data_8S6K
# 
_entry.id   8S6K 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8S6K         pdb_00008s6k 10.2210/pdb8s6k/pdb 
WWPDB D_1292136912 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8S6K 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-27 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rhurtado@bifi.es 
_pdbx_contact_author.name_first         Ramon 
_pdbx_contact_author.name_last          Hurtado-Guerrero 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3122-9401 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Hurtado-Guerrero, R.' 1 ? 
'Macias-Leon, J.'      2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Chem.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1552-4469 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Recognizing Tn and STn Epitopes in Protein Context: Structural Advances in Phage Display Libraries for Tumor-Specific Antibody Discovery
;
_citation.year                      2025 
_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 'Hurtado-Guerrero, R.'        1  ? 
primary 'Gatos, S.'                   2  ? 
primary 'Gines-Alcober, I.'           3  ? 
primary 'Macias-Leon, J.'             4  ? 
primary 'Manuel Gonzalez-Ramirez, A.' 5  ? 
primary 'Kasapoglu, I.'               6  ? 
primary 'Veloz, B.'                   7  ? 
primary 'Companon, I.'                8  ? 
primary 'Ghirardello, M.'             9  ? 
primary 'Merino, P.'                  10 ? 
primary 'Corzana, F.'                 11 ? 
primary 'Blixt, O.'                   12 ? 
# 
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 ScFv-G2D11                                  26933.785 2   ? ? ? 
;SSGGGGSGGGGGSSGSSDVVMTQSHKFMSTSVGDRVSITCKASQDVGTAVAWYQQKPGQSPKLLIYWASTRHTGVPDRFTGSGSGTDFTLTISNVQSEDLADYFCQQYSSYPLTFGGGTKLEMKRGGHHHHHH
;
2 polymer     syn 'Mucin-1 subunit alpha'                     597.642   2   ? ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                              62.068    12  ? ? ? ? 
4 non-polymer syn 2-acetamido-2-deoxy-alpha-D-galactopyranose 221.208   4   ? ? ? ? 
5 water       nat water                                       18.015    455 ? ? ? ? 
# 
_entity_name_com.entity_id   2 
_entity_name_com.name        MUC1-NT,MUC1-alpha 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;QVQLQQSDAELVKPGASVKISCKASGYIFADHAIHWVKRKPEQGLEWIGYISPGNDDIKYNEKFKGKATLTADKSSSTAY
MQLNSLTSEDSAVYFCKRSLPGTFDYWGQGTTLTVSSSSGGGGSGGGGGSSGSSDVVMTQSHKFMSTSVGDRVSITCKAS
QDVGTAVAWYQQKPGQSPKLLIYWASTRHTGVPDRFTGSGSGTDFTLTISNVQSEDLADYFCQQYSSYPLTFGGGTKLEM
KRGGHHHHHH
;
;QVQLQQSDAELVKPGASVKISCKASGYIFADHAIHWVKRKPEQGLEWIGYISPGNDDIKYNEKFKGKATLTADKSSSTAY
MQLNSLTSEDSAVYFCKRSLPGTFDYWGQGTTLTVSSSSGGGGSGGGGGSSGSSDVVMTQSHKFMSTSVGDRVSITCKAS
QDVGTAVAWYQQKPGQSPKLLIYWASTRHTGVPDRFTGSGSGTDFTLTISNVQSEDLADYFCQQYSSYPLTFGGGTKLEM
KRGGHHHHHH
;
A,H ? 
2 'polypeptide(L)' no yes 'APGSTAP(NH2)' APGSTAPX M,N ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 1,2-ETHANEDIOL                              EDO 
4 2-acetamido-2-deoxy-alpha-D-galactopyranose A2G 
5 water                                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   VAL n 
1 3   GLN n 
1 4   LEU n 
1 5   GLN n 
1 6   GLN n 
1 7   SER n 
1 8   ASP n 
1 9   ALA n 
1 10  GLU n 
1 11  LEU n 
1 12  VAL n 
1 13  LYS n 
1 14  PRO n 
1 15  GLY n 
1 16  ALA n 
1 17  SER n 
1 18  VAL n 
1 19  LYS n 
1 20  ILE n 
1 21  SER n 
1 22  CYS n 
1 23  LYS n 
1 24  ALA n 
1 25  SER n 
1 26  GLY n 
1 27  TYR n 
1 28  ILE n 
1 29  PHE n 
1 30  ALA n 
1 31  ASP n 
1 32  HIS n 
1 33  ALA n 
1 34  ILE n 
1 35  HIS n 
1 36  TRP n 
1 37  VAL n 
1 38  LYS n 
1 39  ARG n 
1 40  LYS n 
1 41  PRO n 
1 42  GLU n 
1 43  GLN n 
1 44  GLY n 
1 45  LEU n 
1 46  GLU n 
1 47  TRP n 
1 48  ILE n 
1 49  GLY n 
1 50  TYR n 
1 51  ILE n 
1 52  SER n 
1 53  PRO n 
1 54  GLY n 
1 55  ASN n 
1 56  ASP n 
1 57  ASP n 
1 58  ILE n 
1 59  LYS n 
1 60  TYR n 
1 61  ASN n 
1 62  GLU n 
1 63  LYS n 
1 64  PHE n 
1 65  LYS n 
1 66  GLY n 
1 67  LYS n 
1 68  ALA n 
1 69  THR n 
1 70  LEU n 
1 71  THR n 
1 72  ALA n 
1 73  ASP n 
1 74  LYS n 
1 75  SER n 
1 76  SER n 
1 77  SER n 
1 78  THR n 
1 79  ALA n 
1 80  TYR n 
1 81  MET n 
1 82  GLN n 
1 83  LEU n 
1 84  ASN n 
1 85  SER n 
1 86  LEU n 
1 87  THR n 
1 88  SER n 
1 89  GLU n 
1 90  ASP n 
1 91  SER n 
1 92  ALA n 
1 93  VAL n 
1 94  TYR n 
1 95  PHE n 
1 96  CYS n 
1 97  LYS n 
1 98  ARG n 
1 99  SER n 
1 100 LEU n 
1 101 PRO n 
1 102 GLY n 
1 103 THR n 
1 104 PHE n 
1 105 ASP n 
1 106 TYR n 
1 107 TRP n 
1 108 GLY n 
1 109 GLN n 
1 110 GLY n 
1 111 THR n 
1 112 THR n 
1 113 LEU n 
1 114 THR n 
1 115 VAL n 
1 116 SER n 
1 117 SER n 
1 118 SER n 
1 119 SER n 
1 120 GLY n 
1 121 GLY n 
1 122 GLY n 
1 123 GLY n 
1 124 SER n 
1 125 GLY n 
1 126 GLY n 
1 127 GLY n 
1 128 GLY n 
1 129 GLY n 
1 130 SER n 
1 131 SER n 
1 132 GLY n 
1 133 SER n 
1 134 SER n 
1 135 ASP n 
1 136 VAL n 
1 137 VAL n 
1 138 MET n 
1 139 THR n 
1 140 GLN n 
1 141 SER n 
1 142 HIS n 
1 143 LYS n 
1 144 PHE n 
1 145 MET n 
1 146 SER n 
1 147 THR n 
1 148 SER n 
1 149 VAL n 
1 150 GLY n 
1 151 ASP n 
1 152 ARG n 
1 153 VAL n 
1 154 SER n 
1 155 ILE n 
1 156 THR n 
1 157 CYS n 
1 158 LYS n 
1 159 ALA n 
1 160 SER n 
1 161 GLN n 
1 162 ASP n 
1 163 VAL n 
1 164 GLY n 
1 165 THR n 
1 166 ALA n 
1 167 VAL n 
1 168 ALA n 
1 169 TRP n 
1 170 TYR n 
1 171 GLN n 
1 172 GLN n 
1 173 LYS n 
1 174 PRO n 
1 175 GLY n 
1 176 GLN n 
1 177 SER n 
1 178 PRO n 
1 179 LYS n 
1 180 LEU n 
1 181 LEU n 
1 182 ILE n 
1 183 TYR n 
1 184 TRP n 
1 185 ALA n 
1 186 SER n 
1 187 THR n 
1 188 ARG n 
1 189 HIS n 
1 190 THR n 
1 191 GLY n 
1 192 VAL n 
1 193 PRO n 
1 194 ASP n 
1 195 ARG n 
1 196 PHE n 
1 197 THR n 
1 198 GLY n 
1 199 SER n 
1 200 GLY n 
1 201 SER n 
1 202 GLY n 
1 203 THR n 
1 204 ASP n 
1 205 PHE n 
1 206 THR n 
1 207 LEU n 
1 208 THR n 
1 209 ILE n 
1 210 SER n 
1 211 ASN n 
1 212 VAL n 
1 213 GLN n 
1 214 SER n 
1 215 GLU n 
1 216 ASP n 
1 217 LEU n 
1 218 ALA n 
1 219 ASP n 
1 220 TYR n 
1 221 PHE n 
1 222 CYS n 
1 223 GLN n 
1 224 GLN n 
1 225 TYR n 
1 226 SER n 
1 227 SER n 
1 228 TYR n 
1 229 PRO n 
1 230 LEU n 
1 231 THR n 
1 232 PHE n 
1 233 GLY n 
1 234 GLY n 
1 235 GLY n 
1 236 THR n 
1 237 LYS n 
1 238 LEU n 
1 239 GLU n 
1 240 MET n 
1 241 LYS n 
1 242 ARG n 
1 243 GLY n 
1 244 GLY n 
1 245 HIS n 
1 246 HIS n 
1 247 HIS n 
1 248 HIS n 
1 249 HIS n 
1 250 HIS n 
2 1   ALA n 
2 2   PRO n 
2 3   GLY n 
2 4   SER n 
2 5   THR n 
2 6   ALA n 
2 7   PRO n 
2 8   NH2 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                   250 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Mus musculus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_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      'Komagataella pastoris' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4922 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       8 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
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 
A2G 'D-saccharide, alpha linking' . 2-acetamido-2-deoxy-alpha-D-galactopyranose 
;N-acetyl-alpha-D-galactosamine; 2-acetamido-2-deoxy-alpha-D-galactose; 2-acetamido-2-deoxy-D-galactose; 2-acetamido-2-deoxy-galactose; N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE
;
'C8 H15 N O6'    221.208 
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 
EDO non-polymer                   . 1,2-ETHANEDIOL                              'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking'           y GLUTAMINE                                   ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'                             ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'             y GLYCINE                                     ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'           y HISTIDINE                                   ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                   . WATER                                       ? 'H2 O'           18.015  
ILE 'L-peptide linking'           y ISOLEUCINE                                  ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE                                     ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE                                      ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'           y METHIONINE                                  ? 'C5 H11 N O2 S'  149.211 
NH2 non-polymer                   . 'AMINO GROUP'                               ? 'H2 N'           16.023  
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
A2G 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGalpNAca                        
A2G 'COMMON NAME'                         GMML     1.0 N-acetyl-a-D-galactopyranosamine 
A2G 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-GalpNAc                      
A2G 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GalNAc                           
# 
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   GLN 1   1    1    GLN GLN A . n 
A 1 2   VAL 2   2    2    VAL VAL A . n 
A 1 3   GLN 3   3    3    GLN GLN A . n 
A 1 4   LEU 4   4    4    LEU LEU A . n 
A 1 5   GLN 5   5    5    GLN GLN A . n 
A 1 6   GLN 6   6    6    GLN GLN A . n 
A 1 7   SER 7   7    7    SER SER A . n 
A 1 8   ASP 8   8    8    ASP ASP A . n 
A 1 9   ALA 9   9    9    ALA ALA A . n 
A 1 10  GLU 10  10   10   GLU GLU A . n 
A 1 11  LEU 11  11   11   LEU LEU A . n 
A 1 12  VAL 12  12   12   VAL VAL A . n 
A 1 13  LYS 13  13   13   LYS LYS A . n 
A 1 14  PRO 14  14   14   PRO PRO A . n 
A 1 15  GLY 15  15   15   GLY GLY A . n 
A 1 16  ALA 16  16   16   ALA ALA A . n 
A 1 17  SER 17  17   17   SER SER A . n 
A 1 18  VAL 18  18   18   VAL VAL A . n 
A 1 19  LYS 19  19   19   LYS LYS A . n 
A 1 20  ILE 20  20   20   ILE ILE A . n 
A 1 21  SER 21  21   21   SER SER A . n 
A 1 22  CYS 22  22   22   CYS CYS A . n 
A 1 23  LYS 23  23   23   LYS LYS A . n 
A 1 24  ALA 24  24   24   ALA ALA A . n 
A 1 25  SER 25  25   25   SER SER A . n 
A 1 26  GLY 26  26   26   GLY GLY A . n 
A 1 27  TYR 27  27   27   TYR TYR A . n 
A 1 28  ILE 28  28   28   ILE ILE A . n 
A 1 29  PHE 29  29   29   PHE PHE A . n 
A 1 30  ALA 30  30   30   ALA ALA A . n 
A 1 31  ASP 31  31   31   ASP ASP A . n 
A 1 32  HIS 32  32   32   HIS HIS A . n 
A 1 33  ALA 33  33   33   ALA ALA A . n 
A 1 34  ILE 34  34   34   ILE ILE A . n 
A 1 35  HIS 35  35   35   HIS HIS A . n 
A 1 36  TRP 36  36   36   TRP TRP A . n 
A 1 37  VAL 37  37   37   VAL VAL A . n 
A 1 38  LYS 38  38   38   LYS LYS A . n 
A 1 39  ARG 39  39   39   ARG ARG A . n 
A 1 40  LYS 40  40   40   LYS LYS A . n 
A 1 41  PRO 41  41   41   PRO PRO A . n 
A 1 42  GLU 42  42   42   GLU GLU A . n 
A 1 43  GLN 43  43   43   GLN GLN A . n 
A 1 44  GLY 44  44   44   GLY GLY A . n 
A 1 45  LEU 45  45   45   LEU LEU A . n 
A 1 46  GLU 46  46   46   GLU GLU A . n 
A 1 47  TRP 47  47   47   TRP TRP A . n 
A 1 48  ILE 48  48   48   ILE ILE A . n 
A 1 49  GLY 49  49   49   GLY GLY A . n 
A 1 50  TYR 50  50   50   TYR TYR A . n 
A 1 51  ILE 51  51   51   ILE ILE A . n 
A 1 52  SER 52  52   52   SER SER A . n 
A 1 53  PRO 53  53   53   PRO PRO A . n 
A 1 54  GLY 54  54   54   GLY GLY A . n 
A 1 55  ASN 55  55   55   ASN ASN A . n 
A 1 56  ASP 56  56   56   ASP ASP A . n 
A 1 57  ASP 57  56   56   ASP ASP A A n 
A 1 58  ILE 58  57   57   ILE ILE A . n 
A 1 59  LYS 59  58   58   LYS LYS A . n 
A 1 60  TYR 60  59   59   TYR TYR A . n 
A 1 61  ASN 61  60   60   ASN ASN A . n 
A 1 62  GLU 62  61   61   GLU GLU A . n 
A 1 63  LYS 63  62   62   LYS LYS A . n 
A 1 64  PHE 64  63   63   PHE PHE A . n 
A 1 65  LYS 65  64   64   LYS LYS A . n 
A 1 66  GLY 66  65   65   GLY GLY A . n 
A 1 67  LYS 67  66   66   LYS LYS A . n 
A 1 68  ALA 68  67   67   ALA ALA A . n 
A 1 69  THR 69  68   68   THR THR A . n 
A 1 70  LEU 70  69   69   LEU LEU A . n 
A 1 71  THR 71  70   70   THR THR A . n 
A 1 72  ALA 72  71   71   ALA ALA A . n 
A 1 73  ASP 73  72   72   ASP ASP A . n 
A 1 74  LYS 74  73   73   LYS LYS A . n 
A 1 75  SER 75  74   74   SER SER A . n 
A 1 76  SER 76  75   75   SER SER A . n 
A 1 77  SER 77  76   76   SER SER A . n 
A 1 78  THR 78  77   77   THR THR A . n 
A 1 79  ALA 79  78   78   ALA ALA A . n 
A 1 80  TYR 80  79   79   TYR TYR A . n 
A 1 81  MET 81  80   80   MET MET A . n 
A 1 82  GLN 82  81   81   GLN GLN A . n 
A 1 83  LEU 83  82   82   LEU LEU A . n 
A 1 84  ASN 84  82   82   ASN ASN A A n 
A 1 85  SER 85  82   82   SER SER A B n 
A 1 86  LEU 86  82   82   LEU LEU A C n 
A 1 87  THR 87  83   83   THR THR A . n 
A 1 88  SER 88  84   84   SER SER A . n 
A 1 89  GLU 89  85   85   GLU GLU A . n 
A 1 90  ASP 90  86   86   ASP ASP A . n 
A 1 91  SER 91  87   87   SER SER A . n 
A 1 92  ALA 92  88   88   ALA ALA A . n 
A 1 93  VAL 93  89   89   VAL VAL A . n 
A 1 94  TYR 94  90   90   TYR TYR A . n 
A 1 95  PHE 95  91   91   PHE PHE A . n 
A 1 96  CYS 96  92   92   CYS CYS A . n 
A 1 97  LYS 97  93   93   LYS LYS A . n 
A 1 98  ARG 98  94   94   ARG ARG A . n 
A 1 99  SER 99  95   95   SER SER A . n 
A 1 100 LEU 100 96   96   LEU LEU A . n 
A 1 101 PRO 101 97   97   PRO PRO A . n 
A 1 102 GLY 102 98   98   GLY GLY A . n 
A 1 103 THR 103 99   99   THR THR A . n 
A 1 104 PHE 104 100  100  PHE PHE A . n 
A 1 105 ASP 105 101  101  ASP ASP A . n 
A 1 106 TYR 106 102  102  TYR TYR A . n 
A 1 107 TRP 107 103  103  TRP TRP A . n 
A 1 108 GLY 108 104  104  GLY GLY A . n 
A 1 109 GLN 109 105  105  GLN GLN A . n 
A 1 110 GLY 110 106  106  GLY GLY A . n 
A 1 111 THR 111 107  107  THR THR A . n 
A 1 112 THR 112 108  108  THR THR A . n 
A 1 113 LEU 113 109  109  LEU LEU A . n 
A 1 114 THR 114 110  110  THR THR A . n 
A 1 115 VAL 115 111  111  VAL VAL A . n 
A 1 116 SER 116 112  112  SER SER A . n 
A 1 117 SER 117 113  ?    ?   ?   A . n 
A 1 118 SER 118 114  ?    ?   ?   A . n 
A 1 119 SER 119 115  ?    ?   ?   A . n 
A 1 120 GLY 120 116  ?    ?   ?   A . n 
A 1 121 GLY 121 117  ?    ?   ?   A . n 
A 1 122 GLY 122 118  ?    ?   ?   A . n 
A 1 123 GLY 123 119  ?    ?   ?   A . n 
A 1 124 SER 124 120  ?    ?   ?   A . n 
A 1 125 GLY 125 121  991  GLY GLY A . n 
A 1 126 GLY 126 122  992  GLY GLY A . n 
A 1 127 GLY 127 123  993  GLY GLY A . n 
A 1 128 GLY 128 124  994  GLY GLY A . n 
A 1 129 GLY 129 125  995  GLY GLY A . n 
A 1 130 SER 130 126  996  SER SER A . n 
A 1 131 SER 131 127  997  SER SER A . n 
A 1 132 GLY 132 128  998  GLY GLY A . n 
A 1 133 SER 133 129  999  SER SER A . n 
A 1 134 SER 134 130  1000 SER SER A . n 
A 1 135 ASP 135 1001 1001 ASP ASP A . n 
A 1 136 VAL 136 1002 1002 VAL VAL A . n 
A 1 137 VAL 137 1003 1003 VAL VAL A . n 
A 1 138 MET 138 1004 1004 MET MET A . n 
A 1 139 THR 139 1005 1005 THR THR A . n 
A 1 140 GLN 140 1006 1006 GLN GLN A . n 
A 1 141 SER 141 1007 1007 SER SER A . n 
A 1 142 HIS 142 1008 1008 HIS HIS A . n 
A 1 143 LYS 143 1009 1009 LYS LYS A . n 
A 1 144 PHE 144 1010 1010 PHE PHE A . n 
A 1 145 MET 145 1011 1011 MET MET A . n 
A 1 146 SER 146 1012 1012 SER SER A . n 
A 1 147 THR 147 1013 1013 THR THR A . n 
A 1 148 SER 148 1014 1014 SER SER A . n 
A 1 149 VAL 149 1015 1015 VAL VAL A . n 
A 1 150 GLY 150 1016 1016 GLY GLY A . n 
A 1 151 ASP 151 1017 1017 ASP ASP A . n 
A 1 152 ARG 152 1018 1018 ARG ARG A . n 
A 1 153 VAL 153 1019 1019 VAL VAL A . n 
A 1 154 SER 154 1020 1020 SER SER A . n 
A 1 155 ILE 155 1021 1021 ILE ILE A . n 
A 1 156 THR 156 1022 1022 THR THR A . n 
A 1 157 CYS 157 1023 1023 CYS CYS A . n 
A 1 158 LYS 158 1024 1024 LYS LYS A . n 
A 1 159 ALA 159 1025 1025 ALA ALA A . n 
A 1 160 SER 160 1026 1026 SER SER A . n 
A 1 161 GLN 161 1027 1027 GLN GLN A . n 
A 1 162 ASP 162 1028 1028 ASP ASP A . n 
A 1 163 VAL 163 1029 1029 VAL VAL A . n 
A 1 164 GLY 164 1030 1030 GLY GLY A . n 
A 1 165 THR 165 1031 1031 THR THR A . n 
A 1 166 ALA 166 1032 1032 ALA ALA A . n 
A 1 167 VAL 167 1033 1033 VAL VAL A . n 
A 1 168 ALA 168 1034 1034 ALA ALA A . n 
A 1 169 TRP 169 1035 1035 TRP TRP A . n 
A 1 170 TYR 170 1036 1036 TYR TYR A . n 
A 1 171 GLN 171 1037 1037 GLN GLN A . n 
A 1 172 GLN 172 1038 1038 GLN GLN A . n 
A 1 173 LYS 173 1039 1039 LYS LYS A . n 
A 1 174 PRO 174 1040 1040 PRO PRO A . n 
A 1 175 GLY 175 1041 1041 GLY GLY A . n 
A 1 176 GLN 176 1042 1042 GLN GLN A . n 
A 1 177 SER 177 1043 1043 SER SER A . n 
A 1 178 PRO 178 1044 1044 PRO PRO A . n 
A 1 179 LYS 179 1045 1045 LYS LYS A . n 
A 1 180 LEU 180 1046 1046 LEU LEU A . n 
A 1 181 LEU 181 1047 1047 LEU LEU A . n 
A 1 182 ILE 182 1048 1048 ILE ILE A . n 
A 1 183 TYR 183 1049 1049 TYR TYR A . n 
A 1 184 TRP 184 1050 1050 TRP TRP A . n 
A 1 185 ALA 185 1051 1051 ALA ALA A . n 
A 1 186 SER 186 1052 1052 SER SER A . n 
A 1 187 THR 187 1053 1053 THR THR A . n 
A 1 188 ARG 188 1054 1054 ARG ARG A . n 
A 1 189 HIS 189 1055 1055 HIS HIS A . n 
A 1 190 THR 190 1056 1056 THR THR A . n 
A 1 191 GLY 191 1057 1057 GLY GLY A . n 
A 1 192 VAL 192 1058 1058 VAL VAL A . n 
A 1 193 PRO 193 1059 1059 PRO PRO A . n 
A 1 194 ASP 194 1060 1060 ASP ASP A . n 
A 1 195 ARG 195 1061 1061 ARG ARG A . n 
A 1 196 PHE 196 1062 1062 PHE PHE A . n 
A 1 197 THR 197 1063 1063 THR THR A . n 
A 1 198 GLY 198 1064 1064 GLY GLY A . n 
A 1 199 SER 199 1065 1065 SER SER A . n 
A 1 200 GLY 200 1066 1066 GLY GLY A . n 
A 1 201 SER 201 1067 1067 SER SER A . n 
A 1 202 GLY 202 1068 1068 GLY GLY A . n 
A 1 203 THR 203 1069 1069 THR THR A . n 
A 1 204 ASP 204 1070 1070 ASP ASP A . n 
A 1 205 PHE 205 1071 1071 PHE PHE A . n 
A 1 206 THR 206 1072 1072 THR THR A . n 
A 1 207 LEU 207 1073 1073 LEU LEU A . n 
A 1 208 THR 208 1074 1074 THR THR A . n 
A 1 209 ILE 209 1075 1075 ILE ILE A . n 
A 1 210 SER 210 1076 1076 SER SER A . n 
A 1 211 ASN 211 1077 1077 ASN ASN A . n 
A 1 212 VAL 212 1078 1078 VAL VAL A . n 
A 1 213 GLN 213 1079 1079 GLN GLN A . n 
A 1 214 SER 214 1080 1080 SER SER A . n 
A 1 215 GLU 215 1081 1081 GLU GLU A . n 
A 1 216 ASP 216 1082 1082 ASP ASP A . n 
A 1 217 LEU 217 1083 1083 LEU LEU A . n 
A 1 218 ALA 218 1084 1084 ALA ALA A . n 
A 1 219 ASP 219 1085 1085 ASP ASP A . n 
A 1 220 TYR 220 1086 1086 TYR TYR A . n 
A 1 221 PHE 221 1087 1087 PHE PHE A . n 
A 1 222 CYS 222 1088 1088 CYS CYS A . n 
A 1 223 GLN 223 1089 1089 GLN GLN A . n 
A 1 224 GLN 224 1090 1090 GLN GLN A . n 
A 1 225 TYR 225 1091 1091 TYR TYR A . n 
A 1 226 SER 226 1092 1092 SER SER A . n 
A 1 227 SER 227 1093 1093 SER SER A . n 
A 1 228 TYR 228 1094 1094 TYR TYR A . n 
A 1 229 PRO 229 1095 1095 PRO PRO A . n 
A 1 230 LEU 230 1096 1096 LEU LEU A . n 
A 1 231 THR 231 1097 1097 THR THR A . n 
A 1 232 PHE 232 1098 1098 PHE PHE A . n 
A 1 233 GLY 233 1099 1099 GLY GLY A . n 
A 1 234 GLY 234 1100 1100 GLY GLY A . n 
A 1 235 GLY 235 1101 1101 GLY GLY A . n 
A 1 236 THR 236 1102 1102 THR THR A . n 
A 1 237 LYS 237 1103 1103 LYS LYS A . n 
A 1 238 LEU 238 1104 1104 LEU LEU A . n 
A 1 239 GLU 239 1105 1105 GLU GLU A . n 
A 1 240 MET 240 1106 1106 MET MET A . n 
A 1 241 LYS 241 1107 1107 LYS LYS A . n 
A 1 242 ARG 242 1108 ?    ?   ?   A . n 
A 1 243 GLY 243 1109 ?    ?   ?   A . n 
A 1 244 GLY 244 1110 ?    ?   ?   A . n 
A 1 245 HIS 245 1111 ?    ?   ?   A . n 
A 1 246 HIS 246 1112 ?    ?   ?   A . n 
A 1 247 HIS 247 1113 ?    ?   ?   A . n 
A 1 248 HIS 248 1114 ?    ?   ?   A . n 
A 1 249 HIS 249 1115 ?    ?   ?   A . n 
A 1 250 HIS 250 1116 ?    ?   ?   A . n 
B 1 1   GLN 1   1    1    GLN GLN H . n 
B 1 2   VAL 2   2    2    VAL VAL H . n 
B 1 3   GLN 3   3    3    GLN GLN H . n 
B 1 4   LEU 4   4    4    LEU LEU H . n 
B 1 5   GLN 5   5    5    GLN GLN H . n 
B 1 6   GLN 6   6    6    GLN GLN H . n 
B 1 7   SER 7   7    7    SER SER H . n 
B 1 8   ASP 8   8    8    ASP ASP H . n 
B 1 9   ALA 9   9    9    ALA ALA H . n 
B 1 10  GLU 10  10   10   GLU GLU H . n 
B 1 11  LEU 11  11   11   LEU LEU H . n 
B 1 12  VAL 12  12   12   VAL VAL H . n 
B 1 13  LYS 13  13   13   LYS LYS H . n 
B 1 14  PRO 14  14   14   PRO PRO H . n 
B 1 15  GLY 15  15   15   GLY GLY H . n 
B 1 16  ALA 16  16   16   ALA ALA H . n 
B 1 17  SER 17  17   17   SER SER H . n 
B 1 18  VAL 18  18   18   VAL VAL H . n 
B 1 19  LYS 19  19   19   LYS LYS H . n 
B 1 20  ILE 20  20   20   ILE ILE H . n 
B 1 21  SER 21  21   21   SER SER H . n 
B 1 22  CYS 22  22   22   CYS CYS H . n 
B 1 23  LYS 23  23   23   LYS LYS H . n 
B 1 24  ALA 24  24   24   ALA ALA H . n 
B 1 25  SER 25  25   25   SER SER H . n 
B 1 26  GLY 26  26   26   GLY GLY H . n 
B 1 27  TYR 27  27   27   TYR TYR H . n 
B 1 28  ILE 28  28   28   ILE ILE H . n 
B 1 29  PHE 29  29   29   PHE PHE H . n 
B 1 30  ALA 30  30   30   ALA ALA H . n 
B 1 31  ASP 31  31   31   ASP ASP H . n 
B 1 32  HIS 32  32   32   HIS HIS H . n 
B 1 33  ALA 33  33   33   ALA ALA H . n 
B 1 34  ILE 34  34   34   ILE ILE H . n 
B 1 35  HIS 35  35   35   HIS HIS H . n 
B 1 36  TRP 36  36   36   TRP TRP H . n 
B 1 37  VAL 37  37   37   VAL VAL H . n 
B 1 38  LYS 38  38   38   LYS LYS H . n 
B 1 39  ARG 39  39   39   ARG ARG H . n 
B 1 40  LYS 40  40   40   LYS LYS H . n 
B 1 41  PRO 41  41   41   PRO PRO H . n 
B 1 42  GLU 42  42   42   GLU GLU H . n 
B 1 43  GLN 43  43   43   GLN GLN H . n 
B 1 44  GLY 44  44   44   GLY GLY H . n 
B 1 45  LEU 45  45   45   LEU LEU H . n 
B 1 46  GLU 46  46   46   GLU GLU H . n 
B 1 47  TRP 47  47   47   TRP TRP H . n 
B 1 48  ILE 48  48   48   ILE ILE H . n 
B 1 49  GLY 49  49   49   GLY GLY H . n 
B 1 50  TYR 50  50   50   TYR TYR H . n 
B 1 51  ILE 51  51   51   ILE ILE H . n 
B 1 52  SER 52  52   52   SER SER H . n 
B 1 53  PRO 53  53   53   PRO PRO H . n 
B 1 54  GLY 54  54   54   GLY GLY H . n 
B 1 55  ASN 55  55   55   ASN ASN H . n 
B 1 56  ASP 56  56   56   ASP ASP H . n 
B 1 57  ASP 57  56   56   ASP ASP H A n 
B 1 58  ILE 58  57   57   ILE ILE H . n 
B 1 59  LYS 59  58   58   LYS LYS H . n 
B 1 60  TYR 60  59   59   TYR TYR H . n 
B 1 61  ASN 61  60   60   ASN ASN H . n 
B 1 62  GLU 62  61   61   GLU GLU H . n 
B 1 63  LYS 63  62   62   LYS LYS H . n 
B 1 64  PHE 64  63   63   PHE PHE H . n 
B 1 65  LYS 65  64   64   LYS LYS H . n 
B 1 66  GLY 66  65   65   GLY GLY H . n 
B 1 67  LYS 67  66   66   LYS LYS H . n 
B 1 68  ALA 68  67   67   ALA ALA H . n 
B 1 69  THR 69  68   68   THR THR H . n 
B 1 70  LEU 70  69   69   LEU LEU H . n 
B 1 71  THR 71  70   70   THR THR H . n 
B 1 72  ALA 72  71   71   ALA ALA H . n 
B 1 73  ASP 73  72   72   ASP ASP H . n 
B 1 74  LYS 74  73   73   LYS LYS H . n 
B 1 75  SER 75  74   74   SER SER H . n 
B 1 76  SER 76  75   75   SER SER H . n 
B 1 77  SER 77  76   76   SER SER H . n 
B 1 78  THR 78  77   77   THR THR H . n 
B 1 79  ALA 79  78   78   ALA ALA H . n 
B 1 80  TYR 80  79   79   TYR TYR H . n 
B 1 81  MET 81  80   80   MET MET H . n 
B 1 82  GLN 82  81   81   GLN GLN H . n 
B 1 83  LEU 83  82   82   LEU LEU H . n 
B 1 84  ASN 84  82   82   ASN ASN H A n 
B 1 85  SER 85  82   82   SER SER H B n 
B 1 86  LEU 86  82   82   LEU LEU H C n 
B 1 87  THR 87  83   83   THR THR H . n 
B 1 88  SER 88  84   84   SER SER H . n 
B 1 89  GLU 89  85   85   GLU GLU H . n 
B 1 90  ASP 90  86   86   ASP ASP H . n 
B 1 91  SER 91  87   87   SER SER H . n 
B 1 92  ALA 92  88   88   ALA ALA H . n 
B 1 93  VAL 93  89   89   VAL VAL H . n 
B 1 94  TYR 94  90   90   TYR TYR H . n 
B 1 95  PHE 95  91   91   PHE PHE H . n 
B 1 96  CYS 96  92   92   CYS CYS H . n 
B 1 97  LYS 97  93   93   LYS LYS H . n 
B 1 98  ARG 98  94   94   ARG ARG H . n 
B 1 99  SER 99  95   95   SER SER H . n 
B 1 100 LEU 100 96   96   LEU LEU H . n 
B 1 101 PRO 101 97   97   PRO PRO H . n 
B 1 102 GLY 102 98   98   GLY GLY H . n 
B 1 103 THR 103 99   99   THR THR H . n 
B 1 104 PHE 104 100  100  PHE PHE H . n 
B 1 105 ASP 105 101  101  ASP ASP H . n 
B 1 106 TYR 106 102  102  TYR TYR H . n 
B 1 107 TRP 107 103  103  TRP TRP H . n 
B 1 108 GLY 108 104  104  GLY GLY H . n 
B 1 109 GLN 109 105  105  GLN GLN H . n 
B 1 110 GLY 110 106  106  GLY GLY H . n 
B 1 111 THR 111 107  107  THR THR H . n 
B 1 112 THR 112 108  108  THR THR H . n 
B 1 113 LEU 113 109  109  LEU LEU H . n 
B 1 114 THR 114 110  110  THR THR H . n 
B 1 115 VAL 115 111  111  VAL VAL H . n 
B 1 116 SER 116 112  112  SER SER H . n 
B 1 117 SER 117 113  ?    ?   ?   H . n 
B 1 118 SER 118 114  ?    ?   ?   H . n 
B 1 119 SER 119 115  ?    ?   ?   H . n 
B 1 120 GLY 120 116  ?    ?   ?   H . n 
B 1 121 GLY 121 117  ?    ?   ?   H . n 
B 1 122 GLY 122 118  ?    ?   ?   H . n 
B 1 123 GLY 123 119  ?    ?   ?   H . n 
B 1 124 SER 124 120  ?    ?   ?   H . n 
B 1 125 GLY 125 121  ?    ?   ?   H . n 
B 1 126 GLY 126 122  992  GLY GLY H . n 
B 1 127 GLY 127 123  993  GLY GLY H . n 
B 1 128 GLY 128 124  994  GLY GLY H . n 
B 1 129 GLY 129 125  995  GLY GLY H . n 
B 1 130 SER 130 126  996  SER SER H . n 
B 1 131 SER 131 127  997  SER SER H . n 
B 1 132 GLY 132 128  998  GLY GLY H . n 
B 1 133 SER 133 129  999  SER SER H . n 
B 1 134 SER 134 130  1000 SER SER H . n 
B 1 135 ASP 135 1001 1001 ASP ASP H . n 
B 1 136 VAL 136 1002 1002 VAL VAL H . n 
B 1 137 VAL 137 1003 1003 VAL VAL H . n 
B 1 138 MET 138 1004 1004 MET MET H . n 
B 1 139 THR 139 1005 1005 THR THR H . n 
B 1 140 GLN 140 1006 1006 GLN GLN H . n 
B 1 141 SER 141 1007 1007 SER SER H . n 
B 1 142 HIS 142 1008 1008 HIS HIS H . n 
B 1 143 LYS 143 1009 1009 LYS LYS H . n 
B 1 144 PHE 144 1010 1010 PHE PHE H . n 
B 1 145 MET 145 1011 1011 MET MET H . n 
B 1 146 SER 146 1012 1012 SER SER H . n 
B 1 147 THR 147 1013 1013 THR THR H . n 
B 1 148 SER 148 1014 1014 SER SER H . n 
B 1 149 VAL 149 1015 1015 VAL VAL H . n 
B 1 150 GLY 150 1016 1016 GLY GLY H . n 
B 1 151 ASP 151 1017 1017 ASP ASP H . n 
B 1 152 ARG 152 1018 1018 ARG ARG H . n 
B 1 153 VAL 153 1019 1019 VAL VAL H . n 
B 1 154 SER 154 1020 1020 SER SER H . n 
B 1 155 ILE 155 1021 1021 ILE ILE H . n 
B 1 156 THR 156 1022 1022 THR THR H . n 
B 1 157 CYS 157 1023 1023 CYS CYS H . n 
B 1 158 LYS 158 1024 1024 LYS LYS H . n 
B 1 159 ALA 159 1025 1025 ALA ALA H . n 
B 1 160 SER 160 1026 1026 SER SER H . n 
B 1 161 GLN 161 1027 1027 GLN GLN H . n 
B 1 162 ASP 162 1028 1028 ASP ASP H . n 
B 1 163 VAL 163 1029 1029 VAL VAL H . n 
B 1 164 GLY 164 1030 1030 GLY GLY H . n 
B 1 165 THR 165 1031 1031 THR THR H . n 
B 1 166 ALA 166 1032 1032 ALA ALA H . n 
B 1 167 VAL 167 1033 1033 VAL VAL H . n 
B 1 168 ALA 168 1034 1034 ALA ALA H . n 
B 1 169 TRP 169 1035 1035 TRP TRP H . n 
B 1 170 TYR 170 1036 1036 TYR TYR H . n 
B 1 171 GLN 171 1037 1037 GLN GLN H . n 
B 1 172 GLN 172 1038 1038 GLN GLN H . n 
B 1 173 LYS 173 1039 1039 LYS LYS H . n 
B 1 174 PRO 174 1040 1040 PRO PRO H . n 
B 1 175 GLY 175 1041 1041 GLY GLY H . n 
B 1 176 GLN 176 1042 1042 GLN GLN H . n 
B 1 177 SER 177 1043 1043 SER SER H . n 
B 1 178 PRO 178 1044 1044 PRO PRO H . n 
B 1 179 LYS 179 1045 1045 LYS LYS H . n 
B 1 180 LEU 180 1046 1046 LEU LEU H . n 
B 1 181 LEU 181 1047 1047 LEU LEU H . n 
B 1 182 ILE 182 1048 1048 ILE ILE H . n 
B 1 183 TYR 183 1049 1049 TYR TYR H . n 
B 1 184 TRP 184 1050 1050 TRP TRP H . n 
B 1 185 ALA 185 1051 1051 ALA ALA H . n 
B 1 186 SER 186 1052 1052 SER SER H . n 
B 1 187 THR 187 1053 1053 THR THR H . n 
B 1 188 ARG 188 1054 1054 ARG ARG H . n 
B 1 189 HIS 189 1055 1055 HIS HIS H . n 
B 1 190 THR 190 1056 1056 THR THR H . n 
B 1 191 GLY 191 1057 1057 GLY GLY H . n 
B 1 192 VAL 192 1058 1058 VAL VAL H . n 
B 1 193 PRO 193 1059 1059 PRO PRO H . n 
B 1 194 ASP 194 1060 1060 ASP ASP H . n 
B 1 195 ARG 195 1061 1061 ARG ARG H . n 
B 1 196 PHE 196 1062 1062 PHE PHE H . n 
B 1 197 THR 197 1063 1063 THR THR H . n 
B 1 198 GLY 198 1064 1064 GLY GLY H . n 
B 1 199 SER 199 1065 1065 SER SER H . n 
B 1 200 GLY 200 1066 1066 GLY GLY H . n 
B 1 201 SER 201 1067 1067 SER SER H . n 
B 1 202 GLY 202 1068 1068 GLY GLY H . n 
B 1 203 THR 203 1069 1069 THR THR H . n 
B 1 204 ASP 204 1070 1070 ASP ASP H . n 
B 1 205 PHE 205 1071 1071 PHE PHE H . n 
B 1 206 THR 206 1072 1072 THR THR H . n 
B 1 207 LEU 207 1073 1073 LEU LEU H . n 
B 1 208 THR 208 1074 1074 THR THR H . n 
B 1 209 ILE 209 1075 1075 ILE ILE H . n 
B 1 210 SER 210 1076 1076 SER SER H . n 
B 1 211 ASN 211 1077 1077 ASN ASN H . n 
B 1 212 VAL 212 1078 1078 VAL VAL H . n 
B 1 213 GLN 213 1079 1079 GLN GLN H . n 
B 1 214 SER 214 1080 1080 SER SER H . n 
B 1 215 GLU 215 1081 1081 GLU GLU H . n 
B 1 216 ASP 216 1082 1082 ASP ASP H . n 
B 1 217 LEU 217 1083 1083 LEU LEU H . n 
B 1 218 ALA 218 1084 1084 ALA ALA H . n 
B 1 219 ASP 219 1085 1085 ASP ASP H . n 
B 1 220 TYR 220 1086 1086 TYR TYR H . n 
B 1 221 PHE 221 1087 1087 PHE PHE H . n 
B 1 222 CYS 222 1088 1088 CYS CYS H . n 
B 1 223 GLN 223 1089 1089 GLN GLN H . n 
B 1 224 GLN 224 1090 1090 GLN GLN H . n 
B 1 225 TYR 225 1091 1091 TYR TYR H . n 
B 1 226 SER 226 1092 1092 SER SER H . n 
B 1 227 SER 227 1093 1093 SER SER H . n 
B 1 228 TYR 228 1094 1094 TYR TYR H . n 
B 1 229 PRO 229 1095 1095 PRO PRO H . n 
B 1 230 LEU 230 1096 1096 LEU LEU H . n 
B 1 231 THR 231 1097 1097 THR THR H . n 
B 1 232 PHE 232 1098 1098 PHE PHE H . n 
B 1 233 GLY 233 1099 1099 GLY GLY H . n 
B 1 234 GLY 234 1100 1100 GLY GLY H . n 
B 1 235 GLY 235 1101 1101 GLY GLY H . n 
B 1 236 THR 236 1102 1102 THR THR H . n 
B 1 237 LYS 237 1103 1103 LYS LYS H . n 
B 1 238 LEU 238 1104 1104 LEU LEU H . n 
B 1 239 GLU 239 1105 1105 GLU GLU H . n 
B 1 240 MET 240 1106 1106 MET MET H . n 
B 1 241 LYS 241 1107 1107 LYS LYS H . n 
B 1 242 ARG 242 1108 ?    ?   ?   H . n 
B 1 243 GLY 243 1109 ?    ?   ?   H . n 
B 1 244 GLY 244 1110 ?    ?   ?   H . n 
B 1 245 HIS 245 1111 ?    ?   ?   H . n 
B 1 246 HIS 246 1112 ?    ?   ?   H . n 
B 1 247 HIS 247 1113 ?    ?   ?   H . n 
B 1 248 HIS 248 1114 ?    ?   ?   H . n 
B 1 249 HIS 249 1115 ?    ?   ?   H . n 
B 1 250 HIS 250 1116 ?    ?   ?   H . n 
C 2 1   ALA 1   1    201  ALA DRG M . n 
C 2 2   PRO 2   2    201  PRO DRG M . n 
C 2 3   GLY 3   3    201  GLY DRG M . n 
C 2 4   SER 4   4    201  SER DRG M . n 
C 2 5   THR 5   5    201  THR DRG M . n 
C 2 6   ALA 6   6    201  ALA DRG M . n 
C 2 7   PRO 7   7    201  PRO DRG M . n 
C 2 8   NH2 8   8    201  NH2 DRG M . n 
D 2 1   ALA 1   1    201  ALA DRG N . n 
D 2 2   PRO 2   2    201  PRO DRG N . n 
D 2 3   GLY 3   3    201  GLY DRG N . n 
D 2 4   SER 4   4    201  SER DRG N . n 
D 2 5   THR 5   5    201  THR DRG N . n 
D 2 6   ALA 6   6    201  ALA DRG N . n 
D 2 7   PRO 7   7    201  PRO DRG N . n 
D 2 8   NH2 8   8    201  NH2 DRG N . 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 A2G ? ? A2G ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NH2 ? ? NH2 ? ? '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 
E 3 EDO 1   301 203  EDO EDO A . 
F 3 EDO 1   302 204  EDO EDO A . 
G 3 EDO 1   303 205  EDO EDO A . 
H 3 EDO 1   304 206  EDO EDO A . 
I 3 EDO 1   305 207  EDO EDO A . 
J 3 EDO 1   306 1201 EDO EDO A . 
K 3 EDO 1   307 1202 EDO EDO A . 
L 3 EDO 1   301 202  EDO EDO H . 
M 3 EDO 1   302 202  EDO EDO H . 
N 3 EDO 1   303 203  EDO EDO H . 
O 3 EDO 1   304 1201 EDO EDO H . 
P 3 EDO 1   305 595  EDO EDO H . 
Q 4 A2G 1   101 201  A2G DRG M . 
R 4 A2G 1   102 201  A2G DRG M . 
S 4 A2G 1   101 201  A2G DRG N . 
T 4 A2G 1   102 201  A2G DRG N . 
U 5 HOH 1   401 156  HOH HOH A . 
U 5 HOH 2   402 572  HOH HOH A . 
U 5 HOH 3   403 158  HOH HOH A . 
U 5 HOH 4   404 511  HOH HOH A . 
U 5 HOH 5   405 495  HOH HOH A . 
U 5 HOH 6   406 216  HOH HOH A . 
U 5 HOH 7   407 560  HOH HOH A . 
U 5 HOH 8   408 122  HOH HOH A . 
U 5 HOH 9   409 230  HOH HOH A . 
U 5 HOH 10  410 505  HOH HOH A . 
U 5 HOH 11  411 105  HOH HOH A . 
U 5 HOH 12  412 524  HOH HOH A . 
U 5 HOH 13  413 354  HOH HOH A . 
U 5 HOH 14  414 277  HOH HOH A . 
U 5 HOH 15  415 99   HOH HOH A . 
U 5 HOH 16  416 148  HOH HOH A . 
U 5 HOH 17  417 351  HOH HOH A . 
U 5 HOH 18  418 49   HOH HOH A . 
U 5 HOH 19  419 65   HOH HOH A . 
U 5 HOH 20  420 573  HOH HOH A . 
U 5 HOH 21  421 469  HOH HOH A . 
U 5 HOH 22  422 507  HOH HOH A . 
U 5 HOH 23  423 93   HOH HOH A . 
U 5 HOH 24  424 29   HOH HOH A . 
U 5 HOH 25  425 420  HOH HOH A . 
U 5 HOH 26  426 289  HOH HOH A . 
U 5 HOH 27  427 177  HOH HOH A . 
U 5 HOH 28  428 72   HOH HOH A . 
U 5 HOH 29  429 161  HOH HOH A . 
U 5 HOH 30  430 229  HOH HOH A . 
U 5 HOH 31  431 22   HOH HOH A . 
U 5 HOH 32  432 395  HOH HOH A . 
U 5 HOH 33  433 113  HOH HOH A . 
U 5 HOH 34  434 553  HOH HOH A . 
U 5 HOH 35  435 410  HOH HOH A . 
U 5 HOH 36  436 480  HOH HOH A . 
U 5 HOH 37  437 102  HOH HOH A . 
U 5 HOH 38  438 190  HOH HOH A . 
U 5 HOH 39  439 33   HOH HOH A . 
U 5 HOH 40  440 257  HOH HOH A . 
U 5 HOH 41  441 223  HOH HOH A . 
U 5 HOH 42  442 188  HOH HOH A . 
U 5 HOH 43  443 125  HOH HOH A . 
U 5 HOH 44  444 275  HOH HOH A . 
U 5 HOH 45  445 146  HOH HOH A . 
U 5 HOH 46  446 393  HOH HOH A . 
U 5 HOH 47  447 136  HOH HOH A . 
U 5 HOH 48  448 45   HOH HOH A . 
U 5 HOH 49  449 112  HOH HOH A . 
U 5 HOH 50  450 220  HOH HOH A . 
U 5 HOH 51  451 20   HOH HOH A . 
U 5 HOH 52  452 31   HOH HOH A . 
U 5 HOH 53  453 83   HOH HOH A . 
U 5 HOH 54  454 10   HOH HOH A . 
U 5 HOH 55  455 133  HOH HOH A . 
U 5 HOH 56  456 79   HOH HOH A . 
U 5 HOH 57  457 215  HOH HOH A . 
U 5 HOH 58  458 54   HOH HOH A . 
U 5 HOH 59  459 457  HOH HOH A . 
U 5 HOH 60  460 407  HOH HOH A . 
U 5 HOH 61  461 571  HOH HOH A . 
U 5 HOH 62  462 18   HOH HOH A . 
U 5 HOH 63  463 321  HOH HOH A . 
U 5 HOH 64  464 70   HOH HOH A . 
U 5 HOH 65  465 411  HOH HOH A . 
U 5 HOH 66  466 332  HOH HOH A . 
U 5 HOH 67  467 32   HOH HOH A . 
U 5 HOH 68  468 69   HOH HOH A . 
U 5 HOH 69  469 68   HOH HOH A . 
U 5 HOH 70  470 91   HOH HOH A . 
U 5 HOH 71  471 96   HOH HOH A . 
U 5 HOH 72  472 307  HOH HOH A . 
U 5 HOH 73  473 117  HOH HOH A . 
U 5 HOH 74  474 27   HOH HOH A . 
U 5 HOH 75  475 512  HOH HOH A . 
U 5 HOH 76  476 355  HOH HOH A . 
U 5 HOH 77  477 64   HOH HOH A . 
U 5 HOH 78  478 456  HOH HOH A . 
U 5 HOH 79  479 506  HOH HOH A . 
U 5 HOH 80  480 109  HOH HOH A . 
U 5 HOH 81  481 78   HOH HOH A . 
U 5 HOH 82  482 375  HOH HOH A . 
U 5 HOH 83  483 335  HOH HOH A . 
U 5 HOH 84  484 129  HOH HOH A . 
U 5 HOH 85  485 41   HOH HOH A . 
U 5 HOH 86  486 26   HOH HOH A . 
U 5 HOH 87  487 149  HOH HOH A . 
U 5 HOH 88  488 183  HOH HOH A . 
U 5 HOH 89  489 143  HOH HOH A . 
U 5 HOH 90  490 152  HOH HOH A . 
U 5 HOH 91  491 132  HOH HOH A . 
U 5 HOH 92  492 213  HOH HOH A . 
U 5 HOH 93  493 48   HOH HOH A . 
U 5 HOH 94  494 574  HOH HOH A . 
U 5 HOH 95  495 510  HOH HOH A . 
U 5 HOH 96  496 515  HOH HOH A . 
U 5 HOH 97  497 154  HOH HOH A . 
U 5 HOH 98  498 217  HOH HOH A . 
U 5 HOH 99  499 390  HOH HOH A . 
U 5 HOH 100 500 114  HOH HOH A . 
U 5 HOH 101 501 391  HOH HOH A . 
U 5 HOH 102 502 157  HOH HOH A . 
U 5 HOH 103 503 81   HOH HOH A . 
U 5 HOH 104 504 269  HOH HOH A . 
U 5 HOH 105 505 421  HOH HOH A . 
U 5 HOH 106 506 30   HOH HOH A . 
U 5 HOH 107 507 98   HOH HOH A . 
U 5 HOH 108 508 137  HOH HOH A . 
U 5 HOH 109 509 526  HOH HOH A . 
U 5 HOH 110 510 514  HOH HOH A . 
U 5 HOH 111 511 267  HOH HOH A . 
U 5 HOH 112 512 176  HOH HOH A . 
U 5 HOH 113 513 244  HOH HOH A . 
U 5 HOH 114 514 387  HOH HOH A . 
U 5 HOH 115 515 39   HOH HOH A . 
U 5 HOH 116 516 74   HOH HOH A . 
U 5 HOH 117 517 530  HOH HOH A . 
U 5 HOH 118 518 173  HOH HOH A . 
U 5 HOH 119 519 295  HOH HOH A . 
U 5 HOH 120 520 193  HOH HOH A . 
U 5 HOH 121 521 59   HOH HOH A . 
U 5 HOH 122 522 347  HOH HOH A . 
U 5 HOH 123 523 256  HOH HOH A . 
U 5 HOH 124 524 89   HOH HOH A . 
U 5 HOH 125 525 224  HOH HOH A . 
U 5 HOH 126 526 189  HOH HOH A . 
U 5 HOH 127 527 299  HOH HOH A . 
U 5 HOH 128 528 95   HOH HOH A . 
U 5 HOH 129 529 85   HOH HOH A . 
U 5 HOH 130 530 9    HOH HOH A . 
U 5 HOH 131 531 163  HOH HOH A . 
U 5 HOH 132 532 155  HOH HOH A . 
U 5 HOH 133 533 46   HOH HOH A . 
U 5 HOH 134 534 141  HOH HOH A . 
U 5 HOH 135 535 196  HOH HOH A . 
U 5 HOH 136 536 253  HOH HOH A . 
U 5 HOH 137 537 441  HOH HOH A . 
U 5 HOH 138 538 565  HOH HOH A . 
U 5 HOH 139 539 235  HOH HOH A . 
U 5 HOH 140 540 138  HOH HOH A . 
U 5 HOH 141 541 458  HOH HOH A . 
U 5 HOH 142 542 320  HOH HOH A . 
U 5 HOH 143 543 84   HOH HOH A . 
U 5 HOH 144 544 200  HOH HOH A . 
U 5 HOH 145 545 365  HOH HOH A . 
U 5 HOH 146 546 13   HOH HOH A . 
U 5 HOH 147 547 115  HOH HOH A . 
U 5 HOH 148 548 66   HOH HOH A . 
U 5 HOH 149 549 25   HOH HOH A . 
U 5 HOH 150 550 60   HOH HOH A . 
U 5 HOH 151 551 195  HOH HOH A . 
U 5 HOH 152 552 270  HOH HOH A . 
U 5 HOH 153 553 398  HOH HOH A . 
U 5 HOH 154 554 233  HOH HOH A . 
U 5 HOH 155 555 88   HOH HOH A . 
U 5 HOH 156 556 24   HOH HOH A . 
U 5 HOH 157 557 166  HOH HOH A . 
U 5 HOH 158 558 525  HOH HOH A . 
U 5 HOH 159 559 376  HOH HOH A . 
U 5 HOH 160 560 245  HOH HOH A . 
U 5 HOH 161 561 331  HOH HOH A . 
U 5 HOH 162 562 52   HOH HOH A . 
U 5 HOH 163 563 262  HOH HOH A . 
U 5 HOH 164 564 392  HOH HOH A . 
U 5 HOH 165 565 128  HOH HOH A . 
U 5 HOH 166 566 561  HOH HOH A . 
U 5 HOH 167 567 513  HOH HOH A . 
U 5 HOH 168 568 73   HOH HOH A . 
U 5 HOH 169 569 531  HOH HOH A . 
U 5 HOH 170 570 167  HOH HOH A . 
U 5 HOH 171 571 432  HOH HOH A . 
U 5 HOH 172 572 80   HOH HOH A . 
U 5 HOH 173 573 483  HOH HOH A . 
U 5 HOH 174 574 402  HOH HOH A . 
U 5 HOH 175 575 182  HOH HOH A . 
U 5 HOH 176 576 5    HOH HOH A . 
U 5 HOH 177 577 541  HOH HOH A . 
U 5 HOH 178 578 575  HOH HOH A . 
U 5 HOH 179 579 279  HOH HOH A . 
U 5 HOH 180 580 382  HOH HOH A . 
U 5 HOH 181 581 435  HOH HOH A . 
U 5 HOH 182 582 2    HOH HOH A . 
U 5 HOH 183 583 8    HOH HOH A . 
U 5 HOH 184 584 508  HOH HOH A . 
U 5 HOH 185 585 273  HOH HOH A . 
U 5 HOH 186 586 440  HOH HOH A . 
U 5 HOH 187 587 169  HOH HOH A . 
U 5 HOH 188 588 350  HOH HOH A . 
U 5 HOH 189 589 290  HOH HOH A . 
U 5 HOH 190 590 385  HOH HOH A . 
U 5 HOH 191 591 323  HOH HOH A . 
U 5 HOH 192 592 562  HOH HOH A . 
U 5 HOH 193 593 478  HOH HOH A . 
U 5 HOH 194 594 503  HOH HOH A . 
U 5 HOH 195 595 564  HOH HOH A . 
U 5 HOH 196 596 563  HOH HOH A . 
U 5 HOH 197 597 490  HOH HOH A . 
U 5 HOH 198 598 75   HOH HOH A . 
U 5 HOH 199 599 509  HOH HOH A . 
U 5 HOH 200 600 252  HOH HOH A . 
U 5 HOH 201 601 502  HOH HOH A . 
U 5 HOH 202 602 280  HOH HOH A . 
U 5 HOH 203 603 466  HOH HOH A . 
U 5 HOH 204 604 90   HOH HOH A . 
U 5 HOH 205 605 485  HOH HOH A . 
U 5 HOH 206 606 312  HOH HOH A . 
U 5 HOH 207 607 430  HOH HOH A . 
U 5 HOH 208 608 482  HOH HOH A . 
U 5 HOH 209 609 106  HOH HOH A . 
U 5 HOH 210 610 349  HOH HOH A . 
U 5 HOH 211 611 479  HOH HOH A . 
U 5 HOH 212 612 232  HOH HOH A . 
U 5 HOH 213 613 494  HOH HOH A . 
U 5 HOH 214 614 386  HOH HOH A . 
U 5 HOH 215 615 568  HOH HOH A . 
U 5 HOH 216 616 422  HOH HOH A . 
U 5 HOH 217 617 342  HOH HOH A . 
U 5 HOH 218 618 487  HOH HOH A . 
U 5 HOH 219 619 477  HOH HOH A . 
U 5 HOH 220 620 260  HOH HOH A . 
U 5 HOH 221 621 501  HOH HOH A . 
V 5 HOH 1   401 336  HOH HOH H . 
V 5 HOH 2   402 522  HOH HOH H . 
V 5 HOH 3   403 62   HOH HOH H . 
V 5 HOH 4   404 492  HOH HOH H . 
V 5 HOH 5   405 517  HOH HOH H . 
V 5 HOH 6   406 551  HOH HOH H . 
V 5 HOH 7   407 110  HOH HOH H . 
V 5 HOH 8   408 191  HOH HOH H . 
V 5 HOH 9   409 559  HOH HOH H . 
V 5 HOH 10  410 34   HOH HOH H . 
V 5 HOH 11  411 371  HOH HOH H . 
V 5 HOH 12  412 591  HOH HOH H . 
V 5 HOH 13  413 304  HOH HOH H . 
V 5 HOH 14  414 300  HOH HOH H . 
V 5 HOH 15  415 542  HOH HOH H . 
V 5 HOH 16  416 108  HOH HOH H . 
V 5 HOH 17  417 338  HOH HOH H . 
V 5 HOH 18  418 399  HOH HOH H . 
V 5 HOH 19  419 51   HOH HOH H . 
V 5 HOH 20  420 134  HOH HOH H . 
V 5 HOH 21  421 150  HOH HOH H . 
V 5 HOH 22  422 118  HOH HOH H . 
V 5 HOH 23  423 264  HOH HOH H . 
V 5 HOH 24  424 583  HOH HOH H . 
V 5 HOH 25  425 55   HOH HOH H . 
V 5 HOH 26  426 419  HOH HOH H . 
V 5 HOH 27  427 409  HOH HOH H . 
V 5 HOH 28  428 40   HOH HOH H . 
V 5 HOH 29  429 36   HOH HOH H . 
V 5 HOH 30  430 424  HOH HOH H . 
V 5 HOH 31  431 97   HOH HOH H . 
V 5 HOH 32  432 576  HOH HOH H . 
V 5 HOH 33  433 76   HOH HOH H . 
V 5 HOH 34  434 587  HOH HOH H . 
V 5 HOH 35  435 100  HOH HOH H . 
V 5 HOH 36  436 274  HOH HOH H . 
V 5 HOH 37  437 8    HOH HOH H . 
V 5 HOH 38  438 11   HOH HOH H . 
V 5 HOH 39  439 314  HOH HOH H . 
V 5 HOH 40  440 160  HOH HOH H . 
V 5 HOH 41  441 184  HOH HOH H . 
V 5 HOH 42  442 423  HOH HOH H . 
V 5 HOH 43  443 199  HOH HOH H . 
V 5 HOH 44  444 373  HOH HOH H . 
V 5 HOH 45  445 584  HOH HOH H . 
V 5 HOH 46  446 450  HOH HOH H . 
V 5 HOH 47  447 140  HOH HOH H . 
V 5 HOH 48  448 250  HOH HOH H . 
V 5 HOH 49  449 219  HOH HOH H . 
V 5 HOH 50  450 340  HOH HOH H . 
V 5 HOH 51  451 593  HOH HOH H . 
V 5 HOH 52  452 107  HOH HOH H . 
V 5 HOH 53  453 11   HOH HOH H . 
V 5 HOH 54  454 63   HOH HOH H . 
V 5 HOH 55  455 116  HOH HOH H . 
V 5 HOH 56  456 240  HOH HOH H . 
V 5 HOH 57  457 23   HOH HOH H . 
V 5 HOH 58  458 209  HOH HOH H . 
V 5 HOH 59  459 437  HOH HOH H . 
V 5 HOH 60  460 9    HOH HOH H . 
V 5 HOH 61  461 400  HOH HOH H . 
V 5 HOH 62  462 534  HOH HOH H . 
V 5 HOH 63  463 588  HOH HOH H . 
V 5 HOH 64  464 582  HOH HOH H . 
V 5 HOH 65  465 214  HOH HOH H . 
V 5 HOH 66  466 175  HOH HOH H . 
V 5 HOH 67  467 518  HOH HOH H . 
V 5 HOH 68  468 535  HOH HOH H . 
V 5 HOH 69  469 316  HOH HOH H . 
V 5 HOH 70  470 552  HOH HOH H . 
V 5 HOH 71  471 82   HOH HOH H . 
V 5 HOH 72  472 549  HOH HOH H . 
V 5 HOH 73  473 103  HOH HOH H . 
V 5 HOH 74  474 124  HOH HOH H . 
V 5 HOH 75  475 179  HOH HOH H . 
V 5 HOH 76  476 357  HOH HOH H . 
V 5 HOH 77  477 130  HOH HOH H . 
V 5 HOH 78  478 358  HOH HOH H . 
V 5 HOH 79  479 471  HOH HOH H . 
V 5 HOH 80  480 44   HOH HOH H . 
V 5 HOH 81  481 443  HOH HOH H . 
V 5 HOH 82  482 16   HOH HOH H . 
V 5 HOH 83  483 546  HOH HOH H . 
V 5 HOH 84  484 581  HOH HOH H . 
V 5 HOH 85  485 519  HOH HOH H . 
V 5 HOH 86  486 7    HOH HOH H . 
V 5 HOH 87  487 287  HOH HOH H . 
V 5 HOH 88  488 5    HOH HOH H . 
V 5 HOH 89  489 170  HOH HOH H . 
V 5 HOH 90  490 282  HOH HOH H . 
V 5 HOH 91  491 318  HOH HOH H . 
V 5 HOH 92  492 38   HOH HOH H . 
V 5 HOH 93  493 594  HOH HOH H . 
V 5 HOH 94  494 50   HOH HOH H . 
V 5 HOH 95  495 92   HOH HOH H . 
V 5 HOH 96  496 17   HOH HOH H . 
V 5 HOH 97  497 322  HOH HOH H . 
V 5 HOH 98  498 204  HOH HOH H . 
V 5 HOH 99  499 218  HOH HOH H . 
V 5 HOH 100 500 557  HOH HOH H . 
V 5 HOH 101 501 21   HOH HOH H . 
V 5 HOH 102 502 185  HOH HOH H . 
V 5 HOH 103 503 6    HOH HOH H . 
V 5 HOH 104 504 151  HOH HOH H . 
V 5 HOH 105 505 127  HOH HOH H . 
V 5 HOH 106 506 94   HOH HOH H . 
V 5 HOH 107 507 10   HOH HOH H . 
V 5 HOH 108 508 405  HOH HOH H . 
V 5 HOH 109 509 1    HOH HOH H . 
V 5 HOH 110 510 227  HOH HOH H . 
V 5 HOH 111 511 53   HOH HOH H . 
V 5 HOH 112 512 585  HOH HOH H . 
V 5 HOH 113 513 178  HOH HOH H . 
V 5 HOH 114 514 120  HOH HOH H . 
V 5 HOH 115 515 381  HOH HOH H . 
V 5 HOH 116 516 47   HOH HOH H . 
V 5 HOH 117 517 545  HOH HOH H . 
V 5 HOH 118 518 101  HOH HOH H . 
V 5 HOH 119 519 389  HOH HOH H . 
V 5 HOH 120 520 558  HOH HOH H . 
V 5 HOH 121 521 327  HOH HOH H . 
V 5 HOH 122 522 547  HOH HOH H . 
V 5 HOH 123 523 302  HOH HOH H . 
V 5 HOH 124 524 35   HOH HOH H . 
V 5 HOH 125 525 104  HOH HOH H . 
V 5 HOH 126 526 548  HOH HOH H . 
V 5 HOH 127 527 234  HOH HOH H . 
V 5 HOH 128 528 580  HOH HOH H . 
V 5 HOH 129 529 303  HOH HOH H . 
V 5 HOH 130 530 201  HOH HOH H . 
V 5 HOH 131 531 205  HOH HOH H . 
V 5 HOH 132 532 577  HOH HOH H . 
V 5 HOH 133 533 326  HOH HOH H . 
V 5 HOH 134 534 144  HOH HOH H . 
V 5 HOH 135 535 488  HOH HOH H . 
V 5 HOH 136 536 153  HOH HOH H . 
V 5 HOH 137 537 12   HOH HOH H . 
V 5 HOH 138 538 468  HOH HOH H . 
V 5 HOH 139 539 67   HOH HOH H . 
V 5 HOH 140 540 162  HOH HOH H . 
V 5 HOH 141 541 532  HOH HOH H . 
V 5 HOH 142 542 254  HOH HOH H . 
V 5 HOH 143 543 126  HOH HOH H . 
V 5 HOH 144 544 57   HOH HOH H . 
V 5 HOH 145 545 87   HOH HOH H . 
V 5 HOH 146 546 71   HOH HOH H . 
V 5 HOH 147 547 484  HOH HOH H . 
V 5 HOH 148 548 168  HOH HOH H . 
V 5 HOH 149 549 123  HOH HOH H . 
V 5 HOH 150 550 550  HOH HOH H . 
V 5 HOH 151 551 536  HOH HOH H . 
V 5 HOH 152 552 131  HOH HOH H . 
V 5 HOH 153 553 310  HOH HOH H . 
V 5 HOH 154 554 529  HOH HOH H . 
V 5 HOH 155 555 368  HOH HOH H . 
V 5 HOH 156 556 226  HOH HOH H . 
V 5 HOH 157 557 578  HOH HOH H . 
V 5 HOH 158 558 370  HOH HOH H . 
V 5 HOH 159 559 192  HOH HOH H . 
V 5 HOH 160 560 37   HOH HOH H . 
V 5 HOH 161 561 445  HOH HOH H . 
V 5 HOH 162 562 521  HOH HOH H . 
V 5 HOH 163 563 305  HOH HOH H . 
V 5 HOH 164 564 499  HOH HOH H . 
V 5 HOH 165 565 3    HOH HOH H . 
V 5 HOH 166 566 589  HOH HOH H . 
V 5 HOH 167 567 538  HOH HOH H . 
V 5 HOH 168 568 486  HOH HOH H . 
V 5 HOH 169 569 396  HOH HOH H . 
V 5 HOH 170 570 544  HOH HOH H . 
V 5 HOH 171 571 384  HOH HOH H . 
V 5 HOH 172 572 579  HOH HOH H . 
V 5 HOH 173 573 297  HOH HOH H . 
V 5 HOH 174 574 533  HOH HOH H . 
V 5 HOH 175 575 537  HOH HOH H . 
V 5 HOH 176 576 566  HOH HOH H . 
V 5 HOH 177 577 543  HOH HOH H . 
V 5 HOH 178 578 504  HOH HOH H . 
V 5 HOH 179 579 247  HOH HOH H . 
V 5 HOH 180 580 497  HOH HOH H . 
V 5 HOH 181 581 567  HOH HOH H . 
V 5 HOH 182 582 278  HOH HOH H . 
V 5 HOH 183 583 346  HOH HOH H . 
V 5 HOH 184 584 7    HOH HOH H . 
V 5 HOH 185 585 208  HOH HOH H . 
V 5 HOH 186 586 554  HOH HOH H . 
V 5 HOH 187 587 481  HOH HOH H . 
V 5 HOH 188 588 249  HOH HOH H . 
V 5 HOH 189 589 171  HOH HOH H . 
V 5 HOH 190 590 592  HOH HOH H . 
V 5 HOH 191 591 165  HOH HOH H . 
V 5 HOH 192 592 369  HOH HOH H . 
V 5 HOH 193 593 491  HOH HOH H . 
V 5 HOH 194 594 291  HOH HOH H . 
V 5 HOH 195 595 344  HOH HOH H . 
V 5 HOH 196 596 4    HOH HOH H . 
V 5 HOH 197 597 489  HOH HOH H . 
V 5 HOH 198 598 319  HOH HOH H . 
V 5 HOH 199 599 239  HOH HOH H . 
V 5 HOH 200 600 164  HOH HOH H . 
V 5 HOH 201 601 248  HOH HOH H . 
V 5 HOH 202 602 590  HOH HOH H . 
V 5 HOH 203 603 556  HOH HOH H . 
V 5 HOH 204 604 493  HOH HOH H . 
V 5 HOH 205 605 555  HOH HOH H . 
V 5 HOH 206 606 431  HOH HOH H . 
V 5 HOH 207 607 540  HOH HOH H . 
W 5 HOH 1   201 187  HOH HOH M . 
W 5 HOH 2   202 221  HOH HOH M . 
W 5 HOH 3   203 121  HOH HOH M . 
W 5 HOH 4   204 142  HOH HOH M . 
W 5 HOH 5   205 516  HOH HOH M . 
W 5 HOH 6   206 119  HOH HOH M . 
W 5 HOH 7   207 570  HOH HOH M . 
W 5 HOH 8   208 15   HOH HOH M . 
W 5 HOH 9   209 111  HOH HOH M . 
W 5 HOH 10  210 434  HOH HOH M . 
W 5 HOH 11  211 306  HOH HOH M . 
W 5 HOH 12  212 569  HOH HOH M . 
W 5 HOH 13  213 475  HOH HOH M . 
X 5 HOH 1   201 172  HOH HOH N . 
X 5 HOH 2   202 427  HOH HOH N . 
X 5 HOH 3   203 243  HOH HOH N . 
X 5 HOH 4   204 86   HOH HOH N . 
X 5 HOH 5   205 283  HOH HOH N . 
X 5 HOH 6   206 147  HOH HOH N . 
X 5 HOH 7   207 222  HOH HOH N . 
X 5 HOH 8   208 145  HOH HOH N . 
X 5 HOH 9   209 203  HOH HOH N . 
X 5 HOH 10  210 413  HOH HOH N . 
X 5 HOH 11  211 1    HOH HOH N . 
X 5 HOH 12  212 211  HOH HOH N . 
X 5 HOH 13  213 586  HOH HOH N . 
X 5 HOH 14  214 12   HOH HOH N . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   102.99 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8S6K 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.992 
_cell.length_a_esd                 ? 
_cell.length_b                     69.667 
_cell.length_b_esd                 ? 
_cell.length_c                     87.367 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8S6K 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   8S6K 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.44 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.58 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8 
_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    
;lithium chloride
Tris 
PEG 8000
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-12-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9999 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8S6K 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.75 
_reflns.d_resolution_low                               20 
_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                                     52287 
_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                           96.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_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                              0.085 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.75 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6651 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.778 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          84.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.489 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            1.60 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.81 
_refine.aniso_B[2][2]                            -0.17 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.95 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               23.741 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.940 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8S6K 
_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                            1.75 
_refine.ls_d_res_low                             19.90 
_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                     50086 
_refine.ls_number_reflns_R_free                  2094 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.05 
_refine.ls_percent_reflns_R_free                 4.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18396 
_refine.ls_R_factor_R_free                       0.22142 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18236 
_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                          ? 
_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                       0.117 
_refine.pdbx_overall_ESU_R_Free                  0.116 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                             5.487 
_refine.overall_SU_ML                            0.089 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.75 
_refine_hist.d_res_low                        19.90 
_refine_hist.number_atoms_solvent             456 
_refine_hist.number_atoms_total               4192 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3688 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_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' ? 0.015  0.013  3842 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.018  3507 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.945  1.699  5190 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.611  1.656  8137 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.550  5.000  469  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 30.150 23.497 163  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.896 15.000 608  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 20.628 15.000 12   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.102  0.200  512  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  4289 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  855  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.368  1.677  1870 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.367  1.676  1869 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.139  2.506  2329 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.139  2.507  2330 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.052  1.870  1972 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.051  1.872  1973 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.148  2.692  2858 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.843  20.955 4337 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.840  20.959 4337 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.10 ? 0.05 1 'interatomic distance' ? A 3554 ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.10 ? 0.05 2 'interatomic distance' ? H 3554 ? ? 1 
'X-RAY DIFFRACTION' 1 ? ? 0.07 ? 0.05 3 'interatomic distance' ? A 3404 ? ? 2 
'X-RAY DIFFRACTION' 2 ? ? 0.07 ? 0.05 4 'interatomic distance' ? H 3404 ? ? 2 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.750 
_refine_ls_shell.d_res_low                        1.795 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             120 
_refine_ls_shell.number_reflns_R_work             2867 
_refine_ls_shell.percent_reflns_obs               74.66 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.257 
_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   20 
_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                  0.287 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 A 1 
2 H 1 
1 A 2 
2 H 2 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1 0 A GLN 1   . A SER 116 . A GLN 1   A SER 112  0 ? 
1 2 0 B GLN 1   . B SER 116 . H GLN 1   H SER 112  0 ? 
2 1 0 A GLY 126 . A MET 240 . A GLY 122 A MET 1106 0 ? 
2 2 0 B GLY 126 . B MET 240 . H GLY 122 H MET 1106 0 ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 ? 
2 ? 
# 
_struct.entry_id                     8S6K 
_struct.title                        'Crystal structure of ScFv-G2D11 complexed to a bis-Tn glycopeptide' 
_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        8S6K 
_struct_keywords.text            'Monoclonal antibody, ScFv-G2D11, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 4 ? 
R N N 4 ? 
S N N 4 ? 
T N N 4 ? 
U N N 5 ? 
V N N 5 ? 
W N N 5 ? 
X N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 8S6K       8S6K   ? 1 ?       1   
2 UNP MUC1_HUMAN P15941 ? 2 APGSTAP 127 
# 
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 8S6K A 1 ? 250 ? 8S6K   1   ? 1116 ? 1 1116 
2 1 8S6K H 1 ? 250 ? 8S6K   1   ? 1116 ? 1 1116 
3 2 8S6K M 1 ? 7   ? P15941 127 ? 133  ? 1 7    
4 2 8S6K N 1 ? 7   ? P15941 127 ? 133  ? 1 7    
# 
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 
3 8S6K NH2 M 8 ? UNP P15941 ? ? amidation 8 1 
4 8S6K NH2 N 8 ? UNP P15941 ? ? amidation 8 2 
# 
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 ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,F,G,H,I,J,K,Q,R,U,W 
2 1 B,D,L,M,N,O,P,S,T,V,X     
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'equilibrium centrifugation' 
_pdbx_struct_assembly_auth_evidence.details                'It runs as a monomeric form.' 
# 
_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 ILE A 28  ? HIS A 32  ? ILE A 28   HIS A 32   5 ? 5 
HELX_P HELX_P2 AA2 GLU A 62  ? LYS A 65  ? GLU A 61   LYS A 64   5 ? 4 
HELX_P HELX_P3 AA3 THR A 87  ? SER A 91  ? THR A 83   SER A 87   5 ? 5 
HELX_P HELX_P4 AA4 GLN A 213 ? LEU A 217 ? GLN A 1079 LEU A 1083 5 ? 5 
HELX_P HELX_P5 AA5 ILE B 28  ? HIS B 32  ? ILE H 28   HIS H 32   5 ? 5 
HELX_P HELX_P6 AA6 GLU B 62  ? LYS B 65  ? GLU H 61   LYS H 64   5 ? 4 
HELX_P HELX_P7 AA7 LYS B 74  ? SER B 76  ? LYS H 73   SER H 75   5 ? 3 
HELX_P HELX_P8 AA8 THR B 87  ? SER B 91  ? THR H 83   SER H 87   5 ? 5 
HELX_P HELX_P9 AA9 GLN B 213 ? LEU B 217 ? GLN H 1079 LEU H 1083 5 ? 5 
# 
_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 
disulf1 disulf ?    ? A CYS 22  SG  ? ? ? 1_555 A CYS 96  SG ? ? A CYS 22   A CYS 92   1_555 ? ? ? ? ? ? ? 2.122 ? ?               
disulf2 disulf ?    ? A CYS 157 SG  ? ? ? 1_555 A CYS 222 SG ? ? A CYS 1023 A CYS 1088 1_555 ? ? ? ? ? ? ? 2.141 ? ?               
disulf3 disulf ?    ? B CYS 22  SG  ? ? ? 1_555 B CYS 96  SG ? ? H CYS 22   H CYS 92   1_555 ? ? ? ? ? ? ? 2.102 ? ?               
disulf4 disulf ?    ? B CYS 157 SG  ? ? ? 1_555 B CYS 222 SG ? ? H CYS 1023 H CYS 1088 1_555 ? ? ? ? ? ? ? 2.149 ? ?               
covale1 covale one  ? C SER 4   OG  ? ? ? 1_555 Q A2G .   C1 ? ? M SER 4    M A2G 101  1_555 ? ? ? ? ? ? ? 1.435 ? O-Glycosylation 
covale2 covale one  ? C THR 5   OG1 ? ? ? 1_555 R A2G .   C1 ? ? M THR 5    M A2G 102  1_555 ? ? ? ? ? ? ? 1.471 ? O-Glycosylation 
covale3 covale both ? C PRO 7   C   ? ? ? 1_555 C NH2 8   N  ? ? M PRO 7    M NH2 8    1_555 ? ? ? ? ? ? ? 1.267 ? ?               
covale4 covale one  ? D SER 4   OG  ? ? ? 1_555 S A2G .   C1 ? ? N SER 4    N A2G 101  1_555 ? ? ? ? ? ? ? 1.403 ? O-Glycosylation 
covale5 covale one  ? D THR 5   OG1 ? ? ? 1_555 T A2G .   C1 ? ? N THR 5    N A2G 102  1_555 ? ? ? ? ? ? ? 1.479 ? O-Glycosylation 
covale6 covale both ? D PRO 7   C   ? ? ? 1_555 D NH2 8   N  ? ? N PRO 7    N NH2 8    1_555 ? ? ? ? ? ? ? 1.332 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NH2 C 8   ? PRO C 7   ? NH2 M 8    ? 1_555 PRO M 7    ? 1_555 .  .   PRO 13 NH2 None            'Terminal amidation' 
2  NH2 D 8   ? PRO D 7   ? NH2 N 8    ? 1_555 PRO N 7    ? 1_555 .  .   PRO 13 NH2 None            'Terminal amidation' 
3  A2G Q .   ? SER C 4   ? A2G M 101  ? 1_555 SER M 4    ? 1_555 C1 OG  SER 2  A2G O-Glycosylation Carbohydrate         
4  A2G R .   ? THR C 5   ? A2G M 102  ? 1_555 THR M 5    ? 1_555 C1 OG1 THR 3  A2G O-Glycosylation Carbohydrate         
5  A2G S .   ? SER D 4   ? A2G N 101  ? 1_555 SER N 4    ? 1_555 C1 OG  SER 2  A2G O-Glycosylation Carbohydrate         
6  A2G T .   ? THR D 5   ? A2G N 102  ? 1_555 THR N 5    ? 1_555 C1 OG1 THR 3  A2G O-Glycosylation Carbohydrate         
7  CYS A 22  ? CYS A 96  ? CYS A 22   ? 1_555 CYS A 92   ? 1_555 SG SG  .   .  .   None            'Disulfide bridge'   
8  CYS A 157 ? CYS A 222 ? CYS A 1023 ? 1_555 CYS A 1088 ? 1_555 SG SG  .   .  .   None            'Disulfide bridge'   
9  CYS B 22  ? CYS B 96  ? CYS H 22   ? 1_555 CYS H 92   ? 1_555 SG SG  .   .  .   None            'Disulfide bridge'   
10 CYS B 157 ? CYS B 222 ? CYS H 1023 ? 1_555 CYS H 1088 ? 1_555 SG SG  .   .  .   None            'Disulfide bridge'   
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 228 A . ? TYR 1094 A PRO 229 A ? PRO 1095 A 1 -2.86 
2 TYR 228 B . ? TYR 1094 H PRO 229 B ? PRO 1095 H 1 -1.64 
3 ALA 1   C . ? ALA 1    M PRO 2   C ? PRO 2    M 1 7.14  
4 ALA 1   D . ? ALA 1    N PRO 2   D ? PRO 2    N 1 -0.70 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 6 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 6 ? 
AB3 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB2 5 6 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 3   ? GLN A 6   ? GLN A 3    GLN A 6    
AA1 2 VAL A 18  ? SER A 25  ? VAL A 18   SER A 25   
AA1 3 THR A 78  ? LEU A 83  ? THR A 77   LEU A 82   
AA1 4 ALA A 68  ? ASP A 73  ? ALA A 67   ASP A 72   
AA2 1 GLU A 10  ? VAL A 12  ? GLU A 10   VAL A 12   
AA2 2 THR A 111 ? VAL A 115 ? THR A 107  VAL A 111  
AA2 3 ALA A 92  ? ARG A 98  ? ALA A 88   ARG A 94   
AA2 4 ILE A 34  ? ARG A 39  ? ILE A 34   ARG A 39   
AA2 5 LEU A 45  ? SER A 52  ? LEU A 45   SER A 52   
AA2 6 ASP A 57  A TYR A 60  ? ASP A 56   TYR A 59   
AA3 1 GLU A 10  ? VAL A 12  ? GLU A 10   VAL A 12   
AA3 2 THR A 111 ? VAL A 115 ? THR A 107  VAL A 111  
AA3 3 ALA A 92  ? ARG A 98  ? ALA A 88   ARG A 94   
AA3 4 TYR A 106 ? TRP A 107 ? TYR A 102  TRP A 103  
AA4 1 MET A 138 ? THR A 139 ? MET A 1004 THR A 1005 
AA4 2 VAL A 153 ? ALA A 159 ? VAL A 1019 ALA A 1025 
AA4 3 ASP A 204 ? ILE A 209 ? ASP A 1070 ILE A 1075 
AA4 4 PHE A 196 ? SER A 201 ? PHE A 1062 SER A 1067 
AA5 1 PHE A 144 ? THR A 147 ? PHE A 1010 THR A 1013 
AA5 2 THR A 236 ? MET A 240 ? THR A 1102 MET A 1106 
AA5 3 ALA A 218 ? GLN A 224 ? ALA A 1084 GLN A 1090 
AA5 4 VAL A 167 ? GLN A 172 ? VAL A 1033 GLN A 1038 
AA5 5 LYS A 179 ? TYR A 183 ? LYS A 1045 TYR A 1049 
AA5 6 THR A 187 ? ARG A 188 ? THR A 1053 ARG A 1054 
AA6 1 PHE A 144 ? THR A 147 ? PHE A 1010 THR A 1013 
AA6 2 THR A 236 ? MET A 240 ? THR A 1102 MET A 1106 
AA6 3 ALA A 218 ? GLN A 224 ? ALA A 1084 GLN A 1090 
AA6 4 THR A 231 ? PHE A 232 ? THR A 1097 PHE A 1098 
AA7 1 GLN B 3   ? GLN B 6   ? GLN H 3    GLN H 6    
AA7 2 VAL B 18  ? SER B 25  ? VAL H 18   SER H 25   
AA7 3 THR B 78  ? LEU B 83  ? THR H 77   LEU H 82   
AA7 4 ALA B 68  ? ASP B 73  ? ALA H 67   ASP H 72   
AA8 1 GLU B 10  ? VAL B 12  ? GLU H 10   VAL H 12   
AA8 2 THR B 111 ? VAL B 115 ? THR H 107  VAL H 111  
AA8 3 ALA B 92  ? ARG B 98  ? ALA H 88   ARG H 94   
AA8 4 ILE B 34  ? ARG B 39  ? ILE H 34   ARG H 39   
AA8 5 LEU B 45  ? SER B 52  ? LEU H 45   SER H 52   
AA8 6 ASP B 57  A TYR B 60  ? ASP H 56   TYR H 59   
AA9 1 GLU B 10  ? VAL B 12  ? GLU H 10   VAL H 12   
AA9 2 THR B 111 ? VAL B 115 ? THR H 107  VAL H 111  
AA9 3 ALA B 92  ? ARG B 98  ? ALA H 88   ARG H 94   
AA9 4 TYR B 106 ? TRP B 107 ? TYR H 102  TRP H 103  
AB1 1 MET B 138 ? THR B 139 ? MET H 1004 THR H 1005 
AB1 2 VAL B 153 ? ALA B 159 ? VAL H 1019 ALA H 1025 
AB1 3 ASP B 204 ? ILE B 209 ? ASP H 1070 ILE H 1075 
AB1 4 PHE B 196 ? SER B 201 ? PHE H 1062 SER H 1067 
AB2 1 PHE B 144 ? THR B 147 ? PHE H 1010 THR H 1013 
AB2 2 THR B 236 ? MET B 240 ? THR H 1102 MET H 1106 
AB2 3 ALA B 218 ? GLN B 224 ? ALA H 1084 GLN H 1090 
AB2 4 VAL B 167 ? GLN B 172 ? VAL H 1033 GLN H 1038 
AB2 5 LYS B 179 ? TYR B 183 ? LYS H 1045 TYR H 1049 
AB2 6 THR B 187 ? ARG B 188 ? THR H 1053 ARG H 1054 
AB3 1 PHE B 144 ? THR B 147 ? PHE H 1010 THR H 1013 
AB3 2 THR B 236 ? MET B 240 ? THR H 1102 MET H 1106 
AB3 3 ALA B 218 ? GLN B 224 ? ALA H 1084 GLN H 1090 
AB3 4 THR B 231 ? PHE B 232 ? THR H 1097 PHE H 1098 
# 
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 GLN A 5   ? N GLN A 5    O LYS A 23  ? O LYS A 23   
AA1 2 3 N ILE A 20  ? N ILE A 20   O MET A 81  ? O MET A 80   
AA1 3 4 O THR A 78  ? O THR A 77   N ASP A 73  ? N ASP A 72   
AA2 1 2 N GLU A 10  ? N GLU A 10   O THR A 114 ? O THR A 110  
AA2 2 3 O LEU A 113 ? O LEU A 109  N ALA A 92  ? N ALA A 88   
AA2 3 4 O VAL A 93  ? O VAL A 89   N ARG A 39  ? N ARG A 39   
AA2 4 5 N TRP A 36  ? N TRP A 36   O ILE A 48  ? O ILE A 48   
AA2 5 6 N SER A 52  ? N SER A 52   O ASP A 57  A O ASP A 56   
AA3 1 2 N GLU A 10  ? N GLU A 10   O THR A 114 ? O THR A 110  
AA3 2 3 O LEU A 113 ? O LEU A 109  N ALA A 92  ? N ALA A 88   
AA3 3 4 N ARG A 98  ? N ARG A 94   O TYR A 106 ? O TYR A 102  
AA4 1 2 N THR A 139 ? N THR A 1005 O LYS A 158 ? O LYS A 1024 
AA4 2 3 N CYS A 157 ? N CYS A 1023 O PHE A 205 ? O PHE A 1071 
AA4 3 4 O THR A 208 ? O THR A 1074 N THR A 197 ? N THR A 1063 
AA5 1 2 N MET A 145 ? N MET A 1011 O GLU A 239 ? O GLU A 1105 
AA5 2 3 O LEU A 238 ? O LEU A 1104 N ALA A 218 ? N ALA A 1084 
AA5 3 4 O ASP A 219 ? O ASP A 1085 N GLN A 172 ? N GLN A 1038 
AA5 4 5 N TRP A 169 ? N TRP A 1035 O LEU A 181 ? O LEU A 1047 
AA5 5 6 N TYR A 183 ? N TYR A 1049 O THR A 187 ? O THR A 1053 
AA6 1 2 N MET A 145 ? N MET A 1011 O GLU A 239 ? O GLU A 1105 
AA6 2 3 O LEU A 238 ? O LEU A 1104 N ALA A 218 ? N ALA A 1084 
AA6 3 4 N GLN A 224 ? N GLN A 1090 O THR A 231 ? O THR A 1097 
AA7 1 2 N GLN B 5   ? N GLN H 5    O LYS B 23  ? O LYS H 23   
AA7 2 3 N ILE B 20  ? N ILE H 20   O MET B 81  ? O MET H 80   
AA7 3 4 O THR B 78  ? O THR H 77   N ASP B 73  ? N ASP H 72   
AA8 1 2 N GLU B 10  ? N GLU H 10   O THR B 114 ? O THR H 110  
AA8 2 3 O LEU B 113 ? O LEU H 109  N ALA B 92  ? N ALA H 88   
AA8 3 4 O VAL B 93  ? O VAL H 89   N ARG B 39  ? N ARG H 39   
AA8 4 5 N TRP B 36  ? N TRP H 36   O ILE B 48  ? O ILE H 48   
AA8 5 6 N SER B 52  ? N SER H 52   O ASP B 57  A O ASP H 56   
AA9 1 2 N GLU B 10  ? N GLU H 10   O THR B 114 ? O THR H 110  
AA9 2 3 O LEU B 113 ? O LEU H 109  N ALA B 92  ? N ALA H 88   
AA9 3 4 N ARG B 98  ? N ARG H 94   O TYR B 106 ? O TYR H 102  
AB1 1 2 N THR B 139 ? N THR H 1005 O LYS B 158 ? O LYS H 1024 
AB1 2 3 N ILE B 155 ? N ILE H 1021 O LEU B 207 ? O LEU H 1073 
AB1 3 4 O THR B 208 ? O THR H 1074 N THR B 197 ? N THR H 1063 
AB2 1 2 N MET B 145 ? N MET H 1011 O GLU B 239 ? O GLU H 1105 
AB2 2 3 O LEU B 238 ? O LEU H 1104 N ALA B 218 ? N ALA H 1084 
AB2 3 4 O ASP B 219 ? O ASP H 1085 N GLN B 172 ? N GLN H 1038 
AB2 4 5 N TRP B 169 ? N TRP H 1035 O LEU B 181 ? O LEU H 1047 
AB2 5 6 N TYR B 183 ? N TYR H 1049 O THR B 187 ? O THR H 1053 
AB3 1 2 N MET B 145 ? N MET H 1011 O GLU B 239 ? O GLU H 1105 
AB3 2 3 O LEU B 238 ? O LEU H 1104 N ALA B 218 ? N ALA H 1084 
AB3 3 4 N GLN B 224 ? N GLN H 1090 O THR B 231 ? O THR H 1097 
# 
_pdbx_entry_details.entry_id                   8S6K 
_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   Y 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OD1 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     72 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OD2 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    ASP 
_pdbx_validate_symm_contact.auth_seq_id_2     1070 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   1_655 
_pdbx_validate_symm_contact.dist              1.94 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CA 
_pdbx_validate_rmsd_bond.auth_asym_id_1            N 
_pdbx_validate_rmsd_bond.auth_comp_id_1            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_1             7 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            C 
_pdbx_validate_rmsd_bond.auth_asym_id_2            N 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_2             7 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.400 
_pdbx_validate_rmsd_bond.bond_target_value         1.524 
_pdbx_validate_rmsd_bond.bond_deviation            -0.124 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.020 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A THR 1013 ? ? CA A THR 1013 ? ? C  A THR 1013 ? ? 92.92 111.60 -18.68 2.70 N 
2 1 CG H LYS 93   ? ? CD H LYS 93   ? ? CE H LYS 93   ? ? 93.29 111.90 -18.61 3.00 N 
3 1 CB H THR 1013 ? ? CA H THR 1013 ? ? C  H THR 1013 ? ? 93.38 111.60 -18.22 2.70 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 PRO A 41   ? ? -36.31  124.75  
2 1 SER A 95   ? ? 71.81   -172.94 
3 1 ALA A 1051 ? ? 71.74   -38.21  
4 1 ALA A 1084 ? ? 179.80  175.73  
5 1 GLN H 43   ? ? -112.29 -148.72 
6 1 SER H 95   ? ? 68.81   -170.26 
7 1 ALA H 1051 ? ? 76.61   -37.59  
# 
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 19.5470 -6.2963 30.9222 0.0163 ? -0.0022 ? -0.0089 ? 0.0976 ? 0.0103  ? 0.0422 ? 0.2445 ? -0.1094 
? 0.0885 ? 0.3813 ? -0.0636 ? 0.6536 ? 0.0391  ? 0.0096  ? 0.0007  ? 0.0183  ? -0.0205 ? 0.0296  ? 0.0562  ? 0.0561  ? -0.0187 ? 
