546 N N   . THR B 254 ? 0.7881 0.4626 0.5996 0.0108  -0.2372 -0.0628 251 THR B N   
4547 C CA  . THR B 254 ? 0.7600 0.4536 0.5640 0.0271  -0.2250 -0.0725 251 THR B CA  
4548 C C   . THR B 254 ? 0.7137 0.4340 0.5239 0.0225  -0.2078 -0.0674 251 THR B C   
4549 O O   . THR B 254 ? 0.6819 0.4084 0.5036 0.0080  -0.2029 -0.0561 251 THR B O   
4550 C CB  . THR B 254 ? 0.7490 0.4474 0.5541 0.0314  -0.2189 -0.0719 251 THR B CB  
4551 O OG1 . THR B 254 ? 0.7181 0.4308 0.5362 0.0168  -0.2060 -0.0582 251 THR B OG1 
4552 C CG2 . THR B 254 ? 0.7897 0.4594 0.5887 0.0354  -0.2370 -0.0757 251 THR B CG2 
4553 N N   . PRO B 255 ? 0.7031 0.4403 0.5055 0.0349  -0.1985 -0.0754 252 PRO B N   
4554 C CA  . PRO B 255 ? 0.6715 0.4322 0.4784 0.0309  -0.1825 -0.0699 252 PRO B CA  
4555 C C   . PRO B 255 ? 0.6236 0.3982 0.4439 0.0190  -0.1689 -0.0579 252 PRO B C   
4556 O O   . PRO B 255 ? 0.5940 0.3778 0.4221 0.0096  -0.1621 -0.0500 252 PRO B O   
4557 C CB  . PRO B 255 ? 0.6773 0.4531 0.4726 0.0466  -0.1748 -0.0799 252 PRO B CB  
4558 C CG  . PRO B 255 ? 0.7235 0.4808 0.5060 0.0604  -0.1908 -0.0932 252 PRO B CG  
4559 C CD  . PRO B 255 ? 0.7369 0.4715 0.5252 0.0537  -0.2033 -0.0898 252 PRO B CD  
4560 N N   . ALA B 256 ? 0.6142 0.3896 0.4364 0.0208  -0.1660 -0.0575 253 ALA B N   
4561 C CA  . ALA B 256 ? 0.5772 0.3644 0.4103 0.0106  -0.1542 -0.0472 253 ALA B CA  
4562 C C   . ALA B 256 ? 0.5716 0.3512 0.4144 -0.0046 -0.1581 -0.0365 253 ALA B C   
4563 O O   . ALA B 256 ? 0.5476 0.3415 0.3985 -0.0127 -0.1471 -0.0288 253 ALA B O   
4564 C CB  . ALA B 256 ? 0.5807 0.3668 0.4131 0.0154  -0.1540 -0.0494 253 ALA B CB  
4565 N N   . LEU B 257 ? 0.6089 0.3670 0.4507 -0.0083 -0.1736 -0.0361 254 LEU B N   
4566 C CA  . LEU B 257 ? 0.6132 0.3661 0.4653 -0.0242 -0.1777 -0.0248 254 LEU B CA  
4567 C C   . LEU B 257 ? 0.6071 0.3702 0.4648 -0.0290 -0.1749 -0.0224 254 LEU B C   
4568 O O   . LEU B 257 ? 0.5923 0.3668 0.4613 -0.0403 -0.1682 -0.0125 254 LEU B O   
4569 C CB  . LEU B 257 ? 0.6546 0.3805 0.5035 -0.0274 -0.1966 -0.0249 254 LEU B CB  
4570 C CG  . LEU B 257 ? 0.6759 0.3917 0.5226 -0.0275 -0.1993 -0.0224 254 LEU B CG  
4571 C CD1 . LEU B 257 ? 0.7308 0.4155 0.5709 -0.0279 -0.2205 -0.0245 254 LEU B CD1 
4572 C CD2 . LEU B 257 ? 0.6561 0.3838 0.5132 -0.0415 -0.1892 -0.0087 254 LEU B CD2 
4573 N N   . ILE B 258 ? 0.6138 0.3743 0.4632 -0.0197 -0.1795 -0.0314 255 ILE B N   
4574 C CA  . ILE B 258 ? 0.6056 0.3758 0.4592 -0.0231 -0.1775 -0.0295 255 ILE B CA  
4575 C C   . ILE B 258 ? 0.5568 0.3502 0.4164 -0.0248 -0.1591 -0.0240 255 ILE B C   
4576 O O   . ILE B 258 ? 0.5272 0.3302 0.3978 -0.0342 -0.1552 -0.0160 255 ILE B O   
4577 C CB  . ILE B 258 ? 0.6369 0.4000 0.4776 -0.0112 -0.1856 -0.0409 255 ILE B CB  
4578 C CG1 . ILE B 258 ? 0.6905 0.4274 0.5243 -0.0088 -0.2058 -0.0474 255 ILE B CG1 
4579 C CG2 . ILE B 258 ? 0.6341 0.4076 0.4785 -0.0143 -0.1835 -0.0385 255 ILE B CG2 
4580 C CD1 . ILE B 258 ? 0.7089 0.4341 0.5537 -0.0239 -0.2178 -0.0393 255 ILE B CD1 
4581 N N   . ALA B 259 ? 0.5375 0.3395 0.3905 -0.0163 -0.1489 -0.0280 256 ALA B N   
4582 C CA  . ALA B 259 ? 0.5094 0.3308 0.3658 -0.0170 -0.1327 -0.0239 256 ALA B CA  
4583 C C   . ALA B 259 ? 0.4896 0.3173 0.3581 -0.0280 -0.1263 -0.0140 256 ALA B C   
4584 O O   . ALA B 259 ? 0.4825 0.3235 0.3570 -0.0315 -0.1164 -0.0090 256 ALA B O   
4585 C CB  . ALA B 259 ? 0.5046 0.3333 0.3525 -0.0071 -0.1248 -0.0297 256 ALA B CB  
4586 N N   . LEU B 260 ? 0.4929 0.3116 0.3637 -0.0322 -0.1312 -0.0116 257 LEU B N   
4587 C CA  . LEU B 260 ? 0.4870 0.3122 0.3674 -0.0423 -0.1251 -0.0022 257 LEU B CA  
4588 C C   . LEU B 260 ? 0.4984 0.3261 0.3891 -0.0526 -0.1289 0.0050  257 LEU B C   
4589 O O   . LEU B 260 ? 0.4843 0.3270 0.3834 -0.0581 -0.1193 0.0115  257 LEU B O   
4590 C CB  . LEU B 260 ? 0.4943 0.3074 0.3723 -0.0438 -0.1310 -0.0011 257 LEU B CB  
4591 C CG  . LEU B 260 ? 0.4929 0.3065 0.3636 -0.0346 -0.1270 -0.0071 257 LEU B CG  
4592 C CD1 . LEU B 260 ? 0.5125 0.3128 0.3816 -0.0373 -0.1345 -0.0046 257 LEU B CD1 
4593 C CD2 . LEU B 260 ? 0.4561 0.2878 0.3293 -0.0341 -0.1117 -0.0054 257 LEU B CD2 
4594 N N   . ARG B 261 ? 0.5261 0.3399 0.4164 -0.0549 -0.1430 0.0037  258 ARG B N   
4595 C CA  . ARG B 261 ? 0.5439 0.3601 0.4454 -0.0660 -0.1490 0.0107  258 ARG B CA  
4596 C C   . ARG B 261 ? 0.5151 0.3482 0.4222 -0.0644 -0.1417 0.0109  258 ARG B C   
4597 O O   . ARG B 261 ? 0.5121 0.3593 0.4318 -0.0728 -0.1377 0.0186  258 ARG B O   
4598 C CB  . ARG B 261 ? 0.5888 0.3843 0.4872 -0.0679 -0.1672 0.0078  258 ARG B CB  
4599 C CG  . ARG B 261 ? 0.6164 0.4143 0.5283 -0.0820 -0.1747 0.0166  258 ARG B CG  
4600 C CD  . ARG B 261 ? 0.6240 0.4273 0.5446 -0.0944 -0.1710 0.0283  258 ARG B CD  
4601 N NE  . ARG B 261 ? 0.6429 0.4615 0.5794 -0.1069 -0.1712 0.0374  258 ARG B NE  
4602 C CZ  . ARG B 261 ? 0.6523 0.4808 0.5987 -0.1195 -0.1679 0.0490  258 ARG B CZ  
4603 N NH1 . ARG B 261 ? 0.6628 0.4843 0.6030 -0.1212 -0.1651 0.0527  258 ARG B NH1 
4604 N NH2 . ARG B 261 ? 0.6633 0.5096 0.6254 -0.1303 -0.1676 0.0570  258 ARG B NH2 
4605 N N   . TYR B 262 ? 0.5036 0.3359 0.4014 -0.0538 -0.1406 0.0029  259 TYR B N   
4606 C CA  . TYR B 262 ? 0.4851 0.3311 0.3851 -0.0506 -0.1338 0.0028  259 TYR B CA  
4607 C C   . TYR B 262 ? 0.4491 0.3121 0.3576 -0.0543 -0.1200 0.0094  259 TYR B C   
4608 O O   . TYR B 262 ? 0.4425 0.3180 0.3614 -0.0581 -0.1179 0.0138  259 TYR B O   
4609 C CB  . TYR B 262 ? 0.4837 0.3269 0.3694 -0.0386 -0.1313 -0.0055 259 TYR B CB  
4610 C CG  . TYR B 262 ? 0.4686 0.3235 0.3539 -0.0350 -0.1240 -0.0049 259 TYR B CG  
4611 C CD1 . TYR B 262 ? 0.4801 0.3372 0.3695 -0.0361 -0.1305 -0.0044 259 TYR B CD1 
4612 C CD2 . TYR B 262 ? 0.4546 0.3171 0.3348 -0.0305 -0.1116 -0.0048 259 TYR B CD2 
4613 C CE1 . TYR B 262 ? 0.4727 0.3384 0.3601 -0.0318 -0.1251 -0.0039 259 TYR B CE1 
4614 C CE2 . TYR B 262 ? 0.4446 0.3147 0.3227 -0.0272 -0.1062 -0.0037 259 TYR B CE2 
4615 C CZ  . TYR B 262 ? 0.4655 0.3367 0.3467 -0.0273 -0.1130 -0.0033 259 TYR B CZ  
4616 O OH  . TYR B 262 ? 0.4684 0.3453 0.3464 -0.0234 -0.1090 -0.0021 259 TYR B OH  
4617 N N   . GLN B 263 ? 0.4344 0.2984 0.3388 -0.0524 -0.1113 0.0095  260 GLN B N   
4618 C CA  . GLN B 263 ? 0.4152 0.2935 0.3252 -0.0543 -0.0987 0.0143  260 GLN B CA  
4619 C C   . GLN B 263 ? 0.4266 0.3132 0.3492 -0.0643 -0.0989 0.0222  260 GLN B C   
4620 O O   . GLN B 263 ? 0.4094 0.3106 0.3401 -0.0656 -0.0927 0.0256  260 GLN B O   
4621 C CB  . GLN B 263 ? 0.3997 0.2767 0.3022 -0.0503 -0.0909 0.0120  260 GLN B CB  
4622 C CG  . GLN B 263 ? 0.3972 0.2704 0.2887 -0.0414 -0.0897 0.0052  260 GLN B CG  