2 'X-RAY DIFFRACTION' ? refined -0.3958 -7.4121 24.6951 0.0124 ? -0.0295 ? 0.0108  ? 0.1034 ? -0.0166 ? 0.0372 ? 0.6960 ? 0.3446  
? 0.4813 ? 0.3947 ? -0.0171 ? 0.6446 ? -0.0120 ? -0.0572 ? -0.0541 ? -0.0493 ? 0.0425  ? -0.0530 ? 0.0348  ? -0.0957 ? -0.0306 ? 
3 'X-RAY DIFFRACTION' ? refined 12.5194 23.3694 6.0410  0.1341 ? 0.0013  ? -0.0626 ? 0.0915 ? -0.0074 ? 0.0592 ? 0.0221 ? -0.0438 
? 0.0465 ? 0.3085 ? -0.6467 ? 1.6491 ? 0.0320  ? 0.0164  ? -0.0318 ? 0.0868  ? -0.0980 ? 0.0167  ? -0.3184 ? 0.1308  ? 0.0659  ? 
4 'X-RAY DIFFRACTION' ? refined -0.7522 24.5120 22.0105 0.0707 ? 0.0164  ? -0.0371 ? 0.0689 ? -0.0142 ? 0.0263 ? 0.3533 ? -0.2410 
? 0.0104 ? 0.2747 ? 0.3491  ? 1.1580 ? 0.0185  ? -0.0297 ? 0.0225  ? -0.0504 ? -0.0157 ? -0.0115 ? -0.0977 ? -0.0924 ? -0.0027 ? 
# 
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 1   ? ? ? A 112  ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 121 ? ? ? A 1107 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? H 1   ? ? ? H 112  ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? H 122 ? ? ? H 1107 ? ? ? 
# 
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 SER 113  ? A SER 117 
2  1 Y 1 A SER 114  ? A SER 118 
3  1 Y 1 A SER 115  ? A SER 119 
4  1 Y 1 A GLY 116  ? A GLY 120 
5  1 Y 1 A GLY 117  ? A GLY 121 
6  1 Y 1 A GLY 118  ? A GLY 122 
7  1 Y 1 A GLY 119  ? A GLY 123 
8  1 Y 1 A SER 120  ? A SER 124 
9  1 Y 1 A ARG 1108 ? A ARG 242 
10 1 Y 1 A GLY 1109 ? A GLY 243 
11 1 Y 1 A GLY 1110 ? A GLY 244 
12 1 Y 1 A HIS 1111 ? A HIS 245 
13 1 Y 1 A HIS 1112 ? A HIS 246 
14 1 Y 1 A HIS 1113 ? A HIS 247 
15 1 Y 1 A HIS 1114 ? A HIS 248 
16 1 Y 1 A HIS 1115 ? A HIS 249 
17 1 Y 1 A HIS 1116 ? A HIS 250 
18 1 Y 1 H SER 113  ? B SER 117 
19 1 Y 1 H SER 114  ? B SER 118 
20 1 Y 1 H SER 115  ? B SER 119 
21 1 Y 1 H GLY 116  ? B GLY 120 
22 1 Y 1 H GLY 117  ? B GLY 121 
23 1 Y 1 H GLY 118  ? B GLY 122 
24 1 Y 1 H GLY 119  ? B GLY 123 
25 1 Y 1 H SER 120  ? B SER 124 
26 1 Y 1 H GLY 121  ? B GLY 125 
27 1 Y 1 H ARG 1108 ? B ARG 242 
28 1 Y 1 H GLY 1109 ? B GLY 243 
29 1 Y 1 H GLY 1110 ? B GLY 244 
30 1 Y 1 H HIS 1111 ? B HIS 245 
31 1 Y 1 H HIS 1112 ? B HIS 246 
32 1 Y 1 H HIS 1113 ? B HIS 247 
33 1 Y 1 H HIS 1114 ? B HIS 248 
34 1 Y 1 H HIS 1115 ? B HIS 249 
35 1 Y 1 H HIS 1116 ? B HIS 250 
# 
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 
A2G O5   O N N 1   
A2G C1   C N S 2   
A2G O1   O N N 3   
A2G C2   C N R 4   
A2G N2   N N N 5   
A2G C3   C N R 6   
A2G O3   O N N 7   
A2G C4   C N R 8   
A2G O4   O N N 9   
A2G C5   C N R 10  
A2G C6   C N N 11  
A2G O6   O N N 12  
A2G C7   C N N 13  
A2G O7   O N N 14  
A2G C8   C N N 15  
A2G H1   H N N 16  
A2G HO1  H N N 17  
A2G H2   H N N 18  
A2G HN2  H N N 19  
A2G H3   H N N 20  
A2G HO3  H N N 21  
A2G H4   H N N 22  
A2G HO4  H N N 23  
A2G H5   H N N 24  
A2G H61  H N N 25  
A2G H81  H N N 26  
A2G H82  H N N 27  
A2G H83  H N N 28  
A2G H62  H N N 29  
A2G HO6  H N N 30  
ALA N    N N N 31  
ALA CA   C N S 32  
ALA C    C N N 33  
ALA O    O N N 34  
ALA CB   C N N 35  
ALA OXT  O N N 36  
ALA H    H N N 37  
ALA H2   H N N 38  
ALA HA   H N N 39  
ALA HB1  H N N 40  
ALA HB2  H N N 41  
ALA HB3  H N N 42  
ALA HXT  H N N 43  
ARG N    N N N 44  
ARG CA   C N S 45  
ARG C    C N N 46  
ARG O    O N N 47  
ARG CB   C N N 48  
ARG CG   C N N 49  
ARG CD   C N N 50  
ARG NE   N N N 51  
ARG CZ   C N N 52  
ARG NH1  N N N 53  
ARG NH2  N N N 54  
ARG OXT  O N N 55  
ARG H    H N N 56  
ARG H2   H N N 57  
ARG HA   H N N 58  
ARG HB2  H N N 59  
ARG HB3  H N N 60  
ARG HG2  H N N 61  
ARG HG3  H N N 62  
ARG HD2  H N N 63  
ARG HD3  H N N 64  
ARG HE   H N N 65  
ARG HH11 H N N 66  
ARG HH12 H N N 67  
ARG HH21 H N N 68  
ARG HH22 H N N 69  
ARG HXT  H N N 70  
ASN N    N N N 71  
ASN CA   C N S 72  
ASN C    C N N 73  
ASN O    O N N 74  
ASN CB   C N N 75  
ASN CG   C N N 76  
ASN OD1  O N N 77  
ASN ND2  N N N 78  
ASN OXT  O N N 79  
ASN H    H N N 80  
ASN H2   H N N 81  
ASN HA   H N N 82  
ASN HB2  H N N 83  
ASN HB3  H N N 84  
ASN HD21 H N N 85  
ASN HD22 H N N 86  
ASN HXT  H N N 87  
ASP N    N N N 88  
ASP CA   C N S 89  
ASP C    C N N 90  
ASP O    O N N 91  
ASP CB   C N N 92  
ASP CG   C N N 93  
ASP OD1  O N N 94  
ASP OD2  O N N 95  
ASP OXT  O N N 96  
ASP H    H N N 97  
ASP H2   H N N 98  
ASP HA   H N N 99  
ASP HB2  H N N 100 
ASP HB3  H N N 101 
ASP HD2  H N N 102 
ASP HXT  H N N 103 
CYS N    N N N 104 
CYS CA   C N R 105 
CYS C    C N N 106 
CYS O    O N N 107 
CYS CB   C N N 108 
CYS SG   S N N 109 
CYS OXT  O N N 110 
CYS H    H N N 111 
CYS H2   H N N 112 
CYS HA   H N N 113 
CYS HB2  H N N 114 
CYS HB3  H N N 115 
CYS HG   H N N 116 
CYS HXT  H N N 117 
EDO C1   C N N 118 
EDO O1   O N N 119 
EDO C2   C N N 120 
EDO O2   O N N 121 
EDO H11  H N N 122 
EDO H12  H N N 123 
EDO HO1  H N N 124 
EDO H21  H N N 125 
EDO H22  H N N 126 
EDO HO2  H N N 127 
GLN N    N N N 128 
GLN CA   C N S 129 
GLN C    C N N 130 
GLN O    O N N 131 
GLN CB   C N N 132 
GLN CG   C N N 133 
GLN CD   C N N 134 
GLN OE1  O N N 135 
GLN NE2  N N N 136 
GLN OXT  O N N 137 
GLN H    H N N 138 
GLN H2   H N N 139 
GLN HA   H N N 140 
GLN HB2  H N N 141 
GLN HB3  H N N 142 
GLN HG2  H N N 143 
GLN HG3  H N N 144 
GLN HE21 H N N 145 
GLN HE22 H N N 146 
GLN HXT  H N N 147 
GLU N    N N N 148 
GLU CA   C N S 149 
GLU C    C N N 150 
GLU O    O N N 151 
GLU CB   C N N 152 
GLU CG   C N N 153 
GLU CD   C N N 154 
GLU OE1  O N N 155 
GLU OE2  O N N 156 
GLU OXT  O N N 157 
GLU H    H N N 158 
GLU H2   H N N 159 
GLU HA   H N N 160 
GLU HB2  H N N 161 
GLU HB3  H N N 162 
GLU HG2  H N N 163 
GLU HG3  H N N 164 
GLU HE2  H N N 165 
GLU HXT  H N N 166 
GLY N    N N N 167 
GLY CA   C N N 168 
GLY C    C N N 169 
GLY O    O N N 170 
GLY OXT  O N N 171 
GLY H    H N N 172 
GLY H2   H N N 173 
GLY HA2  H N N 174 
GLY HA3  H N N 175 
GLY HXT  H N N 176 
HIS N    N N N 177 
HIS CA   C N S 178 
HIS C    C N N 179 
HIS O    O N N 180 
HIS CB   C N N 181 
HIS CG   C Y N 182 
HIS ND1  N Y N 183 
HIS CD2  C Y N 184 
HIS CE1  C Y N 185 
HIS NE2  N Y N 186 
HIS OXT  O N N 187 
HIS H    H N N 188 
HIS H2   H N N 189 
HIS HA   H N N 190 
HIS HB2  H N N 191 
HIS HB3  H N N 192 
HIS HD1  H N N 193 
HIS HD2  H N N 194 
HIS HE1  H N N 195 
HIS HE2  H N N 196 
HIS HXT  H N N 197 
HOH O    O N N 198 
HOH H1   H N N 199 
HOH H2   H N N 200 
ILE N    N N N 201 
ILE CA   C N S 202 
ILE C    C N N 203 
ILE O    O N N 204 
ILE CB   C N S 205 
ILE CG1  C N N 206 
ILE CG2  C N N 207 
ILE CD1  C N N 208 
ILE OXT  O N N 209 
ILE H    H N N 210 
ILE H2   H N N 211 
ILE HA   H N N 212 
ILE HB   H N N 213 
ILE HG12 H N N 214 
ILE HG13 H N N 215 
ILE HG21 H N N 216 
ILE HG22 H N N 217 
ILE HG23 H N N 218 
ILE HD11 H N N 219 
ILE HD12 H N N 220 
ILE HD13 H N N 221 
ILE HXT  H N N 222 
LEU N    N N N 223 
LEU CA   C N S 224 
LEU C    C N N 225 
LEU O    O N N 226 
LEU CB   C N N 227 
LEU CG   C N N 228 
LEU CD1  C N N 229 
LEU CD2  C N N 230 
LEU OXT  O N N 231 
LEU H    H N N 232 
LEU H2   H N N 233 
LEU HA   H N N 234 
LEU HB2  H N N 235 
LEU HB3  H N N 236 
LEU HG   H N N 237 
LEU HD11 H N N 238 
LEU HD12 H N N 239 
LEU HD13 H N N 240 
LEU HD21 H N N 241 
LEU HD22 H N N 242 
LEU HD23 H N N 243 
LEU HXT  H N N 244 
LYS N    N N N 245 
LYS CA   C N S 246 
LYS C    C N N 247 
LYS O    O N N 248 
LYS CB   C N N 249 
LYS CG   C N N 250 
LYS CD   C N N 251 
LYS CE   C N N 252 
LYS NZ   N N N 253 
LYS OXT  O N N 254 
LYS H    H N N 255 
LYS H2   H N N 256 
LYS HA   H N N 257 
LYS HB2  H N N 258 
LYS HB3  H N N 259 
LYS HG2  H N N 260 
LYS HG3  H N N 261 
LYS HD2  H N N 262 
LYS HD3  H N N 263 
LYS HE2  H N N 264 
LYS HE3  H N N 265 
LYS HZ1  H N N 266 
LYS HZ2  H N N 267 
LYS HZ3  H N N 268 
LYS HXT  H N N 269 
MET N    N N N 270 
MET CA   C N S 271 
MET C    C N N 272 
MET O    O N N 273 
MET CB   C N N 274 
MET CG   C N N 275 
MET SD   S N N 276 
MET CE   C N N 277 
MET OXT  O N N 278 
MET H    H N N 279 
MET H2   H N N 280 
MET HA   H N N 281 
MET HB2  H N N 282 
MET HB3  H N N 283 
MET HG2  H N N 284 
MET HG3  H N N 285 
MET HE1  H N N 286 
MET HE2  H N N 287 
MET HE3  H N N 288 
MET HXT  H N N 289 
NH2 N    N N N 290 
NH2 HN1  H N N 291 
NH2 HN2  H N N 292 
PHE N    N N N 293 
PHE CA   C N S 294 
PHE C    C N N 295 
PHE O    O N N 296 
PHE CB   C N N 297 
PHE CG   C Y N 298 
PHE CD1  C Y N 299 
PHE CD2  C Y N 300 
PHE CE1  C Y N 301 
PHE CE2  C Y N 302 
PHE CZ   C Y N 303 
PHE OXT  O N N 304 
PHE H    H N N 305 
PHE H2   H N N 306 
PHE HA   H N N 307 
PHE HB2  H N N 308 
PHE HB3  H N N 309 
PHE HD1  H N N 310 
PHE HD2  H N N 311 
PHE HE1  H N N 312 
PHE HE2  H N N 313 
PHE HZ   H N N 314 
PHE HXT  H N N 315 
PRO N    N N N 316 
PRO CA   C N S 317 
PRO C    C N N 318 
PRO O    O N N 319 
PRO CB   C N N 320 
PRO CG   C N N 321 
PRO CD   C N N 322 
PRO OXT  O N N 323 
PRO H    H N N 324 
PRO HA   H N N 325 
PRO HB2  H N N 326 
PRO HB3  H N N 327 
PRO HG2  H N N 328 
PRO HG3  H N N 329 
PRO HD2  H N N 330 
PRO HD3  H N N 331 
PRO HXT  H N N 332 
SER N    N N N 333 
SER CA   C N S 334 
SER C    C N N 335 
SER O    O N N 336 
SER CB   C N N 337 
SER OG   O N N 338 
SER OXT  O N N 339 
SER H    H N N 340 
SER H2   H N N 341 
SER HA   H N N 342 
SER HB2  H N N 343 
SER HB3  H N N 344 
SER HG   H N N 345 
SER HXT  H N N 346 
THR N    N N N 347 
THR CA   C N S 348 
THR C    C N N 349 
THR O    O N N 350 
THR CB   C N R 351 
THR OG1  O N N 352 
THR CG2  C N N 353 
THR OXT  O N N 354 
THR H    H N N 355 
THR H2   H N N 356 
THR HA   H N N 357 
THR HB   H N N 358 
THR HG1  H N N 359 
THR HG21 H N N 360 
THR HG22 H N N 361 
THR HG23 H N N 362 
THR HXT  H N N 363 
TRP N    N N N 364 
TRP CA   C N S 365 
TRP C    C N N 366 
TRP O    O N N 367 
TRP CB   C N N 368 
TRP CG   C Y N 369 
TRP CD1  C Y N 370 
TRP CD2  C Y N 371 
TRP NE1  N Y N 372 
TRP CE2  C Y N 373 
TRP CE3  C Y N 374 
TRP CZ2  C Y N 375 
TRP CZ3  C Y N 376 
TRP CH2  C Y N 377 
TRP OXT  O N N 378 
TRP H    H N N 379 
TRP H2   H N N 380 
TRP HA   H N N 381 
TRP HB2  H N N 382 
TRP HB3  H N N 383 
TRP HD1  H N N 384 
TRP HE1  H N N 385 
TRP HE3  H N N 386 
TRP HZ2  H N N 387 
TRP HZ3  H N N 388 
TRP HH2  H N N 389 
TRP HXT  H N N 390 
TYR N    N N N 391 
TYR CA   C N S 392 
TYR C    C N N 393 
TYR O    O N N 394 
TYR CB   C N N 395 
TYR CG   C Y N 396 
TYR CD1  C Y N 397 
TYR CD2  C Y N 398 
TYR CE1  C Y N 399 
TYR CE2  C Y N 400 
TYR CZ   C Y N 401 
TYR OH   O N N 402 
TYR OXT  O N N 403 
TYR H    H N N 404 
TYR H2   H N N 405 
TYR HA   H N N 406 
TYR HB2  H N N 407 
TYR HB3  H N N 408 
TYR HD1  H N N 409 
TYR HD2  H N N 410 
TYR HE1  H N N 411 
TYR HE2  H N N 412 
TYR HH   H N N 413 
TYR HXT  H N N 414 
VAL N    N N N 415 
VAL CA   C N S 416 
VAL C    C N N 417 
VAL O    O N N 418 
VAL CB   C N N 419 
VAL CG1  C N N 420 
VAL CG2  C N N 421 
VAL OXT  O N N 422 
VAL H    H N N 423 
VAL H2   H N N 424 
VAL HA   H N N 425 
VAL HB   H N N 426 
VAL HG11 H N N 427 
VAL HG12 H N N 428 
VAL HG13 H N N 429 
VAL HG21 H N N 430 
VAL HG22 H N N 431 
VAL HG23 H N N 432 
VAL HXT  H N N 433 
# 
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 
A2G O5  C5   sing N N 1   
A2G C1  O5   sing N N 2   
A2G C1  C2   sing N N 3   
A2G C1  H1   sing N N 4   
A2G O1  C1   sing N N 5   
A2G O1  HO1  sing N N 6   
A2G C2  C3   sing N N 7   
A2G C2  H2   sing N N 8   
A2G N2  C2   sing N N 9   
A2G N2  HN2  sing N N 10  
A2G C3  C4   sing N N 11  
A2G C3  O3   sing N N 12  
A2G C3  H3   sing N N 13  
A2G O3  HO3  sing N N 14  
A2G C4  O4   sing N N 15  
A2G C4  H4   sing N N 16  
A2G O4  HO4  sing N N 17  
A2G C5  C4   sing N N 18  
A2G C5  C6   sing N N 19  
A2G C5  H5   sing N N 20  
A2G C6  O6   sing N N 21  
A2G C6  H61  sing N N 22  
A2G C7  N2   sing N N 23  
A2G O7  C7   doub N N 24  
A2G C8  C7   sing N N 25  
A2G C8  H81  sing N N 26  
A2G C8  H82  sing N N 27  
A2G C8  H83  sing N N 28  
A2G C6  H62  sing N N 29  
A2G O6  HO6  sing N N 30  
ALA N   CA   sing N N 31  
ALA N   H    sing N N 32  
ALA N   H2   sing N N 33  
ALA CA  C    sing N N 34  
ALA CA  CB   sing N N 35  
ALA CA  HA   sing N N 36  
ALA C   O    doub N N 37  
ALA C   OXT  sing N N 38  
ALA CB  HB1  sing N N 39  
ALA CB  HB2  sing N N 40  
ALA CB  HB3  sing N N 41  
ALA OXT HXT  sing N N 42  
ARG N   CA   sing N N 43  
ARG N   H    sing N N 44  
ARG N   H2   sing N N 45  
ARG CA  C    sing N N 46  
ARG CA  CB   sing N N 47  
ARG CA  HA   sing N N 48  
ARG C   O    doub N N 49  
ARG C   OXT  sing N N 50  
ARG CB  CG   sing N N 51  
ARG CB  HB2  sing N N 52  
ARG CB  HB3  sing N N 53  
ARG CG  CD   sing N N 54  
ARG CG  HG2  sing N N 55  
ARG CG  HG3  sing N N 56  
ARG CD  NE   sing N N 57  
ARG CD  HD2  sing N N 58  
ARG CD  HD3  sing N N 59  
ARG NE  CZ   sing N N 60  
ARG NE  HE   sing N N 61  
ARG CZ  NH1  sing N N 62  
ARG CZ  NH2  doub N N 63  
ARG NH1 HH11 sing N N 64  
ARG NH1 HH12 sing N N 65  
ARG NH2 HH21 sing N N 66  
ARG NH2 HH22 sing N N 67  
ARG OXT HXT  sing N N 68  
ASN N   CA   sing N N 69  
ASN N   H    sing N N 70  
ASN N   H2   sing N N 71  
ASN CA  C    sing N N 72  
ASN CA  CB   sing N N 73  
ASN CA  HA   sing N N 74  
ASN C   O    doub N N 75  
ASN C   OXT  sing N N 76  
ASN CB  CG   sing N N 77  
ASN CB  HB2  sing N N 78  
ASN CB  HB3  sing N N 79  
ASN CG  OD1  doub N N 80  
ASN CG  ND2  sing N N 81  
ASN ND2 HD21 sing N N 82  
ASN ND2 HD22 sing N N 83  
ASN OXT HXT  sing N N 84  
ASP N   CA   sing N N 85  
ASP N   H    sing N N 86  
ASP N   H2   sing N N 87  
ASP CA  C    sing N N 88  
ASP CA  CB   sing N N 89  
ASP CA  HA   sing N N 90  
ASP C   O    doub N N 91  
ASP C   OXT  sing N N 92  
ASP CB  CG   sing N N 93  
ASP CB  HB2  sing N N 94  
ASP CB  HB3  sing N N 95  
ASP CG  OD1  doub N N 96  
ASP CG  OD2  sing N N 97  
ASP OD2 HD2  sing N N 98  
ASP OXT HXT  sing N N 99  
CYS N   CA   sing N N 100 
CYS N   H    sing N N 101 
CYS N   H2   sing N N 102 
CYS CA  C    sing N N 103 
CYS CA  CB   sing N N 104 
CYS CA  HA   sing N N 105 
CYS C   O    doub N N 106 
CYS C   OXT  sing N N 107 
CYS CB  SG   sing N N 108 
CYS CB  HB2  sing N N 109 
CYS CB  HB3  sing N N 110 
CYS SG  HG   sing N N 111 
CYS OXT HXT  sing N N 112 
EDO C1  O1   sing N N 113 
EDO C1  C2   sing N N 114 
EDO C1  H11  sing N N 115 
EDO C1  H12  sing N N 116 
EDO O1  HO1  sing N N 117 
EDO C2  O2   sing N N 118 
EDO C2  H21  sing N N 119 
EDO C2  H22  sing N N 120 
EDO O2  HO2  sing N N 121 
GLN N   CA   sing N N 122 
GLN N   H    sing N N 123 
GLN N   H2   sing N N 124 
GLN CA  C    sing N N 125 
GLN CA  CB   sing N N 126 
GLN CA  HA   sing N N 127 
GLN C   O    doub N N 128 
GLN C   OXT  sing N N 129 
GLN CB  CG   sing N N 130 
GLN CB  HB2  sing N N 131 
GLN CB  HB3  sing N N 132 
GLN CG  CD   sing N N 133 
GLN CG  HG2  sing N N 134 
GLN CG  HG3  sing N N 135 
GLN CD  OE1  doub N N 136 
GLN CD  NE2  sing N N 137 
GLN NE2 HE21 sing N N 138 
GLN NE2 HE22 sing N N 139 
GLN OXT HXT  sing N N 140 
GLU N   CA   sing N N 141 
GLU N   H    sing N N 142 
GLU N   H2   sing N N 143 
GLU CA  C    sing N N 144 
GLU CA  CB   sing N N 145 
GLU CA  HA   sing N N 146 
GLU C   O    doub N N 147 
GLU C   OXT  sing N N 148 
GLU CB  CG   sing N N 149 
GLU CB  HB2  sing N N 150 
GLU CB  HB3  sing N N 151 
GLU CG  CD   sing N N 152 
GLU CG  HG2  sing N N 153 
GLU CG  HG3  sing N N 154 
GLU CD  OE1  doub N N 155 
GLU CD  OE2  sing N N 156 
GLU OE2 HE2  sing N N 157 
GLU OXT HXT  sing N N 158 
GLY N   CA   sing N N 159 
GLY N   H    sing N N 160 
GLY N   H2   sing N N 161 
GLY CA  C    sing N N 162 
GLY CA  HA2  sing N N 163 
GLY CA  HA3  sing N N 164 
GLY C   O    doub N N 165 
GLY C   OXT  sing N N 166 
GLY OXT HXT  sing N N 167 
HIS N   CA   sing N N 168 
HIS N   H    sing N N 169 
HIS N   H2   sing N N 170 
HIS CA  C    sing N N 171 
HIS CA  CB   sing N N 172 
HIS CA  HA   sing N N 173 
HIS C   O    doub N N 174 
HIS C   OXT  sing N N 175 
HIS CB  CG   sing N N 176 
HIS CB  HB2  sing N N 177 
HIS CB  HB3  sing N N 178 
HIS CG  ND1  sing Y N 179 
HIS CG  CD2  doub Y N 180 
HIS ND1 CE1  doub Y N 181 
HIS ND1 HD1  sing N N 182 
HIS CD2 NE2  sing Y N 183 
HIS CD2 HD2  sing N N 184 
HIS CE1 NE2  sing Y N 185 
HIS CE1 HE1  sing N N 186 
HIS NE2 HE2  sing N N 187 
HIS OXT HXT  sing N N 188 
HOH O   H1   sing N N 189 
HOH O   H2   sing N N 190 
ILE N   CA   sing N N 191 
ILE N   H    sing N N 192 
ILE N   H2   sing N N 193 
ILE CA  C    sing N N 194 
ILE CA  CB   sing N N 195 
ILE CA  HA   sing N N 196 
ILE C   O    doub N N 197 
ILE C   OXT  sing N N 198 
ILE CB  CG1  sing N N 199 
ILE CB  CG2  sing N N 200 
ILE CB  HB   sing N N 201 
ILE CG1 CD1  sing N N 202 
ILE CG1 HG12 sing N N 203 
ILE CG1 HG13 sing N N 204 
ILE CG2 HG21 sing N N 205 
ILE CG2 HG22 sing N N 206 
ILE CG2 HG23 sing N N 207 
ILE CD1 HD11 sing N N 208 
ILE CD1 HD12 sing N N 209 
ILE CD1 HD13 sing N N 210 
ILE OXT HXT  sing N N 211 
LEU N   CA   sing N N 212 
LEU N   H    sing N N 213 
LEU N   H2   sing N N 214 
LEU CA  C    sing N N 215 
LEU CA  CB   sing N N 216 
LEU CA  HA   sing N N 217 
LEU C   O    doub N N 218 
LEU C   OXT  sing N N 219 
LEU CB  CG   sing N N 220 
LEU CB  HB2  sing N N 221 
LEU CB  HB3  sing N N 222 
LEU CG  CD1  sing N N 223 
LEU CG  CD2  sing N N 224 
LEU CG  HG   sing N N 225 
LEU CD1 HD11 sing N N 226 
LEU CD1 HD12 sing N N 227 
LEU CD1 HD13 sing N N 228 
LEU CD2 HD21 sing N N 229 
LEU CD2 HD22 sing N N 230 
LEU CD2 HD23 sing N N 231 
LEU OXT HXT  sing N N 232 
LYS N   CA   sing N N 233 
LYS N   H    sing N N 234 
LYS N   H2   sing N N 235 
LYS CA  C    sing N N 236 
LYS CA  CB   sing N N 237 
LYS CA  HA   sing N N 238 
LYS C   O    doub N N 239 
LYS C   OXT  sing N N 240 
LYS CB  CG   sing N N 241 
LYS CB  HB2  sing N N 242 
LYS CB  HB3  sing N N 243 
LYS CG  CD   sing N N 244 
LYS CG  HG2  sing N N 245 
LYS CG  HG3  sing N N 246 
LYS CD  CE   sing N N 247 
LYS CD  HD2  sing N N 248 
LYS CD  HD3  sing N N 249 
LYS CE  NZ   sing N N 250 
LYS CE  HE2  sing N N 251 
LYS CE  HE3  sing N N 252 
LYS NZ  HZ1  sing N N 253 
LYS NZ  HZ2  sing N N 254 
LYS NZ  HZ3  sing N N 255 
LYS OXT HXT  sing N N 256 
MET N   CA   sing N N 257 
MET N   H    sing N N 258 
MET N   H2   sing N N 259 
MET CA  C    sing N N 260 
MET CA  CB   sing N N 261 
MET CA  HA   sing N N 262 
MET C   O    doub N N 263 
MET C   OXT  sing N N 264 
MET CB  CG   sing N N 265 
MET CB  HB2  sing N N 266 
MET CB  HB3  sing N N 267 
MET CG  SD   sing N N 268 
MET CG  HG2  sing N N 269 
MET CG  HG3  sing N N 270 
MET SD  CE   sing N N 271 
MET CE  HE1  sing N N 272 
MET CE  HE2  sing N N 273 
MET CE  HE3  sing N N 274 
MET OXT HXT  sing N N 275 
NH2 N   HN1  sing N N 276 
NH2 N   HN2  sing N N 277 
PHE N   CA   sing N N 278 
PHE N   H    sing N N 279 
PHE N   H2   sing N N 280 
PHE CA  C    sing N N 281 
PHE CA  CB   sing N N 282 
PHE CA  HA   sing N N 283 
PHE C   O    doub N N 284 
PHE C   OXT  sing N N 285 
PHE CB  CG   sing N N 286 
PHE CB  HB2  sing N N 287 
PHE CB  HB3  sing N N 288 
PHE CG  CD1  doub Y N 289 
PHE CG  CD2  sing Y N 290 
PHE CD1 CE1  sing Y N 291 
PHE CD1 HD1  sing N N 292 
PHE CD2 CE2  doub Y N 293 
PHE CD2 HD2  sing N N 294 
PHE CE1 CZ   doub Y N 295 
PHE CE1 HE1  sing N N 296 
PHE CE2 CZ   sing Y N 297 
PHE CE2 HE2  sing N N 298 
PHE CZ  HZ   sing N N 299 
PHE OXT HXT  sing N N 300 
PRO N   CA   sing N N 301 
PRO N   CD   sing N N 302 
PRO N   H    sing N N 303 
PRO CA  C    sing N N 304 
PRO CA  CB   sing N N 305 
PRO CA  HA   sing N N 306 
PRO C   O    doub N N 307 
PRO C   OXT  sing N N 308 
PRO CB  CG   sing N N 309 
PRO CB  HB2  sing N N 310 
PRO CB  HB3  sing N N 311 
PRO CG  CD   sing N N 312 
PRO CG  HG2  sing N N 313 
PRO CG  HG3  sing N N 314 
PRO CD  HD2  sing N N 315 
PRO CD  HD3  sing N N 316 
PRO OXT HXT  sing N N 317 
SER N   CA   sing N N 318 
SER N   H    sing N N 319 
SER N   H2   sing N N 320 
SER CA  C    sing N N 321 
SER CA  CB   sing N N 322 
SER CA  HA   sing N N 323 
SER C   O    doub N N 324 
SER C   OXT  sing N N 325 
SER CB  OG   sing N N 326 
SER CB  HB2  sing N N 327 
SER CB  HB3  sing N N 328 
SER OG  HG   sing N N 329 
SER OXT HXT  sing N N 330 
THR N   CA   sing N N 331 
THR N   H    sing N N 332 
THR N   H2   sing N N 333 
THR CA  C    sing N N 334 
THR CA  CB   sing N N 335 
THR CA  HA   sing N N 336 
THR C   O    doub N N 337 
THR C   OXT  sing N N 338 
THR CB  OG1  sing N N 339 
THR CB  CG2  sing N N 340 
THR CB  HB   sing N N 341 
THR OG1 HG1  sing N N 342 
THR CG2 HG21 sing N N 343 
THR CG2 HG22 sing N N 344 
THR CG2 HG23 sing N N 345 
THR OXT HXT  sing N N 346 
TRP N   CA   sing N N 347 
TRP N   H    sing N N 348 
TRP N   H2   sing N N 349 
TRP CA  C    sing N N 350 
TRP CA  CB   sing N N 351 
TRP CA  HA   sing N N 352 
TRP C   O    doub N N 353 
TRP C   OXT  sing N N 354 
TRP CB  CG   sing N N 355 
TRP CB  HB2  sing N N 356 
TRP CB  HB3  sing N N 357 
TRP CG  CD1  doub Y N 358 
TRP CG  CD2  sing Y N 359 
TRP CD1 NE1  sing Y N 360 
TRP CD1 HD1  sing N N 361 
TRP CD2 CE2  doub Y N 362 
TRP CD2 CE3  sing Y N 363 
TRP NE1 CE2  sing Y N 364 
TRP NE1 HE1  sing N N 365 
TRP CE2 CZ2  sing Y N 366 
TRP CE3 CZ3  doub Y N 367 
TRP CE3 HE3  sing N N 368 
TRP CZ2 CH2  doub Y N 369 
TRP CZ2 HZ2  sing N N 370 
TRP CZ3 CH2  sing Y N 371 
TRP CZ3 HZ3  sing N N 372 
TRP CH2 HH2  sing N N 373 
TRP OXT HXT  sing N N 374 
TYR N   CA   sing N N 375 
TYR N   H    sing N N 376 
TYR N   H2   sing N N 377 
TYR CA  C    sing N N 378 
TYR CA  CB   sing N N 379 
TYR CA  HA   sing N N 380 
TYR C   O    doub N N 381 
TYR C   OXT  sing N N 382 
TYR CB  CG   sing N N 383 
TYR CB  HB2  sing N N 384 
TYR CB  HB3  sing N N 385 
TYR CG  CD1  doub Y N 386 
TYR CG  CD2  sing Y N 387 
TYR CD1 CE1  sing Y N 388 
TYR CD1 HD1  sing N N 389 
TYR CD2 CE2  doub Y N 390 
TYR CD2 HD2  sing N N 391 
TYR CE1 CZ   doub Y N 392 
TYR CE1 HE1  sing N N 393 
TYR CE2 CZ   sing Y N 394 
TYR CE2 HE2  sing N N 395 
TYR CZ  OH   sing N N 396 
TYR OH  HH   sing N N 397 
TYR OXT HXT  sing N N 398 
VAL N   CA   sing N N 399 
VAL N   H    sing N N 400 
VAL N   H2   sing N N 401 
VAL CA  C    sing N N 402 
VAL CA  CB   sing N N 403 
VAL CA  HA   sing N N 404 
VAL C   O    doub N N 405 
VAL C   OXT  sing N N 406 
VAL CB  CG1  sing N N 407 
VAL CB  CG2  sing N N 408 
VAL CB  HB   sing N N 409 
VAL CG1 HG11 sing N N 410 
VAL CG1 HG12 sing N N 411 
VAL CG1 HG13 sing N N 412 
VAL CG2 HG21 sing N N 413 
VAL CG2 HG22 sing N N 414 
VAL CG2 HG23 sing N N 415 
VAL OXT HXT  sing N N 416 
# 
_pdbx_audit_support.funding_organization   'Ministerio de Ciencia e Innovacion (MCIN)' 
_pdbx_audit_support.country                Spain 
_pdbx_audit_support.grant_number           PID2022-136362NB-I00 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      SwissModel 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8S6K 
_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]   0.021743 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005015 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014354 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.011747 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLN A 1 1   ? 21.195  -5.000  10.824  1.00 42.41 ? 1    GLN A N   1 
ATOM   2    C CA  . GLN A 1 1   ? 22.526  -4.468  11.226  1.00 38.89 ? 1    GLN A CA  1 
ATOM   3    C C   . GLN A 1 1   ? 22.469  -3.945  12.678  1.00 31.56 ? 1    GLN A C   1 
ATOM   4    O O   . GLN A 1 1   ? 23.492  -4.145  13.303  1.00 29.41 ? 1    GLN A O   1 
ATOM   5    C CB  . GLN A 1 1   ? 23.099  -3.499  10.180  1.00 43.02 ? 1    GLN A CB  1 
ATOM   6    C CG  . GLN A 1 1   ? 23.830  -2.283  10.745  1.00 46.48 ? 1    GLN A CG  1 
ATOM   7    C CD  . GLN A 1 1   ? 24.751  -1.614  9.748   1.00 53.48 ? 1    GLN A CD  1 
ATOM   8    O OE1 . GLN A 1 1   ? 24.693  -1.835  8.536   1.00 59.70 ? 1    GLN A OE1 1 
ATOM   9    N NE2 . GLN A 1 1   ? 25.641  -0.787  10.262  1.00 56.13 ? 1    GLN A NE2 1 
ATOM   10   N N   . VAL A 1 2   ? 21.346  -3.456  13.255  1.00 26.31 ? 2    VAL A N   1 
ATOM   11   C CA  . VAL A 1 2   ? 21.230  -3.408  14.744  1.00 23.34 ? 2    VAL A CA  1 
ATOM   12   C C   . VAL A 1 2   ? 21.259  -4.846  15.273  1.00 22.00 ? 2    VAL A C   1 
ATOM   13   O O   . VAL A 1 2   ? 20.494  -5.711  14.806  1.00 20.26 ? 2    VAL A O   1 
ATOM   14   C CB  . VAL A 1 2   ? 20.005  -2.633  15.274  1.00 23.53 ? 2    VAL A CB  1 
ATOM   15   C CG1 . VAL A 1 2   ? 19.791  -2.887  16.767  1.00 22.89 ? 2    VAL A CG1 1 
ATOM   16   C CG2 . VAL A 1 2   ? 20.148  -1.147  15.030  1.00 24.06 ? 2    VAL A CG2 1 
ATOM   17   N N   . GLN A 1 3   ? 22.080  -5.093  16.283  1.00 22.23 ? 3    GLN A N   1 
ATOM   18   C CA  . GLN A 1 3   ? 22.197  -6.432  16.905  1.00 22.31 ? 3    GLN A CA  1 
ATOM   19   C C   . GLN A 1 3   ? 22.430  -6.268  18.398  1.00 19.68 ? 3    GLN A C   1 
ATOM   20   O O   . GLN A 1 3   ? 23.158  -5.355  18.783  1.00 19.28 ? 3    GLN A O   1 
ATOM   21   C CB  . GLN A 1 3   ? 23.359  -7.210  16.306  1.00 26.15 ? 3    GLN A CB  1 
ATOM   22   C CG  . GLN A 1 3   ? 23.189  -7.517  14.833  1.00 31.59 ? 3    GLN A CG  1 
ATOM   23   C CD  . GLN A 1 3   ? 22.112  -8.537  14.553  1.00 36.94 ? 3    GLN A CD  1 
ATOM   24   O OE1 . GLN A 1 3   ? 20.912  -8.249  14.585  1.00 46.84 ? 3    GLN A OE1 1 
ATOM   25   N NE2 . GLN A 1 3   ? 22.541  -9.759  14.266  1.00 44.52 ? 3    GLN A NE2 1 
ATOM   26   N N   . LEU A 1 4   ? 21.804  -7.119  19.203  1.00 20.11 ? 4    LEU A N   1 
ATOM   27   C CA  . LEU A 1 4   ? 22.094  -7.275  20.638  1.00 19.28 ? 4    LEU A CA  1 
ATOM   28   C C   . LEU A 1 4   ? 22.377  -8.756  20.852  1.00 20.47 ? 4    LEU A C   1 
ATOM   29   O O   . LEU A 1 4   ? 21.410  -9.549  20.836  1.00 21.49 ? 4    LEU A O   1 
ATOM   30   C CB  . LEU A 1 4   ? 20.938  -6.803  21.527  1.00 18.97 ? 4    LEU A CB  1 
ATOM   31   C CG  . LEU A 1 4   ? 20.572  -5.315  21.488  1.00 18.88 ? 4    LEU A CG  1 
ATOM   32   C CD1 . LEU A 1 4   ? 19.402  -5.074  22.427  1.00 19.01 ? 4    LEU A CD1 1 
ATOM   33   C CD2 . LEU A 1 4   ? 21.727  -4.417  21.874  1.00 18.64 ? 4    LEU A CD2 1 
ATOM   34   N N   . GLN A 1 5   ? 23.652  -9.107  21.023  1.00 19.60 ? 5    GLN A N   1 
ATOM   35   C CA  . GLN A 1 5   ? 24.070  -10.512 21.047  1.00 20.82 ? 5    GLN A CA  1 
ATOM   36   C C   . GLN A 1 5   ? 24.395  -10.835 22.506  1.00 19.42 ? 5    GLN A C   1 
ATOM   37   O O   . GLN A 1 5   ? 25.404  -10.269 23.049  1.00 19.73 ? 5    GLN A O   1 
ATOM   38   C CB  . GLN A 1 5   ? 25.289  -10.731 20.134  1.00 23.77 ? 5    GLN A CB  1 
ATOM   39   C CG  . GLN A 1 5   ? 25.780  -12.166 20.175  1.00 29.41 ? 5    GLN A CG  1 
ATOM   40   C CD  . GLN A 1 5   ? 24.796  -13.160 19.608  1.00 35.10 ? 5    GLN A CD  1 
ATOM   41   O OE1 . GLN A 1 5   ? 23.819  -12.821 18.943  1.00 39.73 ? 5    GLN A OE1 1 
ATOM   42   N NE2 . GLN A 1 5   ? 25.078  -14.436 19.839  1.00 43.20 ? 5    GLN A NE2 1 
ATOM   43   N N   . GLN A 1 6   ? 23.609  -11.728 23.111  1.00 18.29 ? 6    GLN A N   1 
ATOM   44   C CA  . GLN A 1 6   ? 23.814  -12.111 24.510  1.00 18.47 ? 6    GLN A CA  1 
ATOM   45   C C   . GLN A 1 6   ? 24.739  -13.319 24.595  1.00 19.67 ? 6    GLN A C   1 
ATOM   46   O O   . GLN A 1 6   ? 24.871  -14.103 23.605  1.00 21.10 ? 6    GLN A O   1 
ATOM   47   C CB  . GLN A 1 6   ? 22.479  -12.379 25.214  1.00 17.46 ? 6    GLN A CB  1 
ATOM   48   C CG  . GLN A 1 6   ? 21.544  -11.206 25.133  1.00 16.49 ? 6    GLN A CG  1 
ATOM   49   C CD  . GLN A 1 6   ? 20.290  -11.414 25.920  1.00 16.10 ? 6    GLN A CD  1 
ATOM   50   O OE1 . GLN A 1 6   ? 19.220  -11.024 25.478  1.00 15.19 ? 6    GLN A OE1 1 
ATOM   51   N NE2 . GLN A 1 6   ? 20.403  -12.057 27.079  1.00 16.44 ? 6    GLN A NE2 1 
ATOM   52   N N   . SER A 1 7   ? 25.290  -13.499 25.773  1.00 20.61 ? 7    SER A N   1 
ATOM   53   C CA  . SER A 1 7   ? 26.120  -14.670 26.125  1.00 21.59 ? 7    SER A CA  1 
ATOM   54   C C   . SER A 1 7   ? 25.276  -15.945 26.212  1.00 22.12 ? 7    SER A C   1 
ATOM   55   O O   . SER A 1 7   ? 24.018  -15.887 26.289  1.00 20.96 ? 7    SER A O   1 
ATOM   56   C CB  . SER A 1 7   ? 26.910  -14.400 27.369  1.00 20.82 ? 7    SER A CB  1 
ATOM   57   O OG  . SER A 1 7   ? 26.127  -13.832 28.399  1.00 19.69 ? 7    SER A OG  1 
ATOM   58   N N   . ASP A 1 8   ? 25.998  -17.064 26.237  1.00 23.39 ? 8    ASP A N   1 
ATOM   59   C CA  . ASP A 1 8   ? 25.497  -18.463 26.251  1.00 25.05 ? 8    ASP A CA  1 
ATOM   60   C C   . ASP A 1 8   ? 24.789  -18.771 27.563  1.00 24.18 ? 8    ASP A C   1 
ATOM   61   O O   . ASP A 1 8   ? 25.055  -18.100 28.594  1.00 23.89 ? 8    ASP A O   1 
ATOM   62   C CB  . ASP A 1 8   ? 26.659  -19.427 25.977  1.00 27.76 ? 8    ASP A CB  1 
ATOM   63   C CG  . ASP A 1 8   ? 27.177  -19.355 24.530  1.00 31.26 ? 8    ASP A CG  1 
ATOM   64   O OD1 . ASP A 1 8   ? 26.526  -18.724 23.697  1.00 31.42 ? 8    ASP A OD1 1 
ATOM   65   O OD2 . ASP A 1 8   ? 28.239  -19.977 24.231  1.00 36.74 ? 8    ASP A OD2 1 
ATOM   66   N N   . ALA A 1 9   ? 23.918  -19.778 27.510  1.00 24.37 ? 9    ALA A N   1 
ATOM   67   C CA  . ALA A 1 9   ? 23.198  -20.360 28.659  1.00 25.63 ? 9    ALA A CA  1 
ATOM   68   C C   . ALA A 1 9   ? 24.193  -20.664 29.787  1.00 25.75 ? 9    ALA A C   1 
ATOM   69   O O   . ALA A 1 9   ? 25.334  -21.025 29.469  1.00 25.21 ? 9    ALA A O   1 
ATOM   70   C CB  . ALA A 1 9   ? 22.441  -21.594 28.214  1.00 27.08 ? 9    ALA A CB  1 
ATOM   71   N N   . GLU A 1 10  ? 23.771  -20.468 31.027  1.00 25.92 ? 10   GLU A N   1 
ATOM   72   C CA  . GLU A 1 10  ? 24.585  -20.644 32.258  1.00 28.58 ? 10   GLU A CA  1 
ATOM   73   C C   . GLU A 1 10  ? 23.923  -21.661 33.173  1.00 28.80 ? 10   GLU A C   1 
ATOM   74   O O   . GLU A 1 10  ? 22.707  -21.587 33.363  1.00 26.58 ? 10   GLU A O   1 
ATOM   75   C CB  . GLU A 1 10  ? 24.712  -19.338 33.021  1.00 30.12 ? 10   GLU A CB  1 
ATOM   76   C CG  . GLU A 1 10  ? 25.354  -18.240 32.206  1.00 32.55 ? 10   GLU A CG  1 
ATOM   77   C CD  . GLU A 1 10  ? 26.817  -17.995 32.515  1.00 36.08 ? 10   GLU A CD  1 
ATOM   78   O OE1 . GLU A 1 10  ? 27.446  -18.875 33.150  1.00 35.31 ? 10   GLU A OE1 1 
ATOM   79   O OE2 . GLU A 1 10  ? 27.321  -16.919 32.090  1.00 36.62 ? 10   GLU A OE2 1 
ATOM   80   N N   . LEU A 1 11  ? 24.734  -22.575 33.701  1.00 28.73 ? 11   LEU A N   1 
ATOM   81   C CA  . LEU A 1 11  ? 24.288  -23.630 34.633  1.00 31.48 ? 11   LEU A CA  1 
ATOM   82   C C   . LEU A 1 11  ? 25.172  -23.466 35.863  1.00 30.41 ? 11   LEU A C   1 
ATOM   83   O O   . LEU A 1 11  ? 26.381  -23.618 35.702  1.00 28.55 ? 11   LEU A O   1 
ATOM   84   C CB  . LEU A 1 11  ? 24.509  -24.988 33.971  1.00 34.47 ? 11   LEU A CB  1 
ATOM   85   C CG  . LEU A 1 11  ? 23.483  -26.088 34.240  1.00 40.41 ? 11   LEU A CG  1 
ATOM   86   C CD1 . LEU A 1 11  ? 22.821  -25.969 35.604  1.00 38.35 ? 11   LEU A CD1 1 
ATOM   87   C CD2 . LEU A 1 11  ? 22.443  -26.111 33.116  1.00 42.61 ? 11   LEU A CD2 1 
ATOM   88   N N   . VAL A 1 12  ? 24.596  -23.078 36.998  1.00 30.11 ? 12   VAL A N   1 
ATOM   89   C CA  . VAL A 1 12  ? 25.402  -22.757 38.204  1.00 31.63 ? 12   VAL A CA  1 
ATOM   90   C C   . VAL A 1 12  ? 24.724  -23.338 39.442  1.00 30.76 ? 12   VAL A C   1 
ATOM   91   O O   . VAL A 1 12  ? 23.555  -23.731 39.374  1.00 27.23 ? 12   VAL A O   1 
ATOM   92   C CB  . VAL A 1 12  ? 25.625  -21.247 38.388  1.00 31.66 ? 12   VAL A CB  1 
ATOM   93   C CG1 . VAL A 1 12  ? 26.499  -20.640 37.313  1.00 32.71 ? 12   VAL A CG1 1 
ATOM   94   C CG2 . VAL A 1 12  ? 24.298  -20.517 38.492  1.00 31.11 ? 12   VAL A CG2 1 
ATOM   95   N N   . LYS A 1 13  ? 25.514  -23.386 40.516  1.00 32.91 ? 13   LYS A N   1 
ATOM   96   C CA  . LYS A 1 13  ? 25.125  -23.833 41.872  1.00 35.14 ? 13   LYS A CA  1 
ATOM   97   C C   . LYS A 1 13  ? 24.447  -22.676 42.593  1.00 31.89 ? 13   LYS A C   1 
ATOM   98   O O   . LYS A 1 13  ? 24.833  -21.524 42.410  1.00 29.85 ? 13   LYS A O   1 
ATOM   99   C CB  . LYS A 1 13  ? 26.391  -24.215 42.648  1.00 38.35 ? 13   LYS A CB  1 
ATOM   100  C CG  . LYS A 1 13  ? 27.128  -25.429 42.102  1.00 43.06 ? 13   LYS A CG  1 
ATOM   101  C CD  . LYS A 1 13  ? 27.106  -26.591 43.097  1.00 47.37 ? 13   LYS A CD  1 
ATOM   102  C CE  . LYS A 1 13  ? 28.236  -27.575 42.902  1.00 49.98 ? 13   LYS A CE  1 
ATOM   103  N NZ  . LYS A 1 13  ? 27.968  -28.486 41.761  1.00 52.13 ? 13   LYS A NZ  1 
ATOM   104  N N   . PRO A 1 14  ? 23.442  -22.965 43.435  1.00 30.92 ? 14   PRO A N   1 
ATOM   105  C CA  . PRO A 1 14  ? 22.920  -21.997 44.392  1.00 30.77 ? 14   PRO A CA  1 
ATOM   106  C C   . PRO A 1 14  ? 24.108  -21.336 45.086  1.00 29.43 ? 14   PRO A C   1 
ATOM   107  O O   . PRO A 1 14  ? 25.087  -22.009 45.356  1.00 31.74 ? 14   PRO A O   1 
ATOM   108  C CB  . PRO A 1 14  ? 22.020  -22.807 45.346  1.00 31.48 ? 14   PRO A CB  1 
ATOM   109  C CG  . PRO A 1 14  ? 21.678  -24.081 44.591  1.00 32.34 ? 14   PRO A CG  1 
ATOM   110  C CD  . PRO A 1 14  ? 22.750  -24.255 43.536  1.00 33.28 ? 14   PRO A CD  1 
ATOM   111  N N   . GLY A 1 15  ? 24.020  -20.026 45.311  1.00 28.98 ? 15   GLY A N   1 
ATOM   112  C CA  . GLY A 1 15  ? 25.036  -19.232 46.028  1.00 27.75 ? 15   GLY A CA  1 
ATOM   113  C C   . GLY A 1 15  ? 26.071  -18.650 45.087  1.00 27.32 ? 15   GLY A C   1 
ATOM   114  O O   . GLY A 1 15  ? 26.779  -17.760 45.483  1.00 28.13 ? 15   GLY A O   1 
ATOM   115  N N   . ALA A 1 16  ? 26.161  -19.119 43.856  1.00 25.53 ? 16   ALA A N   1 
ATOM   116  C CA  . ALA A 1 16  ? 27.161  -18.568 42.920  1.00 25.66 ? 16   ALA A CA  1 
ATOM   117  C C   . ALA A 1 16  ? 26.635  -17.221 42.390  1.00 23.45 ? 16   ALA A C   1 
ATOM   118  O O   . ALA A 1 16  ? 25.501  -16.785 42.739  1.00 21.67 ? 16   ALA A O   1 
ATOM   119  C CB  . ALA A 1 16  ? 27.442  -19.573 41.801  1.00 26.11 ? 16   ALA A CB  1 
ATOM   120  N N   . SER A 1 17  ? 27.465  -16.570 41.603  1.00 23.40 ? 17   SER A N   1 
ATOM   121  C CA  . SER A 1 17  ? 27.116  -15.361 40.801  1.00 22.97 ? 17   SER A CA  1 
ATOM   122  C C   . SER A 1 17  ? 27.253  -15.706 39.326  1.00 23.21 ? 17   SER A C   1 
ATOM   123  O O   . SER A 1 17  ? 28.026  -16.645 38.999  1.00 23.11 ? 17   SER A O   1 
ATOM   124  C CB  . SER A 1 17  ? 28.015  -14.228 41.177  1.00 22.78 ? 17   SER A CB  1 
ATOM   125  O OG  . SER A 1 17  ? 27.649  -13.743 42.443  1.00 23.90 ? 17   SER A OG  1 
ATOM   126  N N   . VAL A 1 18  ? 26.611  -14.927 38.441  1.00 22.36 ? 18   VAL A N   1 
ATOM   127  C CA  . VAL A 1 18  ? 26.812  -15.039 36.966  1.00 22.42 ? 18   VAL A CA  1 
ATOM   128  C C   . VAL A 1 18  ? 26.815  -13.614 36.424  1.00 21.63 ? 18   VAL A C   1 
ATOM   129  O O   . VAL A 1 18  ? 26.181  -12.723 37.024  1.00 21.07 ? 18   VAL A O   1 
ATOM   130  C CB  . VAL A 1 18  ? 25.745  -15.878 36.234  1.00 23.11 ? 18   VAL A CB  1 
ATOM   131  C CG1 . VAL A 1 18  ? 25.785  -17.328 36.644  1.00 25.59 ? 18   VAL A CG1 1 
ATOM   132  C CG2 . VAL A 1 18  ? 24.354  -15.311 36.413  1.00 22.74 ? 18   VAL A CG2 1 
ATOM   133  N N   . LYS A 1 19  ? 27.566  -13.418 35.353  1.00 22.05 ? 19   LYS A N   1 
ATOM   134  C CA  . LYS A 1 19  ? 27.548  -12.131 34.630  1.00 21.71 ? 19   LYS A CA  1 
ATOM   135  C C   . LYS A 1 19  ? 27.174  -12.419 33.186  1.00 22.38 ? 19   LYS A C   1 
ATOM   136  O O   . LYS A 1 19  ? 27.917  -13.189 32.493  1.00 22.10 ? 19   LYS A O   1 
ATOM   137  C CB  . LYS A 1 19  ? 28.928  -11.504 34.694  1.00 23.91 ? 19   LYS A CB  1 
ATOM   138  C CG  . LYS A 1 19  ? 28.965  -10.066 34.206  1.00 24.22 ? 19   LYS A CG  1 
ATOM   139  C CD  . LYS A 1 19  ? 30.371  -9.566  34.402  1.00 28.06 ? 19   LYS A CD  1 
ATOM   140  C CE  . LYS A 1 19  ? 30.483  -8.068  34.374  1.00 28.60 ? 19   LYS A CE  1 
ATOM   141  N NZ  . LYS A 1 19  ? 31.734  -7.625  35.033  1.00 29.51 ? 19   LYS A NZ  1 
ATOM   142  N N   . ILE A 1 20  ? 26.022  -11.915 32.762  1.00 20.42 ? 20   ILE A N   1 
ATOM   143  C CA  . ILE A 1 20  ? 25.454  -12.096 31.395  1.00 20.86 ? 20   ILE A CA  1 
ATOM   144  C C   . ILE A 1 20  ? 25.809  -10.850 30.589  1.00 19.17 ? 20   ILE A C   1 
ATOM   145  O O   . ILE A 1 20  ? 25.741  -9.760  31.151  1.00 19.57 ? 20   ILE A O   1 
ATOM   146  C CB  . ILE A 1 20  ? 23.927  -12.284 31.486  1.00 21.56 ? 20   ILE A CB  1 
ATOM   147  C CG1 . ILE A 1 20  ? 23.572  -13.482 32.369  1.00 22.35 ? 20   ILE A CG1 1 
ATOM   148  C CG2 . ILE A 1 20  ? 23.331  -12.413 30.089  1.00 24.60 ? 20   ILE A CG2 1 
ATOM   149  C CD1 . ILE A 1 20  ? 22.074  -13.586 32.654  1.00 22.64 ? 20   ILE A CD1 1 
ATOM   150  N N   . SER A 1 21  ? 26.281  -11.027 29.368  1.00 19.01 ? 21   SER A N   1 
ATOM   151  C CA  . SER A 1 21  ? 26.686  -9.915  28.497  1.00 18.80 ? 21   SER A CA  1 
ATOM   152  C C   . SER A 1 21  ? 25.640  -9.711  27.413  1.00 18.51 ? 21   SER A C   1 
ATOM   153  O O   . SER A 1 21  ? 24.959  -10.655 26.988  1.00 17.63 ? 21   SER A O   1 
ATOM   154  C CB  . SER A 1 21  ? 28.086  -10.136 27.922  1.00 20.28 ? 21   SER A CB  1 
ATOM   155  O OG  . SER A 1 21  ? 28.123  -11.250 27.066  1.00 20.58 ? 21   SER A OG  1 
ATOM   156  N N   . CYS A 1 22  ? 25.654  -8.511  26.877  1.00 18.15 ? 22   CYS A N   1 
ATOM   157  C CA  . CYS A 1 22  ? 24.747  -8.041  25.808  1.00 19.41 ? 22   CYS A CA  1 
ATOM   158  C C   . CYS A 1 22  ? 25.608  -7.183  24.882  1.00 18.19 ? 22   CYS A C   1 
ATOM   159  O O   . CYS A 1 22  ? 25.811  -6.034  25.230  1.00 17.56 ? 22   CYS A O   1 
ATOM   160  C CB  . CYS A 1 22  ? 23.592  -7.288  26.433  1.00 18.97 ? 22   CYS A CB  1 
ATOM   161  S SG  . CYS A 1 22  ? 22.524  -6.517  25.209  1.00 22.25 ? 22   CYS A SG  1 
ATOM   162  N N   . LYS A 1 23  ? 26.151  -7.760  23.820  1.00 19.22 ? 23   LYS A N   1 
ATOM   163  C CA  . LYS A 1 23  ? 26.997  -6.991  22.879  1.00 20.43 ? 23   LYS A CA  1 
ATOM   164  C C   . LYS A 1 23  ? 26.164  -6.243  21.829  1.00 19.88 ? 23   LYS A C   1 
ATOM   165  O O   . LYS A 1 23  ? 25.509  -6.922  21.024  1.00 18.61 ? 23   LYS A O   1 
ATOM   166  C CB  . LYS A 1 23  ? 27.990  -7.917  22.200  1.00 24.22 ? 23   LYS A CB  1 
ATOM   167  C CG  . LYS A 1 23  ? 28.837  -7.216  21.159  1.00 29.87 ? 23   LYS A CG  1 
ATOM   168  C CD  . LYS A 1 23  ? 29.464  -5.896  21.601  1.00 31.01 ? 23   LYS A CD  1 
ATOM   169  C CE  . LYS A 1 23  ? 29.942  -5.037  20.475  1.00 32.12 ? 23   LYS A CE  1 
ATOM   170  N NZ  . LYS A 1 23  ? 30.618  -5.865  19.449  1.00 37.69 ? 23   LYS A NZ  1 
ATOM   171  N N   . ALA A 1 24  ? 26.266  -4.922  21.789  1.00 18.69 ? 24   ALA A N   1 
ATOM   172  C CA  . ALA A 1 24  ? 25.453  -4.074  20.893  1.00 19.00 ? 24   ALA A CA  1 
ATOM   173  C C   . ALA A 1 24  ? 26.271  -3.763  19.651  1.00 20.11 ? 24   ALA A C   1 
ATOM   174  O O   . ALA A 1 24  ? 27.504  -3.480  19.763  1.00 19.91 ? 24   ALA A O   1 
ATOM   175  C CB  . ALA A 1 24  ? 25.054  -2.818  21.592  1.00 19.23 ? 24   ALA A CB  1 
ATOM   176  N N   . SER A 1 25  ? 25.632  -3.800  18.479  1.00 19.45 ? 25   SER A N   1 
ATOM   177  C CA  . SER A 1 25  ? 26.286  -3.306  17.251  1.00 20.13 ? 25   SER A CA  1 
ATOM   178  C C   . SER A 1 25  ? 25.264  -2.587  16.373  1.00 19.31 ? 25   SER A C   1 
ATOM   179  O O   . SER A 1 25  ? 24.045  -2.747  16.588  1.00 17.53 ? 25   SER A O   1 
ATOM   180  C CB  . SER A 1 25  ? 26.975  -4.424  16.551  1.00 23.13 ? 25   SER A CB  1 
ATOM   181  O OG  . SER A 1 25  ? 26.084  -5.474  16.241  1.00 24.76 ? 25   SER A OG  1 
ATOM   182  N N   . GLY A 1 26  ? 25.770  -1.790  15.447  1.00 18.70 ? 26   GLY A N   1 
ATOM   183  C CA  . GLY A 1 26  ? 24.995  -1.256  14.316  1.00 19.50 ? 26   GLY A CA  1 
ATOM   184  C C   . GLY A 1 26  ? 24.316  0.046   14.682  1.00 19.86 ? 26   GLY A C   1 
ATOM   185  O O   . GLY A 1 26  ? 23.487  0.549   13.863  1.00 21.30 ? 26   GLY A O   1 
ATOM   186  N N   . TYR A 1 27  ? 24.692  0.632   15.816  1.00 18.60 ? 27   TYR A N   1 
ATOM   187  C CA  . TYR A 1 27  ? 24.196  1.961   16.247  1.00 18.63 ? 27   TYR A CA  1 
ATOM   188  C C   . TYR A 1 27  ? 25.188  2.555   17.236  1.00 18.72 ? 27   TYR A C   1 
ATOM   189  O O   . TYR A 1 27  ? 26.080  1.813   17.689  1.00 19.27 ? 27   TYR A O   1 
ATOM   190  C CB  . TYR A 1 27  ? 22.772  1.854   16.799  1.00 18.06 ? 27   TYR A CB  1 
ATOM   191  C CG  . TYR A 1 27  ? 22.688  1.184   18.151  1.00 17.77 ? 27   TYR A CG  1 
ATOM   192  C CD1 . TYR A 1 27  ? 22.608  -0.188  18.287  1.00 18.01 ? 27   TYR A CD1 1 
ATOM   193  C CD2 . TYR A 1 27  ? 22.762  1.936   19.307  1.00 18.09 ? 27   TYR A CD2 1 
ATOM   194  C CE1 . TYR A 1 27  ? 22.548  -0.788  19.536  1.00 18.11 ? 27   TYR A CE1 1 
ATOM   195  C CE2 . TYR A 1 27  ? 22.678  1.357   20.565  1.00 17.36 ? 27   TYR A CE2 1 
ATOM   196  C CZ  . TYR A 1 27  ? 22.601  -0.016  20.689  1.00 17.38 ? 27   TYR A CZ  1 
ATOM   197  O OH  . TYR A 1 27  ? 22.570  -0.575  21.946  1.00 17.56 ? 27   TYR A OH  1 
ATOM   198  N N   . ILE A 1 28  ? 24.991  3.811   17.615  1.00 19.06 ? 28   ILE A N   1 
ATOM   199  C CA  . ILE A 1 28  ? 25.894  4.491   18.588  1.00 20.24 ? 28   ILE A CA  1 
ATOM   200  C C   . ILE A 1 28  ? 25.505  4.015   19.977  1.00 19.54 ? 28   ILE A C   1 
ATOM   201  O O   . ILE A 1 28  ? 24.410  4.374   20.449  1.00 17.49 ? 28   ILE A O   1 
ATOM   202  C CB  . ILE A 1 28  ? 25.839  6.011   18.464  1.00 21.68 ? 28   ILE A CB  1 
ATOM   203  C CG1 . ILE A 1 28  ? 26.233  6.417   17.038  1.00 24.39 ? 28   ILE A CG1 1 
ATOM   204  C CG2 . ILE A 1 28  ? 26.759  6.666   19.509  1.00 21.85 ? 28   ILE A CG2 1 
ATOM   205  C CD1 . ILE A 1 28  ? 26.135  7.886   16.808  1.00 26.85 ? 28   ILE A CD1 1 
ATOM   206  N N   . PHE A 1 29  ? 26.429  3.318   20.636  1.00 18.68 ? 29   PHE A N   1 
ATOM   207  C CA  . PHE A 1 29  ? 26.153  2.669   21.932  1.00 18.83 ? 29   PHE A CA  1 
ATOM   208  C C   . PHE A 1 29  ? 25.648  3.688   22.954  1.00 19.28 ? 29   PHE A C   1 
ATOM   209  O O   . PHE A 1 29  ? 24.735  3.377   23.750  1.00 18.70 ? 29   PHE A O   1 
ATOM   210  C CB  . PHE A 1 29  ? 27.413  1.952   22.405  1.00 19.11 ? 29   PHE A CB  1 
ATOM   211  C CG  . PHE A 1 29  ? 27.235  1.157   23.666  1.00 19.27 ? 29   PHE A CG  1 
ATOM   212  C CD1 . PHE A 1 29  ? 26.420  0.050   23.675  1.00 18.24 ? 29   PHE A CD1 1 
ATOM   213  C CD2 . PHE A 1 29  ? 28.016  1.432   24.783  1.00 19.64 ? 29   PHE A CD2 1 
ATOM   214  C CE1 . PHE A 1 29  ? 26.274  -0.723  24.816  1.00 19.62 ? 29   PHE A CE1 1 
ATOM   215  C CE2 . PHE A 1 29  ? 27.877  0.657   25.914  1.00 19.42 ? 29   PHE A CE2 1 
ATOM   216  C CZ  . PHE A 1 29  ? 26.996  -0.400  25.941  1.00 19.13 ? 29   PHE A CZ  1 
ATOM   217  N N   . ALA A 1 30  ? 26.233  4.871   22.943  1.00 20.03 ? 30   ALA A N   1 
ATOM   218  C CA  . ALA A 1 30  ? 25.988  5.943   23.928  1.00 20.41 ? 30   ALA A CA  1 
ATOM   219  C C   . ALA A 1 30  ? 24.577  6.484   23.803  1.00 19.20 ? 30   ALA A C   1 
ATOM   220  O O   . ALA A 1 30  ? 24.227  7.244   24.660  1.00 20.41 ? 30   ALA A O   1 
ATOM   221  C CB  . ALA A 1 30  ? 26.995  7.068   23.745  1.00 21.73 ? 30   ALA A CB  1 
ATOM   222  N N   . ASP A 1 31  ? 23.863  6.236   22.705  1.00 18.33 ? 31   ASP A N   1 
ATOM   223  C CA  . ASP A 1 31  ? 22.635  6.992   22.368  1.00 18.20 ? 31   ASP A CA  1 
ATOM   224  C C   . ASP A 1 31  ? 21.378  6.263   22.863  1.00 16.44 ? 31   ASP A C   1 
ATOM   225  O O   . ASP A 1 31  ? 20.292  6.778   22.670  1.00 16.65 ? 31   ASP A O   1 
ATOM   226  C CB  . ASP A 1 31  ? 22.661  7.333   20.887  1.00 20.57 ? 31   ASP A CB  1 
ATOM   227  C CG  . ASP A 1 31  ? 23.681  8.441   20.602  1.00 21.14 ? 31   ASP A CG  1 
ATOM   228  O OD1 . ASP A 1 31  ? 24.380  8.937   21.542  1.00 24.40 ? 31   ASP A OD1 1 
ATOM   229  O OD2 . ASP A 1 31  ? 23.762  8.787   19.496  1.00 23.63 ? 31   ASP A OD2 1 
ATOM   230  N N   . HIS A 1 32  ? 21.496  5.072   23.462  1.00 15.53 ? 32   HIS A N   1 
ATOM   231  C CA  . HIS A 1 32  ? 20.274  4.343   23.924  1.00 15.22 ? 32   HIS A CA  1 
ATOM   232  C C   . HIS A 1 32  ? 20.569  3.603   25.204  1.00 14.22 ? 32   HIS A C   1 
ATOM   233  O O   . HIS A 1 32  ? 21.599  2.972   25.313  1.00 14.98 ? 32   HIS A O   1 
ATOM   234  C CB  . HIS A 1 32  ? 19.785  3.346   22.870  1.00 14.60 ? 32   HIS A CB  1 
ATOM   235  C CG  . HIS A 1 32  ? 19.373  4.016   21.606  1.00 14.53 ? 32   HIS A CG  1 
ATOM   236  N ND1 . HIS A 1 32  ? 18.179  4.692   21.494  1.00 14.43 ? 32   HIS A ND1 1 
ATOM   237  C CD2 . HIS A 1 32  ? 20.040  4.182   20.451  1.00 14.93 ? 32   HIS A CD2 1 
ATOM   238  C CE1 . HIS A 1 32  ? 18.116  5.292   20.319  1.00 14.80 ? 32   HIS A CE1 1 
ATOM   239  N NE2 . HIS A 1 32  ? 19.239  4.933   19.606  1.00 14.93 ? 32   HIS A NE2 1 
ATOM   240  N N   . ALA A 1 33  ? 19.656  3.651   26.146  1.00 14.62 ? 33   ALA A N   1 
ATOM   241  C CA  . ALA A 1 33  ? 19.733  2.790   27.340  1.00 13.99 ? 33   ALA A CA  1 
ATOM   242  C C   . ALA A 1 33  ? 19.479  1.325   26.960  1.00 13.50 ? 33   ALA A C   1 
ATOM   243  O O   . ALA A 1 33  ? 18.737  1.012   26.066  1.00 13.63 ? 33   ALA A O   1 
ATOM   244  C CB  . ALA A 1 33  ? 18.777  3.289   28.395  1.00 14.08 ? 33   ALA A CB  1 
ATOM   245  N N   . ILE A 1 34  ? 20.087  0.434   27.698  1.00 14.17 ? 34   ILE A N   1 
ATOM   246  C CA  . ILE A 1 34  ? 19.867  -1.014  27.631  1.00 14.18 ? 34   ILE A CA  1 
ATOM   247  C C   . ILE A 1 34  ? 19.170  -1.430  28.927  1.00 13.66 ? 34   ILE A C   1 
ATOM   248  O O   . ILE A 1 34  ? 19.644  -1.104  30.047  1.00 13.94 ? 34   ILE A O   1 
ATOM   249  C CB  . ILE A 1 34  ? 21.199  -1.733  27.486  1.00 14.70 ? 34   ILE A CB  1 
ATOM   250  C CG1 . ILE A 1 34  ? 21.902  -1.332  26.194  1.00 15.77 ? 34   ILE A CG1 1 
ATOM   251  C CG2 . ILE A 1 34  ? 20.966  -3.233  27.605  1.00 14.98 ? 34   ILE A CG2 1 
ATOM   252  C CD1 . ILE A 1 34  ? 21.307  -1.917  25.011  1.00 16.58 ? 34   ILE A CD1 1 
ATOM   253  N N   . HIS A 1 35  ? 18.014  -2.040  28.746  1.00 13.34 ? 35   HIS A N   1 
ATOM   254  C CA  . HIS A 1 35  ? 17.165  -2.568  29.817  1.00 12.95 ? 35   HIS A CA  1 
ATOM   255  C C   . HIS A 1 35  ? 17.425  -4.059  29.948  1.00 13.25 ? 35   HIS A C   1 
ATOM   256  O O   . HIS A 1 35  ? 17.649  -4.776  28.903  1.00 14.25 ? 35   HIS A O   1 
ATOM   257  C CB  . HIS A 1 35  ? 15.692  -2.265  29.530  1.00 12.35 ? 35   HIS A CB  1 
ATOM   258  C CG  . HIS A 1 35  ? 15.383  -0.816  29.522  1.00 12.82 ? 35   HIS A CG  1 
ATOM   259  N ND1 . HIS A 1 35  ? 14.642  -0.215  30.535  1.00 12.48 ? 35   HIS A ND1 1 
ATOM   260  C CD2 . HIS A 1 35  ? 15.688  0.167   28.627  1.00 12.81 ? 35   HIS A CD2 1 
ATOM   261  C CE1 . HIS A 1 35  ? 14.541  1.054   30.272  1.00 12.68 ? 35   HIS A CE1 1 
ATOM   262  N NE2 . HIS A 1 35  ? 15.223  1.347   29.133  1.00 12.38 ? 35   HIS A NE2 1 
ATOM   263  N N   . TRP A 1 36  ? 17.122  -4.568  31.135  1.00 14.10 ? 36   TRP A N   1 
ATOM   264  C CA  . TRP A 1 36  ? 17.172  -6.021  31.388  1.00 14.31 ? 36   TRP A CA  1 
ATOM   265  C C   . TRP A 1 36  ? 15.833  -6.495  31.915  1.00 14.31 ? 36   TRP A C   1 
ATOM   266  O O   . TRP A 1 36  ? 15.254  -5.803  32.708  1.00 13.13 ? 36   TRP A O   1 
ATOM   267  C CB  . TRP A 1 36  ? 18.313  -6.361  32.315  1.00 14.49 ? 36   TRP A CB  1 
ATOM   268  C CG  . TRP A 1 36  ? 19.670  -6.160  31.697  1.00 14.43 ? 36   TRP A CG  1 
ATOM   269  C CD1 . TRP A 1 36  ? 20.381  -5.009  31.690  1.00 15.51 ? 36   TRP A CD1 1 
ATOM   270  C CD2 . TRP A 1 36  ? 20.473  -7.123  31.004  1.00 15.36 ? 36   TRP A CD2 1 
ATOM   271  N NE1 . TRP A 1 36  ? 21.599  -5.208  31.085  1.00 15.73 ? 36   TRP A NE1 1 
ATOM   272  C CE2 . TRP A 1 36  ? 21.678  -6.484  30.636  1.00 15.71 ? 36   TRP A CE2 1 
ATOM   273  C CE3 . TRP A 1 36  ? 20.318  -8.475  30.678  1.00 16.50 ? 36   TRP A CE3 1 
ATOM   274  C CZ2 . TRP A 1 36  ? 22.700  -7.162  30.001  1.00 16.41 ? 36   TRP A CZ2 1 
ATOM   275  C CZ3 . TRP A 1 36  ? 21.306  -9.136  29.984  1.00 18.02 ? 36   TRP A CZ3 1 
ATOM   276  C CH2 . TRP A 1 36  ? 22.509  -8.486  29.696  1.00 16.95 ? 36   TRP A CH2 1 
ATOM   277  N N   . VAL A 1 37  ? 15.421  -7.649  31.428  1.00 15.74 ? 37   VAL A N   1 
ATOM   278  C CA  . VAL A 1 37  ? 14.078  -8.244  31.663  1.00 16.96 ? 37   VAL A CA  1 
ATOM   279  C C   . VAL A 1 37  ? 14.244  -9.731  31.988  1.00 18.21 ? 37   VAL A C   1 
ATOM   280  O O   . VAL A 1 37  ? 15.039  -10.432 31.287  1.00 20.97 ? 37   VAL A O   1 
ATOM   281  C CB  . VAL A 1 37  ? 13.187  -7.979  30.414  1.00 17.06 ? 37   VAL A CB  1 
ATOM   282  C CG1 . VAL A 1 37  ? 11.832  -8.634  30.508  1.00 18.69 ? 37   VAL A CG1 1 
ATOM   283  C CG2 . VAL A 1 37  ? 12.990  -6.498  30.188  1.00 16.56 ? 37   VAL A CG2 1 
ATOM   284  N N   . LYS A 1 38  ? 13.491  -10.213 32.965  1.00 18.62 ? 38   LYS A N   1 
ATOM   285  C CA  . LYS A 1 38  ? 13.507  -11.626 33.407  1.00 19.84 ? 38   LYS A CA  1 
ATOM   286  C C   . LYS A 1 38  ? 12.201  -12.267 32.936  1.00 22.00 ? 38   LYS A C   1 
ATOM   287  O O   . LYS A 1 38  ? 11.147  -11.700 33.247  1.00 21.04 ? 38   LYS A O   1 
ATOM   288  C CB  . LYS A 1 38  ? 13.600  -11.690 34.914  1.00 20.19 ? 38   LYS A CB  1 
ATOM   289  C CG  . LYS A 1 38  ? 13.635  -13.067 35.544  1.00 20.98 ? 38   LYS A CG  1 
ATOM   290  C CD  . LYS A 1 38  ? 13.608  -12.977 37.024  1.00 21.05 ? 38   LYS A CD  1 
ATOM   291  C CE  . LYS A 1 38  ? 13.544  -14.308 37.714  1.00 22.05 ? 38   LYS A CE  1 
ATOM   292  N NZ  . LYS A 1 38  ? 13.625  -14.158 39.179  1.00 21.96 ? 38   LYS A NZ  1 
ATOM   293  N N   . ARG A 1 39  ? 12.278  -13.408 32.259  1.00 25.23 ? 39   ARG A N   1 
ATOM   294  C CA  . ARG A 1 39  ? 11.102  -14.254 31.907  1.00 29.95 ? 39   ARG A CA  1 
ATOM   295  C C   . ARG A 1 39  ? 11.252  -15.652 32.544  1.00 29.56 ? 39   ARG A C   1 
ATOM   296  O O   . ARG A 1 39  ? 12.175  -16.356 32.126  1.00 25.22 ? 39   ARG A O   1 
ATOM   297  C CB  . ARG A 1 39  ? 11.034  -14.354 30.380  1.00 33.12 ? 39   ARG A CB  1 
ATOM   298  C CG  . ARG A 1 39  ? 9.609   -14.292 29.863  1.00 40.52 ? 39   ARG A CG  1 
ATOM   299  C CD  . ARG A 1 39  ? 9.406   -15.071 28.585  1.00 45.98 ? 39   ARG A CD  1 
ATOM   300  N NE  . ARG A 1 39  ? 7.996   -15.322 28.383  1.00 45.70 ? 39   ARG A NE  1 
ATOM   301  C CZ  . ARG A 1 39  ? 7.232   -15.923 29.268  1.00 48.73 ? 39   ARG A CZ  1 
ATOM   302  N NH1 . ARG A 1 39  ? 5.959   -16.130 29.004  1.00 55.36 ? 39   ARG A NH1 1 
ATOM   303  N NH2 . ARG A 1 39  ? 7.743   -16.353 30.407  1.00 53.52 ? 39   ARG A NH2 1 
ATOM   304  N N   . LYS A 1 40  ? 10.316  -16.066 33.396  1.00 32.59 ? 40   LYS A N   1 
ATOM   305  C CA  . LYS A 1 40  ? 10.170  -17.474 33.877  1.00 37.32 ? 40   LYS A CA  1 
ATOM   306  C C   . LYS A 1 40  ? 9.176   -18.181 32.973  1.00 39.68 ? 40   LYS A C   1 
ATOM   307  O O   . LYS A 1 40  ? 8.179   -17.566 32.597  1.00 39.99 ? 40   LYS A O   1 
ATOM   308  C CB  . LYS A 1 40  ? 9.691   -17.606 35.322  1.00 38.50 ? 40   LYS A CB  1 
ATOM   309  C CG  . LYS A 1 40  ? 10.815  -17.792 36.324  1.00 38.26 ? 40   LYS A CG  1 
ATOM   310  C CD  . LYS A 1 40  ? 10.345  -18.253 37.682  1.00 40.95 ? 40   LYS A CD  1 
ATOM   311  C CE  . LYS A 1 40  ? 11.441  -18.215 38.737  1.00 41.76 ? 40   LYS A CE  1 
ATOM   312  N NZ  . LYS A 1 40  ? 12.294  -19.448 38.701  1.00 41.42 ? 40   LYS A NZ  1 
ATOM   313  N N   . PRO A 1 41  ? 9.483   -19.429 32.531  1.00 46.57 ? 41   PRO A N   1 
ATOM   314  C CA  . PRO A 1 41  ? 8.594   -20.249 31.707  1.00 48.89 ? 41   PRO A CA  1 
ATOM   315  C C   . PRO A 1 41  ? 7.107   -20.113 32.040  1.00 48.39 ? 41   PRO A C   1 
ATOM   316  O O   . PRO A 1 41  ? 6.736   -20.305 33.180  1.00 48.33 ? 41   PRO A O   1 
ATOM   317  C CB  . PRO A 1 41  ? 9.045   -21.687 32.041  1.00 49.71 ? 41   PRO A CB  1 
ATOM   318  C CG  . PRO A 1 41  ? 10.526  -21.550 32.267  1.00 50.03 ? 41   PRO A CG  1 
ATOM   319  C CD  . PRO A 1 41  ? 10.738  -20.152 32.813  1.00 49.25 ? 41   PRO A CD  1 
ATOM   320  N N   . GLU A 1 42  ? 6.296   -19.773 31.032  1.00 53.54 ? 42   GLU A N   1 
ATOM   321  C CA  . GLU A 1 42  ? 4.806   -19.742 31.109  1.00 54.23 ? 42   GLU A CA  1 
ATOM   322  C C   . GLU A 1 42  ? 4.348   -18.526 31.934  1.00 51.67 ? 42   GLU A C   1 
ATOM   323  O O   . GLU A 1 42  ? 3.137   -18.404 32.184  1.00 52.62 ? 42   GLU A O   1 
ATOM   324  C CB  . GLU A 1 42  ? 4.208   -21.001 31.774  1.00 60.55 ? 42   GLU A CB  1 
ATOM   325  C CG  . GLU A 1 42  ? 4.928   -22.337 31.560  1.00 64.76 ? 42   GLU A CG  1 
ATOM   326  C CD  . GLU A 1 42  ? 4.816   -23.266 32.770  1.00 67.26 ? 42   GLU A CD  1 
ATOM   327  O OE1 . GLU A 1 42  ? 5.830   -23.937 33.113  1.00 67.28 ? 42   GLU A OE1 1 
ATOM   328  O OE2 . GLU A 1 42  ? 3.718   -23.289 33.392  1.00 68.06 ? 42   GLU A OE2 1 
ATOM   329  N N   . GLN A 1 43  ? 5.276   -17.698 32.415  1.00 48.62 ? 43   GLN A N   1 
ATOM   330  C CA  . GLN A 1 43  ? 4.984   -16.646 33.419  1.00 46.77 ? 43   GLN A CA  1 
ATOM   331  C C   . GLN A 1 43  ? 5.463   -15.301 32.889  1.00 41.37 ? 43   GLN A C   1 
ATOM   332  O O   . GLN A 1 43  ? 6.155   -15.243 31.831  1.00 42.33 ? 43   GLN A O   1 
ATOM   333  C CB  . GLN A 1 43  ? 5.648   -16.960 34.755  1.00 49.20 ? 43   GLN A CB  1 
ATOM   334  C CG  . GLN A 1 43  ? 5.279   -18.355 35.203  1.00 54.16 ? 43   GLN A CG  1 
ATOM   335  C CD  . GLN A 1 43  ? 5.638   -18.569 36.645  1.00 59.53 ? 43   GLN A CD  1 
ATOM   336  O OE1 . GLN A 1 43  ? 6.067   -17.655 37.347  1.00 63.30 ? 43   GLN A OE1 1 
ATOM   337  N NE2 . GLN A 1 43  ? 5.444   -19.798 37.095  1.00 63.98 ? 43   GLN A NE2 1 
ATOM   338  N N   . GLY A 1 44  ? 5.071   -14.259 33.600  1.00 35.62 ? 44   GLY A N   1 
ATOM   339  C CA  . GLY A 1 44  ? 5.086   -12.871 33.119  1.00 34.51 ? 44   GLY A CA  1 
ATOM   340  C C   . GLY A 1 44  ? 6.511   -12.374 33.039  1.00 30.55 ? 44   GLY A C   1 
ATOM   341  O O   . GLY A 1 44  ? 7.405   -13.090 33.453  1.00 35.55 ? 44   GLY A O   1 
ATOM   342  N N   . LEU A 1 45  ? 6.709   -11.278 32.339  1.00 24.91 ? 45   LEU A N   1 
ATOM   343  C CA  . LEU A 1 45  ? 8.010   -10.591 32.240  1.00 23.39 ? 45   LEU A CA  1 
ATOM   344  C C   . LEU A 1 45  ? 8.124   -9.685  33.453  1.00 20.30 ? 45   LEU A C   1 
ATOM   345  O O   . LEU A 1 45  ? 7.098   -9.229  33.959  1.00 18.72 ? 45   LEU A O   1 
ATOM   346  C CB  . LEU A 1 45  ? 7.986   -9.776  30.944  1.00 23.67 ? 45   LEU A CB  1 
ATOM   347  C CG  . LEU A 1 45  ? 8.060   -10.621 29.670  1.00 28.16 ? 45   LEU A CG  1 
ATOM   348  C CD1 . LEU A 1 45  ? 7.394   -9.905  28.488  1.00 29.39 ? 45   LEU A CD1 1 
ATOM   349  C CD2 . LEU A 1 45  ? 9.485   -10.925 29.343  1.00 28.50 ? 45   LEU A CD2 1 
ATOM   350  N N   . GLU A 1 46  ? 9.340   -9.443  33.876  1.00 17.83 ? 46   GLU A N   1 
ATOM   351  C CA  . GLU A 1 46  ? 9.616   -8.510  34.986  1.00 18.83 ? 46   GLU A CA  1 
ATOM   352  C C   . GLU A 1 46  ? 10.778  -7.638  34.560  1.00 17.29 ? 46   GLU A C   1 
ATOM   353  O O   . GLU A 1 46  ? 11.756  -8.194  34.017  1.00 18.34 ? 46   GLU A O   1 
ATOM   354  C CB  . GLU A 1 46  ? 10.077  -9.219  36.246  1.00 20.88 ? 46   GLU A CB  1 
ATOM   355  C CG  . GLU A 1 46  ? 9.024   -9.950  36.957  1.00 24.27 ? 46   GLU A CG  1 
ATOM   356  C CD  . GLU A 1 46  ? 9.601   -10.470 38.261  1.00 27.03 ? 46   GLU A CD  1 
ATOM   357  O OE1 . GLU A 1 46  ? 10.357  -11.439 38.205  1.00 28.39 ? 46   GLU A OE1 1 
ATOM   358  O OE2 . GLU A 1 46  ? 9.405   -9.790  39.280  1.00 30.56 ? 46   GLU A OE2 1 
ATOM   359  N N   . TRP A 1 47  ? 10.693  -6.356  34.819  1.00 16.60 ? 47   TRP A N   1 
ATOM   360  C CA  . TRP A 1 47  ? 11.754  -5.405  34.454  1.00 16.20 ? 47   TRP A CA  1 
ATOM   361  C C   . TRP A 1 47  ? 12.768  -5.349  35.596  1.00 15.68 ? 47   TRP A C   1 
ATOM   362  O O   . TRP A 1 47  ? 12.363  -5.163  36.760  1.00 17.26 ? 47   TRP A O   1 
ATOM   363  C CB  . TRP A 1 47  ? 11.112  -4.051  34.161  1.00 15.53 ? 47   TRP A CB  1 
ATOM   364  C CG  . TRP A 1 47  ? 12.101  -2.973  33.875  1.00 15.33 ? 47   TRP A CG  1 
ATOM   365  C CD1 . TRP A 1 47  ? 12.833  -2.792  32.736  1.00 15.18 ? 47   TRP A CD1 1 
ATOM   366  C CD2 . TRP A 1 47  ? 12.529  -1.958  34.796  1.00 14.88 ? 47   TRP A CD2 1 
ATOM   367  N NE1 . TRP A 1 47  ? 13.597  -1.665  32.861  1.00 14.96 ? 47   TRP A NE1 1 
ATOM   368  C CE2 . TRP A 1 47  ? 13.461  -1.164  34.130  1.00 14.83 ? 47   TRP A CE2 1 
ATOM   369  C CE3 . TRP A 1 47  ? 12.224  -1.651  36.130  1.00 15.24 ? 47   TRP A CE3 1 
ATOM   370  C CZ2 . TRP A 1 47  ? 14.066  -0.069  34.736  1.00 14.78 ? 47   TRP A CZ2 1 
ATOM   371  C CZ3 . TRP A 1 47  ? 12.835  -0.577  36.725  1.00 14.60 ? 47   TRP A CZ3 1 
ATOM   372  C CH2 . TRP A 1 47  ? 13.747  0.204   36.039  1.00 14.81 ? 47   TRP A CH2 1 
ATOM   373  N N   . ILE A 1 48  ? 14.045  -5.460  35.270  1.00 15.06 ? 48   ILE A N   1 
ATOM   374  C CA  . ILE A 1 48  ? 15.143  -5.468  36.276  1.00 14.72 ? 48   ILE A CA  1 
ATOM   375  C C   . ILE A 1 48  ? 15.705  -4.059  36.480  1.00 14.45 ? 48   ILE A C   1 
ATOM   376  O O   . ILE A 1 48  ? 15.924  -3.648  37.642  1.00 14.68 ? 48   ILE A O   1 
ATOM   377  C CB  . ILE A 1 48  ? 16.221  -6.478  35.834  1.00 14.78 ? 48   ILE A CB  1 
ATOM   378  C CG1 . ILE A 1 48  ? 15.653  -7.906  35.824  1.00 14.68 ? 48   ILE A CG1 1 
ATOM   379  C CG2 . ILE A 1 48  ? 17.410  -6.408  36.751  1.00 14.30 ? 48   ILE A CG2 1 
ATOM   380  C CD1 . ILE A 1 48  ? 16.515  -8.923  35.141  1.00 14.73 ? 48   ILE A CD1 1 
ATOM   381  N N   . GLY A 1 49  ? 16.036  -3.365  35.394  1.00 14.71 ? 49   GLY A N   1 
ATOM   382  C CA  . GLY A 1 49  ? 16.686  -2.040  35.436  1.00 13.62 ? 49   GLY A CA  1 
ATOM   383  C C   . GLY A 1 49  ? 17.183  -1.644  34.060  1.00 13.51 ? 49   GLY A C   1 
ATOM   384  O O   . GLY A 1 49  ? 17.052  -2.457  33.103  1.00 12.97 ? 49   GLY A O   1 
ATOM   385  N N   . TYR A 1 50  ? 17.753  -0.470  33.973  1.00 12.95 ? 50   TYR A N   1 
ATOM   386  C CA  . TYR A 1 50  ? 18.437  -0.003  32.752  1.00 13.31 ? 50   TYR A CA  1 
ATOM   387  C C   . TYR A 1 50  ? 19.787  0.538   33.150  1.00 14.13 ? 50   TYR A C   1 
ATOM   388  O O   . TYR A 1 50  ? 19.949  1.068   34.248  1.00 15.37 ? 50   TYR A O   1 
ATOM   389  C CB  . TYR A 1 50  ? 17.574  0.952   31.901  1.00 13.40 ? 50   TYR A CB  1 
ATOM   390  C CG  . TYR A 1 50  ? 17.436  2.361   32.414  1.00 13.45 ? 50   TYR A CG  1 
ATOM   391  C CD1 . TYR A 1 50  ? 18.482  3.295   32.386  1.00 14.28 ? 50   TYR A CD1 1 
ATOM   392  C CD2 . TYR A 1 50  ? 16.247  2.787   32.957  1.00 13.61 ? 50   TYR A CD2 1 
ATOM   393  C CE1 . TYR A 1 50  ? 18.325  4.588   32.909  1.00 14.29 ? 50   TYR A CE1 1 
ATOM   394  C CE2 . TYR A 1 50  ? 16.057  4.098   33.379  1.00 14.30 ? 50   TYR A CE2 1 
ATOM   395  C CZ  . TYR A 1 50  ? 17.106  4.983   33.444  1.00 14.56 ? 50   TYR A CZ  1 
ATOM   396  O OH  . TYR A 1 50  ? 16.899  6.262   33.926  1.00 15.60 ? 50   TYR A OH  1 
ATOM   397  N N   . ILE A 1 51  ? 20.677  0.519   32.166  1.00 15.27 ? 51   ILE A N   1 
ATOM   398  C CA  . ILE A 1 51  ? 21.897  1.348   32.196  1.00 14.98 ? 51   ILE A CA  1 
ATOM   399  C C   . ILE A 1 51  ? 21.894  2.202   30.929  1.00 14.99 ? 51   ILE A C   1 
ATOM   400  O O   . ILE A 1 51  ? 21.635  1.673   29.814  1.00 16.13 ? 51   ILE A O   1 
ATOM   401  C CB  . ILE A 1 51  ? 23.146  0.492   32.345  1.00 15.60 ? 51   ILE A CB  1 
ATOM   402  C CG1 . ILE A 1 51  ? 24.368  1.393   32.381  1.00 16.46 ? 51   ILE A CG1 1 
ATOM   403  C CG2 . ILE A 1 51  ? 23.251  -0.542  31.233  1.00 15.92 ? 51   ILE A CG2 1 
ATOM   404  C CD1 . ILE A 1 51  ? 25.547  0.736   33.048  1.00 17.16 ? 51   ILE A CD1 1 
ATOM   405  N N   . SER A 1 52  ? 22.121  3.488   31.105  1.00 13.88 ? 52   SER A N   1 
ATOM   406  C CA  . SER A 1 52  ? 22.230  4.503   30.037  1.00 14.51 ? 52   SER A CA  1 
ATOM   407  C C   . SER A 1 52  ? 23.703  4.861   29.884  1.00 15.80 ? 52   SER A C   1 
ATOM   408  O O   . SER A 1 52  ? 24.235  5.635   30.685  1.00 17.62 ? 52   SER A O   1 
ATOM   409  C CB  . SER A 1 52  ? 21.403  5.661   30.380  1.00 14.05 ? 52   SER A CB  1 
ATOM   410  O OG  . SER A 1 52  ? 21.344  6.601   29.315  1.00 13.46 ? 52   SER A OG  1 
ATOM   411  N N   . PRO A 1 53  ? 24.425  4.209   28.974  1.00 16.79 ? 53   PRO A N   1 
ATOM   412  C CA  . PRO A 1 53  ? 25.878  4.379   28.929  1.00 18.09 ? 53   PRO A CA  1 
ATOM   413  C C   . PRO A 1 53  ? 26.355  5.794   28.590  1.00 19.35 ? 53   PRO A C   1 
ATOM   414  O O   . PRO A 1 53  ? 27.460  6.175   29.031  1.00 23.20 ? 53   PRO A O   1 
ATOM   415  C CB  . PRO A 1 53  ? 26.353  3.382   27.886  1.00 18.47 ? 53   PRO A CB  1 
ATOM   416  C CG  . PRO A 1 53  ? 25.162  2.775   27.257  1.00 18.40 ? 53   PRO A CG  1 
ATOM   417  C CD  . PRO A 1 53  ? 23.918  3.301   27.937  1.00 17.21 ? 53   PRO A CD  1 
ATOM   418  N N   . GLY A 1 54  ? 25.578  6.557   27.842  1.00 19.10 ? 54   GLY A N   1 
ATOM   419  C CA  . GLY A 1 54  ? 25.937  7.914   27.384  1.00 20.10 ? 54   GLY A CA  1 
ATOM   420  C C   . GLY A 1 54  ? 25.984  8.919   28.526  1.00 20.48 ? 54   GLY A C   1 
ATOM   421  O O   . GLY A 1 54  ? 26.682  9.913   28.374  1.00 22.64 ? 54   GLY A O   1 
ATOM   422  N N   . ASN A 1 55  ? 25.282  8.694   29.642  1.00 19.60 ? 55   ASN A N   1 
ATOM   423  C CA  . ASN A 1 55  ? 25.229  9.686   30.729  1.00 19.59 ? 55   ASN A CA  1 
ATOM   424  C C   . ASN A 1 55  ? 25.443  8.968   32.078  1.00 19.99 ? 55   ASN A C   1 
ATOM   425  O O   . ASN A 1 55  ? 25.195  9.636   33.099  1.00 19.73 ? 55   ASN A O   1 
ATOM   426  C CB  . ASN A 1 55  ? 23.929  10.505  30.651  1.00 19.58 ? 55   ASN A CB  1 
ATOM   427  C CG  . ASN A 1 55  ? 22.686  9.649   30.794  1.00 19.11 ? 55   ASN A CG  1 
ATOM   428  O OD1 . ASN A 1 55  ? 22.792  8.435   30.735  1.00 18.43 ? 55   ASN A OD1 1 
ATOM   429  N ND2 . ASN A 1 55  ? 21.536  10.227  31.062  1.00 19.16 ? 55   ASN A ND2 1 
ATOM   430  N N   . ASP A 1 56  ? 25.838  7.685   32.060  1.00 20.38 ? 56   ASP A N   1 
ATOM   431  C CA  . ASP A 1 56  ? 26.119  6.803   33.213  1.00 21.01 ? 56   ASP A CA  1 
ATOM   432  C C   . ASP A 1 56  ? 24.965  6.819   34.195  1.00 20.28 ? 56   ASP A C   1 
ATOM   433  O O   . ASP A 1 56  ? 25.178  6.721   35.399  1.00 22.55 ? 56   ASP A O   1 
ATOM   434  C CB  . ASP A 1 56  ? 27.342  7.303   33.963  1.00 24.55 ? 56   ASP A CB  1 
ATOM   435  C CG  . ASP A 1 56  ? 28.541  7.420   33.048  1.00 27.97 ? 56   ASP A CG  1 
ATOM   436  O OD1 . ASP A 1 56  ? 29.185  8.470   33.103  1.00 34.89 ? 56   ASP A OD1 1 
ATOM   437  O OD2 . ASP A 1 56  ? 28.807  6.456   32.308  1.00 32.27 ? 56   ASP A OD2 1 
ATOM   438  N N   . ASP A 1 57  A 23.755  6.855   33.707  1.00 18.19 ? 56   ASP A N   1 
ATOM   439  C CA  . ASP A 1 57  A 22.538  6.789   34.538  1.00 17.72 ? 56   ASP A CA  1 
ATOM   440  C C   . ASP A 1 57  A 22.142  5.311   34.679  1.00 17.93 ? 56   ASP A C   1 
ATOM   441  O O   . ASP A 1 57  A 22.027  4.620   33.637  1.00 19.42 ? 56   ASP A O   1 
ATOM   442  C CB  . ASP A 1 57  A 21.475  7.636   33.831  1.00 17.69 ? 56   ASP A CB  1 
ATOM   443  C CG  . ASP A 1 57  A 20.118  7.548   34.510  1.00 18.44 ? 56   ASP A CG  1 
ATOM   444  O OD1 . ASP A 1 57  A 20.110  7.452   35.720  1.00 20.23 ? 56   ASP A OD1 1 
ATOM   445  O OD2 . ASP A 1 57  A 19.098  7.637   33.847  1.00 16.61 ? 56   ASP A OD2 1 
ATOM   446  N N   . ILE A 1 58  ? 21.963  4.799   35.902  1.00 17.35 ? 57   ILE A N   1 
ATOM   447  C CA  . ILE A 1 58  ? 21.581  3.389   36.147  1.00 17.12 ? 57   ILE A CA  1 
ATOM   448  C C   . ILE A 1 58  ? 20.344  3.483   37.016  1.00 17.70 ? 57   ILE A C   1 
ATOM   449  O O   . ILE A 1 58  ? 20.338  4.270   37.970  1.00 18.87 ? 57   ILE A O   1 
ATOM   450  C CB  . ILE A 1 58  ? 22.707  2.559   36.775  1.00 16.91 ? 57   ILE A CB  1 
ATOM   451  C CG1 . ILE A 1 58  ? 23.996  2.641   35.965  1.00 18.29 ? 57   ILE A CG1 1 
ATOM   452  C CG2 . ILE A 1 58  ? 22.325  1.127   36.996  1.00 17.56 ? 57   ILE A CG2 1 
ATOM   453  C CD1 . ILE A 1 58  ? 25.181  2.003   36.639  1.00 18.90 ? 57   ILE A CD1 1 
ATOM   454  N N   . LYS A 1 59  ? 19.330  2.737   36.668  1.00 16.27 ? 58   LYS A N   1 
ATOM   455  C CA  . LYS A 1 59  ? 18.113  2.703   37.477  1.00 16.40 ? 58   LYS A CA  1 
ATOM   456  C C   . LYS A 1 59  ? 17.737  1.247   37.658  1.00 16.06 ? 58   LYS A C   1 
ATOM   457  O O   . LYS A 1 59  ? 17.622  0.528   36.636  1.00 16.91 ? 58   LYS A O   1 
ATOM   458  C CB  . LYS A 1 59  ? 16.983  3.525   36.852  1.00 17.58 ? 58   LYS A CB  1 
ATOM   459  C CG  . LYS A 1 59  ? 15.695  3.507   37.652  1.00 19.21 ? 58   LYS A CG  1 
ATOM   460  C CD  . LYS A 1 59  ? 14.755  4.630   37.176  1.00 22.78 ? 58   LYS A CD  1 
ATOM   461  C CE  . LYS A 1 59  ? 13.612  4.823   38.145  1.00 26.39 ? 58   LYS A CE  1 
ATOM   462  N NZ  . LYS A 1 59  ? 14.011  5.480   39.431  1.00 28.71 ? 58   LYS A NZ  1 
ATOM   463  N N   . TYR A 1 60  ? 17.385  0.894   38.903  1.00 15.59 ? 59   TYR A N   1 
ATOM   464  C CA  . TYR A 1 60  ? 16.969  -0.461  39.287  1.00 15.80 ? 59   TYR A CA  1 
ATOM   465  C C   . TYR A 1 60  ? 15.501  -0.491  39.665  1.00 15.72 ? 59   TYR A C   1 
ATOM   466  O O   . TYR A 1 60  ? 14.952  0.479   40.224  1.00 16.50 ? 59   TYR A O   1 
ATOM   467  C CB  . TYR A 1 60  ? 17.770  -0.999  40.470  1.00 15.78 ? 59   TYR A CB  1 
ATOM   468  C CG  . TYR A 1 60  ? 19.208  -1.225  40.108  1.00 15.12 ? 59   TYR A CG  1 
ATOM   469  C CD1 . TYR A 1 60  ? 20.143  -0.240  40.344  1.00 15.76 ? 59   TYR A CD1 1 
ATOM   470  C CD2 . TYR A 1 60  ? 19.632  -2.389  39.521  1.00 14.98 ? 59   TYR A CD2 1 
ATOM   471  C CE1 . TYR A 1 60  ? 21.479  -0.407  39.985  1.00 15.38 ? 59   TYR A CE1 1 
ATOM   472  C CE2 . TYR A 1 60  ? 20.957  -2.573  39.150  1.00 15.10 ? 59   TYR A CE2 1 
ATOM   473  C CZ  . TYR A 1 60  ? 21.894  -1.612  39.464  1.00 14.72 ? 59   TYR A CZ  1 
ATOM   474  O OH  . TYR A 1 60  ? 23.196  -1.780  39.123  1.00 13.75 ? 59   TYR A OH  1 
ATOM   475  N N   . ASN A 1 61  ? 14.907  -1.629  39.358  1.00 15.77 ? 60   ASN A N   1 
ATOM   476  C CA  . ASN A 1 61  ? 13.670  -2.092  40.044  1.00 15.98 ? 60   ASN A CA  1 
ATOM   477  C C   . ASN A 1 61  ? 14.103  -2.411  41.481  1.00 16.51 ? 60   ASN A C   1 
ATOM   478  O O   . ASN A 1 61  ? 15.026  -3.250  41.633  1.00 15.49 ? 60   ASN A O   1 
ATOM   479  C CB  . ASN A 1 61  ? 13.108  -3.343  39.362  1.00 15.39 ? 60   ASN A CB  1 
ATOM   480  C CG  . ASN A 1 61  ? 11.739  -3.748  39.874  1.00 15.33 ? 60   ASN A CG  1 
ATOM   481  O OD1 . ASN A 1 61  ? 11.339  -3.394  41.002  1.00 15.36 ? 60   ASN A OD1 1 
ATOM   482  N ND2 . ASN A 1 61  ? 11.056  -4.570  39.075  1.00 15.47 ? 60   ASN A ND2 1 
ATOM   483  N N   . GLU A 1 62  ? 13.482  -1.773  42.490  1.00 17.36 ? 61   GLU A N   1 
ATOM   484  C CA  . GLU A 1 62  ? 13.774  -2.019  43.944  1.00 19.23 ? 61   GLU A CA  1 
ATOM   485  C C   . GLU A 1 62  ? 13.764  -3.523  44.222  1.00 19.12 ? 61   GLU A C   1 
ATOM   486  O O   . GLU A 1 62  ? 14.596  -3.977  45.009  1.00 19.37 ? 61   GLU A O   1 
ATOM   487  C CB  . GLU A 1 62  ? 12.725  -1.258  44.750  1.00 22.08 ? 61   GLU A CB  1 
ATOM   488  C CG  . GLU A 1 62  ? 13.015  -1.138  46.231  1.00 26.84 ? 61   GLU A CG  1 
ATOM   489  C CD  . GLU A 1 62  ? 14.146  -0.197  46.600  1.00 28.87 ? 61   GLU A CD  1 
ATOM   490  O OE1 . GLU A 1 62  ? 14.353  0.845   45.889  1.00 30.09 ? 61   GLU A OE1 1 
ATOM   491  O OE2 . GLU A 1 62  ? 14.748  -0.455  47.702  1.00 32.56 ? 61   GLU A OE2 1 
ATOM   492  N N   . LYS A 1 63  ? 12.910  -4.289  43.541  1.00 18.62 ? 62   LYS A N   1 
ATOM   493  C CA  . LYS A 1 63  ? 12.763  -5.730  43.733  1.00 20.33 ? 62   LYS A CA  1 
ATOM   494  C C   . LYS A 1 63  ? 14.107  -6.428  43.461  1.00 18.23 ? 62   LYS A C   1 
ATOM   495  O O   . LYS A 1 63  ? 14.335  -7.485  44.029  1.00 17.87 ? 62   LYS A O   1 
ATOM   496  C CB  . LYS A 1 63  ? 11.661  -6.215  42.800  1.00 22.20 ? 62   LYS A CB  1 
ATOM   497  C CG  . LYS A 1 63  ? 11.407  -7.701  42.755  1.00 25.88 ? 62   LYS A CG  1 
ATOM   498  C CD  . LYS A 1 63  ? 10.039  -7.944  42.097  1.00 27.32 ? 62   LYS A CD  1 
ATOM   499  C CE  . LYS A 1 63  ? 9.367   -9.280  42.332  1.00 32.12 ? 62   LYS A CE  1 
ATOM   500  N NZ  . LYS A 1 63  ? 10.277  -10.412 42.066  1.00 36.83 ? 62   LYS A NZ  1 
ATOM   501  N N   . PHE A 1 64  ? 14.916  -5.924  42.545  1.00 17.57 ? 63   PHE A N   1 
ATOM   502  C CA  . PHE A 1 64  ? 16.186  -6.580  42.133  1.00 17.08 ? 63   PHE A CA  1 
ATOM   503  C C   . PHE A 1 64  ? 17.426  -5.922  42.763  1.00 16.54 ? 63   PHE A C   1 
ATOM   504  O O   . PHE A 1 64  ? 18.557  -6.360  42.487  1.00 16.32 ? 63   PHE A O   1 
ATOM   505  C CB  . PHE A 1 64  ? 16.311  -6.609  40.606  1.00 17.04 ? 63   PHE A CB  1 
ATOM   506  C CG  . PHE A 1 64  ? 15.389  -7.611  39.961  1.00 17.45 ? 63   PHE A CG  1 
ATOM   507  C CD1 . PHE A 1 64  ? 14.066  -7.272  39.628  1.00 18.22 ? 63   PHE A CD1 1 
ATOM   508  C CD2 . PHE A 1 64  ? 15.792  -8.925  39.756  1.00 18.59 ? 63   PHE A CD2 1 
ATOM   509  C CE1 . PHE A 1 64  ? 13.218  -8.210  39.052  1.00 18.30 ? 63   PHE A CE1 1 
ATOM   510  C CE2 . PHE A 1 64  ? 14.927  -9.868  39.244  1.00 18.39 ? 63   PHE A CE2 1 
ATOM   511  C CZ  . PHE A 1 64  ? 13.664  -9.500  38.839  1.00 19.36 ? 63   PHE A CZ  1 
ATOM   512  N N   . LYS A 1 65  ? 17.270  -4.867  43.564  1.00 17.27 ? 64   LYS A N   1 
ATOM   513  C CA  . LYS A 1 65  ? 18.421  -4.314  44.308  1.00 17.39 ? 64   LYS A CA  1 
ATOM   514  C C   . LYS A 1 65  ? 18.952  -5.374  45.285  1.00 17.23 ? 64   LYS A C   1 
ATOM   515  O O   . LYS A 1 65  ? 18.166  -6.008  45.980  1.00 15.89 ? 64   LYS A O   1 
ATOM   516  C CB  . LYS A 1 65  ? 18.068  -3.030  45.045  1.00 18.40 ? 64   LYS A CB  1 
ATOM   517  C CG  . LYS A 1 65  ? 17.767  -1.846  44.132  1.00 20.09 ? 64   LYS A CG  1 
ATOM   518  C CD  . LYS A 1 65  ? 17.445  -0.567  44.908  1.00 23.25 ? 64   LYS A CD  1 
ATOM   519  C CE  . LYS A 1 65  ? 17.895  0.720   44.249  1.00 26.69 ? 64   LYS A CE  1 
ATOM   520  N NZ  . LYS A 1 65  ? 17.161  1.885   44.805  1.00 29.57 ? 64   LYS A NZ  1 
ATOM   521  N N   . GLY A 1 66  ? 20.274  -5.583  45.306  1.00 17.41 ? 65   GLY A N   1 
ATOM   522  C CA  . GLY A 1 66  ? 20.822  -6.667  46.128  1.00 17.82 ? 65   GLY A CA  1 
ATOM   523  C C   . GLY A 1 66  ? 20.903  -7.997  45.405  1.00 18.31 ? 65   GLY A C   1 
ATOM   524  O O   . GLY A 1 66  ? 21.427  -8.956  45.991  1.00 19.56 ? 65   GLY A O   1 
ATOM   525  N N   . LYS A 1 67  ? 20.453  -8.052  44.162  1.00 17.76 ? 66   LYS A N   1 
ATOM   526  C CA  . LYS A 1 67  ? 20.461  -9.258  43.325  1.00 17.92 ? 66   LYS A CA  1 
ATOM   527  C C   . LYS A 1 67  ? 21.131  -8.983  41.978  1.00 17.57 ? 66   LYS A C   1 
ATOM   528  O O   . LYS A 1 67  ? 21.780  -9.893  41.447  1.00 18.37 ? 66   LYS A O   1 
ATOM   529  C CB  . LYS A 1 67  ? 19.028  -9.734  43.145  1.00 19.20 ? 66   LYS A CB  1 
ATOM   530  C CG  . LYS A 1 67  ? 18.868  -10.887 42.178  1.00 20.42 ? 66   LYS A CG  1 
ATOM   531  C CD  . LYS A 1 67  ? 19.533  -12.149 42.636  1.00 21.70 ? 66   LYS A CD  1 
ATOM   532  C CE  . LYS A 1 67  ? 19.049  -12.605 43.999  1.00 21.96 ? 66   LYS A CE  1 
ATOM   533  N NZ  . LYS A 1 67  ? 19.396  -14.019 44.223  1.00 22.51 ? 66   LYS A NZ  1 
ATOM   534  N N   . ALA A 1 68  ? 20.849  -7.843  41.375  1.00 16.00 ? 67   ALA A N   1 
ATOM   535  C CA  . ALA A 1 68  ? 21.354  -7.500  40.032  1.00 16.64 ? 67   ALA A CA  1 
ATOM   536  C C   . ALA A 1 68  ? 22.277  -6.298  40.091  1.00 16.14 ? 67   ALA A C   1 
ATOM   537  O O   . ALA A 1 68  ? 22.023  -5.324  40.820  1.00 16.74 ? 67   ALA A O   1 
ATOM   538  C CB  . ALA A 1 68  ? 20.182  -7.232  39.109  1.00 16.16 ? 67   ALA A CB  1 
ATOM   539  N N   . THR A 1 69  ? 23.342  -6.340  39.305  1.00 17.05 ? 68   THR A N   1 
ATOM   540  C CA  . THR A 1 69  ? 24.221  -5.174  39.123  1.00 17.30 ? 68   THR A CA  1 
ATOM   541  C C   . THR A 1 69  ? 24.468  -4.934  37.639  1.00 16.37 ? 68   THR A C   1 
ATOM   542  O O   . THR A 1 69  ? 24.892  -5.845  36.950  1.00 16.69 ? 68   THR A O   1 
ATOM   543  C CB  . THR A 1 69  ? 25.537  -5.325  39.901  1.00 18.74 ? 68   THR A CB  1 
ATOM   544  O OG1 . THR A 1 69  ? 25.302  -5.568  41.292  1.00 18.95 ? 68   THR A OG1 1 
ATOM   545  C CG2 . THR A 1 69  ? 26.382  -4.077  39.797  1.00 18.72 ? 68   THR A CG2 1 
ATOM   546  N N   . LEU A 1 70  ? 24.123  -3.749  37.134  1.00 16.70 ? 69   LEU A N   1 
ATOM   547  C CA  . LEU A 1 70  ? 24.287  -3.417  35.703  1.00 16.24 ? 69   LEU A CA  1 
ATOM   548  C C   . LEU A 1 70  ? 25.537  -2.578  35.497  1.00 16.24 ? 69   LEU A C   1 
ATOM   549  O O   . LEU A 1 70  ? 25.766  -1.574  36.249  1.00 17.99 ? 69   LEU A O   1 
ATOM   550  C CB  . LEU A 1 70  ? 23.074  -2.641  35.168  1.00 15.30 ? 69   LEU A CB  1 
ATOM   551  C CG  . LEU A 1 70  ? 21.730  -3.257  35.511  1.00 15.37 ? 69   LEU A CG  1 
ATOM   552  C CD1 . LEU A 1 70  ? 20.589  -2.434  34.903  1.00 16.55 ? 69   LEU A CD1 1 
ATOM   553  C CD2 . LEU A 1 70  ? 21.665  -4.680  35.027  1.00 15.64 ? 69   LEU A CD2 1 
ATOM   554  N N   . THR A 1 71  ? 26.314  -2.955  34.515  1.00 17.18 ? 70   THR A N   1 
ATOM   555  C CA  . THR A 1 71  ? 27.480  -2.163  34.095  1.00 17.54 ? 70   THR A CA  1 
ATOM   556  C C   . THR A 1 71  ? 27.465  -2.097  32.572  1.00 17.51 ? 70   THR A C   1 
ATOM   557  O O   . THR A 1 71  ? 26.694  -2.842  31.909  1.00 16.59 ? 70   THR A O   1 
ATOM   558  C CB  . THR A 1 71  ? 28.779  -2.765  34.655  1.00 18.29 ? 70   THR A CB  1 
ATOM   559  O OG1 . THR A 1 71  ? 28.820  -4.113  34.220  1.00 17.43 ? 70   THR A OG1 1 
ATOM   560  C CG2 . THR A 1 71  ? 28.857  -2.725  36.156  1.00 19.77 ? 70   THR A CG2 1 
ATOM   561  N N   . ALA A 1 72  ? 28.309  -1.248  32.017  1.00 18.19 ? 71   ALA A N   1 
ATOM   562  C CA  . ALA A 1 72  ? 28.473  -1.133  30.557  1.00 17.97 ? 71   ALA A CA  1 
ATOM   563  C C   . ALA A 1 72  ? 29.908  -0.751  30.236  1.00 19.53 ? 71   ALA A C   1 
ATOM   564  O O   . ALA A 1 72  ? 30.508  0.059   30.948  1.00 19.45 ? 71   ALA A O   1 
ATOM   565  C CB  . ALA A 1 72  ? 27.510  -0.154  29.983  1.00 18.02 ? 71   ALA A CB  1 
ATOM   566  N N   . ASP A 1 73  ? 30.450  -1.403  29.233  1.00 19.69 ? 72   ASP A N   1 
ATOM   567  C CA  . ASP A 1 73  ? 31.845  -1.168  28.796  1.00 21.18 ? 72   ASP A CA  1 
ATOM   568  C C   . ASP A 1 73  ? 31.758  -0.423  27.468  1.00 20.01 ? 72   ASP A C   1 
ATOM   569  O O   . ASP A 1 73  ? 31.423  -1.037  26.479  1.00 18.65 ? 72   ASP A O   1 
ATOM   570  C CB  . ASP A 1 73  ? 32.512  -2.515  28.635  1.00 24.85 ? 72   ASP A CB  1 
ATOM   571  C CG  . ASP A 1 73  ? 33.939  -2.435  28.186  1.00 28.99 ? 72   ASP A CG  1 
ATOM   572  O OD1 . ASP A 1 73  ? 34.326  -1.319  27.746  1.00 31.42 ? 72   ASP A OD1 1 
ATOM   573  O OD2 . ASP A 1 73  ? 34.626  -3.519  28.235  1.00 34.77 ? 72   ASP A OD2 1 
ATOM   574  N N   . LYS A 1 74  ? 31.935  0.879   27.450  1.00 19.65 ? 73   LYS A N   1 
ATOM   575  C CA  . LYS A 1 74  ? 31.847  1.617   26.185  1.00 22.05 ? 73   LYS A CA  1 
ATOM   576  C C   . LYS A 1 74  ? 32.935  1.149   25.217  1.00 20.73 ? 73   LYS A C   1 
ATOM   577  O O   . LYS A 1 74  ? 32.686  1.269   24.007  1.00 20.53 ? 73   LYS A O   1 
ATOM   578  C CB  . LYS A 1 74  ? 31.968  3.134   26.359  1.00 26.44 ? 73   LYS A CB  1 
ATOM   579  C CG  . LYS A 1 74  ? 30.688  3.797   26.857  1.00 30.05 ? 73   LYS A CG  1 
ATOM   580  C CD  . LYS A 1 74  ? 30.776  4.382   28.232  1.00 37.65 ? 73   LYS A CD  1 
ATOM   581  C CE  . LYS A 1 74  ? 31.135  5.854   28.295  1.00 40.98 ? 73   LYS A CE  1 
ATOM   582  N NZ  . LYS A 1 74  ? 30.089  6.599   29.057  1.00 45.50 ? 73   LYS A NZ  1 
ATOM   583  N N   . SER A 1 75  ? 34.055  0.622   25.702  1.00 19.03 ? 74   SER A N   1 
ATOM   584  C CA  . SER A 1 75  ? 35.164  0.212   24.815  1.00 18.16 ? 74   SER A CA  1 
ATOM   585  C C   . SER A 1 75  ? 34.720  -0.956  23.924  1.00 18.03 ? 74   SER A C   1 
ATOM   586  O O   . SER A 1 75  ? 35.283  -1.082  22.828  1.00 17.52 ? 74   SER A O   1 
ATOM   587  C CB  . SER A 1 75  ? 36.430  -0.079  25.610  1.00 18.39 ? 74   SER A CB  1 
ATOM   588  O OG  . SER A 1 75  ? 36.357  -1.288  26.362  1.00 17.65 ? 74   SER A OG  1 
ATOM   589  N N   . SER A 1 76  ? 33.745  -1.761  24.359  1.00 17.46 ? 75   SER A N   1 
ATOM   590  C CA  . SER A 1 76  ? 33.314  -3.000  23.685  1.00 17.71 ? 75   SER A CA  1 
ATOM   591  C C   . SER A 1 76  ? 31.838  -2.873  23.286  1.00 18.24 ? 75   SER A C   1 
ATOM   592  O O   . SER A 1 76  ? 31.338  -3.858  22.744  1.00 18.42 ? 75   SER A O   1 
ATOM   593  C CB  . SER A 1 76  ? 33.517  -4.210  24.546  1.00 18.36 ? 75   SER A CB  1 
ATOM   594  O OG  . SER A 1 76  ? 32.683  -4.150  25.693  1.00 17.12 ? 75   SER A OG  1 
ATOM   595  N N   . SER A 1 77  ? 31.196  -1.764  23.594  1.00 17.36 ? 76   SER A N   1 
ATOM   596  C CA  . SER A 1 77  ? 29.735  -1.560  23.367  1.00 18.23 ? 76   SER A CA  1 
ATOM   597  C C   . SER A 1 77  ? 28.990  -2.740  23.970  1.00 17.45 ? 76   SER A C   1 
ATOM   598  O O   . SER A 1 77  ? 28.049  -3.276  23.360  1.00 17.28 ? 76   SER A O   1 
ATOM   599  C CB  . SER A 1 77  ? 29.422  -1.364  21.919  1.00 19.75 ? 76   SER A CB  1 
ATOM   600  O OG  . SER A 1 77  ? 30.081  -0.224  21.403  1.00 21.50 ? 76   SER A OG  1 
ATOM   601  N N   . THR A 1 78  ? 29.379  -3.149  25.178  1.00 17.77 ? 77   THR A N   1 
ATOM   602  C CA  . THR A 1 78  ? 28.765  -4.314  25.858  1.00 17.53 ? 77   THR A CA  1 
ATOM   603  C C   . THR A 1 78  ? 28.144  -3.874  27.167  1.00 16.99 ? 77   THR A C   1 
ATOM   604  O O   . THR A 1 78  ? 28.810  -3.173  27.991  1.00 16.61 ? 77   THR A O   1 
ATOM   605  C CB  . THR A 1 78  ? 29.749  -5.475  26.015  1.00 18.46 ? 77   THR A CB  1 
ATOM   606  O OG1 . THR A 1 78  ? 30.246  -5.829  24.724  1.00 19.20 ? 77   THR A OG1 1 
ATOM   607  C CG2 . THR A 1 78  ? 29.126  -6.715  26.589  1.00 18.41 ? 77   THR A CG2 1 
ATOM   608  N N   . ALA A 1 79  ? 26.901  -4.282  27.353  1.00 15.89 ? 78   ALA A N   1 
ATOM   609  C CA  . ALA A 1 79  ? 26.209  -4.144  28.646  1.00 16.01 ? 78   ALA A CA  1 
ATOM   610  C C   . ALA A 1 79  ? 26.290  -5.490  29.364  1.00 16.19 ? 78   ALA A C   1 
ATOM   611  O O   . ALA A 1 79  ? 26.243  -6.546  28.693  1.00 17.82 ? 78   ALA A O   1 
ATOM   612  C CB  . ALA A 1 79  ? 24.774  -3.731  28.428  1.00 15.84 ? 78   ALA A CB  1 
ATOM   613  N N   . TYR A 1 80  ? 26.420  -5.437  30.674  1.00 16.79 ? 79   TYR A N   1 
ATOM   614  C CA  . TYR A 1 80  ? 26.529  -6.606  31.562  1.00 16.17 ? 79   TYR A CA  1 
ATOM   615  C C   . TYR A 1 80  ? 25.501  -6.515  32.668  1.00 15.92 ? 79   TYR A C   1 
ATOM   616  O O   . TYR A 1 80  ? 25.247  -5.444  33.232  1.00 16.93 ? 79   TYR A O   1 
ATOM   617  C CB  . TYR A 1 80  ? 27.919  -6.687  32.199  1.00 16.73 ? 79   TYR A CB  1 
ATOM   618  C CG  . TYR A 1 80  ? 29.044  -6.875  31.239  1.00 18.23 ? 79   TYR A CG  1 
ATOM   619  C CD1 . TYR A 1 80  ? 29.768  -5.790  30.765  1.00 19.37 ? 79   TYR A CD1 1 
ATOM   620  C CD2 . TYR A 1 80  ? 29.366  -8.131  30.790  1.00 19.39 ? 79   TYR A CD2 1 
ATOM   621  C CE1 . TYR A 1 80  ? 30.801  -5.960  29.866  1.00 20.00 ? 79   TYR A CE1 1 
ATOM   622  C CE2 . TYR A 1 80  ? 30.384  -8.311  29.888  1.00 19.77 ? 79   TYR A CE2 1 
ATOM   623  C CZ  . TYR A 1 80  ? 31.099  -7.235  29.426  1.00 19.54 ? 79   TYR A CZ  1 
ATOM   624  O OH  . TYR A 1 80  ? 32.102  -7.495  28.555  1.00 19.29 ? 79   TYR A OH  1 
ATOM   625  N N   . MET A 1 81  ? 24.928  -7.663  32.986  1.00 16.43 ? 80   MET A N   1 
ATOM   626  C CA  . MET A 1 81  ? 24.105  -7.836  34.186  1.00 16.78 ? 80   MET A CA  1 
ATOM   627  C C   . MET A 1 81  ? 24.712  -8.956  35.030  1.00 17.05 ? 80   MET A C   1 
ATOM   628  O O   . MET A 1 81  ? 24.762  -10.121 34.578  1.00 15.99 ? 80   MET A O   1 
ATOM   629  C CB  . MET A 1 81  ? 22.655  -8.179  33.839  1.00 17.08 ? 80   MET A CB  1 
ATOM   630  C CG  . MET A 1 81  ? 21.905  -8.401  35.097  1.00 18.57 ? 80   MET A CG  1 
ATOM   631  S SD  . MET A 1 81  ? 20.186  -8.629  34.798  1.00 21.59 ? 80   MET A SD  1 
ATOM   632  C CE  . MET A 1 81  ? 20.209  -10.174 33.948  1.00 20.53 ? 80   MET A CE  1 
ATOM   633  N N   . GLN A 1 82  ? 25.184  -8.597  36.226  1.00 18.89 ? 81   GLN A N   1 
ATOM   634  C CA  . GLN A 1 82  ? 25.681  -9.613  37.189  1.00 19.57 ? 81   GLN A CA  1 
ATOM   635  C C   . GLN A 1 82  ? 24.534  -9.924  38.159  1.00 18.24 ? 81   GLN A C   1 
ATOM   636  O O   . GLN A 1 82  ? 23.966  -8.986  38.720  1.00 18.17 ? 81   GLN A O   1 
ATOM   637  C CB  . GLN A 1 82  ? 26.903  -9.098  37.918  1.00 22.22 ? 81   GLN A CB  1 
ATOM   638  C CG  . GLN A 1 82  ? 27.501  -10.161 38.820  1.00 26.56 ? 81   GLN A CG  1 
ATOM   639  C CD  . GLN A 1 82  ? 28.764  -9.660  39.482  1.00 34.19 ? 81   GLN A CD  1 
ATOM   640  O OE1 . GLN A 1 82  ? 29.184  -8.517  39.318  1.00 41.24 ? 81   GLN A OE1 1 
ATOM   641  N NE2 . GLN A 1 82  ? 29.366  -10.516 40.286  1.00 38.51 ? 81   GLN A NE2 1 
ATOM   642  N N   . LEU A 1 83  ? 24.228  -11.190 38.324  1.00 17.84 ? 82   LEU A N   1 
ATOM   643  C CA  . LEU A 1 83  ? 23.263  -11.667 39.332  1.00 18.28 ? 82   LEU A CA  1 
ATOM   644  C C   . LEU A 1 83  ? 24.006  -12.390 40.441  1.00 18.54 ? 82   LEU A C   1 
ATOM   645  O O   . LEU A 1 83  ? 24.773  -13.294 40.115  1.00 20.34 ? 82   LEU A O   1 
ATOM   646  C CB  . LEU A 1 83  ? 22.269  -12.578 38.649  1.00 18.32 ? 82   LEU A CB  1 
ATOM   647  C CG  . LEU A 1 83  ? 21.426  -11.917 37.548  1.00 18.73 ? 82   LEU A CG  1 
ATOM   648  C CD1 . LEU A 1 83  ? 20.720  -12.987 36.725  1.00 19.72 ? 82   LEU A CD1 1 
ATOM   649  C CD2 . LEU A 1 83  ? 20.435  -10.954 38.172  1.00 19.06 ? 82   LEU A CD2 1 
ATOM   650  N N   . ASN A 1 84  A 23.803  -11.956 41.680  1.00 18.67 ? 82   ASN A N   1 
ATOM   651  C CA  . ASN A 1 84  A 24.603  -12.475 42.837  1.00 19.39 ? 82   ASN A CA  1 
ATOM   652  C C   . ASN A 1 84  A 23.716  -13.371 43.692  1.00 19.66 ? 82   ASN A C   1 
ATOM   653  O O   . ASN A 1 84  A 22.482  -13.263 43.619  1.00 19.39 ? 82   ASN A O   1 
ATOM   654  C CB  . ASN A 1 84  A 25.230  -11.371 43.718  1.00 20.10 ? 82   ASN A CB  1 
ATOM   655  C CG  . ASN A 1 84  A 24.210  -10.414 44.306  1.00 19.65 ? 82   ASN A CG  1 
ATOM   656  O OD1 . ASN A 1 84  A 23.783  -10.558 45.463  1.00 20.46 ? 82   ASN A OD1 1 
ATOM   657  N ND2 . ASN A 1 84  A 23.867  -9.387  43.546  1.00 18.40 ? 82   ASN A ND2 1 
ATOM   658  N N   . SER A 1 85  B 24.357  -14.218 44.495  1.00 19.38 ? 82   SER A N   1 
ATOM   659  C CA  . SER A 1 85  B 23.706  -14.923 45.611  1.00 19.67 ? 82   SER A CA  1 
ATOM   660  C C   . SER A 1 85  B 22.547  -15.770 45.067  1.00 19.47 ? 82   SER A C   1 
ATOM   661  O O   . SER A 1 85  B 21.408  -15.669 45.543  1.00 18.90 ? 82   SER A O   1 
ATOM   662  C CB  . SER A 1 85  B 23.284  -13.941 46.669  1.00 19.71 ? 82   SER A CB  1 
ATOM   663  O OG  . SER A 1 85  B 24.309  -13.012 46.978  1.00 19.55 ? 82   SER A OG  1 
ATOM   664  N N   . LEU A 1 86  C 22.832  -16.608 44.085  1.00 19.51 ? 82   LEU A N   1 
ATOM   665  C CA  . LEU A 1 86  C 21.763  -17.200 43.233  1.00 20.51 ? 82   LEU A CA  1 
ATOM   666  C C   . LEU A 1 86  C 20.989  -18.309 43.947  1.00 21.32 ? 82   LEU A C   1 
ATOM   667  O O   . LEU A 1 86  C 21.583  -19.050 44.756  1.00 23.65 ? 82   LEU A O   1 
ATOM   668  C CB  . LEU A 1 86  C 22.393  -17.710 41.946  1.00 21.32 ? 82   LEU A CB  1 
ATOM   669  C CG  . LEU A 1 86  C 22.895  -16.621 40.978  1.00 21.41 ? 82   LEU A CG  1 
ATOM   670  C CD1 . LEU A 1 86  C 23.656  -17.279 39.853  1.00 21.74 ? 82   LEU A CD1 1 
ATOM   671  C CD2 . LEU A 1 86  C 21.757  -15.792 40.430  1.00 22.12 ? 82   LEU A CD2 1 
ATOM   672  N N   . THR A 1 87  ? 19.692  -18.386 43.692  1.00 22.06 ? 83   THR A N   1 
ATOM   673  C CA  . THR A 1 87  ? 18.775  -19.466 44.125  1.00 24.86 ? 83   THR A CA  1 
ATOM   674  C C   . THR A 1 87  ? 17.993  -19.982 42.919  1.00 24.52 ? 83   THR A C   1 
ATOM   675  O O   . THR A 1 87  ? 18.047  -19.359 41.831  1.00 23.06 ? 83   THR A O   1 
ATOM   676  C CB  . THR A 1 87  ? 17.785  -18.963 45.174  1.00 24.52 ? 83   THR A CB  1 
ATOM   677  O OG1 . THR A 1 87  ? 16.833  -18.133 44.507  1.00 26.14 ? 83   THR A OG1 1 
ATOM   678  C CG2 . THR A 1 87  ? 18.478  -18.151 46.248  1.00 24.30 ? 83   THR A CG2 1 
ATOM   679  N N   . SER A 1 88  ? 17.224  -21.047 43.127  1.00 26.08 ? 84   SER A N   1 
ATOM   680  C CA  . SER A 1 88  ? 16.330  -21.592 42.074  1.00 26.18 ? 84   SER A CA  1 
ATOM   681  C C   . SER A 1 88  ? 15.379  -20.498 41.592  1.00 25.76 ? 84   SER A C   1 
ATOM   682  O O   . SER A 1 88  ? 14.930  -20.594 40.436  1.00 23.96 ? 84   SER A O   1 
ATOM   683  C CB  . SER A 1 88  ? 15.572  -22.779 42.592  1.00 29.33 ? 84   SER A CB  1 
ATOM   684  O OG  . SER A 1 88  ? 14.879  -22.405 43.764  1.00 32.23 ? 84   SER A OG  1 
ATOM   685  N N   . GLU A 1 89  ? 15.008  -19.537 42.454  1.00 27.20 ? 85   GLU A N   1 
ATOM   686  C CA  . GLU A 1 89  ? 14.037  -18.470 42.082  1.00 27.69 ? 85   GLU A CA  1 
ATOM   687  C C   . GLU A 1 89  ? 14.668  -17.580 41.003  1.00 24.56 ? 85   GLU A C   1 
ATOM   688  O O   . GLU A 1 89  ? 13.880  -16.896 40.326  1.00 25.72 ? 85   GLU A O   1 
ATOM   689  C CB  . GLU A 1 89  ? 13.592  -17.666 43.310  1.00 32.48 ? 85   GLU A CB  1 
ATOM   690  C CG  . GLU A 1 89  ? 12.639  -18.454 44.210  1.00 37.97 ? 85   GLU A CG  1 
ATOM   691  C CD  . GLU A 1 89  ? 12.392  -17.892 45.606  1.00 45.57 ? 85   GLU A CD  1 
ATOM   692  O OE1 . GLU A 1 89  ? 11.284  -18.158 46.163  1.00 51.42 ? 85   GLU A OE1 1 
ATOM   693  O OE2 . GLU A 1 89  ? 13.277  -17.151 46.148  1.00 52.90 ? 85   GLU A OE2 1 
ATOM   694  N N   . ASP A 1 90  ? 15.987  -17.651 40.782  1.00 21.59 ? 86   ASP A N   1 
ATOM   695  C CA  . ASP A 1 90  ? 16.716  -16.876 39.738  1.00 20.99 ? 86   ASP A CA  1 
ATOM   696  C C   . ASP A 1 90  ? 16.754  -17.598 38.382  1.00 21.03 ? 86   ASP A C   1 
ATOM   697  O O   . ASP A 1 90  ? 17.064  -16.962 37.402  1.00 20.76 ? 86   ASP A O   1 
ATOM   698  C CB  . ASP A 1 90  ? 18.127  -16.539 40.205  1.00 20.55 ? 86   ASP A CB  1 
ATOM   699  C CG  . ASP A 1 90  ? 18.078  -15.642 41.439  1.00 20.79 ? 86   ASP A CG  1 
ATOM   700  O OD1 . ASP A 1 90  ? 17.294  -14.674 41.447  1.00 21.06 ? 86   ASP A OD1 1 
ATOM   701  O OD2 . ASP A 1 90  ? 18.768  -15.969 42.407  1.00 21.26 ? 86   ASP A OD2 1 
ATOM   702  N N   . SER A 1 91  ? 16.466  -18.902 38.341  1.00 21.68 ? 87   SER A N   1 
ATOM   703  C CA  . SER A 1 91  ? 16.331  -19.674 37.085  1.00 21.56 ? 87   SER A CA  1 
ATOM   704  C C   . SER A 1 91  ? 15.277  -19.003 36.205  1.00 21.43 ? 87   SER A C   1 
ATOM   705  O O   . SER A 1 91  ? 14.135  -18.853 36.626  1.00 22.85 ? 87   SER A O   1 
ATOM   706  C CB  . SER A 1 91  ? 16.004  -21.125 37.365  1.00 23.25 ? 87   SER A CB  1 
ATOM   707  O OG  . SER A 1 91  ? 17.077  -21.690 38.093  1.00 23.90 ? 87   SER A OG  1 
ATOM   708  N N   . ALA A 1 92  ? 15.687  -18.562 35.037  1.00 21.57 ? 88   ALA A N   1 
ATOM   709  C CA  . ALA A 1 92  ? 14.830  -17.813 34.098  1.00 20.99 ? 88   ALA A CA  1 
ATOM   710  C C   . ALA A 1 92  ? 15.566  -17.604 32.797  1.00 20.48 ? 88   ALA A C   1 
ATOM   711  O O   . ALA A 1 92  ? 16.752  -17.974 32.680  1.00 21.03 ? 88   ALA A O   1 
ATOM   712  C CB  . ALA A 1 92  ? 14.433  -16.492 34.689  1.00 21.04 ? 88   ALA A CB  1 
ATOM   713  N N   . VAL A 1 93  ? 14.860  -17.003 31.838  1.00 19.15 ? 89   VAL A N   1 
ATOM   714  C CA  . VAL A 1 93  ? 15.470  -16.453 30.625  1.00 18.59 ? 89   VAL A CA  1 
ATOM   715  C C   . VAL A 1 93  ? 15.583  -14.955 30.857  1.00 18.23 ? 89   VAL A C   1 
ATOM   716  O O   . VAL A 1 93  ? 14.628  -14.391 31.388  1.00 18.87 ? 89   VAL A O   1 
ATOM   717  C CB  . VAL A 1 93  ? 14.652  -16.776 29.368  1.00 19.26 ? 89   VAL A CB  1 
ATOM   718  C CG1 . VAL A 1 93  ? 15.293  -16.164 28.146  1.00 19.20 ? 89   VAL A CG1 1 
ATOM   719  C CG2 . VAL A 1 93  ? 14.496  -18.293 29.205  1.00 19.83 ? 89   VAL A CG2 1 
ATOM   720  N N   . TYR A 1 94  ? 16.779  -14.423 30.649  1.00 17.31 ? 90   TYR A N   1 
ATOM   721  C CA  . TYR A 1 94  ? 17.103  -12.984 30.804  1.00 16.79 ? 90   TYR A CA  1 
ATOM   722  C C   . TYR A 1 94  ? 17.327  -12.392 29.418  1.00 16.84 ? 90   TYR A C   1 
ATOM   723  O O   . TYR A 1 94  ? 18.178  -12.887 28.630  1.00 17.17 ? 90   TYR A O   1 
ATOM   724  C CB  . TYR A 1 94  ? 18.306  -12.778 31.733  1.00 16.39 ? 90   TYR A CB  1 
ATOM   725  C CG  . TYR A 1 94  ? 18.011  -13.184 33.151  1.00 16.84 ? 90   TYR A CG  1 
ATOM   726  C CD1 . TYR A 1 94  ? 17.465  -12.296 34.069  1.00 16.52 ? 90   TYR A CD1 1 
ATOM   727  C CD2 . TYR A 1 94  ? 18.207  -14.485 33.565  1.00 18.12 ? 90   TYR A CD2 1 
ATOM   728  C CE1 . TYR A 1 94  ? 17.174  -12.685 35.360  1.00 16.41 ? 90   TYR A CE1 1 
ATOM   729  C CE2 . TYR A 1 94  ? 17.876  -14.905 34.850  1.00 17.75 ? 90   TYR A CE2 1 
ATOM   730  C CZ  . TYR A 1 94  ? 17.368  -13.997 35.764  1.00 17.32 ? 90   TYR A CZ  1 
ATOM   731  O OH  . TYR A 1 94  ? 17.100  -14.389 37.058  1.00 17.66 ? 90   TYR A OH  1 
ATOM   732  N N   . PHE A 1 95  ? 16.647  -11.295 29.151  1.00 16.43 ? 91   PHE A N   1 
ATOM   733  C CA  . PHE A 1 95  ? 16.820  -10.507 27.922  1.00 15.84 ? 91   PHE A CA  1 
ATOM   734  C C   . PHE A 1 95  ? 17.485  -9.171  28.223  1.00 15.91 ? 91   PHE A C   1 
ATOM   735  O O   . PHE A 1 95  ? 17.068  -8.491  29.202  1.00 14.77 ? 91   PHE A O   1 
ATOM   736  C CB  . PHE A 1 95  ? 15.455  -10.293 27.285  1.00 16.03 ? 91   PHE A CB  1 
ATOM   737  C CG  . PHE A 1 95  ? 14.826  -11.535 26.701  1.00 16.69 ? 91   PHE A CG  1 
ATOM   738  C CD1 . PHE A 1 95  ? 15.204  -11.999 25.463  1.00 18.44 ? 91   PHE A CD1 1 
ATOM   739  C CD2 . PHE A 1 95  ? 13.887  -12.283 27.425  1.00 17.85 ? 91   PHE A CD2 1 
ATOM   740  C CE1 . PHE A 1 95  ? 14.617  -13.144 24.912  1.00 18.32 ? 91   PHE A CE1 1 
ATOM   741  C CE2 . PHE A 1 95  ? 13.305  -13.429 26.882  1.00 17.67 ? 91   PHE A CE2 1 
ATOM   742  C CZ  . PHE A 1 95  ? 13.701  -13.860 25.641  1.00 18.60 ? 91   PHE A CZ  1 
ATOM   743  N N   . CYS A 1 96  ? 18.358  -8.721  27.307  1.00 15.75 ? 92   CYS A N   1 
ATOM   744  C CA  . CYS A 1 96  ? 18.673  -7.282  27.220  1.00 15.65 ? 92   CYS A CA  1 
ATOM   745  C C   . CYS A 1 96  ? 17.874  -6.698  26.060  1.00 15.35 ? 92   CYS A C   1 
ATOM   746  O O   . CYS A 1 96  ? 17.500  -7.453  25.143  1.00 16.41 ? 92   CYS A O   1 
ATOM   747  C CB  . CYS A 1 96  ? 20.162  -7.033  27.060  1.00 17.21 ? 92   CYS A CB  1 
ATOM   748  S SG  . CYS A 1 96  ? 20.749  -7.648  25.479  1.00 20.59 ? 92   CYS A SG  1 
ATOM   749  N N   . LYS A 1 97  ? 17.536  -5.433  26.133  1.00 14.62 ? 93   LYS A N   1 
ATOM   750  C CA  . LYS A 1 97  ? 16.791  -4.761  25.059  1.00 14.83 ? 93   LYS A CA  1 
ATOM   751  C C   . LYS A 1 97  ? 17.069  -3.278  25.047  1.00 14.84 ? 93   LYS A C   1 
ATOM   752  O O   . LYS A 1 97  ? 17.438  -2.701  26.093  1.00 14.38 ? 93   LYS A O   1 
ATOM   753  C CB  . LYS A 1 97  ? 15.291  -5.104  25.137  1.00 14.56 ? 93   LYS A CB  1 
ATOM   754  C CG  . LYS A 1 97  ? 14.435  -4.466  26.207  1.00 14.86 ? 93   LYS A CG  1 
ATOM   755  C CD  . LYS A 1 97  ? 13.990  -3.032  25.927  1.00 15.97 ? 93   LYS A CD  1 
ATOM   756  C CE  . LYS A 1 97  ? 12.906  -2.939  24.896  1.00 16.06 ? 93   LYS A CE  1 
ATOM   757  N NZ  . LYS A 1 97  ? 12.522  -1.541  24.588  1.00 16.70 ? 93   LYS A NZ  1 
ATOM   758  N N   . ARG A 1 98  ? 16.850  -2.672  23.877  1.00 14.73 ? 94   ARG A N   1 
ATOM   759  C CA  . ARG A 1 98  ? 17.184  -1.266  23.674  1.00 15.39 ? 94   ARG A CA  1 
ATOM   760  C C   . ARG A 1 98  ? 15.979  -0.369  23.905  1.00 14.61 ? 94   ARG A C   1 
ATOM   761  O O   . ARG A 1 98  ? 14.859  -0.652  23.399  1.00 13.52 ? 94   ARG A O   1 
ATOM   762  C CB  . ARG A 1 98  ? 17.792  -1.061  22.316  1.00 15.75 ? 94   ARG A CB  1 
ATOM   763  C CG  . ARG A 1 98  ? 18.354  0.308   22.077  1.00 16.29 ? 94   ARG A CG  1 
ATOM   764  C CD  . ARG A 1 98  ? 18.907  0.358   20.663  1.00 16.49 ? 94   ARG A CD  1 
ATOM   765  N NE  . ARG A 1 98  ? 17.940  0.244   19.557  1.00 16.67 ? 94   ARG A NE  1 
ATOM   766  C CZ  . ARG A 1 98  ? 18.180  0.649   18.315  1.00 17.11 ? 94   ARG A CZ  1 
ATOM   767  N NH1 . ARG A 1 98  ? 19.353  1.160   17.942  1.00 17.00 ? 94   ARG A NH1 1 
ATOM   768  N NH2 . ARG A 1 98  ? 17.230  0.524   17.415  1.00 17.14 ? 94   ARG A NH2 1 
ATOM   769  N N   . SER A 1 99  ? 16.213  0.685   24.716  1.00 13.68 ? 95   SER A N   1 
ATOM   770  C CA  . SER A 1 99  ? 15.307  1.850   24.805  1.00 13.32 ? 95   SER A CA  1 
ATOM   771  C C   . SER A 1 99  ? 13.998  1.512   25.529  1.00 12.92 ? 95   SER A C   1 
ATOM   772  O O   . SER A 1 99  ? 13.844  0.400   26.046  1.00 12.78 ? 95   SER A O   1 
ATOM   773  C CB  . SER A 1 99  ? 15.069  2.399   23.409  1.00 13.89 ? 95   SER A CB  1 
ATOM   774  O OG  . SER A 1 99  ? 14.545  3.694   23.464  1.00 14.43 ? 95   SER A OG  1 
ATOM   775  N N   . LEU A 1 100 ? 13.095  2.470   25.509  1.00 13.53 ? 96   LEU A N   1 
ATOM   776  C CA  . LEU A 1 100 ? 11.683  2.272   25.927  1.00 13.90 ? 96   LEU A CA  1 
ATOM   777  C C   . LEU A 1 100 ? 10.921  1.763   24.715  1.00 14.45 ? 96   LEU A C   1 
ATOM   778  O O   . LEU A 1 100 ? 11.463  1.720   23.605  1.00 15.00 ? 96   LEU A O   1 
ATOM   779  C CB  . LEU A 1 100 ? 11.109  3.588   26.452  1.00 14.29 ? 96   LEU A CB  1 
ATOM   780  C CG  . LEU A 1 100 ? 11.721  4.152   27.733  1.00 14.92 ? 96   LEU A CG  1 
ATOM   781  C CD1 . LEU A 1 100 ? 11.176  5.529   28.007  1.00 15.13 ? 96   LEU A CD1 1 
ATOM   782  C CD2 . LEU A 1 100 ? 11.468  3.245   28.903  1.00 15.00 ? 96   LEU A CD2 1 
ATOM   783  N N   . PRO A 1 101 ? 9.684   1.275   24.888  1.00 14.63 ? 97   PRO A N   1 
ATOM   784  C CA  . PRO A 1 101 ? 8.843   0.882   23.761  1.00 14.81 ? 97   PRO A CA  1 
ATOM   785  C C   . PRO A 1 101 ? 8.709   2.089   22.826  1.00 15.48 ? 97   PRO A C   1 
ATOM   786  O O   . PRO A 1 101 ? 8.551   3.224   23.262  1.00 15.91 ? 97   PRO A O   1 
ATOM   787  C CB  . PRO A 1 101 ? 7.498   0.530   24.427  1.00 14.88 ? 97   PRO A CB  1 
ATOM   788  C CG  . PRO A 1 101 ? 7.877   0.137   25.775  1.00 15.07 ? 97   PRO A CG  1 
ATOM   789  C CD  . PRO A 1 101 ? 8.926   1.181   26.137  1.00 15.01 ? 97   PRO A CD  1 
ATOM   790  N N   . GLY A 1 102 ? 8.892   1.839   21.529  1.00 15.05 ? 98   GLY A N   1 
ATOM   791  C CA  . GLY A 1 102 ? 8.907   2.885   20.516  1.00 14.83 ? 98   GLY A CA  1 
ATOM   792  C C   . GLY A 1 102 ? 9.841   2.460   19.418  1.00 15.07 ? 98   GLY A C   1 
ATOM   793  O O   . GLY A 1 102 ? 10.152  1.283   19.329  1.00 13.97 ? 98   GLY A O   1 
ATOM   794  N N   . THR A 1 103 ? 10.188  3.384   18.571  1.00 16.07 ? 99   THR A N   1 
ATOM   795  C CA  . THR A 1 103 ? 10.855  3.047   17.306  1.00 17.89 ? 99   THR A CA  1 
ATOM   796  C C   . THR A 1 103 ? 12.210  2.368   17.504  1.00 15.88 ? 99   THR A C   1 
ATOM   797  O O   . THR A 1 103 ? 12.554  1.581   16.609  1.00 15.56 ? 99   THR A O   1 
ATOM   798  C CB  . THR A 1 103 ? 10.884  4.260   16.371  1.00 21.56 ? 99   THR A CB  1 
ATOM   799  O OG1 . THR A 1 103 ? 10.979  3.559   15.120  1.00 28.10 ? 99   THR A OG1 1 
ATOM   800  C CG2 . THR A 1 103 ? 12.059  5.143   16.609  1.00 23.05 ? 99   THR A CG2 1 
ATOM   801  N N   . PHE A 1 104 ? 12.861  2.462   18.661  1.00 15.10 ? 100  PHE A N   1 
ATOM   802  C CA  . PHE A 1 104 ? 14.220  1.884   18.825  1.00 14.87 ? 100  PHE A CA  1 
ATOM   803  C C   . PHE A 1 104 ? 14.113  0.540   19.546  1.00 15.21 ? 100  PHE A C   1 
ATOM   804  O O   . PHE A 1 104 ? 15.163  -0.051  19.832  1.00 14.71 ? 100  PHE A O   1 
ATOM   805  C CB  . PHE A 1 104 ? 15.109  2.862   19.604  1.00 14.92 ? 100  PHE A CB  1 
ATOM   806  C CG  . PHE A 1 104 ? 15.327  4.162   18.875  1.00 14.70 ? 100  PHE A CG  1 
ATOM   807  C CD1 . PHE A 1 104 ? 16.196  4.239   17.796  1.00 14.83 ? 100  PHE A CD1 1 
ATOM   808  C CD2 . PHE A 1 104 ? 14.660  5.312   19.272  1.00 14.92 ? 100  PHE A CD2 1 
ATOM   809  C CE1 . PHE A 1 104 ? 16.381  5.438   17.125  1.00 15.21 ? 100  PHE A CE1 1 
ATOM   810  C CE2 . PHE A 1 104 ? 14.861  6.516   18.599  1.00 15.30 ? 100  PHE A CE2 1 
ATOM   811  C CZ  . PHE A 1 104 ? 15.730  6.570   17.526  1.00 15.08 ? 100  PHE A CZ  1 
ATOM   812  N N   . ASP A 1 105 ? 12.886  0.089   19.859  1.00 14.51 ? 101  ASP A N   1 
ATOM   813  C CA  . ASP A 1 105 ? 12.725  -1.207  20.569  1.00 14.43 ? 101  ASP A CA  1 
ATOM   814  C C   . ASP A 1 105 ? 13.466  -2.313  19.794  1.00 14.71 ? 101  ASP A C   1 
ATOM   815  O O   . ASP A 1 105 ? 13.258  -2.450  18.591  1.00 13.67 ? 101  ASP A O   1 
ATOM   816  C CB  . ASP A 1 105 ? 11.242  -1.534  20.706  1.00 14.44 ? 101  ASP A CB  1 
ATOM   817  C CG  . ASP A 1 105 ? 10.919  -2.679  21.617  1.00 14.11 ? 101  ASP A CG  1 
ATOM   818  O OD1 . ASP A 1 105 ? 10.618  -2.379  22.781  1.00 16.48 ? 101  ASP A OD1 1 
ATOM   819  O OD2 . ASP A 1 105 ? 10.882  -3.806  21.166  1.00 14.39 ? 101  ASP A OD2 1 
ATOM   820  N N   . TYR A 1 106 ? 14.309  -3.096  20.452  1.00 14.54 ? 102  TYR A N   1 
ATOM   821  C CA  . TYR A 1 106 ? 15.106  -4.176  19.850  1.00 15.88 ? 102  TYR A CA  1 
ATOM   822  C C   . TYR A 1 106 ? 15.585  -5.052  21.003  1.00 15.75 ? 102  TYR A C   1 
ATOM   823  O O   . TYR A 1 106 ? 15.989  -4.506  22.041  1.00 15.37 ? 102  TYR A O   1 
ATOM   824  C CB  . TYR A 1 106 ? 16.268  -3.623  19.000  1.00 19.10 ? 102  TYR A CB  1 
ATOM   825  C CG  . TYR A 1 106 ? 16.830  -4.659  18.053  1.00 23.03 ? 102  TYR A CG  1 
ATOM   826  C CD1 . TYR A 1 106 ? 16.443  -4.780  16.717  1.00 29.60 ? 102  TYR A CD1 1 
ATOM   827  C CD2 . TYR A 1 106 ? 17.742  -5.561  18.551  1.00 27.22 ? 102  TYR A CD2 1 
ATOM   828  C CE1 . TYR A 1 106 ? 16.962  -5.814  15.925  1.00 31.52 ? 102  TYR A CE1 1 
ATOM   829  C CE2 . TYR A 1 106 ? 18.207  -6.613  17.794  1.00 30.47 ? 102  TYR A CE2 1 
ATOM   830  C CZ  . TYR A 1 106 ? 17.865  -6.718  16.475  1.00 30.20 ? 102  TYR A CZ  1 
ATOM   831  O OH  . TYR A 1 106 ? 18.462  -7.819  15.891  1.00 36.60 ? 102  TYR A OH  1 
ATOM   832  N N   . TRP A 1 107 ? 15.512  -6.355  20.834  1.00 15.85 ? 103  TRP A N   1 
ATOM   833  C CA  . TRP A 1 107 ? 15.770  -7.349  21.898  1.00 16.19 ? 103  TRP A CA  1 
ATOM   834  C C   . TRP A 1 107 ? 16.939  -8.262  21.528  1.00 17.38 ? 103  TRP A C   1 
ATOM   835  O O   . TRP A 1 107 ? 17.105  -8.644  20.356  1.00 17.21 ? 103  TRP A O   1 
ATOM   836  C CB  . TRP A 1 107 ? 14.530  -8.164  22.163  1.00 16.93 ? 103  TRP A CB  1 
ATOM   837  C CG  . TRP A 1 107 ? 13.389  -7.381  22.681  1.00 16.86 ? 103  TRP A CG  1 
ATOM   838  C CD1 . TRP A 1 107 ? 12.677  -6.401  22.039  1.00 16.64 ? 103  TRP A CD1 1 
ATOM   839  C CD2 . TRP A 1 107 ? 12.838  -7.490  23.990  1.00 17.17 ? 103  TRP A CD2 1 
ATOM   840  N NE1 . TRP A 1 107 ? 11.747  -5.878  22.878  1.00 16.70 ? 103  TRP A NE1 1 
ATOM   841  C CE2 . TRP A 1 107 ? 11.769  -6.573  24.055  1.00 17.11 ? 103  TRP A CE2 1 
ATOM   842  C CE3 . TRP A 1 107 ? 13.151  -8.244  25.130  1.00 17.49 ? 103  TRP A CE3 1 
ATOM   843  C CZ2 . TRP A 1 107 ? 11.049  -6.363  25.220  1.00 16.91 ? 103  TRP A CZ2 1 
ATOM   844  C CZ3 . TRP A 1 107 ? 12.360  -8.109  26.244  1.00 17.24 ? 103  TRP A CZ3 1 
ATOM   845  C CH2 . TRP A 1 107 ? 11.311  -7.197  26.291  1.00 18.33 ? 103  TRP A CH2 1 
ATOM   846  N N   . GLY A 1 108 ? 17.760  -8.599  22.521  1.00 17.64 ? 104  GLY A N   1 
ATOM   847  C CA  . GLY A 1 108 ? 18.704  -9.725  22.452  1.00 18.76 ? 104  GLY A CA  1 
ATOM   848  C C   . GLY A 1 108 ? 17.939  -11.032 22.317  1.00 18.64 ? 104  GLY A C   1 
ATOM   849  O O   . GLY A 1 108 ? 16.711  -11.037 22.480  1.00 17.95 ? 104  GLY A O   1 
ATOM   850  N N   . GLN A 1 109 ? 18.652  -12.114 22.031  1.00 18.88 ? 105  GLN A N   1 
ATOM   851  C CA  . GLN A 1 109 ? 18.055  -13.447 21.808  1.00 19.47 ? 105  GLN A CA  1 
ATOM   852  C C   . GLN A 1 109 ? 17.740  -14.105 23.142  1.00 19.06 ? 105  GLN A C   1 
ATOM   853  O O   . GLN A 1 109 ? 17.096  -15.172 23.123  1.00 19.03 ? 105  GLN A O   1 
ATOM   854  C CB  . GLN A 1 109 ? 18.958  -14.296 20.905  1.00 20.10 ? 105  GLN A CB  1 
ATOM   855  C CG  . GLN A 1 109 ? 20.070  -15.038 21.639  1.00 20.93 ? 105  GLN A CG  1 
ATOM   856  C CD  . GLN A 1 109 ? 21.307  -14.212 21.896  1.00 20.44 ? 105  GLN A CD  1 
ATOM   857  O OE1 . GLN A 1 109 ? 21.295  -12.972 21.844  1.00 19.72 ? 105  GLN A OE1 1 
ATOM   858  N NE2 . GLN A 1 109 ? 22.383  -14.928 22.187  1.00 20.45 ? 105  GLN A NE2 1 
ATOM   859  N N   . GLY A 1 110 ? 18.172  -13.509 24.271  1.00 17.81 ? 106  GLY A N   1 
ATOM   860  C CA  . GLY A 1 110 ? 17.922  -14.106 25.581  1.00 19.11 ? 106  GLY A CA  1 
ATOM   861  C C   . GLY A 1 110 ? 19.047  -15.063 26.008  1.00 19.28 ? 106  GLY A C   1 
ATOM   862  O O   . GLY A 1 110 ? 19.807  -15.603 25.122  1.00 19.20 ? 106  GLY A O   1 
ATOM   863  N N   . THR A 1 111 ? 19.206  -15.213 27.313  1.00 18.34 ? 107  THR A N   1 
ATOM   864  C CA  . THR A 1 111 ? 20.210  -16.104 27.964  1.00 19.84 ? 107  THR A CA  1 
ATOM   865  C C   . THR A 1 111 ? 19.448  -16.885 29.044  1.00 19.54 ? 107  THR A C   1 
ATOM   866  O O   . THR A 1 111 ? 18.849  -16.253 29.970  1.00 18.37 ? 107  THR A O   1 
ATOM   867  C CB  . THR A 1 111 ? 21.363  -15.300 28.568  1.00 19.44 ? 107  THR A CB  1 
ATOM   868  O OG1 . THR A 1 111 ? 22.108  -14.597 27.559  1.00 19.03 ? 107  THR A OG1 1 
ATOM   869  C CG2 . THR A 1 111 ? 22.308  -16.160 29.379  1.00 19.73 ? 107  THR A CG2 1 
ATOM   870  N N   . THR A 1 112 ? 19.468  -18.205 28.953  1.00 21.70 ? 108  THR A N   1 
ATOM   871  C CA  . THR A 1 112 ? 18.850  -19.078 29.976  1.00 22.32 ? 108  THR A CA  1 
ATOM   872  C C   . THR A 1 112 ? 19.827  -19.231 31.129  1.00 22.61 ? 108  THR A C   1 
ATOM   873  O O   . THR A 1 112 ? 20.978  -19.637 30.886  1.00 24.94 ? 108  THR A O   1 
ATOM   874  C CB  . THR A 1 112 ? 18.485  -20.455 29.408  1.00 25.20 ? 108  THR A CB  1 
ATOM   875  O OG1 . THR A 1 112 ? 17.601  -20.152 28.329  1.00 23.99 ? 108  THR A OG1 1 
ATOM   876  C CG2 . THR A 1 112 ? 17.854  -21.344 30.463  1.00 25.48 ? 108  THR A CG2 1 
ATOM   877  N N   . LEU A 1 113 ? 19.393  -18.897 32.340  1.00 21.63 ? 109  LEU A N   1 
ATOM   878  C CA  . LEU A 1 113 ? 20.145  -19.225 33.566  1.00 22.64 ? 109  LEU A CA  1 
ATOM   879  C C   . LEU A 1 113 ? 19.416  -20.374 34.251  1.00 23.29 ? 109  LEU A C   1 
ATOM   880  O O   . LEU A 1 113 ? 18.219  -20.265 34.515  1.00 24.06 ? 109  LEU A O   1 
ATOM   881  C CB  . LEU A 1 113 ? 20.267  -17.983 34.442  1.00 22.09 ? 109  LEU A CB  1 
ATOM   882  C CG  . LEU A 1 113 ? 20.802  -18.245 35.838  1.00 22.53 ? 109  LEU A CG  1 
ATOM   883  C CD1 . LEU A 1 113 ? 22.239  -18.705 35.730  1.00 22.51 ? 109  LEU A CD1 1 
ATOM   884  C CD2 . LEU A 1 113 ? 20.669  -17.000 36.718  1.00 22.20 ? 109  LEU A CD2 1 
ATOM   885  N N   . THR A 1 114 ? 20.134  -21.464 34.481  1.00 24.65 ? 110  THR A N   1 
ATOM   886  C CA  . THR A 1 114 ? 19.635  -22.570 35.328  1.00 25.07 ? 110  THR A CA  1 
ATOM   887  C C   . THR A 1 114 ? 20.471  -22.629 36.603  1.00 25.17 ? 110  THR A C   1 
ATOM   888  O O   . THR A 1 114 ? 21.683  -22.801 36.468  1.00 25.98 ? 110  THR A O   1 
ATOM   889  C CB  . THR A 1 114 ? 19.743  -23.908 34.598  1.00 25.75 ? 110  THR A CB  1 
ATOM   890  O OG1 . THR A 1 114 ? 19.035  -23.725 33.368  1.00 26.84 ? 110  THR A OG1 1 
ATOM   891  C CG2 . THR A 1 114 ? 19.174  -25.048 35.426  1.00 26.24 ? 110  THR A CG2 1 
ATOM   892  N N   . VAL A 1 115 ? 19.836  -22.445 37.765  1.00 25.46 ? 111  VAL A N   1 
ATOM   893  C CA  . VAL A 1 115 ? 20.456  -22.644 39.099  1.00 26.60 ? 111  VAL A CA  1 
ATOM   894  C C   . VAL A 1 115 ? 20.124  -24.070 39.565  1.00 29.84 ? 111  VAL A C   1 
ATOM   895  O O   . VAL A 1 115 ? 18.910  -24.335 39.714  1.00 30.73 ? 111  VAL A O   1 
ATOM   896  C CB  . VAL A 1 115 ? 19.980  -21.563 40.090  1.00 26.59 ? 111  VAL A CB  1 
ATOM   897  C CG1 . VAL A 1 115 ? 20.687  -21.665 41.413  1.00 27.82 ? 111  VAL A CG1 1 
ATOM   898  C CG2 . VAL A 1 115 ? 20.185  -20.181 39.527  1.00 25.87 ? 111  VAL A CG2 1 
ATOM   899  N N   . SER A 1 116 ? 21.136  -24.941 39.700  1.00 33.32 ? 112  SER A N   1 
ATOM   900  C CA  . SER A 1 116 ? 21.054  -26.273 40.384  1.00 37.05 ? 112  SER A CA  1 
ATOM   901  C C   . SER A 1 116 ? 20.033  -26.223 41.528  1.00 37.60 ? 112  SER A C   1 
ATOM   902  O O   . SER A 1 116 ? 19.108  -27.016 41.371  1.00 46.13 ? 112  SER A O   1 
ATOM   903  C CB  . SER A 1 116 ? 22.373  -26.725 40.973  1.00 37.79 ? 112  SER A CB  1 
ATOM   904  O OG  . SER A 1 116 ? 23.431  -26.601 40.059  1.00 41.53 ? 112  SER A OG  1 
ATOM   905  N N   . GLY A 1 125 ? 15.046  -19.812 51.760  1.00 49.07 ? 121  GLY A N   1 
ATOM   906  C CA  . GLY A 1 125 ? 13.670  -19.368 51.448  1.00 45.84 ? 121  GLY A CA  1 
ATOM   907  C C   . GLY A 1 125 ? 13.477  -17.884 51.764  1.00 42.82 ? 121  GLY A C   1 
ATOM   908  O O   . GLY A 1 125 ? 14.075  -17.388 52.800  1.00 37.29 ? 121  GLY A O   1 
ATOM   909  N N   . GLY A 1 126 ? 12.701  -17.232 50.885  1.00 37.25 ? 122  GLY A N   1 
ATOM   910  C CA  . GLY A 1 126 ? 12.234  -15.835 50.947  1.00 36.00 ? 122  GLY A CA  1 
ATOM   911  C C   . GLY A 1 126 ? 13.366  -14.828 50.905  1.00 34.59 ? 122  GLY A C   1 
ATOM   912  O O   . GLY A 1 126 ? 13.157  -13.744 51.451  1.00 34.18 ? 122  GLY A O   1 
ATOM   913  N N   . GLY A 1 127 ? 14.526  -15.168 50.323  1.00 31.76 ? 123  GLY A N   1 
ATOM   914  C CA  . GLY A 1 127 ? 15.651  -14.229 50.158  1.00 29.17 ? 123  GLY A CA  1 
ATOM   915  C C   . GLY A 1 127 ? 15.516  -13.343 48.915  1.00 28.64 ? 123  GLY A C   1 
ATOM   916  O O   . GLY A 1 127 ? 16.344  -12.373 48.747  1.00 26.93 ? 123  GLY A O   1 
ATOM   917  N N   . GLY A 1 128 ? 14.553  -13.615 48.027  1.00 28.48 ? 124  GLY A N   1 
ATOM   918  C CA  . GLY A 1 128 ? 14.396  -12.751 46.834  1.00 28.72 ? 124  GLY A CA  1 
ATOM   919  C C   . GLY A 1 128 ? 13.681  -11.456 47.174  1.00 29.63 ? 124  GLY A C   1 
ATOM   920  O O   . GLY A 1 128 ? 13.121  -11.347 48.312  1.00 28.09 ? 124  GLY A O   1 
ATOM   921  N N   . GLY A 1 129 ? 13.696  -10.489 46.253  1.00 29.06 ? 125  GLY A N   1 
ATOM   922  C CA  . GLY A 1 129 ? 13.035  -9.185  46.481  1.00 28.85 ? 125  GLY A CA  1 
ATOM   923  C C   . GLY A 1 129 ? 11.538  -9.318  46.327  1.00 29.94 ? 125  GLY A C   1 
ATOM   924  O O   . GLY A 1 129 ? 11.115  -10.316 45.774  1.00 30.43 ? 125  GLY A O   1 
ATOM   925  N N   . SER A 1 130 ? 10.771  -8.339  46.796  1.00 30.78 ? 126  SER A N   1 
ATOM   926  C CA  . SER A 1 130 ? 9.304   -8.214  46.576  1.00 31.16 ? 126  SER A CA  1 
ATOM   927  C C   . SER A 1 130 ? 9.029   -6.915  45.823  1.00 31.04 ? 126  SER A C   1 
ATOM   928  O O   . SER A 1 130 ? 9.838   -5.978  45.973  1.00 31.78 ? 126  SER A O   1 
ATOM   929  C CB  . SER A 1 130 ? 8.562   -8.208  47.878  1.00 32.63 ? 126  SER A CB  1 
ATOM   930  O OG  . SER A 1 130 ? 8.829   -9.393  48.577  1.00 36.72 ? 126  SER A OG  1 
ATOM   931  N N   . SER A 1 131 ? 7.915   -6.860  45.088  1.00 32.40 ? 127  SER A N   1 
ATOM   932  C CA  . SER A 1 131 ? 7.366   -5.619  44.488  1.00 31.30 ? 127  SER A CA  1 
ATOM   933  C C   . SER A 1 131 ? 6.965   -4.654  45.616  1.00 32.80 ? 127  SER A C   1 
ATOM   934  O O   . SER A 1 131 ? 6.618   -5.136  46.727  1.00 34.68 ? 127  SER A O   1 
ATOM   935  C CB  . SER A 1 131 ? 6.174   -5.948  43.599  1.00 31.82 ? 127  SER A CB  1 
ATOM   936  O OG  . SER A 1 131 ? 6.526   -6.917  42.603  1.00 30.94 ? 127  SER A OG  1 
ATOM   937  N N   . GLY A 1 132 ? 7.003   -3.353  45.334  1.00 31.34 ? 128  GLY A N   1 
ATOM   938  C CA  . GLY A 1 132 ? 6.464   -2.292  46.196  1.00 31.59 ? 128  GLY A CA  1 
ATOM   939  C C   . GLY A 1 132 ? 4.947   -2.270  46.127  1.00 32.93 ? 128  GLY A C   1 
ATOM   940  O O   . GLY A 1 132 ? 4.355   -2.578  45.046  1.00 29.94 ? 128  GLY A O   1 
ATOM   941  N N   . SER A 1 133 ? 4.311   -1.860  47.215  1.00 32.03 ? 129  SER A N   1 
ATOM   942  C CA  . SER A 1 133 ? 2.839   -1.699  47.285  1.00 35.11 ? 129  SER A CA  1 
ATOM   943  C C   . SER A 1 133 ? 2.415   -0.575  46.333  1.00 32.72 ? 129  SER A C   1 
ATOM   944  O O   . SER A 1 133 ? 1.262   -0.562  45.913  1.00 34.88 ? 129  SER A O   1 
ATOM   945  C CB  . SER A 1 133 ? 2.421   -1.435  48.709  1.00 36.90 ? 129  SER A CB  1 
ATOM   946  O OG  . SER A 1 133 ? 2.962   -0.189  49.155  1.00 40.11 ? 129  SER A OG  1 
ATOM   947  N N   . SER A 1 134 ? 3.351   0.281   45.950  1.00 31.63 ? 130  SER A N   1 
ATOM   948  C CA  . SER A 1 134 ? 3.195   1.451   45.053  1.00 32.04 ? 130  SER A CA  1 
ATOM   949  C C   . SER A 1 134 ? 3.304   1.069   43.559  1.00 28.28 ? 130  SER A C   1 
ATOM   950  O O   . SER A 1 134 ? 2.883   1.884   42.699  1.00 28.80 ? 130  SER A O   1 
ATOM   951  C CB  . SER A 1 134 ? 4.265   2.416   45.420  1.00 37.23 ? 130  SER A CB  1 
ATOM   952  O OG  . SER A 1 134 ? 4.384   3.445   44.454  1.00 43.34 ? 130  SER A OG  1 
ATOM   953  N N   . ASP A 1 135 ? 3.872   -0.093  43.235  1.00 24.29 ? 1001 ASP A N   1 
ATOM   954  C CA  . ASP A 1 135 ? 4.145   -0.441  41.806  1.00 22.15 ? 1001 ASP A CA  1 
ATOM   955  C C   . ASP A 1 135 ? 2.828   -0.620  41.025  1.00 21.14 ? 1001 ASP A C   1 
ATOM   956  O O   . ASP A 1 135 ? 1.824   -1.118  41.575  1.00 20.55 ? 1001 ASP A O   1 
ATOM   957  C CB  . ASP A 1 135 ? 4.962   -1.721  41.687  1.00 20.87 ? 1001 ASP A CB  1 
ATOM   958  C CG  . ASP A 1 135 ? 6.316   -1.625  42.354  1.00 20.48 ? 1001 ASP A CG  1 
ATOM   959  O OD1 . ASP A 1 135 ? 6.956   -2.685  42.460  1.00 21.20 ? 1001 ASP A OD1 1 
ATOM   960  O OD2 . ASP A 1 135 ? 6.687   -0.490  42.807  1.00 19.72 ? 1001 ASP A OD2 1 
ATOM   961  N N   . VAL A 1 136 ? 2.801   -0.254  39.742  1.00 20.23 ? 1002 VAL A N   1 
ATOM   962  C CA  . VAL A 1 136 ? 1.587   -0.479  38.920  1.00 19.51 ? 1002 VAL A CA  1 
ATOM   963  C C   . VAL A 1 136 ? 1.490   -1.988  38.622  1.00 18.64 ? 1002 VAL A C   1 
ATOM   964  O O   . VAL A 1 136 ? 2.526   -2.611  38.239  1.00 18.97 ? 1002 VAL A O   1 
ATOM   965  C CB  . VAL A 1 136 ? 1.612   0.331   37.607  1.00 19.45 ? 1002 VAL A CB  1 
ATOM   966  C CG1 . VAL A 1 136 ? 0.342   0.071   36.813  1.00 19.23 ? 1002 VAL A CG1 1 
ATOM   967  C CG2 . VAL A 1 136 ? 1.815   1.803   37.834  1.00 19.92 ? 1002 VAL A CG2 1 
ATOM   968  N N   . VAL A 1 137 ? 0.302   -2.556  38.780  1.00 18.66 ? 1003 VAL A N   1 
ATOM   969  C CA  . VAL A 1 137 ? -0.008  -3.958  38.432  1.00 19.31 ? 1003 VAL A CA  1 
ATOM   970  C C   . VAL A 1 137 ? -0.768  -3.925  37.114  1.00 18.58 ? 1003 VAL A C   1 
ATOM   971  O O   . VAL A 1 137 ? -1.787  -3.225  37.034  1.00 18.34 ? 1003 VAL A O   1 
ATOM   972  C CB  . VAL A 1 137 ? -0.834  -4.710  39.498  1.00 21.07 ? 1003 VAL A CB  1 
ATOM   973  C CG1 . VAL A 1 137 ? -1.123  -6.147  39.063  1.00 20.80 ? 1003 VAL A CG1 1 