4623 C CD  . GLN B 263 ? 0.3894 0.2700 0.2795 -0.0378 -0.0837 0.0052  260 GLN B CD  
4624 O OE1 . GLN B 263 ? 0.3922 0.2803 0.2900 -0.0407 -0.0814 0.0092  260 GLN B OE1 
4625 N NE2 . GLN B 263 ? 0.4020 0.2809 0.2820 -0.0312 -0.0816 0.0007  260 GLN B NE2 
4626 N N   . LEU B 264 ? 0.4606 0.3386 0.3849 -0.0712 -0.1068 0.0253  261 LEU B N   
4627 C CA  . LEU B 264 ? 0.4880 0.3767 0.4240 -0.0820 -0.1057 0.0345  261 LEU B CA  
4628 C C   . LEU B 264 ? 0.4972 0.3978 0.4456 -0.0863 -0.1093 0.0376  261 LEU B C   
4629 O O   . LEU B 264 ? 0.4880 0.4069 0.4473 -0.0913 -0.1028 0.0437  261 LEU B O   
4630 C CB  . LEU B 264 ? 0.5208 0.3951 0.4549 -0.0893 -0.1150 0.0383  261 LEU B CB  
4631 C CG  . LEU B 264 ? 0.5181 0.3839 0.4422 -0.0861 -0.1114 0.0369  261 LEU B CG  
4632 C CD1 . LEU B 264 ? 0.5605 0.4130 0.4840 -0.0950 -0.1211 0.0430  261 LEU B CD1 
4633 C CD2 . LEU B 264 ? 0.5025 0.3845 0.4279 -0.0850 -0.0970 0.0394  261 LEU B CD2 
4634 N N   . GLN B 265 ? 0.5252 0.4167 0.4721 -0.0841 -0.1196 0.0331  262 GLN B N   
4635 C CA  . GLN B 265 ? 0.5227 0.4248 0.4824 -0.0892 -0.1255 0.0360  262 GLN B CA  
4636 C C   . GLN B 265 ? 0.5113 0.4297 0.4742 -0.0817 -0.1163 0.0340  262 GLN B C   
4637 O O   . GLN B 265 ? 0.5354 0.4688 0.5112 -0.0850 -0.1181 0.0372  262 GLN B O   
4638 C CB  . GLN B 265 ? 0.5572 0.4413 0.5128 -0.0898 -0.1415 0.0317  262 GLN B CB  
4639 C CG  . GLN B 265 ? 0.5801 0.4508 0.5378 -0.1007 -0.1524 0.0365  262 GLN B CG  
4640 C CD  . GLN B 265 ? 0.6104 0.4635 0.5660 -0.1025 -0.1702 0.0325  262 GLN B CD  
4641 O OE1 . GLN B 265 ? 0.6271 0.4581 0.5741 -0.1036 -0.1806 0.0304  262 GLN B OE1 
4642 N NE2 . GLN B 265 ? 0.6046 0.4663 0.5674 -0.1021 -0.1748 0.0309  262 GLN B NE2 
4643 N N   . ARG B 266 ? 0.4807 0.3969 0.4329 -0.0722 -0.1073 0.0294  263 ARG B N   
4644 C CA  . ARG B 266 ? 0.4764 0.4052 0.4306 -0.0652 -0.0995 0.0281  263 ARG B CA  
4645 C C   . ARG B 266 ? 0.4522 0.3943 0.4104 -0.0654 -0.0871 0.0316  263 ARG B C   
4646 O O   . ARG B 266 ? 0.4326 0.3827 0.3912 -0.0589 -0.0811 0.0300  263 ARG B O   
4647 C CB  . ARG B 266 ? 0.4705 0.3879 0.4102 -0.0551 -0.0993 0.0213  263 ARG B CB  
4648 C CG  . ARG B 266 ? 0.4590 0.3661 0.3857 -0.0512 -0.0934 0.0181  263 ARG B CG  
4649 C CD  . ARG B 266 ? 0.4626 0.3579 0.3757 -0.0438 -0.0978 0.0118  263 ARG B CD  
4650 N NE  . ARG B 266 ? 0.4505 0.3498 0.3599 -0.0376 -0.0944 0.0109  263 ARG B NE  
4651 C CZ  . ARG B 266 ? 0.4318 0.3303 0.3325 -0.0327 -0.0861 0.0100  263 ARG B CZ  
4652 N NH1 . ARG B 266 ? 0.4282 0.3237 0.3237 -0.0329 -0.0800 0.0093  263 ARG B NH1 
4653 N NH2 . ARG B 266 ? 0.4321 0.3320 0.3289 -0.0277 -0.0849 0.0102  263 ARG B NH2 
4654 N N   . GLY B 267 ? 0.4474 0.3917 0.4082 -0.0726 -0.0846 0.0362  264 GLY B N   
4655 C CA  . GLY B 267 ? 0.4349 0.3933 0.3992 -0.0731 -0.0736 0.0396  264 GLY B CA  
4656 C C   . GLY B 267 ? 0.4183 0.3672 0.3695 -0.0665 -0.0664 0.0353  264 GLY B C   
4657 O O   . GLY B 267 ? 0.4178 0.3757 0.3689 -0.0627 -0.0576 0.0349  264 GLY B O   
4658 N N   . VAL B 268 ? 0.4063 0.3379 0.3467 -0.0639 -0.0706 0.0310  265 VAL B N   
4659 C CA  . VAL B 268 ? 0.3864 0.3101 0.3156 -0.0588 -0.0646 0.0272  265 VAL B CA  
4660 C C   . VAL B 268 ? 0.3870 0.3054 0.3134 -0.0638 -0.0652 0.0295  265 VAL B C   
4661 O O   . VAL B 268 ? 0.4070 0.3177 0.3342 -0.0686 -0.0735 0.0312  265 VAL B O   
4662 C CB  . VAL B 268 ? 0.3839 0.2962 0.3033 -0.0524 -0.0675 0.0214  265 VAL B CB  
4663 C CG1 . VAL B 268 ? 0.3833 0.2884 0.2928 -0.0491 -0.0631 0.0181  265 VAL B CG1 
4664 C CG2 . VAL B 268 ? 0.3747 0.2918 0.2948 -0.0471 -0.0656 0.0201  265 VAL B CG2 
4665 N N   . VAL B 269 ? 0.3722 0.2931 0.2946 -0.0626 -0.0575 0.0295  266 VAL B N   
4666 C CA  . VAL B 269 ? 0.3788 0.2926 0.2958 -0.0654 -0.0583 0.0305  266 VAL B CA  
4667 C C   . VAL B 269 ? 0.3759 0.2773 0.2840 -0.0599 -0.0610 0.0243  266 VAL B C   
4668 O O   . VAL B 269 ? 0.3765 0.2784 0.2811 -0.0544 -0.0570 0.0202  266 VAL B O   
4669 C CB  . VAL B 269 ? 0.3717 0.2943 0.2877 -0.0659 -0.0497 0.0325  266 VAL B CB  
4670 C CG1 . VAL B 269 ? 0.3670 0.2818 0.2757 -0.0671 -0.0503 0.0325  266 VAL B CG1 
4671 C CG2 . VAL B 269 ? 0.3790 0.3166 0.3040 -0.0714 -0.0474 0.0390  266 VAL B CG2 
4672 N N   . VAL B 270 ? 0.3868 0.2773 0.2914 -0.0612 -0.0685 0.0238  267 VAL B N   
4673 C CA  . VAL B 270 ? 0.3852 0.2665 0.2824 -0.0546 -0.0721 0.0170  267 VAL B CA  
4674 C C   . VAL B 270 ? 0.3827 0.2588 0.2747 -0.0533 -0.0725 0.0156  267 VAL B C   
4675 O O   . VAL B 270 ? 0.4268 0.2987 0.3195 -0.0583 -0.0763 0.0201  267 VAL B O   
4676 C CB  . VAL B 270 ? 0.4049 0.2769 0.3014 -0.0537 -0.0826 0.0148  267 VAL B CB  
4677 C CG1 . VAL B 270 ? 0.4304 0.2917 0.3280 -0.0592 -0.0926 0.0182  267 VAL B CG1 
4678 C CG2 . VAL B 270 ? 0.4155 0.2825 0.3039 -0.0450 -0.0843 0.0070  267 VAL B CG2 
4679 N N   . LEU B 271 ? 0.3622 0.2401 0.2497 -0.0474 -0.0685 0.0104  268 LEU B N   
4680 C CA  . LEU B 271 ? 0.3697 0.2445 0.2530 -0.0445 -0.0696 0.0076  268 LEU B CA  
4681 C C   . LEU B 271 ? 0.3848 0.2514 0.2639 -0.0382 -0.0780 0.0018  268 LEU B C   
4682 O O   . LEU B 271 ? 0.3774 0.2444 0.2550 -0.0347 -0.0790 -0.0015 268 LEU B O   
4683 C CB  . LEU B 271 ? 0.3613 0.2451 0.2437 -0.0422 -0.0610 0.0052  268 LEU B CB  
4684 C CG  . LEU B 271 ? 0.3545 0.2450 0.2396 -0.0466 -0.0534 0.0092  268 LEU B CG  
4685 C CD1 . LEU B 271 ? 0.3526 0.2485 0.2361 -0.0448 -0.0472 0.0064  268 LEU B CD1 
4686 C CD2 . LEU B 271 ? 0.3579 0.2473 0.2437 -0.0516 -0.0543 0.0142  268 LEU B CD2 
4687 N N   . ALA B 272 ? 0.3910 0.2504 0.2671 -0.0359 -0.0840 -0.0001 269 ALA B N   
4688 C CA  . ALA B 272 ? 0.4170 0.2690 0.2880 -0.0272 -0.0921 -0.0074 269 ALA B CA  
4689 C C   . ALA B 272 ? 0.4209 0.2757 0.2904 -0.0226 -0.0918 -0.0106 269 ALA B C   
4690 O O   . ALA B 272 ? 0.4374 0.2861 0.3068 -0.0265 -0.0949 -0.0064 269 ALA B O   
4691 C CB  . ALA B 272 ? 0.4350 0.2701 0.3040 -0.0286 -0.1048 -0.0067 269 ALA B CB  
4692 N N   . LYS B 273 ? 0.4155 0.2815 0.2843 -0.0154 -0.0873 -0.0168 270 LYS B N   
4693 C CA  . LYS B 273 ? 0.4274 0.2985 0.2962 -0.0096 -0.0881 -0.0211 270 LYS B CA  
4694 C C   . LYS B 273 ? 0.4582 0.3192 0.3218 0.0005  -0.0993 -0.0283 270 LYS B C   
4695 O O   . LYS B 273 ? 0.4758 0.3364 0.3360 0.0062  -0.1014 -0.0334 270 LYS B O   
4696 C CB  . LYS B 273 ? 0.4202 0.3109 0.2921 -0.0074 -0.0779 -0.0239 270 LYS B CB  
4697 C CG  . LYS B 273 ? 0.4259 0.3262 0.2997 -0.0007 -0.0787 -0.0291 270 LYS B CG  
4698 C CD  . LYS B 273 ? 0.4416 0.3472 0.3127 0.0114  -0.0827 -0.0379 270 LYS B CD  
4699 C CE  . LYS B 273 ? 0.4487 0.3682 0.3235 0.0189  -0.0830 -0.0435 270 LYS B CE  