ATOM   974  C CG2 . VAL A 1 137 ? -0.169  -4.640  40.855  1.00 21.74 ? 1003 VAL A CG2 1 
ATOM   975  N N   . MET A 1 138 ? -0.318  -4.720  36.161  1.00 18.88 ? 1004 MET A N   1 
ATOM   976  C CA  . MET A 1 138 ? -0.993  -4.866  34.853  1.00 19.44 ? 1004 MET A CA  1 
ATOM   977  C C   . MET A 1 138 ? -1.619  -6.247  34.803  1.00 21.13 ? 1004 MET A C   1 
ATOM   978  O O   . MET A 1 138 ? -0.884  -7.216  34.929  1.00 22.60 ? 1004 MET A O   1 
ATOM   979  C CB  . MET A 1 138 ? 0.008   -4.693  33.705  1.00 18.91 ? 1004 MET A CB  1 
ATOM   980  C CG  . MET A 1 138 ? 0.721   -3.358  33.708  1.00 19.08 ? 1004 MET A CG  1 
ATOM   981  S SD  . MET A 1 138 ? -0.339  -1.946  33.488  1.00 20.63 ? 1004 MET A SD  1 
ATOM   982  C CE  . MET A 1 138 ? -0.827  -2.127  31.789  1.00 20.96 ? 1004 MET A CE  1 
ATOM   983  N N   . THR A 1 139 ? -2.960  -6.309  34.761  1.00 21.73 ? 1005 THR A N   1 
ATOM   984  C CA  . THR A 1 139 ? -3.696  -7.575  34.884  1.00 21.41 ? 1005 THR A CA  1 
ATOM   985  C C   . THR A 1 139 ? -4.262  -7.962  33.510  1.00 21.53 ? 1005 THR A C   1 
ATOM   986  O O   . THR A 1 139 ? -5.135  -7.254  32.998  1.00 23.13 ? 1005 THR A O   1 
ATOM   987  C CB  . THR A 1 139 ? -4.795  -7.491  35.945  1.00 22.92 ? 1005 THR A CB  1 
ATOM   988  O OG1 . THR A 1 139 ? -4.158  -7.102  37.174  1.00 25.40 ? 1005 THR A OG1 1 
ATOM   989  C CG2 . THR A 1 139 ? -5.533  -8.814  36.004  1.00 23.36 ? 1005 THR A CG2 1 
ATOM   990  N N   . GLN A 1 140 ? -3.804  -9.064  32.935  1.00 21.31 ? 1006 GLN A N   1 
ATOM   991  C CA  . GLN A 1 140 ? -4.473  -9.667  31.745  1.00 22.40 ? 1006 GLN A CA  1 
ATOM   992  C C   . GLN A 1 140 ? -5.397  -10.757 32.291  1.00 26.18 ? 1006 GLN A C   1 
ATOM   993  O O   . GLN A 1 140 ? -4.859  -11.700 32.860  1.00 27.88 ? 1006 GLN A O   1 
ATOM   994  C CB  . GLN A 1 140 ? -3.428  -10.222 30.783  1.00 21.70 ? 1006 GLN A CB  1 
ATOM   995  C CG  . GLN A 1 140 ? -2.672  -9.108  30.102  1.00 21.23 ? 1006 GLN A CG  1 
ATOM   996  C CD  . GLN A 1 140 ? -1.542  -9.563  29.211  1.00 20.33 ? 1006 GLN A CD  1 
ATOM   997  O OE1 . GLN A 1 140 ? -0.401  -9.219  29.447  1.00 20.45 ? 1006 GLN A OE1 1 
ATOM   998  N NE2 . GLN A 1 140 ? -1.838  -10.305 28.170  1.00 19.99 ? 1006 GLN A NE2 1 
ATOM   999  N N   . SER A 1 141 ? -6.700  -10.574 32.191  1.00 30.76 ? 1007 SER A N   1 
ATOM   1000 C CA  . SER A 1 141 ? -7.745  -11.477 32.759  1.00 36.90 ? 1007 SER A CA  1 
ATOM   1001 C C   . SER A 1 141 ? -7.627  -12.914 32.237  1.00 36.36 ? 1007 SER A C   1 
ATOM   1002 O O   . SER A 1 141 ? -7.839  -13.839 33.058  1.00 39.59 ? 1007 SER A O   1 
ATOM   1003 C CB  . SER A 1 141 ? -9.110  -10.953 32.447  1.00 38.34 ? 1007 SER A CB  1 
ATOM   1004 O OG  . SER A 1 141 ? -9.206  -10.745 31.043  1.00 46.43 ? 1007 SER A OG  1 
ATOM   1005 N N   . HIS A 1 142 ? -7.240  -13.116 30.969  1.00 31.44 ? 1008 HIS A N   1 
ATOM   1006 C CA  . HIS A 1 142 ? -7.167  -14.482 30.381  1.00 30.12 ? 1008 HIS A CA  1 
ATOM   1007 C C   . HIS A 1 142 ? -5.713  -14.898 30.160  1.00 27.43 ? 1008 HIS A C   1 
ATOM   1008 O O   . HIS A 1 142 ? -5.038  -14.269 29.342  1.00 26.90 ? 1008 HIS A O   1 
ATOM   1009 C CB  . HIS A 1 142 ? -7.998  -14.549 29.111  1.00 31.19 ? 1008 HIS A CB  1 
ATOM   1010 C CG  . HIS A 1 142 ? -9.417  -14.183 29.375  1.00 34.65 ? 1008 HIS A CG  1 
ATOM   1011 N ND1 . HIS A 1 142 ? -10.073 -14.571 30.554  1.00 37.87 ? 1008 HIS A ND1 1 
ATOM   1012 C CD2 . HIS A 1 142 ? -10.298 -13.461 28.658  1.00 36.57 ? 1008 HIS A CD2 1 
ATOM   1013 C CE1 . HIS A 1 142 ? -11.319 -14.125 30.524  1.00 38.57 ? 1008 HIS A CE1 1 
ATOM   1014 N NE2 . HIS A 1 142 ? -11.480 -13.450 29.357  1.00 36.48 ? 1008 HIS A NE2 1 
ATOM   1015 N N   . LYS A 1 143 ? -5.291  -15.986 30.784  1.00 25.44 ? 1009 LYS A N   1 
ATOM   1016 C CA  . LYS A 1 143 ? -3.934  -16.548 30.553  1.00 26.81 ? 1009 LYS A CA  1 
ATOM   1017 C C   . LYS A 1 143 ? -3.933  -17.330 29.241  1.00 23.40 ? 1009 LYS A C   1 
ATOM   1018 O O   . LYS A 1 143 ? -2.869  -17.479 28.583  1.00 21.71 ? 1009 LYS A O   1 
ATOM   1019 C CB  . LYS A 1 143 ? -3.555  -17.483 31.716  1.00 30.48 ? 1009 LYS A CB  1 
ATOM   1020 C CG  . LYS A 1 143 ? -3.860  -16.976 33.130  1.00 37.67 ? 1009 LYS A CG  1 
ATOM   1021 C CD  . LYS A 1 143 ? -5.191  -17.474 33.801  1.00 44.96 ? 1009 LYS A CD  1 
ATOM   1022 C CE  . LYS A 1 143 ? -6.002  -16.380 34.488  1.00 45.83 ? 1009 LYS A CE  1 
ATOM   1023 N NZ  . LYS A 1 143 ? -5.236  -15.750 35.598  1.00 46.64 ? 1009 LYS A NZ  1 
ATOM   1024 N N   . PHE A 1 144 ? -5.096  -17.849 28.884  1.00 23.96 ? 1010 PHE A N   1 
ATOM   1025 C CA  . PHE A 1 144 ? -5.294  -18.612 27.621  1.00 25.11 ? 1010 PHE A CA  1 
ATOM   1026 C C   . PHE A 1 144 ? -6.512  -18.125 26.888  1.00 24.13 ? 1010 PHE A C   1 
ATOM   1027 O O   . PHE A 1 144 ? -7.559  -17.954 27.522  1.00 22.32 ? 1010 PHE A O   1 
ATOM   1028 C CB  . PHE A 1 144 ? -5.518  -20.095 27.911  1.00 27.60 ? 1010 PHE A CB  1 
ATOM   1029 C CG  . PHE A 1 144 ? -4.319  -20.691 28.588  1.00 27.97 ? 1010 PHE A CG  1 
ATOM   1030 C CD1 . PHE A 1 144 ? -3.241  -21.097 27.843  1.00 29.23 ? 1010 PHE A CD1 1 
ATOM   1031 C CD2 . PHE A 1 144 ? -4.262  -20.800 29.966  1.00 31.02 ? 1010 PHE A CD2 1 
ATOM   1032 C CE1 . PHE A 1 144 ? -2.108  -21.617 28.457  1.00 31.26 ? 1010 PHE A CE1 1 
ATOM   1033 C CE2 . PHE A 1 144 ? -3.123  -21.306 30.581  1.00 31.99 ? 1010 PHE A CE2 1 
ATOM   1034 C CZ  . PHE A 1 144 ? -2.051  -21.712 29.824  1.00 31.07 ? 1010 PHE A CZ  1 
ATOM   1035 N N   . MET A 1 145 ? -6.382  -17.996 25.571  1.00 23.73 ? 1011 MET A N   1 
ATOM   1036 C CA  . MET A 1 145 ? -7.524  -17.621 24.721  1.00 25.56 ? 1011 MET A CA  1 
ATOM   1037 C C   . MET A 1 145 ? -7.501  -18.475 23.458  1.00 24.93 ? 1011 MET A C   1 
ATOM   1038 O O   . MET A 1 145 ? -6.396  -18.752 22.955  1.00 23.31 ? 1011 MET A O   1 
ATOM   1039 C CB  . MET A 1 145 ? -7.414  -16.142 24.371  1.00 27.22 ? 1011 MET A CB  1 
ATOM   1040 C CG  . MET A 1 145 ? -8.647  -15.524 23.764  1.00 32.01 ? 1011 MET A CG  1 
ATOM   1041 S SD  . MET A 1 145 ? -8.326  -13.703 23.593  1.00 37.44 ? 1011 MET A SD  1 
ATOM   1042 C CE  . MET A 1 145 ? -7.838  -13.265 25.244  1.00 28.01 ? 1011 MET A CE  1 
ATOM   1043 N N   . SER A 1 146 ? -8.700  -18.898 23.032  1.00 24.23 ? 1012 SER A N   1 
ATOM   1044 C CA  . SER A 1 146 ? -8.910  -19.725 21.819  1.00 27.19 ? 1012 SER A CA  1 
ATOM   1045 C C   . SER A 1 146 ? -9.516  -18.865 20.716  1.00 26.03 ? 1012 SER A C   1 
ATOM   1046 O O   . SER A 1 146 ? -10.375 -18.029 21.058  1.00 24.98 ? 1012 SER A O   1 
ATOM   1047 C CB  . SER A 1 146 ? -9.842  -20.866 22.135  1.00 29.76 ? 1012 SER A CB  1 
ATOM   1048 O OG  . SER A 1 146 ? -9.053  -21.946 22.541  1.00 35.79 ? 1012 SER A OG  1 
ATOM   1049 N N   . THR A 1 147 ? -9.105  -19.060 19.461  1.00 25.71 ? 1013 THR A N   1 
ATOM   1050 C CA  . THR A 1 147 ? -9.753  -18.396 18.308  1.00 26.62 ? 1013 THR A CA  1 
ATOM   1051 C C   . THR A 1 147 ? -9.810  -19.336 17.108  1.00 25.46 ? 1013 THR A C   1 
ATOM   1052 O O   . THR A 1 147 ? -9.139  -20.395 17.118  1.00 27.28 ? 1013 THR A O   1 
ATOM   1053 C CB  . THR A 1 147 ? -8.963  -17.333 17.537  1.00 28.49 ? 1013 THR A CB  1 
ATOM   1054 O OG1 . THR A 1 147 ? -7.595  -17.173 17.874  1.00 32.08 ? 1013 THR A OG1 1 
ATOM   1055 C CG2 . THR A 1 147 ? -9.743  -16.063 17.347  1.00 27.16 ? 1013 THR A CG2 1 
ATOM   1056 N N   . SER A 1 148 ? -10.476 -18.889 16.061  1.00 25.02 ? 1014 SER A N   1 
ATOM   1057 C CA  . SER A 1 148 ? -10.448 -19.534 14.727  1.00 24.44 ? 1014 SER A CA  1 
ATOM   1058 C C   . SER A 1 148 ? -9.839  -18.548 13.728  1.00 23.65 ? 1014 SER A C   1 
ATOM   1059 O O   . SER A 1 148 ? -10.097 -17.338 13.849  1.00 23.28 ? 1014 SER A O   1 
ATOM   1060 C CB  . SER A 1 148 ? -11.826 -19.940 14.323  1.00 25.45 ? 1014 SER A CB  1 
ATOM   1061 O OG  . SER A 1 148 ? -12.441 -20.697 15.330  1.00 27.49 ? 1014 SER A OG  1 
ATOM   1062 N N   . VAL A 1 149 ? -9.070  -19.029 12.768  1.00 24.33 ? 1015 VAL A N   1 
ATOM   1063 C CA  . VAL A 1 149 ? -8.552  -18.154 11.677  1.00 24.73 ? 1015 VAL A CA  1 
ATOM   1064 C C   . VAL A 1 149 ? -9.701  -17.310 11.084  1.00 24.37 ? 1015 VAL A C   1 
ATOM   1065 O O   . VAL A 1 149 ? -10.819 -17.850 10.770  1.00 25.08 ? 1015 VAL A O   1 
ATOM   1066 C CB  . VAL A 1 149 ? -7.795  -18.988 10.621  1.00 26.12 ? 1015 VAL A CB  1 
ATOM   1067 C CG1 . VAL A 1 149 ? -7.470  -18.165 9.391   1.00 26.93 ? 1015 VAL A CG1 1 
ATOM   1068 C CG2 . VAL A 1 149 ? -6.515  -19.620 11.185  1.00 26.06 ? 1015 VAL A CG2 1 
ATOM   1069 N N   . GLY A 1 150 ? -9.459  -16.006 10.928  1.00 23.64 ? 1016 GLY A N   1 
ATOM   1070 C CA  . GLY A 1 150 ? -10.397 -15.025 10.345  1.00 23.73 ? 1016 GLY A CA  1 
ATOM   1071 C C   . GLY A 1 150 ? -11.236 -14.308 11.394  1.00 23.63 ? 1016 GLY A C   1 
ATOM   1072 O O   . GLY A 1 150 ? -11.833 -13.289 11.040  1.00 22.64 ? 1016 GLY A O   1 
ATOM   1073 N N   . ASP A 1 151 ? -11.241 -14.776 12.655  1.00 23.24 ? 1017 ASP A N   1 
ATOM   1074 C CA  . ASP A 1 151 ? -12.015 -14.119 13.729  1.00 25.00 ? 1017 ASP A CA  1 
ATOM   1075 C C   . ASP A 1 151 ? -11.304 -12.853 14.210  1.00 24.25 ? 1017 ASP A C   1 
ATOM   1076 O O   . ASP A 1 151 ? -10.085 -12.680 13.935  1.00 22.98 ? 1017 ASP A O   1 
ATOM   1077 C CB  . ASP A 1 151 ? -12.239 -15.090 14.881  1.00 27.71 ? 1017 ASP A CB  1 
ATOM   1078 C CG  . ASP A 1 151 ? -13.327 -16.108 14.556  1.00 31.99 ? 1017 ASP A CG  1 
ATOM   1079 O OD1 . ASP A 1 151 ? -13.937 -15.987 13.486  1.00 30.66 ? 1017 ASP A OD1 1 
ATOM   1080 O OD2 . ASP A 1 151 ? -13.493 -17.029 15.340  1.00 36.48 ? 1017 ASP A OD2 1 
ATOM   1081 N N   . ARG A 1 152 ? -12.024 -12.047 14.981  1.00 24.66 ? 1018 ARG A N   1 
ATOM   1082 C CA  . ARG A 1 152 ? -11.413 -10.889 15.675  1.00 24.53 ? 1018 ARG A CA  1 
ATOM   1083 C C   . ARG A 1 152 ? -11.040 -11.345 17.076  1.00 24.52 ? 1018 ARG A C   1 
ATOM   1084 O O   . ARG A 1 152 ? -11.879 -11.965 17.799  1.00 24.50 ? 1018 ARG A O   1 
ATOM   1085 C CB  . ARG A 1 152 ? -12.350 -9.688  15.681  1.00 27.92 ? 1018 ARG A CB  1 
ATOM   1086 C CG  . ARG A 1 152 ? -11.829 -8.484  16.454  1.00 30.99 ? 1018 ARG A CG  1 
ATOM   1087 C CD  . ARG A 1 152 ? -12.547 -7.193  16.087  1.00 37.50 ? 1018 ARG A CD  1 
ATOM   1088 N NE  . ARG A 1 152 ? -12.158 -6.944  14.698  1.00 43.47 ? 1018 ARG A NE  1 
ATOM   1089 C CZ  . ARG A 1 152 ? -12.976 -6.632  13.704  1.00 47.92 ? 1018 ARG A CZ  1 
ATOM   1090 N NH1 . ARG A 1 152 ? -14.268 -6.435  13.922  1.00 54.55 ? 1018 ARG A NH1 1 
ATOM   1091 N NH2 . ARG A 1 152 ? -12.487 -6.498  12.487  1.00 48.08 ? 1018 ARG A NH2 1 
ATOM   1092 N N   . VAL A 1 153 ? -9.834  -11.007 17.502  1.00 21.10 ? 1019 VAL A N   1 
ATOM   1093 C CA  . VAL A 1 153 ? -9.323  -11.349 18.846  1.00 22.21 ? 1019 VAL A CA  1 
ATOM   1094 C C   . VAL A 1 153 ? -9.189  -10.040 19.631  1.00 20.48 ? 1019 VAL A C   1 
ATOM   1095 O O   . VAL A 1 153 ? -8.663  -9.111  19.034  1.00 18.98 ? 1019 VAL A O   1 
ATOM   1096 C CB  . VAL A 1 153 ? -7.961  -12.046 18.685  1.00 23.20 ? 1019 VAL A CB  1 
ATOM   1097 C CG1 . VAL A 1 153 ? -7.214  -12.107 19.995  1.00 23.70 ? 1019 VAL A CG1 1 
ATOM   1098 C CG2 . VAL A 1 153 ? -8.144  -13.422 18.073  1.00 24.34 ? 1019 VAL A CG2 1 
ATOM   1099 N N   . SER A 1 154 ? -9.700  -9.945  20.857  1.00 20.09 ? 1020 SER A N   1 
ATOM   1100 C CA  . SER A 1 154 ? -9.483  -8.770  21.748  1.00 20.28 ? 1020 SER A CA  1 
ATOM   1101 C C   . SER A 1 154 ? -8.778  -9.262  23.019  1.00 18.91 ? 1020 SER A C   1 
ATOM   1102 O O   . SER A 1 154 ? -9.320  -10.113 23.713  1.00 19.64 ? 1020 SER A O   1 
ATOM   1103 C CB  . SER A 1 154 ? -10.778 -8.051  22.123  1.00 23.59 ? 1020 SER A CB  1 
ATOM   1104 O OG  . SER A 1 154 ? -11.429 -7.621  20.941  1.00 29.71 ? 1020 SER A OG  1 
ATOM   1105 N N   . ILE A 1 155 ? -7.614  -8.706  23.326  1.00 17.83 ? 1021 ILE A N   1 
ATOM   1106 C CA  . ILE A 1 155 ? -6.829  -9.102  24.509  1.00 17.71 ? 1021 ILE A CA  1 
ATOM   1107 C C   . ILE A 1 155 ? -6.771  -7.853  25.367  1.00 17.87 ? 1021 ILE A C   1 
ATOM   1108 O O   . ILE A 1 155 ? -6.278  -6.796  24.862  1.00 16.63 ? 1021 ILE A O   1 
ATOM   1109 C CB  . ILE A 1 155 ? -5.439  -9.613  24.106  1.00 19.07 ? 1021 ILE A CB  1 
ATOM   1110 C CG1 . ILE A 1 155 ? -5.515  -10.892 23.277  1.00 20.41 ? 1021 ILE A CG1 1 
ATOM   1111 C CG2 . ILE A 1 155 ? -4.624  -9.813  25.371  1.00 19.60 ? 1021 ILE A CG2 1 
ATOM   1112 C CD1 . ILE A 1 155 ? -4.202  -11.344 22.715  1.00 20.75 ? 1021 ILE A CD1 1 
ATOM   1113 N N   . THR A 1 156 ? -7.232  -7.916  26.605  1.00 18.25 ? 1022 THR A N   1 
ATOM   1114 C CA  . THR A 1 156 ? -7.335  -6.725  27.446  1.00 19.05 ? 1022 THR A CA  1 
ATOM   1115 C C   . THR A 1 156 ? -6.365  -6.782  28.604  1.00 20.17 ? 1022 THR A C   1 
ATOM   1116 O O   . THR A 1 156 ? -6.009  -7.879  29.132  1.00 20.89 ? 1022 THR A O   1 
ATOM   1117 C CB  . THR A 1 156 ? -8.766  -6.520  27.965  1.00 21.75 ? 1022 THR A CB  1 
ATOM   1118 O OG1 . THR A 1 156 ? -8.984  -7.772  28.631  1.00 30.13 ? 1022 THR A OG1 1 
ATOM   1119 C CG2 . THR A 1 156 ? -9.674  -6.157  26.814  1.00 19.70 ? 1022 THR A CG2 1 
ATOM   1120 N N   . CYS A 1 157 ? -5.985  -5.597  29.014  1.00 21.62 ? 1023 CYS A N   1 
ATOM   1121 C CA  . CYS A 1 157 ? -5.004  -5.392  30.092  1.00 22.30 ? 1023 CYS A CA  1 
ATOM   1122 C C   . CYS A 1 157 ? -5.568  -4.256  30.945  1.00 22.16 ? 1023 CYS A C   1 
ATOM   1123 O O   . CYS A 1 157 ? -5.985  -3.230  30.378  1.00 21.43 ? 1023 CYS A O   1 
ATOM   1124 C CB  . CYS A 1 157 ? -3.654  -5.105  29.484  1.00 26.75 ? 1023 CYS A CB  1 
ATOM   1125 S SG  . CYS A 1 157 ? -2.462  -5.032  30.822  1.00 38.63 ? 1023 CYS A SG  1 
ATOM   1126 N N   . LYS A 1 158 ? -5.751  -4.496  32.235  1.00 21.98 ? 1024 LYS A N   1 
ATOM   1127 C CA  . LYS A 1 158 ? -6.182  -3.449  33.173  1.00 23.03 ? 1024 LYS A CA  1 
ATOM   1128 C C   . LYS A 1 158 ? -4.989  -3.043  34.043  1.00 22.23 ? 1024 LYS A C   1 
ATOM   1129 O O   . LYS A 1 158 ? -4.360  -3.937  34.624  1.00 21.56 ? 1024 LYS A O   1 
ATOM   1130 C CB  . LYS A 1 158 ? -7.306  -3.937  34.097  1.00 27.05 ? 1024 LYS A CB  1 
ATOM   1131 C CG  . LYS A 1 158 ? -7.985  -2.834  34.893  1.00 31.37 ? 1024 LYS A CG  1 
ATOM   1132 C CD  . LYS A 1 158 ? -9.498  -2.997  34.953  1.00 36.41 ? 1024 LYS A CD  1 
ATOM   1133 C CE  . LYS A 1 158 ? -10.243 -1.908  35.700  1.00 39.64 ? 1024 LYS A CE  1 
ATOM   1134 N NZ  . LYS A 1 158 ? -10.390 -0.659  34.905  1.00 40.51 ? 1024 LYS A NZ  1 
ATOM   1135 N N   . ALA A 1 159 ? -4.765  -1.743  34.174  1.00 19.80 ? 1025 ALA A N   1 
ATOM   1136 C CA  . ALA A 1 159 ? -3.704  -1.186  35.038  1.00 19.73 ? 1025 ALA A CA  1 
ATOM   1137 C C   . ALA A 1 159 ? -4.352  -0.865  36.371  1.00 19.92 ? 1025 ALA A C   1 
ATOM   1138 O O   . ALA A 1 159 ? -5.483  -0.368  36.358  1.00 20.78 ? 1025 ALA A O   1 
ATOM   1139 C CB  . ALA A 1 159 ? -3.093  0.074   34.459  1.00 19.04 ? 1025 ALA A CB  1 
ATOM   1140 N N   . SER A 1 160 ? -3.602  -1.051  37.456  1.00 19.08 ? 1026 SER A N   1 
ATOM   1141 C CA  . SER A 1 160 ? -4.057  -0.756  38.839  1.00 21.13 ? 1026 SER A CA  1 
ATOM   1142 C C   . SER A 1 160 ? -4.061  0.760   39.090  1.00 21.41 ? 1026 SER A C   1 
ATOM   1143 O O   . SER A 1 160 ? -4.619  1.166   40.107  1.00 22.07 ? 1026 SER A O   1 
ATOM   1144 C CB  . SER A 1 160 ? -3.195  -1.475  39.842  1.00 20.85 ? 1026 SER A CB  1 
ATOM   1145 O OG  . SER A 1 160 ? -1.842  -0.970  39.831  1.00 19.25 ? 1026 SER A OG  1 
ATOM   1146 N N   . GLN A 1 161 ? -3.434  1.583   38.255  1.00 21.48 ? 1027 GLN A N   1 
ATOM   1147 C CA  . GLN A 1 161 ? -3.540  3.061   38.362  1.00 23.32 ? 1027 GLN A CA  1 
ATOM   1148 C C   . GLN A 1 161 ? -3.515  3.670   36.976  1.00 21.31 ? 1027 GLN A C   1 
ATOM   1149 O O   . GLN A 1 161 ? -3.171  2.931   36.027  1.00 19.19 ? 1027 GLN A O   1 
ATOM   1150 C CB  . GLN A 1 161 ? -2.444  3.732   39.205  1.00 26.81 ? 1027 GLN A CB  1 
ATOM   1151 C CG  . GLN A 1 161 ? -1.106  3.087   39.176  1.00 28.75 ? 1027 GLN A CG  1 
ATOM   1152 C CD  . GLN A 1 161 ? -0.260  3.508   40.377  1.00 30.23 ? 1027 GLN A CD  1 
ATOM   1153 O OE1 . GLN A 1 161 ? 0.129   4.658   40.510  1.00 31.03 ? 1027 GLN A OE1 1 
ATOM   1154 N NE2 . GLN A 1 161 ? 0.120   2.549   41.201  1.00 29.44 ? 1027 GLN A NE2 1 
ATOM   1155 N N   . ASP A 1 162 ? -3.909  4.934   36.883  1.00 20.63 ? 1028 ASP A N   1 
ATOM   1156 C CA  . ASP A 1 162 ? -3.892  5.710   35.617  1.00 21.07 ? 1028 ASP A CA  1 
ATOM   1157 C C   . ASP A 1 162 ? -2.441  5.714   35.072  1.00 20.04 ? 1028 ASP A C   1 
ATOM   1158 O O   . ASP A 1 162 ? -1.583  6.293   35.700  1.00 19.86 ? 1028 ASP A O   1 
ATOM   1159 C CB  . ASP A 1 162 ? -4.395  7.124   35.836  1.00 22.90 ? 1028 ASP A CB  1 
ATOM   1160 C CG  . ASP A 1 162 ? -4.556  7.988   34.601  1.00 25.08 ? 1028 ASP A CG  1 
ATOM   1161 O OD1 . ASP A 1 162 ? -4.249  7.513   33.501  1.00 23.45 ? 1028 ASP A OD1 1 
ATOM   1162 O OD2 . ASP A 1 162 ? -5.056  9.143   34.772  1.00 28.41 ? 1028 ASP A OD2 1 
ATOM   1163 N N   . VAL A 1 163 ? -2.227  5.126   33.911  1.00 18.53 ? 1029 VAL A N   1 
ATOM   1164 C CA  . VAL A 1 163 ? -0.907  5.130   33.223  1.00 17.52 ? 1029 VAL A CA  1 
ATOM   1165 C C   . VAL A 1 163 ? -1.024  5.963   31.951  1.00 17.16 ? 1029 VAL A C   1 
ATOM   1166 O O   . VAL A 1 163 ? -0.080  5.848   31.111  1.00 17.05 ? 1029 VAL A O   1 
ATOM   1167 C CB  . VAL A 1 163 ? -0.414  3.704   32.944  1.00 16.67 ? 1029 VAL A CB  1 
ATOM   1168 C CG1 . VAL A 1 163 ? -0.052  2.988   34.251  1.00 16.99 ? 1029 VAL A CG1 1 
ATOM   1169 C CG2 . VAL A 1 163 ? -1.409  2.897   32.141  1.00 16.27 ? 1029 VAL A CG2 1 
ATOM   1170 N N   . GLY A 1 164 ? -2.085  6.751   31.801  1.00 16.18 ? 1030 GLY A N   1 
ATOM   1171 C CA  . GLY A 1 164 ? -2.242  7.636   30.615  1.00 16.30 ? 1030 GLY A CA  1 
ATOM   1172 C C   . GLY A 1 164 ? -2.343  6.798   29.362  1.00 15.83 ? 1030 GLY A C   1 
ATOM   1173 O O   . GLY A 1 164 ? -3.258  5.942   29.338  1.00 15.12 ? 1030 GLY A O   1 
ATOM   1174 N N   . THR A 1 165 ? -1.466  6.993   28.357  1.00 15.24 ? 1031 THR A N   1 
ATOM   1175 C CA  . THR A 1 165 ? -1.446  6.140   27.144  1.00 15.35 ? 1031 THR A CA  1 
ATOM   1176 C C   . THR A 1 165 ? -0.058  5.495   26.989  1.00 15.00 ? 1031 THR A C   1 
ATOM   1177 O O   . THR A 1 165 ? 0.221   4.970   25.898  1.00 14.75 ? 1031 THR A O   1 
ATOM   1178 C CB  . THR A 1 165 ? -1.869  6.955   25.905  1.00 16.14 ? 1031 THR A CB  1 
ATOM   1179 O OG1 . THR A 1 165 ? -1.005  8.089   25.808  1.00 16.19 ? 1031 THR A OG1 1 
ATOM   1180 C CG2 . THR A 1 165 ? -3.313  7.412   26.028  1.00 17.08 ? 1031 THR A CG2 1 
ATOM   1181 N N   . ALA A 1 166 ? 0.720   5.389   28.055  1.00 15.80 ? 1032 ALA A N   1 
ATOM   1182 C CA  . ALA A 1 166 ? 2.084   4.824   27.987  1.00 15.63 ? 1032 ALA A CA  1 
ATOM   1183 C C   . ALA A 1 166 ? 1.996   3.316   28.187  1.00 15.10 ? 1032 ALA A C   1 
ATOM   1184 O O   . ALA A 1 166 ? 2.443   2.749   29.190  1.00 14.53 ? 1032 ALA A O   1 
ATOM   1185 C CB  . ALA A 1 166 ? 2.981   5.589   28.955  1.00 16.41 ? 1032 ALA A CB  1 
ATOM   1186 N N   . VAL A 1 167 ? 1.427   2.645   27.181  1.00 15.03 ? 1033 VAL A N   1 
ATOM   1187 C CA  . VAL A 1 167 ? 1.243   1.183   27.210  1.00 15.09 ? 1033 VAL A CA  1 
ATOM   1188 C C   . VAL A 1 167 ? 1.736   0.650   25.875  1.00 15.05 ? 1033 VAL A C   1 
ATOM   1189 O O   . VAL A 1 167 ? 1.465   1.245   24.780  1.00 14.70 ? 1033 VAL A O   1 
ATOM   1190 C CB  . VAL A 1 167 ? -0.212  0.784   27.497  1.00 16.02 ? 1033 VAL A CB  1 
ATOM   1191 C CG1 . VAL A 1 167 ? -0.487  -0.683  27.204  1.00 16.67 ? 1033 VAL A CG1 1 
ATOM   1192 C CG2 . VAL A 1 167 ? -0.520  1.066   28.957  1.00 16.80 ? 1033 VAL A CG2 1 
ATOM   1193 N N   . ALA A 1 168 ? 2.434   -0.453  25.959  1.00 13.91 ? 1034 ALA A N   1 
ATOM   1194 C CA  . ALA A 1 168 ? 2.915   -1.196  24.803  1.00 13.52 ? 1034 ALA A CA  1 
ATOM   1195 C C   . ALA A 1 168 ? 2.310   -2.593  24.797  1.00 13.38 ? 1034 ALA A C   1 
ATOM   1196 O O   . ALA A 1 168 ? 1.996   -3.123  25.889  1.00 14.31 ? 1034 ALA A O   1 
ATOM   1197 C CB  . ALA A 1 168 ? 4.426   -1.158  24.854  1.00 13.72 ? 1034 ALA A CB  1 
ATOM   1198 N N   . TRP A 1 169 ? 2.279   -3.209  23.605  1.00 13.36 ? 1035 TRP A N   1 
ATOM   1199 C CA  . TRP A 1 169 ? 1.965   -4.617  23.400  1.00 14.26 ? 1035 TRP A CA  1 
ATOM   1200 C C   . TRP A 1 169 ? 3.105   -5.306  22.667  1.00 15.16 ? 1035 TRP A C   1 
ATOM   1201 O O   . TRP A 1 169 ? 3.558   -4.779  21.666  1.00 15.72 ? 1035 TRP A O   1 
ATOM   1202 C CB  . TRP A 1 169 ? 0.661   -4.792  22.643  1.00 14.03 ? 1035 TRP A CB  1 
ATOM   1203 C CG  . TRP A 1 169 ? -0.537  -4.367  23.430  1.00 14.29 ? 1035 TRP A CG  1 
ATOM   1204 C CD1 . TRP A 1 169 ? -1.147  -3.157  23.418  1.00 14.46 ? 1035 TRP A CD1 1 
ATOM   1205 C CD2 . TRP A 1 169 ? -1.276  -5.180  24.344  1.00 14.26 ? 1035 TRP A CD2 1 
ATOM   1206 N NE1 . TRP A 1 169 ? -2.248  -3.169  24.242  1.00 14.31 ? 1035 TRP A NE1 1 
ATOM   1207 C CE2 . TRP A 1 169 ? -2.329  -4.390  24.833  1.00 14.41 ? 1035 TRP A CE2 1 
ATOM   1208 C CE3 . TRP A 1 169 ? -1.151  -6.502  24.774  1.00 14.35 ? 1035 TRP A CE3 1 
ATOM   1209 C CZ2 . TRP A 1 169 ? -3.264  -4.896  25.710  1.00 14.31 ? 1035 TRP A CZ2 1 
ATOM   1210 C CZ3 . TRP A 1 169 ? -2.078  -7.012  25.651  1.00 14.96 ? 1035 TRP A CZ3 1 
ATOM   1211 C CH2 . TRP A 1 169 ? -3.130  -6.216  26.107  1.00 14.06 ? 1035 TRP A CH2 1 
ATOM   1212 N N   . TYR A 1 170 ? 3.442   -6.493  23.178  1.00 15.53 ? 1036 TYR A N   1 
ATOM   1213 C CA  . TYR A 1 170 ? 4.465   -7.424  22.627  1.00 15.76 ? 1036 TYR A CA  1 
ATOM   1214 C C   . TYR A 1 170 ? 3.813   -8.763  22.261  1.00 15.80 ? 1036 TYR A C   1 
ATOM   1215 O O   . TYR A 1 170 ? 2.894   -9.213  22.945  1.00 16.38 ? 1036 TYR A O   1 
ATOM   1216 C CB  . TYR A 1 170 ? 5.563   -7.623  23.665  1.00 15.08 ? 1036 TYR A CB  1 
ATOM   1217 C CG  . TYR A 1 170 ? 6.398   -6.405  23.850  1.00 14.63 ? 1036 TYR A CG  1 
ATOM   1218 C CD1 . TYR A 1 170 ? 7.487   -6.189  23.025  1.00 14.69 ? 1036 TYR A CD1 1 
ATOM   1219 C CD2 . TYR A 1 170 ? 6.167   -5.501  24.882  1.00 15.06 ? 1036 TYR A CD2 1 
ATOM   1220 C CE1 . TYR A 1 170 ? 8.295   -5.103  23.231  1.00 14.41 ? 1036 TYR A CE1 1 
ATOM   1221 C CE2 . TYR A 1 170 ? 6.950   -4.379  25.053  1.00 15.16 ? 1036 TYR A CE2 1 
ATOM   1222 C CZ  . TYR A 1 170 ? 8.047   -4.201  24.232  1.00 14.72 ? 1036 TYR A CZ  1 
ATOM   1223 O OH  . TYR A 1 170 ? 8.770   -3.058  24.346  1.00 15.93 ? 1036 TYR A OH  1 
ATOM   1224 N N   . GLN A 1 171 ? 4.295   -9.352  21.180  1.00 16.29 ? 1037 GLN A N   1 
ATOM   1225 C CA  . GLN A 1 171 ? 4.091   -10.769 20.818  1.00 17.97 ? 1037 GLN A CA  1 
ATOM   1226 C C   . GLN A 1 171 ? 5.350   -11.546 21.171  1.00 18.88 ? 1037 GLN A C   1 
ATOM   1227 O O   . GLN A 1 171 ? 6.452   -11.027 20.927  1.00 17.48 ? 1037 GLN A O   1 
ATOM   1228 C CB  . GLN A 1 171 ? 3.929   -10.849 19.292  1.00 19.36 ? 1037 GLN A CB  1 
ATOM   1229 C CG  . GLN A 1 171 ? 3.516   -12.222 18.760  1.00 19.88 ? 1037 GLN A CG  1 
ATOM   1230 C CD  . GLN A 1 171 ? 3.375   -12.203 17.260  1.00 21.49 ? 1037 GLN A CD  1 
ATOM   1231 O OE1 . GLN A 1 171 ? 2.293   -12.388 16.681  1.00 25.60 ? 1037 GLN A OE1 1 
ATOM   1232 N NE2 . GLN A 1 171 ? 4.471   -11.986 16.590  1.00 20.55 ? 1037 GLN A NE2 1 
ATOM   1233 N N   . GLN A 1 172 ? 5.204   -12.762 21.708  1.00 20.85 ? 1038 GLN A N   1 
ATOM   1234 C CA  . GLN A 1 172 ? 6.358   -13.668 21.816  1.00 23.00 ? 1038 GLN A CA  1 
ATOM   1235 C C   . GLN A 1 172 ? 5.993   -15.100 21.413  1.00 23.75 ? 1038 GLN A C   1 
ATOM   1236 O O   . GLN A 1 172 ? 5.032   -15.622 21.929  1.00 23.85 ? 1038 GLN A O   1 
ATOM   1237 C CB  . GLN A 1 172 ? 6.958   -13.685 23.198  1.00 23.12 ? 1038 GLN A CB  1 
ATOM   1238 C CG  . GLN A 1 172 ? 8.360   -14.255 23.173  1.00 23.23 ? 1038 GLN A CG  1 
ATOM   1239 C CD  . GLN A 1 172 ? 8.913   -14.412 24.557  1.00 24.69 ? 1038 GLN A CD  1 
ATOM   1240 O OE1 . GLN A 1 172 ? 10.087  -14.685 24.788  1.00 27.15 ? 1038 GLN A OE1 1 
ATOM   1241 N NE2 . GLN A 1 172 ? 8.061   -14.211 25.508  1.00 24.04 ? 1038 GLN A NE2 1 
ATOM   1242 N N   . LYS A 1 173 ? 6.810   -15.679 20.538  1.00 26.44 ? 1039 LYS A N   1 
ATOM   1243 C CA  . LYS A 1 173 ? 6.736   -17.108 20.145  1.00 28.25 ? 1039 LYS A CA  1 
ATOM   1244 C C   . LYS A 1 173 ? 7.792   -17.910 20.906  1.00 30.44 ? 1039 LYS A C   1 
ATOM   1245 O O   . LYS A 1 173 ? 8.831   -17.403 21.302  1.00 27.27 ? 1039 LYS A O   1 
ATOM   1246 C CB  . LYS A 1 173 ? 6.863   -17.203 18.635  1.00 29.11 ? 1039 LYS A CB  1 
ATOM   1247 C CG  . LYS A 1 173 ? 5.805   -16.397 17.900  1.00 28.70 ? 1039 LYS A CG  1 
ATOM   1248 C CD  . LYS A 1 173 ? 5.652   -16.812 16.472  1.00 30.55 ? 1039 LYS A CD  1 
ATOM   1249 C CE  . LYS A 1 173 ? 4.804   -15.813 15.713  1.00 31.29 ? 1039 LYS A CE  1 
ATOM   1250 N NZ  . LYS A 1 173 ? 4.661   -16.208 14.295  1.00 32.26 ? 1039 LYS A NZ  1 
ATOM   1251 N N   . PRO A 1 174 ? 7.576   -19.221 21.095  1.00 33.83 ? 1040 PRO A N   1 
ATOM   1252 C CA  . PRO A 1 174 ? 8.511   -20.037 21.869  1.00 34.12 ? 1040 PRO A CA  1 
ATOM   1253 C C   . PRO A 1 174 ? 9.939   -19.967 21.285  1.00 32.88 ? 1040 PRO A C   1 
ATOM   1254 O O   . PRO A 1 174 ? 10.117  -19.958 20.081  1.00 33.87 ? 1040 PRO A O   1 
ATOM   1255 C CB  . PRO A 1 174 ? 7.866   -21.436 21.766  1.00 37.27 ? 1040 PRO A CB  1 
ATOM   1256 C CG  . PRO A 1 174 ? 6.376   -21.143 21.551  1.00 35.72 ? 1040 PRO A CG  1 
ATOM   1257 C CD  . PRO A 1 174 ? 6.408   -19.971 20.597  1.00 36.00 ? 1040 PRO A CD  1 
ATOM   1258 N N   . GLY A 1 175 ? 10.908  -19.806 22.170  1.00 33.64 ? 1041 GLY A N   1 
ATOM   1259 C CA  . GLY A 1 175 ? 12.348  -19.689 21.849  1.00 34.53 ? 1041 GLY A CA  1 
ATOM   1260 C C   . GLY A 1 175 ? 12.712  -18.409 21.113  1.00 35.52 ? 1041 GLY A C   1 
ATOM   1261 O O   . GLY A 1 175 ? 13.883  -18.317 20.639  1.00 37.24 ? 1041 GLY A O   1 
ATOM   1262 N N   . GLN A 1 176 ? 11.787  -17.451 20.977  1.00 30.27 ? 1042 GLN A N   1 
ATOM   1263 C CA  . GLN A 1 176 ? 12.067  -16.191 20.240  1.00 29.99 ? 1042 GLN A CA  1 
ATOM   1264 C C   . GLN A 1 176 ? 11.971  -15.028 21.228  1.00 26.20 ? 1042 GLN A C   1 
ATOM   1265 O O   . GLN A 1 176 ? 11.373  -15.178 22.283  1.00 27.48 ? 1042 GLN A O   1 
ATOM   1266 C CB  . GLN A 1 176 ? 11.126  -15.986 19.055  1.00 29.15 ? 1042 GLN A CB  1 
ATOM   1267 C CG  . GLN A 1 176 ? 11.236  -17.078 17.980  1.00 34.48 ? 1042 GLN A CG  1 
ATOM   1268 C CD  . GLN A 1 176 ? 10.371  -16.768 16.781  1.00 36.67 ? 1042 GLN A CD  1 
ATOM   1269 O OE1 . GLN A 1 176 ? 10.176  -17.599 15.906  1.00 45.10 ? 1042 GLN A OE1 1 
ATOM   1270 N NE2 . GLN A 1 176 ? 9.801   -15.575 16.709  1.00 38.08 ? 1042 GLN A NE2 1 
ATOM   1271 N N   . SER A 1 177 ? 12.497  -13.874 20.880  1.00 23.22 ? 1043 SER A N   1 
ATOM   1272 C CA  . SER A 1 177 ? 12.457  -12.702 21.772  1.00 23.85 ? 1043 SER A CA  1 
ATOM   1273 C C   . SER A 1 177 ? 11.126  -11.979 21.526  1.00 22.17 ? 1043 SER A C   1 
ATOM   1274 O O   . SER A 1 177 ? 10.468  -12.179 20.498  1.00 20.65 ? 1043 SER A O   1 
ATOM   1275 C CB  . SER A 1 177 ? 13.694  -11.883 21.521  1.00 26.40 ? 1043 SER A CB  1 
ATOM   1276 O OG  . SER A 1 177 ? 13.589  -11.311 20.231  1.00 28.44 ? 1043 SER A OG  1 
ATOM   1277 N N   . PRO A 1 178 ? 10.612  -11.219 22.517  1.00 20.74 ? 1044 PRO A N   1 
ATOM   1278 C CA  . PRO A 1 178 ? 9.428   -10.397 22.309  1.00 20.63 ? 1044 PRO A CA  1 
ATOM   1279 C C   . PRO A 1 178 ? 9.580   -9.464  21.105  1.00 19.83 ? 1044 PRO A C   1 
ATOM   1280 O O   . PRO A 1 178 ? 10.675  -9.046  20.747  1.00 19.35 ? 1044 PRO A O   1 
ATOM   1281 C CB  . PRO A 1 178 ? 9.353   -9.591  23.601  1.00 20.37 ? 1044 PRO A CB  1 
ATOM   1282 C CG  . PRO A 1 178 ? 9.978   -10.495 24.645  1.00 20.79 ? 1044 PRO A CG  1 
ATOM   1283 C CD  . PRO A 1 178 ? 11.157  -11.055 23.875  1.00 21.32 ? 1044 PRO A CD  1 
ATOM   1284 N N   . LYS A 1 179 ? 8.465   -9.206  20.457  1.00 18.78 ? 1045 LYS A N   1 
ATOM   1285 C CA  . LYS A 1 179 ? 8.400   -8.322  19.275  1.00 19.80 ? 1045 LYS A CA  1 
ATOM   1286 C C   . LYS A 1 179 ? 7.404   -7.210  19.559  1.00 17.23 ? 1045 LYS A C   1 
ATOM   1287 O O   . LYS A 1 179 ? 6.256   -7.527  19.899  1.00 16.39 ? 1045 LYS A O   1 
ATOM   1288 C CB  . LYS A 1 179 ? 8.000   -9.132  18.039  1.00 23.13 ? 1045 LYS A CB  1 
ATOM   1289 C CG  . LYS A 1 179 ? 9.096   -10.108 17.624  1.00 28.87 ? 1045 LYS A CG  1 
ATOM   1290 C CD  . LYS A 1 179 ? 10.372  -9.468  17.074  1.00 32.84 ? 1045 LYS A CD  1 
ATOM   1291 C CE  . LYS A 1 179 ? 11.600  -10.363 17.047  1.00 36.77 ? 1045 LYS A CE  1 
ATOM   1292 N NZ  . LYS A 1 179 ? 11.372  -11.675 17.709  1.00 37.87 ? 1045 LYS A NZ  1 
ATOM   1293 N N   . LEU A 1 180 ? 7.813   -5.956  19.408  1.00 16.80 ? 1046 LEU A N   1 
ATOM   1294 C CA  . LEU A 1 180 ? 6.931   -4.821  19.710  1.00 16.00 ? 1046 LEU A CA  1 
ATOM   1295 C C   . LEU A 1 180 ? 5.844   -4.793  18.643  1.00 15.66 ? 1046 LEU A C   1 
ATOM   1296 O O   . LEU A 1 180 ? 6.209   -4.796  17.455  1.00 15.49 ? 1046 LEU A O   1 
ATOM   1297 C CB  . LEU A 1 180 ? 7.699   -3.511  19.778  1.00 16.44 ? 1046 LEU A CB  1 
ATOM   1298 C CG  . LEU A 1 180 ? 6.886   -2.278  20.090  1.00 16.27 ? 1046 LEU A CG  1 
ATOM   1299 C CD1 . LEU A 1 180 ? 6.180   -2.353  21.469  1.00 15.31 ? 1046 LEU A CD1 1 
ATOM   1300 C CD2 . LEU A 1 180 ? 7.747   -1.048  20.016  1.00 17.36 ? 1046 LEU A CD2 1 
ATOM   1301 N N   . LEU A 1 181 ? 4.581   -4.728  19.065  1.00 15.49 ? 1047 LEU A N   1 
ATOM   1302 C CA  . LEU A 1 181 ? 3.448   -4.547  18.121  1.00 15.40 ? 1047 LEU A CA  1 
ATOM   1303 C C   . LEU A 1 181 ? 2.936   -3.082  18.159  1.00 15.08 ? 1047 LEU A C   1 
ATOM   1304 O O   . LEU A 1 181 ? 2.691   -2.453  17.069  1.00 15.38 ? 1047 LEU A O   1 
ATOM   1305 C CB  . LEU A 1 181 ? 2.325   -5.462  18.559  1.00 15.97 ? 1047 LEU A CB  1 
ATOM   1306 C CG  . LEU A 1 181 ? 2.625   -6.955  18.631  1.00 17.13 ? 1047 LEU A CG  1 
ATOM   1307 C CD1 . LEU A 1 181 ? 1.448   -7.645  19.286  1.00 18.92 ? 1047 LEU A CD1 1 
ATOM   1308 C CD2 . LEU A 1 181 ? 3.006   -7.540  17.267  1.00 18.35 ? 1047 LEU A CD2 1 
ATOM   1309 N N   . ILE A 1 182 ? 2.655   -2.581  19.376  1.00 14.30 ? 1048 ILE A N   1 
ATOM   1310 C CA  . ILE A 1 182 ? 1.907   -1.336  19.606  1.00 14.41 ? 1048 ILE A CA  1 
ATOM   1311 C C   . ILE A 1 182 ? 2.641   -0.567  20.684  1.00 13.79 ? 1048 ILE A C   1 
ATOM   1312 O O   . ILE A 1 182 ? 3.034   -1.179  21.706  1.00 13.20 ? 1048 ILE A O   1 
ATOM   1313 C CB  . ILE A 1 182 ? 0.450   -1.621  20.052  1.00 15.18 ? 1048 ILE A CB  1 
ATOM   1314 C CG1 . ILE A 1 182 ? -0.353  -2.379  18.985  1.00 15.84 ? 1048 ILE A CG1 1 
ATOM   1315 C CG2 . ILE A 1 182 ? -0.216  -0.361  20.533  1.00 15.71 ? 1048 ILE A CG2 1 
ATOM   1316 C CD1 . ILE A 1 182 ? -0.637  -1.580  17.692  1.00 16.21 ? 1048 ILE A CD1 1 
ATOM   1317 N N   . TYR A 1 183 ? 2.732   0.739   20.525  1.00 13.78 ? 1049 TYR A N   1 
ATOM   1318 C CA  . TYR A 1 183 ? 3.203   1.595   21.641  1.00 13.94 ? 1049 TYR A CA  1 
ATOM   1319 C C   . TYR A 1 183 ? 2.411   2.878   21.678  1.00 14.51 ? 1049 TYR A C   1 
ATOM   1320 O O   . TYR A 1 183 ? 1.615   3.177   20.792  1.00 15.69 ? 1049 TYR A O   1 
ATOM   1321 C CB  . TYR A 1 183 ? 4.718   1.815   21.595  1.00 13.59 ? 1049 TYR A CB  1 
ATOM   1322 C CG  . TYR A 1 183 ? 5.203   2.519   20.350  1.00 14.28 ? 1049 TYR A CG  1 
ATOM   1323 C CD1 . TYR A 1 183 ? 5.360   3.885   20.324  1.00 15.53 ? 1049 TYR A CD1 1 
ATOM   1324 C CD2 . TYR A 1 183 ? 5.363   1.819   19.176  1.00 14.44 ? 1049 TYR A CD2 1 
ATOM   1325 C CE1 . TYR A 1 183 ? 5.792   4.547   19.181  1.00 15.70 ? 1049 TYR A CE1 1 
ATOM   1326 C CE2 . TYR A 1 183 ? 5.783   2.449   18.007  1.00 14.90 ? 1049 TYR A CE2 1 
ATOM   1327 C CZ  . TYR A 1 183 ? 5.987   3.808   18.026  1.00 15.47 ? 1049 TYR A CZ  1 
ATOM   1328 O OH  . TYR A 1 183 ? 6.372   4.433   16.891  1.00 17.68 ? 1049 TYR A OH  1 
ATOM   1329 N N   . TRP A 1 184 ? 2.545   3.609   22.798  1.00 15.13 ? 1050 TRP A N   1 
ATOM   1330 C CA  . TRP A 1 184 ? 1.686   4.783   23.031  1.00 16.67 ? 1050 TRP A CA  1 
ATOM   1331 C C   . TRP A 1 184 ? 0.209   4.400   22.900  1.00 15.98 ? 1050 TRP A C   1 
ATOM   1332 O O   . TRP A 1 184 ? -0.544  5.191   22.358  1.00 15.86 ? 1050 TRP A O   1 
ATOM   1333 C CB  . TRP A 1 184 ? 2.137   5.966   22.154  1.00 18.40 ? 1050 TRP A CB  1 
ATOM   1334 C CG  . TRP A 1 184 ? 3.372   6.627   22.699  1.00 21.85 ? 1050 TRP A CG  1 
ATOM   1335 C CD1 . TRP A 1 184 ? 4.594   6.742   22.080  1.00 25.24 ? 1050 TRP A CD1 1 
ATOM   1336 C CD2 . TRP A 1 184 ? 3.516   7.279   23.973  1.00 22.45 ? 1050 TRP A CD2 1 
ATOM   1337 N NE1 . TRP A 1 184 ? 5.468   7.401   22.889  1.00 27.45 ? 1050 TRP A NE1 1 
ATOM   1338 C CE2 . TRP A 1 184 ? 4.855   7.710   24.072  1.00 25.37 ? 1050 TRP A CE2 1 
ATOM   1339 C CE3 . TRP A 1 184 ? 2.659   7.501   25.042  1.00 22.98 ? 1050 TRP A CE3 1 
ATOM   1340 C CZ2 . TRP A 1 184 ? 5.293   8.472   25.152  1.00 24.94 ? 1050 TRP A CZ2 1 
ATOM   1341 C CZ3 . TRP A 1 184 ? 3.096   8.219   26.130  1.00 24.80 ? 1050 TRP A CZ3 1 
ATOM   1342 C CH2 . TRP A 1 184 ? 4.413   8.675   26.175  1.00 23.47 ? 1050 TRP A CH2 1 
ATOM   1343 N N   . ALA A 1 185 ? -0.120  3.186   23.351  1.00 14.89 ? 1051 ALA A N   1 
ATOM   1344 C CA  . ALA A 1 185 ? -1.465  2.560   23.404  1.00 15.01 ? 1051 ALA A CA  1 
ATOM   1345 C C   . ALA A 1 185 ? -1.990  2.170   22.033  1.00 15.13 ? 1051 ALA A C   1 
ATOM   1346 O O   . ALA A 1 185 ? -2.651  1.151   21.965  1.00 15.16 ? 1051 ALA A O   1 
ATOM   1347 C CB  . ALA A 1 185 ? -2.463  3.417   24.120  1.00 15.24 ? 1051 ALA A CB  1 
ATOM   1348 N N   . SER A 1 186 ? -1.758  2.966   20.987  1.00 15.92 ? 1052 SER A N   1 
ATOM   1349 C CA  . SER A 1 186 ? -2.466  2.785   19.682  1.00 16.53 ? 1052 SER A CA  1 
ATOM   1350 C C   . SER A 1 186 ? -1.556  2.924   18.462  1.00 16.56 ? 1052 SER A C   1 
ATOM   1351 O O   . SER A 1 186 ? -2.059  2.729   17.328  1.00 16.97 ? 1052 SER A O   1 
ATOM   1352 C CB  . SER A 1 186 ? -3.610  3.777   19.545  1.00 17.98 ? 1052 SER A CB  1 
ATOM   1353 O OG  . SER A 1 186 ? -3.081  5.103   19.573  1.00 17.86 ? 1052 SER A OG  1 
ATOM   1354 N N   . THR A 1 187 ? -0.263  3.144   18.645  1.00 16.64 ? 1053 THR A N   1 
ATOM   1355 C CA  . THR A 1 187 ? 0.651   3.370   17.491  1.00 17.92 ? 1053 THR A CA  1 
ATOM   1356 C C   . THR A 1 187 ? 1.260   2.020   17.096  1.00 17.98 ? 1053 THR A C   1 
ATOM   1357 O O   . THR A 1 187 ? 1.967   1.349   17.911  1.00 16.08 ? 1053 THR A O   1 
ATOM   1358 C CB  . THR A 1 187 ? 1.729   4.409   17.802  1.00 19.65 ? 1053 THR A CB  1 
ATOM   1359 O OG1 . THR A 1 187 ? 1.008   5.606   18.089  1.00 23.00 ? 1053 THR A OG1 1 
ATOM   1360 C CG2 . THR A 1 187 ? 2.694   4.591   16.637  1.00 20.21 ? 1053 THR A CG2 1 
ATOM   1361 N N   . ARG A 1 188 ? 1.087   1.640   15.830  1.00 18.15 ? 1054 ARG A N   1 
ATOM   1362 C CA  A ARG A 1 188 ? 1.636   0.373   15.322  0.50 18.50 ? 1054 ARG A CA  1 
ATOM   1363 C CA  B ARG A 1 188 ? 1.640   0.374   15.331  0.50 19.15 ? 1054 ARG A CA  1 
ATOM   1364 C C   . ARG A 1 188 ? 3.133   0.571   15.064  1.00 18.87 ? 1054 ARG A C   1 
ATOM   1365 O O   . ARG A 1 188 ? 3.493   1.534   14.423  1.00 19.75 ? 1054 ARG A O   1 
ATOM   1366 C CB  A ARG A 1 188 ? 0.855   -0.043  14.071  0.50 18.94 ? 1054 ARG A CB  1 
ATOM   1367 C CB  B ARG A 1 188 ? 0.866   -0.058  14.085  0.50 20.56 ? 1054 ARG A CB  1 
ATOM   1368 C CG  A ARG A 1 188 ? 0.948   -1.524  13.774  0.50 19.28 ? 1054 ARG A CG  1 
ATOM   1369 C CG  B ARG A 1 188 ? 0.945   -1.547  13.844  0.50 21.97 ? 1054 ARG A CG  1 
ATOM   1370 C CD  A ARG A 1 188 ? 0.202   -2.004  12.545  0.50 19.24 ? 1054 ARG A CD  1 
ATOM   1371 C CD  B ARG A 1 188 ? 0.253   -1.990  12.585  0.50 22.77 ? 1054 ARG A CD  1 
ATOM   1372 N NE  A ARG A 1 188 ? -0.077  -0.978  11.554  0.50 19.45 ? 1054 ARG A NE  1 
ATOM   1373 N NE  B ARG A 1 188 ? -1.174  -1.866  12.768  0.50 24.56 ? 1054 ARG A NE  1 
ATOM   1374 C CZ  A ARG A 1 188 ? 0.742   -0.629  10.553  0.50 20.46 ? 1054 ARG A CZ  1 
ATOM   1375 C CZ  B ARG A 1 188 ? -1.901  -0.972  12.146  0.50 24.32 ? 1054 ARG A CZ  1 
ATOM   1376 N NH1 A ARG A 1 188 ? 1.931   -1.191  10.368  0.50 20.29 ? 1054 ARG A NH1 1 
ATOM   1377 N NH1 B ARG A 1 188 ? -1.298  -0.128  11.324  0.50 25.27 ? 1054 ARG A NH1 1 
ATOM   1378 N NH2 A ARG A 1 188 ? 0.368   0.325   9.733   0.50 21.77 ? 1054 ARG A NH2 1 
ATOM   1379 N NH2 B ARG A 1 188 ? -3.200  -0.923  12.357  0.50 23.67 ? 1054 ARG A NH2 1 
ATOM   1380 N N   . HIS A 1 189 ? 3.949   -0.344  15.525  1.00 18.32 ? 1055 HIS A N   1 
ATOM   1381 C CA  . HIS A 1 189 ? 5.419   -0.366  15.262  1.00 18.46 ? 1055 HIS A CA  1 
ATOM   1382 C C   . HIS A 1 189 ? 5.663   -0.711  13.787  1.00 20.19 ? 1055 HIS A C   1 
ATOM   1383 O O   . HIS A 1 189 ? 4.893   -1.478  13.151  1.00 18.67 ? 1055 HIS A O   1 
ATOM   1384 C CB  . HIS A 1 189 ? 6.065   -1.368  16.208  1.00 18.55 ? 1055 HIS A CB  1 
ATOM   1385 C CG  . HIS A 1 189 ? 7.567   -1.361  16.149  1.00 19.26 ? 1055 HIS A CG  1 
ATOM   1386 N ND1 . HIS A 1 189 ? 8.305   -0.225  15.966  1.00 21.16 ? 1055 HIS A ND1 1 
ATOM   1387 C CD2 . HIS A 1 189 ? 8.450   -2.367  16.272  1.00 20.32 ? 1055 HIS A CD2 1 
ATOM   1388 C CE1 . HIS A 1 189 ? 9.593   -0.527  15.895  1.00 22.24 ? 1055 HIS A CE1 1 
ATOM   1389 N NE2 . HIS A 1 189 ? 9.700   -1.861  16.076  1.00 21.89 ? 1055 HIS A NE2 1 
ATOM   1390 N N   . THR A 1 190 ? 6.752   -0.188  13.253  1.00 21.85 ? 1056 THR A N   1 
ATOM   1391 C CA  . THR A 1 190 ? 7.123   -0.383  11.834  1.00 23.84 ? 1056 THR A CA  1 
ATOM   1392 C C   . THR A 1 190 ? 7.093   -1.873  11.526  1.00 23.91 ? 1056 THR A C   1 
ATOM   1393 O O   . THR A 1 190 ? 7.697   -2.643  12.287  1.00 23.96 ? 1056 THR A O   1 
ATOM   1394 C CB  . THR A 1 190 ? 8.492   0.246   11.523  1.00 25.25 ? 1056 THR A CB  1 
ATOM   1395 O OG1 . THR A 1 190 ? 8.574   1.577   12.048  1.00 23.76 ? 1056 THR A OG1 1 
ATOM   1396 C CG2 . THR A 1 190 ? 8.733   0.244   10.027  1.00 27.24 ? 1056 THR A CG2 1 
ATOM   1397 N N   . GLY A 1 191 ? 6.430   -2.263  10.447  1.00 24.46 ? 1057 GLY A N   1 
ATOM   1398 C CA  . GLY A 1 191 ? 6.520   -3.656  9.956   1.00 25.69 ? 1057 GLY A CA  1 
ATOM   1399 C C   . GLY A 1 191 ? 5.399   -4.523  10.469  1.00 25.02 ? 1057 GLY A C   1 
ATOM   1400 O O   . GLY A 1 191 ? 5.239   -5.648  9.940   1.00 29.06 ? 1057 GLY A O   1 
ATOM   1401 N N   . VAL A 1 192 ? 4.639   -4.062  11.462  1.00 22.09 ? 1058 VAL A N   1 
ATOM   1402 C CA  . VAL A 1 192 ? 3.607   -4.897  12.112  1.00 21.48 ? 1058 VAL A CA  1 
ATOM   1403 C C   . VAL A 1 192 ? 2.421   -4.893  11.170  1.00 20.96 ? 1058 VAL A C   1 
ATOM   1404 O O   . VAL A 1 192 ? 2.097   -3.831  10.631  1.00 20.99 ? 1058 VAL A O   1 
ATOM   1405 C CB  . VAL A 1 192 ? 3.237   -4.319  13.489  1.00 21.42 ? 1058 VAL A CB  1 
ATOM   1406 C CG1 . VAL A 1 192 ? 1.989   -4.964  14.098  1.00 21.71 ? 1058 VAL A CG1 1 
ATOM   1407 C CG2 . VAL A 1 192 ? 4.449   -4.404  14.405  1.00 21.40 ? 1058 VAL A CG2 1 
ATOM   1408 N N   . PRO A 1 193 ? 1.766   -6.046  10.930  1.00 21.57 ? 1059 PRO A N   1 
ATOM   1409 C CA  . PRO A 1 193 ? 0.655   -6.074  10.002  1.00 21.57 ? 1059 PRO A CA  1 
ATOM   1410 C C   . PRO A 1 193 ? -0.478  -5.154  10.427  1.00 21.53 ? 1059 PRO A C   1 
ATOM   1411 O O   . PRO A 1 193 ? -0.735  -4.964  11.629  1.00 20.58 ? 1059 PRO A O   1 
ATOM   1412 C CB  . PRO A 1 193 ? 0.195   -7.554  9.946   1.00 21.62 ? 1059 PRO A CB  1 
ATOM   1413 C CG  . PRO A 1 193 ? 1.414   -8.327  10.432  1.00 21.80 ? 1059 PRO A CG  1 
ATOM   1414 C CD  . PRO A 1 193 ? 2.126   -7.396  11.399  1.00 21.24 ? 1059 PRO A CD  1 
ATOM   1415 N N   . ASP A 1 194 ? -1.186  -4.660  9.413   1.00 21.55 ? 1060 ASP A N   1 
ATOM   1416 C CA  . ASP A 1 194 ? -2.332  -3.723  9.560   1.00 23.43 ? 1060 ASP A CA  1 
ATOM   1417 C C   . ASP A 1 194 ? -3.358  -4.277  10.529  1.00 20.42 ? 1060 ASP A C   1 
ATOM   1418 O O   . ASP A 1 194 ? -4.004  -3.467  11.210  1.00 20.92 ? 1060 ASP A O   1 
ATOM   1419 C CB  . ASP A 1 194 ? -3.050  -3.456  8.233   1.00 25.07 ? 1060 ASP A CB  1 
ATOM   1420 C CG  . ASP A 1 194 ? -2.191  -2.722  7.229   1.00 28.03 ? 1060 ASP A CG  1 
ATOM   1421 O OD1 . ASP A 1 194 ? -1.267  -2.008  7.690   1.00 28.38 ? 1060 ASP A OD1 1 
ATOM   1422 O OD2 . ASP A 1 194 ? -2.464  -2.899  5.983   1.00 28.81 ? 1060 ASP A OD2 1 
ATOM   1423 N N   . ARG A 1 195 ? -3.535  -5.600  10.590  1.00 20.08 ? 1061 ARG A N   1 
ATOM   1424 C CA  . ARG A 1 195 ? -4.611  -6.223  11.402  1.00 18.81 ? 1061 ARG A CA  1 
ATOM   1425 C C   . ARG A 1 195 ? -4.405  -6.032  12.913  1.00 18.71 ? 1061 ARG A C   1 
ATOM   1426 O O   . ARG A 1 195 ? -5.335  -6.365  13.634  1.00 18.94 ? 1061 ARG A O   1 
ATOM   1427 C CB  . ARG A 1 195 ? -4.780  -7.695  11.013  1.00 19.91 ? 1061 ARG A CB  1 
ATOM   1428 C CG  . ARG A 1 195 ? -3.679  -8.635  11.468  1.00 19.70 ? 1061 ARG A CG  1 
ATOM   1429 C CD  . ARG A 1 195 ? -3.917  -10.016 10.878  1.00 20.68 ? 1061 ARG A CD  1 
ATOM   1430 N NE  . ARG A 1 195 ? -2.760  -10.887 11.051  1.00 20.26 ? 1061 ARG A NE  1 
ATOM   1431 C CZ  . ARG A 1 195 ? -1.724  -10.995 10.213  1.00 20.44 ? 1061 ARG A CZ  1 
ATOM   1432 N NH1 . ARG A 1 195 ? -1.624  -10.225 9.153   1.00 19.86 ? 1061 ARG A NH1 1 
ATOM   1433 N NH2 . ARG A 1 195 ? -0.750  -11.846 10.482  1.00 21.09 ? 1061 ARG A NH2 1 
ATOM   1434 N N   . PHE A 1 196 ? -3.220  -5.587  13.371  1.00 17.37 ? 1062 PHE A N   1 
ATOM   1435 C CA  . PHE A 1 196 ? -2.989  -5.370  14.824  1.00 17.92 ? 1062 PHE A CA  1 
ATOM   1436 C C   . PHE A 1 196 ? -3.304  -3.918  15.152  1.00 17.30 ? 1062 PHE A C   1 
ATOM   1437 O O   . PHE A 1 196 ? -2.656  -3.013  14.595  1.00 17.05 ? 1062 PHE A O   1 
ATOM   1438 C CB  . PHE A 1 196 ? -1.544  -5.669  15.229  1.00 18.01 ? 1062 PHE A CB  1 
ATOM   1439 C CG  . PHE A 1 196 ? -1.210  -7.136  15.167  1.00 18.61 ? 1062 PHE A CG  1 
ATOM   1440 C CD1 . PHE A 1 196 ? -0.783  -7.718  13.976  1.00 19.65 ? 1062 PHE A CD1 1 
ATOM   1441 C CD2 . PHE A 1 196 ? -1.321  -7.922  16.295  1.00 18.39 ? 1062 PHE A CD2 1 
ATOM   1442 C CE1 . PHE A 1 196 ? -0.455  -9.068  13.947  1.00 20.16 ? 1062 PHE A CE1 1 
ATOM   1443 C CE2 . PHE A 1 196 ? -0.998  -9.261  16.261  1.00 19.15 ? 1062 PHE A CE2 1 
ATOM   1444 C CZ  . PHE A 1 196 ? -0.587  -9.844  15.081  1.00 19.09 ? 1062 PHE A CZ  1 
ATOM   1445 N N   . THR A 1 197 ? -4.251  -3.707  16.056  1.00 17.18 ? 1063 THR A N   1 
ATOM   1446 C CA  . THR A 1 197 ? -4.586  -2.352  16.528  1.00 17.85 ? 1063 THR A CA  1 
ATOM   1447 C C   . THR A 1 197 ? -4.594  -2.342  18.056  1.00 17.07 ? 1063 THR A C   1 
ATOM   1448 O O   . THR A 1 197 ? -4.801  -3.363  18.731  1.00 17.45 ? 1063 THR A O   1 
ATOM   1449 C CB  . THR A 1 197 ? -5.929  -1.851  15.968  1.00 18.98 ? 1063 THR A CB  1 
ATOM   1450 O OG1 . THR A 1 197 ? -6.974  -2.762  16.294  1.00 18.35 ? 1063 THR A OG1 1 
ATOM   1451 C CG2 . THR A 1 197 ? -5.890  -1.624  14.492  1.00 19.30 ? 1063 THR A CG2 1 
ATOM   1452 N N   . GLY A 1 198 ? -4.323  -1.182  18.597  1.00 16.24 ? 1064 GLY A N   1 
ATOM   1453 C CA  . GLY A 1 198 ? -4.314  -0.957  20.044  1.00 15.93 ? 1064 GLY A CA  1 
ATOM   1454 C C   . GLY A 1 198 ? -5.248  0.171   20.362  1.00 15.60 ? 1064 GLY A C   1 
ATOM   1455 O O   . GLY A 1 198 ? -5.389  1.130   19.588  1.00 13.97 ? 1064 GLY A O   1 
ATOM   1456 N N   . SER A 1 199 ? -5.857  0.108   21.520  1.00 16.41 ? 1065 SER A N   1 
ATOM   1457 C CA  . SER A 1 199 ? -6.697  1.213   22.008  1.00 17.36 ? 1065 SER A CA  1 
ATOM   1458 C C   . SER A 1 199 ? -6.561  1.308   23.517  1.00 17.63 ? 1065 SER A C   1 
ATOM   1459 O O   . SER A 1 199 ? -6.165  0.312   24.196  1.00 16.37 ? 1065 SER A O   1 
ATOM   1460 C CB  . SER A 1 199 ? -8.152  0.941   21.559  1.00 19.00 ? 1065 SER A CB  1 
ATOM   1461 O OG  . SER A 1 199 ? -8.525  -0.352  22.050  1.00 20.98 ? 1065 SER A OG  1 
ATOM   1462 N N   . GLY A 1 200 ? -6.994  2.440   24.038  1.00 18.56 ? 1066 GLY A N   1 
ATOM   1463 C CA  . GLY A 1 200 ? -7.182  2.582   25.483  1.00 19.87 ? 1066 GLY A CA  1 
ATOM   1464 C C   . GLY A 1 200 ? -6.409  3.734   26.096  1.00 19.50 ? 1066 GLY A C   1 
ATOM   1465 O O   . GLY A 1 200 ? -5.573  4.345   25.474  1.00 19.75 ? 1066 GLY A O   1 
ATOM   1466 N N   . SER A 1 201 ? -6.811  4.091   27.287  1.00 19.91 ? 1067 SER A N   1 
ATOM   1467 C CA  . SER A 1 201 ? -6.155  5.129   28.098  1.00 20.60 ? 1067 SER A CA  1 
ATOM   1468 C C   . SER A 1 201 ? -6.598  4.958   29.527  1.00 20.29 ? 1067 SER A C   1 
ATOM   1469 O O   . SER A 1 201 ? -7.671  4.326   29.747  1.00 20.53 ? 1067 SER A O   1 
ATOM   1470 C CB  . SER A 1 201 ? -6.513  6.521   27.609  1.00 23.80 ? 1067 SER A CB  1 
ATOM   1471 O OG  . SER A 1 201 ? -7.875  6.748   27.853  1.00 28.36 ? 1067 SER A OG  1 
ATOM   1472 N N   . GLY A 1 202 ? -5.814  5.503   30.449  1.00 19.22 ? 1068 GLY A N   1 
ATOM   1473 C CA  . GLY A 1 202 ? -6.135  5.445   31.875  1.00 19.74 ? 1068 GLY A CA  1 
ATOM   1474 C C   . GLY A 1 202 ? -5.804  4.076   32.432  1.00 18.85 ? 1068 GLY A C   1 
ATOM   1475 O O   . GLY A 1 202 ? -4.636  3.838   32.692  1.00 17.62 ? 1068 GLY A O   1 
ATOM   1476 N N   . THR A 1 203 ? -6.810  3.223   32.639  1.00 18.46 ? 1069 THR A N   1 
ATOM   1477 C CA  . THR A 1 203 ? -6.617  1.882   33.231  1.00 18.74 ? 1069 THR A CA  1 
ATOM   1478 C C   . THR A 1 203 ? -7.027  0.757   32.288  1.00 19.34 ? 1069 THR A C   1 
ATOM   1479 O O   . THR A 1 203 ? -6.739  -0.399  32.644  1.00 20.33 ? 1069 THR A O   1 
ATOM   1480 C CB  . THR A 1 203 ? -7.352  1.783   34.555  1.00 20.14 ? 1069 THR A CB  1 
ATOM   1481 O OG1 . THR A 1 203 ? -8.749  1.877   34.245  1.00 21.28 ? 1069 THR A OG1 1 
ATOM   1482 C CG2 . THR A 1 203 ? -6.890  2.883   35.484  1.00 20.72 ? 1069 THR A CG2 1 
ATOM   1483 N N   . ASP A 1 204 ? -7.593  1.023   31.120  1.00 18.57 ? 1070 ASP A N   1 
ATOM   1484 C CA  A ASP A 1 204 ? -8.111  -0.082  30.269  0.50 18.23 ? 1070 ASP A CA  1 
ATOM   1485 C CA  B ASP A 1 204 ? -8.089  -0.103  30.278  0.50 18.91 ? 1070 ASP A CA  1 
ATOM   1486 C C   . ASP A 1 204 ? -7.418  -0.037  28.909  1.00 17.08 ? 1070 ASP A C   1 
ATOM   1487 O O   . ASP A 1 204 ? -7.505  0.999   28.257  1.00 15.36 ? 1070 ASP A O   1 
ATOM   1488 C CB  A ASP A 1 204 ? -9.625  0.017   30.104  0.50 19.22 ? 1070 ASP A CB  1 
ATOM   1489 C CB  B ASP A 1 204 ? -9.612  -0.135  30.152  0.50 20.84 ? 1070 ASP A CB  1 
ATOM   1490 C CG  A ASP A 1 204 ? -10.400 -0.193  31.394  0.50 19.97 ? 1070 ASP A CG  1 
ATOM   1491 C CG  B ASP A 1 204 ? -10.191 0.841   29.148  0.50 22.55 ? 1070 ASP A CG  1 
ATOM   1492 O OD1 A ASP A 1 204 ? -10.096 -1.151  32.114  0.50 20.07 ? 1070 ASP A OD1 1 
ATOM   1493 O OD1 B ASP A 1 204 ? -9.893  2.052   29.245  0.50 26.32 ? 1070 ASP A OD1 1 
ATOM   1494 O OD2 A ASP A 1 204 ? -11.359 0.588   31.655  0.50 21.75 ? 1070 ASP A OD2 1 
ATOM   1495 O OD2 B ASP A 1 204 ? -10.974 0.404   28.309  0.50 22.22 ? 1070 ASP A OD2 1 
ATOM   1496 N N   . PHE A 1 205 ? -6.840  -1.160  28.502  1.00 15.97 ? 1071 PHE A N   1 
ATOM   1497 C CA  . PHE A 1 205 ? -6.079  -1.221  27.250  1.00 15.11 ? 1071 PHE A CA  1 
ATOM   1498 C C   . PHE A 1 205 ? -6.391  -2.531  26.562  1.00 14.53 ? 1071 PHE A C   1 
ATOM   1499 O O   . PHE A 1 205 ? -6.502  -3.550  27.237  1.00 14.83 ? 1071 PHE A O   1 
ATOM   1500 C CB  . PHE A 1 205 ? -4.570  -1.088  27.484  1.00 14.76 ? 1071 PHE A CB  1 
ATOM   1501 C CG  . PHE A 1 205 ? -4.244  0.194   28.179  1.00 15.17 ? 1071 PHE A CG  1 
ATOM   1502 C CD1 . PHE A 1 205 ? -3.946  1.335   27.472  1.00 15.18 ? 1071 PHE A CD1 1 
ATOM   1503 C CD2 . PHE A 1 205 ? -4.316  0.261   29.530  1.00 15.82 ? 1071 PHE A CD2 1 
ATOM   1504 C CE1 . PHE A 1 205 ? -3.750  2.538   28.116  1.00 15.88 ? 1071 PHE A CE1 1 
ATOM   1505 C CE2 . PHE A 1 205 ? -4.095  1.455   30.194  1.00 16.91 ? 1071 PHE A CE2 1 
ATOM   1506 C CZ  . PHE A 1 205 ? -3.779  2.586   29.483  1.00 16.44 ? 1071 PHE A CZ  1 
ATOM   1507 N N   . THR A 1 206 ? -6.531  -2.457  25.247  1.00 14.61 ? 1072 THR A N   1 
ATOM   1508 C CA  . THR A 1 206 ? -6.881  -3.626  24.424  1.00 14.45 ? 1072 THR A CA  1 
ATOM   1509 C C   . THR A 1 206 ? -5.966  -3.694  23.187  1.00 14.71 ? 1072 THR A C   1 
ATOM   1510 O O   . THR A 1 206 ? -5.866  -2.681  22.451  1.00 15.44 ? 1072 THR A O   1 
ATOM   1511 C CB  . THR A 1 206 ? -8.348  -3.612  23.979  1.00 14.96 ? 1072 THR A CB  1 
ATOM   1512 O OG1 . THR A 1 206 ? -9.054  -3.595  25.221  1.00 15.13 ? 1072 THR A OG1 1 
ATOM   1513 C CG2 . THR A 1 206 ? -8.683  -4.847  23.181  1.00 15.68 ? 1072 THR A CG2 1 
ATOM   1514 N N   . LEU A 1 207 ? -5.477  -4.884  22.924  1.00 14.41 ? 1073 LEU A N   1 
ATOM   1515 C CA  . LEU A 1 207 ? -4.891  -5.259  21.629  1.00 15.44 ? 1073 LEU A CA  1 
ATOM   1516 C C   . LEU A 1 207 ? -5.944  -6.034  20.840  1.00 16.00 ? 1073 LEU A C   1 
ATOM   1517 O O   . LEU A 1 207 ? -6.491  -7.022  21.366  1.00 16.88 ? 1073 LEU A O   1 
ATOM   1518 C CB  . LEU A 1 207 ? -3.645  -6.112  21.825  1.00 15.72 ? 1073 LEU A CB  1 
ATOM   1519 C CG  . LEU A 1 207 ? -3.016  -6.654  20.549  1.00 15.66 ? 1073 LEU A CG  1 
ATOM   1520 C CD1 . LEU A 1 207 ? -2.317  -5.580  19.804  1.00 15.79 ? 1073 LEU A CD1 1 
ATOM   1521 C CD2 . LEU A 1 207 ? -2.062  -7.797  20.820  1.00 17.15 ? 1073 LEU A CD2 1 
ATOM   1522 N N   . THR A 1 208 ? -6.250  -5.551  19.654  1.00 16.43 ? 1074 THR A N   1 
ATOM   1523 C CA  . THR A 1 208 ? -7.214  -6.229  18.742  1.00 17.29 ? 1074 THR A CA  1 
ATOM   1524 C C   . THR A 1 208 ? -6.420  -6.816  17.594  1.00 18.44 ? 1074 THR A C   1 
ATOM   1525 O O   . THR A 1 208 ? -5.570  -6.105  17.005  1.00 17.51 ? 1074 THR A O   1 
ATOM   1526 C CB  . THR A 1 208 ? -8.330  -5.288  18.309  1.00 18.78 ? 1074 THR A CB  1 
ATOM   1527 O OG1 . THR A 1 208 ? -8.966  -4.837  19.492  1.00 18.09 ? 1074 THR A OG1 1 
ATOM   1528 C CG2 . THR A 1 208 ? -9.364  -5.986  17.434  1.00 19.39 ? 1074 THR A CG2 1 
ATOM   1529 N N   . ILE A 1 209 ? -6.666  -8.089  17.314  1.00 19.49 ? 1075 ILE A N   1 
ATOM   1530 C CA  . ILE A 1 209 ? -6.148  -8.731  16.081  1.00 19.29 ? 1075 ILE A CA  1 
ATOM   1531 C C   . ILE A 1 209 ? -7.357  -9.031  15.214  1.00 18.98 ? 1075 ILE A C   1 
ATOM   1532 O O   . ILE A 1 209 ? -8.113  -9.899  15.609  1.00 20.97 ? 1075 ILE A O   1 
ATOM   1533 C CB  . ILE A 1 209 ? -5.331  -9.985  16.363  1.00 20.16 ? 1075 ILE A CB  1 
ATOM   1534 C CG1 . ILE A 1 209 ? -4.397  -9.817  17.580  1.00 21.18 ? 1075 ILE A CG1 1 
ATOM   1535 C CG2 . ILE A 1 209 ? -4.582  -10.317 15.087  1.00 21.62 ? 1075 ILE A CG2 1 
ATOM   1536 C CD1 . ILE A 1 209 ? -3.677  -11.086 17.963  1.00 21.37 ? 1075 ILE A CD1 1 
ATOM   1537 N N   . SER A 1 210 ? -7.596  -8.222  14.188  1.00 19.56 ? 1076 SER A N   1 
ATOM   1538 C CA  . SER A 1 210 ? -8.639  -8.473  13.156  1.00 19.18 ? 1076 SER A CA  1 
ATOM   1539 C C   . SER A 1 210 ? -8.213  -9.632  12.239  1.00 19.26 ? 1076 SER A C   1 
ATOM   1540 O O   . SER A 1 210 ? -7.007  -9.758  11.894  1.00 17.75 ? 1076 SER A O   1 
ATOM   1541 C CB  . SER A 1 210 ? -8.953  -7.204  12.397  1.00 19.51 ? 1076 SER A CB  1 
ATOM   1542 O OG  . SER A 1 210 ? -9.487  -6.231  13.321  1.00 20.96 ? 1076 SER A OG  1 
ATOM   1543 N N   . ASN A 1 211 ? -9.173  -10.420 11.760  1.00 19.68 ? 1077 ASN A N   1 
ATOM   1544 C CA  . ASN A 1 211 ? -8.856  -11.391 10.668  1.00 20.07 ? 1077 ASN A CA  1 
ATOM   1545 C C   . ASN A 1 211 ? -7.617  -12.210 11.077  1.00 20.71 ? 1077 ASN A C   1 
ATOM   1546 O O   . ASN A 1 211 ? -6.624  -12.300 10.308  1.00 20.11 ? 1077 ASN A O   1 
ATOM   1547 C CB  . ASN A 1 211 ? -8.673  -10.676 9.332   1.00 20.69 ? 1077 ASN A CB  1 
ATOM   1548 C CG  . ASN A 1 211 ? -8.704  -11.594 8.113   1.00 21.43 ? 1077 ASN A CG  1 
ATOM   1549 O OD1 . ASN A 1 211 ? -8.415  -11.179 6.968   1.00 23.62 ? 1077 ASN A OD1 1 
ATOM   1550 N ND2 . ASN A 1 211 ? -9.056  -12.833 8.323   1.00 20.28 ? 1077 ASN A ND2 1 
ATOM   1551 N N   . VAL A 1 212 ? -7.655  -12.793 12.279  1.00 20.48 ? 1078 VAL A N   1 
ATOM   1552 C CA  . VAL A 1 212 ? -6.477  -13.428 12.914  1.00 20.28 ? 1078 VAL A CA  1 
ATOM   1553 C C   . VAL A 1 212 ? -6.024  -14.606 12.052  1.00 21.24 ? 1078 VAL A C   1 
ATOM   1554 O O   . VAL A 1 212 ? -6.900  -15.307 11.514  1.00 20.82 ? 1078 VAL A O   1 
ATOM   1555 C CB  . VAL A 1 212 ? -6.786  -13.856 14.355  1.00 20.66 ? 1078 VAL A CB  1 
ATOM   1556 C CG1 . VAL A 1 212 ? -7.757  -15.018 14.440  1.00 21.27 ? 1078 VAL A CG1 1 
ATOM   1557 C CG2 . VAL A 1 212 ? -5.492  -14.183 15.113  1.00 20.76 ? 1078 VAL A CG2 1 
ATOM   1558 N N   . GLN A 1 213 ? -4.702  -14.750 11.900  1.00 20.53 ? 1079 GLN A N   1 
ATOM   1559 C CA  . GLN A 1 213 ? -4.075  -15.842 11.144  1.00 21.17 ? 1079 GLN A CA  1 
ATOM   1560 C C   . GLN A 1 213 ? -3.342  -16.827 12.061  1.00 22.04 ? 1079 GLN A C   1 
ATOM   1561 O O   . GLN A 1 213 ? -2.973  -16.469 13.159  1.00 20.30 ? 1079 GLN A O   1 
ATOM   1562 C CB  . GLN A 1 213 ? -3.137  -15.221 10.115  1.00 21.32 ? 1079 GLN A CB  1 
ATOM   1563 C CG  . GLN A 1 213 ? -3.850  -14.288 9.126   1.00 21.49 ? 1079 GLN A CG  1 
ATOM   1564 C CD  . GLN A 1 213 ? -4.953  -14.992 8.367   1.00 22.38 ? 1079 GLN A CD  1 
ATOM   1565 O OE1 . GLN A 1 213 ? -4.751  -15.988 7.685   1.00 23.41 ? 1079 GLN A OE1 1 
ATOM   1566 N NE2 . GLN A 1 213 ? -6.154  -14.467 8.492   1.00 22.43 ? 1079 GLN A NE2 1 
ATOM   1567 N N   . SER A 1 214 ? -2.996  -18.005 11.523  1.00 23.91 ? 1080 SER A N   1 
ATOM   1568 C CA  . SER A 1 214 ? -2.273  -19.049 12.293  1.00 24.50 ? 1080 SER A CA  1 
ATOM   1569 C C   . SER A 1 214 ? -0.893  -18.501 12.730  1.00 24.39 ? 1080 SER A C   1 
ATOM   1570 O O   . SER A 1 214 ? -0.430  -18.851 13.846  1.00 23.26 ? 1080 SER A O   1 
ATOM   1571 C CB  . SER A 1 214 ? -2.220  -20.356 11.513  1.00 26.35 ? 1080 SER A CB  1 
ATOM   1572 O OG  . SER A 1 214 ? -1.429  -20.191 10.354  1.00 29.58 ? 1080 SER A OG  1 
ATOM   1573 N N   . GLU A 1 215 ? -0.255  -17.611 11.977  1.00 24.02 ? 1081 GLU A N   1 
ATOM   1574 C CA  . GLU A 1 215 ? 1.094   -17.114 12.376  1.00 24.20 ? 1081 GLU A CA  1 
ATOM   1575 C C   . GLU A 1 215 ? 0.952   -16.198 13.606  1.00 22.70 ? 1081 GLU A C   1 
ATOM   1576 O O   . GLU A 1 215 ? 1.987   -15.819 14.178  1.00 23.54 ? 1081 GLU A O   1 
ATOM   1577 C CB  . GLU A 1 215 ? 1.812   -16.378 11.243  1.00 26.05 ? 1081 GLU A CB  1 
ATOM   1578 C CG  . GLU A 1 215 ? 1.110   -15.113 10.817  1.00 27.06 ? 1081 GLU A CG  1 
ATOM   1579 C CD  . GLU A 1 215 ? 1.892   -14.234 9.860   1.00 30.57 ? 1081 GLU A CD  1 
ATOM   1580 O OE1 . GLU A 1 215 ? 1.250   -13.617 8.977   1.00 34.39 ? 1081 GLU A OE1 1 
ATOM   1581 O OE2 . GLU A 1 215 ? 3.131   -14.107 10.030  1.00 32.50 ? 1081 GLU A OE2 1 
ATOM   1582 N N   . ASP A 1 216 ? -0.277  -15.798 13.954  1.00 21.58 ? 1082 ASP A N   1 
ATOM   1583 C CA  . ASP A 1 216 ? -0.556  -14.863 15.091  1.00 20.95 ? 1082 ASP A CA  1 
ATOM   1584 C C   . ASP A 1 216 ? -0.736  -15.643 16.412  1.00 21.39 ? 1082 ASP A C   1 
ATOM   1585 O O   . ASP A 1 216 ? -0.881  -15.013 17.463  1.00 20.72 ? 1082 ASP A O   1 
ATOM   1586 C CB  . ASP A 1 216 ? -1.795  -14.014 14.820  1.00 20.53 ? 1082 ASP A CB  1 
ATOM   1587 C CG  . ASP A 1 216 ? -1.723  -13.134 13.590  1.00 20.63 ? 1082 ASP A CG  1 
ATOM   1588 O OD1 . ASP A 1 216 ? -0.580  -12.844 13.115  1.00 20.17 ? 1082 ASP A OD1 1 
ATOM   1589 O OD2 . ASP A 1 216 ? -2.817  -12.829 13.028  1.00 20.85 ? 1082 ASP A OD2 1 
ATOM   1590 N N   . LEU A 1 217 ? -0.789  -16.978 16.369  1.00 21.30 ? 1083 LEU A N   1 
ATOM   1591 C CA  . LEU A 1 217 ? -0.871  -17.801 17.602  1.00 23.03 ? 1083 LEU A CA  1 
ATOM   1592 C C   . LEU A 1 217 ? 0.477   -17.688 18.315  1.00 23.18 ? 1083 LEU A C   1 
ATOM   1593 O O   . LEU A 1 217 ? 1.527   -17.914 17.675  1.00 24.10 ? 1083 LEU A O   1 
ATOM   1594 C CB  . LEU A 1 217 ? -1.208  -19.248 17.231  1.00 25.26 ? 1083 LEU A CB  1 
ATOM   1595 C CG  . LEU A 1 217 ? -2.498  -19.415 16.444  1.00 27.09 ? 1083 LEU A CG  1 
ATOM   1596 C CD1 . LEU A 1 217 ? -2.679  -20.854 16.014  1.00 29.61 ? 1083 LEU A CD1 1 
ATOM   1597 C CD2 . LEU A 1 217 ? -3.670  -18.900 17.235  1.00 27.88 ? 1083 LEU A CD2 1 
ATOM   1598 N N   . ALA A 1 218 ? 0.456   -17.201 19.546  1.00 22.64 ? 1084 ALA A N   1 
ATOM   1599 C CA  . ALA A 1 218 ? 1.652   -16.743 20.277  1.00 22.47 ? 1084 ALA A CA  1 
ATOM   1600 C C   . ALA A 1 218 ? 1.204   -16.256 21.644  1.00 21.02 ? 1084 ALA A C   1 
ATOM   1601 O O   . ALA A 1 218 ? -0.028  -16.221 21.889  1.00 19.92 ? 1084 ALA A O   1 
ATOM   1602 C CB  . ALA A 1 218 ? 2.297   -15.604 19.520  1.00 23.43 ? 1084 ALA A CB  1 
ATOM   1603 N N   . ASP A 1 219 ? 2.142   -15.879 22.498  1.00 21.04 ? 1085 ASP A N   1 
ATOM   1604 C CA  . ASP A 1 219 ? 1.839   -15.161 23.756  1.00 22.43 ? 1085 ASP A CA  1 
ATOM   1605 C C   . ASP A 1 219 ? 1.822   -13.666 23.476  1.00 21.16 ? 1085 ASP A C   1 
ATOM   1606 O O   . ASP A 1 219 ? 2.615   -13.203 22.614  1.00 20.68 ? 1085 ASP A O   1 
ATOM   1607 C CB  . ASP A 1 219 ? 2.898   -15.332 24.834  1.00 24.72 ? 1085 ASP A CB  1 
ATOM   1608 C CG  . ASP A 1 219 ? 3.022   -16.710 25.427  1.00 29.19 ? 1085 ASP A CG  1 
ATOM   1609 O OD1 . ASP A 1 219 ? 2.181   -17.608 25.140  1.00 30.36 ? 1085 ASP A OD1 1 
ATOM   1610 O OD2 . ASP A 1 219 ? 3.975   -16.859 26.174  1.00 30.67 ? 1085 ASP A OD2 1 
ATOM   1611 N N   . TYR A 1 220 ? 0.917   -12.952 24.141  1.00 19.01 ? 1086 TYR A N   1 
ATOM   1612 C CA  . TYR A 1 220 ? 0.826   -11.471 24.041  1.00 17.94 ? 1086 TYR A CA  1 
ATOM   1613 C C   . TYR A 1 220 ? 0.933   -10.908 25.452  1.00 18.08 ? 1086 TYR A C   1 
ATOM   1614 O O   . TYR A 1 220 ? 0.248   -11.423 26.387  1.00 18.25 ? 1086 TYR A O   1 
ATOM   1615 C CB  . TYR A 1 220 ? -0.486  -11.079 23.346  1.00 18.55 ? 1086 TYR A CB  1 
ATOM   1616 C CG  . TYR A 1 220 ? -0.516  -11.491 21.905  1.00 18.19 ? 1086 TYR A CG  1 
ATOM   1617 C CD1 . TYR A 1 220 ? -0.944  -12.758 21.530  1.00 18.68 ? 1086 TYR A CD1 1 
ATOM   1618 C CD2 . TYR A 1 220 ? -0.000  -10.669 20.917  1.00 17.50 ? 1086 TYR A CD2 1 
ATOM   1619 C CE1 . TYR A 1 220 ? -0.901  -13.160 20.195  1.00 18.87 ? 1086 TYR A CE1 1 
ATOM   1620 C CE2 . TYR A 1 220 ? 0.045   -11.061 19.592  1.00 18.35 ? 1086 TYR A CE2 1 
ATOM   1621 C CZ  . TYR A 1 220 ? -0.431  -12.295 19.217  1.00 19.00 ? 1086 TYR A CZ  1 
ATOM   1622 O OH  . TYR A 1 220 ? -0.337  -12.631 17.890  1.00 20.07 ? 1086 TYR A OH  1 
ATOM   1623 N N   . PHE A 1 221 ? 1.679   -9.823  25.624  1.00 17.66 ? 1087 PHE A N   1 
ATOM   1624 C CA  . PHE A 1 221 ? 1.944   -9.155  26.912  1.00 17.74 ? 1087 PHE A CA  1 
ATOM   1625 C C   . PHE A 1 221 ? 1.749   -7.645  26.742  1.00 16.59 ? 1087 PHE A C   1 
ATOM   1626 O O   . PHE A 1 221 ? 2.289   -7.094  25.772  1.00 15.33 ? 1087 PHE A O   1 
ATOM   1627 C CB  . PHE A 1 221 ? 3.404   -9.363  27.345  1.00 21.18 ? 1087 PHE A CB  1 
ATOM   1628 C CG  . PHE A 1 221 ? 3.738   -10.735 27.814  1.00 25.58 ? 1087 PHE A CG  1 
ATOM   1629 C CD1 . PHE A 1 221 ? 4.364   -11.617 26.959  1.00 28.11 ? 1087 PHE A CD1 1 
ATOM   1630 C CD2 . PHE A 1 221 ? 3.521   -11.127 29.132  1.00 27.83 ? 1087 PHE A CD2 1 
ATOM   1631 C CE1 . PHE A 1 221 ? 4.668   -12.901 27.397  1.00 29.12 ? 1087 PHE A CE1 1 
ATOM   1632 C CE2 . PHE A 1 221 ? 3.812   -12.423 29.532  1.00 26.74 ? 1087 PHE A CE2 1 
ATOM   1633 C CZ  . PHE A 1 221 ? 4.347   -13.308 28.657  1.00 25.08 ? 1087 PHE A CZ  1 
ATOM   1634 N N   . CYS A 1 222 ? 1.084   -6.978  27.672  1.00 16.26 ? 1088 CYS A N   1 
ATOM   1635 C CA  . CYS A 1 222 ? 1.038   -5.508  27.760  1.00 17.26 ? 1088 CYS A CA  1 
ATOM   1636 C C   . CYS A 1 222 ? 2.175   -5.073  28.704  1.00 16.83 ? 1088 CYS A C   1 
ATOM   1637 O O   . CYS A 1 222 ? 2.709   -5.887  29.517  1.00 17.84 ? 1088 CYS A O   1 
ATOM   1638 C CB  . CYS A 1 222 ? -0.300  -4.953  28.270  1.00 21.22 ? 1088 CYS A CB  1 
ATOM   1639 S SG  . CYS A 1 222 ? -0.643  -5.661  29.885  1.00 29.16 ? 1088 CYS A SG  1 
ATOM   1640 N N   . GLN A 1 223 ? 2.600   -3.829  28.565  1.00 15.12 ? 1089 GLN A N   1 
ATOM   1641 C CA  . GLN A 1 223 ? 3.622   -3.232  29.447  1.00 14.99 ? 1089 GLN A CA  1 
ATOM   1642 C C   . GLN A 1 223 ? 3.219   -1.766  29.638  1.00 14.89 ? 1089 GLN A C   1 
ATOM   1643 O O   . GLN A 1 223 ? 2.931   -1.095  28.646  1.00 15.49 ? 1089 GLN A O   1 
ATOM   1644 C CB  . GLN A 1 223 ? 5.017   -3.324  28.817  1.00 15.43 ? 1089 GLN A CB  1 
ATOM   1645 C CG  . GLN A 1 223 ? 6.079   -2.763  29.760  1.00 15.70 ? 1089 GLN A CG  1 
ATOM   1646 C CD  . GLN A 1 223 ? 7.429   -2.552  29.144  1.00 17.76 ? 1089 GLN A CD  1 
ATOM   1647 O OE1 . GLN A 1 223 ? 7.704   -2.682  27.973  1.00 17.92 ? 1089 GLN A OE1 1 
ATOM   1648 N NE2 . GLN A 1 223 ? 8.370   -2.341  30.028  1.00 20.88 ? 1089 GLN A NE2 1 
ATOM   1649 N N   . GLN A 1 224 ? 3.296   -1.255  30.838  1.00 14.85 ? 1090 GLN A N   1 
ATOM   1650 C CA  . GLN A 1 224 ? 3.179   0.182   31.115  1.00 14.55 ? 1090 GLN A CA  1 
ATOM   1651 C C   . GLN A 1 224 ? 4.590   0.746   31.264  1.00 14.69 ? 1090 GLN A C   1 
ATOM   1652 O O   . GLN A 1 224 ? 5.448   0.087   31.842  1.00 15.22 ? 1090 GLN A O   1 
ATOM   1653 C CB  . GLN A 1 224 ? 2.288   0.468   32.327  1.00 14.45 ? 1090 GLN A CB  1 
ATOM   1654 C CG  . GLN A 1 224 ? 2.907   0.086   33.672  1.00 15.24 ? 1090 GLN A CG  1 
ATOM   1655 C CD  . GLN A 1 224 ? 3.875   1.090   34.248  1.00 14.79 ? 1090 GLN A CD  1 
ATOM   1656 O OE1 . GLN A 1 224 ? 3.932   2.270   33.879  1.00 14.99 ? 1090 GLN A OE1 1 
ATOM   1657 N NE2 . GLN A 1 224 ? 4.689   0.612   35.170  1.00 15.06 ? 1090 GLN A NE2 1 
ATOM   1658 N N   . TYR A 1 225 ? 4.805   1.913   30.685  1.00 14.34 ? 1091 TYR A N   1 
ATOM   1659 C CA  . TYR A 1 225 ? 6.032   2.701   30.869  1.00 13.98 ? 1091 TYR A CA  1 
ATOM   1660 C C   . TYR A 1 225 ? 5.708   4.127   31.312  1.00 14.09 ? 1091 TYR A C   1 
ATOM   1661 O O   . TYR A 1 225 ? 6.438   5.086   30.991  1.00 14.83 ? 1091 TYR A O   1 
ATOM   1662 C CB  . TYR A 1 225 ? 6.910   2.544   29.652  1.00 14.04 ? 1091 TYR A CB  1 
ATOM   1663 C CG  . TYR A 1 225 ? 6.303   3.005   28.348  1.00 13.67 ? 1091 TYR A CG  1 
ATOM   1664 C CD1 . TYR A 1 225 ? 6.611   4.245   27.818  1.00 14.07 ? 1091 TYR A CD1 1 
ATOM   1665 C CD2 . TYR A 1 225 ? 5.464   2.155   27.602  1.00 14.16 ? 1091 TYR A CD2 1 
ATOM   1666 C CE1 . TYR A 1 225 ? 6.081   4.648   26.587  1.00 14.08 ? 1091 TYR A CE1 1 
ATOM   1667 C CE2 . TYR A 1 225 ? 4.917   2.558   26.414  1.00 14.07 ? 1091 TYR A CE2 1 
ATOM   1668 C CZ  . TYR A 1 225 ? 5.266   3.782   25.876  1.00 14.48 ? 1091 TYR A CZ  1 
ATOM   1669 O OH  . TYR A 1 225 ? 4.732   4.137   24.674  1.00 14.51 ? 1091 TYR A OH  1 
ATOM   1670 N N   . SER A 1 226 ? 4.580   4.284   32.022  1.00 15.11 ? 1092 SER A N   1 
ATOM   1671 C CA  . SER A 1 226 ? 4.177   5.520   32.717  1.00 15.97 ? 1092 SER A CA  1 
ATOM   1672 C C   . SER A 1 226 ? 5.136   5.803   33.855  1.00 17.04 ? 1092 SER A C   1 
ATOM   1673 O O   . SER A 1 226 ? 5.466   6.975   34.077  1.00 17.85 ? 1092 SER A O   1 
ATOM   1674 C CB  . SER A 1 226 ? 2.773   5.383   33.242  1.00 16.70 ? 1092 SER A CB  1 
ATOM   1675 O OG  . SER A 1 226 ? 2.381   6.539   33.894  1.00 17.99 ? 1092 SER A OG  1 
ATOM   1676 N N   . SER A 1 227 ? 5.494   4.799   34.639  1.00 16.49 ? 1093 SER A N   1 
ATOM   1677 C CA  . SER A 1 227 ? 6.277   5.037   35.877  1.00 17.83 ? 1093 SER A CA  1 
ATOM   1678 C C   . SER A 1 227 ? 7.162   3.827   36.123  1.00 16.79 ? 1093 SER A C   1 
ATOM   1679 O O   . SER A 1 227 ? 6.864   2.737   35.642  1.00 15.19 ? 1093 SER A O   1 
ATOM   1680 C CB  . SER A 1 227 ? 5.355   5.305   37.050  1.00 19.25 ? 1093 SER A CB  1 
ATOM   1681 O OG  . SER A 1 227 ? 4.545   4.171   37.258  1.00 21.77 ? 1093 SER A OG  1 
ATOM   1682 N N   . TYR A 1 228 ? 8.266   4.047   36.802  1.00 15.83 ? 1094 TYR A N   1 
ATOM   1683 C CA  . TYR A 1 228 ? 9.159   2.960   37.263  1.00 16.26 ? 1094 TYR A CA  1 
ATOM   1684 C C   . TYR A 1 228 ? 8.647   2.401   38.586  1.00 16.43 ? 1094 TYR A C   1 
ATOM   1685 O O   . TYR A 1 228 ? 8.183   3.137   39.438  1.00 16.84 ? 1094 TYR A O   1 
ATOM   1686 C CB  . TYR A 1 228 ? 10.603  3.457   37.360  1.00 16.06 ? 1094 TYR A CB  1 
ATOM   1687 C CG  . TYR A 1 228 ? 11.212  3.774   36.038  1.00 15.50 ? 1094 TYR A CG  1 
ATOM   1688 C CD1 . TYR A 1 228 ? 11.251  5.073   35.531  1.00 16.83 ? 1094 TYR A CD1 1 
ATOM   1689 C CD2 . TYR A 1 228 ? 11.665  2.748   35.243  1.00 15.32 ? 1094 TYR A CD2 1 
ATOM   1690 C CE1 . TYR A 1 228 ? 11.826  5.336   34.301  1.00 16.57 ? 1094 TYR A CE1 1 
ATOM   1691 C CE2 . TYR A 1 228 ? 12.244  3.007   34.026  1.00 15.79 ? 1094 TYR A CE2 1 
ATOM   1692 C CZ  . TYR A 1 228 ? 12.240  4.288   33.512  1.00 16.06 ? 1094 TYR A CZ  1 
ATOM   1693 O OH  . TYR A 1 228 ? 12.737  4.506   32.263  1.00 17.51 ? 1094 TYR A OH  1 
ATOM   1694 N N   . PRO A 1 229 ? 8.794   1.093   38.840  1.00 16.26 ? 1095 PRO A N   1 
ATOM   1695 C CA  . PRO A 1 229 ? 9.371   0.167   37.875  1.00 16.07 ? 1095 PRO A CA  1 
ATOM   1696 C C   . PRO A 1 229 ? 8.412   -0.142  36.735  1.00 15.21 ? 1095 PRO A C   1 
ATOM   1697 O O   . PRO A 1 229 ? 7.198   -0.146  36.928  1.00 14.54 ? 1095 PRO A O   1 
ATOM   1698 C CB  . PRO A 1 229 ? 9.626   -1.099  38.697  1.00 16.81 ? 1095 PRO A CB  1 
ATOM   1699 C CG  . PRO A 1 229 ? 8.574   -1.016  39.817  1.00 17.42 ? 1095 PRO A CG  1 
ATOM   1700 C CD  . PRO A 1 229 ? 8.377   0.453   40.099  1.00 16.90 ? 1095 PRO A CD  1 
ATOM   1701 N N   . LEU A 1 230 ? 8.963   -0.349  35.548  1.00 14.71 ? 1096 LEU A N   1 
ATOM   1702 C CA  . LEU A 1 230 ? 8.165   -0.721  34.356  1.00 15.11 ? 1096 LEU A CA  1 
ATOM   1703 C C   . LEU A 1 230 ? 7.590   -2.090  34.682  1.00 15.09 ? 1096 LEU A C   1 
ATOM   1704 O O   . LEU A 1 230 ? 8.294   -2.896  35.328  1.00 15.18 ? 1096 LEU A O   1 
ATOM   1705 C CB  . LEU A 1 230 ? 9.054   -0.794  33.113  1.00 15.11 ? 1096 LEU A CB  1 
ATOM   1706 C CG  . LEU A 1 230 ? 9.904   0.412   32.861  1.00 15.64 ? 1096 LEU A CG  1 
ATOM   1707 C CD1 . LEU A 1 230 ? 10.693  0.230   31.546  1.00 16.12 ? 1096 LEU A CD1 1 
ATOM   1708 C CD2 . LEU A 1 230 ? 9.089   1.712   32.897  1.00 15.47 ? 1096 LEU A CD2 1 
ATOM   1709 N N   . THR A 1 231 ? 6.320   -2.320  34.388  1.00 15.06 ? 1097 THR A N   1 
ATOM   1710 C CA  . THR A 1 231 ? 5.661   -3.600  34.738  1.00 15.31 ? 1097 THR A CA  1 
ATOM   1711 C C   . THR A 1 231 ? 4.866   -4.106  33.534  1.00 14.12 ? 1097 THR A C   1 
ATOM   1712 O O   . THR A 1 231 ? 4.382   -3.308  32.732  1.00 14.45 ? 1097 THR A O   1 
ATOM   1713 C CB  . THR A 1 231 ? 4.786   -3.485  35.984  1.00 15.75 ? 1097 THR A CB  1 
ATOM   1714 O OG1 . THR A 1 231 ? 3.901   -2.390  35.796  1.00 17.16 ? 1097 THR A OG1 1 
ATOM   1715 C CG2 . THR A 1 231 ? 5.610   -3.256  37.228  1.00 16.46 ? 1097 THR A CG2 1 
ATOM   1716 N N   . PHE A 1 232 ? 4.777   -5.410  33.455  1.00 14.54 ? 1098 PHE A N   1 
ATOM   1717 C CA  . PHE A 1 232 ? 4.179   -6.179  32.352  1.00 14.60 ? 1098 PHE A CA  1 
ATOM   1718 C C   . PHE A 1 232 ? 2.935   -6.897  32.876  1.00 15.58 ? 1098 PHE A C   1 
ATOM   1719 O O   . PHE A 1 232 ? 2.865   -7.313  34.044  1.00 16.17 ? 1098 PHE A O   1 
ATOM   1720 C CB  . PHE A 1 232 ? 5.126   -7.208  31.791  1.00 14.93 ? 1098 PHE A CB  1 
ATOM   1721 C CG  . PHE A 1 232 ? 6.390   -6.690  31.166  1.00 15.36 ? 1098 PHE A CG  1 
ATOM   1722 C CD1 . PHE A 1 232 ? 7.510   -6.432  31.935  1.00 14.65 ? 1098 PHE A CD1 1 
ATOM   1723 C CD2 . PHE A 1 232 ? 6.447   -6.443  29.793  1.00 15.92 ? 1098 PHE A CD2 1 
ATOM   1724 C CE1 . PHE A 1 232 ? 8.688   -6.013  31.317  1.00 15.25 ? 1098 PHE A CE1 1 
ATOM   1725 C CE2 . PHE A 1 232 ? 7.627   -6.037  29.194  1.00 15.51 ? 1098 PHE A CE2 1 
ATOM   1726 C CZ  . PHE A 1 232 ? 8.731   -5.777  29.958  1.00 15.83 ? 1098 PHE A CZ  1 
ATOM   1727 N N   . GLY A 1 233 ? 1.971   -7.111  31.998  1.00 16.12 ? 1099 GLY A N   1 
ATOM   1728 C CA  . GLY A 1 233 ? 0.855   -8.023  32.267  1.00 17.49 ? 1099 GLY A CA  1 
ATOM   1729 C C   . GLY A 1 233 ? 1.343   -9.451  32.339  1.00 18.20 ? 1099 GLY A C   1 
ATOM   1730 O O   . GLY A 1 233 ? 2.499   -9.700  31.962  1.00 18.25 ? 1099 GLY A O   1 
ATOM   1731 N N   . GLY A 1 234 ? 0.500   -10.349 32.832  1.00 18.68 ? 1100 GLY A N   1 
ATOM   1732 C CA  . GLY A 1 234 ? 0.866   -11.755 33.052  1.00 20.69 ? 1100 GLY A CA  1 
ATOM   1733 C C   . GLY A 1 234 ? 0.928   -12.550 31.749  1.00 21.58 ? 1100 GLY A C   1 
ATOM   1734 O O   . GLY A 1 234 ? 1.415   -13.683 31.770  1.00 21.19 ? 1100 GLY A O   1 
ATOM   1735 N N   . GLY A 1 235 ? 0.456   -11.988 30.628  1.00 20.91 ? 1101 GLY A N   1 
ATOM   1736 C CA  . GLY A 1 235 ? 0.500   -12.701 29.337  1.00 20.42 ? 1101 GLY A CA  1 
ATOM   1737 C C   . GLY A 1 235 ? -0.803  -13.426 29.037  1.00 20.33 ? 1101 GLY A C   1 
ATOM   1738 O O   . GLY A 1 235 ? -1.528  -13.807 29.940  1.00 19.24 ? 1101 GLY A O   1 
ATOM   1739 N N   . THR A 1 236 ? -1.109  -13.503 27.750  1.00 19.73 ? 1102 THR A N   1 
ATOM   1740 C CA  . THR A 1 236 ? -2.221  -14.291 27.185  1.00 20.82 ? 1102 THR A CA  1 
ATOM   1741 C C   . THR A 1 236 ? -1.626  -15.143 26.074  1.00 19.86 ? 1102 THR A C   1 
ATOM   1742 O O   . THR A 1 236 ? -1.024  -14.591 25.168  1.00 20.84 ? 1102 THR A O   1 
ATOM   1743 C CB  . THR A 1 236 ? -3.371  -13.407 26.691  1.00 20.72 ? 1102 THR A CB  1 
ATOM   1744 O OG1 . THR A 1 236 ? -3.873  -12.690 27.829  1.00 20.27 ? 1102 THR A OG1 1 
ATOM   1745 C CG2 . THR A 1 236 ? -4.472  -14.214 26.016  1.00 21.49 ? 1102 THR A CG2 1 
ATOM   1746 N N   . LYS A 1 237 ? -1.791  -16.458 26.176  1.00 20.33 ? 1103 LYS A N   1 
ATOM   1747 C CA  . LYS A 1 237 ? -1.412  -17.407 25.103  1.00 21.41 ? 1103 LYS A CA  1 
ATOM   1748 C C   . LYS A 1 237 ? -2.619  -17.597 24.201  1.00 21.76 ? 1103 LYS A C   1 
ATOM   1749 O O   . LYS A 1 237 ? -3.660  -18.095 24.671  1.00 20.09 ? 1103 LYS A O   1 
ATOM   1750 C CB  . LYS A 1 237 ? -0.963  -18.744 25.671  1.00 24.03 ? 1103 LYS A CB  1 
ATOM   1751 C CG  . LYS A 1 237 ? -0.403  -19.682 24.627  1.00 26.77 ? 1103 LYS A CG  1 
ATOM   1752 C CD  . LYS A 1 237 ? 0.008   -21.005 25.222  1.00 31.05 ? 1103 LYS A CD  1 
ATOM   1753 C CE  . LYS A 1 237 ? 0.210   -22.070 24.179  1.00 35.56 ? 1103 LYS A CE  1 
ATOM   1754 N NZ  . LYS A 1 237 ? 1.492   -21.798 23.498  1.00 38.81 ? 1103 LYS A NZ  1 
ATOM   1755 N N   . LEU A 1 238 ? -2.504  -17.150 22.966  1.00 21.49 ? 1104 LEU A N   1 
ATOM   1756 C CA  . LEU A 1 238 ? -3.598  -17.263 21.978  1.00 20.92 ? 1104 LEU A CA  1 
ATOM   1757 C C   . LEU A 1 238 ? -3.384  -18.563 21.207  1.00 22.29 ? 1104 LEU A C   1 
ATOM   1758 O O   . LEU A 1 238 ? -2.282  -18.745 20.620  1.00 21.68 ? 1104 LEU A O   1 
ATOM   1759 C CB  . LEU A 1 238 ? -3.547  -16.045 21.066  1.00 20.78 ? 1104 LEU A CB  1 
ATOM   1760 C CG  . LEU A 1 238 ? -4.583  -16.019 19.970  1.00 21.06 ? 1104 LEU A CG  1 
ATOM   1761 C CD1 . LEU A 1 238 ? -5.973  -15.902 20.608  1.00 21.66 ? 1104 LEU A CD1 1 
ATOM   1762 C CD2 . LEU A 1 238 ? -4.303  -14.876 19.013  1.00 21.53 ? 1104 LEU A CD2 1 
ATOM   1763 N N   . GLU A 1 239 ? -4.396  -19.420 21.192  1.00 23.93 ? 1105 GLU A N   1 
ATOM   1764 C CA  . GLU A 1 239 ? -4.298  -20.769 20.573  1.00 26.44 ? 1105 GLU A CA  1 
ATOM   1765 C C   . GLU A 1 239 ? -5.477  -20.993 19.627  1.00 26.55 ? 1105 GLU A C   1 
ATOM   1766 O O   . GLU A 1 239 ? -6.479  -20.276 19.757  1.00 24.03 ? 1105 GLU A O   1 
ATOM   1767 C CB  . GLU A 1 239 ? -4.353  -21.862 21.651  1.00 29.51 ? 1105 GLU A CB  1 
ATOM   1768 C CG  . GLU A 1 239 ? -3.333  -21.677 22.752  1.00 32.31 ? 1105 GLU A CG  1 
ATOM   1769 C CD  . GLU A 1 239 ? -3.501  -22.676 23.901  1.00 34.85 ? 1105 GLU A CD  1 
ATOM   1770 O OE1 . GLU A 1 239 ? -2.586  -23.469 24.081  1.00 38.17 ? 1105 GLU A OE1 1 
ATOM   1771 O OE2 . GLU A 1 239 ? -4.550  -22.669 24.587  1.00 39.36 ? 1105 GLU A OE2 1 
ATOM   1772 N N   . MET A 1 240 ? -5.376  -22.026 18.793  1.00 29.32 ? 1106 MET A N   1 
ATOM   1773 C CA  . MET A 1 240 ? -6.474  -22.454 17.881  1.00 34.85 ? 1106 MET A CA  1 
ATOM   1774 C C   . MET A 1 240 ? -7.568  -23.146 18.689  1.00 32.57 ? 1106 MET A C   1 
ATOM   1775 O O   . MET A 1 240 ? -7.220  -24.043 19.409  1.00 29.20 ? 1106 MET A O   1 
ATOM   1776 C CB  . MET A 1 240 ? -5.970  -23.478 16.864  1.00 40.15 ? 1106 MET A CB  1 
ATOM   1777 C CG  . MET A 1 240 ? -5.354  -22.858 15.671  1.00 47.74 ? 1106 MET A CG  1 
ATOM   1778 S SD  . MET A 1 240 ? -6.663  -22.198 14.594  1.00 57.47 ? 1106 MET A SD  1 
ATOM   1779 C CE  . MET A 1 240 ? -6.519  -20.447 14.962  1.00 51.35 ? 1106 MET A CE  1 
ATOM   1780 N N   . LYS A 1 241 ? -8.828  -22.755 18.513  1.00 35.38 ? 1107 LYS A N   1 
ATOM   1781 C CA  . LYS A 1 241 ? -9.998  -23.589 18.910  1.00 39.15 ? 1107 LYS A CA  1 
ATOM   1782 C C   . LYS A 1 241 ? -9.868  -24.980 18.281  1.00 41.41 ? 1107 LYS A C   1 
ATOM   1783 O O   . LYS A 1 241 ? -9.729  -25.035 17.056  1.00 41.37 ? 1107 LYS A O   1 
ATOM   1784 C CB  . LYS A 1 241 ? -11.317 -22.960 18.464  1.00 42.76 ? 1107 LYS A CB  1 
ATOM   1785 C CG  . LYS A 1 241 ? -11.870 -21.976 19.472  1.00 48.31 ? 1107 LYS A CG  1 
ATOM   1786 C CD  . LYS A 1 241 ? -13.234 -21.410 19.156  1.00 52.68 ? 1107 LYS A CD  1 
ATOM   1787 C CE  . LYS A 1 241 ? -13.499 -20.191 20.021  1.00 55.64 ? 1107 LYS A CE  1 
ATOM   1788 N NZ  . LYS A 1 241 ? -14.334 -19.194 19.303  1.00 58.69 ? 1107 LYS A NZ  1 
ATOM   1789 N N   . GLN B 1 1   ? 25.487  18.809  21.806  1.00 45.72 ? 1    GLN H N   1 
ATOM   1790 C CA  . GLN B 1 1   ? 25.093  20.170  21.352  1.00 45.73 ? 1    GLN H CA  1 
ATOM   1791 C C   . GLN B 1 1   ? 24.641  20.168  19.878  1.00 42.60 ? 1    GLN H C   1 
ATOM   1792 O O   . GLN B 1 1   ? 25.416  20.358  18.920  1.00 43.47 ? 1    GLN H O   1 
ATOM   1793 C CB  . GLN B 1 1   ? 26.160  21.227  21.613  1.00 49.30 ? 1    GLN H CB  1 
ATOM   1794 C CG  . GLN B 1 1   ? 25.540  22.601  21.809  1.00 52.46 ? 1    GLN H CG  1 
ATOM   1795 C CD  . GLN B 1 1   ? 24.133  22.553  22.371  1.00 54.98 ? 1    GLN H CD  1 
ATOM   1796 O OE1 . GLN B 1 1   ? 23.714  21.582  23.001  1.00 57.86 ? 1    GLN H OE1 1 
ATOM   1797 N NE2 . GLN B 1 1   ? 23.367  23.610  22.140  1.00 58.11 ? 1    GLN H NE2 1 
ATOM   1798 N N   . VAL B 1 2   ? 23.353  19.998  19.715  1.00 37.05 ? 2    VAL H N   1 
ATOM   1799 C CA  . VAL B 1 2   ? 22.703  19.934  18.386  1.00 36.52 ? 2    VAL H CA  1 
ATOM   1800 C C   . VAL B 1 2   ? 22.549  21.376  17.922  1.00 35.39 ? 2    VAL H C   1 
ATOM   1801 O O   . VAL B 1 2   ? 22.167  22.220  18.731  1.00 34.38 ? 2    VAL H O   1 
ATOM   1802 C CB  . VAL B 1 2   ? 21.351  19.216  18.483  1.00 34.39 ? 2    VAL H CB  1 
ATOM   1803 C CG1 . VAL B 1 2   ? 20.500  19.447  17.241  1.00 34.03 ? 2    VAL H CG1 1 
ATOM   1804 C CG2 . VAL B 1 2   ? 21.561  17.748  18.787  1.00 34.96 ? 2    VAL H CG2 1 
ATOM   1805 N N   . GLN B 1 3   ? 22.782  21.630  16.648  1.00 35.20 ? 3    GLN H N   1 
ATOM   1806 C CA  . GLN B 1 3   ? 22.505  22.952  16.060  1.00 36.18 ? 3    GLN H CA  1 
ATOM   1807 C C   . GLN B 1 3   ? 21.866  22.807  14.687  1.00 32.79 ? 3    GLN H C   1 
ATOM   1808 O O   . GLN B 1 3   ? 22.273  21.920  13.939  1.00 33.17 ? 3    GLN H O   1 
ATOM   1809 C CB  . GLN B 1 3   ? 23.820  23.709  15.927  1.00 40.43 ? 3    GLN H CB  1 
ATOM   1810 C CG  . GLN B 1 3   ? 23.585  25.202  15.874  1.00 46.26 ? 3    GLN H CG  1 
ATOM   1811 C CD  . GLN B 1 3   ? 24.408  25.913  16.919  1.00 48.06 ? 3    GLN H CD  1 
ATOM   1812 O OE1 . GLN B 1 3   ? 24.482  25.502  18.078  1.00 53.13 ? 3    GLN H OE1 1 
ATOM   1813 N NE2 . GLN B 1 3   ? 25.051  26.979  16.488  1.00 51.99 ? 3    GLN H NE2 1 
ATOM   1814 N N   . LEU B 1 4   ? 20.908  23.673  14.389  1.00 31.76 ? 4    LEU H N   1 
ATOM   1815 C CA  . LEU B 1 4   ? 20.369  23.884  13.022  1.00 30.80 ? 4    LEU H CA  1 
ATOM   1816 C C   . LEU B 1 4   ? 20.576  25.364  12.682  1.00 31.09 ? 4    LEU H C   1 
ATOM   1817 O O   . LEU B 1 4   ? 19.862  26.215  13.223  1.00 29.46 ? 4    LEU H O   1 
ATOM   1818 C CB  . LEU B 1 4   ? 18.887  23.469  12.946  1.00 30.73 ? 4    LEU H CB  1 
ATOM   1819 C CG  . LEU B 1 4   ? 18.563  21.981  13.173  1.00 30.85 ? 4    LEU H CG  1 
ATOM   1820 C CD1 . LEU B 1 4   ? 17.065  21.716  13.032  1.00 30.87 ? 4    LEU H CD1 1 
ATOM   1821 C CD2 . LEU B 1 4   ? 19.329  21.075  12.197  1.00 30.48 ? 4    LEU H CD2 1 
ATOM   1822 N N   . GLN B 1 5   ? 21.542  25.646  11.819  1.00 31.93 ? 5    GLN H N   1 
ATOM   1823 C CA  . GLN B 1 5   ? 21.974  27.026  11.479  1.00 33.73 ? 5    GLN H CA  1 
ATOM   1824 C C   . GLN B 1 5   ? 21.385  27.382  10.119  1.00 31.39 ? 5    GLN H C   1 
ATOM   1825 O O   . GLN B 1 5   ? 21.784  26.766  9.114   1.00 31.74 ? 5    GLN H O   1 
ATOM   1826 C CB  . GLN B 1 5   ? 23.501  27.117  11.446  1.00 36.63 ? 5    GLN H CB  1 
ATOM   1827 C CG  . GLN B 1 5   ? 24.038  28.475  11.018  1.00 40.29 ? 5    GLN H CG  1 
ATOM   1828 C CD  . GLN B 1 5   ? 23.652  29.593  11.963  1.00 45.26 ? 5    GLN H CD  1 
ATOM   1829 O OE1 . GLN B 1 5   ? 23.335  29.355  13.130  1.00 45.72 ? 5    GLN H OE1 1 
ATOM   1830 N NE2 . GLN B 1 5   ? 23.662  30.826  11.463  1.00 46.77 ? 5    GLN H NE2 1 
ATOM   1831 N N   . GLN B 1 6   ? 20.436  28.309  10.101  1.00 29.12 ? 6    GLN H N   1 
ATOM   1832 C CA  . GLN B 1 6   ? 19.813  28.731  8.831   1.00 28.82 ? 6    GLN H CA  1 
ATOM   1833 C C   . GLN B 1 6   ? 20.581  29.916  8.256   1.00 29.86 ? 6    GLN H C   1 
ATOM   1834 O O   . GLN B 1 6   ? 21.297  30.647  9.019   1.00 30.57 ? 6    GLN H O   1 
ATOM   1835 C CB  . GLN B 1 6   ? 18.335  29.043  8.988   1.00 27.61 ? 6    GLN H CB  1 
ATOM   1836 C CG  . GLN B 1 6   ? 17.577  27.868  9.580   1.00 27.84 ? 6    GLN H CG  1 
ATOM   1837 C CD  . GLN B 1 6   ? 16.095  28.132  9.641   1.00 27.35 ? 6    GLN H CD  1 
ATOM   1838 O OE1 . GLN B 1 6   ? 15.442  27.790  10.616  1.00 26.23 ? 6    GLN H OE1 1 
ATOM   1839 N NE2 . GLN B 1 6   ? 15.553  28.764  8.608   1.00 26.88 ? 6    GLN H NE2 1 
ATOM   1840 N N   . SER B 1 7   ? 20.379  30.106  6.961   1.00 31.06 ? 7    SER H N   1 
ATOM   1841 C CA  . SER B 1 7   ? 20.952  31.252  6.215   1.00 31.97 ? 7    SER H CA  1 
ATOM   1842 C C   . SER B 1 7   ? 20.202  32.551  6.565   1.00 33.36 ? 7    SER H C   1 
ATOM   1843 O O   . SER B 1 7   ? 19.102  32.506  7.206   1.00 32.29 ? 7    SER H O   1 
ATOM   1844 C CB  . SER B 1 7   ? 20.969  30.924  4.772   1.00 30.33 ? 7    SER H CB  1 
ATOM   1845 O OG  . SER B 1 7   ? 19.704  30.423  4.347   1.00 28.22 ? 7    SER H OG  1 
ATOM   1846 N N   . ASP B 1 8   ? 20.758  33.667  6.085   1.00 35.58 ? 8    ASP H N   1 
ATOM   1847 C CA  . ASP B 1 8   ? 20.413  35.059  6.459   1.00 37.72 ? 8    ASP H CA  1 
ATOM   1848 C C   . ASP B 1 8   ? 19.067  35.440  5.848   1.00 37.10 ? 8    ASP H C   1 
ATOM   1849 O O   . ASP B 1 8   ? 18.661  34.805  4.837   1.00 36.07 ? 8    ASP H O   1 
ATOM   1850 C CB  . ASP B 1 8   ? 21.518  36.014  5.977   1.00 41.14 ? 8    ASP H CB  1 
ATOM   1851 C CG  . ASP B 1 8   ? 22.827  35.918  6.737   1.00 45.45 ? 8    ASP H CG  1 
ATOM   1852 O OD1 . ASP B 1 8   ? 22.830  35.310  7.825   1.00 46.28 ? 8    ASP H OD1 1 
ATOM   1853 O OD2 . ASP B 1 8   ? 23.843  36.468  6.233   1.00 49.34 ? 8    ASP H OD2 1 
ATOM   1854 N N   . ALA B 1 9   ? 18.428  36.477  6.404   1.00 38.11 ? 9    ALA H N   1 
ATOM   1855 C CA  . ALA B 1 9   ? 17.229  37.144  5.849   1.00 40.00 ? 9    ALA H CA  1 
ATOM   1856 C C   . ALA B 1 9   ? 17.444  37.443  4.357   1.00 39.18 ? 9    ALA H C   1 
ATOM   1857 O O   . ALA B 1 9   ? 18.590  37.733  3.964   1.00 38.75 ? 9    ALA H O   1 
ATOM   1858 C CB  . ALA B 1 9   ? 16.915  38.405  6.613   1.00 41.46 ? 9    ALA H CB  1 
ATOM   1859 N N   . GLU B 1 10  ? 16.381  37.314  3.569   1.00 38.70 ? 10   GLU H N   1 
ATOM   1860 C CA  . GLU B 1 10  ? 16.375  37.469  2.099   1.00 40.03 ? 10   GLU H CA  1 
ATOM   1861 C C   . GLU B 1 10  ? 15.341  38.523  1.726   1.00 39.54 ? 10   GLU H C   1 
ATOM   1862 O O   . GLU B 1 10  ? 14.217  38.456  2.240   1.00 36.42 ? 10   GLU H O   1 
ATOM   1863 C CB  . GLU B 1 10  ? 15.990  36.152  1.433   1.00 41.79 ? 10   GLU H CB  1 
ATOM   1864 C CG  . GLU B 1 10  ? 16.999  35.058  1.660   1.00 44.55 ? 10   GLU H CG  1 
ATOM   1865 C CD  . GLU B 1 10  ? 17.972  34.836  0.519   1.00 47.89 ? 10   GLU H CD  1 
ATOM   1866 O OE1 . GLU B 1 10  ? 18.028  35.698  -0.383  1.00 47.24 ? 10   GLU H OE1 1 
ATOM   1867 O OE2 . GLU B 1 10  ? 18.672  33.792  0.552   1.00 51.21 ? 10   GLU H OE2 1 
ATOM   1868 N N   . LEU B 1 11  ? 15.705  39.411  0.800   1.00 41.12 ? 11   LEU H N   1 
ATOM   1869 C CA  . LEU B 1 11  ? 14.834  40.479  0.263   1.00 42.58 ? 11   LEU H CA  1 
ATOM   1870 C C   . LEU B 1 11  ? 14.856  40.326  -1.257  1.00 40.98 ? 11   LEU H C   1 
ATOM   1871 O O   . LEU B 1 11  ? 15.951  40.417  -1.797  1.00 40.18 ? 11   LEU H O   1 
ATOM   1872 C CB  . LEU B 1 11  ? 15.444  41.816  0.705   1.00 45.88 ? 11   LEU H CB  1 
ATOM   1873 C CG  . LEU B 1 11  ? 14.500  42.966  1.064   1.00 49.10 ? 11   LEU H CG  1 
ATOM   1874 C CD1 . LEU B 1 11  ? 13.192  42.901  0.302   1.00 47.23 ? 11   LEU H CD1 1 
ATOM   1875 C CD2 . LEU B 1 11  ? 14.271  43.020  2.586   1.00 50.88 ? 11   LEU H CD2 1 
ATOM   1876 N N   . VAL B 1 12  ? 13.731  40.014  -1.901  1.00 41.57 ? 12   VAL H N   1 
ATOM   1877 C CA  . VAL B 1 12  ? 13.692  39.654  -3.346  1.00 42.21 ? 12   VAL H CA  1 
ATOM   1878 C C   . VAL B 1 12  ? 12.454  40.265  -3.996  1.00 43.25 ? 12   VAL H C   1 
ATOM   1879 O O   . VAL B 1 12  ? 11.506  40.662  -3.278  1.00 42.49 ? 12   VAL H O   1 
ATOM   1880 C CB  . VAL B 1 12  ? 13.714  38.133  -3.592  1.00 42.83 ? 12   VAL H CB  1 
ATOM   1881 C CG1 . VAL B 1 12  ? 15.017  37.477  -3.175  1.00 42.13 ? 12   VAL H CG1 1 
ATOM   1882 C CG2 . VAL B 1 12  ? 12.528  37.434  -2.939  1.00 42.41 ? 12   VAL H CG2 1 
ATOM   1883 N N   . LYS B 1 13  ? 12.503  40.313  -5.333  1.00 46.01 ? 13   LYS H N   1 
ATOM   1884 C CA  . LYS B 1 13  ? 11.439  40.801  -6.249  1.00 46.69 ? 13   LYS H CA  1 
ATOM   1885 C C   . LYS B 1 13  ? 10.418  39.694  -6.459  1.00 42.85 ? 13   LYS H C   1 
ATOM   1886 O O   . LYS B 1 13  ? 10.795  38.535  -6.562  1.00 40.99 ? 13   LYS H O   1 
ATOM   1887 C CB  . LYS B 1 13  ? 12.034  41.173  -7.616  1.00 48.57 ? 13   LYS H CB  1 
ATOM   1888 C CG  . LYS B 1 13  ? 12.581  42.592  -7.745  1.00 53.44 ? 13   LYS H CG  1 
ATOM   1889 C CD  . LYS B 1 13  ? 11.479  43.658  -7.799  1.00 57.47 ? 13   LYS H CD  1 
ATOM   1890 C CE  . LYS B 1 13  ? 11.753  44.801  -8.756  1.00 59.49 ? 13   LYS H CE  1 
ATOM   1891 N NZ  . LYS B 1 13  ? 12.714  45.757  -8.161  1.00 60.99 ? 13   LYS H NZ  1 
ATOM   1892 N N   . PRO B 1 14  ? 9.118   40.038  -6.562  1.00 42.65 ? 14   PRO H N   1 
ATOM   1893 C CA  . PRO B 1 14  ? 8.107   39.106  -7.027  1.00 40.28 ? 14   PRO H CA  1 
ATOM   1894 C C   . PRO B 1 14  ? 8.623   38.426  -8.302  1.00 37.32 ? 14   PRO H C   1 
ATOM   1895 O O   . PRO B 1 14  ? 9.302   39.088  -9.101  1.00 35.42 ? 14   PRO H O   1 
ATOM   1896 C CB  . PRO B 1 14  ? 6.855   39.950  -7.278  1.00 42.77 ? 14   PRO H CB  1 
ATOM   1897 C CG  . PRO B 1 14  ? 7.062   41.223  -6.467  1.00 44.42 ? 14   PRO H CG  1 
ATOM   1898 C CD  . PRO B 1 14  ? 8.556   41.358  -6.234  1.00 45.26 ? 14   PRO H CD  1 
ATOM   1899 N N   . GLY B 1 15  ? 8.396   37.116  -8.404  1.00 34.03 ? 15   GLY H N   1 
ATOM   1900 C CA  . GLY B 1 15  ? 8.789   36.298  -9.569  1.00 32.43 ? 15   GLY H CA  1 
ATOM   1901 C C   . GLY B 1 15  ? 10.145  35.652  -9.387  1.00 31.96 ? 15   GLY H C   1 
ATOM   1902 O O   . GLY B 1 15  ? 10.452  34.708  -10.095 1.00 33.77 ? 15   GLY H O   1 
ATOM   1903 N N   . ALA B 1 16  ? 10.969  36.109  -8.459  1.00 32.61 ? 16   ALA H N   1 
ATOM   1904 C CA  . ALA B 1 16  ? 12.285  35.476  -8.252  1.00 31.50 ? 16   ALA H CA  1 
ATOM   1905 C C   . ALA B 1 16  ? 12.122  34.146  -7.477  1.00 30.96 ? 16   ALA H C   1 
ATOM   1906 O O   . ALA B 1 16  ? 10.975  33.759  -7.097  1.00 28.39 ? 16   ALA H O   1 
ATOM   1907 C CB  . ALA B 1 16  ? 13.221  36.434  -7.563  1.00 32.99 ? 16   ALA H CB  1 
ATOM   1908 N N   . SER B 1 17  ? 13.242  33.453  -7.308  1.00 29.50 ? 17   SER H N   1 
ATOM   1909 C CA  . SER B 1 17  ? 13.384  32.222  -6.472  1.00 29.88 ? 17   SER H CA  1 
ATOM   1910 C C   . SER B 1 17  ? 14.354  32.509  -5.340  1.00 29.52 ? 17   SER H C   1 
ATOM   1911 O O   . SER B 1 17  ? 15.164  33.445  -5.481  1.00 31.44 ? 17   SER H O   1 
ATOM   1912 C CB  . SER B 1 17  ? 13.852  31.051  -7.288  1.00 28.94 ? 17   SER H CB  1 
ATOM   1913 O OG  . SER B 1 17  ? 12.818  30.699  -8.197  1.00 31.07 ? 17   SER H OG  1 
ATOM   1914 N N   . VAL B 1 18  ? 14.296  31.725  -4.264  1.00 28.10 ? 18   VAL H N   1 
ATOM   1915 C CA  . VAL B 1 18  ? 15.290  31.813  -3.153  1.00 29.54 ? 18   VAL H CA  1 
ATOM   1916 C C   . VAL B 1 18  ? 15.554  30.379  -2.709  1.00 27.27 ? 18   VAL H C   1 
ATOM   1917 O O   . VAL B 1 18  ? 14.672  29.537  -2.837  1.00 25.34 ? 18   VAL H O   1 
ATOM   1918 C CB  . VAL B 1 18  ? 14.867  32.680  -1.939  1.00 31.31 ? 18   VAL H CB  1 
ATOM   1919 C CG1 . VAL B 1 18  ? 14.687  34.134  -2.312  1.00 33.32 ? 18   VAL H CG1 1 
ATOM   1920 C CG2 . VAL B 1 18  ? 13.612  32.144  -1.270  1.00 29.79 ? 18   VAL H CG2 1 
ATOM   1921 N N   . LYS B 1 19  ? 16.771  30.132  -2.279  1.00 28.34 ? 19   LYS H N   1 
ATOM   1922 C CA  . LYS B 1 19  ? 17.179  28.878  -1.636  1.00 29.94 ? 19   LYS H CA  1 
ATOM   1923 C C   . LYS B 1 19  ? 17.694  29.197  -0.240  1.00 30.06 ? 19   LYS H C   1 
ATOM   1924 O O   . LYS B 1 19  ? 18.689  29.920  -0.120  1.00 30.10 ? 19   LYS H O   1 
ATOM   1925 C CB  . LYS B 1 19  ? 18.283  28.234  -2.457  1.00 32.30 ? 19   LYS H CB  1 
ATOM   1926 C CG  . LYS B 1 19  ? 18.627  26.809  -2.081  1.00 33.44 ? 19   LYS H CG  1 
ATOM   1927 C CD  . LYS B 1 19  ? 19.168  26.103  -3.300  1.00 35.48 ? 19   LYS H CD  1 
ATOM   1928 C CE  . LYS B 1 19  ? 20.102  24.977  -2.982  1.00 38.25 ? 19   LYS H CE  1 
ATOM   1929 N NZ  . LYS B 1 19  ? 20.551  24.332  -4.235  1.00 38.72 ? 19   LYS H NZ  1 
ATOM   1930 N N   . ILE B 1 20  ? 17.003  28.669  0.772   1.00 29.17 ? 20   ILE H N   1 
ATOM   1931 C CA  . ILE B 1 20  ? 17.314  28.823  2.226   1.00 29.98 ? 20   ILE H CA  1 
ATOM   1932 C C   . ILE B 1 20  ? 18.061  27.561  2.639   1.00 27.88 ? 20   ILE H C   1 
ATOM   1933 O O   . ILE B 1 20  ? 17.673  26.471  2.159   1.00 26.99 ? 20   ILE H O   1 
ATOM   1934 C CB  . ILE B 1 20  ? 16.016  28.994  3.035   1.00 31.09 ? 20   ILE H CB  1 
ATOM   1935 C CG1 . ILE B 1 20  ? 15.264  30.245  2.566   1.00 34.29 ? 20   ILE H CG1 1 
ATOM   1936 C CG2 . ILE B 1 20  ? 16.304  29.041  4.517   1.00 34.02 ? 20   ILE H CG2 1 
ATOM   1937 C CD1 . ILE B 1 20  ? 13.857  30.362  3.112   1.00 34.32 ? 20   ILE H CD1 1 
ATOM   1938 N N   . SER B 1 21  ? 19.134  27.698  3.393   1.00 27.06 ? 21   SER H N   1 
ATOM   1939 C CA  . SER B 1 21  ? 19.932  26.552  3.870   1.00 26.72 ? 21   SER H CA  1 
ATOM   1940 C C   . SER B 1 21  ? 19.673  26.336  5.366   1.00 27.47 ? 21   SER H C   1 
ATOM   1941 O O   . SER B 1 21  ? 19.348  27.275  6.109   1.00 27.43 ? 21   SER H O   1 
ATOM   1942 C CB  . SER B 1 21  ? 21.396  26.725  3.531   1.00 27.85 ? 21   SER H CB  1 
ATOM   1943 O OG  . SER B 1 21  ? 21.970  27.763  4.286   1.00 28.65 ? 21   SER H OG  1 
ATOM   1944 N N   . CYS B 1 22  ? 19.868  25.105  5.778   1.00 28.28 ? 22   CYS H N   1 
ATOM   1945 C CA  . CYS B 1 22  ? 19.702  24.640  7.184   1.00 29.40 ? 22   CYS H CA  1 
ATOM   1946 C C   . CYS B 1 22  ? 20.874  23.735  7.490   1.00 28.90 ? 22   CYS H C   1 
ATOM   1947 O O   . CYS B 1 22  ? 20.856  22.633  6.994   1.00 30.13 ? 22   CYS H O   1 
ATOM   1948 C CB  . CYS B 1 22  ? 18.377  23.910  7.325   1.00 28.88 ? 22   CYS H CB  1 
ATOM   1949 S SG  . CYS B 1 22  ? 18.175  23.232  8.980   1.00 31.91 ? 22   CYS H SG  1 
ATOM   1950 N N   . LYS B 1 23  ? 21.898  24.243  8.159   1.00 29.89 ? 23   LYS H N   1 
ATOM   1951 C CA  . LYS B 1 23  ? 23.139  23.473  8.374   1.00 31.20 ? 23   LYS H CA  1 
ATOM   1952 C C   . LYS B 1 23  ? 23.020  22.725  9.705   1.00 28.85 ? 23   LYS H C   1 
ATOM   1953 O O   . LYS B 1 23  ? 22.888  23.370  10.724  1.00 27.47 ? 23   LYS H O   1 
ATOM   1954 C CB  . LYS B 1 23  ? 24.357  24.384  8.321   1.00 34.23 ? 23   LYS H CB  1 
ATOM   1955 C CG  . LYS B 1 23  ? 25.628  23.756  8.888   1.00 38.87 ? 23   LYS H CG  1 
ATOM   1956 C CD  . LYS B 1 23  ? 26.029  22.430  8.265   1.00 41.13 ? 23   LYS H CD  1 
ATOM   1957 C CE  . LYS B 1 23  ? 27.468  22.471  7.769   1.00 46.22 ? 23   LYS H CE  1 
ATOM   1958 N NZ  . LYS B 1 23  ? 28.437  22.458  8.883   1.00 48.50 ? 23   LYS H NZ  1 
ATOM   1959 N N   . ALA B 1 24  ? 23.080  21.406  9.675   1.00 27.72 ? 24   ALA H N   1 
ATOM   1960 C CA  . ALA B 1 24  ? 22.869  20.558  10.882  1.00 29.33 ? 24   ALA H CA  1 
ATOM   1961 C C   . ALA B 1 24  ? 24.215  20.189  11.471  1.00 30.00 ? 24   ALA H C   1 
ATOM   1962 O O   . ALA B 1 24  ? 25.114  19.889  10.704  1.00 31.89 ? 24   ALA H O   1 
ATOM   1963 C CB  . ALA B 1 24  ? 22.090  19.326  10.512  1.00 28.91 ? 24   ALA H CB  1 
ATOM   1964 N N   . SER B 1 25  ? 24.351  20.194  12.786  1.00 31.34 ? 25   SER H N   1 
ATOM   1965 C CA  . SER B 1 25  ? 25.577  19.694  13.460  1.00 30.31 ? 25   SER H CA  1 
ATOM   1966 C C   . SER B 1 25  ? 25.197  19.035  14.790  1.00 29.55 ? 25   SER H C   1 
ATOM   1967 O O   . SER B 1 25  ? 24.117  19.342  15.307  1.00 28.29 ? 25   SER H O   1 
ATOM   1968 C CB  . SER B 1 25  ? 26.599  20.801  13.637  1.00 33.16 ? 25   SER H CB  1 
ATOM   1969 O OG  . SER B 1 25  ? 26.077  21.879  14.406  1.00 34.04 ? 25   SER H OG  1 
ATOM   1970 N N   . GLY B 1 26  ? 26.119  18.233  15.335  1.00 29.90 ? 26   GLY H N   1 
ATOM   1971 C CA  . GLY B 1 26  ? 26.026  17.649  16.678  1.00 29.68 ? 26   GLY H CA  1 
ATOM   1972 C C   . GLY B 1 26  ? 25.179  16.389  16.707  1.00 27.66 ? 26   GLY H C   1 
ATOM   1973 O O   . GLY B 1 26  ? 24.911  15.896  17.834  1.00 26.11 ? 26   GLY H O   1 
ATOM   1974 N N   . TYR B 1 27  ? 24.879  15.796  15.554  1.00 26.35 ? 27   TYR H N   1 
ATOM   1975 C CA  . TYR B 1 27  ? 24.161  14.505  15.478  1.00 25.66 ? 27   TYR H CA  1 
ATOM   1976 C C   . TYR B 1 27  ? 24.396  13.891  14.100  1.00 26.94 ? 27   TYR H C   1 
ATOM   1977 O O   . TYR B 1 27  ? 24.935  14.594  13.207  1.00 26.74 ? 27   TYR H O   1 
ATOM   1978 C CB  . TYR B 1 27  ? 22.674  14.710  15.804  1.00 25.10 ? 27   TYR H CB  1 
ATOM   1979 C CG  . TYR B 1 27  ? 21.884  15.390  14.719  1.00 24.34 ? 27   TYR H CG  1 
ATOM   1980 C CD1 . TYR B 1 27  ? 21.799  16.773  14.655  1.00 24.34 ? 27   TYR H CD1 1 
ATOM   1981 C CD2 . TYR B 1 27  ? 21.272  14.653  13.724  1.00 24.13 ? 27   TYR H CD2 1 
ATOM   1982 C CE1 . TYR B 1 27  ? 21.087  17.401  13.644  1.00 24.69 ? 27   TYR H CE1 1 
ATOM   1983 C CE2 . TYR B 1 27  ? 20.554  15.268  12.701  1.00 24.09 ? 27   TYR H CE2 1 
ATOM   1984 C CZ  . TYR B 1 27  ? 20.469  16.652  12.663  1.00 24.27 ? 27   TYR H CZ  1 
ATOM   1985 O OH  . TYR B 1 27  ? 19.770  17.235  11.640  1.00 24.89 ? 27   TYR H OH  1 
ATOM   1986 N N   . ILE B 1 28  ? 23.964  12.654  13.890  1.00 24.87 ? 28   ILE H N   1 
ATOM   1987 C CA  . ILE B 1 28  ? 24.171  11.969  12.588  1.00 24.91 ? 28   ILE H CA  1 
ATOM   1988 C C   . ILE B 1 28  ? 23.097  12.481  11.636  1.00 24.21 ? 28   ILE H C   1 
ATOM   1989 O O   . ILE B 1 28  ? 21.927  12.202  11.865  1.00 21.21 ? 28   ILE H O   1 
ATOM   1990 C CB  . ILE B 1 28  ? 24.184  10.444  12.711  1.00 25.95 ? 28   ILE H CB  1 
ATOM   1991 C CG1 . ILE B 1 28  ? 25.326  10.026  13.644  1.00 28.41 ? 28   ILE H CG1 1 
ATOM   1992 C CG2 . ILE B 1 28  ? 24.312  9.788   11.359  1.00 26.91 ? 28   ILE H CG2 1 
ATOM   1993 C CD1 . ILE B 1 28  ? 25.219  8.589   14.066  1.00 29.73 ? 28   ILE H CD1 1 
ATOM   1994 N N   . PHE B 1 29  ? 23.524  13.190  10.595  1.00 23.26 ? 29   PHE H N   1 
ATOM   1995 C CA  . PHE B 1 29  ? 22.604  13.856  9.654   1.00 23.74 ? 29   PHE H CA  1 
ATOM   1996 C C   . PHE B 1 29  ? 21.610  12.853  9.071   1.00 22.21 ? 29   PHE H C   1 
ATOM   1997 O O   . PHE B 1 29  ? 20.430  13.204  8.912   1.00 22.07 ? 29   PHE H O   1 
ATOM   1998 C CB  . PHE B 1 29  ? 23.422  14.516  8.544   1.00 25.55 ? 29   PHE H CB  1 
ATOM   1999 C CG  . PHE B 1 29  ? 22.617  15.357  7.595   1.00 25.29 ? 29   PHE H CG  1 
ATOM   2000 C CD1 . PHE B 1 29  ? 21.956  16.489  8.038   1.00 25.90 ? 29   PHE H CD1 1 
ATOM   2001 C CD2 . PHE B 1 29  ? 22.611  15.081  6.239   1.00 26.55 ? 29   PHE H CD2 1 
ATOM   2002 C CE1 . PHE B 1 29  ? 21.262  17.302  7.149   1.00 26.09 ? 29   PHE H CE1 1 
ATOM   2003 C CE2 . PHE B 1 29  ? 21.914  15.892  5.361   1.00 25.42 ? 29   PHE H CE2 1 
ATOM   2004 C CZ  . PHE B 1 29  ? 21.211  16.978  5.823   1.00 25.85 ? 29   PHE H CZ  1 
ATOM   2005 N N   . ALA B 1 30  ? 22.089  11.649  8.744   1.00 22.01 ? 30   ALA H N   1 
ATOM   2006 C CA  . ALA B 1 30  ? 21.312  10.563  8.118   1.00 22.33 ? 30   ALA H CA  1 
ATOM   2007 C C   . ALA B 1 30  ? 20.165  10.102  9.042   1.00 21.65 ? 30   ALA H C   1 
ATOM   2008 O O   . ALA B 1 30  ? 19.338  9.348   8.553   1.00 22.50 ? 30   ALA H O   1 
ATOM   2009 C CB  . ALA B 1 30  ? 22.217  9.386   7.818   1.00 23.51 ? 30   ALA H CB  1 
ATOM   2010 N N   . ASP B 1 31  ? 20.219  10.402  10.343  1.00 21.49 ? 31   ASP H N   1 
ATOM   2011 C CA  . ASP B 1 31  ? 19.352  9.695   11.327  1.00 21.46 ? 31   ASP H CA  1 
ATOM   2012 C C   . ASP B 1 31  ? 18.062  10.460  11.659  1.00 20.08 ? 31   ASP H C   1 
ATOM   2013 O O   . ASP B 1 31  ? 17.258  9.930   12.425  1.00 19.09 ? 31   ASP H O   1 
ATOM   2014 C CB  . ASP B 1 31  ? 20.178  9.270   12.523  1.00 23.52 ? 31   ASP H CB  1 
ATOM   2015 C CG  . ASP B 1 31  ? 21.116  8.117   12.196  1.00 23.85 ? 31   ASP H CG  1 
ATOM   2016 O OD1 . ASP B 1 31  ? 21.135  7.612   11.042  1.00 27.43 ? 31   ASP H OD1 1 
ATOM   2017 O OD2 . ASP B 1 31  ? 21.766  7.712   13.083  1.00 27.67 ? 31   ASP H OD2 1 
ATOM   2018 N N   . HIS B 1 32  ? 17.805  11.621  11.079  1.00 19.28 ? 32   HIS H N   1 
ATOM   2019 C CA  . HIS B 1 32  ? 16.545  12.380  11.323  1.00 18.53 ? 32   HIS H CA  1 
ATOM   2020 C C   . HIS B 1 32  ? 16.159  13.159  10.075  1.00 18.58 ? 32   HIS H C   1 
ATOM   2021 O O   . HIS B 1 32  ? 17.023  13.776  9.437   1.00 18.83 ? 32   HIS H O   1 
ATOM   2022 C CB  . HIS B 1 32  ? 16.672  13.398  12.490  1.00 17.91 ? 32   HIS H CB  1 
ATOM   2023 C CG  . HIS B 1 32  ? 17.046  12.744  13.783  1.00 18.14 ? 32   HIS H CG  1 
ATOM   2024 N ND1 . HIS B 1 32  ? 16.123  12.040  14.532  1.00 17.98 ? 32   HIS H ND1 1 
ATOM   2025 C CD2 . HIS B 1 32  ? 18.256  12.567  14.367  1.00 18.24 ? 32   HIS H CD2 1 
ATOM   2026 C CE1 . HIS B 1 32  ? 16.757  11.459  15.543  1.00 17.39 ? 32   HIS H CE1 1 
ATOM   2027 N NE2 . HIS B 1 32  ? 18.081  11.771  15.476  1.00 17.21 ? 32   HIS H NE2 1 
ATOM   2028 N N   . ALA B 1 33  ? 14.880  13.171  9.800   1.00 18.02 ? 33   ALA H N   1 
ATOM   2029 C CA  . ALA B 1 33  ? 14.278  14.043  8.780   1.00 18.13 ? 33   ALA H CA  1 
ATOM   2030 C C   . ALA B 1 33  ? 14.321  15.500  9.237   1.00 18.06 ? 33   ALA H C   1 
ATOM   2031 O O   . ALA B 1 33  ? 14.182  15.815  10.399  1.00 17.53 ? 33   ALA H O   1 
ATOM   2032 C CB  . ALA B 1 33  ? 12.880  13.598  8.441   1.00 18.06 ? 33   ALA H CB  1 
ATOM   2033 N N   . ILE B 1 34  ? 14.440  16.391  8.262   1.00 18.05 ? 34   ILE H N   1 
ATOM   2034 C CA  . ILE B 1 34  ? 14.371  17.842  8.457   1.00 18.53 ? 34   ILE H CA  1 
ATOM   2035 C C   . ILE B 1 34  ? 13.093  18.289  7.799   1.00 18.19 ? 34   ILE H C   1 
ATOM   2036 O O   . ILE B 1 34  ? 12.861  17.973  6.564   1.00 17.86 ? 34   ILE H O   1 
ATOM   2037 C CB  . ILE B 1 34  ? 15.591  18.511  7.816   1.00 20.22 ? 34   ILE H CB  1 
ATOM   2038 C CG1 . ILE B 1 34  ? 16.883  18.096  8.508   1.00 20.99 ? 34   ILE H CG1 1 
ATOM   2039 C CG2 . ILE B 1 34  ? 15.394  20.009  7.801   1.00 19.86 ? 34   ILE H CG2 1 
ATOM   2040 C CD1 . ILE B 1 34  ? 16.990  18.672  9.883   1.00 23.00 ? 34   ILE H CD1 1 
ATOM   2041 N N   . HIS B 1 35  ? 12.287  18.960  8.593   1.00 17.95 ? 35   HIS H N   1 
ATOM   2042 C CA  . HIS B 1 35  ? 10.997  19.475  8.109   1.00 17.83 ? 35   HIS H CA  1 
ATOM   2043 C C   . HIS B 1 35  ? 11.128  20.977  7.921   1.00 19.19 ? 35   HIS H C   1 
ATOM   2044 O O   . HIS B 1 35  ? 11.993  21.579  8.540   1.00 19.75 ? 35   HIS H O   1 
ATOM   2045 C CB  . HIS B 1 35  ? 9.888   19.198  9.124   1.00 17.68 ? 35   HIS H CB  1 
ATOM   2046 C CG  . HIS B 1 35  ? 9.592   17.759  9.349   1.00 17.03 ? 35   HIS H CG  1 
ATOM   2047 N ND1 . HIS B 1 35  ? 8.347   17.228  9.120   1.00 17.39 ? 35   HIS H ND1 1 
ATOM   2048 C CD2 . HIS B 1 35  ? 10.358  16.749  9.798   1.00 15.97 ? 35   HIS H CD2 1 
ATOM   2049 C CE1 . HIS B 1 35  ? 8.357   15.951  9.411   1.00 15.90 ? 35   HIS H CE1 1 
ATOM   2050 N NE2 . HIS B 1 35  ? 9.576   15.639  9.819   1.00 17.76 ? 35   HIS H NE2 1 
ATOM   2051 N N   . TRP B 1 36  ? 10.263  21.532  7.095   1.00 19.90 ? 36   TRP H N   1 
ATOM   2052 C CA  . TRP B 1 36  ? 10.220  22.980  6.866   1.00 20.39 ? 36   TRP H CA  1 
ATOM   2053 C C   . TRP B 1 36  ? 8.831   23.491  7.200   1.00 20.93 ? 36   TRP H C   1 
ATOM   2054 O O   . TRP B 1 36  ? 7.868   22.857  6.849   1.00 20.51 ? 36   TRP H O   1 
ATOM   2055 C CB  . TRP B 1 36  ? 10.679  23.302  5.462   1.00 20.56 ? 36   TRP H CB  1 
ATOM   2056 C CG  . TRP B 1 36  ? 12.142  23.042  5.230   1.00 20.67 ? 36   TRP H CG  1 
ATOM   2057 C CD1 . TRP B 1 36  ? 12.689  21.883  4.782   1.00 21.50 ? 36   TRP H CD1 1 
ATOM   2058 C CD2 . TRP B 1 36  ? 13.247  23.960  5.343   1.00 21.79 ? 36   TRP H CD2 1 
ATOM   2059 N NE1 . TRP B 1 36  ? 14.042  22.020  4.578   1.00 21.79 ? 36   TRP H NE1 1 
ATOM   2060 C CE2 . TRP B 1 36  ? 14.414  23.277  4.926   1.00 22.31 ? 36   TRP H CE2 1 
ATOM   2061 C CE3 . TRP B 1 36  ? 13.360  25.296  5.685   1.00 22.90 ? 36   TRP H CE3 1 
ATOM   2062 C CZ2 . TRP B 1 36  ? 15.669  23.881  4.887   1.00 23.84 ? 36   TRP H CZ2 1 
ATOM   2063 C CZ3 . TRP B 1 36  ? 14.605  25.891  5.687   1.00 24.64 ? 36   TRP H CZ3 1 
ATOM   2064 C CH2 . TRP B 1 36  ? 15.743  25.187  5.276   1.00 24.20 ? 36   TRP H CH2 1 
ATOM   2065 N N   . VAL B 1 37  ? 8.810   24.632  7.875   1.00 22.06 ? 37   VAL H N   1 
ATOM   2066 C CA  . VAL B 1 37  ? 7.602   25.267  8.464   1.00 23.96 ? 37   VAL H CA  1 
ATOM   2067 C C   . VAL B 1 37  ? 7.632   26.769  8.120   1.00 24.52 ? 37   VAL H C   1 
ATOM   2068 O O   . VAL B 1 37  ? 8.686   27.402  8.225   1.00 24.50 ? 37   VAL H O   1 
ATOM   2069 C CB  . VAL B 1 37  ? 7.564   24.981  9.985   1.00 24.56 ? 37   VAL H CB  1 
ATOM   2070 C CG1 . VAL B 1 37  ? 6.476   25.742  10.720  1.00 24.92 ? 37   VAL H CG1 1 
ATOM   2071 C CG2 . VAL B 1 37  ? 7.427   23.490  10.229  1.00 24.36 ? 37   VAL H CG2 1 
ATOM   2072 N N   . LYS B 1 38  ? 6.489   27.305  7.725   1.00 25.49 ? 38   LYS H N   1 
ATOM   2073 C CA  . LYS B 1 38  ? 6.293   28.731  7.362   1.00 26.23 ? 38   LYS H CA  1 
ATOM   2074 C C   . LYS B 1 38  ? 5.531   29.386  8.507   1.00 28.35 ? 38   LYS H C   1 
ATOM   2075 O O   . LYS B 1 38  ? 4.502   28.844  8.871   1.00 26.70 ? 38   LYS H O   1 
ATOM   2076 C CB  . LYS B 1 38  ? 5.488   28.785  6.080   1.00 26.32 ? 38   LYS H CB  1 
ATOM   2077 C CG  . LYS B 1 38  ? 5.133   30.160  5.571   1.00 26.61 ? 38   LYS H CG  1 
ATOM   2078 C CD  . LYS B 1 38  ? 4.276   30.077  4.350   1.00 26.49 ? 38   LYS H CD  1 
ATOM   2079 C CE  . LYS B 1 38  ? 3.913   31.454  3.860   1.00 27.20 ? 38   LYS H CE  1 
ATOM   2080 N NZ  . LYS B 1 38  ? 3.149   31.335  2.599   1.00 26.31 ? 38   LYS H NZ  1 
ATOM   2081 N N   . ARG B 1 39  ? 6.048   30.508  9.018   1.00 30.97 ? 39   ARG H N   1 
ATOM   2082 C CA  . ARG B 1 39  ? 5.401   31.341  10.060  1.00 34.29 ? 39   ARG H CA  1 
ATOM   2083 C C   . ARG B 1 39  ? 5.140   32.730  9.449   1.00 35.20 ? 39   ARG H C   1 
ATOM   2084 O O   . ARG B 1 39  ? 6.105   33.487  9.259   1.00 32.46 ? 39   ARG H O   1 
ATOM   2085 C CB  . ARG B 1 39  ? 6.313   31.391  11.282  1.00 36.80 ? 39   ARG H CB  1 
ATOM   2086 C CG  . ARG B 1 39  ? 5.564   31.385  12.601  1.00 41.06 ? 39   ARG H CG  1 
ATOM   2087 C CD  . ARG B 1 39  ? 5.273   32.756  13.082  1.00 45.68 ? 39   ARG H CD  1 
ATOM   2088 N NE  . ARG B 1 39  ? 4.226   32.778  14.101  1.00 46.16 ? 39   ARG H NE  1 
ATOM   2089 C CZ  . ARG B 1 39  ? 2.967   33.112  13.858  1.00 49.54 ? 39   ARG H CZ  1 
ATOM   2090 N NH1 . ARG B 1 39  ? 2.126   33.210  14.863  1.00 53.00 ? 39   ARG H NH1 1 
ATOM   2091 N NH2 . ARG B 1 39  ? 2.549   33.402  12.633  1.00 51.30 ? 39   ARG H NH2 1 
ATOM   2092 N N   . LYS B 1 40  ? 3.897   32.975  9.055   1.00 37.69 ? 40   LYS H N   1 
ATOM   2093 C CA  . LYS B 1 40  ? 3.486   34.217  8.362   1.00 42.95 ? 40   LYS H CA  1 
ATOM   2094 C C   . LYS B 1 40  ? 2.765   35.042  9.404   1.00 48.27 ? 40   LYS H C   1 
ATOM   2095 O O   . LYS B 1 40  ? 1.807   34.522  9.955   1.00 48.32 ? 40   LYS H O   1 
ATOM   2096 C CB  . LYS B 1 40  ? 2.607   33.929  7.139   1.00 43.27 ? 40   LYS H CB  1 
ATOM   2097 C CG  . LYS B 1 40  ? 2.352   35.132  6.246   1.00 45.43 ? 40   LYS H CG  1 
ATOM   2098 C CD  . LYS B 1 40  ? 1.464   34.856  5.058   1.00 45.87 ? 40   LYS H CD  1 
ATOM   2099 C CE  . LYS B 1 40  ? 1.289   36.073  4.148   1.00 47.46 ? 40   LYS H CE  1 
ATOM   2100 N NZ  . LYS B 1 40  ? 2.584   36.689  3.739   1.00 44.95 ? 40   LYS H NZ  1 
ATOM   2101 N N   . PRO B 1 41  ? 3.183   36.323  9.632   1.00 53.82 ? 41   PRO H N   1 
ATOM   2102 C CA  . PRO B 1 41  ? 2.718   37.155  10.741  1.00 59.35 ? 41   PRO H CA  1 
ATOM   2103 C C   . PRO B 1 41  ? 1.232   37.028  11.113  1.00 62.82 ? 41   PRO H C   1 
ATOM   2104 O O   . PRO B 1 41  ? 0.943   36.600  12.219  1.00 69.07 ? 41   PRO H O   1 
ATOM   2105 C CB  . PRO B 1 41  ? 3.023   38.602  10.280  1.00 59.12 ? 41   PRO H CB  1 
ATOM   2106 C CG  . PRO B 1 41  ? 3.608   38.489  8.868   1.00 58.87 ? 41   PRO H CG  1 
ATOM   2107 C CD  . PRO B 1 41  ? 4.136   37.071  8.797   1.00 55.74 ? 41   PRO H CD  1 
ATOM   2108 N N   . GLU B 1 42  ? 0.334   37.406  10.207  1.00 69.56 ? 42   GLU H N   1 
ATOM   2109 C CA  . GLU B 1 42  ? -1.117  37.561  10.518  1.00 73.81 ? 42   GLU H CA  1 
ATOM   2110 C C   . GLU B 1 42  ? -1.792  36.189  10.500  1.00 67.13 ? 42   GLU H C   1 
ATOM   2111 O O   . GLU B 1 42  ? -3.022  36.128  10.605  1.00 74.72 ? 42   GLU H O   1 
ATOM   2112 C CB  . GLU B 1 42  ? -1.791  38.522  9.534   1.00 77.57 ? 42   GLU H CB  1 
ATOM   2113 C CG  . GLU B 1 42  ? -1.070  39.856  9.395   1.00 82.88 ? 42   GLU H CG  1 
ATOM   2114 C CD  . GLU B 1 42  ? -0.690  40.526  10.711  1.00 87.77 ? 42   GLU H CD  1 
ATOM   2115 O OE1 . GLU B 1 42  ? -1.432  40.339  11.701  1.00 90.73 ? 42   GLU H OE1 1 
ATOM   2116 O OE2 . GLU B 1 42  ? 0.344   41.245  10.746  1.00 89.68 ? 42   GLU H OE2 1 
ATOM   2117 N N   . GLN B 1 43  ? -1.016  35.131  10.326  1.00 62.15 ? 43   GLN H N   1 
ATOM   2118 C CA  . GLN B 1 43  ? -1.494  33.741  10.404  1.00 56.12 ? 43   GLN H CA  1 
ATOM   2119 C C   . GLN B 1 43  ? -0.855  33.106  11.652  1.00 54.78 ? 43   GLN H C   1 
ATOM   2120 O O   . GLN B 1 43  ? -0.679  33.850  12.699  1.00 53.67 ? 43   GLN H O   1 
ATOM   2121 C CB  . GLN B 1 43  ? -1.151  33.057  9.080   1.00 59.98 ? 43   GLN H CB  1 
ATOM   2122 C CG  . GLN B 1 43  ? -2.194  32.041  8.589   1.00 61.59 ? 43   GLN H CG  1 
ATOM   2123 C CD  . GLN B 1 43  ? -1.652  30.650  8.304   1.00 60.13 ? 43   GLN H CD  1 
ATOM   2124 O OE1 . GLN B 1 43  ? -2.072  29.963  7.364   1.00 56.76 ? 43   GLN H OE1 1 
ATOM   2125 N NE2 . GLN B 1 43  ? -0.717  30.209  9.130   1.00 54.61 ? 43   GLN H NE2 1 
ATOM   2126 N N   . GLY B 1 44  ? -0.617  31.792  11.557  1.00 43.83 ? 44   GLY H N   1 
ATOM   2127 C CA  . GLY B 1 44  ? 0.212   30.953  12.428  1.00 40.35 ? 44   GLY H CA  1 
ATOM   2128 C C   . GLY B 1 44  ? 1.245   30.140  11.643  1.00 36.20 ? 44   GLY H C   1 
ATOM   2129 O O   . GLY B 1 44  ? 2.173   30.783  11.027  1.00 33.73 ? 44   GLY H O   1 
ATOM   2130 N N   . LEU B 1 45  ? 1.174   28.798  11.730  1.00 32.28 ? 45   LEU H N   1 
ATOM   2131 C CA  . LEU B 1 45  ? 2.232   27.878  11.246  1.00 28.43 ? 45   LEU H CA  1 
ATOM   2132 C C   . LEU B 1 45  ? 1.682   26.942  10.174  1.00 27.33 ? 45   LEU H C   1 
ATOM   2133 O O   . LEU B 1 45  ? 0.545   26.486  10.283  1.00 26.34 ? 45   LEU H O   1 
ATOM   2134 C CB  . LEU B 1 45  ? 2.810   27.039  12.395  1.00 27.65 ? 45   LEU H CB  1 
ATOM   2135 C CG  . LEU B 1 45  ? 3.609   27.810  13.447  1.00 28.55 ? 45   LEU H CG  1 
ATOM   2136 C CD1 . LEU B 1 45  ? 3.664   27.001  14.723  1.00 28.33 ? 45   LEU H CD1 1 
ATOM   2137 C CD2 . LEU B 1 45  ? 5.018   28.090  12.969  1.00 29.25 ? 45   LEU H CD2 1 
ATOM   2138 N N   . GLU B 1 46  ? 2.503   26.673  9.169   1.00 25.46 ? 46   GLU H N   1 
ATOM   2139 C CA  . GLU B 1 46  ? 2.128   25.763  8.073   1.00 25.82 ? 46   GLU H CA  1 
ATOM   2140 C C   . GLU B 1 46  ? 3.295   24.832  7.817   1.00 23.71 ? 46   GLU H C   1 
ATOM   2141 O O   . GLU B 1 46  ? 4.441   25.318  7.731   1.00 23.31 ? 46   GLU H O   1 
ATOM   2142 C CB  . GLU B 1 46  ? 1.850   26.481  6.759   1.00 28.13 ? 46   GLU H CB  1 
ATOM   2143 C CG  . GLU B 1 46  ? 0.653   27.374  6.805   1.00 32.33 ? 46   GLU H CG  1 
ATOM   2144 C CD  . GLU B 1 46  ? 0.415   28.169  5.548   1.00 35.34 ? 46   GLU H CD  1 
ATOM   2145 O OE1 . GLU B 1 46  ? 0.742   29.409  5.529   1.00 41.09 ? 46   GLU H OE1 1 
ATOM   2146 O OE2 . GLU B 1 46  ? -0.206  27.569  4.643   1.00 40.15 ? 46   GLU H OE2 1 
ATOM   2147 N N   . TRP B 1 47  ? 3.000   23.553  7.664   1.00 22.02 ? 47   TRP H N   1 
ATOM   2148 C CA  . TRP B 1 47  ? 4.026   22.554  7.356   1.00 20.56 ? 47   TRP H CA  1 
ATOM   2149 C C   . TRP B 1 47  ? 4.196   22.477  5.842   1.00 20.67 ? 47   TRP H C   1 
ATOM   2150 O O   . TRP B 1 47  ? 3.190   22.379  5.124   1.00 19.75 ? 47   TRP H O   1 
ATOM   2151 C CB  . TRP B 1 47  ? 3.634   21.227  8.007   1.00 20.55 ? 47   TRP H CB  1 
ATOM   2152 C CG  . TRP B 1 47  ? 4.546   20.108  7.671   1.00 19.84 ? 47   TRP H CG  1 
ATOM   2153 C CD1 . TRP B 1 47  ? 5.778   19.874  8.184   1.00 20.36 ? 47   TRP H CD1 1 
ATOM   2154 C CD2 . TRP B 1 47  ? 4.301   19.086  6.682   1.00 20.05 ? 47   TRP H CD2 1 
ATOM   2155 N NE1 . TRP B 1 47  ? 6.291   18.741  7.630   1.00 20.16 ? 47   TRP H NE1 1 
ATOM   2156 C CE2 . TRP B 1 47  ? 5.430   18.254  6.680   1.00 19.70 ? 47   TRP H CE2 1 
ATOM   2157 C CE3 . TRP B 1 47  ? 3.259   18.797  5.801   1.00 19.64 ? 47   TRP H CE3 1 
ATOM   2158 C CZ2 . TRP B 1 47  ? 5.542   17.160  5.830   1.00 19.57 ? 47   TRP H CZ2 1 
ATOM   2159 C CZ3 . TRP B 1 47  ? 3.363   17.705  4.969   1.00 19.55 ? 47   TRP H CZ3 1 
ATOM   2160 C CH2 . TRP B 1 47  ? 4.506   16.907  4.977   1.00 19.24 ? 47   TRP H CH2 1 
ATOM   2161 N N   . ILE B 1 48  ? 5.438   22.492  5.391   1.00 20.64 ? 48   ILE H N   1 
ATOM   2162 C CA  . ILE B 1 48  ? 5.759   22.548  3.928   1.00 20.21 ? 48   ILE H CA  1 
ATOM   2163 C C   . ILE B 1 48  ? 6.092   21.143  3.434   1.00 19.87 ? 48   ILE H C   1 
ATOM   2164 O O   . ILE B 1 48  ? 5.606   20.737  2.372   1.00 19.03 ? 48   ILE H O   1 
ATOM   2165 C CB  . ILE B 1 48  ? 6.923   23.524  3.711   1.00 20.51 ? 48   ILE H CB  1 
ATOM   2166 C CG1 . ILE B 1 48  ? 6.526   24.964  4.064   1.00 20.59 ? 48   ILE H CG1 1 
ATOM   2167 C CG2 . ILE B 1 48  ? 7.450   23.436  2.293   1.00 20.68 ? 48   ILE H CG2 1 
ATOM   2168 C CD1 . ILE B 1 48  ? 7.697   25.902  4.155   1.00 21.05 ? 48   ILE H CD1 1 
ATOM   2169 N N   . GLY B 1 49  ? 6.914   20.408  4.193   1.00 20.43 ? 49   GLY H N   1 
ATOM   2170 C CA  . GLY B 1 49  ? 7.384   19.071  3.815   1.00 19.59 ? 49   GLY H CA  1 
ATOM   2171 C C   . GLY B 1 49  ? 8.546   18.651  4.665   1.00 18.66 ? 49   GLY H C   1 
ATOM   2172 O O   . GLY B 1 49  ? 8.997   19.469  5.510   1.00 18.28 ? 49   GLY H O   1 
ATOM   2173 N N   . TYR B 1 50  ? 9.045   17.445  4.431   1.00 18.24 ? 50   TYR H N   1 
ATOM   2174 C CA  . TYR B 1 50  ? 10.312  16.998  5.008   1.00 18.17 ? 50   TYR H CA  1 
ATOM   2175 C C   . TYR B 1 50  ? 11.193  16.385  3.926   1.00 18.74 ? 50   TYR H C   1 
ATOM   2176 O O   . TYR B 1 50  ? 10.689  15.867  2.933   1.00 19.10 ? 50   TYR H O   1 
ATOM   2177 C CB  . TYR B 1 50  ? 10.068  16.030  6.181   1.00 18.34 ? 50   TYR H CB  1 
ATOM   2178 C CG  . TYR B 1 50  ? 9.599   14.646  5.828   1.00 17.83 ? 50   TYR H CG  1 
ATOM   2179 C CD1 . TYR B 1 50  ? 10.439  13.690  5.272   1.00 17.84 ? 50   TYR H CD1 1 
ATOM   2180 C CD2 . TYR B 1 50  ? 8.295   14.265  6.097   1.00 18.33 ? 50   TYR H CD2 1 
ATOM   2181 C CE1 . TYR B 1 50  ? 9.993   12.411  4.982   1.00 18.10 ? 50   TYR H CE1 1 
ATOM   2182 C CE2 . TYR B 1 50  ? 7.836   12.995  5.804   1.00 17.90 ? 50   TYR H CE2 1 
ATOM   2183 C CZ  . TYR B 1 50  ? 8.684   12.048  5.256   1.00 18.36 ? 50   TYR H CZ  1 
ATOM   2184 O OH  . TYR B 1 50  ? 8.230   10.782  4.937   1.00 18.69 ? 50   TYR H OH  1 
ATOM   2185 N N   . ILE B 1 51  ? 12.475  16.370  4.217   1.00 18.17 ? 51   ILE H N   1 
ATOM   2186 C CA  . ILE B 1 51  ? 13.461  15.504  3.536   1.00 18.76 ? 51   ILE H CA  1 
ATOM   2187 C C   . ILE B 1 51  ? 14.151  14.629  4.592   1.00 18.62 ? 51   ILE H C   1 
ATOM   2188 O O   . ILE B 1 51  ? 14.640  15.142  5.654   1.00 19.10 ? 51   ILE H O   1 
ATOM   2189 C CB  . ILE B 1 51  ? 14.444  16.354  2.740   1.00 18.60 ? 51   ILE H CB  1 
ATOM   2190 C CG1 . ILE B 1 51  ? 15.413  15.446  2.014   1.00 19.37 ? 51   ILE H CG1 1 
ATOM   2191 C CG2 . ILE B 1 51  ? 15.135  17.397  3.575   1.00 19.31 ? 51   ILE H CG2 1 
ATOM   2192 C CD1 . ILE B 1 51  ? 16.082  16.110  0.793   1.00 19.88 ? 51   ILE H CD1 1 
ATOM   2193 N N   . SER B 1 52  ? 14.176  13.332  4.307   1.00 18.12 ? 52   SER H N   1 
ATOM   2194 C CA  . SER B 1 52  ? 14.821  12.299  5.134   1.00 19.13 ? 52   SER H CA  1 
ATOM   2195 C C   . SER B 1 52  ? 16.117  11.886  4.449   1.00 19.59 ? 52   SER H C   1 
ATOM   2196 O O   . SER B 1 52  ? 16.070  11.105  3.514   1.00 20.08 ? 52   SER H O   1 
ATOM   2197 C CB  . SER B 1 52  ? 13.886  11.192  5.335   1.00 19.18 ? 52   SER H CB  1 
ATOM   2198 O OG  . SER B 1 52  ? 14.423  10.213  6.203   1.00 19.52 ? 52   SER H OG  1 
ATOM   2199 N N   . PRO B 1 53  ? 17.265  12.471  4.814   1.00 21.37 ? 53   PRO H N   1 
ATOM   2200 C CA  . PRO B 1 53  ? 18.501  12.247  4.058   1.00 23.04 ? 53   PRO H CA  1 
ATOM   2201 C C   . PRO B 1 53  ? 19.035  10.820  4.127   1.00 24.24 ? 53   PRO H C   1 
ATOM   2202 O O   . PRO B 1 53  ? 19.708  10.414  3.178   1.00 26.41 ? 53   PRO H O   1 
ATOM   2203 C CB  . PRO B 1 53  ? 19.541  13.179  4.633   1.00 24.31 ? 53   PRO H CB  1 