4700 N NZ  . LYS B 273 ? 0.4620 0.3893 0.3337 0.0319  -0.0859 -0.0528 270 LYS B NZ  
4701 N N   . SER B 274 ? 0.4662 0.3184 0.3283 0.0032  -0.1071 -0.0291 271 SER B N   
4702 C CA  . SER B 274 ? 0.4975 0.3418 0.3549 0.0156  -0.1181 -0.0377 271 SER B CA  
4703 C C   . SER B 274 ? 0.5031 0.3486 0.3617 0.0184  -0.1210 -0.0380 271 SER B C   
4704 O O   . SER B 274 ? 0.5028 0.3396 0.3613 0.0098  -0.1224 -0.0302 271 SER B O   
4705 C CB  . SER B 274 ? 0.5234 0.3433 0.3746 0.0158  -0.1316 -0.0375 271 SER B CB  
4706 O OG  . SER B 274 ? 0.5532 0.3628 0.3986 0.0292  -0.1436 -0.0469 271 SER B OG  
4707 N N   . TYR B 275 ? 0.5177 0.3751 0.3773 0.0304  -0.1218 -0.0469 272 TYR B N   
4708 C CA  . TYR B 275 ? 0.5373 0.3963 0.3982 0.0366  -0.1271 -0.0497 272 TYR B CA  
4709 C C   . TYR B 275 ? 0.5807 0.4199 0.4342 0.0487  -0.1430 -0.0566 272 TYR B C   
4710 O O   . TYR B 275 ? 0.5874 0.4287 0.4412 0.0584  -0.1491 -0.0620 272 TYR B O   
4711 C CB  . TYR B 275 ? 0.5154 0.4035 0.3844 0.0415  -0.1175 -0.0547 272 TYR B CB  
4712 C CG  . TYR B 275 ? 0.4864 0.3863 0.3617 0.0295  -0.1070 -0.0471 272 TYR B CG  
4713 C CD1 . TYR B 275 ? 0.4616 0.3562 0.3362 0.0169  -0.1004 -0.0388 272 TYR B CD1 
4714 C CD2 . TYR B 275 ? 0.4800 0.3958 0.3618 0.0312  -0.1048 -0.0488 272 TYR B CD2 
4715 C CE1 . TYR B 275 ? 0.4367 0.3395 0.3154 0.0072  -0.0922 -0.0330 272 TYR B CE1 
4716 C CE2 . TYR B 275 ? 0.4595 0.3835 0.3458 0.0203  -0.0969 -0.0426 272 TYR B CE2 
4717 C CZ  . TYR B 275 ? 0.4351 0.3518 0.3192 0.0088  -0.0906 -0.0350 272 TYR B CZ  
4718 O OH  . TYR B 275 ? 0.4107 0.3338 0.2979 -0.0005 -0.0836 -0.0301 272 TYR B OH  
4719 N N   . ASN B 276 ? 0.6025 0.4225 0.4494 0.0483  -0.1505 -0.0569 273 ASN B N   
4720 C CA  . ASN B 276 ? 0.6503 0.4482 0.4886 0.0604  -0.1673 -0.0647 273 ASN B CA  
4721 C C   . ASN B 276 ? 0.6842 0.4513 0.5169 0.0503  -0.1792 -0.0555 273 ASN B C   
4722 O O   . ASN B 276 ? 0.6704 0.4324 0.5041 0.0369  -0.1756 -0.0470 273 ASN B O   
4723 C CB  . ASN B 276 ? 0.6703 0.4703 0.5044 0.0697  -0.1683 -0.0740 273 ASN B CB  
4724 C CG  . ASN B 276 ? 0.7116 0.4857 0.5356 0.0824  -0.1871 -0.0828 273 ASN B CG  
4725 O OD1 . ASN B 276 ? 0.7287 0.4758 0.5469 0.0757  -0.1980 -0.0785 273 ASN B OD1 
4726 N ND2 . ASN B 276 ? 0.7334 0.5156 0.5555 0.1004  -0.1915 -0.0950 273 ASN B ND2 
4727 N N   . GLU B 277 ? 0.7319 0.4792 0.5588 0.0564  -0.1936 -0.0568 274 GLU B N   
4728 C CA  . GLU B 277 ? 0.7701 0.4889 0.5914 0.0447  -0.2046 -0.0457 274 GLU B CA  
4729 C C   . GLU B 277 ? 0.7786 0.4757 0.5951 0.0395  -0.2136 -0.0441 274 GLU B C   
4730 O O   . GLU B 277 ? 0.7594 0.4463 0.5766 0.0230  -0.2138 -0.0315 274 GLU B O   
4731 C CB  . GLU B 277 ? 0.8375 0.5361 0.6517 0.0530  -0.2201 -0.0473 274 GLU B CB  
4732 C CG  . GLU B 277 ? 0.8985 0.5674 0.7059 0.0393  -0.2315 -0.0342 274 GLU B CG  
4733 C CD  . GLU B 277 ? 0.9498 0.6002 0.7498 0.0454  -0.2452 -0.0331 274 GLU B CD  
4734 O OE1 . GLU B 277 ? 0.9695 0.6280 0.7698 0.0626  -0.2483 -0.0447 274 GLU B OE1 
4735 O OE2 . GLU B 277 ? 0.9903 0.6207 0.7845 0.0328  -0.2521 -0.0201 274 GLU B OE2 
4736 N N   . GLN B 278 ? 0.7993 0.4901 0.6111 0.0526  -0.2213 -0.0563 275 GLN B N   
4737 C CA  . GLN B 278 ? 0.8274 0.4957 0.6342 0.0479  -0.2320 -0.0558 275 GLN B CA  
4738 C C   . GLN B 278 ? 0.7614 0.4476 0.5757 0.0352  -0.2175 -0.0495 275 GLN B C   
4739 O O   . GLN B 278 ? 0.7590 0.4307 0.5738 0.0217  -0.2226 -0.0406 275 GLN B O   
4740 C CB  . GLN B 278 ? 0.9020 0.5586 0.7001 0.0669  -0.2446 -0.0719 275 GLN B CB  
4741 C CG  . GLN B 278 ? 0.9947 0.6415 0.7868 0.0838  -0.2561 -0.0808 275 GLN B CG  
4742 C CD  . GLN B 278 ? 1.0761 0.7209 0.8605 0.1063  -0.2646 -0.0991 275 GLN B CD  
4743 O OE1 . GLN B 278 ? 1.1193 0.7851 0.9050 0.1123  -0.2548 -0.1067 275 GLN B OE1 
4744 N NE2 . GLN B 278 ? 1.1622 0.7816 0.9375 0.1198  -0.2834 -0.1066 275 GLN B NE2 
4745 N N   . ARG B 279 ? 0.7034 0.4200 0.5236 0.0390  -0.2009 -0.0535 276 ARG B N   
4746 C CA  . ARG B 279 ? 0.6718 0.4051 0.4982 0.0291  -0.1876 -0.0486 276 ARG B CA  
4747 C C   . ARG B 279 ? 0.6386 0.3767 0.4721 0.0116  -0.1793 -0.0341 276 ARG B C   
4748 O O   . ARG B 279 ? 0.6277 0.3650 0.4648 0.0005  -0.1771 -0.0273 276 ARG B O   
4749 C CB  . ARG B 279 ? 0.6458 0.4071 0.4746 0.0390  -0.1742 -0.0570 276 ARG B CB  
4750 C CG  . ARG B 279 ? 0.6833 0.4391 0.5035 0.0552  -0.1829 -0.0708 276 ARG B CG  
4751 C CD  . ARG B 279 ? 0.6678 0.4506 0.4889 0.0621  -0.1697 -0.0770 276 ARG B CD  
4752 N NE  . ARG B 279 ? 0.6590 0.4645 0.4839 0.0709  -0.1612 -0.0816 276 ARG B NE  
4753 C CZ  . ARG B 279 ? 0.6943 0.5014 0.5149 0.0875  -0.1680 -0.0930 276 ARG B CZ  
4754 N NH1 . ARG B 279 ? 0.7285 0.5125 0.5391 0.0986  -0.1844 -0.1018 276 ARG B NH1 
4755 N NH2 . ARG B 279 ? 0.6919 0.5244 0.5187 0.0935  -0.1587 -0.0959 276 ARG B NH2 
4756 N N   . ILE B 280 ? 0.6339 0.3762 0.4690 0.0098  -0.1762 -0.0296 277 ILE B N   
4757 C CA  . ILE B 280 ? 0.6102 0.3573 0.4501 -0.0057 -0.1686 -0.0163 277 ILE B CA  
4758 C C   . ILE B 280 ? 0.6372 0.3618 0.4749 -0.0177 -0.1797 -0.0067 277 ILE B C   
4759 O O   . ILE B 280 ? 0.6194 0.3513 0.4629 -0.0306 -0.1728 0.0024  277 ILE B O   
4760 C CB  . ILE B 280 ? 0.5989 0.3521 0.4384 -0.0035 -0.1657 -0.0149 277 ILE B CB  
4761 C CG1 . ILE B 280 ? 0.5697 0.3495 0.4145 0.0040  -0.1525 -0.0220 277 ILE B CG1 
4762 C CG2 . ILE B 280 ? 0.5966 0.3486 0.4371 -0.0180 -0.1620 -0.0015 277 ILE B CG2 
4763 C CD1 . ILE B 280 ? 0.5696 0.3559 0.4145 0.0092  -0.1522 -0.0236 277 ILE B CD1 
4764 N N   . ARG B 281 ? 0.6949 0.3935 0.5249 -0.0137 -0.1968 -0.0084 278 ARG B N   
4765 C CA  . ARG B 281 ? 0.7537 0.4270 0.5808 -0.0256 -0.2105 0.0008  278 ARG B CA  
4766 C C   . ARG B 281 ? 0.7438 0.4152 0.5741 -0.0288 -0.2129 -0.0014 278 ARG B C   
4767 O O   . ARG B 281 ? 0.7470 0.4161 0.5823 -0.0441 -0.2136 0.0095  278 ARG B O   
4768 C CB  . ARG B 281 ? 0.8262 0.4690 0.6428 -0.0183 -0.2302 -0.0023 278 ARG B CB  
4769 C CG  . ARG B 281 ? 0.8633 0.5046 0.6761 -0.0172 -0.2303 0.0023  278 ARG B CG  
4770 C CD  . ARG B 281 ? 0.9378 0.5528 0.7446 -0.0306 -0.2433 0.0162  278 ARG B CD  
4771 N NE  . ARG B 281 ? 0.9719 0.5927 0.7768 -0.0377 -0.2377 0.0269  278 ARG B NE  
4772 C CZ  . ARG B 281 ? 1.0080 0.6220 0.8114 -0.0551 -0.2388 0.0432  278 ARG B CZ  
4773 N NH1 . ARG B 281 ? 1.0478 0.6503 0.8536 -0.0684 -0.2450 0.0514  278 ARG B NH1 
4774 N NH2 . ARG B 281 ? 1.0306 0.6502 0.8302 -0.0594 -0.2339 0.0516  278 ARG B NH2 
4775 N N   . GLN B 282 ? 0.7382 0.4139 0.5663 -0.0153 -0.2131 -0.0147 279 GLN B N   