ATOM   2204 C CG  . PRO B 1 53  ? 18.879  13.891  5.784   1.00 23.96 ? 53   PRO H CG  1 
ATOM   2205 C CD  . PRO B 1 53  ? 17.451  13.408  5.930   1.00 22.01 ? 53   PRO H CD  1 
ATOM   2206 N N   . GLY B 1 54  ? 18.714  10.069  5.193   1.00 23.18 ? 54   GLY H N   1 
ATOM   2207 C CA  . GLY B 1 54  ? 19.205  8.681   5.364   1.00 24.13 ? 54   GLY H CA  1 
ATOM   2208 C C   . GLY B 1 54  ? 18.621  7.713   4.359   1.00 24.29 ? 54   GLY H C   1 
ATOM   2209 O O   . GLY B 1 54  ? 19.277  6.713   4.056   1.00 24.54 ? 54   GLY H O   1 
ATOM   2210 N N   . ASN B 1 55  ? 17.404  7.965   3.865   1.00 22.41 ? 55   ASN H N   1 
ATOM   2211 C CA  . ASN B 1 55  ? 16.725  7.019   2.953   1.00 23.20 ? 55   ASN H CA  1 
ATOM   2212 C C   . ASN B 1 55  ? 16.221  7.785   1.709   1.00 23.37 ? 55   ASN H C   1 
ATOM   2213 O O   . ASN B 1 55  ? 15.471  7.177   0.967   1.00 24.04 ? 55   ASN H O   1 
ATOM   2214 C CB  . ASN B 1 55  ? 15.639  6.236   3.709   1.00 22.14 ? 55   ASN H CB  1 
ATOM   2215 C CG  . ASN B 1 55  ? 14.496  7.082   4.254   1.00 21.66 ? 55   ASN H CG  1 
ATOM   2216 O OD1 . ASN B 1 55  ? 13.459  6.571   4.727   1.00 22.85 ? 55   ASN H OD1 1 
ATOM   2217 N ND2 . ASN B 1 55  ? 14.624  8.376   4.206   1.00 21.00 ? 55   ASN H ND2 1 
ATOM   2218 N N   . ASP B 1 56  ? 16.634  9.038   1.511   1.00 24.63 ? 56   ASP H N   1 
ATOM   2219 C CA  . ASP B 1 56  ? 16.250  9.910   0.364   1.00 26.57 ? 56   ASP H CA  1 
ATOM   2220 C C   . ASP B 1 56  ? 14.735  9.992   0.198   1.00 26.40 ? 56   ASP H C   1 
ATOM   2221 O O   . ASP B 1 56  ? 14.256  10.125  -0.931  1.00 28.71 ? 56   ASP H O   1 
ATOM   2222 C CB  . ASP B 1 56  ? 16.844  9.363   -0.928  1.00 29.03 ? 56   ASP H CB  1 
ATOM   2223 C CG  . ASP B 1 56  ? 18.362  9.329   -0.868  1.00 32.07 ? 56   ASP H CG  1 
ATOM   2224 O OD1 . ASP B 1 56  ? 18.938  10.102  -0.106  1.00 33.19 ? 56   ASP H OD1 1 
ATOM   2225 O OD2 . ASP B 1 56  ? 18.956  8.517   -1.583  1.00 39.05 ? 56   ASP H OD2 1 
ATOM   2226 N N   . ASP B 1 57  A 13.979  9.975   1.274   1.00 24.31 ? 56   ASP H N   1 
ATOM   2227 C CA  . ASP B 1 57  A 12.502  10.094  1.241   1.00 23.85 ? 56   ASP H CA  1 
ATOM   2228 C C   . ASP B 1 57  A 12.146  11.584  1.332   1.00 23.91 ? 56   ASP H C   1 
ATOM   2229 O O   . ASP B 1 57  A 12.639  12.246  2.283   1.00 24.17 ? 56   ASP H O   1 
ATOM   2230 C CB  . ASP B 1 57  A 11.956  9.258   2.401   1.00 23.32 ? 56   ASP H CB  1 
ATOM   2231 C CG  . ASP B 1 57  A 10.473  9.387   2.619   1.00 24.32 ? 56   ASP H CG  1 
ATOM   2232 O OD1 . ASP B 1 57  A 9.747   9.598   1.609   1.00 23.29 ? 56   ASP H OD1 1 
ATOM   2233 O OD2 . ASP B 1 57  A 10.039  9.322   3.800   1.00 21.60 ? 56   ASP H OD2 1 
ATOM   2234 N N   . ILE B 1 58  ? 11.322  12.126  0.424   1.00 22.81 ? 57   ILE H N   1 
ATOM   2235 C CA  . ILE B 1 58  ? 10.929  13.555  0.442   1.00 22.45 ? 57   ILE H CA  1 
ATOM   2236 C C   . ILE B 1 58  ? 9.415   13.560  0.402   1.00 22.52 ? 57   ILE H C   1 
ATOM   2237 O O   . ILE B 1 58  ? 8.822   12.789  -0.365  1.00 22.13 ? 57   ILE H O   1 
ATOM   2238 C CB  . ILE B 1 58  ? 11.561  14.373  -0.702  1.00 22.69 ? 57   ILE H CB  1 
ATOM   2239 C CG1 . ILE B 1 58  ? 13.077  14.286  -0.703  1.00 23.85 ? 57   ILE H CG1 1 
ATOM   2240 C CG2 . ILE B 1 58  ? 11.133  15.818  -0.680  1.00 21.62 ? 57   ILE H CG2 1 
ATOM   2241 C CD1 . ILE B 1 58  ? 13.731  14.855  -1.944  1.00 24.45 ? 57   ILE H CD1 1 
ATOM   2242 N N   . LYS B 1 59  ? 8.803   14.314  1.292   1.00 21.21 ? 58   LYS H N   1 
ATOM   2243 C CA  . LYS B 1 59  ? 7.341   14.381  1.308   1.00 21.66 ? 58   LYS H CA  1 
ATOM   2244 C C   . LYS B 1 59  ? 6.945   15.836  1.383   1.00 20.79 ? 58   LYS H C   1 
ATOM   2245 O O   . LYS B 1 59  ? 7.456   16.543  2.292   1.00 20.10 ? 58   LYS H O   1 
ATOM   2246 C CB  . LYS B 1 59  ? 6.736   13.565  2.445   1.00 22.95 ? 58   LYS H CB  1 
ATOM   2247 C CG  . LYS B 1 59  ? 5.221   13.563  2.443   1.00 26.86 ? 58   LYS H CG  1 
ATOM   2248 C CD  . LYS B 1 59  ? 4.645   12.494  3.373   1.00 29.82 ? 58   LYS H CD  1 
ATOM   2249 C CE  . LYS B 1 59  ? 3.900   11.406  2.623   1.00 34.08 ? 58   LYS H CE  1 
ATOM   2250 N NZ  . LYS B 1 59  ? 4.756   10.244  2.346   1.00 35.81 ? 58   LYS H NZ  1 
ATOM   2251 N N   . TYR B 1 60  ? 6.022   16.245  0.503   1.00 19.39 ? 59   TYR H N   1 
ATOM   2252 C CA  . TYR B 1 60  ? 5.505   17.621  0.446   1.00 19.02 ? 59   TYR H CA  1 
ATOM   2253 C C   . TYR B 1 60  ? 4.076   17.642  0.970   1.00 19.02 ? 59   TYR H C   1 
ATOM   2254 O O   . TYR B 1 60  ? 3.313   16.681  0.724   1.00 19.31 ? 59   TYR H O   1 
ATOM   2255 C CB  . TYR B 1 60  ? 5.511   18.197  -0.975  1.00 19.33 ? 59   TYR H CB  1 
ATOM   2256 C CG  . TYR B 1 60  ? 6.910   18.327  -1.535  1.00 18.48 ? 59   TYR H CG  1 
ATOM   2257 C CD1 . TYR B 1 60  ? 7.503   17.295  -2.239  1.00 18.27 ? 59   TYR H CD1 1 
ATOM   2258 C CD2 . TYR B 1 60  ? 7.652   19.457  -1.280  1.00 18.88 ? 59   TYR H CD2 1 
ATOM   2259 C CE1 . TYR B 1 60  ? 8.782   17.446  -2.774  1.00 18.95 ? 59   TYR H CE1 1 
ATOM   2260 C CE2 . TYR B 1 60  ? 8.956   19.574  -1.728  1.00 18.83 ? 59   TYR H CE2 1 
ATOM   2261 C CZ  . TYR B 1 60  ? 9.504   18.594  -2.510  1.00 18.28 ? 59   TYR H CZ  1 
ATOM   2262 O OH  . TYR B 1 60  ? 10.803  18.726  -2.910  1.00 18.22 ? 59   TYR H OH  1 
ATOM   2263 N N   . ASN B 1 61  ? 3.753   18.764  1.600   1.00 19.10 ? 60   ASN H N   1 
ATOM   2264 C CA  . ASN B 1 61  ? 2.363   19.255  1.709   1.00 19.91 ? 60   ASN H CA  1 
ATOM   2265 C C   . ASN B 1 61  ? 1.890   19.561  0.271   1.00 21.05 ? 60   ASN H C   1 
ATOM   2266 O O   . ASN B 1 61  ? 2.589   20.378  -0.392  1.00 20.83 ? 60   ASN H O   1 
ATOM   2267 C CB  . ASN B 1 61  ? 2.321   20.506  2.576   1.00 19.88 ? 60   ASN H CB  1 
ATOM   2268 C CG  . ASN B 1 61  ? 0.920   20.937  2.921   1.00 20.25 ? 60   ASN H CG  1 
ATOM   2269 O OD1 . ASN B 1 61  ? -0.037  20.578  2.238   1.00 21.12 ? 60   ASN H OD1 1 
ATOM   2270 N ND2 . ASN B 1 61  ? 0.806   21.785  3.944   1.00 21.05 ? 60   ASN H ND2 1 
ATOM   2271 N N   . GLU B 1 62  ? 0.802   18.935  -0.190  1.00 22.75 ? 61   GLU H N   1 
ATOM   2272 C CA  . GLU B 1 62  ? 0.193   19.210  -1.523  1.00 24.93 ? 61   GLU H CA  1 
ATOM   2273 C C   . GLU B 1 62  ? 0.083   20.724  -1.767  1.00 25.46 ? 61   GLU H C   1 
ATOM   2274 O O   . GLU B 1 62  ? 0.344   21.166  -2.905  1.00 24.46 ? 61   GLU H O   1 
ATOM   2275 C CB  . GLU B 1 62  ? -1.182  18.539  -1.578  1.00 28.75 ? 61   GLU H CB  1 
ATOM   2276 C CG  . GLU B 1 62  ? -1.732  18.324  -2.973  1.00 31.58 ? 61   GLU H CG  1 
ATOM   2277 C CD  . GLU B 1 62  ? -0.932  17.400  -3.898  1.00 34.27 ? 61   GLU H CD  1 
ATOM   2278 O OE1 . GLU B 1 62  ? -0.264  16.460  -3.431  1.00 34.53 ? 61   GLU H OE1 1 
ATOM   2279 O OE2 . GLU B 1 62  ? -1.026  17.632  -5.105  1.00 42.42 ? 61   GLU H OE2 1 
ATOM   2280 N N   . LYS B 1 63  ? -0.255  21.505  -0.729  1.00 24.53 ? 62   LYS H N   1 
ATOM   2281 C CA  . LYS B 1 63  ? -0.418  22.968  -0.830  1.00 25.66 ? 62   LYS H CA  1 
ATOM   2282 C C   . LYS B 1 63  ? 0.868   23.614  -1.396  1.00 23.97 ? 62   LYS H C   1 
ATOM   2283 O O   . LYS B 1 63  ? 0.778   24.684  -1.997  1.00 22.58 ? 62   LYS H O   1 
ATOM   2284 C CB  . LYS B 1 63  ? -0.801  23.480  0.566   1.00 27.44 ? 62   LYS H CB  1 
ATOM   2285 C CG  . LYS B 1 63  ? -0.859  24.983  0.721   1.00 30.71 ? 62   LYS H CG  1 
ATOM   2286 C CD  . LYS B 1 63  ? -1.571  25.456  1.986   1.00 32.62 ? 62   LYS H CD  1 
ATOM   2287 C CE  . LYS B 1 63  ? -1.757  26.956  1.984   1.00 34.55 ? 62   LYS H CE  1 
ATOM   2288 N NZ  . LYS B 1 63  ? -2.740  27.367  3.002   1.00 37.34 ? 62   LYS H NZ  1 
ATOM   2289 N N   . PHE B 1 64  ? 2.048   23.079  -1.078  1.00 21.70 ? 63   PHE H N   1 
ATOM   2290 C CA  . PHE B 1 64  ? 3.349   23.708  -1.417  1.00 22.02 ? 63   PHE H CA  1 
ATOM   2291 C C   . PHE B 1 64  ? 3.992   23.047  -2.640  1.00 21.24 ? 63   PHE H C   1 
ATOM   2292 O O   . PHE B 1 64  ? 5.069   23.475  -3.021  1.00 20.13 ? 63   PHE H O   1 
ATOM   2293 C CB  . PHE B 1 64  ? 4.294   23.686  -0.217  1.00 20.98 ? 63   PHE H CB  1 
ATOM   2294 C CG  . PHE B 1 64  ? 3.940   24.729  0.817   1.00 22.17 ? 63   PHE H CG  1 
ATOM   2295 C CD1 . PHE B 1 64  ? 3.038   24.439  1.836   1.00 22.37 ? 63   PHE H CD1 1 
ATOM   2296 C CD2 . PHE B 1 64  ? 4.447   26.017  0.747   1.00 22.41 ? 63   PHE H CD2 1 
ATOM   2297 C CE1 . PHE B 1 64  ? 2.682   25.407  2.758   1.00 22.99 ? 63   PHE H CE1 1 
ATOM   2298 C CE2 . PHE B 1 64  ? 4.058   26.997  1.654   1.00 23.57 ? 63   PHE H CE2 1 
ATOM   2299 C CZ  . PHE B 1 64  ? 3.203   26.684  2.688   1.00 23.24 ? 63   PHE H CZ  1 
ATOM   2300 N N   . LYS B 1 65  ? 3.365   22.040  -3.230  1.00 21.99 ? 64   LYS H N   1 
ATOM   2301 C CA  . LYS B 1 65  ? 3.891   21.473  -4.506  1.00 21.96 ? 64   LYS H CA  1 
ATOM   2302 C C   . LYS B 1 65  ? 3.801   22.582  -5.576  1.00 21.46 ? 64   LYS H C   1 
ATOM   2303 O O   . LYS B 1 65  ? 2.753   23.247  -5.685  1.00 21.30 ? 64   LYS H O   1 
ATOM   2304 C CB  . LYS B 1 65  ? 3.145   20.216  -4.920  1.00 22.92 ? 64   LYS H CB  1 
ATOM   2305 C CG  . LYS B 1 65  ? 3.364   18.982  -4.041  1.00 24.60 ? 64   LYS H CG  1 
ATOM   2306 C CD  . LYS B 1 65  ? 2.817   17.717  -4.690  1.00 27.31 ? 64   LYS H CD  1 
ATOM   2307 C CE  . LYS B 1 65  ? 2.901   16.491  -3.809  1.00 30.22 ? 64   LYS H CE  1 
ATOM   2308 N NZ  . LYS B 1 65  ? 2.500   15.265  -4.537  1.00 31.93 ? 64   LYS H NZ  1 
ATOM   2309 N N   . GLY B 1 66  ? 4.874   22.784  -6.333  1.00 20.75 ? 65   GLY H N   1 
ATOM   2310 C CA  . GLY B 1 66  ? 4.934   23.871  -7.327  1.00 21.15 ? 65   GLY H CA  1 
ATOM   2311 C C   . GLY B 1 66  ? 5.450   25.161  -6.750  1.00 22.26 ? 65   GLY H C   1 
ATOM   2312 O O   . GLY B 1 66  ? 5.542   26.150  -7.499  1.00 23.08 ? 65   GLY H O   1 
ATOM   2313 N N   . LYS B 1 67  ? 5.769   25.183  -5.454  1.00 22.43 ? 66   LYS H N   1 
ATOM   2314 C CA  . LYS B 1 67  ? 6.250   26.376  -4.737  1.00 22.66 ? 66   LYS H CA  1 
ATOM   2315 C C   . LYS B 1 67  ? 7.561   26.066  -4.012  1.00 22.18 ? 66   LYS H C   1 
ATOM   2316 O O   . LYS B 1 67  ? 8.418   26.942  -3.941  1.00 21.85 ? 66   LYS H O   1 
ATOM   2317 C CB  . LYS B 1 67  ? 5.161   26.858  -3.786  1.00 23.68 ? 66   LYS H CB  1 
ATOM   2318 C CG  . LYS B 1 67  ? 5.587   28.018  -2.895  1.00 26.18 ? 66   LYS H CG  1 
ATOM   2319 C CD  . LYS B 1 67  ? 5.925   29.280  -3.718  1.00 26.29 ? 66   LYS H CD  1 
ATOM   2320 C CE  . LYS B 1 67  ? 4.762   29.790  -4.548  1.00 27.92 ? 66   LYS H CE  1 
ATOM   2321 N NZ  . LYS B 1 67  ? 4.974   31.218  -4.920  1.00 27.58 ? 66   LYS H NZ  1 
ATOM   2322 N N   . ALA B 1 68  ? 7.664   24.875  -3.406  1.00 22.57 ? 67   ALA H N   1 
ATOM   2323 C CA  . ALA B 1 68  ? 8.821   24.508  -2.565  1.00 23.33 ? 67   ALA H CA  1 
ATOM   2324 C C   . ALA B 1 68  ? 9.520   23.288  -3.150  1.00 22.74 ? 67   ALA H C   1 
ATOM   2325 O O   . ALA B 1 68  ? 8.840   22.360  -3.665  1.00 23.14 ? 67   ALA H O   1 
ATOM   2326 C CB  . ALA B 1 68  ? 8.381   24.257  -1.125  1.00 23.66 ? 67   ALA H CB  1 
ATOM   2327 N N   . THR B 1 69  ? 10.847  23.290  -3.073  1.00 23.40 ? 68   THR H N   1 
ATOM   2328 C CA  . THR B 1 69  ? 11.652  22.112  -3.461  1.00 22.88 ? 68   THR H CA  1 
ATOM   2329 C C   . THR B 1 69  ? 12.696  21.852  -2.390  1.00 21.97 ? 68   THR H C   1 
ATOM   2330 O O   . THR B 1 69  ? 13.507  22.737  -2.107  1.00 22.47 ? 68   THR H O   1 
ATOM   2331 C CB  . THR B 1 69  ? 12.324  22.243  -4.827  1.00 23.29 ? 68   THR H CB  1 
ATOM   2332 O OG1 . THR B 1 69  ? 11.376  22.488  -5.861  1.00 23.23 ? 68   THR H OG1 1 
ATOM   2333 C CG2 . THR B 1 69  ? 12.984  20.964  -5.241  1.00 23.38 ? 68   THR H CG2 1 
ATOM   2334 N N   . LEU B 1 70  ? 12.682  20.647  -1.823  1.00 22.02 ? 69   LEU H N   1 
ATOM   2335 C CA  . LEU B 1 70  ? 13.621  20.291  -0.729  1.00 21.20 ? 69   LEU H CA  1 
ATOM   2336 C C   . LEU B 1 70  ? 14.750  19.450  -1.290  1.00 21.10 ? 69   LEU H C   1 
ATOM   2337 O O   . LEU B 1 70  ? 14.485  18.438  -2.018  1.00 20.70 ? 69   LEU H O   1 
ATOM   2338 C CB  . LEU B 1 70  ? 12.873  19.521  0.371   1.00 21.60 ? 69   LEU H CB  1 
ATOM   2339 C CG  . LEU B 1 70  ? 11.609  20.205  0.885   1.00 21.34 ? 69   LEU H CG  1 
ATOM   2340 C CD1 . LEU B 1 70  ? 10.973  19.416  2.049   1.00 22.36 ? 69   LEU H CD1 1 
ATOM   2341 C CD2 . LEU B 1 70  ? 11.898  21.635  1.301   1.00 22.41 ? 69   LEU H CD2 1 
ATOM   2342 N N   . THR B 1 71  ? 15.968  19.787  -0.886  1.00 22.01 ? 70   THR H N   1 
ATOM   2343 C CA  . THR B 1 71  ? 17.147  18.948  -1.202  1.00 23.89 ? 70   THR H CA  1 
ATOM   2344 C C   . THR B 1 71  ? 18.010  18.853  0.049   1.00 23.98 ? 70   THR H C   1 
ATOM   2345 O O   . THR B 1 71  ? 17.716  19.560  1.039   1.00 24.29 ? 70   THR H O   1 
ATOM   2346 C CB  . THR B 1 71  ? 17.935  19.494  -2.397  1.00 23.88 ? 70   THR H CB  1 
ATOM   2347 O OG1 . THR B 1 71  ? 18.258  20.825  -2.015  1.00 25.07 ? 70   THR H OG1 1 
ATOM   2348 C CG2 . THR B 1 71  ? 17.161  19.382  -3.688  1.00 25.17 ? 70   THR H CG2 1 
ATOM   2349 N N   . ALA B 1 72  ? 19.046  18.028  -0.011  1.00 25.25 ? 71   ALA H N   1 
ATOM   2350 C CA  . ALA B 1 72  ? 20.027  17.893  1.084   1.00 26.92 ? 71   ALA H CA  1 
ATOM   2351 C C   . ALA B 1 72  ? 21.393  17.526  0.501   1.00 28.50 ? 71   ALA H C   1 
ATOM   2352 O O   . ALA B 1 72  ? 21.484  16.773  -0.520  1.00 28.92 ? 71   ALA H O   1 
ATOM   2353 C CB  . ALA B 1 72  ? 19.543  16.888  2.084   1.00 26.00 ? 71   ALA H CB  1 
ATOM   2354 N N   . ASP B 1 73  ? 22.427  18.087  1.082   1.00 28.74 ? 72   ASP H N   1 
ATOM   2355 C CA  . ASP B 1 73  ? 23.822  17.771  0.696   1.00 30.86 ? 72   ASP H CA  1 
ATOM   2356 C C   . ASP B 1 73  ? 24.410  16.961  1.856   1.00 31.29 ? 72   ASP H C   1 
ATOM   2357 O O   . ASP B 1 73  ? 24.688  17.549  2.905   1.00 29.70 ? 72   ASP H O   1 
ATOM   2358 C CB  . ASP B 1 73  ? 24.618  19.042  0.425   1.00 32.48 ? 72   ASP H CB  1 
ATOM   2359 C CG  . ASP B 1 73  ? 26.064  18.764  0.045   1.00 35.21 ? 72   ASP H CG  1 
ATOM   2360 O OD1 . ASP B 1 73  ? 26.548  17.683  0.362   1.00 36.87 ? 72   ASP H OD1 1 
ATOM   2361 O OD2 . ASP B 1 73  ? 26.648  19.613  -0.680  1.00 38.91 ? 72   ASP H OD2 1 
ATOM   2362 N N   . LYS B 1 74  ? 24.449  15.645  1.716   1.00 33.59 ? 73   LYS H N   1 
ATOM   2363 C CA  . LYS B 1 74  ? 24.932  14.740  2.785   1.00 37.36 ? 73   LYS H CA  1 
ATOM   2364 C C   . LYS B 1 74  ? 26.363  15.142  3.179   1.00 39.22 ? 73   LYS H C   1 
ATOM   2365 O O   . LYS B 1 74  ? 26.667  15.069  4.388   1.00 38.64 ? 73   LYS H O   1 
ATOM   2366 C CB  . LYS B 1 74  ? 24.753  13.296  2.306   1.00 40.10 ? 73   LYS H CB  1 
ATOM   2367 C CG  . LYS B 1 74  ? 23.378  12.720  2.640   1.00 42.69 ? 73   LYS H CG  1 
ATOM   2368 C CD  . LYS B 1 74  ? 22.501  12.362  1.475   1.00 44.82 ? 73   LYS H CD  1 
ATOM   2369 C CE  . LYS B 1 74  ? 22.460  10.863  1.240   1.00 47.00 ? 73   LYS H CE  1 
ATOM   2370 N NZ  . LYS B 1 74  ? 21.375  10.460  0.316   1.00 45.41 ? 73   LYS H NZ  1 
ATOM   2371 N N   . SER B 1 75  ? 27.190  15.593  2.228   1.00 40.59 ? 74   SER H N   1 
ATOM   2372 C CA  . SER B 1 75  ? 28.624  15.916  2.468   1.00 42.36 ? 74   SER H CA  1 
ATOM   2373 C C   . SER B 1 75  ? 28.760  17.044  3.495   1.00 41.44 ? 74   SER H C   1 
ATOM   2374 O O   . SER B 1 75  ? 29.758  17.055  4.236   1.00 42.73 ? 74   SER H O   1 
ATOM   2375 C CB  . SER B 1 75  ? 29.335  16.329  1.213   1.00 45.64 ? 74   SER H CB  1 
ATOM   2376 O OG  . SER B 1 75  ? 29.067  15.421  0.170   1.00 51.51 ? 74   SER H OG  1 
ATOM   2377 N N   . SER B 1 76  ? 27.820  17.989  3.513   1.00 36.25 ? 75   SER H N   1 
ATOM   2378 C CA  . SER B 1 76  ? 27.900  19.238  4.307   1.00 35.18 ? 75   SER H CA  1 
ATOM   2379 C C   . SER B 1 76  ? 26.848  19.215  5.416   1.00 32.72 ? 75   SER H C   1 
ATOM   2380 O O   . SER B 1 76  ? 26.738  20.218  6.137   1.00 31.68 ? 75   SER H O   1 
ATOM   2381 C CB  . SER B 1 76  ? 27.725  20.437  3.415   1.00 35.44 ? 75   SER H CB  1 
ATOM   2382 O OG  . SER B 1 76  ? 26.404  20.516  2.869   1.00 33.88 ? 75   SER H OG  1 
ATOM   2383 N N   . SER B 1 77  ? 26.091  18.120  5.514   1.00 31.43 ? 76   SER H N   1 
ATOM   2384 C CA  . SER B 1 77  ? 24.964  17.970  6.479   1.00 29.42 ? 76   SER H CA  1 
ATOM   2385 C C   . SER B 1 77  ? 24.076  19.206  6.375   1.00 27.29 ? 76   SER H C   1 
ATOM   2386 O O   . SER B 1 77  ? 23.731  19.796  7.407   1.00 26.28 ? 76   SER H O   1 
ATOM   2387 C CB  . SER B 1 77  ? 25.484  17.777  7.896   1.00 29.98 ? 76   SER H CB  1 
ATOM   2388 O OG  . SER B 1 77  ? 26.268  16.619  7.986   1.00 31.32 ? 76   SER H OG  1 
ATOM   2389 N N   . THR B 1 78  ? 23.740  19.620  5.158   1.00 26.19 ? 77   THR H N   1 
ATOM   2390 C CA  . THR B 1 78  ? 22.917  20.826  4.921   1.00 26.27 ? 77   THR H CA  1 
ATOM   2391 C C   . THR B 1 78  ? 21.644  20.434  4.163   1.00 24.98 ? 77   THR H C   1 
ATOM   2392 O O   . THR B 1 78  ? 21.730  19.754  3.152   1.00 24.23 ? 77   THR H O   1 
ATOM   2393 C CB  . THR B 1 78  ? 23.696  21.923  4.182   1.00 27.60 ? 77   THR H CB  1 
ATOM   2394 O OG1 . THR B 1 78  ? 24.854  22.188  4.964   1.00 29.71 ? 77   THR H OG1 1 
ATOM   2395 C CG2 . THR B 1 78  ? 22.903  23.205  4.031   1.00 28.50 ? 77   THR H CG2 1 
ATOM   2396 N N   . ALA B 1 79  ? 20.511  20.891  4.674   1.00 24.29 ? 78   ALA H N   1 
ATOM   2397 C CA  . ALA B 1 79  ? 19.195  20.799  4.040   1.00 23.79 ? 78   ALA H CA  1 
ATOM   2398 C C   . ALA B 1 79  ? 18.916  22.145  3.392   1.00 23.20 ? 78   ALA H C   1 
ATOM   2399 O O   . ALA B 1 79  ? 19.276  23.199  3.994   1.00 24.86 ? 78   ALA H O   1 
ATOM   2400 C CB  . ALA B 1 79  ? 18.155  20.426  5.075   1.00 23.52 ? 78   ALA H CB  1 
ATOM   2401 N N   . TYR B 1 80  ? 18.297  22.114  2.211   1.00 24.71 ? 79   TYR H N   1 
ATOM   2402 C CA  . TYR B 1 80  ? 17.934  23.318  1.439   1.00 23.33 ? 79   TYR H CA  1 
ATOM   2403 C C   . TYR B 1 80  ? 16.465  23.288  1.102   1.00 23.17 ? 79   TYR H C   1 
ATOM   2404 O O   . TYR B 1 80  ? 15.916  22.249  0.737   1.00 22.56 ? 79   TYR H O   1 
ATOM   2405 C CB  . TYR B 1 80  ? 18.749  23.401  0.163   1.00 24.16 ? 79   TYR H CB  1 
ATOM   2406 C CG  . TYR B 1 80  ? 20.230  23.487  0.344   1.00 25.01 ? 79   TYR H CG  1 
ATOM   2407 C CD1 . TYR B 1 80  ? 21.001  22.346  0.265   1.00 26.37 ? 79   TYR H CD1 1 
ATOM   2408 C CD2 . TYR B 1 80  ? 20.856  24.702  0.518   1.00 25.86 ? 79   TYR H CD2 1 
ATOM   2409 C CE1 . TYR B 1 80  ? 22.376  22.397  0.388   1.00 26.53 ? 79   TYR H CE1 1 
ATOM   2410 C CE2 . TYR B 1 80  ? 22.236  24.778  0.595   1.00 26.92 ? 79   TYR H CE2 1 
ATOM   2411 C CZ  . TYR B 1 80  ? 22.991  23.619  0.510   1.00 27.58 ? 79   TYR H CZ  1 
ATOM   2412 O OH  . TYR B 1 80  ? 24.348  23.655  0.635   1.00 29.73 ? 79   TYR H OH  1 
ATOM   2413 N N   . MET B 1 81  ? 15.881  24.474  1.116   1.00 23.67 ? 80   MET H N   1 
ATOM   2414 C CA  . MET B 1 81  ? 14.526  24.689  0.620   1.00 22.89 ? 80   MET H CA  1 
ATOM   2415 C C   . MET B 1 81  ? 14.579  25.821  -0.418  1.00 23.26 ? 80   MET H C   1 
ATOM   2416 O O   . MET B 1 81  ? 14.905  26.990  -0.054  1.00 22.81 ? 80   MET H O   1 
ATOM   2417 C CB  . MET B 1 81  ? 13.575  25.089  1.733   1.00 22.80 ? 80   MET H CB  1 
ATOM   2418 C CG  . MET B 1 81  ? 12.216  25.278  1.113   1.00 24.17 ? 80   MET H CG  1 
ATOM   2419 S SD  . MET B 1 81  ? 10.907  25.503  2.308   1.00 26.14 ? 80   MET H SD  1 
ATOM   2420 C CE  . MET B 1 81  ? 11.444  27.047  3.018   1.00 26.15 ? 80   MET H CE  1 
ATOM   2421 N N   . GLN B 1 82  ? 14.242  25.485  -1.643  1.00 23.14 ? 81   GLN H N   1 
ATOM   2422 C CA  . GLN B 1 82  ? 14.056  26.483  -2.713  1.00 25.37 ? 81   GLN H CA  1 
ATOM   2423 C C   . GLN B 1 82  ? 12.577  26.837  -2.796  1.00 23.93 ? 81   GLN H C   1 
ATOM   2424 O O   . GLN B 1 82  ? 11.755  25.917  -2.892  1.00 25.90 ? 81   GLN H O   1 
ATOM   2425 C CB  . GLN B 1 82  ? 14.603  25.938  -4.024  1.00 27.40 ? 81   GLN H CB  1 
ATOM   2426 C CG  . GLN B 1 82  ? 14.567  26.987  -5.123  1.00 31.93 ? 81   GLN H CG  1 
ATOM   2427 C CD  . GLN B 1 82  ? 15.608  26.786  -6.202  1.00 38.11 ? 81   GLN H CD  1 
ATOM   2428 O OE1 . GLN B 1 82  ? 16.737  26.365  -5.941  1.00 46.53 ? 81   GLN H OE1 1 
ATOM   2429 N NE2 . GLN B 1 82  ? 15.261  27.155  -7.423  1.00 41.56 ? 81   GLN H NE2 1 
ATOM   2430 N N   . LEU B 1 83  ? 12.269  28.121  -2.771  1.00 24.07 ? 82   LEU H N   1 
ATOM   2431 C CA  . LEU B 1 83  ? 10.905  28.636  -3.041  1.00 23.97 ? 82   LEU H CA  1 
ATOM   2432 C C   . LEU B 1 83  ? 10.929  29.351  -4.390  1.00 24.19 ? 82   LEU H C   1 
ATOM   2433 O O   . LEU B 1 83  ? 11.764  30.214  -4.553  1.00 25.40 ? 82   LEU H O   1 
ATOM   2434 C CB  . LEU B 1 83  ? 10.480  29.569  -1.920  1.00 24.24 ? 82   LEU H CB  1 
ATOM   2435 C CG  . LEU B 1 83  ? 10.407  28.903  -0.548  1.00 25.20 ? 82   LEU H CG  1 
ATOM   2436 C CD1 . LEU B 1 83  ? 10.276  29.940  0.555   1.00 26.32 ? 82   LEU H CD1 1 
ATOM   2437 C CD2 . LEU B 1 83  ? 9.244   27.927  -0.510  1.00 25.54 ? 82   LEU H CD2 1 
ATOM   2438 N N   . ASN B 1 84  A 9.978   29.051  -5.262  1.00 24.05 ? 82   ASN H N   1 
ATOM   2439 C CA  . ASN B 1 84  A 10.007  29.546  -6.670  1.00 23.02 ? 82   ASN H CA  1 
ATOM   2440 C C   . ASN B 1 84  A 8.828   30.478  -6.899  1.00 23.20 ? 82   ASN H C   1 
ATOM   2441 O O   . ASN B 1 84  A 7.828   30.392  -6.142  1.00 22.70 ? 82   ASN H O   1 
ATOM   2442 C CB  . ASN B 1 84  A 10.032  28.418  -7.716  1.00 23.00 ? 82   ASN H CB  1 
ATOM   2443 C CG  . ASN B 1 84  A 8.808   27.531  -7.669  1.00 22.84 ? 82   ASN H CG  1 
ATOM   2444 O OD1 . ASN B 1 84  A 7.804   27.744  -8.372  1.00 21.92 ? 82   ASN H OD1 1 
ATOM   2445 N ND2 . ASN B 1 84  A 8.923   26.462  -6.903  1.00 21.88 ? 82   ASN H ND2 1 
ATOM   2446 N N   . SER B 1 85  B 8.903   31.318  -7.954  1.00 22.89 ? 82   SER H N   1 
ATOM   2447 C CA  . SER B 1 85  B 7.713   32.049  -8.439  1.00 23.96 ? 82   SER H CA  1 
ATOM   2448 C C   . SER B 1 85  B 7.144   32.917  -7.325  1.00 24.72 ? 82   SER H C   1 
ATOM   2449 O O   . SER B 1 85  B 5.935   32.920  -7.114  1.00 25.19 ? 82   SER H O   1 
ATOM   2450 C CB  . SER B 1 85  B 6.688   31.077  -8.993  1.00 23.51 ? 82   SER H CB  1 
ATOM   2451 O OG  . SER B 1 85  B 7.253   30.159  -9.926  1.00 23.56 ? 82   SER H OG  1 
ATOM   2452 N N   . LEU B 1 86  C 7.985   33.694  -6.665  1.00 25.95 ? 82   LEU H N   1 
ATOM   2453 C CA  . LEU B 1 86  C 7.643   34.301  -5.349  1.00 27.87 ? 82   LEU H CA  1 
ATOM   2454 C C   . LEU B 1 86  C 6.643   35.451  -5.492  1.00 29.38 ? 82   LEU H C   1 
ATOM   2455 O O   . LEU B 1 86  C 6.731   36.235  -6.459  1.00 30.21 ? 82   LEU H O   1 
ATOM   2456 C CB  . LEU B 1 86  C 8.921   34.741  -4.648  1.00 28.24 ? 82   LEU H CB  1 
ATOM   2457 C CG  . LEU B 1 86  C 9.859   33.623  -4.189  1.00 27.45 ? 82   LEU H CG  1 
ATOM   2458 C CD1 . LEU B 1 86  C 11.172  34.208  -3.712  1.00 27.90 ? 82   LEU H CD1 1 
ATOM   2459 C CD2 . LEU B 1 86  C 9.196   32.773  -3.106  1.00 27.56 ? 82   LEU H CD2 1 
ATOM   2460 N N   . THR B 1 87  ? 5.698   35.532  -4.556  1.00 29.98 ? 83   THR H N   1 
ATOM   2461 C CA  . THR B 1 87  ? 4.758   36.670  -4.384  1.00 30.62 ? 83   THR H CA  1 
ATOM   2462 C C   . THR B 1 87  ? 4.849   37.172  -2.943  1.00 32.64 ? 83   THR H C   1 
ATOM   2463 O O   . THR B 1 87  ? 5.484   36.496  -2.102  1.00 30.69 ? 83   THR H O   1 
ATOM   2464 C CB  . THR B 1 87  ? 3.331   36.227  -4.682  1.00 31.09 ? 83   THR H CB  1 
ATOM   2465 O OG1 . THR B 1 87  ? 2.900   35.386  -3.602  1.00 31.92 ? 83   THR H OG1 1 
ATOM   2466 C CG2 . THR B 1 87  ? 3.255   35.446  -5.981  1.00 30.31 ? 83   THR H CG2 1 
ATOM   2467 N N   . SER B 1 88  ? 4.186   38.285  -2.666  1.00 33.07 ? 84   SER H N   1 
ATOM   2468 C CA  . SER B 1 88  ? 4.037   38.807  -1.289  1.00 35.42 ? 84   SER H CA  1 
ATOM   2469 C C   . SER B 1 88  ? 3.495   37.710  -0.364  1.00 34.52 ? 84   SER H C   1 
ATOM   2470 O O   . SER B 1 88  ? 3.797   37.780  0.839   1.00 33.87 ? 84   SER H O   1 
ATOM   2471 C CB  . SER B 1 88  ? 3.159   40.020  -1.260  1.00 36.49 ? 84   SER H CB  1 
ATOM   2472 O OG  . SER B 1 88  ? 1.942   39.730  -1.928  1.00 36.75 ? 84   SER H OG  1 
ATOM   2473 N N   . GLU B 1 89  ? 2.673   36.789  -0.862  1.00 34.58 ? 85   GLU H N   1 
ATOM   2474 C CA  . GLU B 1 89  ? 2.066   35.726  -0.014  1.00 37.30 ? 85   GLU H CA  1 
ATOM   2475 C C   . GLU B 1 89  ? 3.154   34.768  0.492   1.00 34.16 ? 85   GLU H C   1 
ATOM   2476 O O   . GLU B 1 89  ? 2.851   34.064  1.436   1.00 36.85 ? 85   GLU H O   1 
ATOM   2477 C CB  . GLU B 1 89  ? 0.978   34.963  -0.759  1.00 41.25 ? 85   GLU H CB  1 
ATOM   2478 C CG  . GLU B 1 89  ? -0.293  35.767  -0.923  1.00 46.23 ? 85   GLU H CG  1 
ATOM   2479 C CD  . GLU B 1 89  ? -1.184  35.390  -2.099  1.00 51.60 ? 85   GLU H CD  1 
ATOM   2480 O OE1 . GLU B 1 89  ? -2.384  35.748  -2.032  1.00 57.84 ? 85   GLU H OE1 1 
ATOM   2481 O OE2 . GLU B 1 89  ? -0.693  34.758  -3.083  1.00 56.90 ? 85   GLU H OE2 1 
ATOM   2482 N N   . ASP B 1 90  ? 4.373   34.802  -0.060  1.00 31.31 ? 86   ASP H N   1 
ATOM   2483 C CA  . ASP B 1 90  ? 5.525   33.971  0.376   1.00 31.26 ? 86   ASP H CA  1 
ATOM   2484 C C   . ASP B 1 90  ? 6.355   34.674  1.464   1.00 31.16 ? 86   ASP H C   1 
ATOM   2485 O O   . ASP B 1 90  ? 7.193   33.990  2.101   1.00 28.36 ? 86   ASP H O   1 
ATOM   2486 C CB  . ASP B 1 90  ? 6.388   33.626  -0.834  1.00 31.49 ? 86   ASP H CB  1 
ATOM   2487 C CG  . ASP B 1 90  ? 5.626   32.757  -1.819  1.00 32.09 ? 86   ASP H CG  1 
ATOM   2488 O OD1 . ASP B 1 90  ? 5.072   31.741  -1.367  1.00 30.71 ? 86   ASP H OD1 1 
ATOM   2489 O OD2 . ASP B 1 90  ? 5.549   33.109  -3.029  1.00 29.04 ? 86   ASP H OD2 1 
ATOM   2490 N N   . SER B 1 91  ? 6.183   35.981  1.664   1.00 30.06 ? 87   SER H N   1 
ATOM   2491 C CA  . SER B 1 91  ? 6.795   36.728  2.776   1.00 31.50 ? 87   SER H CA  1 
ATOM   2492 C C   . SER B 1 91  ? 6.416   36.035  4.093   1.00 30.11 ? 87   SER H C   1 
ATOM   2493 O O   . SER B 1 91  ? 5.245   35.959  4.429   1.00 30.11 ? 87   SER H O   1 
ATOM   2494 C CB  . SER B 1 91  ? 6.395   38.186  2.750   1.00 32.32 ? 87   SER H CB  1 
ATOM   2495 O OG  . SER B 1 91  ? 6.893   38.789  1.562   1.00 33.30 ? 87   SER H OG  1 
ATOM   2496 N N   . ALA B 1 92  ? 7.407   35.587  4.831   1.00 30.87 ? 88   ALA H N   1 
ATOM   2497 C CA  . ALA B 1 92  ? 7.201   34.874  6.110   1.00 29.25 ? 88   ALA H CA  1 
ATOM   2498 C C   . ALA B 1 92  ? 8.553   34.644  6.755   1.00 29.81 ? 88   ALA H C   1 
ATOM   2499 O O   . ALA B 1 92  ? 9.607   34.930  6.133   1.00 28.19 ? 88   ALA H O   1 
ATOM   2500 C CB  . ALA B 1 92  ? 6.486   33.564  5.844   1.00 28.67 ? 88   ALA H CB  1 
ATOM   2501 N N   . VAL B 1 93  ? 8.520   34.011  7.931   1.00 28.64 ? 89   VAL H N   1 
ATOM   2502 C CA  . VAL B 1 93  ? 9.719   33.426  8.533   1.00 29.45 ? 89   VAL H CA  1 
ATOM   2503 C C   . VAL B 1 93  ? 9.606   31.930  8.257   1.00 27.94 ? 89   VAL H C   1 
ATOM   2504 O O   . VAL B 1 93  ? 8.500   31.396  8.399   1.00 28.00 ? 89   VAL H O   1 
ATOM   2505 C CB  . VAL B 1 93  ? 9.805   33.738  10.036  1.00 29.83 ? 89   VAL H CB  1 
ATOM   2506 C CG1 . VAL B 1 93  ? 11.009  33.067  10.658  1.00 29.76 ? 89   VAL H CG1 1 
ATOM   2507 C CG2 . VAL B 1 93  ? 9.870   35.229  10.286  1.00 31.25 ? 89   VAL H CG2 1 
ATOM   2508 N N   . TYR B 1 94  ? 10.676  31.348  7.743   1.00 26.68 ? 90   TYR H N   1 
ATOM   2509 C CA  . TYR B 1 94  ? 10.755  29.905  7.404   1.00 25.16 ? 90   TYR H CA  1 
ATOM   2510 C C   . TYR B 1 94  ? 11.713  29.251  8.388   1.00 24.34 ? 90   TYR H C   1 
ATOM   2511 O O   . TYR B 1 94  ? 12.884  29.687  8.565   1.00 24.64 ? 90   TYR H O   1 
ATOM   2512 C CB  . TYR B 1 94  ? 11.186  29.673  5.954   1.00 24.79 ? 90   TYR H CB  1 
ATOM   2513 C CG  . TYR B 1 94  ? 10.147  30.125  4.972   1.00 24.08 ? 90   TYR H CG  1 
ATOM   2514 C CD1 . TYR B 1 94  ? 9.124   29.300  4.564   1.00 23.70 ? 90   TYR H CD1 1 
ATOM   2515 C CD2 . TYR B 1 94  ? 10.150  31.431  4.512   1.00 25.41 ? 90   TYR H CD2 1 
ATOM   2516 C CE1 . TYR B 1 94  ? 8.151   29.750  3.677   1.00 23.89 ? 90   TYR H CE1 1 
ATOM   2517 C CE2 . TYR B 1 94  ? 9.201   31.885  3.609   1.00 25.14 ? 90   TYR H CE2 1 
ATOM   2518 C CZ  . TYR B 1 94  ? 8.171   31.053  3.213   1.00 24.84 ? 90   TYR H CZ  1 
ATOM   2519 O OH  . TYR B 1 94  ? 7.198   31.482  2.349   1.00 24.58 ? 90   TYR H OH  1 
ATOM   2520 N N   . PHE B 1 95  ? 11.239  28.164  9.003   1.00 23.52 ? 91   PHE H N   1 
ATOM   2521 C CA  . PHE B 1 95  ? 12.045  27.377  9.948   1.00 22.96 ? 91   PHE H CA  1 
ATOM   2522 C C   . PHE B 1 95  ? 12.360  26.016  9.356   1.00 22.27 ? 91   PHE H C   1 
ATOM   2523 O O   . PHE B 1 95  ? 11.466  25.388  8.748   1.00 22.89 ? 91   PHE H O   1 
ATOM   2524 C CB  . PHE B 1 95  ? 11.262  27.214  11.250  1.00 22.33 ? 91   PHE H CB  1 
ATOM   2525 C CG  . PHE B 1 95  ? 11.081  28.473  12.043  1.00 22.14 ? 91   PHE H CG  1 
ATOM   2526 C CD1 . PHE B 1 95  ? 12.118  28.926  12.847  1.00 22.81 ? 91   PHE H CD1 1 
ATOM   2527 C CD2 . PHE B 1 95  ? 9.917   29.234  11.950  1.00 21.96 ? 91   PHE H CD2 1 
ATOM   2528 C CE1 . PHE B 1 95  ? 11.980  30.097  13.583  1.00 23.12 ? 91   PHE H CE1 1 
ATOM   2529 C CE2 . PHE B 1 95  ? 9.789   30.401  12.692  1.00 23.40 ? 91   PHE H CE2 1 
ATOM   2530 C CZ  . PHE B 1 95  ? 10.793  30.792  13.558  1.00 22.83 ? 91   PHE H CZ  1 
ATOM   2531 N N   . CYS B 1 96  ? 13.580  25.551  9.579   1.00 22.76 ? 92   CYS H N   1 
ATOM   2532 C CA  . CYS B 1 96  ? 13.857  24.113  9.493   1.00 23.01 ? 92   CYS H CA  1 
ATOM   2533 C C   . CYS B 1 96  ? 13.811  23.539  10.904  1.00 22.94 ? 92   CYS H C   1 
ATOM   2534 O O   . CYS B 1 96  ? 14.033  24.275  11.890  1.00 22.61 ? 92   CYS H O   1 
ATOM   2535 C CB  . CYS B 1 96  ? 15.170  23.802  8.785   1.00 25.55 ? 92   CYS H CB  1 
ATOM   2536 S SG  . CYS B 1 96  ? 16.583  24.371  9.746   1.00 27.66 ? 92   CYS H SG  1 
ATOM   2537 N N   . LYS B 1 97  ? 13.495  22.257  10.997  1.00 22.01 ? 93   LYS H N   1 
ATOM   2538 C CA  . LYS B 1 97  ? 13.392  21.617  12.312  1.00 23.04 ? 93   LYS H CA  1 
ATOM   2539 C C   . LYS B 1 97  ? 13.589  20.127  12.154  1.00 21.22 ? 93   LYS H C   1 
ATOM   2540 O O   . LYS B 1 97  ? 13.239  19.563  11.101  1.00 19.86 ? 93   LYS H O   1 
ATOM   2541 C CB  . LYS B 1 97  ? 12.038  22.120  12.806  1.00 25.15 ? 93   LYS H CB  1 
ATOM   2542 C CG  . LYS B 1 97  ? 11.286  21.242  13.710  1.00 29.55 ? 93   LYS H CG  1 
ATOM   2543 C CD  . LYS B 1 97  ? 10.542  20.024  13.248  1.00 26.69 ? 93   LYS H CD  1 
ATOM   2544 C CE  . LYS B 1 97  ? 9.915   19.787  14.601  1.00 25.42 ? 93   LYS H CE  1 
ATOM   2545 N NZ  . LYS B 1 97  ? 10.009  18.405  15.070  1.00 26.92 ? 93   LYS H NZ  1 
ATOM   2546 N N   . ARG B 1 98  ? 13.989  19.502  13.261  1.00 20.80 ? 94   ARG H N   1 
ATOM   2547 C CA  . ARG B 1 98  ? 14.379  18.090  13.230  1.00 20.02 ? 94   ARG H CA  1 
ATOM   2548 C C   . ARG B 1 98  ? 13.228  17.211  13.723  1.00 19.15 ? 94   ARG H C   1 
ATOM   2549 O O   . ARG B 1 98  ? 12.614  17.554  14.671  1.00 17.33 ? 94   ARG H O   1 
ATOM   2550 C CB  . ARG B 1 98  ? 15.612  17.897  14.100  1.00 19.94 ? 94   ARG H CB  1 
ATOM   2551 C CG  . ARG B 1 98  ? 16.223  16.534  13.948  1.00 21.01 ? 94   ARG H CG  1 
ATOM   2552 C CD  . ARG B 1 98  ? 17.433  16.434  14.833  1.00 21.55 ? 94   ARG H CD  1 
ATOM   2553 N NE  . ARG B 1 98  ? 17.227  16.521  16.279  1.00 21.06 ? 94   ARG H NE  1 
ATOM   2554 C CZ  . ARG B 1 98  ? 18.094  16.056  17.171  1.00 22.25 ? 94   ARG H CZ  1 
ATOM   2555 N NH1 . ARG B 1 98  ? 19.237  15.506  16.767  1.00 21.97 ? 94   ARG H NH1 1 
ATOM   2556 N NH2 . ARG B 1 98  ? 17.808  16.118  18.466  1.00 22.15 ? 94   ARG H NH2 1 
ATOM   2557 N N   . SER B 1 99  ? 12.930  16.163  12.966  1.00 17.73 ? 95   SER H N   1 
ATOM   2558 C CA  . SER B 1 99  ? 12.054  15.038  13.372  1.00 17.55 ? 95   SER H CA  1 
ATOM   2559 C C   . SER B 1 99  ? 10.586  15.437  13.515  1.00 16.79 ? 95   SER H C   1 
ATOM   2560 O O   . SER B 1 99  ? 10.169  16.508  13.092  1.00 16.61 ? 95   SER H O   1 
ATOM   2561 C CB  . SER B 1 99  ? 12.562  14.427  14.673  1.00 17.64 ? 95   SER H CB  1 
ATOM   2562 O OG  . SER B 1 99  ? 12.063  13.101  14.820  1.00 17.35 ? 95   SER H OG  1 
ATOM   2563 N N   . LEU B 1 100 ? 9.830   14.514  14.065  1.00 17.46 ? 96   LEU H N   1 
ATOM   2564 C CA  . LEU B 1 100 ? 8.424   14.709  14.475  1.00 17.63 ? 96   LEU H CA  1 
ATOM   2565 C C   . LEU B 1 100 ? 8.474   15.273  15.882  1.00 18.31 ? 96   LEU H C   1 
ATOM   2566 O O   . LEU B 1 100 ? 9.528   15.254  16.524  1.00 17.45 ? 96   LEU H O   1 
ATOM   2567 C CB  . LEU B 1 100 ? 7.701   13.365  14.411  1.00 17.94 ? 96   LEU H CB  1 
ATOM   2568 C CG  . LEU B 1 100 ? 7.407   12.856  12.981  1.00 18.17 ? 96   LEU H CG  1 
ATOM   2569 C CD1 . LEU B 1 100 ? 6.848   11.442  13.016  1.00 18.20 ? 96   LEU H CD1 1 
ATOM   2570 C CD2 . LEU B 1 100 ? 6.492   13.790  12.200  1.00 18.51 ? 96   LEU H CD2 1 
ATOM   2571 N N   . PRO B 1 101 ? 7.344   15.751  16.405  1.00 18.54 ? 97   PRO H N   1 
ATOM   2572 C CA  . PRO B 1 101 ? 7.255   16.161  17.793  1.00 18.65 ? 97   PRO H CA  1 
ATOM   2573 C C   . PRO B 1 101 ? 7.624   14.974  18.688  1.00 18.85 ? 97   PRO H C   1 
ATOM   2574 O O   . PRO B 1 101 ? 7.211   13.839  18.452  1.00 18.50 ? 97   PRO H O   1 
ATOM   2575 C CB  . PRO B 1 101 ? 5.771   16.552  17.934  1.00 19.27 ? 97   PRO H CB  1 
ATOM   2576 C CG  . PRO B 1 101 ? 5.378   16.920  16.536  1.00 19.11 ? 97   PRO H CG  1 
ATOM   2577 C CD  . PRO B 1 101 ? 6.046   15.824  15.732  1.00 18.19 ? 97   PRO H CD  1 
ATOM   2578 N N   . GLY B 1 102 ? 8.492   15.231  19.650  1.00 17.90 ? 98   GLY H N   1 
ATOM   2579 C CA  . GLY B 1 102 ? 9.018   14.152  20.500  1.00 18.37 ? 98   GLY H CA  1 
ATOM   2580 C C   . GLY B 1 102 ? 10.422  14.506  20.918  1.00 18.41 ? 98   GLY H C   1 
ATOM   2581 O O   . GLY B 1 102 ? 10.784  15.678  20.846  1.00 18.19 ? 98   GLY H O   1 
ATOM   2582 N N   . THR B 1 103 ? 11.174  13.528  21.352  1.00 19.44 ? 99   THR H N   1 
ATOM   2583 C CA  . THR B 1 103 ? 12.421  13.826  22.069  1.00 20.66 ? 99   THR H CA  1 
ATOM   2584 C C   . THR B 1 103 ? 13.463  14.494  21.147  1.00 19.28 ? 99   THR H C   1 
ATOM   2585 O O   . THR B 1 103 ? 14.304  15.219  21.683  1.00 18.30 ? 99   THR H O   1 
ATOM   2586 C CB  . THR B 1 103 ? 12.921  12.591  22.819  1.00 25.28 ? 99   THR H CB  1 
ATOM   2587 O OG1 . THR B 1 103 ? 13.600  13.266  23.892  1.00 30.07 ? 99   THR H OG1 1 
ATOM   2588 C CG2 . THR B 1 103 ? 13.937  11.786  22.058  1.00 26.23 ? 99   THR H CG2 1 
ATOM   2589 N N   . PHE B 1 104 ? 13.357  14.346  19.826  1.00 18.41 ? 100  PHE H N   1 
ATOM   2590 C CA  . PHE B 1 104 ? 14.402  14.886  18.924  1.00 18.02 ? 100  PHE H CA  1 
ATOM   2591 C C   . PHE B 1 104 ? 14.011  16.267  18.415  1.00 19.09 ? 100  PHE H C   1 
ATOM   2592 O O   . PHE B 1 104 ? 14.758  16.820  17.584  1.00 19.70 ? 100  PHE H O   1 
ATOM   2593 C CB  . PHE B 1 104 ? 14.706  13.910  17.787  1.00 17.45 ? 100  PHE H CB  1 
ATOM   2594 C CG  . PHE B 1 104 ? 15.258  12.604  18.265  1.00 17.04 ? 100  PHE H CG  1 
ATOM   2595 C CD1 . PHE B 1 104 ? 16.584  12.498  18.659  1.00 17.37 ? 100  PHE H CD1 1 
ATOM   2596 C CD2 . PHE B 1 104 ? 14.461  11.467  18.317  1.00 17.08 ? 100  PHE H CD2 1 
ATOM   2597 C CE1 . PHE B 1 104 ? 17.093  11.290  19.123  1.00 17.42 ? 100  PHE H CE1 1 
ATOM   2598 C CE2 . PHE B 1 104 ? 14.967  10.269  18.807  1.00 17.20 ? 100  PHE H CE2 1 
ATOM   2599 C CZ  . PHE B 1 104 ? 16.286  10.179  19.179  1.00 16.94 ? 100  PHE H CZ  1 
ATOM   2600 N N   . ASP B 1 105 ? 12.842  16.763  18.800  1.00 18.85 ? 101  ASP H N   1 
ATOM   2601 C CA  . ASP B 1 105 ? 12.350  18.080  18.331  1.00 19.79 ? 101  ASP H CA  1 
ATOM   2602 C C   . ASP B 1 105 ? 13.433  19.151  18.575  1.00 19.79 ? 101  ASP H C   1 
ATOM   2603 O O   . ASP B 1 105 ? 13.970  19.278  19.686  1.00 19.28 ? 101  ASP H O   1 
ATOM   2604 C CB  . ASP B 1 105 ? 11.057  18.458  19.039  1.00 19.61 ? 101  ASP H CB  1 
ATOM   2605 C CG  . ASP B 1 105 ? 10.321  19.617  18.420  1.00 19.57 ? 101  ASP H CG  1 
ATOM   2606 O OD1 . ASP B 1 105 ? 9.405   19.337  17.655  1.00 20.71 ? 101  ASP H OD1 1 
ATOM   2607 O OD2 . ASP B 1 105 ? 10.583  20.748  18.810  1.00 19.94 ? 101  ASP H OD2 1 
ATOM   2608 N N   . TYR B 1 106 ? 13.786  19.900  17.531  1.00 20.25 ? 102  TYR H N   1 
ATOM   2609 C CA  . TYR B 1 106 ? 14.863  20.909  17.571  1.00 21.76 ? 102  TYR H CA  1 
ATOM   2610 C C   . TYR B 1 106 ? 14.675  21.796  16.347  1.00 21.41 ? 102  TYR H C   1 
ATOM   2611 O O   . TYR B 1 106 ? 14.327  21.264  15.308  1.00 21.55 ? 102  TYR H O   1 
ATOM   2612 C CB  . TYR B 1 106 ? 16.254  20.279  17.514  1.00 24.25 ? 102  TYR H CB  1 
ATOM   2613 C CG  . TYR B 1 106 ? 17.306  21.152  18.121  1.00 28.73 ? 102  TYR H CG  1 
ATOM   2614 C CD1 . TYR B 1 106 ? 17.691  20.949  19.443  1.00 33.19 ? 102  TYR H CD1 1 
ATOM   2615 C CD2 . TYR B 1 106 ? 17.880  22.193  17.413  1.00 33.47 ? 102  TYR H CD2 1 
ATOM   2616 C CE1 . TYR B 1 106 ? 18.661  21.741  20.031  1.00 37.38 ? 102  TYR H CE1 1 
ATOM   2617 C CE2 . TYR B 1 106 ? 18.838  23.007  18.002  1.00 36.95 ? 102  TYR H CE2 1 
ATOM   2618 C CZ  . TYR B 1 106 ? 19.204  22.789  19.318  1.00 39.49 ? 102  TYR H CZ  1 
ATOM   2619 O OH  . TYR B 1 106 ? 20.135  23.544  19.975  1.00 48.83 ? 102  TYR H OH  1 
ATOM   2620 N N   . TRP B 1 107 ? 14.793  23.092  16.515  1.00 21.68 ? 103  TRP H N   1 
ATOM   2621 C CA  . TRP B 1 107 ? 14.446  24.084  15.465  1.00 22.14 ? 103  TRP H CA  1 
ATOM   2622 C C   . TRP B 1 107 ? 15.642  24.956  15.100  1.00 23.52 ? 103  TRP H C   1 
ATOM   2623 O O   . TRP B 1 107 ? 16.459  25.310  15.981  1.00 24.17 ? 103  TRP H O   1 
ATOM   2624 C CB  . TRP B 1 107 ? 13.304  24.964  15.949  1.00 21.97 ? 103  TRP H CB  1 
ATOM   2625 C CG  . TRP B 1 107 ? 12.041  24.210  16.135  1.00 21.42 ? 103  TRP H CG  1 
ATOM   2626 C CD1 . TRP B 1 107 ? 11.746  23.299  17.127  1.00 20.87 ? 103  TRP H CD1 1 
ATOM   2627 C CD2 . TRP B 1 107 ? 10.847  24.411  15.393  1.00 20.93 ? 103  TRP H CD2 1 
ATOM   2628 N NE1 . TRP B 1 107 ? 10.483  22.825  16.957  1.00 20.75 ? 103  TRP H NE1 1 
ATOM   2629 C CE2 . TRP B 1 107 ? 9.891   23.520  15.916  1.00 21.49 ? 103  TRP H CE2 1 
ATOM   2630 C CE3 . TRP B 1 107 ? 10.492  25.229  14.315  1.00 21.58 ? 103  TRP H CE3 1 
ATOM   2631 C CZ2 . TRP B 1 107 ? 8.606   23.422  15.387  1.00 21.67 ? 103  TRP H CZ2 1 
ATOM   2632 C CZ3 . TRP B 1 107 ? 9.226   25.131  13.790  1.00 21.68 ? 103  TRP H CZ3 1 
ATOM   2633 C CH2 . TRP B 1 107 ? 8.291   24.239  14.315  1.00 22.53 ? 103  TRP H CH2 1 
ATOM   2634 N N   . GLY B 1 108 ? 15.734  25.322  13.817  1.00 23.02 ? 104  GLY H N   1 
ATOM   2635 C CA  . GLY B 1 108 ? 16.612  26.415  13.371  1.00 23.91 ? 104  GLY H CA  1 
ATOM   2636 C C   . GLY B 1 108 ? 16.130  27.736  13.925  1.00 25.18 ? 104  GLY H C   1 
ATOM   2637 O O   . GLY B 1 108 ? 14.959  27.800  14.413  1.00 24.13 ? 104  GLY H O   1 
ATOM   2638 N N   . GLN B 1 109 ? 16.935  28.791  13.768  1.00 26.05 ? 105  GLN H N   1 
ATOM   2639 C CA  . GLN B 1 109 ? 16.606  30.143  14.309  1.00 27.31 ? 105  GLN H CA  1 
ATOM   2640 C C   . GLN B 1 109 ? 15.616  30.854  13.371  1.00 27.43 ? 105  GLN H C   1 
ATOM   2641 O O   . GLN B 1 109 ? 15.057  31.871  13.776  1.00 26.77 ? 105  GLN H O   1 
ATOM   2642 C CB  . GLN B 1 109 ? 17.893  30.935  14.526  1.00 29.73 ? 105  GLN H CB  1 
ATOM   2643 C CG  . GLN B 1 109 ? 18.419  31.677  13.300  1.00 30.50 ? 105  GLN H CG  1 
ATOM   2644 C CD  . GLN B 1 109 ? 19.271  30.811  12.405  1.00 32.38 ? 105  GLN H CD  1 
ATOM   2645 O OE1 . GLN B 1 109 ? 19.210  29.579  12.419  1.00 32.34 ? 105  GLN H OE1 1 
ATOM   2646 N NE2 . GLN B 1 109 ? 20.107  31.453  11.607  1.00 33.36 ? 105  GLN H NE2 1 
ATOM   2647 N N   . GLY B 1 110 ? 15.358  30.308  12.205  1.00 27.00 ? 106  GLY H N   1 
ATOM   2648 C CA  . GLY B 1 110 ? 14.445  30.903  11.216  1.00 26.96 ? 106  GLY H CA  1 
ATOM   2649 C C   . GLY B 1 110 ? 15.169  31.828  10.235  1.00 27.12 ? 106  GLY H C   1 
ATOM   2650 O O   . GLY B 1 110 ? 16.237  32.370  10.566  1.00 27.55 ? 106  GLY H O   1 
ATOM   2651 N N   . THR B 1 111 ? 14.570  31.971  9.065   1.00 27.35 ? 107  THR H N   1 
ATOM   2652 C CA  . THR B 1 111 ? 15.013  32.830  7.939   1.00 28.25 ? 107  THR H CA  1 
ATOM   2653 C C   . THR B 1 111 ? 13.806  33.672  7.549   1.00 27.96 ? 107  THR H C   1 
ATOM   2654 O O   . THR B 1 111 ? 12.804  33.099  7.102   1.00 27.49 ? 107  THR H O   1 
ATOM   2655 C CB  . THR B 1 111 ? 15.576  31.992  6.794   1.00 27.77 ? 107  THR H CB  1 
ATOM   2656 O OG1 . THR B 1 111 ? 16.727  31.271  7.211   1.00 28.04 ? 107  THR H OG1 1 
ATOM   2657 C CG2 . THR B 1 111 ? 15.968  32.878  5.624   1.00 29.44 ? 107  THR H CG2 1 
ATOM   2658 N N   . THR B 1 112 ? 13.916  34.982  7.679   1.00 31.15 ? 108  THR H N   1 
ATOM   2659 C CA  . THR B 1 112 ? 12.891  35.927  7.173   1.00 33.09 ? 108  THR H CA  1 
ATOM   2660 C C   . THR B 1 112 ? 13.046  36.076  5.663   1.00 34.05 ? 108  THR H C   1 
ATOM   2661 O O   . THR B 1 112 ? 14.143  36.408  5.222   1.00 37.32 ? 108  THR H O   1 
ATOM   2662 C CB  . THR B 1 112 ? 12.987  37.299  7.849   1.00 35.63 ? 108  THR H CB  1 
ATOM   2663 O OG1 . THR B 1 112 ? 12.906  36.999  9.239   1.00 35.69 ? 108  THR H OG1 1 
ATOM   2664 C CG2 . THR B 1 112 ? 11.899  38.235  7.368   1.00 36.94 ? 108  THR H CG2 1 
ATOM   2665 N N   . LEU B 1 113 ? 11.986  35.819  4.920   1.00 33.48 ? 109  LEU H N   1 
ATOM   2666 C CA  . LEU B 1 113 ? 11.928  36.140  3.479   1.00 34.15 ? 109  LEU H CA  1 
ATOM   2667 C C   . LEU B 1 113 ? 10.975  37.318  3.323   1.00 33.55 ? 109  LEU H C   1 
ATOM   2668 O O   . LEU B 1 113 ? 9.829   37.213  3.750   1.00 31.16 ? 109  LEU H O   1 
ATOM   2669 C CB  . LEU B 1 113 ? 11.444  34.924  2.692   1.00 33.76 ? 109  LEU H CB  1 
ATOM   2670 C CG  . LEU B 1 113 ? 11.150  35.185  1.216   1.00 34.41 ? 109  LEU H CG  1 
ATOM   2671 C CD1 . LEU B 1 113 ? 12.424  35.593  0.510   1.00 34.17 ? 109  LEU H CD1 1 
ATOM   2672 C CD2 . LEU B 1 113 ? 10.513  33.975  0.562   1.00 33.80 ? 109  LEU H CD2 1 
ATOM   2673 N N   . THR B 1 114 ? 11.454  38.396  2.711   1.00 35.73 ? 110  THR H N   1 
ATOM   2674 C CA  . THR B 1 114 ? 10.597  39.529  2.298   1.00 36.11 ? 110  THR H CA  1 
ATOM   2675 C C   . THR B 1 114 ? 10.560  39.575  0.780   1.00 37.16 ? 110  THR H C   1 
ATOM   2676 O O   . THR B 1 114 ? 11.646  39.707  0.188   1.00 37.37 ? 110  THR H O   1 
ATOM   2677 C CB  . THR B 1 114 ? 11.160  40.859  2.802   1.00 38.49 ? 110  THR H CB  1 
ATOM   2678 O OG1 . THR B 1 114 ? 11.279  40.669  4.205   1.00 38.32 ? 110  THR H OG1 1 
ATOM   2679 C CG2 . THR B 1 114 ? 10.301  42.054  2.438   1.00 38.77 ? 110  THR H CG2 1 
ATOM   2680 N N   . VAL B 1 115 ? 9.364   39.449  0.209   1.00 36.76 ? 111  VAL H N   1 
ATOM   2681 C CA  . VAL B 1 115 ? 9.119   39.662  -1.243  1.00 39.73 ? 111  VAL H CA  1 
ATOM   2682 C C   . VAL B 1 115 ? 8.628   41.103  -1.410  1.00 43.08 ? 111  VAL H C   1 
ATOM   2683 O O   . VAL B 1 115 ? 7.563   41.419  -0.845  1.00 45.38 ? 111  VAL H O   1 
ATOM   2684 C CB  . VAL B 1 115 ? 8.141   38.615  -1.805  1.00 37.80 ? 111  VAL H CB  1 
ATOM   2685 C CG1 . VAL B 1 115 ? 7.965   38.754  -3.304  1.00 37.67 ? 111  VAL H CG1 1 
ATOM   2686 C CG2 . VAL B 1 115 ? 8.584   37.203  -1.441  1.00 36.72 ? 111  VAL H CG2 1 
ATOM   2687 N N   . SER B 1 116 ? 9.431   41.951  -2.072  1.00 48.17 ? 112  SER H N   1 
ATOM   2688 C CA  . SER B 1 116 ? 9.074   43.343  -2.480  1.00 50.89 ? 112  SER H CA  1 
ATOM   2689 C C   . SER B 1 116 ? 7.632   43.352  -2.989  1.00 51.55 ? 112  SER H C   1 
ATOM   2690 O O   . SER B 1 116 ? 6.827   44.058  -2.411  1.00 54.99 ? 112  SER H O   1 
ATOM   2691 C CB  . SER B 1 116 ? 10.000  43.861  -3.560  1.00 52.89 ? 112  SER H CB  1 
ATOM   2692 O OG  . SER B 1 116 ? 11.371  43.660  -3.220  1.00 55.43 ? 112  SER H OG  1 
ATOM   2693 N N   . GLY B 1 126 ? -4.569  34.534  -6.468  1.00 38.07 ? 122  GLY H N   1 
ATOM   2694 C CA  . GLY B 1 126 ? -4.867  33.111  -6.287  1.00 36.32 ? 122  GLY H CA  1 
ATOM   2695 C C   . GLY B 1 126 ? -3.831  32.222  -6.940  1.00 35.58 ? 122  GLY H C   1 
ATOM   2696 O O   . GLY B 1 126 ? -4.233  31.154  -7.406  1.00 40.90 ? 122  GLY H O   1 
ATOM   2697 N N   . GLY B 1 127 ? -2.562  32.636  -7.032  1.00 33.75 ? 123  GLY H N   1 
ATOM   2698 C CA  . GLY B 1 127 ? -1.488  31.763  -7.574  1.00 31.39 ? 123  GLY H CA  1 
ATOM   2699 C C   . GLY B 1 127 ? -0.922  30.801  -6.521  1.00 30.73 ? 123  GLY H C   1 
ATOM   2700 O O   . GLY B 1 127 ? -0.205  29.825  -6.890  1.00 30.19 ? 123  GLY H O   1 
ATOM   2701 N N   . GLY B 1 128 ? -1.203  31.051  -5.244  1.00 30.91 ? 124  GLY H N   1 
ATOM   2702 C CA  . GLY B 1 128 ? -0.728  30.162  -4.163  1.00 31.00 ? 124  GLY H CA  1 
ATOM   2703 C C   . GLY B 1 128 ? -1.492  28.857  -4.105  1.00 30.62 ? 124  GLY H C   1 
ATOM   2704 O O   . GLY B 1 128 ? -2.553  28.719  -4.752  1.00 31.47 ? 124  GLY H O   1 
ATOM   2705 N N   . GLY B 1 129 ? -0.940  27.887  -3.374  1.00 32.97 ? 125  GLY H N   1 
ATOM   2706 C CA  . GLY B 1 129 ? -1.565  26.575  -3.173  1.00 31.98 ? 125  GLY H CA  1 
ATOM   2707 C C   . GLY B 1 129 ? -2.707  26.746  -2.197  1.00 32.86 ? 125  GLY H C   1 
ATOM   2708 O O   . GLY B 1 129 ? -2.644  27.715  -1.414  1.00 33.21 ? 125  GLY H O   1 
ATOM   2709 N N   . SER B 1 130 ? -3.669  25.825  -2.201  1.00 32.42 ? 126  SER H N   1 
ATOM   2710 C CA  . SER B 1 130 ? -4.758  25.742  -1.188  1.00 33.64 ? 126  SER H CA  1 
ATOM   2711 C C   . SER B 1 130 ? -4.631  24.418  -0.437  1.00 33.34 ? 126  SER H C   1 
ATOM   2712 O O   . SER B 1 130 ? -3.991  23.506  -0.955  1.00 31.23 ? 126  SER H O   1 
ATOM   2713 C CB  . SER B 1 130 ? -6.092  25.857  -1.851  1.00 33.88 ? 126  SER H CB  1 
ATOM   2714 O OG  . SER B 1 130 ? -6.193  27.147  -2.433  1.00 39.26 ? 126  SER H OG  1 
ATOM   2715 N N   . SER B 1 131 ? -5.181  24.343  0.778   1.00 35.52 ? 127  SER H N   1 
ATOM   2716 C CA  . SER B 1 131 ? -5.309  23.079  1.545   1.00 35.81 ? 127  SER H CA  1 
ATOM   2717 C C   . SER B 1 131 ? -6.268  22.141  0.800   1.00 38.33 ? 127  SER H C   1 
ATOM   2718 O O   . SER B 1 131 ? -7.138  22.659  0.066   1.00 44.68 ? 127  SER H O   1 
ATOM   2719 C CB  . SER B 1 131 ? -5.789  23.358  2.963   1.00 36.05 ? 127  SER H CB  1 
ATOM   2720 O OG  . SER B 1 131 ? -4.974  24.326  3.628   1.00 34.76 ? 127  SER H OG  1 
ATOM   2721 N N   . GLY B 1 132 ? -6.123  20.827  0.985   1.00 37.17 ? 128  GLY H N   1 
ATOM   2722 C CA  . GLY B 1 132 ? -7.099  19.797  0.582   1.00 38.13 ? 128  GLY H CA  1 
ATOM   2723 C C   . GLY B 1 132 ? -8.341  19.837  1.460   1.00 38.70 ? 128  GLY H C   1 
ATOM   2724 O O   . GLY B 1 132 ? -8.226  20.118  2.659   1.00 34.79 ? 128  GLY H O   1 
ATOM   2725 N N   . SER B 1 133 ? -9.501  19.494  0.906   1.00 39.39 ? 129  SER H N   1 
ATOM   2726 C CA  . SER B 1 133 ? -10.761 19.378  1.681   1.00 41.71 ? 129  SER H CA  1 
ATOM   2727 C C   . SER B 1 133 ? -10.629 18.210  2.668   1.00 39.29 ? 129  SER H C   1 
ATOM   2728 O O   . SER B 1 133 ? -11.342 18.191  3.678   1.00 39.09 ? 129  SER H O   1 
ATOM   2729 C CB  . SER B 1 133 ? -11.946 19.216  0.761   1.00 42.54 ? 129  SER H CB  1 
ATOM   2730 O OG  . SER B 1 133 ? -11.822 18.005  0.023   1.00 44.01 ? 129  SER H OG  1 
ATOM   2731 N N   . SER B 1 134 ? -9.682  17.317  2.432   1.00 38.19 ? 130  SER H N   1 
ATOM   2732 C CA  . SER B 1 134 ? -9.399  16.114  3.253   1.00 36.83 ? 130  SER H CA  1 
ATOM   2733 C C   . SER B 1 134 ? -8.400  16.387  4.393   1.00 34.10 ? 130  SER H C   1 
ATOM   2734 O O   . SER B 1 134 ? -8.219  15.497  5.296   1.00 32.89 ? 130  SER H O   1 
ATOM   2735 C CB  . SER B 1 134 ? -8.862  15.063  2.349   1.00 42.22 ? 130  SER H CB  1 
ATOM   2736 O OG  . SER B 1 134 ? -8.508  13.933  3.108   1.00 45.50 ? 130  SER H OG  1 
ATOM   2737 N N   . ASP B 1 135 ? -7.706  17.520  4.359   1.00 30.64 ? 1001 ASP H N   1 
ATOM   2738 C CA  . ASP B 1 135 ? -6.700  17.840  5.415   1.00 27.68 ? 1001 ASP H CA  1 
ATOM   2739 C C   . ASP B 1 135 ? -7.352  17.994  6.792   1.00 26.85 ? 1001 ASP H C   1 
ATOM   2740 O O   . ASP B 1 135 ? -8.483  18.524  6.889   1.00 25.79 ? 1001 ASP H O   1 
ATOM   2741 C CB  . ASP B 1 135 ? -5.936  19.120  5.117   1.00 28.65 ? 1001 ASP H CB  1 
ATOM   2742 C CG  . ASP B 1 135 ? -5.128  19.034  3.837   1.00 29.06 ? 1001 ASP H CG  1 
ATOM   2743 O OD1 . ASP B 1 135 ? -4.604  20.097  3.435   1.00 31.02 ? 1001 ASP H OD1 1 
ATOM   2744 O OD2 . ASP B 1 135 ? -5.097  17.941  3.255   1.00 26.05 ? 1001 ASP H OD2 1 
ATOM   2745 N N   . VAL B 1 136 ? -6.652  17.590  7.872   1.00 24.58 ? 1002 VAL H N   1 
ATOM   2746 C CA  . VAL B 1 136 ? -7.179  17.855  9.237   1.00 23.66 ? 1002 VAL H CA  1 
ATOM   2747 C C   . VAL B 1 136 ? -7.054  19.354  9.514   1.00 23.27 ? 1002 VAL H C   1 
ATOM   2748 O O   . VAL B 1 136 ? -5.966  19.920  9.265   1.00 23.56 ? 1002 VAL H O   1 
ATOM   2749 C CB  . VAL B 1 136 ? -6.488  17.019  10.342  1.00 23.26 ? 1002 VAL H CB  1 
ATOM   2750 C CG1 . VAL B 1 136 ? -7.093  17.312  11.705  1.00 23.37 ? 1002 VAL H CG1 1 
ATOM   2751 C CG2 . VAL B 1 136 ? -6.522  15.545  10.062  1.00 23.15 ? 1002 VAL H CG2 1 
ATOM   2752 N N   . VAL B 1 137 ? -8.129  19.969  10.016  1.00 23.88 ? 1003 VAL H N   1 
ATOM   2753 C CA  . VAL B 1 137 ? -8.135  21.376  10.494  1.00 23.22 ? 1003 VAL H CA  1 
ATOM   2754 C C   . VAL B 1 137 ? -8.066  21.349  12.005  1.00 23.46 ? 1003 VAL H C   1 
ATOM   2755 O O   . VAL B 1 137 ? -8.909  20.675  12.668  1.00 23.84 ? 1003 VAL H O   1 
ATOM   2756 C CB  . VAL B 1 137 ? -9.359  22.152  9.986   1.00 24.18 ? 1003 VAL H CB  1 
ATOM   2757 C CG1 . VAL B 1 137 ? -9.476  23.539  10.575  1.00 24.93 ? 1003 VAL H CG1 1 
ATOM   2758 C CG2 . VAL B 1 137 ? -9.325  22.216  8.466   1.00 24.83 ? 1003 VAL H CG2 1 
ATOM   2759 N N   . MET B 1 138 ? -7.107  22.084  12.548  1.00 22.68 ? 1004 MET H N   1 
ATOM   2760 C CA  . MET B 1 138 ? -6.966  22.264  14.006  1.00 23.27 ? 1004 MET H CA  1 
ATOM   2761 C C   . MET B 1 138 ? -7.424  23.664  14.346  1.00 24.44 ? 1004 MET H C   1 
ATOM   2762 O O   . MET B 1 138 ? -6.883  24.632  13.763  1.00 26.41 ? 1004 MET H O   1 
ATOM   2763 C CB  . MET B 1 138 ? -5.506  22.042  14.425  1.00 22.89 ? 1004 MET H CB  1 
ATOM   2764 C CG  . MET B 1 138 ? -4.963  20.652  14.036  1.00 22.78 ? 1004 MET H CG  1 
ATOM   2765 S SD  . MET B 1 138 ? -5.770  19.275  14.877  1.00 23.18 ? 1004 MET H SD  1 
ATOM   2766 C CE  . MET B 1 138 ? -5.200  19.496  16.557  1.00 26.27 ? 1004 MET H CE  1 
ATOM   2767 N N   . THR B 1 139 ? -8.470  23.757  15.164  1.00 25.29 ? 1005 THR H N   1 
ATOM   2768 C CA  . THR B 1 139 ? -9.120  25.038  15.477  1.00 25.55 ? 1005 THR H CA  1 
ATOM   2769 C C   . THR B 1 139 ? -8.833  25.398  16.934  1.00 24.77 ? 1005 THR H C   1 
ATOM   2770 O O   . THR B 1 139 ? -9.276  24.691  17.846  1.00 23.90 ? 1005 THR H O   1 
ATOM   2771 C CB  . THR B 1 139 ? -10.635 24.992  15.233  1.00 26.93 ? 1005 THR H CB  1 
ATOM   2772 O OG1 . THR B 1 139 ? -10.800 24.679  13.859  1.00 27.63 ? 1005 THR H OG1 1 
ATOM   2773 C CG2 . THR B 1 139 ? -11.290 26.299  15.594  1.00 26.67 ? 1005 THR H CG2 1 
ATOM   2774 N N   . GLN B 1 140 ? -8.143  26.501  17.145  1.00 24.71 ? 1006 GLN H N   1 
ATOM   2775 C CA  . GLN B 1 140 ? -8.035  27.115  18.493  1.00 25.02 ? 1006 GLN H CA  1 
ATOM   2776 C C   . GLN B 1 140 ? -9.076  28.237  18.500  1.00 28.08 ? 1006 GLN H C   1 
ATOM   2777 O O   . GLN B 1 140 ? -8.870  29.245  17.807  1.00 30.97 ? 1006 GLN H O   1 
ATOM   2778 C CB  . GLN B 1 140 ? -6.609  27.604  18.724  1.00 22.49 ? 1006 GLN H CB  1 
ATOM   2779 C CG  . GLN B 1 140 ? -5.645  26.461  18.872  1.00 21.96 ? 1006 GLN H CG  1 
ATOM   2780 C CD  . GLN B 1 140 ? -4.212  26.909  18.989  1.00 21.42 ? 1006 GLN H CD  1 
ATOM   2781 O OE1 . GLN B 1 140 ? -3.386  26.616  18.138  1.00 19.03 ? 1006 GLN H OE1 1 
ATOM   2782 N NE2 . GLN B 1 140 ? -3.907  27.620  20.058  1.00 22.55 ? 1006 GLN H NE2 1 
ATOM   2783 N N   . SER B 1 141 ? -10.173 28.037  19.205  1.00 31.42 ? 1007 SER H N   1 
ATOM   2784 C CA  . SER B 1 141 ? -11.333 28.955  19.192  1.00 36.66 ? 1007 SER H CA  1 
ATOM   2785 C C   . SER B 1 141 ? -11.002 30.302  19.841  1.00 37.56 ? 1007 SER H C   1 
ATOM   2786 O O   . SER B 1 141 ? -11.599 31.300  19.347  1.00 39.37 ? 1007 SER H O   1 
ATOM   2787 C CB  . SER B 1 141 ? -12.542 28.288  19.763  1.00 38.98 ? 1007 SER H CB  1 
ATOM   2788 O OG  . SER B 1 141 ? -12.852 27.161  18.954  1.00 40.55 ? 1007 SER H OG  1 
ATOM   2789 N N   . HIS B 1 142 ? -9.994  30.396  20.729  1.00 36.42 ? 1008 HIS H N   1 
ATOM   2790 C CA  . HIS B 1 142 ? -9.579  31.706  21.300  1.00 36.05 ? 1008 HIS H CA  1 
ATOM   2791 C C   . HIS B 1 142 ? -8.241  32.147  20.718  1.00 32.58 ? 1008 HIS H C   1 
ATOM   2792 O O   . HIS B 1 142 ? -7.226  31.542  21.056  1.00 31.13 ? 1008 HIS H O   1 
ATOM   2793 C CB  . HIS B 1 142 ? -9.612  31.646  22.824  1.00 40.75 ? 1008 HIS H CB  1 
ATOM   2794 C CG  . HIS B 1 142 ? -10.958 31.251  23.332  1.00 46.59 ? 1008 HIS H CG  1 
ATOM   2795 N ND1 . HIS B 1 142 ? -12.136 31.654  22.717  1.00 50.76 ? 1008 HIS H ND1 1 
ATOM   2796 C CD2 . HIS B 1 142 ? -11.324 30.458  24.357  1.00 49.37 ? 1008 HIS H CD2 1 
ATOM   2797 C CE1 . HIS B 1 142 ? -13.168 31.141  23.350  1.00 52.38 ? 1008 HIS H CE1 1 
ATOM   2798 N NE2 . HIS B 1 142 ? -12.694 30.407  24.369  1.00 53.71 ? 1008 HIS H NE2 1 
ATOM   2799 N N   . LYS B 1 143 ? -8.232  33.224  19.924  1.00 30.23 ? 1009 LYS H N   1 
ATOM   2800 C CA  . LYS B 1 143 ? -6.975  33.803  19.393  1.00 30.53 ? 1009 LYS H CA  1 
ATOM   2801 C C   . LYS B 1 143 ? -6.258  34.573  20.506  1.00 27.56 ? 1009 LYS H C   1 
ATOM   2802 O O   . LYS B 1 143 ? -5.028  34.750  20.427  1.00 26.51 ? 1009 LYS H O   1 
ATOM   2803 C CB  . LYS B 1 143 ? -7.279  34.741  18.229  1.00 33.33 ? 1009 LYS H CB  1 
ATOM   2804 C CG  . LYS B 1 143 ? -8.032  34.056  17.099  1.00 37.87 ? 1009 LYS H CG  1 
ATOM   2805 C CD  . LYS B 1 143 ? -7.337  34.174  15.766  1.00 41.35 ? 1009 LYS H CD  1 
ATOM   2806 C CE  . LYS B 1 143 ? -7.738  33.090  14.785  1.00 42.00 ? 1009 LYS H CE  1 
ATOM   2807 N NZ  . LYS B 1 143 ? -6.565  32.292  14.363  1.00 41.94 ? 1009 LYS H NZ  1 
ATOM   2808 N N   . PHE B 1 144 ? -7.026  35.040  21.471  1.00 28.30 ? 1010 PHE H N   1 
ATOM   2809 C CA  . PHE B 1 144 ? -6.497  35.800  22.637  1.00 28.44 ? 1010 PHE H CA  1 
ATOM   2810 C C   . PHE B 1 144 ? -7.069  35.251  23.920  1.00 28.91 ? 1010 PHE H C   1 
ATOM   2811 O O   . PHE B 1 144 ? -8.300  35.010  23.979  1.00 28.87 ? 1010 PHE H O   1 
ATOM   2812 C CB  . PHE B 1 144 ? -6.894  37.266  22.572  1.00 30.40 ? 1010 PHE H CB  1 
ATOM   2813 C CG  . PHE B 1 144 ? -6.334  37.913  21.348  1.00 33.41 ? 1010 PHE H CG  1 
ATOM   2814 C CD1 . PHE B 1 144 ? -5.023  38.348  21.319  1.00 34.75 ? 1010 PHE H CD1 1 
ATOM   2815 C CD2 . PHE B 1 144 ? -7.116  38.036  20.209  1.00 36.10 ? 1010 PHE H CD2 1 
ATOM   2816 C CE1 . PHE B 1 144 ? -4.493  38.897  20.166  1.00 37.55 ? 1010 PHE H CE1 1 
ATOM   2817 C CE2 . PHE B 1 144 ? -6.594  38.620  19.066  1.00 37.01 ? 1010 PHE H CE2 1 
ATOM   2818 C CZ  . PHE B 1 144 ? -5.277  39.036  19.047  1.00 36.85 ? 1010 PHE H CZ  1 