4776 C CA  . GLN B 282 ? 0.7434 0.4182 0.5735 -0.0176 -0.2154 -0.0175 279 GLN B CA  
4777 C C   . GLN B 282 ? 0.6947 0.3940 0.5358 -0.0295 -0.1992 -0.0091 279 GLN B C   
4778 O O   . GLN B 282 ? 0.6989 0.3948 0.5446 -0.0397 -0.2028 -0.0037 279 GLN B O   
4779 C CB  . GLN B 282 ? 0.7486 0.4281 0.5730 0.0001  -0.2160 -0.0333 279 GLN B CB  
4780 C CG  . GLN B 282 ? 0.7740 0.4480 0.5974 -0.0006 -0.2217 -0.0373 279 GLN B CG  
4781 C CD  . GLN B 282 ? 0.7723 0.4577 0.5893 0.0168  -0.2180 -0.0518 279 GLN B CD  
4782 O OE1 . GLN B 282 ? 0.7436 0.4509 0.5643 0.0170  -0.2049 -0.0526 279 GLN B OE1 
4783 N NE2 . GLN B 282 ? 0.8121 0.4851 0.6196 0.0323  -0.2283 -0.0631 279 GLN B NE2 
4784 N N   . ASN B 283 ? 0.6507 0.3743 0.4962 -0.0282 -0.1824 -0.0082 280 ASN B N   
4785 C CA  . ASN B 283 ? 0.6129 0.3586 0.4673 -0.0358 -0.1681 -0.0033 280 ASN B CA  
4786 C C   . ASN B 283 ? 0.6089 0.3555 0.4704 -0.0526 -0.1668 0.0107  280 ASN B C   
4787 O O   . ASN B 283 ? 0.5727 0.3330 0.4420 -0.0590 -0.1597 0.0144  280 ASN B O   
4788 C CB  . ASN B 283 ? 0.5839 0.3530 0.4405 -0.0305 -0.1517 -0.0059 280 ASN B CB  
4789 C CG  . ASN B 283 ? 0.5868 0.3618 0.4385 -0.0157 -0.1502 -0.0184 280 ASN B CG  
4790 O OD1 . ASN B 283 ? 0.6169 0.3816 0.4635 -0.0093 -0.1594 -0.0254 280 ASN B OD1 
4791 N ND2 . ASN B 283 ? 0.5495 0.3420 0.4025 -0.0106 -0.1390 -0.0211 280 ASN B ND2 
4792 N N   . VAL B 284 ? 0.6286 0.3619 0.4878 -0.0596 -0.1739 0.0186  281 VAL B N   
4793 C CA  . VAL B 284 ? 0.6376 0.3741 0.5035 -0.0765 -0.1724 0.0330  281 VAL B CA  
4794 C C   . VAL B 284 ? 0.6696 0.3919 0.5385 -0.0844 -0.1856 0.0357  281 VAL B C   
4795 O O   . VAL B 284 ? 0.6653 0.3968 0.5430 -0.0981 -0.1827 0.0465  281 VAL B O   
4796 C CB  . VAL B 284 ? 0.6576 0.3872 0.5190 -0.0826 -0.1741 0.0421  281 VAL B CB  
4797 C CG1 . VAL B 284 ? 0.6299 0.3737 0.4884 -0.0740 -0.1623 0.0378  281 VAL B CG1 
4798 C CG2 . VAL B 284 ? 0.7158 0.4145 0.5681 -0.0819 -0.1931 0.0425  281 VAL B CG2 
4799 N N   . GLN B 285 ? 0.7008 0.4039 0.5633 -0.0754 -0.1989 0.0256  282 GLN B N   
4800 C CA  . GLN B 285 ? 0.7483 0.4369 0.6131 -0.0814 -0.2128 0.0259  282 GLN B CA  
4801 C C   . GLN B 285 ? 0.7196 0.4309 0.5949 -0.0847 -0.2029 0.0260  282 GLN B C   
4802 O O   . GLN B 285 ? 0.7464 0.4498 0.6256 -0.0908 -0.2132 0.0269  282 GLN B O   
4803 C CB  . GLN B 285 ? 0.8072 0.4690 0.6601 -0.0684 -0.2298 0.0131  282 GLN B CB  
4804 C CG  . GLN B 285 ? 0.8638 0.4994 0.7073 -0.0673 -0.2429 0.0151  282 GLN B CG  
4805 C CD  . GLN B 285 ? 0.9218 0.5365 0.7521 -0.0487 -0.2553 0.0004  282 GLN B CD  
4806 O OE1 . GLN B 285 ? 0.9539 0.5608 0.7792 -0.0383 -0.2629 -0.0116 282 GLN B OE1 
4807 N NE2 . GLN B 285 ? 0.9736 0.5775 0.7972 -0.0440 -0.2591 0.0011  282 GLN B NE2 
4808 N N   . VAL B 286 ? 0.6614 0.3989 0.5415 -0.0820 -0.1847 0.0262  283 VAL B N   
4809 C CA  . VAL B 286 ? 0.6496 0.4081 0.5391 -0.0842 -0.1755 0.0265  283 VAL B CA  
4810 C C   . VAL B 286 ? 0.6605 0.4266 0.5625 -0.1012 -0.1767 0.0395  283 VAL B C   
4811 O O   . VAL B 286 ? 0.6691 0.4469 0.5797 -0.1042 -0.1755 0.0398  283 VAL B O   
4812 C CB  . VAL B 286 ? 0.5948 0.3769 0.4857 -0.0774 -0.1568 0.0241  283 VAL B CB  
4813 C CG1 . VAL B 286 ? 0.5769 0.3725 0.4726 -0.0855 -0.1460 0.0340  283 VAL B CG1 
4814 C CG2 . VAL B 286 ? 0.5710 0.3688 0.4677 -0.0756 -0.1503 0.0215  283 VAL B CG2 
4815 N N   . PHE B 287 ? 0.6803 0.4430 0.5840 -0.1123 -0.1782 0.0506  284 PHE B N   
4816 C CA  . PHE B 287 ? 0.6905 0.4659 0.6072 -0.1293 -0.1774 0.0641  284 PHE B CA  
4817 C C   . PHE B 287 ? 0.7367 0.4908 0.6554 -0.1389 -0.1967 0.0674  284 PHE B C   
4818 O O   . PHE B 287 ? 0.7556 0.5198 0.6862 -0.1541 -0.1980 0.0788  284 PHE B O   
4819 C CB  . PHE B 287 ? 0.6935 0.4779 0.6107 -0.1380 -0.1693 0.0758  284 PHE B CB  
4820 C CG  . PHE B 287 ? 0.6567 0.4621 0.5724 -0.1295 -0.1512 0.0726  284 PHE B CG  
4821 C CD1 . PHE B 287 ? 0.6351 0.4676 0.5611 -0.1298 -0.1380 0.0736  284 PHE B CD1 
4822 C CD2 . PHE B 287 ? 0.6512 0.4485 0.5554 -0.1206 -0.1482 0.0680  284 PHE B CD2 
4823 C CE1 . PHE B 287 ? 0.5956 0.4444 0.5194 -0.1219 -0.1230 0.0700  284 PHE B CE1 
4824 C CE2 . PHE B 287 ? 0.6182 0.4337 0.5214 -0.1134 -0.1328 0.0647  284 PHE B CE2 
4825 C CZ  . PHE B 287 ? 0.6008 0.4408 0.5133 -0.1143 -0.1205 0.0658  284 PHE B CZ  
4826 N N   . GLU B 288 ? 0.7713 0.4977 0.6788 -0.1302 -0.2114 0.0575  285 GLU B N   
4827 C CA  . GLU B 288 ? 0.8338 0.5316 0.7394 -0.1389 -0.2331 0.0602  285 GLU B CA  
4828 C C   . GLU B 288 ? 0.8403 0.5359 0.7508 -0.1381 -0.2423 0.0535  285 GLU B C   
4829 O O   . GLU B 288 ? 0.8551 0.5255 0.7635 -0.1442 -0.2618 0.0539  285 GLU B O   
4830 C CB  . GLU B 288 ? 0.8828 0.5478 0.7715 -0.1279 -0.2467 0.0516  285 GLU B CB  
4831 C CG  . GLU B 288 ? 0.8955 0.5559 0.7772 -0.1281 -0.2425 0.0576  285 GLU B CG  
4832 C CD  . GLU B 288 ? 0.9460 0.5748 0.8116 -0.1154 -0.2567 0.0482  285 GLU B CD  
4833 O OE1 . GLU B 288 ? 0.9726 0.5829 0.8317 -0.1056 -0.2697 0.0363  285 GLU B OE1 
4834 O OE2 . GLU B 288 ? 0.9764 0.5995 0.8352 -0.1140 -0.2550 0.0522  285 GLU B OE2 
4835 N N   . PHE B 289 ? 0.7938 0.5123 0.7093 -0.1303 -0.2305 0.0472  286 PHE B N   
4836 C CA  . PHE B 289 ? 0.8095 0.5250 0.7274 -0.1276 -0.2400 0.0397  286 PHE B CA  
4837 C C   . PHE B 289 ? 0.7760 0.5230 0.7037 -0.1245 -0.2245 0.0387  286 PHE B C   
4838 O O   . PHE B 289 ? 0.7309 0.4979 0.6597 -0.1201 -0.2067 0.0403  286 PHE B O   
4839 C CB  . PHE B 289 ? 0.8244 0.5157 0.7248 -0.1105 -0.2506 0.0237  286 PHE B CB  
4840 C CG  . PHE B 289 ? 0.7817 0.4862 0.6735 -0.0925 -0.2359 0.0130  286 PHE B CG  
4841 C CD1 . PHE B 289 ? 0.7624 0.4676 0.6467 -0.0849 -0.2268 0.0114  286 PHE B CD1 
4842 C CD2 . PHE B 289 ? 0.7660 0.4809 0.6563 -0.0835 -0.2326 0.0044  286 PHE B CD2 
4843 C CE1 . PHE B 289 ? 0.7276 0.4462 0.6053 -0.0702 -0.2138 0.0024  286 PHE B CE1 
4844 C CE2 . PHE B 289 ? 0.7275 0.4534 0.6090 -0.0683 -0.2201 -0.0044 286 PHE B CE2 
4845 C CZ  . PHE B 289 ? 0.7109 0.4386 0.5866 -0.0620 -0.2110 -0.0054 286 PHE B CZ  
4846 N N   . GLN B 290 ? 0.7949 0.5440 0.7287 -0.1263 -0.2326 0.0358  287 GLN B N   
4847 C CA  . GLN B 290 ? 0.7800 0.5563 0.7231 -0.1232 -0.2214 0.0347  287 GLN B CA  
4848 C C   . GLN B 290 ? 0.7636 0.5313 0.6966 -0.1097 -0.2281 0.0213  287 GLN B C   
4849 O O   . GLN B 290 ? 0.7921 0.5360 0.7185 -0.1096 -0.2465 0.0157  287 GLN B O   
4850 C CB  . GLN B 290 ? 0.8346 0.6273 0.7978 -0.1399 -0.2249 0.0459  287 GLN B CB  
4851 C CG  . GLN B 290 ? 0.8527 0.6684 0.8281 -0.1508 -0.2111 0.0591  287 GLN B CG  
4852 C CD  . GLN B 290 ? 0.8913 0.7243 0.8872 -0.1678 -0.2160 0.0702  287 GLN B CD  
4853 O OE1 . GLN B 290 ? 0.9064 0.7570 0.9130 -0.1665 -0.2152 0.0681  287 GLN B OE1 
4854 N NE2 . GLN B 290 ? 0.9471 0.7753 0.9489 -0.1840 -0.2218 0.0823  287 GLN B NE2 
4855 N N   . LEU B 291 ? 0.7041 0.4906 0.6358 -0.0995 -0.2145 0.0170  288 LEU B N   
4856 C CA  . LEU B 291 ? 0.6950 0.4801 0.6186 -0.0880 -0.2183 0.0065  288 LEU B CA  
4857 C C   . LEU B 291 ? 0.6907 0.4910 0.6301 -0.0963 -0.2225 0.0113  288 LEU B C   
4858 O O   . LEU B 291 ? 0.6616 0.4831 0.6174 -0.1062 -0.2139 0.0214  288 LEU B O   
4859 C CB  . LEU B 291 ? 0.6549 0.4529 0.5698 -0.0748 -0.2011 0.0018  288 LEU B CB  
4860 C CG  . LEU B 291 ? 0.6390 0.4269 0.5405 -0.0664 -0.1956 -0.0028 288 LEU B CG  
4861 C CD1 . LEU B 291 ? 0.5971 0.4015 0.4942 -0.0573 -0.1779 -0.0045 288 LEU B CD1 
4862 C CD2 . LEU B 291 ? 0.6703 0.4342 0.5555 -0.0565 -0.2095 -0.0142 288 LEU B CD2 
4863 N N   . THR B 292 ? 0.7239 0.5146 0.6579 -0.0917 -0.2354 0.0036  289 THR B N   
4864 C CA  . THR B 292 ? 0.7330 0.5375 0.6810 -0.0977 -0.2417 0.0062  289 THR B CA  
4865 C C   . THR B 292 ? 0.7007 0.5261 0.6478 -0.0874 -0.2275 0.0042  289 THR B C   
4866 O O   . THR B 292 ? 0.6800 0.5052 0.6142 -0.0765 -0.2153 0.0002  289 THR B O   
4867 C CB  . THR B 292 ? 0.7798 0.5627 0.7202 -0.0962 -0.2630 -0.0021 289 THR B CB  
4868 O OG1 . THR B 292 ? 0.7666 0.5404 0.6856 -0.0783 -0.2618 -0.0145 289 THR B OG1 
4869 C CG2 . THR B 292 ? 0.8224 0.5794 0.7608 -0.1052 -0.2787 -0.0010 289 THR B CG2 
4870 N N   . ALA B 293 ? 0.7020 0.5449 0.6633 -0.0914 -0.2298 0.0074  290 ALA B N   
4871 C CA  . ALA B 293 ? 0.6813 0.5436 0.6436 -0.0824 -0.2188 0.0065  290 ALA B CA  
4872 C C   . ALA B 293 ? 0.6869 0.5341 0.6257 -0.0670 -0.2209 -0.0046 290 ALA B C   
4873 O O   . ALA B 293 ? 0.6559 0.5102 0.5857 -0.0571 -0.2073 -0.0061 290 ALA B O   
4874 C CB  . ALA B 293 ? 0.6924 0.5725 0.6740 -0.0896 -0.2260 0.0107  290 ALA B CB  
4875 N N   . GLU B 294 ? 0.7222 0.5492 0.6510 -0.0653 -0.2378 -0.0120 291 GLU B N   
4876 C CA  . GLU B 294 ? 0.7429 0.5560 0.6480 -0.0503 -0.2416 -0.0233 291 GLU B CA  
4877 C C   . GLU B 294 ? 0.7102 0.5140 0.5988 -0.0417 -0.2314 -0.0274 291 GLU B C   
4878 O O   . GLU B 294 ? 0.6906 0.4965 0.5637 -0.0297 -0.2232 -0.0323 291 GLU B O   
4879 C CB  . GLU B 294 ? 0.8070 0.6005 0.7055 -0.0505 -0.2636 -0.0310 291 GLU B CB  
4880 C CG  . GLU B 294 ? 0.8414 0.6450 0.7488 -0.0525 -0.2731 -0.0306 291 GLU B CG  
4881 C CD  . GLU B 294 ? 0.8319 0.6481 0.7300 -0.0405 -0.2642 -0.0327 291 GLU B CD  
4882 O OE1 . GLU B 294 ? 0.8303 0.6377 0.7053 -0.0272 -0.2596 -0.0400 291 GLU B OE1 
4883 O OE2 . GLU B 294 ? 0.8430 0.6783 0.7570 -0.0445 -0.2624 -0.0267 291 GLU B OE2 
4884 N N   . ASP B 295 ? 0.7100 0.5043 0.6019 -0.0481 -0.2326 -0.0252 292 ASP B N   
4885 C CA  . ASP B 295 ? 0.6866 0.4752 0.5662 -0.0408 -0.2224 -0.0281 292 ASP B CA  
4886 C C   . ASP B 295 ? 0.6396 0.4487 0.5216 -0.0377 -0.2020 -0.0231 292 ASP B C   
4887 O O   . ASP B 295 ? 0.6208 0.4298 0.4878 -0.0268 -0.1938 -0.0283 292 ASP B O   
4888 C CB  . ASP B 295 ? 0.6967 0.4746 0.5833 -0.0502 -0.2264 -0.0237 292 ASP B CB  
4889 C CG  . ASP B 295 ? 0.7544 0.5063 0.6360 -0.0529 -0.2473 -0.0289 292 ASP B CG  
4890 O OD1 . ASP B 295 ? 0.7734 0.5125 0.6427 -0.0448 -0.2598 -0.0388 292 ASP B OD1 
4891 O OD2 . ASP B 295 ? 0.7824 0.5257 0.6719 -0.0634 -0.2516 -0.0227 292 ASP B OD2 
4892 N N   . MET B 296 ? 0.6256 0.4517 0.5258 -0.0473 -0.1946 -0.0133 293 MET B N   
4893 C CA  . MET B 296 ? 0.5952 0.4392 0.4990 -0.0453 -0.1765 -0.0083 293 MET B CA  
4894 C C   . MET B 296 ? 0.5967 0.4465 0.4909 -0.0353 -0.1726 -0.0117 293 MET B C   
4895 O O   . MET B 296 ? 0.5756 0.4298 0.4613 -0.0290 -0.1600 -0.0119 293 MET B O   
4896 C CB  . MET B 296 ? 0.5839 0.4456 0.5090 -0.0562 -0.1716 0.0016  293 MET B CB  
4897 C CG  . MET B 296 ? 0.5924 0.4515 0.5257 -0.0666 -0.1714 0.0073  293 MET B CG  
4898 S SD  . MET B 296 ? 0.5755 0.4314 0.4990 -0.0623 -0.1574 0.0072  293 MET B SD  
4899 C CE  . MET B 296 ? 0.5366 0.4157 0.4677 -0.0604 -0.1404 0.0121  293 MET B CE  
4900 N N   . LYS B 297 ? 0.6134 0.4623 0.5080 -0.0342 -0.1837 -0.0142 294 LYS B N   
4901 C CA  . LYS B 297 ? 0.6160 0.4683 0.4994 -0.0245 -0.1823 -0.0172 294 LYS B CA  
4902 C C   . LYS B 297 ? 0.6085 0.4489 0.4682 -0.0135 -0.1808 -0.0251 294 LYS B C   
4903 O O   . LYS B 297 ? 0.5854 0.4310 0.4341 -0.0064 -0.1707 -0.0248 294 LYS B O   
4904 C CB  . LYS B 297 ? 0.6691 0.5223 0.5592 -0.0267 -0.1969 -0.0183 294 LYS B CB  
4905 C CG  . LYS B 297 ? 0.7009 0.5585 0.5818 -0.0179 -0.1973 -0.0199 294 LYS B CG  
4906 C CD  . LYS B 297 ? 0.7451 0.6087 0.6386 -0.0217 -0.2108 -0.0192 294 LYS B CD  
4907 C CE  . LYS B 297 ? 0.7904 0.6449 0.6665 -0.0125 -0.2220 -0.0262 294 LYS B CE  
4908 N NZ  . LYS B 297 ? 0.8353 0.6882 0.7225 -0.0184 -0.2405 -0.0283 294 LYS B NZ  
4909 N N   . ALA B 298 ? 0.6162 0.4415 0.4677 -0.0118 -0.1904 -0.0319 295 ALA B N   
4910 C CA  . ALA B 298 ? 0.6258 0.4426 0.4550 0.0001  -0.1892 -0.0405 295 ALA B CA  
4911 C C   . ALA B 298 ? 0.5959 0.4207 0.4230 0.0018  -0.1723 -0.0375 295 ALA B C   
4912 O O   . ALA B 298 ? 0.5971 0.4250 0.4085 0.0108  -0.1653 -0.0408 295 ALA B O   
4913 C CB  . ALA B 298 ? 0.6556 0.4542 0.4776 0.0025  -0.2036 -0.0491 295 ALA B CB  
4914 N N   . ILE B 299 ? 0.5738 0.4017 0.4151 -0.0066 -0.1668 -0.0318 296 ILE B N   
4915 C CA  . ILE B 299 ? 0.5485 0.3833 0.3880 -0.0052 -0.1519 -0.0295 296 ILE B CA  
4916 C C   . ILE B 299 ? 0.5285 0.3766 0.3693 -0.0050 -0.1397 -0.0234 296 ILE B C   
4917 O O   . ILE B 299 ? 0.5085 0.3611 0.3391 0.0002  -0.1298 -0.0240 296 ILE B O   
4918 C CB  . ILE B 299 ? 0.5346 0.3676 0.3867 -0.0135 -0.1505 -0.0254 296 ILE B CB  
4919 C CG1 . ILE B 299 ? 0.5629 0.3789 0.4115 -0.0131 -0.1644 -0.0313 296 ILE B CG1 
4920 C CG2 . ILE B 299 ? 0.5105 0.3510 0.3613 -0.0122 -0.1363 -0.0233 296 ILE B CG2 
4921 C CD1 . ILE B 299 ? 0.5565 0.3688 0.4189 -0.0240 -0.1672 -0.0252 296 ILE B CD1 
4922 N N   . ASP B 300 ? 0.5263 0.3807 0.3794 -0.0105 -0.1413 -0.0179 297 ASP B N   
4923 C CA  . ASP B 300 ? 0.5180 0.3823 0.3719 -0.0092 -0.1324 -0.0127 297 ASP B CA  
4924 C C   . ASP B 300 ? 0.5245 0.3863 0.3590 -0.0001 -0.1314 -0.0160 297 ASP B C   
4925 O O   . ASP B 300 ? 0.5017 0.3682 0.3302 0.0020  -0.1210 -0.0124 297 ASP B O   
4926 C CB  . ASP B 300 ? 0.5301 0.4011 0.3985 -0.0135 -0.1381 -0.0087 297 ASP B CB  
4927 C CG  . ASP B 300 ? 0.5317 0.4116 0.4200 -0.0226 -0.1351 -0.0031 297 ASP B CG  
4928 O OD1 . ASP B 300 ? 0.5249 0.4066 0.4155 -0.0254 -0.1257 -0.0008 297 ASP B OD1 
4929 O OD2 . ASP B 300 ? 0.5485 0.4349 0.4503 -0.0272 -0.1423 -0.0008 297 ASP B OD2 