ATOM   2819 N N   . MET B 1 145 ? -6.205  35.124  24.924  1.00 26.87 ? 1011 MET H N   1 
ATOM   2820 C CA  . MET B 1 145 ? -6.623  34.779  26.295  1.00 28.36 ? 1011 MET H CA  1 
ATOM   2821 C C   . MET B 1 145 ? -5.872  35.675  27.277  1.00 26.54 ? 1011 MET H C   1 
ATOM   2822 O O   . MET B 1 145 ? -4.698  35.925  27.060  1.00 25.30 ? 1011 MET H O   1 
ATOM   2823 C CB  . MET B 1 145 ? -6.356  33.304  26.597  1.00 28.51 ? 1011 MET H CB  1 
ATOM   2824 C CG  . MET B 1 145 ? -7.254  32.389  25.780  1.00 30.83 ? 1011 MET H CG  1 
ATOM   2825 S SD  . MET B 1 145 ? -7.168  30.630  26.308  1.00 33.46 ? 1011 MET H SD  1 
ATOM   2826 C CE  . MET B 1 145 ? -7.915  30.745  27.929  1.00 35.81 ? 1011 MET H CE  1 
ATOM   2827 N N   . SER B 1 146 ? -6.558  36.094  28.324  1.00 27.89 ? 1012 SER H N   1 
ATOM   2828 C CA  . SER B 1 146 ? -6.000  36.928  29.422  1.00 27.98 ? 1012 SER H CA  1 
ATOM   2829 C C   . SER B 1 146 ? -5.852  36.076  30.675  1.00 27.19 ? 1012 SER H C   1 
ATOM   2830 O O   . SER B 1 146 ? -6.784  35.361  30.975  1.00 25.73 ? 1012 SER H O   1 
ATOM   2831 C CB  . SER B 1 146 ? -6.872  38.121  29.695  1.00 30.38 ? 1012 SER H CB  1 
ATOM   2832 O OG  . SER B 1 146 ? -6.541  39.121  28.736  1.00 35.57 ? 1012 SER H OG  1 
ATOM   2833 N N   . THR B 1 147 ? -4.771  36.248  31.451  1.00 27.37 ? 1013 THR H N   1 
ATOM   2834 C CA  . THR B 1 147 ? -4.663  35.629  32.789  1.00 27.91 ? 1013 THR H CA  1 
ATOM   2835 C C   . THR B 1 147 ? -4.014  36.579  33.797  1.00 27.91 ? 1013 THR H C   1 
ATOM   2836 O O   . THR B 1 147 ? -3.478  37.612  33.405  1.00 29.59 ? 1013 THR H O   1 
ATOM   2837 C CB  . THR B 1 147 ? -3.601  34.539  32.995  1.00 30.55 ? 1013 THR H CB  1 
ATOM   2838 O OG1 . THR B 1 147 ? -2.662  34.368  31.938  1.00 30.84 ? 1013 THR H OG1 1 
ATOM   2839 C CG2 . THR B 1 147 ? -4.220  33.292  33.534  1.00 28.54 ? 1013 THR H CG2 1 
ATOM   2840 N N   . SER B 1 148 ? -3.988  36.149  35.046  1.00 28.55 ? 1014 SER H N   1 
ATOM   2841 C CA  . SER B 1 148 ? -3.228  36.788  36.132  1.00 27.04 ? 1014 SER H CA  1 
ATOM   2842 C C   . SER B 1 148 ? -2.186  35.794  36.626  1.00 26.84 ? 1014 SER H C   1 
ATOM   2843 O O   . SER B 1 148 ? -2.469  34.572  36.644  1.00 23.23 ? 1014 SER H O   1 
ATOM   2844 C CB  . SER B 1 148 ? -4.162  37.209  37.222  1.00 29.19 ? 1014 SER H CB  1 
ATOM   2845 O OG  . SER B 1 148 ? -5.070  38.155  36.673  1.00 31.83 ? 1014 SER H OG  1 
ATOM   2846 N N   . VAL B 1 149 ? -1.010  36.284  36.992  1.00 24.09 ? 1015 VAL H N   1 
ATOM   2847 C CA  . VAL B 1 149 ? 0.047   35.397  37.532  1.00 23.89 ? 1015 VAL H CA  1 
ATOM   2848 C C   . VAL B 1 149 ? -0.537  34.518  38.652  1.00 22.57 ? 1015 VAL H C   1 
ATOM   2849 O O   . VAL B 1 149 ? -1.215  35.029  39.559  1.00 23.67 ? 1015 VAL H O   1 
ATOM   2850 C CB  . VAL B 1 149 ? 1.285   36.199  37.965  1.00 24.97 ? 1015 VAL H CB  1 
ATOM   2851 C CG1 . VAL B 1 149 ? 2.246   35.384  38.818  1.00 24.53 ? 1015 VAL H CG1 1 
ATOM   2852 C CG2 . VAL B 1 149 ? 2.018   36.810  36.774  1.00 25.90 ? 1015 VAL H CG2 1 
ATOM   2853 N N   . GLY B 1 150 ? -0.272  33.206  38.584  1.00 21.69 ? 1016 GLY H N   1 
ATOM   2854 C CA  . GLY B 1 150 ? -0.702  32.222  39.588  1.00 21.68 ? 1016 GLY H CA  1 
ATOM   2855 C C   . GLY B 1 150 ? -1.995  31.510  39.254  1.00 21.28 ? 1016 GLY H C   1 
ATOM   2856 O O   . GLY B 1 150 ? -2.315  30.487  39.945  1.00 20.28 ? 1016 GLY H O   1 
ATOM   2857 N N   . ASP B 1 151 ? -2.719  31.985  38.248  1.00 22.81 ? 1017 ASP H N   1 
ATOM   2858 C CA  . ASP B 1 151 ? -3.963  31.322  37.820  1.00 24.11 ? 1017 ASP H CA  1 
ATOM   2859 C C   . ASP B 1 151 ? -3.666  30.048  37.022  1.00 23.88 ? 1017 ASP H C   1 
ATOM   2860 O O   . ASP B 1 151 ? -2.536  29.845  36.543  1.00 21.89 ? 1017 ASP H O   1 
ATOM   2861 C CB  . ASP B 1 151 ? -4.803  32.303  37.009  1.00 26.63 ? 1017 ASP H CB  1 
ATOM   2862 C CG  . ASP B 1 151 ? -5.472  33.368  37.859  1.00 27.61 ? 1017 ASP H CG  1 
ATOM   2863 O OD1 . ASP B 1 151 ? -5.409  33.275  39.089  1.00 30.19 ? 1017 ASP H OD1 1 
ATOM   2864 O OD2 . ASP B 1 151 ? -6.032  34.283  37.265  1.00 31.18 ? 1017 ASP H OD2 1 
ATOM   2865 N N   . ARG B 1 152 ? -4.708  29.259  36.801  1.00 24.42 ? 1018 ARG H N   1 
ATOM   2866 C CA  . ARG B 1 152 ? -4.631  28.095  35.890  1.00 25.67 ? 1018 ARG H CA  1 
ATOM   2867 C C   . ARG B 1 152 ? -5.144  28.566  34.534  1.00 25.57 ? 1018 ARG H C   1 
ATOM   2868 O O   . ARG B 1 152 ? -6.166  29.286  34.484  1.00 25.17 ? 1018 ARG H O   1 
ATOM   2869 C CB  . ARG B 1 152 ? -5.381  26.885  36.450  1.00 28.85 ? 1018 ARG H CB  1 
ATOM   2870 C CG  . ARG B 1 152 ? -5.440  25.702  35.485  1.00 31.14 ? 1018 ARG H CG  1 
ATOM   2871 C CD  . ARG B 1 152 ? -5.777  24.373  36.158  1.00 35.17 ? 1018 ARG H CD  1 
ATOM   2872 N NE  . ARG B 1 152 ? -4.768  23.920  37.130  1.00 39.02 ? 1018 ARG H NE  1 
ATOM   2873 C CZ  . ARG B 1 152 ? -4.930  23.847  38.455  1.00 44.47 ? 1018 ARG H CZ  1 
ATOM   2874 N NH1 . ARG B 1 152 ? -3.937  23.426  39.227  1.00 45.05 ? 1018 ARG H NH1 1 
ATOM   2875 N NH2 . ARG B 1 152 ? -6.093  24.143  39.018  1.00 46.55 ? 1018 ARG H NH2 1 
ATOM   2876 N N   . VAL B 1 153 ? -4.414  28.225  33.483  1.00 23.33 ? 1019 VAL H N   1 
ATOM   2877 C CA  . VAL B 1 153 ? -4.747  28.620  32.096  1.00 24.59 ? 1019 VAL H CA  1 
ATOM   2878 C C   . VAL B 1 153 ? -5.102  27.332  31.365  1.00 22.83 ? 1019 VAL H C   1 
ATOM   2879 O O   . VAL B 1 153 ? -4.332  26.382  31.522  1.00 19.85 ? 1019 VAL H O   1 
ATOM   2880 C CB  . VAL B 1 153 ? -3.521  29.301  31.446  1.00 25.36 ? 1019 VAL H CB  1 
ATOM   2881 C CG1 . VAL B 1 153 ? -3.600  29.340  29.928  1.00 27.68 ? 1019 VAL H CG1 1 
ATOM   2882 C CG2 . VAL B 1 153 ? -3.329  30.671  32.022  1.00 27.40 ? 1019 VAL H CG2 1 
ATOM   2883 N N   . SER B 1 154 ? -6.222  27.285  30.642  1.00 22.18 ? 1020 SER H N   1 
ATOM   2884 C CA  . SER B 1 154 ? -6.585  26.141  29.760  1.00 23.11 ? 1020 SER H CA  1 
ATOM   2885 C C   . SER B 1 154 ? -6.772  26.638  28.323  1.00 23.27 ? 1020 SER H C   1 
ATOM   2886 O O   . SER B 1 154 ? -7.752  27.357  28.049  1.00 23.93 ? 1020 SER H O   1 
ATOM   2887 C CB  . SER B 1 154 ? -7.850  25.434  30.267  1.00 25.37 ? 1020 SER H CB  1 
ATOM   2888 O OG  . SER B 1 154 ? -7.656  25.037  31.628  1.00 25.96 ? 1020 SER H OG  1 
ATOM   2889 N N   . ILE B 1 155 ? -5.949  26.141  27.392  1.00 21.89 ? 1021 ILE H N   1 
ATOM   2890 C CA  . ILE B 1 155 ? -5.964  26.543  25.967  1.00 22.33 ? 1021 ILE H CA  1 
ATOM   2891 C C   . ILE B 1 155 ? -6.435  25.323  25.182  1.00 22.34 ? 1021 ILE H C   1 
ATOM   2892 O O   . ILE B 1 155 ? -5.912  24.267  25.407  1.00 21.28 ? 1021 ILE H O   1 
ATOM   2893 C CB  . ILE B 1 155 ? -4.576  27.012  25.514  1.00 22.15 ? 1021 ILE H CB  1 
ATOM   2894 C CG1 . ILE B 1 155 ? -4.155  28.288  26.245  1.00 22.45 ? 1021 ILE H CG1 1 
ATOM   2895 C CG2 . ILE B 1 155 ? -4.565  27.185  24.007  1.00 21.39 ? 1021 ILE H CG2 1 
ATOM   2896 C CD1 . ILE B 1 155 ? -2.712  28.728  25.914  1.00 23.44 ? 1021 ILE H CD1 1 
ATOM   2897 N N   . THR B 1 156 ? -7.518  25.468  24.435  1.00 23.22 ? 1022 THR H N   1 
ATOM   2898 C CA  . THR B 1 156 ? -8.217  24.334  23.795  1.00 25.23 ? 1022 THR H CA  1 
ATOM   2899 C C   . THR B 1 156 ? -7.957  24.342  22.309  1.00 24.57 ? 1022 THR H C   1 
ATOM   2900 O O   . THR B 1 156 ? -7.805  25.420  21.667  1.00 24.65 ? 1022 THR H O   1 
ATOM   2901 C CB  . THR B 1 156 ? -9.711  24.339  24.132  1.00 27.01 ? 1022 THR H CB  1 
ATOM   2902 O OG1 . THR B 1 156 ? -10.294 25.475  23.466  1.00 29.76 ? 1022 THR H OG1 1 
ATOM   2903 C CG2 . THR B 1 156 ? -9.910  24.405  25.624  1.00 28.24 ? 1022 THR H CG2 1 
ATOM   2904 N N   . CYS B 1 157 ? -7.995  23.142  21.761  1.00 25.51 ? 1023 CYS H N   1 
ATOM   2905 C CA  . CYS B 1 157 ? -7.786  22.901  20.339  1.00 26.48 ? 1023 CYS H CA  1 
ATOM   2906 C C   . CYS B 1 157 ? -8.763  21.800  19.936  1.00 26.15 ? 1023 CYS H C   1 
ATOM   2907 O O   . CYS B 1 157 ? -8.854  20.797  20.683  1.00 25.09 ? 1023 CYS H O   1 
ATOM   2908 C CB  . CYS B 1 157 ? -6.344  22.509  20.083  1.00 30.10 ? 1023 CYS H CB  1 
ATOM   2909 S SG  . CYS B 1 157 ? -6.043  22.363  18.317  1.00 37.56 ? 1023 CYS H SG  1 
ATOM   2910 N N   . LYS B 1 158 ? -9.547  22.014  18.895  1.00 24.79 ? 1024 LYS H N   1 
ATOM   2911 C CA  . LYS B 1 158 ? -10.429 20.974  18.340  1.00 26.60 ? 1024 LYS H CA  1 
ATOM   2912 C C   . LYS B 1 158 ? -9.896  20.545  16.967  1.00 25.22 ? 1024 LYS H C   1 
ATOM   2913 O O   . LYS B 1 158 ? -9.660  21.409  16.114  1.00 27.17 ? 1024 LYS H O   1 
ATOM   2914 C CB  . LYS B 1 158 ? -11.859 21.506  18.196  1.00 30.04 ? 1024 LYS H CB  1 
ATOM   2915 C CG  . LYS B 1 158 ? -12.864 20.459  17.781  1.00 34.15 ? 1024 LYS H CG  1 
ATOM   2916 C CD  . LYS B 1 158 ? -14.216 20.550  18.494  1.00 39.85 ? 1024 LYS H CD  1 
ATOM   2917 C CE  . LYS B 1 158 ? -15.115 19.391  18.112  1.00 42.59 ? 1024 LYS H CE  1 
ATOM   2918 N NZ  . LYS B 1 158 ? -14.852 18.188  18.948  1.00 43.14 ? 1024 LYS H NZ  1 
ATOM   2919 N N   . ALA B 1 159 ? -9.826  19.249  16.738  1.00 25.23 ? 1025 ALA H N   1 
ATOM   2920 C CA  . ALA B 1 159 ? -9.460  18.655  15.441  1.00 23.32 ? 1025 ALA H CA  1 
ATOM   2921 C C   . ALA B 1 159 ? -10.750 18.361  14.676  1.00 25.02 ? 1025 ALA H C   1 
ATOM   2922 O O   . ALA B 1 159 ? -11.756 17.906  15.327  1.00 24.28 ? 1025 ALA H O   1 
ATOM   2923 C CB  . ALA B 1 159 ? -8.668  17.386  15.635  1.00 23.48 ? 1025 ALA H CB  1 
ATOM   2924 N N   . SER B 1 160 ? -10.703 18.550  13.363  1.00 25.16 ? 1026 SER H N   1 
ATOM   2925 C CA  . SER B 1 160 ? -11.856 18.317  12.443  1.00 26.51 ? 1026 SER H CA  1 
ATOM   2926 C C   . SER B 1 160 ? -12.085 16.809  12.270  1.00 27.77 ? 1026 SER H C   1 
ATOM   2927 O O   . SER B 1 160 ? -13.179 16.415  11.776  1.00 27.96 ? 1026 SER H O   1 
ATOM   2928 C CB  . SER B 1 160 ? -11.661 18.995  11.095  1.00 25.73 ? 1026 SER H CB  1 
ATOM   2929 O OG  . SER B 1 160 ? -10.536 18.479  10.413  1.00 23.52 ? 1026 SER H OG  1 
ATOM   2930 N N   . GLN B 1 161 ? -11.089 15.972  12.577  1.00 27.79 ? 1027 GLN H N   1 
ATOM   2931 C CA  . GLN B 1 161 ? -11.266 14.501  12.577  1.00 28.43 ? 1027 GLN H CA  1 
ATOM   2932 C C   . GLN B 1 161 ? -10.465 13.884  13.700  1.00 27.63 ? 1027 GLN H C   1 
ATOM   2933 O O   . GLN B 1 161 ? -9.623  14.602  14.279  1.00 26.70 ? 1027 GLN H O   1 
ATOM   2934 C CB  . GLN B 1 161 ? -10.895 13.833  11.258  1.00 31.01 ? 1027 GLN H CB  1 
ATOM   2935 C CG  . GLN B 1 161 ? -9.751  14.465  10.526  1.00 32.86 ? 1027 GLN H CG  1 
ATOM   2936 C CD  . GLN B 1 161 ? -9.672  14.003  9.082   1.00 32.99 ? 1027 GLN H CD  1 
ATOM   2937 O OE1 . GLN B 1 161 ? -9.412  12.841  8.799   1.00 35.46 ? 1027 GLN H OE1 1 
ATOM   2938 N NE2 . GLN B 1 161 ? -9.790  14.941  8.161   1.00 32.87 ? 1027 GLN H NE2 1 
ATOM   2939 N N   . ASP B 1 162 ? -10.757 12.620  13.988  1.00 27.27 ? 1028 ASP H N   1 
ATOM   2940 C CA  . ASP B 1 162 ? -10.102 11.840  15.061  1.00 25.87 ? 1028 ASP H CA  1 
ATOM   2941 C C   . ASP B 1 162 ? -8.603  11.800  14.767  1.00 24.60 ? 1028 ASP H C   1 
ATOM   2942 O O   . ASP B 1 162 ? -8.226  11.164  13.810  1.00 22.75 ? 1028 ASP H O   1 
ATOM   2943 C CB  . ASP B 1 162 ? -10.723 10.447  15.160  1.00 27.71 ? 1028 ASP H CB  1 
ATOM   2944 C CG  . ASP B 1 162 ? -10.218 9.594   16.328  1.00 29.02 ? 1028 ASP H CG  1 
ATOM   2945 O OD1 . ASP B 1 162 ? -9.242  10.005  17.028  1.00 26.23 ? 1028 ASP H OD1 1 
ATOM   2946 O OD2 . ASP B 1 162 ? -10.767 8.474   16.486  1.00 30.81 ? 1028 ASP H OD2 1 
ATOM   2947 N N   . VAL B 1 163 ? -7.764  12.400  15.619  1.00 22.51 ? 1029 VAL H N   1 
ATOM   2948 C CA  . VAL B 1 163 ? -6.295  12.341  15.426  1.00 20.96 ? 1029 VAL H CA  1 
ATOM   2949 C C   . VAL B 1 163 ? -5.675  11.497  16.566  1.00 20.49 ? 1029 VAL H C   1 
ATOM   2950 O O   . VAL B 1 163 ? -4.426  11.565  16.755  1.00 20.46 ? 1029 VAL H O   1 
ATOM   2951 C CB  . VAL B 1 163 ? -5.693  13.748  15.353  1.00 21.36 ? 1029 VAL H CB  1 
ATOM   2952 C CG1 . VAL B 1 163 ? -6.094  14.452  14.066  1.00 21.87 ? 1029 VAL H CG1 1 
ATOM   2953 C CG2 . VAL B 1 163 ? -6.018  14.594  16.584  1.00 20.69 ? 1029 VAL H CG2 1 
ATOM   2954 N N   . GLY B 1 164 ? -6.477  10.722  17.297  1.00 19.60 ? 1030 GLY H N   1 
ATOM   2955 C CA  . GLY B 1 164 ? -5.967  9.828   18.362  1.00 19.35 ? 1030 GLY H CA  1 
ATOM   2956 C C   . GLY B 1 164 ? -5.365  10.684  19.461  1.00 18.84 ? 1030 GLY H C   1 
ATOM   2957 O O   . GLY B 1 164 ? -6.076  11.593  19.942  1.00 18.96 ? 1030 GLY H O   1 
ATOM   2958 N N   . THR B 1 165 ? -4.116  10.414  19.849  1.00 17.86 ? 1031 THR H N   1 
ATOM   2959 C CA  . THR B 1 165 ? -3.351  11.235  20.799  1.00 18.02 ? 1031 THR H CA  1 
ATOM   2960 C C   . THR B 1 165 ? -2.082  11.825  20.136  1.00 18.19 ? 1031 THR H C   1 
ATOM   2961 O O   . THR B 1 165 ? -1.261  12.364  20.870  1.00 18.43 ? 1031 THR H O   1 
ATOM   2962 C CB  . THR B 1 165 ? -3.038  10.416  22.062  1.00 18.07 ? 1031 THR H CB  1 
ATOM   2963 O OG1 . THR B 1 165 ? -2.301  9.255   21.670  1.00 17.67 ? 1031 THR H OG1 1 
ATOM   2964 C CG2 . THR B 1 165 ? -4.311  10.034  22.802  1.00 18.35 ? 1031 THR H CG2 1 
ATOM   2965 N N   . ALA B 1 166 ? -2.028  11.934  18.808  1.00 18.47 ? 1032 ALA H N   1 
ATOM   2966 C CA  . ALA B 1 166 ? -0.856  12.489  18.077  1.00 18.13 ? 1032 ALA H CA  1 
ATOM   2967 C C   . ALA B 1 166 ? -1.009  14.006  17.972  1.00 18.11 ? 1032 ALA H C   1 
ATOM   2968 O O   . ALA B 1 166 ? -1.139  14.563  16.879  1.00 18.23 ? 1032 ALA H O   1 
ATOM   2969 C CB  . ALA B 1 166 ? -0.688  11.783  16.742  1.00 18.23 ? 1032 ALA H CB  1 
ATOM   2970 N N   . VAL B 1 167 ? -0.931  14.666  19.112  1.00 17.34 ? 1033 VAL H N   1 
ATOM   2971 C CA  . VAL B 1 167 ? -1.062  16.136  19.196  1.00 17.13 ? 1033 VAL H CA  1 
ATOM   2972 C C   . VAL B 1 167 ? 0.120   16.650  20.006  1.00 16.81 ? 1033 VAL H C   1 
ATOM   2973 O O   . VAL B 1 167 ? 0.500   16.031  21.064  1.00 16.76 ? 1033 VAL H O   1 
ATOM   2974 C CB  . VAL B 1 167 ? -2.411  16.557  19.801  1.00 17.29 ? 1033 VAL H CB  1 
ATOM   2975 C CG1 . VAL B 1 167 ? -2.431  18.032  20.206  1.00 17.85 ? 1033 VAL H CG1 1 
ATOM   2976 C CG2 . VAL B 1 167 ? -3.529  16.243  18.818  1.00 17.94 ? 1033 VAL H CG2 1 
ATOM   2977 N N   . ALA B 1 168 ? 0.667   17.726  19.510  1.00 16.03 ? 1034 ALA H N   1 
ATOM   2978 C CA  . ALA B 1 168 ? 1.764   18.463  20.156  1.00 16.03 ? 1034 ALA H CA  1 
ATOM   2979 C C   . ALA B 1 168 ? 1.317   19.871  20.472  1.00 16.32 ? 1034 ALA H C   1 
ATOM   2980 O O   . ALA B 1 168 ? 0.431   20.434  19.777  1.00 16.58 ? 1034 ALA H O   1 
ATOM   2981 C CB  . ALA B 1 168 ? 2.983   18.419  19.304  1.00 16.33 ? 1034 ALA H CB  1 
ATOM   2982 N N   . TRP B 1 169 ? 1.963   20.475  21.474  1.00 15.96 ? 1035 TRP H N   1 
ATOM   2983 C CA  . TRP B 1 169 ? 1.780   21.908  21.821  1.00 17.32 ? 1035 TRP H CA  1 
ATOM   2984 C C   . TRP B 1 169 ? 3.131   22.583  21.810  1.00 17.20 ? 1035 TRP H C   1 
ATOM   2985 O O   . TRP B 1 169 ? 4.044   22.014  22.396  1.00 17.42 ? 1035 TRP H O   1 
ATOM   2986 C CB  . TRP B 1 169 ? 1.108   22.081  23.157  1.00 17.19 ? 1035 TRP H CB  1 
ATOM   2987 C CG  . TRP B 1 169 ? -0.322  21.660  23.154  1.00 17.62 ? 1035 TRP H CG  1 
ATOM   2988 C CD1 . TRP B 1 169 ? -0.818  20.461  23.586  1.00 18.79 ? 1035 TRP H CD1 1 
ATOM   2989 C CD2 . TRP B 1 169 ? -1.453  22.488  22.884  1.00 17.99 ? 1035 TRP H CD2 1 
ATOM   2990 N NE1 . TRP B 1 169 ? -2.199  20.486  23.556  1.00 18.20 ? 1035 TRP H NE1 1 
ATOM   2991 C CE2 . TRP B 1 169 ? -2.606  21.709  23.117  1.00 18.13 ? 1035 TRP H CE2 1 
ATOM   2992 C CE3 . TRP B 1 169 ? -1.594  23.797  22.425  1.00 18.44 ? 1035 TRP H CE3 1 
ATOM   2993 C CZ2 . TRP B 1 169 ? -3.877  22.212  22.946  1.00 18.26 ? 1035 TRP H CZ2 1 
ATOM   2994 C CZ3 . TRP B 1 169 ? -2.863  24.296  22.225  1.00 19.16 ? 1035 TRP H CZ3 1 
ATOM   2995 C CH2 . TRP B 1 169 ? -3.984  23.505  22.498  1.00 19.02 ? 1035 TRP H CH2 1 
ATOM   2996 N N   . TYR B 1 170 ? 3.194   23.734  21.119  1.00 18.20 ? 1036 TYR H N   1 
ATOM   2997 C CA  . TYR B 1 170 ? 4.375   24.624  21.036  1.00 18.80 ? 1036 TYR H CA  1 
ATOM   2998 C C   . TYR B 1 170 ? 4.070   25.983  21.670  1.00 19.39 ? 1036 TYR H C   1 
ATOM   2999 O O   . TYR B 1 170 ? 2.927   26.478  21.568  1.00 18.74 ? 1036 TYR H O   1 
ATOM   3000 C CB  . TYR B 1 170 ? 4.781   24.788  19.581  1.00 18.90 ? 1036 TYR H CB  1 
ATOM   3001 C CG  . TYR B 1 170 ? 5.363   23.556  18.969  1.00 18.60 ? 1036 TYR H CG  1 
ATOM   3002 C CD1 . TYR B 1 170 ? 6.721   23.300  19.075  1.00 18.39 ? 1036 TYR H CD1 1 
ATOM   3003 C CD2 . TYR B 1 170 ? 4.580   22.663  18.255  1.00 19.34 ? 1036 TYR H CD2 1 
ATOM   3004 C CE1 . TYR B 1 170 ? 7.269   22.199  18.453  1.00 18.62 ? 1036 TYR H CE1 1 
ATOM   3005 C CE2 . TYR B 1 170 ? 5.110   21.528  17.691  1.00 19.42 ? 1036 TYR H CE2 1 
ATOM   3006 C CZ  . TYR B 1 170 ? 6.473   21.307  17.784  1.00 19.67 ? 1036 TYR H CZ  1 
ATOM   3007 O OH  . TYR B 1 170 ? 7.032   20.190  17.285  1.00 21.34 ? 1036 TYR H OH  1 
ATOM   3008 N N   . GLN B 1 171 ? 5.092   26.572  22.293  1.00 19.02 ? 1037 GLN H N   1 
ATOM   3009 C CA  . GLN B 1 171 ? 5.127   27.986  22.698  1.00 20.12 ? 1037 GLN H CA  1 
ATOM   3010 C C   . GLN B 1 171 ? 5.962   28.738  21.652  1.00 20.97 ? 1037 GLN H C   1 
ATOM   3011 O O   . GLN B 1 171 ? 7.075   28.213  21.269  1.00 20.49 ? 1037 GLN H O   1 
ATOM   3012 C CB  . GLN B 1 171 ? 5.834   28.080  24.053  1.00 21.09 ? 1037 GLN H CB  1 
ATOM   3013 C CG  . GLN B 1 171 ? 5.813   29.443  24.697  1.00 22.42 ? 1037 GLN H CG  1 
ATOM   3014 C CD  . GLN B 1 171 ? 6.567   29.449  26.012  1.00 23.43 ? 1037 GLN H CD  1 
ATOM   3015 O OE1 . GLN B 1 171 ? 5.993   29.548  27.107  1.00 24.18 ? 1037 GLN H OE1 1 
ATOM   3016 N NE2 . GLN B 1 171 ? 7.867   29.233  25.924  1.00 22.80 ? 1037 GLN H NE2 1 
ATOM   3017 N N   . GLN B 1 172 ? 5.557   29.952  21.323  1.00 22.19 ? 1038 GLN H N   1 
ATOM   3018 C CA  . GLN B 1 172 ? 6.424   30.837  20.511  1.00 24.51 ? 1038 GLN H CA  1 
ATOM   3019 C C   . GLN B 1 172 ? 6.407   32.265  21.055  1.00 24.96 ? 1038 GLN H C   1 
ATOM   3020 O O   . GLN B 1 172 ? 5.320   32.811  21.270  1.00 24.29 ? 1038 GLN H O   1 
ATOM   3021 C CB  . GLN B 1 172 ? 6.084   30.871  19.033  1.00 26.22 ? 1038 GLN H CB  1 
ATOM   3022 C CG  . GLN B 1 172 ? 7.342   31.321  18.281  1.00 27.74 ? 1038 GLN H CG  1 
ATOM   3023 C CD  . GLN B 1 172 ? 7.106   31.462  16.812  1.00 30.26 ? 1038 GLN H CD  1 
ATOM   3024 O OE1 . GLN B 1 172 ? 8.027   31.738  16.044  1.00 34.95 ? 1038 GLN H OE1 1 
ATOM   3025 N NE2 . GLN B 1 172 ? 5.867   31.216  16.427  1.00 30.25 ? 1038 GLN H NE2 1 
ATOM   3026 N N   . LYS B 1 173 ? 7.593   32.777  21.344  1.00 26.47 ? 1039 LYS H N   1 
ATOM   3027 C CA  . LYS B 1 173 ? 7.832   34.200  21.646  1.00 28.19 ? 1039 LYS H CA  1 
ATOM   3028 C C   . LYS B 1 173 ? 8.320   34.938  20.394  1.00 30.17 ? 1039 LYS H C   1 
ATOM   3029 O O   . LYS B 1 173 ? 8.943   34.377  19.496  1.00 28.91 ? 1039 LYS H O   1 
ATOM   3030 C CB  . LYS B 1 173 ? 8.790   34.275  22.833  1.00 28.32 ? 1039 LYS H CB  1 
ATOM   3031 C CG  . LYS B 1 173 ? 8.205   33.663  24.084  1.00 28.77 ? 1039 LYS H CG  1 
ATOM   3032 C CD  . LYS B 1 173 ? 8.992   33.951  25.295  1.00 28.97 ? 1039 LYS H CD  1 
ATOM   3033 C CE  . LYS B 1 173 ? 8.449   33.189  26.476  1.00 29.85 ? 1039 LYS H CE  1 
ATOM   3034 N NZ  . LYS B 1 173 ? 9.206   33.483  27.710  1.00 30.77 ? 1039 LYS H NZ  1 
ATOM   3035 N N   . PRO B 1 174 ? 8.113   36.269  20.348  1.00 34.03 ? 1040 PRO H N   1 
ATOM   3036 C CA  . PRO B 1 174 ? 8.507   37.062  19.188  1.00 35.80 ? 1040 PRO H CA  1 
ATOM   3037 C C   . PRO B 1 174 ? 10.010  36.922  18.906  1.00 35.08 ? 1040 PRO H C   1 
ATOM   3038 O O   . PRO B 1 174 ? 10.798  36.862  19.846  1.00 33.92 ? 1040 PRO H O   1 
ATOM   3039 C CB  . PRO B 1 174 ? 8.067   38.478  19.593  1.00 38.89 ? 1040 PRO H CB  1 
ATOM   3040 C CG  . PRO B 1 174 ? 6.931   38.234  20.593  1.00 38.57 ? 1040 PRO H CG  1 
ATOM   3041 C CD  . PRO B 1 174 ? 7.446   37.062  21.400  1.00 37.88 ? 1040 PRO H CD  1 
ATOM   3042 N N   . GLY B 1 175 ? 10.345  36.741  17.622  1.00 36.08 ? 1041 GLY H N   1 
ATOM   3043 C CA  . GLY B 1 175 ? 11.722  36.541  17.103  1.00 37.98 ? 1041 GLY H CA  1 
ATOM   3044 C C   . GLY B 1 175 ? 12.421  35.288  17.630  1.00 38.56 ? 1041 GLY H C   1 
ATOM   3045 O O   . GLY B 1 175 ? 13.667  35.168  17.447  1.00 40.13 ? 1041 GLY H O   1 
ATOM   3046 N N   . GLN B 1 176 ? 11.691  34.371  18.268  1.00 35.40 ? 1042 GLN H N   1 
ATOM   3047 C CA  . GLN B 1 176 ? 12.279  33.103  18.768  1.00 34.92 ? 1042 GLN H CA  1 
ATOM   3048 C C   . GLN B 1 176 ? 11.660  31.930  18.001  1.00 31.44 ? 1042 GLN H C   1 
ATOM   3049 O O   . GLN B 1 176 ? 10.601  32.072  17.381  1.00 32.09 ? 1042 GLN H O   1 
ATOM   3050 C CB  . GLN B 1 176 ? 12.046  32.953  20.269  1.00 36.31 ? 1042 GLN H CB  1 
ATOM   3051 C CG  . GLN B 1 176 ? 12.819  33.958  21.117  1.00 39.58 ? 1042 GLN H CG  1 
ATOM   3052 C CD  . GLN B 1 176 ? 12.813  33.557  22.575  1.00 41.90 ? 1042 GLN H CD  1 
ATOM   3053 O OE1 . GLN B 1 176 ? 13.310  34.281  23.425  1.00 47.42 ? 1042 GLN H OE1 1 
ATOM   3054 N NE2 . GLN B 1 176 ? 12.211  32.419  22.898  1.00 42.15 ? 1042 GLN H NE2 1 
ATOM   3055 N N   . SER B 1 177 ? 12.322  30.791  18.026  1.00 29.77 ? 1043 SER H N   1 
ATOM   3056 C CA  . SER B 1 177 ? 11.810  29.578  17.367  1.00 27.85 ? 1043 SER H CA  1 
ATOM   3057 C C   . SER B 1 177 ? 10.766  28.931  18.280  1.00 26.01 ? 1043 SER H C   1 
ATOM   3058 O O   . SER B 1 177 ? 10.770  29.122  19.501  1.00 26.18 ? 1043 SER H O   1 
ATOM   3059 C CB  . SER B 1 177 ? 12.952  28.676  17.018  1.00 30.09 ? 1043 SER H CB  1 
ATOM   3060 O OG  . SER B 1 177 ? 13.520  28.145  18.204  1.00 31.83 ? 1043 SER H OG  1 
ATOM   3061 N N   . PRO B 1 178 ? 9.756   28.244  17.715  1.00 24.16 ? 1044 PRO H N   1 
ATOM   3062 C CA  . PRO B 1 178 ? 8.802   27.489  18.526  1.00 23.75 ? 1044 PRO H CA  1 
ATOM   3063 C C   . PRO B 1 178 ? 9.532   26.519  19.467  1.00 24.13 ? 1044 PRO H C   1 
ATOM   3064 O O   . PRO B 1 178 ? 10.587  26.003  19.099  1.00 23.50 ? 1044 PRO H O   1 
ATOM   3065 C CB  . PRO B 1 178 ? 8.010   26.675  17.487  1.00 22.74 ? 1044 PRO H CB  1 
ATOM   3066 C CG  . PRO B 1 178 ? 8.062   27.550  16.242  1.00 23.98 ? 1044 PRO H CG  1 
ATOM   3067 C CD  . PRO B 1 178 ? 9.464   28.134  16.271  1.00 24.00 ? 1044 PRO H CD  1 
ATOM   3068 N N   . LYS B 1 179 ? 8.980   26.321  20.658  1.00 21.76 ? 1045 LYS H N   1 
ATOM   3069 C CA  . LYS B 1 179 ? 9.523   25.388  21.662  1.00 23.87 ? 1045 LYS H CA  1 
ATOM   3070 C C   . LYS B 1 179 ? 8.477   24.320  21.964  1.00 21.01 ? 1045 LYS H C   1 
ATOM   3071 O O   . LYS B 1 179 ? 7.355   24.682  22.376  1.00 19.45 ? 1045 LYS H O   1 
ATOM   3072 C CB  . LYS B 1 179 ? 9.920   26.194  22.906  1.00 27.68 ? 1045 LYS H CB  1 
ATOM   3073 C CG  . LYS B 1 179 ? 11.220  26.945  22.595  1.00 35.17 ? 1045 LYS H CG  1 
ATOM   3074 C CD  . LYS B 1 179 ? 11.659  28.123  23.451  1.00 40.60 ? 1045 LYS H CD  1 
ATOM   3075 C CE  . LYS B 1 179 ? 12.954  28.710  22.910  1.00 45.99 ? 1045 LYS H CE  1 
ATOM   3076 N NZ  . LYS B 1 179 ? 13.014  28.687  21.420  1.00 46.74 ? 1045 LYS H NZ  1 
ATOM   3077 N N   . LEU B 1 180 ? 8.868   23.054  21.870  1.00 19.84 ? 1046 LEU H N   1 
ATOM   3078 C CA  . LEU B 1 180 ? 7.918   21.945  22.112  1.00 18.91 ? 1046 LEU H CA  1 
ATOM   3079 C C   . LEU B 1 180 ? 7.601   21.933  23.609  1.00 17.92 ? 1046 LEU H C   1 
ATOM   3080 O O   . LEU B 1 180 ? 8.551   21.903  24.430  1.00 17.54 ? 1046 LEU H O   1 
ATOM   3081 C CB  . LEU B 1 180 ? 8.536   20.616  21.712  1.00 19.12 ? 1046 LEU H CB  1 
ATOM   3082 C CG  . LEU B 1 180 ? 7.654   19.377  21.888  1.00 18.74 ? 1046 LEU H CG  1 
ATOM   3083 C CD1 . LEU B 1 180 ? 6.346   19.494  21.123  1.00 18.74 ? 1046 LEU H CD1 1 
ATOM   3084 C CD2 . LEU B 1 180 ? 8.443   18.170  21.410  1.00 18.91 ? 1046 LEU H CD2 1 
ATOM   3085 N N   . LEU B 1 181 ? 6.321   21.884  23.958  1.00 17.04 ? 1047 LEU H N   1 
ATOM   3086 C CA  . LEU B 1 181 ? 5.927   21.716  25.375  1.00 18.21 ? 1047 LEU H CA  1 
ATOM   3087 C C   . LEU B 1 181 ? 5.504   20.263  25.674  1.00 17.42 ? 1047 LEU H C   1 
ATOM   3088 O O   . LEU B 1 181 ? 5.910   19.666  26.698  1.00 18.78 ? 1047 LEU H O   1 
ATOM   3089 C CB  . LEU B 1 181 ? 4.727   22.627  25.622  1.00 18.48 ? 1047 LEU H CB  1 
ATOM   3090 C CG  . LEU B 1 181 ? 4.897   24.084  25.983  1.00 20.71 ? 1047 LEU H CG  1 
ATOM   3091 C CD1 . LEU B 1 181 ? 6.312   24.632  26.205  1.00 20.67 ? 1047 LEU H CD1 1 
ATOM   3092 C CD2 . LEU B 1 181 ? 3.885   24.980  25.298  1.00 20.56 ? 1047 LEU H CD2 1 
ATOM   3093 N N   . ILE B 1 182 ? 4.599   19.754  24.862  1.00 17.74 ? 1048 ILE H N   1 
ATOM   3094 C CA  . ILE B 1 182 ? 3.780   18.543  25.087  1.00 17.08 ? 1048 ILE H CA  1 
ATOM   3095 C C   . ILE B 1 182 ? 3.758   17.781  23.776  1.00 16.72 ? 1048 ILE H C   1 
ATOM   3096 O O   . ILE B 1 182 ? 3.504   18.428  22.720  1.00 15.91 ? 1048 ILE H O   1 
ATOM   3097 C CB  . ILE B 1 182 ? 2.351   18.909  25.530  1.00 17.85 ? 1048 ILE H CB  1 
ATOM   3098 C CG1 . ILE B 1 182 ? 2.306   19.660  26.870  1.00 17.98 ? 1048 ILE H CG1 1 
ATOM   3099 C CG2 . ILE B 1 182 ? 1.485   17.671  25.536  1.00 18.65 ? 1048 ILE H CG2 1 
ATOM   3100 C CD1 . ILE B 1 182 ? 2.757   18.843  28.082  1.00 18.71 ? 1048 ILE H CD1 1 
ATOM   3101 N N   . TYR B 1 183 ? 3.908   16.481  23.847  1.00 16.56 ? 1049 TYR H N   1 
ATOM   3102 C CA  . TYR B 1 183 ? 3.646   15.595  22.689  1.00 16.74 ? 1049 TYR H CA  1 
ATOM   3103 C C   . TYR B 1 183 ? 2.930   14.337  23.154  1.00 18.03 ? 1049 TYR H C   1 
ATOM   3104 O O   . TYR B 1 183 ? 2.761   14.080  24.342  1.00 18.17 ? 1049 TYR H O   1 
ATOM   3105 C CB  . TYR B 1 183 ? 4.936   15.331  21.895  1.00 17.27 ? 1049 TYR H CB  1 
ATOM   3106 C CG  . TYR B 1 183 ? 5.988   14.604  22.674  1.00 17.30 ? 1049 TYR H CG  1 
ATOM   3107 C CD1 . TYR B 1 183 ? 6.150   13.229  22.572  1.00 17.85 ? 1049 TYR H CD1 1 
ATOM   3108 C CD2 . TYR B 1 183 ? 6.834   15.299  23.503  1.00 17.96 ? 1049 TYR H CD2 1 
ATOM   3109 C CE1 . TYR B 1 183 ? 7.099   12.562  23.334  1.00 18.51 ? 1049 TYR H CE1 1 
ATOM   3110 C CE2 . TYR B 1 183 ? 7.813   14.650  24.228  1.00 18.17 ? 1049 TYR H CE2 1 
ATOM   3111 C CZ  . TYR B 1 183 ? 7.918   13.283  24.179  1.00 17.57 ? 1049 TYR H CZ  1 
ATOM   3112 O OH  . TYR B 1 183 ? 8.911   12.643  24.871  1.00 19.96 ? 1049 TYR H OH  1 
ATOM   3113 N N   . TRP B 1 184 ? 2.411   13.588  22.187  1.00 19.91 ? 1050 TRP H N   1 
ATOM   3114 C CA  . TRP B 1 184 ? 1.458   12.484  22.453  1.00 20.67 ? 1050 TRP H CA  1 
ATOM   3115 C C   . TRP B 1 184 ? 0.353   12.944  23.406  1.00 19.44 ? 1050 TRP H C   1 
ATOM   3116 O O   . TRP B 1 184 ? -0.018  12.179  24.295  1.00 19.46 ? 1050 TRP H O   1 
ATOM   3117 C CB  . TRP B 1 184 ? 2.180   11.233  22.975  1.00 23.39 ? 1050 TRP H CB  1 
ATOM   3118 C CG  . TRP B 1 184 ? 3.021   10.575  21.934  1.00 24.80 ? 1050 TRP H CG  1 
ATOM   3119 C CD1 . TRP B 1 184 ? 4.383   10.387  21.935  1.00 27.56 ? 1050 TRP H CD1 1 
ATOM   3120 C CD2 . TRP B 1 184 ? 2.522   9.895   20.785  1.00 24.10 ? 1050 TRP H CD2 1 
ATOM   3121 N NE1 . TRP B 1 184 ? 4.756   9.783   20.770  1.00 28.66 ? 1050 TRP H NE1 1 
ATOM   3122 C CE2 . TRP B 1 184 ? 3.644   9.462   20.050  1.00 24.23 ? 1050 TRP H CE2 1 
ATOM   3123 C CE3 . TRP B 1 184 ? 1.237   9.710   20.272  1.00 22.31 ? 1050 TRP H CE3 1 
ATOM   3124 C CZ2 . TRP B 1 184 ? 3.503   8.745   18.869  1.00 24.20 ? 1050 TRP H CZ2 1 
ATOM   3125 C CZ3 . TRP B 1 184 ? 1.113   9.037   19.082  1.00 24.14 ? 1050 TRP H CZ3 1 
ATOM   3126 C CH2 . TRP B 1 184 ? 2.230   8.582   18.387  1.00 23.12 ? 1050 TRP H CH2 1 
ATOM   3127 N N   . ALA B 1 185 ? -0.101  14.176  23.242  1.00 18.33 ? 1051 ALA H N   1 
ATOM   3128 C CA  . ALA B 1 185 ? -1.249  14.814  23.908  1.00 18.05 ? 1051 ALA H CA  1 
ATOM   3129 C C   . ALA B 1 185 ? -0.919  15.223  25.339  1.00 18.19 ? 1051 ALA H C   1 
ATOM   3130 O O   . ALA B 1 185 ? -1.475  16.233  25.764  1.00 18.57 ? 1051 ALA H O   1 
ATOM   3131 C CB  . ALA B 1 185 ? -2.480  13.938  23.857  1.00 18.53 ? 1051 ALA H CB  1 
ATOM   3132 N N   . SER B 1 186 ? -0.139  14.421  26.070  1.00 19.35 ? 1052 SER H N   1 
ATOM   3133 C CA  . SER B 1 186 ? 0.010   14.576  27.548  1.00 18.99 ? 1052 SER H CA  1 
ATOM   3134 C C   . SER B 1 186 ? 1.442   14.418  28.049  1.00 19.50 ? 1052 SER H C   1 
ATOM   3135 O O   . SER B 1 186 ? 1.623   14.599  29.299  1.00 19.09 ? 1052 SER H O   1 
ATOM   3136 C CB  . SER B 1 186 ? -0.888  13.618  28.268  1.00 19.52 ? 1052 SER H CB  1 
ATOM   3137 O OG  . SER B 1 186 ? -0.511  12.280  27.978  1.00 20.69 ? 1052 SER H OG  1 
ATOM   3138 N N   . THR B 1 187 ? 2.420   14.186  27.177  1.00 19.13 ? 1053 THR H N   1 
ATOM   3139 C CA  . THR B 1 187 ? 3.827   13.949  27.591  1.00 20.09 ? 1053 THR H CA  1 
ATOM   3140 C C   . THR B 1 187 ? 4.626   15.247  27.551  1.00 19.62 ? 1053 THR H C   1 
ATOM   3141 O O   . THR B 1 187 ? 4.761   15.888  26.480  1.00 17.54 ? 1053 THR H O   1 
ATOM   3142 C CB  . THR B 1 187 ? 4.505   12.839  26.783  1.00 21.66 ? 1053 THR H CB  1 
ATOM   3143 O OG1 . THR B 1 187 ? 3.766   11.667  27.102  1.00 23.34 ? 1053 THR H OG1 1 
ATOM   3144 C CG2 . THR B 1 187 ? 5.965   12.647  27.159  1.00 22.63 ? 1053 THR H CG2 1 
ATOM   3145 N N   . ARG B 1 188 ? 5.166   15.645  28.698  1.00 18.37 ? 1054 ARG H N   1 
ATOM   3146 C CA  A ARG B 1 188 ? 5.960   16.889  28.780  0.50 18.01 ? 1054 ARG H CA  1 
ATOM   3147 C CA  B ARG B 1 188 ? 5.949   16.892  28.748  0.50 19.36 ? 1054 ARG H CA  1 
ATOM   3148 C C   . ARG B 1 188 ? 7.343   16.629  28.168  1.00 18.96 ? 1054 ARG H C   1 
ATOM   3149 O O   . ARG B 1 188 ? 7.974   15.644  28.563  1.00 17.25 ? 1054 ARG H O   1 
ATOM   3150 C CB  A ARG B 1 188 ? 6.032   17.378  30.225  0.50 17.22 ? 1054 ARG H CB  1 
ATOM   3151 C CB  B ARG B 1 188 ? 5.984   17.434  30.171  0.50 20.31 ? 1054 ARG H CB  1 
ATOM   3152 C CG  A ARG B 1 188 ? 6.343   18.854  30.349  0.50 16.32 ? 1054 ARG H CG  1 
ATOM   3153 C CG  B ARG B 1 188 ? 6.891   18.632  30.309  0.50 21.41 ? 1054 ARG H CG  1 
ATOM   3154 C CD  A ARG B 1 188 ? 6.556   19.362  31.762  0.50 16.00 ? 1054 ARG H CD  1 
ATOM   3155 C CD  B ARG B 1 188 ? 6.675   19.325  31.641  0.50 22.65 ? 1054 ARG H CD  1 
ATOM   3156 N NE  A ARG B 1 188 ? 6.841   18.336  32.743  0.50 15.08 ? 1054 ARG H NE  1 
ATOM   3157 N NE  B ARG B 1 188 ? 5.342   19.092  32.169  0.50 23.95 ? 1054 ARG H NE  1 
ATOM   3158 C CZ  A ARG B 1 188 ? 8.067   17.960  33.113  0.50 15.18 ? 1054 ARG H CZ  1 
ATOM   3159 C CZ  B ARG B 1 188 ? 5.100   18.277  33.184  0.50 22.02 ? 1054 ARG H CZ  1 
ATOM   3160 N NH1 A ARG B 1 188 ? 9.147   18.463  32.543  0.50 14.80 ? 1054 ARG H NH1 1 
ATOM   3161 N NH1 B ARG B 1 188 ? 3.877   18.104  33.625  0.50 20.17 ? 1054 ARG H NH1 1 
ATOM   3162 N NH2 A ARG B 1 188 ? 8.204   17.011  34.008  0.50 15.71 ? 1054 ARG H NH2 1 
ATOM   3163 N NH2 B ARG B 1 188 ? 6.104   17.615  33.712  0.50 24.04 ? 1054 ARG H NH2 1 
ATOM   3164 N N   . HIS B 1 189 ? 7.782   17.515  27.290  1.00 18.17 ? 1055 HIS H N   1 
ATOM   3165 C CA  . HIS B 1 189 ? 9.138   17.475  26.714  1.00 19.89 ? 1055 HIS H CA  1 
ATOM   3166 C C   . HIS B 1 189 ? 10.214  17.780  27.768  1.00 19.80 ? 1055 HIS H C   1 
ATOM   3167 O O   . HIS B 1 189 ? 9.988   18.606  28.716  1.00 19.04 ? 1055 HIS H O   1 
ATOM   3168 C CB  . HIS B 1 189 ? 9.191   18.467  25.556  1.00 21.14 ? 1055 HIS H CB  1 
ATOM   3169 C CG  . HIS B 1 189 ? 10.410  18.268  24.740  1.00 21.42 ? 1055 HIS H CG  1 
ATOM   3170 N ND1 . HIS B 1 189 ? 11.165  19.288  24.249  1.00 23.78 ? 1055 HIS H ND1 1 
ATOM   3171 C CD2 . HIS B 1 189 ? 11.003  17.139  24.333  1.00 22.51 ? 1055 HIS H CD2 1 
ATOM   3172 C CE1 . HIS B 1 189 ? 12.163  18.772  23.538  1.00 22.37 ? 1055 HIS H CE1 1 
ATOM   3173 N NE2 . HIS B 1 189 ? 12.084  17.488  23.591  1.00 23.08 ? 1055 HIS H NE2 1 
ATOM   3174 N N   . THR B 1 190 ? 11.392  17.182  27.600  1.00 21.82 ? 1056 THR H N   1 
ATOM   3175 C CA  . THR B 1 190 ? 12.534  17.377  28.518  1.00 23.77 ? 1056 THR H CA  1 
ATOM   3176 C C   . THR B 1 190 ? 12.746  18.863  28.790  1.00 22.55 ? 1056 THR H C   1 
ATOM   3177 O O   . THR B 1 190 ? 12.849  19.584  27.810  1.00 22.75 ? 1056 THR H O   1 
ATOM   3178 C CB  . THR B 1 190 ? 13.838  16.862  27.899  1.00 26.89 ? 1056 THR H CB  1 
ATOM   3179 O OG1 . THR B 1 190 ? 13.641  15.488  27.560  1.00 29.22 ? 1056 THR H OG1 1 
ATOM   3180 C CG2 . THR B 1 190 ? 14.984  17.037  28.862  1.00 27.73 ? 1056 THR H CG2 1 
ATOM   3181 N N   . GLY B 1 191 ? 12.839  19.298  30.049  1.00 23.78 ? 1057 GLY H N   1 
ATOM   3182 C CA  . GLY B 1 191 ? 13.236  20.686  30.359  1.00 23.85 ? 1057 GLY H CA  1 
ATOM   3183 C C   . GLY B 1 191 ? 12.077  21.652  30.410  1.00 23.10 ? 1057 GLY H C   1 
ATOM   3184 O O   . GLY B 1 191 ? 12.279  22.770  30.886  1.00 25.27 ? 1057 GLY H O   1 
ATOM   3185 N N   . VAL B 1 192 ? 10.880  21.240  30.012  1.00 19.79 ? 1058 VAL H N   1 
ATOM   3186 C CA  . VAL B 1 192 ? 9.677   22.101  30.091  1.00 19.33 ? 1058 VAL H CA  1 
ATOM   3187 C C   . VAL B 1 192 ? 9.269   22.169  31.551  1.00 19.21 ? 1058 VAL H C   1 
ATOM   3188 O O   . VAL B 1 192 ? 9.312   21.138  32.236  1.00 19.04 ? 1058 VAL H O   1 
ATOM   3189 C CB  . VAL B 1 192 ? 8.558   21.529  29.220  1.00 19.05 ? 1058 VAL H CB  1 
ATOM   3190 C CG1 . VAL B 1 192 ? 7.247   22.253  29.413  1.00 19.52 ? 1058 VAL H CG1 1 
ATOM   3191 C CG2 . VAL B 1 192 ? 9.001   21.533  27.755  1.00 18.37 ? 1058 VAL H CG2 1 
ATOM   3192 N N   . PRO B 1 193 ? 8.930   23.365  32.062  1.00 20.09 ? 1059 PRO H N   1 
ATOM   3193 C CA  . PRO B 1 193 ? 8.468   23.477  33.439  1.00 19.96 ? 1059 PRO H CA  1 
ATOM   3194 C C   . PRO B 1 193 ? 7.302   22.549  33.778  1.00 19.35 ? 1059 PRO H C   1 
ATOM   3195 O O   . PRO B 1 193 ? 6.398   22.296  32.971  1.00 16.82 ? 1059 PRO H O   1 
ATOM   3196 C CB  . PRO B 1 193 ? 8.091   24.961  33.588  1.00 20.50 ? 1059 PRO H CB  1 
ATOM   3197 C CG  . PRO B 1 193 ? 8.988   25.641  32.586  1.00 20.92 ? 1059 PRO H CG  1 
ATOM   3198 C CD  . PRO B 1 193 ? 9.012   24.682  31.416  1.00 20.49 ? 1059 PRO H CD  1 
ATOM   3199 N N   . ASP B 1 194 ? 7.349   22.036  35.020  1.00 19.55 ? 1060 ASP H N   1 
ATOM   3200 C CA  . ASP B 1 194 ? 6.395   21.039  35.541  1.00 20.01 ? 1060 ASP H CA  1 
ATOM   3201 C C   . ASP B 1 194 ? 4.958   21.519  35.360  1.00 19.45 ? 1060 ASP H C   1 
ATOM   3202 O O   . ASP B 1 194 ? 4.072   20.662  35.191  1.00 20.50 ? 1060 ASP H O   1 
ATOM   3203 C CB  . ASP B 1 194 ? 6.636   20.780  37.038  1.00 20.34 ? 1060 ASP H CB  1 
ATOM   3204 C CG  . ASP B 1 194 ? 7.943   20.081  37.312  1.00 21.81 ? 1060 ASP H CG  1 
ATOM   3205 O OD1 . ASP B 1 194 ? 8.360   19.329  36.419  1.00 19.29 ? 1060 ASP H OD1 1 
ATOM   3206 O OD2 . ASP B 1 194 ? 8.466   20.201  38.467  1.00 20.54 ? 1060 ASP H OD2 1 
ATOM   3207 N N   . ARG B 1 195 ? 4.720   22.827  35.437  1.00 19.71 ? 1061 ARG H N   1 
ATOM   3208 C CA  . ARG B 1 195 ? 3.332   23.402  35.424  1.00 19.05 ? 1061 ARG H CA  1 
ATOM   3209 C C   . ARG B 1 195 ? 2.624   23.229  34.071  1.00 19.20 ? 1061 ARG H C   1 
ATOM   3210 O O   . ARG B 1 195 ? 1.427   23.522  34.028  1.00 18.02 ? 1061 ARG H O   1 
ATOM   3211 C CB  . ARG B 1 195 ? 3.390   24.870  35.845  1.00 18.85 ? 1061 ARG H CB  1 
ATOM   3212 C CG  . ARG B 1 195 ? 4.087   25.806  34.864  1.00 18.76 ? 1061 ARG H CG  1 
ATOM   3213 C CD  . ARG B 1 195 ? 4.235   27.196  35.448  1.00 19.07 ? 1061 ARG H CD  1 
ATOM   3214 N NE  . ARG B 1 195 ? 5.043   28.093  34.617  1.00 19.13 ? 1061 ARG H NE  1 
ATOM   3215 C CZ  . ARG B 1 195 ? 6.359   28.241  34.718  1.00 19.27 ? 1061 ARG H CZ  1 
ATOM   3216 N NH1 . ARG B 1 195 ? 7.069   27.506  35.542  1.00 18.19 ? 1061 ARG H NH1 1 
ATOM   3217 N NH2 . ARG B 1 195 ? 6.999   29.093  33.927  1.00 19.25 ? 1061 ARG H NH2 1 
ATOM   3218 N N   . PHE B 1 196 ? 3.316   22.807  33.005  1.00 17.87 ? 1062 PHE H N   1 
ATOM   3219 C CA  . PHE B 1 196 ? 2.669   22.562  31.682  1.00 18.88 ? 1062 PHE H CA  1 
ATOM   3220 C C   . PHE B 1 196 ? 2.196   21.115  31.632  1.00 18.14 ? 1062 PHE H C   1 
ATOM   3221 O O   . PHE B 1 196 ? 2.984   20.191  31.835  1.00 18.31 ? 1062 PHE H O   1 
ATOM   3222 C CB  . PHE B 1 196 ? 3.637   22.824  30.532  1.00 17.69 ? 1062 PHE H CB  1 
ATOM   3223 C CG  . PHE B 1 196 ? 3.986   24.280  30.370  1.00 17.55 ? 1062 PHE H CG  1 
ATOM   3224 C CD1 . PHE B 1 196 ? 5.011   24.864  31.110  1.00 18.41 ? 1062 PHE H CD1 1 
ATOM   3225 C CD2 . PHE B 1 196 ? 3.253   25.075  29.510  1.00 17.57 ? 1062 PHE H CD2 1 
ATOM   3226 C CE1 . PHE B 1 196 ? 5.319   26.212  30.941  1.00 18.79 ? 1062 PHE H CE1 1 
ATOM   3227 C CE2 . PHE B 1 196 ? 3.563   26.404  29.335  1.00 18.59 ? 1062 PHE H CE2 1 
ATOM   3228 C CZ  . PHE B 1 196 ? 4.583   26.975  30.050  1.00 18.53 ? 1062 PHE H CZ  1 
ATOM   3229 N N   . THR B 1 197 ? 0.896   20.924  31.416  1.00 18.51 ? 1063 THR H N   1 
ATOM   3230 C CA  . THR B 1 197 ? 0.301   19.578  31.221  1.00 18.79 ? 1063 THR H CA  1 
ATOM   3231 C C   . THR B 1 197 ? -0.569  19.591  29.978  1.00 18.49 ? 1063 THR H C   1 
ATOM   3232 O O   . THR B 1 197 ? -0.990  20.699  29.515  1.00 19.73 ? 1063 THR H O   1 
ATOM   3233 C CB  . THR B 1 197 ? -0.469  19.064  32.441  1.00 18.59 ? 1063 THR H CB  1 
ATOM   3234 O OG1 . THR B 1 197 ? -1.466  20.042  32.747  1.00 18.25 ? 1063 THR H OG1 1 
ATOM   3235 C CG2 . THR B 1 197 ? 0.486   18.828  33.607  1.00 19.78 ? 1063 THR H CG2 1 
ATOM   3236 N N   . GLY B 1 198 ? -0.777  18.414  29.419  1.00 19.07 ? 1064 GLY H N   1 
ATOM   3237 C CA  . GLY B 1 198 ? -1.719  18.283  28.294  1.00 18.55 ? 1064 GLY H CA  1 
ATOM   3238 C C   . GLY B 1 198 ? -2.709  17.189  28.533  1.00 18.35 ? 1064 GLY H C   1 
ATOM   3239 O O   . GLY B 1 198 ? -2.390  16.209  29.194  1.00 17.79 ? 1064 GLY H O   1 
ATOM   3240 N N   . SER B 1 199 ? -3.868  17.292  27.917  1.00 19.63 ? 1065 SER H N   1 
ATOM   3241 C CA  . SER B 1 199 ? -4.868  16.220  27.970  1.00 20.98 ? 1065 SER H CA  1 
ATOM   3242 C C   . SER B 1 199 ? -5.636  16.180  26.655  1.00 20.21 ? 1065 SER H C   1 
ATOM   3243 O O   . SER B 1 199 ? -5.574  17.147  25.806  1.00 20.67 ? 1065 SER H O   1 
ATOM   3244 C CB  . SER B 1 199 ? -5.827  16.426  29.116  1.00 20.76 ? 1065 SER H CB  1 
ATOM   3245 O OG  . SER B 1 199 ? -6.390  17.709  28.929  1.00 22.23 ? 1065 SER H OG  1 
ATOM   3246 N N   . GLY B 1 200 ? -6.334  15.082  26.476  1.00 21.01 ? 1066 GLY H N   1 
ATOM   3247 C CA  . GLY B 1 200 ? -7.248  14.957  25.331  1.00 21.56 ? 1066 GLY H CA  1 
ATOM   3248 C C   . GLY B 1 200 ? -6.923  13.758  24.454  1.00 22.13 ? 1066 GLY H C   1 
ATOM   3249 O O   . GLY B 1 200 ? -5.840  13.144  24.514  1.00 21.22 ? 1066 GLY H O   1 
ATOM   3250 N N   . SER B 1 201 ? -7.904  13.416  23.656  1.00 22.30 ? 1067 SER H N   1 
ATOM   3251 C CA  A SER B 1 201 ? -7.791  12.364  22.625  0.50 22.35 ? 1067 SER H CA  1 
ATOM   3252 C CA  B SER B 1 201 ? -7.867  12.282  22.706  0.50 22.60 ? 1067 SER H CA  1 
ATOM   3253 C C   . SER B 1 201 ? -8.963  12.534  21.667  1.00 23.44 ? 1067 SER H C   1 
ATOM   3254 O O   . SER B 1 201 ? -9.970  13.181  22.075  1.00 25.73 ? 1067 SER H O   1 
ATOM   3255 C CB  A SER B 1 201 ? -7.816  11.000  23.248  0.50 22.86 ? 1067 SER H CB  1 
ATOM   3256 C CB  B SER B 1 201 ? -8.087  10.987  23.460  0.50 23.29 ? 1067 SER H CB  1 
ATOM   3257 O OG  A SER B 1 201 ? -9.079  10.769  23.853  0.50 22.45 ? 1067 SER H OG  1 
ATOM   3258 O OG  B SER B 1 201 ? -8.000  9.856   22.603  0.50 22.99 ? 1067 SER H OG  1 
ATOM   3259 N N   . GLY B 1 202 ? -8.822  11.990  20.479  1.00 21.82 ? 1068 GLY H N   1 
ATOM   3260 C CA  . GLY B 1 202 ? -9.893  12.044  19.482  1.00 22.47 ? 1068 GLY H CA  1 
ATOM   3261 C C   . GLY B 1 202 ? -9.887  13.416  18.831  1.00 21.51 ? 1068 GLY H C   1 
ATOM   3262 O O   . GLY B 1 202 ? -9.072  13.641  17.947  1.00 20.77 ? 1068 GLY H O   1 
ATOM   3263 N N   . THR B 1 203 ? -10.781 14.304  19.244  1.00 23.61 ? 1069 THR H N   1 
ATOM   3264 C CA  . THR B 1 203 ? -10.950 15.624  18.585  1.00 24.01 ? 1069 THR H CA  1 
ATOM   3265 C C   . THR B 1 203 ? -10.769 16.774  19.568  1.00 24.86 ? 1069 THR H C   1 
ATOM   3266 O O   . THR B 1 203 ? -10.772 17.932  19.095  1.00 27.13 ? 1069 THR H O   1 
ATOM   3267 C CB  . THR B 1 203 ? -12.303 15.716  17.873  1.00 25.28 ? 1069 THR H CB  1 
ATOM   3268 O OG1 . THR B 1 203 ? -13.318 15.614  18.879  1.00 25.15 ? 1069 THR H OG1 1 
ATOM   3269 C CG2 . THR B 1 203 ? -12.471 14.636  16.836  1.00 26.81 ? 1069 THR H CG2 1 
ATOM   3270 N N   . ASP B 1 204 ? -10.599 16.529  20.862  1.00 24.27 ? 1070 ASP H N   1 
ATOM   3271 C CA  . ASP B 1 204 ? -10.591 17.652  21.837  1.00 24.59 ? 1070 ASP H CA  1 
ATOM   3272 C C   . ASP B 1 204 ? -9.283  17.598  22.609  1.00 22.97 ? 1070 ASP H C   1 
ATOM   3273 O O   . ASP B 1 204 ? -9.011  16.543  23.222  1.00 22.04 ? 1070 ASP H O   1 
ATOM   3274 C CB  . ASP B 1 204 ? -11.774 17.632  22.790  1.00 27.13 ? 1070 ASP H CB  1 
ATOM   3275 C CG  . ASP B 1 204 ? -13.090 17.789  22.059  1.00 31.97 ? 1070 ASP H CG  1 
ATOM   3276 O OD1 . ASP B 1 204 ? -13.245 18.811  21.348  1.00 34.25 ? 1070 ASP H OD1 1 
ATOM   3277 O OD2 . ASP B 1 204 ? -13.840 16.801  22.088  1.00 37.32 ? 1070 ASP H OD2 1 
ATOM   3278 N N   . PHE B 1 205 ? -8.549  18.698  22.596  1.00 20.55 ? 1071 PHE H N   1 
ATOM   3279 C CA  . PHE B 1 205 ? -7.248  18.769  23.301  1.00 19.91 ? 1071 PHE H CA  1 
ATOM   3280 C C   . PHE B 1 205 ? -7.158  20.051  24.103  1.00 20.28 ? 1071 PHE H C   1 
ATOM   3281 O O   . PHE B 1 205 ? -7.734  21.117  23.706  1.00 21.07 ? 1071 PHE H O   1 
ATOM   3282 C CB  . PHE B 1 205 ? -6.106  18.643  22.279  1.00 19.21 ? 1071 PHE H CB  1 
ATOM   3283 C CG  . PHE B 1 205 ? -6.190  17.366  21.514  1.00 19.40 ? 1071 PHE H CG  1 
ATOM   3284 C CD1 . PHE B 1 205 ? -5.577  16.199  21.973  1.00 19.51 ? 1071 PHE H CD1 1 
ATOM   3285 C CD2 . PHE B 1 205 ? -6.980  17.299  20.388  1.00 20.24 ? 1071 PHE H CD2 1 
ATOM   3286 C CE1 . PHE B 1 205 ? -5.776  15.000  21.320  1.00 20.51 ? 1071 PHE H CE1 1 
ATOM   3287 C CE2 . PHE B 1 205 ? -7.169  16.090  19.734  1.00 20.81 ? 1071 PHE H CE2 1 
ATOM   3288 C CZ  . PHE B 1 205 ? -6.542  14.953  20.183  1.00 19.61 ? 1071 PHE H CZ  1 
ATOM   3289 N N   . THR B 1 206 ? -6.427  19.961  25.219  1.00 19.17 ? 1072 THR H N   1 
ATOM   3290 C CA  . THR B 1 206 ? -6.192  21.096  26.129  1.00 19.48 ? 1072 THR H CA  1 
ATOM   3291 C C   . THR B 1 206 ? -4.729  21.127  26.568  1.00 19.26 ? 1072 THR H C   1 
ATOM   3292 O O   . THR B 1 206 ? -4.236  20.102  27.044  1.00 21.24 ? 1072 THR H O   1 
ATOM   3293 C CB  . THR B 1 206 ? -7.071  21.045  27.377  1.00 20.94 ? 1072 THR H CB  1 
ATOM   3294 O OG1 . THR B 1 206 ? -8.435  20.961  26.926  1.00 23.32 ? 1072 THR H OG1 1 
ATOM   3295 C CG2 . THR B 1 206 ? -6.853  22.259  28.238  1.00 20.99 ? 1072 THR H CG2 1 
ATOM   3296 N N   . LEU B 1 207 ? -4.134  22.312  26.472  1.00 18.87 ? 1073 LEU H N   1 
ATOM   3297 C CA  . LEU B 1 207 ? -2.864  22.637  27.175  1.00 19.25 ? 1073 LEU H CA  1 
ATOM   3298 C C   . LEU B 1 207 ? -3.229  23.368  28.450  1.00 19.28 ? 1073 LEU H C   1 
ATOM   3299 O O   . LEU B 1 207 ? -3.922  24.399  28.346  1.00 19.62 ? 1073 LEU H O   1 
ATOM   3300 C CB  . LEU B 1 207 ? -1.988  23.512  26.290  1.00 18.90 ? 1073 LEU H CB  1 
ATOM   3301 C CG  . LEU B 1 207 ? -0.699  24.017  26.938  1.00 19.38 ? 1073 LEU H CG  1 
ATOM   3302 C CD1 . LEU B 1 207 ? 0.302   22.900  27.115  1.00 18.52 ? 1073 LEU H CD1 1 
ATOM   3303 C CD2 . LEU B 1 207 ? -0.084  25.117  26.103  1.00 19.08 ? 1073 LEU H CD2 1 
ATOM   3304 N N   . THR B 1 208 ? -2.784  22.838  29.599  1.00 19.75 ? 1074 THR H N   1 
ATOM   3305 C CA  . THR B 1 208 ? -3.015  23.508  30.900  1.00 20.15 ? 1074 THR H CA  1 
ATOM   3306 C C   . THR B 1 208 ? -1.696  24.073  31.392  1.00 19.70 ? 1074 THR H C   1 
ATOM   3307 O O   . THR B 1 208 ? -0.680  23.353  31.345  1.00 19.52 ? 1074 THR H O   1 
ATOM   3308 C CB  . THR B 1 208 ? -3.690  22.575  31.897  1.00 20.09 ? 1074 THR H CB  1 
ATOM   3309 O OG1 . THR B 1 208 ? -4.912  22.148  31.286  1.00 20.89 ? 1074 THR H OG1 1 
ATOM   3310 C CG2 . THR B 1 208 ? -3.955  23.255  33.230  1.00 21.79 ? 1074 THR H CG2 1 
ATOM   3311 N N   . ILE B 1 209 ? -1.726  25.335  31.818  1.00 20.70 ? 1075 ILE H N   1 
ATOM   3312 C CA  . ILE B 1 209 ? -0.583  25.963  32.512  1.00 19.83 ? 1075 ILE H CA  1 
ATOM   3313 C C   . ILE B 1 209 ? -1.079  26.254  33.912  1.00 20.64 ? 1075 ILE H C   1 
ATOM   3314 O O   . ILE B 1 209 ? -1.883  27.164  34.043  1.00 22.09 ? 1075 ILE H O   1 
ATOM   3315 C CB  . ILE B 1 209 ? -0.040  27.218  31.817  1.00 20.41 ? 1075 ILE H CB  1 
ATOM   3316 C CG1 . ILE B 1 209 ? 0.085   27.020  30.304  1.00 20.56 ? 1075 ILE H CG1 1 
ATOM   3317 C CG2 . ILE B 1 209 ? 1.316   27.574  32.425  1.00 19.93 ? 1075 ILE H CG2 1 
ATOM   3318 C CD1 . ILE B 1 209 ? 0.443   28.301  29.543  1.00 21.63 ? 1075 ILE H CD1 1 
ATOM   3319 N N   . SER B 1 210 ? -0.675  25.438  34.878  1.00 19.46 ? 1076 SER H N   1 
ATOM   3320 C CA  . SER B 1 210 ? -0.973  25.661  36.318  1.00 19.54 ? 1076 SER H CA  1 
ATOM   3321 C C   . SER B 1 210 ? -0.055  26.772  36.837  1.00 19.21 ? 1076 SER H C   1 
ATOM   3322 O O   . SER B 1 210 ? 1.135   26.863  36.367  1.00 19.38 ? 1076 SER H O   1 
ATOM   3323 C CB  . SER B 1 210 ? -0.833  24.386  37.111  1.00 20.77 ? 1076 SER H CB  1 
ATOM   3324 O OG  . SER B 1 210 ? -1.766  23.422  36.667  1.00 22.45 ? 1076 SER H OG  1 
ATOM   3325 N N   . ASN B 1 211 ? -0.532  27.565  37.792  1.00 18.48 ? 1077 ASN H N   1 
ATOM   3326 C CA  . ASN B 1 211 ? 0.341   28.565  38.466  1.00 18.24 ? 1077 ASN H CA  1 
ATOM   3327 C C   . ASN B 1 211 ? 1.103   29.389  37.420  1.00 18.32 ? 1077 ASN H C   1 
ATOM   3328 O O   . ASN B 1 211 ? 2.338   29.484  37.458  1.00 17.86 ? 1077 ASN H O   1 
ATOM   3329 C CB  . ASN B 1 211 ? 1.271   27.839  39.439  1.00 18.01 ? 1077 ASN H CB  1 
ATOM   3330 C CG  . ASN B 1 211 ? 1.940   28.731  40.460  1.00 18.92 ? 1077 ASN H CG  1 
ATOM   3331 O OD1 . ASN B 1 211 ? 2.821   28.263  41.240  1.00 19.93 ? 1077 ASN H OD1 1 
ATOM   3332 N ND2 . ASN B 1 211 ? 1.499   29.951  40.510  1.00 16.89 ? 1077 ASN H ND2 1 
ATOM   3333 N N   . VAL B 1 212 ? 0.388   29.944  36.454  1.00 19.52 ? 1078 VAL H N   1 
ATOM   3334 C CA  . VAL B 1 212 ? 1.005   30.631  35.287  1.00 19.73 ? 1078 VAL H CA  1 
ATOM   3335 C C   . VAL B 1 212 ? 1.883   31.797  35.743  1.00 20.16 ? 1078 VAL H C   1 
ATOM   3336 O O   . VAL B 1 212 ? 1.500   32.526  36.684  1.00 19.73 ? 1078 VAL H O   1 
ATOM   3337 C CB  . VAL B 1 212 ? -0.079  31.061  34.291  1.00 20.89 ? 1078 VAL H CB  1 
ATOM   3338 C CG1 . VAL B 1 212 ? -0.947  32.174  34.820  1.00 21.68 ? 1078 VAL H CG1 1 
ATOM   3339 C CG2 . VAL B 1 212 ? 0.509   31.451  32.947  1.00 21.43 ? 1078 VAL H CG2 1 
ATOM   3340 N N   . GLN B 1 213 ? 3.053   31.924  35.108  1.00 19.31 ? 1079 GLN H N   1 
ATOM   3341 C CA  . GLN B 1 213 ? 4.036   32.994  35.384  1.00 19.70 ? 1079 GLN H CA  1 
ATOM   3342 C C   . GLN B 1 213 ? 4.135   33.968  34.196  1.00 21.43 ? 1079 GLN H C   1 
ATOM   3343 O O   . GLN B 1 213 ? 3.737   33.619  33.082  1.00 19.52 ? 1079 GLN H O   1 
ATOM   3344 C CB  . GLN B 1 213 ? 5.390   32.381  35.705  1.00 19.15 ? 1079 GLN H CB  1 
ATOM   3345 C CG  . GLN B 1 213 ? 5.334   31.432  36.923  1.00 19.83 ? 1079 GLN H CG  1 
ATOM   3346 C CD  . GLN B 1 213 ? 4.866   32.137  38.174  1.00 20.03 ? 1079 GLN H CD  1 
ATOM   3347 O OE1 . GLN B 1 213 ? 5.434   33.141  38.587  1.00 21.09 ? 1079 GLN H OE1 1 
ATOM   3348 N NE2 . GLN B 1 213 ? 3.765   31.672  38.733  1.00 19.72 ? 1079 GLN H NE2 1 
ATOM   3349 N N   . SER B 1 214 ? 4.644   35.182  34.453  1.00 23.15 ? 1080 SER H N   1 
ATOM   3350 C CA  . SER B 1 214 ? 4.817   36.227  33.418  1.00 24.97 ? 1080 SER H CA  1 
ATOM   3351 C C   . SER B 1 214 ? 5.704   35.690  32.269  1.00 25.42 ? 1080 SER H C   1 
ATOM   3352 O O   . SER B 1 214 ? 5.464   36.064  31.123  1.00 25.32 ? 1080 SER H O   1 
ATOM   3353 C CB  . SER B 1 214 ? 5.331   37.519  34.031  1.00 28.02 ? 1080 SER H CB  1 
ATOM   3354 O OG  . SER B 1 214 ? 6.603   37.305  34.589  1.00 31.02 ? 1080 SER H OG  1 
ATOM   3355 N N   . GLU B 1 215 ? 6.651   34.787  32.513  1.00 24.02 ? 1081 GLU H N   1 
ATOM   3356 C CA  . GLU B 1 215 ? 7.518   34.270  31.416  1.00 24.22 ? 1081 GLU H CA  1 
ATOM   3357 C C   . GLU B 1 215 ? 6.693   33.360  30.472  1.00 21.79 ? 1081 GLU H C   1 
ATOM   3358 O O   . GLU B 1 215 ? 7.190   33.030  29.425  1.00 22.26 ? 1081 GLU H O   1 
ATOM   3359 C CB  . GLU B 1 215 ? 8.724   33.516  31.962  1.00 24.62 ? 1081 GLU H CB  1 
ATOM   3360 C CG  . GLU B 1 215 ? 8.365   32.218  32.631  1.00 26.01 ? 1081 GLU H CG  1 
ATOM   3361 C CD  . GLU B 1 215 ? 9.581   31.366  32.967  1.00 30.00 ? 1081 GLU H CD  1 
ATOM   3362 O OE1 . GLU B 1 215 ? 9.527   30.580  33.948  1.00 29.64 ? 1081 GLU H OE1 1 
ATOM   3363 O OE2 . GLU B 1 215 ? 10.524  31.380  32.168  1.00 30.84 ? 1081 GLU H OE2 1 
ATOM   3364 N N   . ASP B 1 216 ? 5.477   32.980  30.862  1.00 20.42 ? 1082 ASP H N   1 
ATOM   3365 C CA  . ASP B 1 216 ? 4.579   32.085  30.083  1.00 20.15 ? 1082 ASP H CA  1 
ATOM   3366 C C   . ASP B 1 216 ? 3.685   32.891  29.121  1.00 21.53 ? 1082 ASP H C   1 
ATOM   3367 O O   . ASP B 1 216 ? 2.942   32.273  28.319  1.00 21.13 ? 1082 ASP H O   1 
ATOM   3368 C CB  . ASP B 1 216 ? 3.704   31.228  30.985  1.00 19.25 ? 1082 ASP H CB  1 
ATOM   3369 C CG  . ASP B 1 216 ? 4.450   30.369  31.982  1.00 19.67 ? 1082 ASP H CG  1 
ATOM   3370 O OD1 . ASP B 1 216 ? 5.623   30.008  31.686  1.00 18.57 ? 1082 ASP H OD1 1 
ATOM   3371 O OD2 . ASP B 1 216 ? 3.869   30.105  33.081  1.00 19.04 ? 1082 ASP H OD2 1 
ATOM   3372 N N   . LEU B 1 217 ? 3.743   34.219  29.162  1.00 22.61 ? 1083 LEU H N   1 
ATOM   3373 C CA  . LEU B 1 217 ? 2.965   35.065  28.203  1.00 24.03 ? 1083 LEU H CA  1 
ATOM   3374 C C   . LEU B 1 217 ? 3.643   34.928  26.844  1.00 24.78 ? 1083 LEU H C   1 
ATOM   3375 O O   . LEU B 1 217 ? 4.864   35.141  26.746  1.00 27.28 ? 1083 LEU H O   1 
ATOM   3376 C CB  . LEU B 1 217 ? 2.957   36.503  28.725  1.00 26.38 ? 1083 LEU H CB  1 
ATOM   3377 C CG  . LEU B 1 217 ? 2.318   36.669  30.099  1.00 28.07 ? 1083 LEU H CG  1 
ATOM   3378 C CD1 . LEU B 1 217 ? 2.374   38.119  30.552  1.00 31.48 ? 1083 LEU H CD1 1 
ATOM   3379 C CD2 . LEU B 1 217 ? 0.885   36.147  30.123  1.00 28.61 ? 1083 LEU H CD2 1 
ATOM   3380 N N   . ALA B 1 218 ? 2.918   34.443  25.850  1.00 23.75 ? 1084 ALA H N   1 
ATOM   3381 C CA  . ALA B 1 218 ? 3.486   33.954  24.578  1.00 24.03 ? 1084 ALA H CA  1 
ATOM   3382 C C   . ALA B 1 218 ? 2.333   33.500  23.701  1.00 23.58 ? 1084 ALA H C   1 
ATOM   3383 O O   . ALA B 1 218 ? 1.196   33.476  24.213  1.00 22.63 ? 1084 ALA H O   1 
ATOM   3384 C CB  . ALA B 1 218 ? 4.418   32.779  24.826  1.00 24.06 ? 1084 ALA H CB  1 
ATOM   3385 N N   . ASP B 1 219 ? 2.641   33.097  22.467  1.00 23.81 ? 1085 ASP H N   1 
ATOM   3386 C CA  . ASP B 1 219 ? 1.659   32.411  21.594  1.00 23.75 ? 1085 ASP H CA  1 
ATOM   3387 C C   . ASP B 1 219 ? 1.778   30.907  21.802  1.00 22.16 ? 1085 ASP H C   1 
ATOM   3388 O O   . ASP B 1 219 ? 2.890   30.432  21.999  1.00 22.92 ? 1085 ASP H O   1 
ATOM   3389 C CB  . ASP B 1 219 ? 1.863   32.738  20.124  1.00 26.64 ? 1085 ASP H CB  1 
ATOM   3390 C CG  . ASP B 1 219 ? 1.596   34.201  19.757  1.00 30.00 ? 1085 ASP H CG  1 
ATOM   3391 O OD1 . ASP B 1 219 ? 0.833   34.872  20.449  1.00 32.94 ? 1085 ASP H OD1 1 
ATOM   3392 O OD2 . ASP B 1 219 ? 2.224   34.673  18.807  1.00 34.47 ? 1085 ASP H OD2 1 
ATOM   3393 N N   . TYR B 1 220 ? 0.656   30.218  21.757  1.00 20.64 ? 1086 TYR H N   1 
ATOM   3394 C CA  . TYR B 1 220 ? 0.590   28.728  21.906  1.00 20.33 ? 1086 TYR H CA  1 
ATOM   3395 C C   . TYR B 1 220 ? -0.121  28.170  20.691  1.00 20.00 ? 1086 TYR H C   1 
ATOM   3396 O O   . TYR B 1 220 ? -1.176  28.684  20.324  1.00 20.51 ? 1086 TYR H O   1 
ATOM   3397 C CB  . TYR B 1 220 ? -0.085  28.352  23.220  1.00 19.61 ? 1086 TYR H CB  1 
ATOM   3398 C CG  . TYR B 1 220 ? 0.741   28.754  24.410  1.00 19.80 ? 1086 TYR H CG  1 
ATOM   3399 C CD1 . TYR B 1 220 ? 0.614   30.013  24.989  1.00 19.59 ? 1086 TYR H CD1 1 
ATOM   3400 C CD2 . TYR B 1 220 ? 1.719   27.900  24.905  1.00 19.06 ? 1086 TYR H CD2 1 
ATOM   3401 C CE1 . TYR B 1 220 ? 1.413   30.377  26.068  1.00 20.56 ? 1086 TYR H CE1 1 
ATOM   3402 C CE2 . TYR B 1 220 ? 2.504   28.259  25.988  1.00 18.67 ? 1086 TYR H CE2 1 
ATOM   3403 C CZ  . TYR B 1 220 ? 2.337   29.486  26.596  1.00 19.07 ? 1086 TYR H CZ  1 
ATOM   3404 O OH  . TYR B 1 220 ? 3.211   29.799  27.621  1.00 18.94 ? 1086 TYR H OH  1 
ATOM   3405 N N   . PHE B 1 221 ? 0.439   27.101  20.105  1.00 20.15 ? 1087 PHE H N   1 
ATOM   3406 C CA  . PHE B 1 221 ? -0.097  26.448  18.885  1.00 21.41 ? 1087 PHE H CA  1 
ATOM   3407 C C   . PHE B 1 221 ? -0.209  24.955  19.183  1.00 20.51 ? 1087 PHE H C   1 
ATOM   3408 O O   . PHE B 1 221 ? 0.766   24.385  19.664  1.00 19.59 ? 1087 PHE H O   1 
ATOM   3409 C CB  . PHE B 1 221 ? 0.834   26.651  17.690  1.00 22.09 ? 1087 PHE H CB  1 
ATOM   3410 C CG  . PHE B 1 221 ? 0.962   28.059  17.200  1.00 25.52 ? 1087 PHE H CG  1 
ATOM   3411 C CD1 . PHE B 1 221 ? 1.996   28.878  17.610  1.00 25.79 ? 1087 PHE H CD1 1 
ATOM   3412 C CD2 . PHE B 1 221 ? 0.029   28.573  16.319  1.00 26.21 ? 1087 PHE H CD2 1 
ATOM   3413 C CE1 . PHE B 1 221 ? 2.088   30.179  17.137  1.00 26.46 ? 1087 PHE H CE1 1 
ATOM   3414 C CE2 . PHE B 1 221 ? 0.120   29.870  15.846  1.00 27.32 ? 1087 PHE H CE2 1 
ATOM   3415 C CZ  . PHE B 1 221 ? 1.139   30.680  16.279  1.00 27.26 ? 1087 PHE H CZ  1 
ATOM   3416 N N   . CYS B 1 222 ? -1.325  24.335  18.827  1.00 21.58 ? 1088 CYS H N   1 
ATOM   3417 C CA  . CYS B 1 222 ? -1.431  22.847  18.768  1.00 22.05 ? 1088 CYS H CA  1 
ATOM   3418 C C   . CYS B 1 222 ? -0.984  22.404  17.376  1.00 21.10 ? 1088 CYS H C   1 
ATOM   3419 O O   . CYS B 1 222 ? -1.050  23.186  16.382  1.00 20.86 ? 1088 CYS H O   1 
ATOM   3420 C CB  . CYS B 1 222 ? -2.825  22.302  19.098  1.00 25.40 ? 1088 CYS H CB  1 
ATOM   3421 S SG  . CYS B 1 222 ? -4.033  23.056  18.006  1.00 30.98 ? 1088 CYS H SG  1 
ATOM   3422 N N   . GLN B 1 223 ? -0.578  21.160  17.269  1.00 19.74 ? 1089 GLN H N   1 
ATOM   3423 C CA  . GLN B 1 223 ? -0.255  20.519  15.972  1.00 20.16 ? 1089 GLN H CA  1 
ATOM   3424 C C   . GLN B 1 223 ? -0.782  19.089  16.039  1.00 19.75 ? 1089 GLN H C   1 
ATOM   3425 O O   . GLN B 1 223 ? -0.504  18.430  17.025  1.00 19.39 ? 1089 GLN H O   1 
ATOM   3426 C CB  . GLN B 1 223 ? 1.255   20.526  15.741  1.00 20.92 ? 1089 GLN H CB  1 
ATOM   3427 C CG  . GLN B 1 223 ? 1.602   19.950  14.376  1.00 22.98 ? 1089 GLN H CG  1 
ATOM   3428 C CD  . GLN B 1 223 ? 3.075   19.753  14.168  1.00 24.77 ? 1089 GLN H CD  1 
ATOM   3429 O OE1 . GLN B 1 223 ? 3.895   19.885  15.056  1.00 23.53 ? 1089 GLN H OE1 1 
ATOM   3430 N NE2 . GLN B 1 223 ? 3.410   19.432  12.947  1.00 29.94 ? 1089 GLN H NE2 1 
ATOM   3431 N N   . GLN B 1 224 ? -1.379  18.576  14.967  1.00 19.19 ? 1090 GLN H N   1 
ATOM   3432 C CA  . GLN B 1 224 ? -1.600  17.110  14.879  1.00 18.74 ? 1090 GLN H CA  1 
ATOM   3433 C C   . GLN B 1 224 ? -0.511  16.508  13.987  1.00 18.25 ? 1090 GLN H C   1 