4930 N N   . GLY B 301 ? 0.5510 0.4052 0.3752 0.0050  -0.1425 -0.0225 298 GLY B N   
4931 C CA  . GLY B 301 ? 0.5777 0.4300 0.3814 0.0141  -0.1430 -0.0261 298 GLY B CA  
4932 C C   . GLY B 301 ? 0.5877 0.4423 0.3774 0.0194  -0.1329 -0.0283 298 GLY B C   
4933 O O   . GLY B 301 ? 0.6050 0.4621 0.3784 0.0255  -0.1297 -0.0284 298 GLY B O   
4934 N N   . LEU B 302 ? 0.5742 0.4297 0.3699 0.0168  -0.1277 -0.0291 299 LEU B N   
4935 C CA  . LEU B 302 ? 0.5743 0.4350 0.3592 0.0217  -0.1182 -0.0315 299 LEU B CA  
4936 C C   . LEU B 302 ? 0.5565 0.4268 0.3433 0.0177  -0.1041 -0.0232 299 LEU B C   
4937 O O   . LEU B 302 ? 0.5476 0.4254 0.3261 0.0206  -0.0952 -0.0237 299 LEU B O   
4938 C CB  . LEU B 302 ? 0.5749 0.4320 0.3671 0.0203  -0.1197 -0.0355 299 LEU B CB  
4939 C CG  . LEU B 302 ? 0.6116 0.4562 0.4002 0.0247  -0.1345 -0.0445 299 LEU B CG  
4940 C CD1 . LEU B 302 ? 0.6121 0.4512 0.4085 0.0225  -0.1363 -0.0468 299 LEU B CD1 
4941 C CD2 . LEU B 302 ? 0.6466 0.4910 0.4143 0.0369  -0.1373 -0.0530 299 LEU B CD2 
4942 N N   . ASP B 303 ? 0.5451 0.4159 0.3434 0.0113  -0.1023 -0.0161 300 ASP B N   
4943 C CA  . ASP B 303 ? 0.5420 0.4185 0.3431 0.0071  -0.0906 -0.0086 300 ASP B CA  
4944 C C   . ASP B 303 ? 0.5722 0.4521 0.3563 0.0110  -0.0849 -0.0061 300 ASP B C   
4945 O O   . ASP B 303 ? 0.5838 0.4609 0.3566 0.0156  -0.0903 -0.0064 300 ASP B O   
4946 C CB  . ASP B 303 ? 0.5395 0.4153 0.3536 0.0024  -0.0916 -0.0030 300 ASP B CB  
4947 C CG  . ASP B 303 ? 0.5286 0.4074 0.3476 -0.0020 -0.0814 0.0030  300 ASP B CG  
4948 O OD1 . ASP B 303 ? 0.5002 0.3818 0.3199 -0.0042 -0.0746 0.0029  300 ASP B OD1 
4949 O OD2 . ASP B 303 ? 0.5639 0.4415 0.3860 -0.0026 -0.0813 0.0074  300 ASP B OD2 
4950 N N   . ARG B 304 ? 0.5823 0.4686 0.3642 0.0087  -0.0745 -0.0031 301 ARG B N   
4951 C CA  . ARG B 304 ? 0.6166 0.5082 0.3830 0.0104  -0.0679 0.0010  301 ARG B CA  
4952 C C   . ARG B 304 ? 0.6233 0.5185 0.3938 0.0032  -0.0577 0.0087  301 ARG B C   
4953 O O   . ARG B 304 ? 0.6568 0.5592 0.4161 0.0028  -0.0509 0.0123  301 ARG B O   
4954 C CB  . ARG B 304 ? 0.6446 0.5440 0.3982 0.0176  -0.0675 -0.0057 301 ARG B CB  
4955 C CG  . ARG B 304 ? 0.6365 0.5440 0.3966 0.0177  -0.0628 -0.0104 301 ARG B CG  
4956 C CD  . ARG B 304 ? 0.6724 0.5846 0.4197 0.0282  -0.0667 -0.0198 301 ARG B CD  
4957 N NE  . ARG B 304 ? 0.6906 0.5900 0.4391 0.0324  -0.0800 -0.0270 301 ARG B NE  
4958 C CZ  . ARG B 304 ? 0.7109 0.6077 0.4510 0.0417  -0.0880 -0.0373 301 ARG B CZ  
4959 N NH1 . ARG B 304 ? 0.7298 0.6382 0.4583 0.0499  -0.0835 -0.0428 301 ARG B NH1 
4960 N NH2 . ARG B 304 ? 0.7087 0.5915 0.4524 0.0428  -0.1010 -0.0422 301 ARG B NH2 
4961 N N   . ASN B 305 ? 0.6041 0.4949 0.3889 -0.0023 -0.0567 0.0113  302 ASN B N   
4962 C CA  . ASN B 305 ? 0.6029 0.4946 0.3905 -0.0090 -0.0484 0.0180  302 ASN B CA  
4963 C C   . ASN B 305 ? 0.5962 0.4997 0.3817 -0.0107 -0.0408 0.0170  302 ASN B C   
4964 O O   . ASN B 305 ? 0.6070 0.5145 0.3872 -0.0155 -0.0340 0.0235  302 ASN B O   
4965 C CB  . ASN B 305 ? 0.6413 0.5271 0.4177 -0.0103 -0.0476 0.0259  302 ASN B CB  
4966 C CG  . ASN B 305 ? 0.6601 0.5409 0.4409 -0.0174 -0.0425 0.0327  302 ASN B CG  
4967 O OD1 . ASN B 305 ? 0.6761 0.5541 0.4698 -0.0196 -0.0426 0.0309  302 ASN B OD1 
4968 N ND2 . ASN B 305 ? 0.6891 0.5685 0.4586 -0.0213 -0.0385 0.0404  302 ASN B ND2 
4969 N N   . LEU B 306 ? 0.5671 0.4766 0.3565 -0.0069 -0.0423 0.0094  303 LEU B N   
4970 C CA  . LEU B 306 ? 0.5691 0.4921 0.3586 -0.0072 -0.0355 0.0076  303 LEU B CA  
4971 C C   . LEU B 306 ? 0.5412 0.4645 0.3449 -0.0133 -0.0323 0.0083  303 LEU B C   
4972 O O   . LEU B 306 ? 0.5324 0.4509 0.3448 -0.0120 -0.0370 0.0036  303 LEU B O   
4973 C CB  . LEU B 306 ? 0.5989 0.5270 0.3844 0.0017  -0.0399 -0.0019 303 LEU B CB  
4974 C CG  . LEU B 306 ? 0.6194 0.5640 0.4051 0.0039  -0.0336 -0.0052 303 LEU B CG  
4975 C CD1 . LEU B 306 ? 0.6581 0.6167 0.4328 0.0026  -0.0252 0.0004  303 LEU B CD1 
4976 C CD2 . LEU B 306 ? 0.6339 0.5797 0.4165 0.0144  -0.0402 -0.0163 303 LEU B CD2 
4977 N N   . HIS B 307 ? 0.5714 0.4991 0.3771 -0.0201 -0.0256 0.0141  304 HIS B N   
4978 C CA  . HIS B 307 ? 0.5576 0.4880 0.3754 -0.0246 -0.0229 0.0131  304 HIS B CA  
4979 C C   . HIS B 307 ? 0.5460 0.4940 0.3639 -0.0230 -0.0181 0.0102  304 HIS B C   
4980 O O   . HIS B 307 ? 0.5824 0.5413 0.3928 -0.0240 -0.0130 0.0137  304 HIS B O   
4981 C CB  . HIS B 307 ? 0.5885 0.5105 0.4115 -0.0328 -0.0207 0.0195  304 HIS B CB  
4982 C CG  . HIS B 307 ? 0.6174 0.5367 0.4322 -0.0378 -0.0175 0.0277  304 HIS B CG  
4983 N ND1 . HIS B 307 ? 0.6513 0.5805 0.4652 -0.0445 -0.0113 0.0325  304 HIS B ND1 
4984 C CD2 . HIS B 307 ? 0.6408 0.5477 0.4490 -0.0381 -0.0204 0.0325  304 HIS B CD2 
4985 C CE1 . HIS B 307 ? 0.6945 0.6163 0.5004 -0.0495 -0.0105 0.0407  304 HIS B CE1 
4986 N NE2 . HIS B 307 ? 0.7054 0.6127 0.5068 -0.0448 -0.0163 0.0406  304 HIS B NE2 
4987 N N   . TYR B 308 ? 0.4935 0.4440 0.3193 -0.0198 -0.0206 0.0036  305 TYR B N   
4988 C CA  . TYR B 308 ? 0.4893 0.4572 0.3162 -0.0153 -0.0177 -0.0015 305 TYR B CA  
4989 C C   . TYR B 308 ? 0.5086 0.4897 0.3416 -0.0233 -0.0101 0.0036  305 TYR B C   
4990 O O   . TYR B 308 ? 0.5295 0.5304 0.3612 -0.0214 -0.0049 0.0029  305 TYR B O   
4991 C CB  . TYR B 308 ? 0.4697 0.4324 0.3024 -0.0093 -0.0245 -0.0095 305 TYR B CB  
4992 C CG  . TYR B 308 ? 0.4629 0.4192 0.2877 0.0003  -0.0320 -0.0162 305 TYR B CG  
4993 C CD1 . TYR B 308 ? 0.4795 0.4481 0.2950 0.0091  -0.0310 -0.0214 305 TYR B CD1 
4994 C CD2 . TYR B 308 ? 0.4465 0.3855 0.2725 0.0004  -0.0401 -0.0173 305 TYR B CD2 
4995 C CE1 . TYR B 308 ? 0.4900 0.4511 0.2967 0.0186  -0.0391 -0.0287 305 TYR B CE1 
4996 C CE2 . TYR B 308 ? 0.4558 0.3875 0.2748 0.0084  -0.0485 -0.0237 305 TYR B CE2 
4997 C CZ  . TYR B 308 ? 0.4799 0.4214 0.2887 0.0178  -0.0484 -0.0298 305 TYR B CZ  
4998 O OH  . TYR B 308 ? 0.5046 0.4380 0.3047 0.0266  -0.0576 -0.0372 305 TYR B OH  
4999 N N   . PHE B 309 ? 0.7936 0.6904 0.5362 0.0090  0.0127  -0.0597 306 PHE B N   
5000 C CA  . PHE B 309 ? 0.7672 0.6990 0.5378 -0.0001 0.0421  -0.0485 306 PHE B CA  
5001 C C   . PHE B 309 ? 0.7919 0.7311 0.5332 -0.0037 0.0663  -0.0364 306 PHE B C   
5002 O O   . PHE B 309 ? 0.7654 0.6909 0.4910 -0.0143 0.0577  -0.0259 306 PHE B O   
5003 C CB  . PHE B 309 ? 0.6901 0.6312 0.5010 -0.0202 0.0314  -0.0339 306 PHE B CB  
5004 C CG  . PHE B 309 ? 0.6932 0.6228 0.5275 -0.0197 0.0035  -0.0395 306 PHE B CG  
5005 C CD1 . PHE B 309 ? 0.7158 0.6512 0.5746 -0.0099 0.0015  -0.0520 306 PHE B CD1 
5006 C CD2 . PHE B 309 ? 0.7036 0.6146 0.5360 -0.0270 -0.0235 -0.0326 306 PHE B CD2 
5007 C CE1 . PHE B 309 ? 0.7254 0.6445 0.6056 -0.0093 -0.0295 -0.0565 306 PHE B CE1 
5008 C CE2 . PHE B 309 ? 0.7247 0.6235 0.5823 -0.0286 -0.0526 -0.0331 306 PHE B CE2 
5009 C CZ  . PHE B 309 ? 0.7236 0.6242 0.6037 -0.0204 -0.0569 -0.0447 306 PHE B CZ  
5010 N N   A ASN B 310 ? 0.8578 0.8204 0.5940 0.0060  0.0953  -0.0368 307 ASN B N   
5011 N N   B ASN B 310 ? 0.8504 0.8140 0.5890 0.0041  0.0958  -0.0351 307 ASN B N   
5012 C CA  A ASN B 310 ? 0.8967 0.8749 0.6180 -0.0021 0.1216  -0.0170 307 ASN B CA  
5013 C CA  B ASN B 310 ? 0.8864 0.8598 0.6051 -0.0046 0.1180  -0.0155 307 ASN B CA  
5014 C C   A ASN B 310 ? 0.8594 0.8634 0.6366 -0.0207 0.1307  -0.0003 307 ASN B C   
5015 C C   B ASN B 310 ? 0.8832 0.8913 0.6529 -0.0173 0.1378  0.0001  307 ASN B C   
5016 O O   A ASN B 310 ? 0.8098 0.8243 0.6289 -0.0209 0.1239  -0.0079 307 ASN B O   
5017 O O   B ASN B 310 ? 0.8776 0.9085 0.6826 -0.0095 0.1460  -0.0086 307 ASN B O   
5018 C CB  A ASN B 310 ? 0.9924 0.9888 0.6795 0.0180  0.1503  -0.0205 307 ASN B CB  
5019 C CB  B ASN B 310 ? 0.9789 0.9471 0.6381 0.0147  0.1329  -0.0207 307 ASN B CB  
5020 C CG  A ASN B 310 ? 1.0087 1.0477 0.7391 0.0264  0.1746  -0.0235 307 ASN B CG  
5021 C CG  B ASN B 310 ? 0.9881 0.9137 0.5987 0.0170  0.1069  -0.0258 307 ASN B CG  
5022 O OD1 A ASN B 310 ? 0.9477 0.9938 0.7306 0.0200  0.1635  -0.0286 307 ASN B OD1 
5023 O OD1 B ASN B 310 ? 0.9447 0.8584 0.5517 -0.0001 0.0995  -0.0097 307 ASN B OD1 
5024 N ND2 A ASN B 310 ? 1.0992 1.1689 0.8078 0.0419  0.2079  -0.0196 307 ASN B ND2 
5025 N ND2 B ASN B 310 ? 1.0401 0.9407 0.6189 0.0388  0.0880  -0.0495 307 ASN B ND2 
5026 N N   . SER B 311 ? 0.8943 0.9024 0.6717 -0.0358 0.1395  0.0214  308 SER B N   
5027 C CA  . SER B 311 ? 0.9478 0.9837 0.7767 -0.0494 0.1525  0.0391  308 SER B CA  
5028 C C   . SER B 311 ? 1.0180 1.0514 0.8351 -0.0637 0.1592  0.0645  308 SER B C   
5029 O O   . SER B 311 ? 1.0062 1.0132 0.8126 -0.0732 0.1372  0.0675  308 SER B O   
5030 C CB  . SER B 311 ? 0.9164 0.9491 0.7894 -0.0585 0.1312  0.0348  308 SER B CB  
5031 O OG  . SER B 311 ? 0.9683 1.0291 0.8962 -0.0635 0.1419  0.0427  308 SER B OG  
5032 N N   . ASP B 312 ? 1.1231 1.1858 0.9431 -0.0636 0.1886  0.0825  309 ASP B N   
5033 C CA  . ASP B 312 ? 1.1657 1.2350 0.9924 -0.0821 0.1972  0.1163  309 ASP B CA  
5034 C C   . ASP B 312 ? 1.0818 1.1447 0.9688 -0.1010 0.1731  0.1247  309 ASP B C   
5035 O O   . ASP B 312 ? 1.0936 1.1296 0.9731 -0.1136 0.1520  0.1357  309 ASP B O   
5036 C CB  . ASP B 312 ? 1.2689 1.3858 1.1062 -0.0790 0.2369  0.1375  309 ASP B CB  
5037 C CG  . ASP B 312 ? 1.3589 1.4812 1.1266 -0.0533 0.2592  0.1242  309 ASP B CG  
5038 O OD1 . ASP B 312 ? 1.3168 1.4037 1.0401 -0.0378 0.2390  0.0944  309 ASP B OD1 
5039 O OD2 . ASP B 312 ? 1.4531 1.6157 1.2118 -0.0481 0.2951  0.1449  309 ASP B OD2 
5040 N N   . SER B 313 ? 1.0260 1.1091 0.9673 -0.0997 0.1724  0.1161  310 SER B N   
5041 C CA  . SER B 313 ? 0.9654 1.0368 0.9564 -0.1092 0.1432  0.1118  310 SER B CA  
5042 C C   . SER B 313 ? 0.9085 0.9406 0.8739 -0.1117 0.1110  0.1028  310 SER B C   
5043 O O   . SER B 313 ? 0.9125 0.9314 0.9040 -0.1237 0.0901  0.1150  310 SER B O   
5044 C CB  . SER B 313 ? 0.9203 0.9997 0.9350 -0.0977 0.1381  0.0881  310 SER B CB  
5045 O OG  . SER B 313 ? 0.9816 1.0996 1.0340 -0.0931 0.1631  0.0923  310 SER B OG  
5046 N N   . PHE B 314 ? 0.8500 0.8652 0.7684 -0.0998 0.1058  0.0830  311 PHE B N   
5047 C CA  . PHE B 314 ? 0.7868 0.7762 0.6879 -0.0974 0.0783  0.0702  311 PHE B CA  
5048 C C   . PHE B 314 ? 0.7827 0.7507 0.6406 -0.0994 0.0743  0.0769  311 PHE B C   
5049 O O   . PHE B 314 ? 0.7402 0.6902 0.5948 -0.0998 0.0511  0.0725  311 PHE B O   
5050 C CB  . PHE B 314 ? 0.7517 0.7419 0.6444 -0.0861 0.0721  0.0493  311 PHE B CB  
5051 C CG  . PHE B 314 ? 0.7382 0.7435 0.6744 -0.0856 0.0694  0.0446  311 PHE B CG  
5052 C CD1 . PHE B 314 ? 0.7421 0.7434 0.7098 -0.0903 0.0509  0.0469  311 PHE B CD1 
5053 C CD2 . PHE B 314 ? 0.7660 0.7866 0.7135 -0.0792 0.0823  0.0374  311 PHE B CD2 
5054 C CE1 . PHE B 314 ? 0.7414 0.7527 0.7498 -0.0898 0.0448  0.0432  311 PHE B CE1 
5055 C CE2 . PHE B 314 ? 0.7667 0.7992 0.7578 -0.0791 0.0773  0.0338  311 PHE B CE2 
5056 C CZ  . PHE B 314 ? 0.7588 0.7863 0.7800 -0.0852 0.0586  0.0376  311 PHE B CZ  
5057 N N   . ALA B 315 ? 0.8218 0.7925 0.6479 -0.0985 0.0948  0.0867  312 ALA B N   
5058 C CA  . ALA B 315 ? 0.8559 0.8023 0.6339 -0.0993 0.0897  0.0936  312 ALA B CA  
5059 C C   . ALA B 315 ? 0.8541 0.7830 0.6474 -0.1128 0.0689  0.1094  312 ALA B C   
5060 O O   . ALA B 315 ? 0.8735 0.7758 0.6373 -0.1116 0.0508  0.1068  312 ALA B O   
5061 C CB  . ALA B 315 ? 0.9380 0.8942 0.6806 -0.0959 0.1170  0.1063  312 ALA B CB  
5062 N N   . SER B 316 ? 0.8603 0.8017 0.7010 -0.1252 0.0688  0.1265  313 SER B N   
5063 C CA  . SER B 316 ? 0.8730 0.7946 0.7360 -0.1396 0.0444  0.1455  313 SER B CA  
5064 C C   . SER B 316 ? 0.8079 0.7136 0.6976 -0.1334 0.0099  0.1245  313 SER B C   
5065 O O   . SER B 316 ? 0.8303 0.7134 0.7380 -0.1404 -0.0188 0.1327  313 SER B O   
5066 C CB  . SER B 316 ? 0.9349 0.8782 0.8421 -0.1569 0.0575  0.1775  313 SER B CB  
5067 O OG  . SER B 316 ? 0.9030 0.8718 0.8586 -0.1545 0.0639  0.1691  313 SER B OG  
5068 N N   . HIS B 317 ? 0.7206 0.6372 0.6112 -0.1193 0.0106  0.0989  314 HIS B N   
5069 C CA  . HIS B 317 ? 0.6792 0.5864 0.5867 -0.1087 -0.0189 0.0784  314 HIS B CA  
5070 C C   . HIS B 317 ? 0.6783 0.5636 0.5573 -0.1004 -0.0398 0.0681  314 HIS B C   
5071 O O   . HIS B 317 ? 0.6561 0.5417 0.5004 -0.0957 -0.0296 0.0634  314 HIS B O   
5072 C CB  . HIS B 317 ? 0.6150 0.5424 0.5229 -0.0963 -0.0098 0.0587  314 HIS B CB  
5073 C CG  . HIS B 317 ? 0.5924 0.5167 0.5186 -0.0849 -0.0351 0.0419  314 HIS B CG  
5074 N ND1 . HIS B 317 ? 0.5886 0.5033 0.4972 -0.0705 -0.0561 0.0259  314 HIS B ND1 
5075 C CD2 . HIS B 317 ? 0.5843 0.5151 0.5406 -0.0823 -0.0428 0.0366  314 HIS B CD2 
5076 C CE1 . HIS B 317 ? 0.5902 0.5061 0.5117 -0.0575 -0.0748 0.0107  314 HIS B CE1 
5077 N NE2 . HIS B 317 ? 0.5866 0.5090 0.5364 -0.0654 -0.0689 0.0173  314 HIS B NE2 
5078 N N   . PRO B 318 ? 0.7100 0.5759 0.6050 -0.0948 -0.0733 0.0601  315 PRO B N   
5079 C CA  . PRO B 318 ? 0.7236 0.5736 0.5956 -0.0828 -0.0933 0.0464  315 PRO B CA  
5080 C C   . PRO B 318 ? 0.6819 0.5540 0.5295 -0.0671 -0.0800 0.0277  315 PRO B C   
5081 O O   . PRO B 318 ? 0.6949 0.5594 0.5227 -0.0622 -0.0863 0.0236  315 PRO B O   
5082 C CB  . PRO B 318 ? 0.7607 0.5933 0.6577 -0.0706 -0.1324 0.0313  315 PRO B CB  
5083 C CG  . PRO B 318 ? 0.7831 0.6102 0.7209 -0.0857 -0.1386 0.0480  315 PRO B CG  
5084 C CD  . PRO B 318 ? 0.7444 0.6017 0.6821 -0.0964 -0.0978 0.0604  315 PRO B CD  
5085 N N   . ASN B 319 ? 0.6310 0.5290 0.4849 -0.0603 -0.0659 0.0187  316 ASN B N   
5086 C CA  . ASN B 319 ? 0.5895 0.5129 0.4288 -0.0477 -0.0558 0.0064  316 ASN B CA  
5087 C C   . ASN B 319 ? 0.5689 0.5023 0.3963 -0.0576 -0.0305 0.0162  316 ASN B C   
5088 O O   . ASN B 319 ? 0.5311 0.4859 0.3558 -0.0516 -0.0233 0.0114  316 ASN B O   
5089 C CB  . ASN B 319 ? 0.5877 0.5317 0.4371 -0.0322 -0.0614 -0.0082 316 ASN B CB  
5090 C CG  . ASN B 319 ? 0.6273 0.5664 0.4773 -0.0119 -0.0882 -0.0263 316 ASN B CG  
5091 O OD1 . ASN B 319 ? 0.6666 0.5862 0.5143 -0.0110 -0.1038 -0.0277 316 ASN B OD1 
5092 N ND2 . ASN B 319 ? 0.6376 0.5907 0.4885 0.0065  -0.0969 -0.0416 316 ASN B ND2 
5093 N N   . TYR B 320 ? 0.5957 0.5155 0.4162 -0.0709 -0.0187 0.0303  317 TYR B N   
5094 C CA  . TYR B 320 ? 0.5967 0.5195 0.3976 -0.0749 0.0007  0.0351  317 TYR B CA  
5095 C C   . TYR B 320 ? 0.5974 0.5171 0.3795 -0.0686 -0.0075 0.0289  317 TYR B C   
5096 O O   . TYR B 320 ? 0.6219 0.5248 0.3920 -0.0677 -0.0211 0.0295  317 TYR B O   
5097 C CB  . TYR B 320 ? 0.6595 0.5682 0.4447 -0.0848 0.0128  0.0507  317 TYR B CB  
5098 C CG  . TYR B 320 ? 0.6819 0.5941 0.4432 -0.0826 0.0320  0.0505  317 TYR B CG  
5099 C CD1 . TYR B 320 ? 0.6616 0.5929 0.4393 -0.0787 0.0434  0.0433  317 TYR B CD1 
5100 C CD2 . TYR B 320 ? 0.7464 0.6396 0.4665 -0.0816 0.0348  0.0555  317 TYR B CD2 
5101 C CE1 . TYR B 320 ? 0.6908 0.6225 0.4480 -0.0724 0.0558  0.0386  317 TYR B CE1 
5102 C CE2 . TYR B 320 ? 0.7761 0.6694 0.4696 -0.0739 0.0481  0.0503  317 TYR B CE2 
5103 C CZ  . TYR B 320 ? 0.7582 0.6708 0.4718 -0.0684 0.0580  0.0405  317 TYR B CZ  
5104 O OH  . TYR B 320 ? 0.7890 0.6990 0.4777 -0.0569 0.0664  0.0313  317 TYR B OH  
5105 N N   . PRO B 321 ? 0.5721 0.5085 0.3582 -0.0648 -0.0035 0.0243  318 PRO B N   
5106 C CA  . PRO B 321 ? 0.5717 0.5109 0.3539 -0.0606 -0.0141 0.0220  318 PRO B CA  
5107 C C   . PRO B 321 ? 0.6071 0.5179 0.3606 -0.0631 -0.0191 0.0247  318 PRO B C   
5108 O O   . PRO B 321 ? 0.6127 0.5196 0.3660 -0.0604 -0.0330 0.0235  318 PRO B O   
5109 C CB  . PRO B 321 ? 0.5439 0.5075 0.3434 -0.0600 -0.0098 0.0229  318 PRO B CB  
5110 C CG  . PRO B 321 ? 0.5360 0.4977 0.3371 -0.0637 0.0029  0.0230  318 PRO B CG  
5111 C CD  . PRO B 321 ? 0.5501 0.5040 0.3516 -0.0653 0.0072  0.0232  318 PRO B CD  
5112 N N   . TYR B 322 ? 0.6491 0.5427 0.3787 -0.0663 -0.0079 0.0281  319 TYR B N   
5113 C CA  . TYR B 322 ? 0.7200 0.5849 0.4110 -0.0641 -0.0130 0.0283  319 TYR B CA  
5114 C C   . TYR B 322 ? 0.7944 0.6366 0.4577 -0.0680 -0.0141 0.0376  319 TYR B C   
5115 O O   . TYR B 322 ? 0.8617 0.6831 0.4851 -0.0658 -0.0105 0.0408  319 TYR B O   
5116 C CB  . TYR B 322 ? 0.7269 0.5914 0.4042 -0.0594 -0.0005 0.0237  319 TYR B CB  
5117 C CG  . TYR B 322 ? 0.6831 0.5649 0.3899 -0.0578 -0.0042 0.0175  319 TYR B CG  
5118 C CD1 . TYR B 322 ? 0.6607 0.5451 0.3865 -0.0586 -0.0238 0.0174  319 TYR B CD1 
5119 C CD2 . TYR B 322 ? 0.6653 0.5613 0.3841 -0.0560 0.0105  0.0142  319 TYR B CD2 
5120 C CE1 . TYR B 322 ? 0.6336 0.5331 0.3879 -0.0601 -0.0290 0.0179  319 TYR B CE1 
5121 C CE2 . TYR B 322 ? 0.6367 0.5438 0.3816 -0.0555 0.0033  0.0106  319 TYR B CE2 
5122 C CZ  . TYR B 322 ? 0.6200 0.5275 0.3810 -0.0585 -0.0171 0.0139  319 TYR B CZ  
5123 O OH  . TYR B 322 ? 0.6119 0.5293 0.4000 -0.0607 -0.0259 0.0156  319 TYR B OH  
5124 N N   . SER B 323 ? 0.8476 0.6919 0.5302 -0.0723 -0.0221 0.0417  320 SER B N   
5125 C CA  . SER B 323 ? 0.9393 0.7671 0.6110 -0.0807 -0.0225 0.0564  320 SER B CA  
5126 C C   . SER B 323 ? 1.0294 0.8217 0.6605 -0.0822 -0.0373 0.0641  320 SER B C   
5127 O O   . SER B 323 ? 1.1398 0.9186 0.7566 -0.0917 -0.0347 0.0828  320 SER B O   
5128 C CB  . SER B 323 ? 0.9310 0.7661 0.6398 -0.0826 -0.0354 0.0553  320 SER B CB  
5129 O OG  . SER B 323 ? 1.0051 0.8284 0.7155 -0.0944 -0.0344 0.0740  320 SER B OG  
5130 N N   . ASP B 324 ? 1.0434 0.8194 0.6586 -0.0748 -0.0550 0.0542  321 ASP B N   
5131 C CA  . ASP B 324 ? 1.1237 0.8596 0.6935 -0.0757 -0.0717 0.0621  321 ASP B CA  
5132 C C   . ASP B 324 ? 1.1223 0.8420 0.6542 -0.0659 -0.0743 0.0532  321 ASP B C   
5133 O O   . ASP B 324 ? 1.1216 0.8132 0.6375 -0.0610 -0.1009 0.0474  321 ASP B O   
5134 C CB  . ASP B 324 ? 1.1639 0.8842 0.7532 -0.0760 -0.1023 0.0596  321 ASP B CB  
5135 C CG  . ASP B 324 ? 1.2477 0.9335 0.8124 -0.0852 -0.1174 0.0777  321 ASP B CG  
5136 O OD1 . ASP B 324 ? 1.2890 0.9761 0.8422 -0.0962 -0.1004 0.0979  321 ASP B OD1 
5137 O OD2 . ASP B 324 ? 1.2819 0.9409 0.8436 -0.0822 -0.1481 0.0736  321 ASP B OD2 
5138 N N   . GLU B 325 ? 1.0838 0.8183 0.6033 -0.0615 -0.0508 0.0506  322 GLU B N   
5139 C CA  . GLU B 325 ? 1.0889 0.8076 0.5768 -0.0484 -0.0567 0.0372  322 GLU B CA  
5140 C C   . GLU B 325 ? 1.1623 0.8463 0.5760 -0.0409 -0.0569 0.0431  322 GLU B C   
5141 O O   . GLU B 325 ? 1.2215 0.8802 0.5976 -0.0261 -0.0710 0.0291  322 GLU B O   
5142 C CB  . GLU B 325 ? 1.0643 0.8126 0.5741 -0.0439 -0.0363 0.0286  322 GLU B CB  
5143 C CG  . GLU B 325 ? 1.0724 0.8476 0.5855 -0.0481 -0.0028 0.0393  322 GLU B CG  
5144 C CD  . GLU B 325 ? 1.1248 0.9140 0.6298 -0.0355 0.0143  0.0275  322 GLU B CD  
5145 O OE1 . GLU B 325 ? 1.2434 1.0279 0.6996 -0.0247 0.0310  0.0293  322 GLU B OE1 
5146 O OE2 . GLU B 325 ? 1.0680 0.8718 0.6122 -0.0342 0.0089  0.0160  322 GLU B OE2 
5147 N N   . TYR B 326 ? 1.1685 0.8496 0.5614 -0.0504 -0.0452 0.0643  323 TYR B N   
5148 C CA  . TYR B 326 ? 1.2628 0.9079 0.5832 -0.0467 -0.0509 0.0771  323 TYR B CA  
5149 C C   . TYR B 326 ? 1.2702 0.9112 0.5992 -0.0656 -0.0526 0.1046  323 TYR B C   
5150 O O   . TYR B 326 ? 1.3305 0.9386 0.6060 -0.0676 -0.0634 0.1211  323 TYR B O   
5151 C CB  . TYR B 326 ? 1.3418 0.9955 0.6042 -0.0323 -0.0211 0.0789  323 TYR B CB  
5152 C CG  . TYR B 326 ? 1.3329 1.0325 0.6180 -0.0419 0.0197  0.0991  323 TYR B CG  
5153 C CD1 . TYR B 326 ? 1.2446 0.9832 0.5920 -0.0443 0.0358  0.0894  323 TYR B CD1 
5154 C CD2 . TYR B 326 ? 1.4221 1.1271 0.6724 -0.0503 0.0399  0.1310  323 TYR B CD2 
5155 C CE1 . TYR B 326 ? 1.2436 1.0238 0.6198 -0.0531 0.0696  0.1076  323 TYR B CE1 
5156 C CE2 . TYR B 326 ? 1.4254 1.1769 0.7084 -0.0611 0.0760  0.1534  323 TYR B CE2 
5157 C CZ  . TYR B 326 ? 1.3377 1.1261 0.6846 -0.0615 0.0901  0.1396  323 TYR B CZ  
5158 O OH  . TYR B 326 ? 1.3616 1.1951 0.7484 -0.0721 0.1218  0.1610  323 TYR B OH  
5159 O OXT . TYR B 326 ? 1.1903 0.8594 0.5818 -0.0780 -0.0462 0.1093  323 TYR B OXT 
# 