ATOM   3434 O O   . GLN B 1 224 ? -0.112  17.153  13.000  1.00 18.14 ? 1090 GLN H O   1 
ATOM   3435 C CB  . GLN B 1 224 ? -3.001  16.783  14.351  1.00 19.13 ? 1090 GLN H CB  1 
ATOM   3436 C CG  . GLN B 1 224 ? -3.227  17.172  12.907  1.00 19.64 ? 1090 GLN H CG  1 
ATOM   3437 C CD  . GLN B 1 224 ? -2.754  16.158  11.882  1.00 18.68 ? 1090 GLN H CD  1 
ATOM   3438 O OE1 . GLN B 1 224 ? -2.532  14.968  12.148  1.00 18.76 ? 1090 GLN H OE1 1 
ATOM   3439 N NE2 . GLN B 1 224 ? -2.555  16.641  10.675  1.00 19.95 ? 1090 GLN H NE2 1 
ATOM   3440 N N   . TYR B 1 225 ? -0.028  15.337  14.345  1.00 16.80 ? 1091 TYR H N   1 
ATOM   3441 C CA  . TYR B 1 225 ? 0.887   14.538  13.498  1.00 18.18 ? 1091 TYR H CA  1 
ATOM   3442 C C   . TYR B 1 225 ? 0.352   13.119  13.312  1.00 19.34 ? 1091 TYR H C   1 
ATOM   3443 O O   . TYR B 1 225 ? 1.132   12.198  13.091  1.00 19.63 ? 1091 TYR H O   1 
ATOM   3444 C CB  . TYR B 1 225 ? 2.300   14.701  14.038  1.00 17.72 ? 1091 TYR H CB  1 
ATOM   3445 C CG  . TYR B 1 225 ? 2.525   14.211  15.450  1.00 17.86 ? 1091 TYR H CG  1 
ATOM   3446 C CD1 . TYR B 1 225 ? 3.061   12.975  15.721  1.00 18.20 ? 1091 TYR H CD1 1 
ATOM   3447 C CD2 . TYR B 1 225 ? 2.234   15.041  16.532  1.00 18.14 ? 1091 TYR H CD2 1 
ATOM   3448 C CE1 . TYR B 1 225 ? 3.299   12.575  17.041  1.00 18.51 ? 1091 TYR H CE1 1 
ATOM   3449 C CE2 . TYR B 1 225 ? 2.427   14.659  17.845  1.00 18.71 ? 1091 TYR H CE2 1 
ATOM   3450 C CZ  . TYR B 1 225 ? 2.993   13.428  18.104  1.00 18.56 ? 1091 TYR H CZ  1 
ATOM   3451 O OH  . TYR B 1 225 ? 3.178   13.059  19.403  1.00 18.38 ? 1091 TYR H OH  1 
ATOM   3452 N N   . SER B 1 226 ? -0.979  12.980  13.373  1.00 20.92 ? 1092 SER H N   1 
ATOM   3453 C CA  . SER B 1 226 ? -1.722  11.746  13.046  1.00 21.44 ? 1092 SER H CA  1 
ATOM   3454 C C   . SER B 1 226 ? -1.624  11.437  11.548  1.00 22.56 ? 1092 SER H C   1 
ATOM   3455 O O   . SER B 1 226 ? -1.505  10.264  11.226  1.00 23.06 ? 1092 SER H O   1 
ATOM   3456 C CB  . SER B 1 226 ? -3.147  11.909  13.492  1.00 23.24 ? 1092 SER H CB  1 
ATOM   3457 O OG  . SER B 1 226 ? -3.943  10.819  13.074  1.00 24.46 ? 1092 SER H OG  1 
ATOM   3458 N N   . SER B 1 227 ? -1.725  12.424  10.648  1.00 21.15 ? 1093 SER H N   1 
ATOM   3459 C CA  . SER B 1 227 ? -1.768  12.177  9.188   1.00 23.28 ? 1093 SER H CA  1 
ATOM   3460 C C   . SER B 1 227 ? -1.106  13.353  8.484   1.00 21.42 ? 1093 SER H C   1 
ATOM   3461 O O   . SER B 1 227 ? -1.083  14.497  9.070   1.00 21.10 ? 1093 SER H O   1 
ATOM   3462 C CB  . SER B 1 227 ? -3.193  12.001  8.700   1.00 24.22 ? 1093 SER H CB  1 
ATOM   3463 O OG  . SER B 1 227 ? -3.912  13.182  8.997   1.00 27.56 ? 1093 SER H OG  1 
ATOM   3464 N N   . TYR B 1 228 ? -0.556  13.101  7.303   1.00 19.29 ? 1094 TYR H N   1 
ATOM   3465 C CA  . TYR B 1 228 ? -0.026  14.183  6.433   1.00 19.80 ? 1094 TYR H CA  1 
ATOM   3466 C C   . TYR B 1 228 ? -1.174  14.790  5.624   1.00 20.60 ? 1094 TYR H C   1 
ATOM   3467 O O   . TYR B 1 228 ? -2.066  14.094  5.216   1.00 21.21 ? 1094 TYR H O   1 
ATOM   3468 C CB  . TYR B 1 228 ? 1.090   13.642  5.541   1.00 19.17 ? 1094 TYR H CB  1 
ATOM   3469 C CG  . TYR B 1 228 ? 2.336   13.310  6.323   1.00 19.79 ? 1094 TYR H CG  1 
ATOM   3470 C CD1 . TYR B 1 228 ? 2.648   12.011  6.697   1.00 19.84 ? 1094 TYR H CD1 1 
ATOM   3471 C CD2 . TYR B 1 228 ? 3.156   14.329  6.755   1.00 19.37 ? 1094 TYR H CD2 1 
ATOM   3472 C CE1 . TYR B 1 228 ? 3.787   11.725  7.430   1.00 19.46 ? 1094 TYR H CE1 1 
ATOM   3473 C CE2 . TYR B 1 228 ? 4.310   14.052  7.460   1.00 20.08 ? 1094 TYR H CE2 1 
ATOM   3474 C CZ  . TYR B 1 228 ? 4.605   12.758  7.841   1.00 20.05 ? 1094 TYR H CZ  1 
ATOM   3475 O OH  . TYR B 1 228 ? 5.733   12.571  8.616   1.00 21.58 ? 1094 TYR H OH  1 
ATOM   3476 N N   . PRO B 1 229 ? -1.187  16.097  5.347   1.00 20.81 ? 1095 PRO H N   1 
ATOM   3477 C CA  . PRO B 1 229 ? -0.144  16.986  5.827   1.00 21.03 ? 1095 PRO H CA  1 
ATOM   3478 C C   . PRO B 1 229 ? -0.294  17.306  7.315   1.00 19.70 ? 1095 PRO H C   1 
ATOM   3479 O O   . PRO B 1 229 ? -1.412  17.370  7.839   1.00 18.42 ? 1095 PRO H O   1 
ATOM   3480 C CB  . PRO B 1 229 ? -0.392  18.262  5.000   1.00 21.07 ? 1095 PRO H CB  1 
ATOM   3481 C CG  . PRO B 1 229 ? -1.885  18.239  4.707   1.00 21.91 ? 1095 PRO H CG  1 
ATOM   3482 C CD  . PRO B 1 229 ? -2.212  16.772  4.517   1.00 21.62 ? 1095 PRO H CD  1 
ATOM   3483 N N   . LEU B 1 230 ? 0.835   17.488  7.989   1.00 19.71 ? 1096 LEU H N   1 
ATOM   3484 C CA  . LEU B 1 230 ? 0.828   17.882  9.407   1.00 19.94 ? 1096 LEU H CA  1 
ATOM   3485 C C   . LEU B 1 230 ? 0.199   19.263  9.441   1.00 19.40 ? 1096 LEU H C   1 
ATOM   3486 O O   . LEU B 1 230 ? 0.510   20.046  8.526   1.00 18.90 ? 1096 LEU H O   1 
ATOM   3487 C CB  . LEU B 1 230 ? 2.271   17.931  9.958   1.00 20.56 ? 1096 LEU H CB  1 
ATOM   3488 C CG  . LEU B 1 230 ? 3.095   16.674  9.721   1.00 21.77 ? 1096 LEU H CG  1 
ATOM   3489 C CD1 . LEU B 1 230 ? 4.433   16.746  10.466  1.00 21.80 ? 1096 LEU H CD1 1 
ATOM   3490 C CD2 . LEU B 1 230 ? 2.354   15.414  10.155  1.00 22.04 ? 1096 LEU H CD2 1 
ATOM   3491 N N   . THR B 1 231 ? -0.691  19.542  10.393  1.00 19.03 ? 1097 THR H N   1 
ATOM   3492 C CA  . THR B 1 231 ? -1.403  20.840  10.444  1.00 19.08 ? 1097 THR H CA  1 
ATOM   3493 C C   . THR B 1 231 ? -1.383  21.386  11.873  1.00 18.98 ? 1097 THR H C   1 
ATOM   3494 O O   . THR B 1 231 ? -1.352  20.585  12.838  1.00 19.24 ? 1097 THR H O   1 
ATOM   3495 C CB  . THR B 1 231 ? -2.828  20.759  9.888   1.00 19.76 ? 1097 THR H CB  1 
ATOM   3496 O OG1 . THR B 1 231 ? -3.504  19.692  10.547  1.00 21.39 ? 1097 THR H OG1 1 
ATOM   3497 C CG2 . THR B 1 231 ? -2.825  20.536  8.402   1.00 20.18 ? 1097 THR H CG2 1 
ATOM   3498 N N   . PHE B 1 232 ? -1.392  22.696  11.962  1.00 19.72 ? 1098 PHE H N   1 
ATOM   3499 C CA  . PHE B 1 232 ? -1.298  23.471  13.227  1.00 20.63 ? 1098 PHE H CA  1 
ATOM   3500 C C   . PHE B 1 232 ? -2.611  24.183  13.461  1.00 20.94 ? 1098 PHE H C   1 
ATOM   3501 O O   . PHE B 1 232 ? -3.276  24.604  12.513  1.00 22.50 ? 1098 PHE H O   1 
ATOM   3502 C CB  . PHE B 1 232 ? -0.160  24.477  13.177  1.00 20.82 ? 1098 PHE H CB  1 
ATOM   3503 C CG  . PHE B 1 232 ? 1.226   23.903  13.077  1.00 20.70 ? 1098 PHE H CG  1 
ATOM   3504 C CD1 . PHE B 1 232 ? 1.793   23.591  11.850  1.00 21.06 ? 1098 PHE H CD1 1 
ATOM   3505 C CD2 . PHE B 1 232 ? 1.977   23.710  14.232  1.00 19.73 ? 1098 PHE H CD2 1 
ATOM   3506 C CE1 . PHE B 1 232 ? 3.100   23.143  11.772  1.00 21.63 ? 1098 PHE H CE1 1 
ATOM   3507 C CE2 . PHE B 1 232 ? 3.291   23.278  14.146  1.00 20.42 ? 1098 PHE H CE2 1 
ATOM   3508 C CZ  . PHE B 1 232 ? 3.834   22.960  12.926  1.00 20.94 ? 1098 PHE H CZ  1 
ATOM   3509 N N   . GLY B 1 233 ? -2.922  24.435  14.723  1.00 21.99 ? 1099 GLY H N   1 
ATOM   3510 C CA  . GLY B 1 233 ? -3.950  25.397  15.124  1.00 21.71 ? 1099 GLY H CA  1 
ATOM   3511 C C   . GLY B 1 233 ? -3.544  26.807  14.735  1.00 22.48 ? 1099 GLY H C   1 
ATOM   3512 O O   . GLY B 1 233 ? -2.317  27.053  14.443  1.00 21.93 ? 1099 GLY H O   1 
ATOM   3513 N N   . GLY B 1 234 ? -4.498  27.725  14.743  1.00 22.75 ? 1100 GLY H N   1 
ATOM   3514 C CA  . GLY B 1 234 ? -4.213  29.135  14.401  1.00 23.66 ? 1100 GLY H CA  1 
ATOM   3515 C C   . GLY B 1 234 ? -3.518  29.912  15.512  1.00 23.01 ? 1100 GLY H C   1 
ATOM   3516 O O   . GLY B 1 234 ? -3.125  31.070  15.248  1.00 23.53 ? 1100 GLY H O   1 
ATOM   3517 N N   . GLY B 1 235 ? -3.312  29.344  16.699  1.00 22.19 ? 1101 GLY H N   1 
ATOM   3518 C CA  . GLY B 1 235 ? -2.570  30.053  17.753  1.00 22.62 ? 1101 GLY H CA  1 
ATOM   3519 C C   . GLY B 1 235 ? -3.476  30.736  18.747  1.00 22.09 ? 1101 GLY H C   1 
ATOM   3520 O O   . GLY B 1 235 ? -4.573  31.170  18.374  1.00 22.44 ? 1101 GLY H O   1 
ATOM   3521 N N   . THR B 1 236 ? -3.043  30.773  19.999  1.00 22.37 ? 1102 THR H N   1 
ATOM   3522 C CA  . THR B 1 236 ? -3.628  31.587  21.077  1.00 24.25 ? 1102 THR H CA  1 
ATOM   3523 C C   . THR B 1 236 ? -2.492  32.441  21.641  1.00 25.05 ? 1102 THR H C   1 
ATOM   3524 O O   . THR B 1 236 ? -1.476  31.864  22.106  1.00 24.82 ? 1102 THR H O   1 
ATOM   3525 C CB  . THR B 1 236 ? -4.262  30.710  22.158  1.00 23.89 ? 1102 THR H CB  1 
ATOM   3526 O OG1 . THR B 1 236 ? -5.277  29.916  21.581  1.00 24.04 ? 1102 THR H OG1 1 
ATOM   3527 C CG2 . THR B 1 236 ? -4.838  31.485  23.318  1.00 24.53 ? 1102 THR H CG2 1 
ATOM   3528 N N   . LYS B 1 237 ? -2.721  33.747  21.709  1.00 25.99 ? 1103 LYS H N   1 
ATOM   3529 C CA  . LYS B 1 237 ? -1.833  34.700  22.411  1.00 27.94 ? 1103 LYS H CA  1 
ATOM   3530 C C   . LYS B 1 237 ? -2.306  34.827  23.855  1.00 25.62 ? 1103 LYS H C   1 
ATOM   3531 O O   . LYS B 1 237 ? -3.428  35.268  24.078  1.00 23.23 ? 1103 LYS H O   1 
ATOM   3532 C CB  . LYS B 1 237 ? -1.839  36.075  21.731  1.00 31.91 ? 1103 LYS H CB  1 
ATOM   3533 C CG  . LYS B 1 237 ? -0.803  37.026  22.283  1.00 34.73 ? 1103 LYS H CG  1 
ATOM   3534 C CD  . LYS B 1 237 ? -0.855  38.371  21.581  1.00 39.15 ? 1103 LYS H CD  1 
ATOM   3535 C CE  . LYS B 1 237 ? -0.196  39.493  22.363  1.00 43.54 ? 1103 LYS H CE  1 
ATOM   3536 N NZ  . LYS B 1 237 ? 1.211   39.194  22.739  1.00 45.29 ? 1103 LYS H NZ  1 
ATOM   3537 N N   . LEU B 1 238 ? -1.478  34.371  24.792  1.00 24.33 ? 1104 LEU H N   1 
ATOM   3538 C CA  . LEU B 1 238 ? -1.787  34.503  26.231  1.00 24.31 ? 1104 LEU H CA  1 
ATOM   3539 C C   . LEU B 1 238 ? -1.213  35.816  26.721  1.00 23.58 ? 1104 LEU H C   1 
ATOM   3540 O O   . LEU B 1 238 ? 0.006   36.020  26.580  1.00 25.09 ? 1104 LEU H O   1 
ATOM   3541 C CB  . LEU B 1 238 ? -1.173  33.309  26.961  1.00 24.35 ? 1104 LEU H CB  1 
ATOM   3542 C CG  . LEU B 1 238 ? -1.432  33.271  28.458  1.00 25.11 ? 1104 LEU H CG  1 
ATOM   3543 C CD1 . LEU B 1 238 ? -2.930  33.188  28.767  1.00 25.64 ? 1104 LEU H CD1 1 
ATOM   3544 C CD2 . LEU B 1 238 ? -0.700  32.085  29.057  1.00 24.51 ? 1104 LEU H CD2 1 
ATOM   3545 N N   . GLU B 1 239 ? -2.057  36.661  27.295  1.00 26.22 ? 1105 GLU H N   1 
ATOM   3546 C CA  . GLU B 1 239 ? -1.660  38.009  27.796  1.00 27.18 ? 1105 GLU H CA  1 
ATOM   3547 C C   . GLU B 1 239 ? -2.059  38.193  29.248  1.00 27.14 ? 1105 GLU H C   1 
ATOM   3548 O O   . GLU B 1 239 ? -2.897  37.468  29.708  1.00 23.62 ? 1105 GLU H O   1 
ATOM   3549 C CB  . GLU B 1 239 ? -2.362  39.108  26.978  1.00 28.92 ? 1105 GLU H CB  1 
ATOM   3550 C CG  . GLU B 1 239 ? -2.285  38.905  25.491  1.00 32.18 ? 1105 GLU H CG  1 
ATOM   3551 C CD  . GLU B 1 239 ? -3.146  39.918  24.712  1.00 34.19 ? 1105 GLU H CD  1 
ATOM   3552 O OE1 . GLU B 1 239 ? -2.565  40.702  24.020  1.00 34.60 ? 1105 GLU H OE1 1 
ATOM   3553 O OE2 . GLU B 1 239 ? -4.408  39.916  24.839  1.00 36.95 ? 1105 GLU H OE2 1 
ATOM   3554 N N   . MET B 1 240 ? -1.448  39.177  29.914  1.00 30.41 ? 1106 MET H N   1 
ATOM   3555 C CA  . MET B 1 240 ? -1.809  39.635  31.279  1.00 33.12 ? 1106 MET H CA  1 
ATOM   3556 C C   . MET B 1 240 ? -3.146  40.387  31.243  1.00 32.81 ? 1106 MET H C   1 
ATOM   3557 O O   . MET B 1 240 ? -3.258  41.301  30.419  1.00 31.68 ? 1106 MET H O   1 
ATOM   3558 C CB  . MET B 1 240 ? -0.734  40.577  31.814  1.00 36.89 ? 1106 MET H CB  1 
ATOM   3559 C CG  . MET B 1 240 ? -0.693  40.617  33.333  1.00 42.74 ? 1106 MET H CG  1 
ATOM   3560 S SD  . MET B 1 240 ? -0.025  39.033  33.941  1.00 49.60 ? 1106 MET H SD  1 
ATOM   3561 C CE  . MET B 1 240 ? 1.727   39.451  34.012  1.00 46.89 ? 1106 MET H CE  1 
ATOM   3562 N N   . LYS B 1 241 ? -4.122  40.023  32.068  1.00 34.64 ? 1107 LYS H N   1 
ATOM   3563 C CA  . LYS B 1 241 ? -5.350  40.838  32.299  1.00 40.90 ? 1107 LYS H CA  1 
ATOM   3564 C C   . LYS B 1 241 ? -5.004  42.337  32.260  1.00 43.96 ? 1107 LYS H C   1 
ATOM   3565 O O   . LYS B 1 241 ? -4.142  42.757  33.068  1.00 45.05 ? 1107 LYS H O   1 
ATOM   3566 C CB  . LYS B 1 241 ? -5.947  40.583  33.685  1.00 44.94 ? 1107 LYS H CB  1 
ATOM   3567 C CG  . LYS B 1 241 ? -7.300  39.896  33.699  1.00 49.12 ? 1107 LYS H CG  1 
ATOM   3568 C CD  . LYS B 1 241 ? -7.182  38.399  33.668  1.00 52.65 ? 1107 LYS H CD  1 
ATOM   3569 C CE  . LYS B 1 241 ? -8.476  37.714  33.285  1.00 56.31 ? 1107 LYS H CE  1 
ATOM   3570 N NZ  . LYS B 1 241 ? -8.615  36.421  33.997  1.00 58.81 ? 1107 LYS H NZ  1 
ATOM   3571 N N   . ALA C 2 1   ? 10.553  8.504   31.827  1.00 21.46 ? 1    ALA M N   1 
ATOM   3572 C CA  . ALA C 2 1   ? 9.415   7.726   31.312  1.00 20.54 ? 1    ALA M CA  1 
ATOM   3573 C C   . ALA C 2 1   ? 8.176   8.542   31.714  1.00 21.14 ? 1    ALA M C   1 
ATOM   3574 O O   . ALA C 2 1   ? 8.176   9.251   32.728  1.00 21.79 ? 1    ALA M O   1 
ATOM   3575 C CB  . ALA C 2 1   ? 9.376   6.321   31.930  1.00 20.80 ? 1    ALA M CB  1 
ATOM   3576 N N   . PRO C 2 2   ? 7.153   8.623   30.841  1.00 19.25 ? 2    PRO M N   1 
ATOM   3577 C CA  . PRO C 2 2   ? 7.090   7.829   29.553  1.00 18.40 ? 2    PRO M CA  1 
ATOM   3578 C C   . PRO C 2 2   ? 7.817   8.365   28.420  1.00 17.49 ? 2    PRO M C   1 
ATOM   3579 O O   . PRO C 2 2   ? 8.053   7.663   27.431  1.00 18.58 ? 2    PRO M O   1 
ATOM   3580 C CB  . PRO C 2 2   ? 5.551   7.795   29.342  1.00 19.27 ? 2    PRO M CB  1 
ATOM   3581 C CG  . PRO C 2 2   ? 5.128   9.144   29.817  1.00 19.45 ? 2    PRO M CG  1 
ATOM   3582 C CD  . PRO C 2 2   ? 5.819   9.360   31.095  1.00 19.74 ? 2    PRO M CD  1 
ATOM   3583 N N   . GLY C 2 3   ? 8.169   9.651   28.477  1.00 17.59 ? 3    GLY M N   1 
ATOM   3584 C CA  . GLY C 2 3   ? 8.996   10.401  27.475  1.00 18.58 ? 3    GLY M CA  1 
ATOM   3585 C C   . GLY C 2 3   ? 10.455  10.014  27.707  1.00 18.47 ? 3    GLY M C   1 
ATOM   3586 O O   . GLY C 2 3   ? 10.810  9.434   28.743  1.00 20.28 ? 3    GLY M O   1 
ATOM   3587 N N   . SER C 2 4   ? 11.290  10.193  26.709  1.00 18.11 ? 4    SER M N   1 
ATOM   3588 C CA  . SER C 2 4   ? 12.701  9.729   26.829  1.00 17.59 ? 4    SER M CA  1 
ATOM   3589 C C   . SER C 2 4   ? 13.616  10.850  26.516  1.00 18.27 ? 4    SER M C   1 
ATOM   3590 O O   . SER C 2 4   ? 13.315  11.729  25.736  1.00 20.70 ? 4    SER M O   1 
ATOM   3591 C CB  . SER C 2 4   ? 12.909  8.606   25.775  1.00 17.70 ? 4    SER M CB  1 
ATOM   3592 O OG  . SER C 2 4   ? 14.136  7.922   26.143  1.00 16.74 ? 4    SER M OG  1 
ATOM   3593 N N   . THR C 2 5   ? 14.817  10.827  26.978  1.00 17.48 ? 5    THR M N   1 
ATOM   3594 C CA  . THR C 2 5   ? 15.709  11.977  26.796  1.00 17.44 ? 5    THR M CA  1 
ATOM   3595 C C   . THR C 2 5   ? 16.609  11.792  25.628  1.00 17.84 ? 5    THR M C   1 
ATOM   3596 O O   . THR C 2 5   ? 16.942  10.688  25.241  1.00 16.93 ? 5    THR M O   1 
ATOM   3597 C CB  . THR C 2 5   ? 16.592  12.112  28.048  1.00 17.04 ? 5    THR M CB  1 
ATOM   3598 O OG1 . THR C 2 5   ? 17.134  10.789  28.345  1.00 16.81 ? 5    THR M OG1 1 
ATOM   3599 C CG2 . THR C 2 5   ? 15.777  12.712  29.231  1.00 17.39 ? 5    THR M CG2 1 
ATOM   3600 N N   . ALA C 2 6   ? 16.942  12.888  25.013  1.00 19.25 ? 6    ALA M N   1 
ATOM   3601 C CA  . ALA C 2 6   ? 17.813  12.860  23.874  1.00 21.14 ? 6    ALA M CA  1 
ATOM   3602 C C   . ALA C 2 6   ? 19.275  12.661  24.297  1.00 22.60 ? 6    ALA M C   1 
ATOM   3603 O O   . ALA C 2 6   ? 19.652  12.861  25.452  1.00 22.62 ? 6    ALA M O   1 
ATOM   3604 C CB  . ALA C 2 6   ? 17.728  14.185  23.165  1.00 23.01 ? 6    ALA M CB  1 
ATOM   3605 N N   . PRO C 2 7   ? 20.134  12.341  23.285  1.00 21.88 ? 7    PRO M N   1 
ATOM   3606 C CA  . PRO C 2 7   ? 21.523  12.144  23.592  1.00 23.50 ? 7    PRO M CA  1 
ATOM   3607 C C   . PRO C 2 7   ? 22.253  13.272  24.018  1.00 26.05 ? 7    PRO M C   1 
ATOM   3608 O O   . PRO C 2 7   ? 23.390  13.138  24.520  1.00 31.35 ? 7    PRO M O   1 
ATOM   3609 C CB  . PRO C 2 7   ? 22.198  11.620  22.312  1.00 22.88 ? 7    PRO M CB  1 
ATOM   3610 C CG  . PRO C 2 7   ? 21.148  11.208  21.397  1.00 22.57 ? 7    PRO M CG  1 
ATOM   3611 C CD  . PRO C 2 7   ? 19.894  11.990  21.879  1.00 22.53 ? 7    PRO M CD  1 
HETATM 3612 N N   . NH2 C 2 8   ? 21.799  14.438  23.816  1.00 26.63 ? 8    NH2 M N   1 
ATOM   3613 N N   . ALA D 2 1   ? 4.183   8.601   10.373  1.00 26.31 ? 1    ALA N N   1 
ATOM   3614 C CA  . ALA D 2 1   ? 3.390   9.395   11.352  1.00 24.63 ? 1    ALA N CA  1 
ATOM   3615 C C   . ALA D 2 1   ? 2.117   8.610   11.760  1.00 24.83 ? 1    ALA N C   1 
ATOM   3616 O O   . ALA D 2 1   ? 1.447   7.927   10.977  1.00 26.68 ? 1    ALA N O   1 
ATOM   3617 C CB  . ALA D 2 1   ? 3.016   10.828  10.835  1.00 24.67 ? 1    ALA N CB  1 
ATOM   3618 N N   . PRO D 2 2   ? 1.765   8.653   13.034  1.00 24.61 ? 2    PRO N N   1 
ATOM   3619 C CA  . PRO D 2 2   ? 2.464   9.360   14.121  1.00 22.67 ? 2    PRO N CA  1 
ATOM   3620 C C   . PRO D 2 2   ? 3.676   8.776   14.577  1.00 21.14 ? 2    PRO N C   1 
ATOM   3621 O O   . PRO D 2 2   ? 4.455   9.519   15.180  1.00 21.75 ? 2    PRO N O   1 
ATOM   3622 C CB  . PRO D 2 2   ? 1.373   9.481   15.180  1.00 23.30 ? 2    PRO N CB  1 
ATOM   3623 C CG  . PRO D 2 2   ? 0.482   8.266   14.973  1.00 24.46 ? 2    PRO N CG  1 
ATOM   3624 C CD  . PRO D 2 2   ? 0.506   7.994   13.494  1.00 25.74 ? 2    PRO N CD  1 
ATOM   3625 N N   . GLY D 2 3   ? 3.905   7.485   14.376  1.00 20.15 ? 3    GLY N N   1 
ATOM   3626 C CA  . GLY D 2 3   ? 5.162   6.766   14.755  1.00 20.53 ? 3    GLY N CA  1 
ATOM   3627 C C   . GLY D 2 3   ? 6.236   7.162   13.753  1.00 19.96 ? 3    GLY N C   1 
ATOM   3628 O O   . GLY D 2 3   ? 5.885   7.628   12.642  1.00 20.47 ? 3    GLY N O   1 
ATOM   3629 N N   . SER D 2 4   ? 7.486   6.919   14.075  1.00 19.03 ? 4    SER N N   1 
ATOM   3630 C CA  . SER D 2 4   ? 8.558   7.297   13.166  1.00 18.97 ? 4    SER N CA  1 
ATOM   3631 C C   . SER D 2 4   ? 9.396   6.116   12.890  1.00 19.67 ? 4    SER N C   1 
ATOM   3632 O O   . SER D 2 4   ? 9.583   5.269   13.744  1.00 24.33 ? 4    SER N O   1 
ATOM   3633 C CB  . SER D 2 4   ? 9.384   8.348   13.852  1.00 18.67 ? 4    SER N CB  1 
ATOM   3634 O OG  . SER D 2 4   ? 10.248  8.965   12.887  1.00 17.44 ? 4    SER N OG  1 
ATOM   3635 N N   . THR D 2 5   ? 10.147  6.085   11.811  1.00 19.26 ? 5    THR N N   1 
ATOM   3636 C CA  . THR D 2 5   ? 10.925  4.974   11.448  1.00 19.31 ? 5    THR N CA  1 
ATOM   3637 C C   . THR D 2 5   ? 12.379  5.111   11.922  1.00 19.56 ? 5    THR N C   1 
ATOM   3638 O O   . THR D 2 5   ? 12.963  6.179   12.070  1.00 19.17 ? 5    THR N O   1 
ATOM   3639 C CB  . THR D 2 5   ? 10.850  4.859   9.890   1.00 19.86 ? 5    THR N CB  1 
ATOM   3640 O OG1 . THR D 2 5   ? 11.241  6.168   9.423   1.00 18.48 ? 5    THR N OG1 1 
ATOM   3641 C CG2 . THR D 2 5   ? 9.438   4.437   9.401   1.00 19.96 ? 5    THR N CG2 1 
ATOM   3642 N N   . ALA D 2 6   ? 12.915  3.982   12.328  1.00 20.53 ? 6    ALA N N   1 
ATOM   3643 C CA  . ALA D 2 6   ? 14.305  3.903   12.756  1.00 20.98 ? 6    ALA N CA  1 
ATOM   3644 C C   . ALA D 2 6   ? 15.272  4.062   11.577  1.00 22.29 ? 6    ALA N C   1 
ATOM   3645 O O   . ALA D 2 6   ? 14.961  4.012   10.402  1.00 23.32 ? 6    ALA N O   1 
ATOM   3646 C CB  . ALA D 2 6   ? 14.509  2.499   13.311  1.00 22.71 ? 6    ALA N CB  1 
ATOM   3647 N N   . PRO D 2 7   ? 16.511  4.425   11.887  1.00 23.06 ? 7    PRO N N   1 
ATOM   3648 C CA  . PRO D 2 7   ? 17.523  4.654   10.824  1.00 24.50 ? 7    PRO N CA  1 
ATOM   3649 C C   . PRO D 2 7   ? 18.007  3.501   10.195  1.00 26.85 ? 7    PRO N C   1 
ATOM   3650 O O   . PRO D 2 7   ? 18.887  3.669   9.339   1.00 29.94 ? 7    PRO N O   1 
ATOM   3651 C CB  . PRO D 2 7   ? 18.587  5.389   11.615  1.00 24.45 ? 7    PRO N CB  1 
ATOM   3652 C CG  . PRO D 2 7   ? 18.504  5.010   12.969  1.00 24.02 ? 7    PRO N CG  1 
ATOM   3653 C CD  . PRO D 2 7   ? 17.031  4.632   13.182  1.00 22.57 ? 7    PRO N CD  1 
HETATM 3654 N N   . NH2 D 2 8   ? 17.618  2.295   10.606  1.00 25.75 ? 8    NH2 N N   1 
HETATM 3655 C C1  . EDO E 3 .   ? 11.786  -1.417  28.392  1.00 25.43 ? 301  EDO A C1  1 
HETATM 3656 O O1  . EDO E 3 .   ? 11.502  -2.628  29.271  1.00 22.90 ? 301  EDO A O1  1 
HETATM 3657 C C2  . EDO E 3 .   ? 10.954  -1.659  27.101  1.00 23.46 ? 301  EDO A C2  1 
HETATM 3658 O O2  . EDO E 3 .   ? 10.001  -2.873  27.006  1.00 27.21 ? 301  EDO A O2  1 
HETATM 3659 C C1  . EDO F 3 .   ? 10.424  -14.001 36.482  1.00 55.28 ? 302  EDO A C1  1 
HETATM 3660 O O1  . EDO F 3 .   ? 10.249  -13.623 37.807  1.00 53.59 ? 302  EDO A O1  1 
HETATM 3661 C C2  . EDO F 3 .   ? 9.246   -13.709 35.649  1.00 57.49 ? 302  EDO A C2  1 
HETATM 3662 O O2  . EDO F 3 .   ? 9.649   -12.896 34.587  1.00 54.67 ? 302  EDO A O2  1 
HETATM 3663 C C1  . EDO G 3 .   ? 21.646  -2.684  43.013  1.00 17.24 ? 303  EDO A C1  1 
HETATM 3664 O O1  . EDO G 3 .   ? 21.584  -4.149  43.196  1.00 16.45 ? 303  EDO A O1  1 
HETATM 3665 C C2  . EDO G 3 .   ? 22.992  -2.200  42.561  1.00 17.80 ? 303  EDO A C2  1 
HETATM 3666 O O2  . EDO G 3 .   ? 23.917  -2.482  43.616  1.00 18.40 ? 303  EDO A O2  1 
HETATM 3667 C C1  . EDO H 3 .   ? 20.846  3.418   40.765  1.00 46.89 ? 304  EDO A C1  1 
HETATM 3668 O O1  . EDO H 3 .   ? 22.141  3.651   40.264  1.00 45.22 ? 304  EDO A O1  1 
HETATM 3669 C C2  . EDO H 3 .   ? 20.736  3.058   42.184  1.00 48.96 ? 304  EDO A C2  1 
HETATM 3670 O O2  . EDO H 3 .   ? 19.628  3.694   42.783  1.00 51.23 ? 304  EDO A O2  1 
HETATM 3671 C C1  . EDO I 3 .   ? 17.312  7.956   37.908  1.00 47.05 ? 305  EDO A C1  1 
HETATM 3672 O O1  . EDO I 3 .   ? 17.170  8.455   36.569  1.00 47.33 ? 305  EDO A O1  1 
HETATM 3673 C C2  . EDO I 3 .   ? 18.246  6.817   37.905  1.00 45.99 ? 305  EDO A C2  1 
HETATM 3674 O O2  . EDO I 3 .   ? 18.327  6.173   39.144  1.00 48.03 ? 305  EDO A O2  1 
HETATM 3675 C C1  . EDO J 3 .   ? -4.679  -24.534 28.986  1.00 46.19 ? 306  EDO A C1  1 
HETATM 3676 O O1  . EDO J 3 .   ? -5.268  -24.410 30.282  1.00 47.88 ? 306  EDO A O1  1 
HETATM 3677 C C2  . EDO J 3 .   ? -5.684  -24.432 27.911  1.00 48.41 ? 306  EDO A C2  1 
HETATM 3678 O O2  . EDO J 3 .   ? -5.140  -24.260 26.626  1.00 48.06 ? 306  EDO A O2  1 
HETATM 3679 C C1  . EDO K 3 .   ? -7.874  -13.930 5.814   1.00 28.10 ? 307  EDO A C1  1 
HETATM 3680 O O1  . EDO K 3 .   ? -6.887  -13.750 5.133   1.00 25.87 ? 307  EDO A O1  1 
HETATM 3681 C C2  . EDO K 3 .   ? -8.528  -15.243 5.720   1.00 27.64 ? 307  EDO A C2  1 
HETATM 3682 O O2  . EDO K 3 .   ? -9.042  -15.207 7.032   1.00 24.16 ? 307  EDO A O2  1 
HETATM 3683 C C1  . EDO L 3 .   ? 20.713  14.696  19.219  1.00 30.20 ? 301  EDO H C1  1 
HETATM 3684 O O1  . EDO L 3 .   ? 20.805  13.548  18.562  1.00 28.10 ? 301  EDO H O1  1 
HETATM 3685 C C2  . EDO L 3 .   ? 19.783  14.648  20.346  1.00 32.93 ? 301  EDO H C2  1 
HETATM 3686 O O2  . EDO L 3 .   ? 19.395  15.922  20.763  1.00 33.72 ? 301  EDO H O2  1 
HETATM 3687 C C1  . EDO M 3 .   ? 16.967  25.119  19.618  1.00 41.53 ? 302  EDO H C1  1 
HETATM 3688 O O1  . EDO M 3 .   ? 16.351  26.371  19.803  1.00 44.72 ? 302  EDO H O1  1 
HETATM 3689 C C2  . EDO M 3 .   ? 16.058  23.973  19.911  1.00 38.46 ? 302  EDO H C2  1 
HETATM 3690 O O2  . EDO M 3 .   ? 14.930  23.991  19.130  1.00 31.52 ? 302  EDO H O2  1 
HETATM 3691 C C1  . EDO N 3 .   ? 7.210   18.288  12.440  1.00 32.11 ? 303  EDO H C1  1 
HETATM 3692 O O1  . EDO N 3 .   ? 6.652   19.506  11.783  1.00 33.68 ? 303  EDO H O1  1 
HETATM 3693 C C2  . EDO N 3 .   ? 7.232   18.566  13.929  1.00 30.00 ? 303  EDO H C2  1 
HETATM 3694 O O2  . EDO N 3 .   ? 6.493   19.782  14.469  1.00 33.66 ? 303  EDO H O2  1 
HETATM 3695 C C1  . EDO O 3 .   ? -1.530  23.173  -5.814  1.00 34.15 ? 304  EDO H C1  1 
HETATM 3696 O O1  . EDO O 3 .   ? -2.229  23.365  -4.550  1.00 35.00 ? 304  EDO H O1  1 
HETATM 3697 C C2  . EDO O 3 .   ? -1.340  24.445  -6.582  1.00 34.62 ? 304  EDO H C2  1 
HETATM 3698 O O2  . EDO O 3 .   ? -0.898  24.242  -7.924  1.00 31.26 ? 304  EDO H O2  1 
HETATM 3699 C C1  . EDO P 3 .   ? 14.202  21.795  22.229  1.00 47.96 ? 305  EDO H C1  1 
HETATM 3700 O O1  . EDO P 3 .   ? 14.243  20.422  21.960  1.00 48.36 ? 305  EDO H O1  1 
HETATM 3701 C C2  . EDO P 3 .   ? 13.077  22.124  23.109  1.00 46.07 ? 305  EDO H C2  1 
HETATM 3702 O O2  . EDO P 3 .   ? 12.648  23.449  22.963  1.00 45.44 ? 305  EDO H O2  1 
HETATM 3703 O O5  . A2G Q 4 .   ? 14.440  6.709   24.149  1.00 16.36 ? 101  A2G M O5  1 
HETATM 3704 C C1  . A2G Q 4 .   ? 14.319  6.640   25.524  1.00 16.23 ? 101  A2G M C1  1 
HETATM 3705 C C2  . A2G Q 4 .   ? 15.555  5.962   26.255  1.00 15.57 ? 101  A2G M C2  1 
HETATM 3706 N N2  . A2G Q 4 .   ? 15.393  5.961   27.660  1.00 14.24 ? 101  A2G M N2  1 
HETATM 3707 C C3  . A2G Q 4 .   ? 16.884  6.677   25.782  1.00 15.51 ? 101  A2G M C3  1 
HETATM 3708 O O3  . A2G Q 4 .   ? 17.913  5.909   26.404  1.00 14.72 ? 101  A2G M O3  1 
HETATM 3709 C C4  . A2G Q 4 .   ? 16.877  6.572   24.227  1.00 15.81 ? 101  A2G M C4  1 
HETATM 3710 O O4  . A2G Q 4 .   ? 16.875  5.205   23.837  1.00 15.82 ? 101  A2G M O4  1 
HETATM 3711 C C5  . A2G Q 4 .   ? 15.618  7.298   23.653  1.00 16.24 ? 101  A2G M C5  1 
HETATM 3712 C C6  . A2G Q 4 .   ? 15.713  7.397   22.133  1.00 17.09 ? 101  A2G M C6  1 
HETATM 3713 O O6  . A2G Q 4 .   ? 14.981  8.430   21.642  1.00 16.61 ? 101  A2G M O6  1 
HETATM 3714 C C7  . A2G Q 4 .   ? 15.401  4.812   28.360  1.00 14.06 ? 101  A2G M C7  1 
HETATM 3715 O O7  . A2G Q 4 .   ? 15.437  3.671   27.842  1.00 13.95 ? 101  A2G M O7  1 
HETATM 3716 C C8  . A2G Q 4 .   ? 15.334  4.960   29.837  1.00 13.51 ? 101  A2G M C8  1 
HETATM 3717 O O5  . A2G R 4 .   ? 18.359  10.769  30.365  1.00 18.43 ? 102  A2G M O5  1 
HETATM 3718 C C1  . A2G R 4 .   ? 18.483  10.717  28.926  1.00 17.32 ? 102  A2G M C1  1 
HETATM 3719 C C2  . A2G R 4 .   ? 19.090  9.396   28.557  1.00 16.74 ? 102  A2G M C2  1 
HETATM 3720 N N2  . A2G R 4 .   ? 19.068  9.318   27.090  1.00 16.34 ? 102  A2G M N2  1 
HETATM 3721 C C3  . A2G R 4 .   ? 18.185  8.274   29.177  1.00 16.35 ? 102  A2G M C3  1 
HETATM 3722 O O3  . A2G R 4 .   ? 18.740  7.042   28.748  1.00 15.19 ? 102  A2G M O3  1 
HETATM 3723 C C4  . A2G R 4 .   ? 18.048  8.448   30.710  1.00 17.20 ? 102  A2G M C4  1 
HETATM 3724 O O4  . A2G R 4 .   ? 19.347  8.285   31.265  1.00 17.20 ? 102  A2G M O4  1 
HETATM 3725 C C5  . A2G R 4 .   ? 17.477  9.775   30.957  1.00 18.08 ? 102  A2G M C5  1 
HETATM 3726 C C6  . A2G R 4 .   ? 17.557  10.054  32.449  1.00 19.41 ? 102  A2G M C6  1 
HETATM 3727 O O6  . A2G R 4 .   ? 16.901  11.301  32.733  1.00 19.87 ? 102  A2G M O6  1 
HETATM 3728 C C7  . A2G R 4 .   ? 20.230  9.036   26.452  1.00 17.16 ? 102  A2G M C7  1 
HETATM 3729 O O7  . A2G R 4 .   ? 21.258  8.703   27.043  1.00 18.64 ? 102  A2G M O7  1 
HETATM 3730 C C8  . A2G R 4 .   ? 20.175  8.925   24.942  1.00 17.12 ? 102  A2G M C8  1 
HETATM 3731 O O5  . A2G S 4 .   ? 11.539  10.213  14.429  1.00 17.48 ? 101  A2G N O5  1 
HETATM 3732 C C1  . A2G S 4 .   ? 10.641  10.248  13.298  1.00 17.36 ? 101  A2G N C1  1 
HETATM 3733 C C2  . A2G S 4 .   ? 11.304  10.980  12.107  1.00 17.46 ? 101  A2G N C2  1 
HETATM 3734 N N2  . A2G S 4 .   ? 10.354  10.955  11.007  1.00 17.36 ? 101  A2G N N2  1 
HETATM 3735 C C3  . A2G S 4 .   ? 12.586  10.266  11.757  1.00 17.85 ? 101  A2G N C3  1 
HETATM 3736 O O3  . A2G S 4 .   ? 13.273  10.866  10.639  1.00 17.19 ? 101  A2G N O3  1 
HETATM 3737 C C4  . A2G S 4 .   ? 13.502  10.254  12.942  1.00 17.53 ? 101  A2G N C4  1 
HETATM 3738 O O4  . A2G S 4 .   ? 13.719  11.603  13.353  1.00 18.26 ? 101  A2G N O4  1 
HETATM 3739 C C5  . A2G S 4 .   ? 12.758  9.551   14.093  1.00 18.15 ? 101  A2G N C5  1 
HETATM 3740 C C6  . A2G S 4 .   ? 13.646  9.493   15.304  1.00 19.16 ? 101  A2G N C6  1 
HETATM 3741 O O6  . A2G S 4 .   ? 13.262  8.412   16.123  1.00 19.28 ? 101  A2G N O6  1 
HETATM 3742 C C7  . A2G S 4 .   ? 10.104  12.112  10.342  1.00 17.41 ? 101  A2G N C7  1 
HETATM 3743 O O7  . A2G S 4 .   ? 10.414  13.246  10.774  1.00 17.28 ? 101  A2G N O7  1 
HETATM 3744 C C8  . A2G S 4 .   ? 9.148   11.954  9.178   1.00 17.90 ? 101  A2G N C8  1 
HETATM 3745 O O5  . A2G T 4 .   ? 11.172  6.163   7.064   1.00 19.74 ? 102  A2G N O5  1 
HETATM 3746 C C1  . A2G T 4 .   ? 12.069  6.096   8.200   1.00 19.38 ? 102  A2G N C1  1 
HETATM 3747 C C2  . A2G T 4 .   ? 12.793  7.434   8.216   1.00 19.37 ? 102  A2G N C2  1 
HETATM 3748 N N2  . A2G T 4 .   ? 13.627  7.505   9.400   1.00 19.51 ? 102  A2G N N2  1 
HETATM 3749 C C3  . A2G T 4 .   ? 11.837  8.617   8.205   1.00 19.03 ? 102  A2G N C3  1 
HETATM 3750 O O3  . A2G T 4 .   ? 12.516  9.904   8.240   1.00 18.26 ? 102  A2G N O3  1 
HETATM 3751 C C4  . A2G T 4 .   ? 10.865  8.481   6.938   1.00 19.27 ? 102  A2G N C4  1 
HETATM 3752 O O4  . A2G T 4 .   ? 11.578  8.613   5.677   1.00 18.29 ? 102  A2G N O4  1 
HETATM 3753 C C5  . A2G T 4 .   ? 10.180  7.154   7.017   1.00 19.69 ? 102  A2G N C5  1 
HETATM 3754 C C6  . A2G T 4 .   ? 9.394   6.875   5.693   1.00 21.27 ? 102  A2G N C6  1 
HETATM 3755 O O6  . A2G T 4 .   ? 8.699   5.653   5.911   1.00 21.39 ? 102  A2G N O6  1 
HETATM 3756 C C7  . A2G T 4 .   ? 14.898  7.869   9.283   1.00 21.00 ? 102  A2G N C7  1 
HETATM 3757 O O7  . A2G T 4 .   ? 15.457  8.108   8.208   1.00 21.08 ? 102  A2G N O7  1 
HETATM 3758 C C8  . A2G T 4 .   ? 15.669  7.888   10.570  1.00 20.38 ? 102  A2G N C8  1 
HETATM 3759 O O   . HOH U 5 .   ? 12.727  -15.525 47.543  1.00 35.42 ? 401  HOH A O   1 
HETATM 3760 O O   . HOH U 5 .   ? 7.704   -8.190  39.640  1.00 28.05 ? 402  HOH A O   1 
HETATM 3761 O O   . HOH U 5 .   ? 22.314  7.967   17.797  1.00 28.55 ? 403  HOH A O   1 
HETATM 3762 O O   . HOH U 5 .   ? 11.435  -12.639 40.022  1.00 26.43 ? 404  HOH A O   1 
HETATM 3763 O O   . HOH U 5 .   ? 8.598   -20.211 18.196  1.00 50.58 ? 405  HOH A O   1 
HETATM 3764 O O   . HOH U 5 .   ? 25.535  -5.482  13.767  1.00 35.71 ? 406  HOH A O   1 
HETATM 3765 O O   . HOH U 5 .   ? -6.945  2.183   17.959  1.00 38.93 ? 407  HOH A O   1 
HETATM 3766 O O   . HOH U 5 .   ? -1.216  0.128   41.998  1.00 29.66 ? 408  HOH A O   1 
HETATM 3767 O O   . HOH U 5 .   ? 15.950  -16.011 45.536  1.00 23.77 ? 409  HOH A O   1 
HETATM 3768 O O   . HOH U 5 .   ? 26.444  10.346  21.120  1.00 35.96 ? 410  HOH A O   1 
HETATM 3769 O O   . HOH U 5 .   ? 9.054   -15.158 39.442  1.00 44.46 ? 411  HOH A O   1 
HETATM 3770 O O   . HOH U 5 .   ? -11.432 -5.102  20.595  1.00 34.33 ? 412  HOH A O   1 
HETATM 3771 O O   . HOH U 5 .   ? 7.198   5.388   23.292  1.00 37.21 ? 413  HOH A O   1 
HETATM 3772 O O   . HOH U 5 .   ? -1.460  -1.679  3.976   1.00 29.90 ? 414  HOH A O   1 
HETATM 3773 O O   . HOH U 5 .   ? 9.575   -3.118  42.851  1.00 22.41 ? 415  HOH A O   1 
HETATM 3774 O O   . HOH U 5 .   ? -4.291  -4.571  37.605  1.00 23.05 ? 416  HOH A O   1 
HETATM 3775 O O   . HOH U 5 .   ? 10.247  -2.591  12.653  1.00 39.56 ? 417  HOH A O   1 
HETATM 3776 O O   . HOH U 5 .   ? 24.994  -0.142  39.978  1.00 18.63 ? 418  HOH A O   1 
HETATM 3777 O O   . HOH U 5 .   ? -12.243 -12.689 8.565   1.00 30.59 ? 419  HOH A O   1 
HETATM 3778 O O   . HOH U 5 .   ? 10.307  -3.487  45.487  1.00 30.10 ? 420  HOH A O   1 
HETATM 3779 O O   . HOH U 5 .   ? 5.983   -7.274  11.813  1.00 41.26 ? 421  HOH A O   1 
HETATM 3780 O O   . HOH U 5 .   ? 8.071   -21.239 35.197  1.00 52.48 ? 422  HOH A O   1 
HETATM 3781 O O   . HOH U 5 .   ? 25.827  -16.011 29.929  1.00 23.05 ? 423  HOH A O   1 
HETATM 3782 O O   . HOH U 5 .   ? 17.846  2.723   41.148  1.00 19.14 ? 424  HOH A O   1 
HETATM 3783 O O   . HOH U 5 .   ? 29.077  -6.267  37.993  1.00 29.68 ? 425  HOH A O   1 
HETATM 3784 O O   . HOH U 5 .   ? 26.276  -0.084  19.477  1.00 39.59 ? 426  HOH A O   1 
HETATM 3785 O O   . HOH U 5 .   ? 27.418  -11.321 24.351  1.00 27.12 ? 427  HOH A O   1 
HETATM 3786 O O   . HOH U 5 .   ? -0.657  6.618   19.839  1.00 37.25 ? 428  HOH A O   1 
HETATM 3787 O O   . HOH U 5 .   ? 2.647   -14.610 34.530  1.00 38.40 ? 429  HOH A O   1 
HETATM 3788 O O   . HOH U 5 .   ? 6.548   2.113   43.083  1.00 39.40 ? 430  HOH A O   1 
HETATM 3789 O O   . HOH U 5 .   ? 26.245  -14.215 48.279  1.00 19.07 ? 431  HOH A O   1 
HETATM 3790 O O   . HOH U 5 .   ? 17.237  -10.261 47.456  1.00 31.30 ? 432  HOH A O   1 
HETATM 3791 O O   . HOH U 5 .   ? 30.756  2.211   22.485  1.00 29.95 ? 433  HOH A O   1 
HETATM 3792 O O   . HOH U 5 .   ? -1.470  6.293   17.524  1.00 35.39 ? 434  HOH A O   1 
HETATM 3793 O O   . HOH U 5 .   ? 9.187   0.040   43.474  1.00 28.54 ? 435  HOH A O   1 
HETATM 3794 O O   . HOH U 5 .   ? -10.966 -17.018 7.195   1.00 19.40 ? 436  HOH A O   1 
HETATM 3795 O O   . HOH U 5 .   ? 28.391  -1.460  15.267  1.00 36.68 ? 437  HOH A O   1 
HETATM 3796 O O   . HOH U 5 .   ? 27.149  -14.617 44.893  1.00 32.39 ? 438  HOH A O   1 
HETATM 3797 O O   . HOH U 5 .   ? 21.914  -17.208 24.965  1.00 19.65 ? 439  HOH A O   1 
HETATM 3798 O O   . HOH U 5 .   ? -13.476 -17.069 11.105  1.00 30.09 ? 440  HOH A O   1 
HETATM 3799 O O   . HOH U 5 .   ? 1.791   -19.241 15.252  1.00 30.65 ? 441  HOH A O   1 
HETATM 3800 O O   . HOH U 5 .   ? 11.211  1.598   11.705  1.00 31.58 ? 442  HOH A O   1 
HETATM 3801 O O   . HOH U 5 .   ? -5.494  8.887   31.593  1.00 35.53 ? 443  HOH A O   1 
HETATM 3802 O O   . HOH U 5 .   ? 31.349  -4.937  34.154  1.00 28.91 ? 444  HOH A O   1 
HETATM 3803 O O   . HOH U 5 .   ? 15.631  -14.345 43.498  1.00 24.27 ? 445  HOH A O   1 
HETATM 3804 O O   . HOH U 5 .   ? -8.277  7.909   30.214  1.00 36.82 ? 446  HOH A O   1 
HETATM 3805 O O   . HOH U 5 .   ? 11.991  -7.715  18.853  1.00 35.58 ? 447  HOH A O   1 
HETATM 3806 O O   . HOH U 5 .   ? -2.114  -13.386 32.504  1.00 23.38 ? 448  HOH A O   1 
HETATM 3807 O O   . HOH U 5 .   ? 1.976   -12.327 13.666  1.00 21.57 ? 449  HOH A O   1 
HETATM 3808 O O   . HOH U 5 .   ? 20.772  -22.910 31.511  1.00 28.30 ? 450  HOH A O   1 
HETATM 3809 O O   . HOH U 5 .   ? 19.086  8.503   21.026  1.00 16.94 ? 451  HOH A O   1 
HETATM 3810 O O   . HOH U 5 .   ? 23.873  -3.544  31.952  1.00 23.51 ? 452  HOH A O   1 
HETATM 3811 O O   . HOH U 5 .   ? -8.404  -1.508  18.170  1.00 30.10 ? 453  HOH A O   1 
HETATM 3812 O O   . HOH U 5 .   ? 23.179  1.166   23.879  1.00 18.37 ? 454  HOH A O   1 
HETATM 3813 O O   . HOH U 5 .   ? -0.277  -17.409 29.230  1.00 44.67 ? 455  HOH A O   1 
HETATM 3814 O O   . HOH U 5 .   ? -0.154  -20.344 20.904  1.00 27.16 ? 456  HOH A O   1 
HETATM 3815 O O   . HOH U 5 .   ? 30.767  -11.675 27.181  1.00 46.54 ? 457  HOH A O   1 
HETATM 3816 O O   . HOH U 5 .   ? 16.293  -13.275 39.390  1.00 19.93 ? 458  HOH A O   1 
HETATM 3817 O O   . HOH U 5 .   ? -7.690  -7.939  32.529  1.00 46.33 ? 459  HOH A O   1 
HETATM 3818 O O   . HOH U 5 .   ? 19.079  -2.570  12.114  1.00 47.68 ? 460  HOH A O   1 
HETATM 3819 O O   . HOH U 5 .   ? 12.373  -21.954 42.900  1.00 40.10 ? 461  HOH A O   1 
HETATM 3820 O O   . HOH U 5 .   ? 8.472   -5.387  36.326  1.00 14.49 ? 462  HOH A O   1 
HETATM 3821 O O   . HOH U 5 .   ? 7.877   -5.835  15.617  1.00 27.54 ? 463  HOH A O   1 
HETATM 3822 O O   . HOH U 5 .   ? 27.080  -0.506  38.342  1.00 18.71 ? 464  HOH A O   1 
HETATM 3823 O O   . HOH U 5 .   ? 1.935   -2.926  43.573  1.00 30.70 ? 465  HOH A O   1 
HETATM 3824 O O   . HOH U 5 .   ? 4.246   -18.839 13.872  1.00 37.27 ? 466  HOH A O   1 
HETATM 3825 O O   . HOH U 5 .   ? -3.881  0.929   16.478  1.00 16.58 ? 467  HOH A O   1 
HETATM 3826 O O   . HOH U 5 .   ? 12.994  7.120   31.642  1.00 21.54 ? 468  HOH A O   1 
HETATM 3827 O O   . HOH U 5 .   ? 6.442   -4.614  40.640  1.00 26.32 ? 469  HOH A O   1 
HETATM 3828 O O   . HOH U 5 .   ? 5.285   0.595   38.696  1.00 18.04 ? 470  HOH A O   1 
HETATM 3829 O O   . HOH U 5 .   ? 27.647  -5.969  35.825  1.00 21.04 ? 471  HOH A O   1 
HETATM 3830 O O   . HOH U 5 .   ? 7.001   -12.760 17.226  1.00 31.76 ? 472  HOH A O   1 
HETATM 3831 O O   . HOH U 5 .   ? 25.024  -8.279  41.300  1.00 21.42 ? 473  HOH A O   1 
HETATM 3832 O O   . HOH U 5 .   ? -3.437  -0.409  24.060  1.00 14.26 ? 474  HOH A O   1 
HETATM 3833 O O   . HOH U 5 .   ? 12.867  -11.141 42.517  1.00 30.95 ? 475  HOH A O   1 
HETATM 3834 O O   . HOH U 5 .   ? 5.214   3.462   13.519  1.00 35.43 ? 476  HOH A O   1 
HETATM 3835 O O   . HOH U 5 .   ? 27.352  -21.970 33.167  1.00 38.76 ? 477  HOH A O   1 
HETATM 3836 O O   . HOH U 5 .   ? -11.335 -20.517 10.403  1.00 43.50 ? 478  HOH A O   1 
HETATM 3837 O O   . HOH U 5 .   ? 24.240  10.916  17.836  1.00 29.78 ? 479  HOH A O   1 
HETATM 3838 O O   . HOH U 5 .   ? 1.931   -6.259  36.464  1.00 21.11 ? 480  HOH A O   1 
HETATM 3839 O O   . HOH U 5 .   ? -7.454  -4.704  14.354  1.00 19.76 ? 481  HOH A O   1 
HETATM 3840 O O   . HOH U 5 .   ? 7.670   -5.309  12.946  1.00 32.44 ? 482  HOH A O   1 
HETATM 3841 O O   . HOH U 5 .   ? 21.629  8.800   37.569  1.00 35.30 ? 483  HOH A O   1 
HETATM 3842 O O   . HOH U 5 .   ? -5.365  5.855   23.186  1.00 23.00 ? 484  HOH A O   1 
HETATM 3843 O O   . HOH U 5 .   ? -3.563  -18.260 8.692   1.00 25.66 ? 485  HOH A O   1 
HETATM 3844 O O   . HOH U 5 .   ? 10.598  -5.273  18.846  1.00 19.79 ? 486  HOH A O   1 
HETATM 3845 O O   . HOH U 5 .   ? 3.956   -13.746 12.640  1.00 30.98 ? 487  HOH A O   1 
HETATM 3846 O O   . HOH U 5 .   ? 26.247  -7.338  18.395  1.00 21.44 ? 488  HOH A O   1 
HETATM 3847 O O   . HOH U 5 .   ? 12.364  1.338   39.719  1.00 27.45 ? 489  HOH A O   1 
HETATM 3848 O O   . HOH U 5 .   ? 15.225  2.788   41.741  1.00 37.39 ? 490  HOH A O   1 
HETATM 3849 O O   . HOH U 5 .   ? 32.530  -1.198  20.527  1.00 39.92 ? 491  HOH A O   1 
HETATM 3850 O O   . HOH U 5 .   ? 14.532  7.716   33.788  1.00 24.82 ? 492  HOH A O   1 
HETATM 3851 O O   . HOH U 5 .   ? -7.809  -2.406  20.194  1.00 22.83 ? 493  HOH A O   1 
HETATM 3852 O O   . HOH U 5 .   ? 12.293  -6.517  48.252  1.00 40.49 ? 494  HOH A O   1 
HETATM 3853 O O   . HOH U 5 .   ? 16.174  -24.046 39.278  1.00 45.38 ? 495  HOH A O   1 
HETATM 3854 O O   . HOH U 5 .   ? 13.507  5.689   42.163  1.00 43.98 ? 496  HOH A O   1 
HETATM 3855 O O   . HOH U 5 .   ? 8.547   -13.684 19.152  1.00 21.98 ? 497  HOH A O   1 
HETATM 3856 O O   . HOH U 5 .   ? 23.160  6.314   37.916  1.00 36.96 ? 498  HOH A O   1 
HETATM 3857 O O   . HOH U 5 .   ? 21.753  -18.720 47.525  1.00 28.74 ? 499  HOH A O   1 
HETATM 3858 O O   . HOH U 5 .   ? -2.999  -23.493 18.712  1.00 27.14 ? 500  HOH A O   1 
HETATM 3859 O O   . HOH U 5 .   ? -0.623  -15.191 7.620   1.00 37.19 ? 501  HOH A O   1 
HETATM 3860 O O   . HOH U 5 .   ? 21.521  2.539   13.716  1.00 26.18 ? 502  HOH A O   1 
HETATM 3861 O O   . HOH U 5 .   ? 19.887  -9.998  48.091  1.00 16.97 ? 503  HOH A O   1 
HETATM 3862 O O   . HOH U 5 .   ? 3.612   -4.579  39.921  1.00 23.03 ? 504  HOH A O   1 
HETATM 3863 O O   . HOH U 5 .   ? 3.178   4.190   41.117  1.00 44.80 ? 505  HOH A O   1 
HETATM 3864 O O   . HOH U 5 .   ? 27.724  -8.521  41.722  1.00 41.03 ? 506  HOH A O   1 
HETATM 3865 O O   . HOH U 5 .   ? 6.546   3.439   11.446  1.00 41.82 ? 507  HOH A O   1 
HETATM 3866 O O   . HOH U 5 .   ? 0.227   -9.168  36.633  1.00 34.21 ? 508  HOH A O   1 
HETATM 3867 O O   . HOH U 5 .   ? -11.933 -9.956  12.109  1.00 27.92 ? 509  HOH A O   1 
HETATM 3868 O O   . HOH U 5 .   ? 25.872  -0.811  42.452  1.00 18.14 ? 510  HOH A O   1 
HETATM 3869 O O   . HOH U 5 .   ? 3.739   -19.250 18.817  1.00 32.28 ? 511  HOH A O   1 
HETATM 3870 O O   . HOH U 5 .   ? -2.045  10.717  25.901  1.00 25.50 ? 512  HOH A O   1 
HETATM 3871 O O   . HOH U 5 .   ? 16.160  -17.435 24.546  1.00 39.16 ? 513  HOH A O   1 
HETATM 3872 O O   . HOH U 5 .   ? 30.153  -17.466 41.565  1.00 32.61 ? 514  HOH A O   1 
HETATM 3873 O O   . HOH U 5 .   ? -5.590  -0.783  10.836  1.00 34.63 ? 515  HOH A O   1 
HETATM 3874 O O   . HOH U 5 .   ? 4.365   -10.338 34.002  1.00 35.50 ? 516  HOH A O   1 
HETATM 3875 O O   . HOH U 5 .   ? 3.629   -6.477  7.752   1.00 41.18 ? 517  HOH A O   1 
HETATM 3876 O O   . HOH U 5 .   ? 7.883   2.474   15.186  1.00 29.57 ? 518  HOH A O   1 
HETATM 3877 O O   . HOH U 5 .   ? -11.050 -12.290 21.734  1.00 31.65 ? 519  HOH A O   1 
HETATM 3878 O O   . HOH U 5 .   ? 17.386  1.329   14.688  1.00 29.29 ? 520  HOH A O   1 
HETATM 3879 O O   . HOH U 5 .   ? 6.286   -6.995  35.528  1.00 15.63 ? 521  HOH A O   1 
HETATM 3880 O O   . HOH U 5 .   ? 13.919  -10.998 51.567  1.00 34.82 ? 522  HOH A O   1 
HETATM 3881 O O   . HOH U 5 .   ? 33.128  2.228   29.664  1.00 26.77 ? 523  HOH A O   1 
HETATM 3882 O O   . HOH U 5 .   ? 9.619   6.134   19.081  1.00 22.63 ? 524  HOH A O   1 
HETATM 3883 O O   . HOH U 5 .   ? 29.049  3.234   19.502  1.00 30.38 ? 525  HOH A O   1 
HETATM 3884 O O   . HOH U 5 .   ? -1.853  -10.508 34.447  1.00 22.01 ? 526  HOH A O   1 
HETATM 3885 O O   . HOH U 5 .   ? 16.482  -8.308  45.749  1.00 26.71 ? 527  HOH A O   1 
HETATM 3886 O O   . HOH U 5 .   ? 20.004  5.136   16.857  1.00 16.16 ? 528  HOH A O   1 
HETATM 3887 O O   . HOH U 5 .   ? 12.065  3.298   21.294  1.00 15.58 ? 529  HOH A O   1 
HETATM 3888 O O   . HOH U 5 .   ? 22.815  6.062   26.852  1.00 16.70 ? 530  HOH A O   1 
HETATM 3889 O O   . HOH U 5 .   ? 28.601  0.183   18.980  1.00 37.00 ? 531  HOH A O   1 
HETATM 3890 O O   . HOH U 5 .   ? 8.416   -5.702  39.127  1.00 17.73 ? 532  HOH A O   1 
HETATM 3891 O O   . HOH U 5 .   ? 28.830  5.462   21.845  1.00 25.06 ? 533  HOH A O   1 
HETATM 3892 O O   . HOH U 5 .   ? 14.385  -0.643  16.646  1.00 31.45 ? 534  HOH A O   1 
HETATM 3893 O O   . HOH U 5 .   ? -7.365  4.458   22.012  1.00 26.73 ? 535  HOH A O   1 
HETATM 3894 O O   . HOH U 5 .   ? 22.220  -17.792 22.482  1.00 29.26 ? 536  HOH A O   1 
HETATM 3895 O O   . HOH U 5 .   ? 9.936   5.750   23.405  1.00 34.11 ? 537  HOH A O   1 
HETATM 3896 O O   . HOH U 5 .   ? -9.053  7.106   25.240  1.00 38.14 ? 538  HOH A O   1 
HETATM 3897 O O   . HOH U 5 .   ? 20.267  -9.229  17.655  1.00 32.62 ? 539  HOH A O   1 
HETATM 3898 O O   . HOH U 5 .   ? 29.118  -15.674 34.408  1.00 35.60 ? 540  HOH A O   1 
HETATM 3899 O O   . HOH U 5 .   ? -11.137 -18.476 24.541  1.00 35.07 ? 541  HOH A O   1 
HETATM 3900 O O   . HOH U 5 .   ? 26.289  -16.792 48.170  1.00 33.19 ? 542  HOH A O   1 
HETATM 3901 O O   . HOH U 5 .   ? 15.505  -15.804 20.782  1.00 33.36 ? 543  HOH A O   1 
HETATM 3902 O O   . HOH U 5 .   ? -4.700  6.253   39.348  1.00 33.08 ? 544  HOH A O   1 
HETATM 3903 O O   . HOH U 5 .   ? 24.477  10.137  24.548  1.00 29.83 ? 545  HOH A O   1 
HETATM 3904 O O   . HOH U 5 .   ? 19.440  2.575   15.400  1.00 17.02 ? 546  HOH A O   1 
HETATM 3905 O O   . HOH U 5 .   ? -7.509  0.573   38.228  1.00 35.63 ? 547  HOH A O   1 
HETATM 3906 O O   . HOH U 5 .   ? 23.625  -20.978 24.862  1.00 24.06 ? 548  HOH A O   1 
HETATM 3907 O O   . HOH U 5 .   ? 20.804  -19.189 26.547  1.00 21.49 ? 549  HOH A O   1 
HETATM 3908 O O   . HOH U 5 .   ? -0.566  3.187   13.954  1.00 25.86 ? 550  HOH A O   1 
HETATM 3909 O O   . HOH U 5 .   ? 7.922   6.925   17.075  1.00 25.31 ? 551  HOH A O   1 
HETATM 3910 O O   . HOH U 5 .   ? 13.656  -13.815 18.177  1.00 27.47 ? 552  HOH A O   1 
HETATM 3911 O O   . HOH U 5 .   ? 5.548   -1.413  49.859  1.00 44.50 ? 553  HOH A O   1 
HETATM 3912 O O   . HOH U 5 .   ? 18.391  -5.383  12.768  1.00 41.98 ? 554  HOH A O   1 
HETATM 3913 O O   . HOH U 5 .   ? 28.913  -16.950 25.777  1.00 30.53 ? 555  HOH A O   1 
HETATM 3914 O O   . HOH U 5 .   ? 14.381  -7.326  18.282  1.00 21.17 ? 556  HOH A O   1 
HETATM 3915 O O   . HOH U 5 .   ? -11.575 -14.813 18.596  1.00 34.80 ? 557  HOH A O   1 
HETATM 3916 O O   . HOH U 5 .   ? -13.249 -9.710  19.858  1.00 36.04 ? 558  HOH A O   1 
HETATM 3917 O O   . HOH U 5 .   ? 27.277  10.260  25.478  1.00 44.68 ? 559  HOH A O   1 
HETATM 3918 O O   . HOH U 5 .   ? 18.360  -22.598 45.401  1.00 33.29 ? 560  HOH A O   1 
HETATM 3919 O O   . HOH U 5 .   ? 11.289  -15.785 41.287  1.00 32.76 ? 561  HOH A O   1 
HETATM 3920 O O   . HOH U 5 .   ? 11.329  0.216   41.910  1.00 19.42 ? 562  HOH A O   1 
HETATM 3921 O O   . HOH U 5 .   ? -9.367  -21.997 12.444  1.00 36.21 ? 563  HOH A O   1 
HETATM 3922 O O   . HOH U 5 .   ? 29.129  -6.316  41.370  1.00 37.85 ? 564  HOH A O   1 
HETATM 3923 O O   . HOH U 5 .   ? 22.605  5.372   16.647  1.00 19.87 ? 565  HOH A O   1 
HETATM 3924 O O   . HOH U 5 .   ? 8.668   6.954   37.480  1.00 30.01 ? 566  HOH A O   1 
HETATM 3925 O O   . HOH U 5 .   ? 15.165  -11.505 43.821  1.00 28.20 ? 567  HOH A O   1 
HETATM 3926 O O   . HOH U 5 .   ? 29.378  0.651   34.155  1.00 19.16 ? 568  HOH A O   1 
HETATM 3927 O O   . HOH U 5 .   ? -0.588  -17.516 8.936   1.00 27.02 ? 569  HOH A O   1 
HETATM 3928 O O   . HOH U 5 .   ? 1.663   8.569   31.702  1.00 35.46 ? 570  HOH A O   1 
HETATM 3929 O O   . HOH U 5 .   ? 28.534  -22.891 40.206  1.00 35.81 ? 571  HOH A O   1 
HETATM 3930 O O   . HOH U 5 .   ? 11.416  -16.695 26.707  1.00 16.97 ? 572  HOH A O   1 
HETATM 3931 O O   . HOH U 5 .   ? 21.399  13.291  30.446  1.00 40.23 ? 573  HOH A O   1 
HETATM 3932 O O   . HOH U 5 .   ? -10.951 -10.627 26.333  1.00 42.07 ? 574  HOH A O   1 
HETATM 3933 O O   . HOH U 5 .   ? -9.828  3.811   31.955  1.00 34.77 ? 575  HOH A O   1 
HETATM 3934 O O   . HOH U 5 .   ? -7.390  -18.483 30.922  1.00 33.54 ? 576  HOH A O   1 
HETATM 3935 O O   . HOH U 5 .   ? -6.199  -18.213 6.014   1.00 33.30 ? 577  HOH A O   1 
HETATM 3936 O O   . HOH U 5 .   ? 15.714  -5.643  47.905  1.00 46.46 ? 578  HOH A O   1 
HETATM 3937 O O   . HOH U 5 .   ? 8.011   6.950   21.094  1.00 35.69 ? 579  HOH A O   1 
HETATM 3938 O O   . HOH U 5 .   ? 2.076   6.127   42.506  1.00 51.94 ? 580  HOH A O   1 
HETATM 3939 O O   . HOH U 5 .   ? -10.691 -23.460 14.460  1.00 38.14 ? 581  HOH A O   1 
HETATM 3940 O O   . HOH U 5 .   ? 28.242  -19.668 29.516  1.00 43.77 ? 582  HOH A O   1 
HETATM 3941 O O   . HOH U 5 .   ? 3.658   -10.165 14.043  1.00 38.37 ? 583  HOH A O   1 
HETATM 3942 O O   . HOH U 5 .   ? 12.772  -21.387 35.144  1.00 50.82 ? 584  HOH A O   1 
HETATM 3943 O O   . HOH U 5 .   ? 7.704   -13.993 14.780  1.00 42.00 ? 585  HOH A O   1 
HETATM 3944 O O   . HOH U 5 .   ? 3.456   -5.767  47.287  1.00 60.23 ? 586  HOH A O   1 
HETATM 3945 O O   . HOH U 5 .   ? 35.501  3.552   25.413  1.00 41.34 ? 587  HOH A O   1 
HETATM 3946 O O   . HOH U 5 .   ? -7.316  3.971   19.678  1.00 45.17 ? 588  HOH A O   1 
HETATM 3947 O O   . HOH U 5 .   ? 15.852  -13.511 18.644  1.00 47.74 ? 589  HOH A O   1 
HETATM 3948 O O   . HOH U 5 .   ? -4.612  9.191   29.009  1.00 31.83 ? 590  HOH A O   1 
HETATM 3949 O O   . HOH U 5 .   ? 25.405  4.631   39.303  1.00 38.22 ? 591  HOH A O   1 
HETATM 3950 O O   . HOH U 5 .   ? -1.046  9.413   34.070  1.00 46.99 ? 592  HOH A O   1 
HETATM 3951 O O   . HOH U 5 .   ? -6.338  9.608   26.359  1.00 23.67 ? 593  HOH A O   1 
HETATM 3952 O O   . HOH U 5 .   ? 29.878  -13.470 38.191  1.00 38.43 ? 594  HOH A O   1 
HETATM 3953 O O   . HOH U 5 .   ? -7.798  2.698   39.333  1.00 43.10 ? 595  HOH A O   1 
HETATM 3954 O O   . HOH U 5 .   ? -7.714  6.617   34.854  1.00 50.12 ? 596  HOH A O   1 
HETATM 3955 O O   . HOH U 5 .   ? 3.295   -4.975  42.457  1.00 35.00 ? 597  HOH A O   1 
HETATM 3956 O O   . HOH U 5 .   ? -1.708  -15.044 34.480  1.00 44.57 ? 598  HOH A O   1 
HETATM 3957 O O   . HOH U 5 .   ? 13.953  -20.900 32.559  1.00 38.63 ? 599  HOH A O   1 
HETATM 3958 O O   . HOH U 5 .   ? 5.084   -11.290 36.482  1.00 49.93 ? 600  HOH A O   1 
HETATM 3959 O O   . HOH U 5 .   ? 25.304  -24.853 30.114  1.00 45.69 ? 601  HOH A O   1 
HETATM 3960 O O   . HOH U 5 .   ? 9.211   2.834   43.186  1.00 57.63 ? 602  HOH A O   1 
HETATM 3961 O O   . HOH U 5 .   ? 12.070  -0.852  13.109  1.00 41.15 ? 603  HOH A O   1 
HETATM 3962 O O   . HOH U 5 .   ? 19.923  8.842   18.484  1.00 16.22 ? 604  HOH A O   1 
HETATM 3963 O O   . HOH U 5 .   ? 6.448   -12.249 38.268  1.00 44.63 ? 605  HOH A O   1 
HETATM 3964 O O   . HOH U 5 .   ? 4.074   7.121   39.916  1.00 50.61 ? 606  HOH A O   1 
HETATM 3965 O O   . HOH U 5 .   ? -13.437 -15.803 8.362   1.00 28.18 ? 607  HOH A O   1 
HETATM 3966 O O   . HOH U 5 .   ? 10.031  -19.473 52.946  1.00 48.88 ? 608  HOH A O   1 
HETATM 3967 O O   . HOH U 5 .   ? -6.055  2.059   15.673  1.00 31.13 ? 609  HOH A O   1 
HETATM 3968 O O   . HOH U 5 .   ? 28.721  1.290   36.660  1.00 37.21 ? 610  HOH A O   1 
HETATM 3969 O O   . HOH U 5 .   ? 3.217   -6.685  38.789  1.00 26.26 ? 611  HOH A O   1 
HETATM 3970 O O   . HOH U 5 .   ? 5.337   -8.052  37.740  1.00 33.87 ? 612  HOH A O   1 
HETATM 3971 O O   . HOH U 5 .   ? 30.308  -4.284  38.943  1.00 30.66 ? 613  HOH A O   1 
HETATM 3972 O O   . HOH U 5 .   ? 14.533  -1.587  14.291  1.00 36.98 ? 614  HOH A O   1 
HETATM 3973 O O   . HOH U 5 .   ? 3.669   10.892  33.077  1.00 34.64 ? 615  HOH A O   1 
HETATM 3974 O O   . HOH U 5 .   ? 5.555   -20.706 17.441  1.00 48.65 ? 616  HOH A O   1 
HETATM 3975 O O   . HOH U 5 .   ? 25.391  5.968   42.288  1.00 48.61 ? 617  HOH A O   1 
HETATM 3976 O O   . HOH U 5 .   ? 13.004  -23.014 49.386  1.00 43.38 ? 618  HOH A O   1 
HETATM 3977 O O   . HOH U 5 .   ? 29.039  -1.714  39.586  1.00 23.36 ? 619  HOH A O   1 
HETATM 3978 O O   . HOH U 5 .   ? 11.548  -8.290  14.419  1.00 48.09 ? 620  HOH A O   1 
HETATM 3979 O O   . HOH U 5 .   ? 1.614   -8.355  40.397  1.00 46.99 ? 621  HOH A O   1 
HETATM 3980 O O   . HOH V 5 .   ? 16.019  27.396  17.812  1.00 35.73 ? 401  HOH H O   1 
HETATM 3981 O O   . HOH V 5 .   ? 12.483  14.219  29.131  1.00 38.25 ? 402  HOH H O   1 
HETATM 3982 O O   . HOH V 5 .   ? 20.255  11.566  17.453  1.00 19.39 ? 403  HOH H O   1 
HETATM 3983 O O   . HOH V 5 .   ? 7.081   9.750   1.795   1.00 34.69 ? 404  HOH H O   1 
HETATM 3984 O O   . HOH V 5 .   ? 12.642  24.988  19.962  1.00 34.47 ? 405  HOH H O   1 
HETATM 3985 O O   . HOH V 5 .   ? -7.100  34.102  35.025  1.00 40.44 ? 406  HOH H O   1 
HETATM 3986 O O   . HOH V 5 .   ? 11.209  31.949  -9.640  1.00 36.66 ? 407  HOH H O   1 
HETATM 3987 O O   . HOH V 5 .   ? 21.535  8.762   15.339  1.00 27.48 ? 408  HOH H O   1 
HETATM 3988 O O   . HOH V 5 .   ? 2.061   11.179  28.864  1.00 34.54 ? 409  HOH H O   1 
HETATM 3989 O O   . HOH V 5 .   ? 0.654   16.294  30.876  1.00 20.48 ? 410  HOH H O   1 
HETATM 3990 O O   . HOH V 5 .   ? 11.118  22.964  24.897  1.00 30.77 ? 411  HOH H O   1 
HETATM 3991 O O   . HOH V 5 .   ? 0.713   29.981  3.055   1.00 33.43 ? 412  HOH H O   1 
HETATM 3992 O O   . HOH V 5 .   ? -10.280 27.123  28.295  1.00 34.72 ? 413  HOH H O   1 
HETATM 3993 O O   . HOH V 5 .   ? 9.117   35.959  28.333  1.00 39.22 ? 414  HOH H O   1 
HETATM 3994 O O   . HOH V 5 .   ? -0.303  20.729  -5.339  1.00 32.06 ? 415  HOH H O   1 
HETATM 3995 O O   . HOH V 5 .   ? 8.177   31.343  -11.995 1.00 23.57 ? 416  HOH H O   1 
HETATM 3996 O O   . HOH V 5 .   ? 23.073  5.769   14.113  1.00 31.56 ? 417  HOH H O   1 
HETATM 3997 O O   . HOH V 5 .   ? -10.116 8.811   21.606  1.00 42.38 ? 418  HOH H O   1 
HETATM 3998 O O   . HOH V 5 .   ? -2.763  20.553  1.694   1.00 32.91 ? 419  HOH H O   1 
HETATM 3999 O O   . HOH V 5 .   ? 11.705  17.078  -4.671  1.00 23.11 ? 420  HOH H O   1 
HETATM 4000 O O   . HOH V 5 .   ? -11.245 22.148  13.540  1.00 30.20 ? 421  HOH H O   1 
HETATM 4001 O O   . HOH V 5 .   ? -4.155  21.982  5.162   1.00 26.36 ? 422  HOH H O   1 
HETATM 4002 O O   . HOH V 5 .   ? -10.420 21.962  28.272  1.00 38.70 ? 423  HOH H O   1 
HETATM 4003 O O   . HOH V 5 .   ? 22.080  33.479  9.517   1.00 41.72 ? 424  HOH H O   1 
HETATM 4004 O O   . HOH V 5 .   ? -3.686  18.742  32.328  1.00 34.26 ? 425  HOH H O   1 
HETATM 4005 O O   . HOH V 5 .   ? -1.682  37.541  40.156  1.00 38.27 ? 426  HOH H O   1 
HETATM 4006 O O   . HOH V 5 .   ? 5.011   30.414  0.901   1.00 24.56 ? 427  HOH H O   1 
HETATM 4007 O O   . HOH V 5 .   ? 16.978  8.179   14.371  1.00 19.58 ? 428  HOH H O   1 
HETATM 4008 O O   . HOH V 5 .   ? -4.681  19.805  30.104  1.00 25.55 ? 429  HOH H O   1 
HETATM 4009 O O   . HOH V 5 .   ? 1.174   27.630  -6.419  1.00 31.71 ? 430  HOH H O   1 
HETATM 4010 O O   . HOH V 5 .   ? -1.375  27.984  12.165  1.00 36.43 ? 431  HOH H O   1 
HETATM 4011 O O   . HOH V 5 .   ? 6.096   8.041   2.914   1.00 45.21 ? 432  HOH H O   1 
HETATM 4012 O O   . HOH V 5 .   ? 14.408  17.422  -4.472  1.00 21.33 ? 433  HOH H O   1 
HETATM 4013 O O   . HOH V 5 .   ? -3.505  20.893  -1.048  1.00 35.29 ? 434  HOH H O   1 
HETATM 4014 O O   . HOH V 5 .   ? 10.930  38.239  10.519  1.00 48.39 ? 435  HOH H O   1 
HETATM 4015 O O   . HOH V 5 .   ? 18.517  32.523  3.221   1.00 29.65 ? 436  HOH H O   1 
HETATM 4016 O O   . HOH V 5 .   ? 19.008  15.532  9.693   1.00 25.27 ? 437  HOH H O   1 
HETATM 4017 O O   . HOH V 5 .   ? 11.515  22.303  20.762  1.00 25.43 ? 438  HOH H O   1 
HETATM 4018 O O   . HOH V 5 .   ? -7.008  7.896   24.115  1.00 23.14 ? 439  HOH H O   1 
HETATM 4019 O O   . HOH V 5 .   ? -3.947  16.620  7.470   1.00 20.33 ? 440  HOH H O   1 
HETATM 4020 O O   . HOH V 5 .   ? -4.470  11.598  26.209  1.00 20.35 ? 441  HOH H O   1 
HETATM 4021 O O   . HOH V 5 .   ? 26.313  24.396  4.573   1.00 35.16 ? 442  HOH H O   1 
HETATM 4022 O O   . HOH V 5 .   ? 6.525   36.435  28.405  1.00 34.76 ? 443  HOH H O   1 
HETATM 4023 O O   . HOH V 5 .   ? 14.517  30.817  19.577  1.00 40.80 ? 444  HOH H O   1 
HETATM 4024 O O   . HOH V 5 .   ? 22.962  27.655  6.867   1.00 31.80 ? 445  HOH H O   1 
HETATM 4025 O O   . HOH V 5 .   ? -1.828  25.604  5.506   1.00 43.85 ? 446  HOH H O   1 
HETATM 4026 O O   . HOH V 5 .   ? 16.375  22.634  -2.689  1.00 24.55 ? 447  HOH H O   1 
HETATM 4027 O O   . HOH V 5 .   ? 1.548   37.718  25.160  1.00 31.74 ? 448  HOH H O   1 
HETATM 4028 O O   . HOH V 5 .   ? 14.742  23.851  31.122  1.00 46.96 ? 449  HOH H O   1 
HETATM 4029 O O   . HOH V 5 .   ? 6.180   9.925   8.946   1.00 23.73 ? 450  HOH H O   1 
HETATM 4030 O O   . HOH V 5 .   ? 14.807  15.507  24.810  1.00 32.26 ? 451  HOH H O   1 
HETATM 4031 O O   . HOH V 5 .   ? 15.535  20.219  2.502   1.00 32.02 ? 452  HOH H O   1 
HETATM 4032 O O   . HOH V 5 .   ? 13.623  3.926   5.285   1.00 33.69 ? 453  HOH H O   1 
HETATM 4033 O O   . HOH V 5 .   ? -0.768  21.958  34.618  1.00 21.43 ? 454  HOH H O   1 
HETATM 4034 O O   . HOH V 5 .   ? -6.579  30.583  16.647  1.00 24.71 ? 455  HOH H O   1 
HETATM 4035 O O   . HOH V 5 .   ? -1.194  29.737  42.299  1.00 30.54 ? 456  HOH H O   1 
HETATM 4036 O O   . HOH V 5 .   ? -7.191  27.949  14.994  1.00 29.22 ? 457  HOH H O   1 
HETATM 4037 O O   . HOH V 5 .   ? -10.382 21.047  24.302  1.00 31.86 ? 458  HOH H O   1 
HETATM 4038 O O   . HOH V 5 .   ? 23.062  5.912   10.150  1.00 43.40 ? 459  HOH H O   1 
HETATM 4039 O O   . HOH V 5 .   ? -3.257  23.644  -9.139  1.00 37.32 ? 460  HOH H O   1 
HETATM 4040 O O   . HOH V 5 .   ? -6.562  38.620  25.886  1.00 37.27 ? 461  HOH H O   1 
HETATM 4041 O O   . HOH V 5 .   ? 11.192  25.619  -5.543  1.00 24.45 ? 462  HOH H O   1 
HETATM 4042 O O   . HOH V 5 .   ? -3.312  17.466  1.248   1.00 35.66 ? 463  HOH H O   1 
HETATM 4043 O O   . HOH V 5 .   ? 18.204  33.901  9.457   1.00 33.19 ? 464  HOH H O   1 
HETATM 4044 O O   . HOH V 5 .   ? 9.934   10.248  24.058  1.00 22.60 ? 465  HOH H O   1 
HETATM 4045 O O   . HOH V 5 .   ? 1.354   25.355  -4.663  1.00 27.56 ? 466  HOH H O   1 
HETATM 4046 O O   . HOH V 5 .   ? 9.738   30.868  21.337  1.00 30.05 ? 467  HOH H O   1 
HETATM 4047 O O   . HOH V 5 .   ? 14.609  39.463  -6.863  1.00 48.74 ? 468  HOH H O   1 
HETATM 4048 O O   . HOH V 5 .   ? 22.787  15.782  -2.724  1.00 48.96 ? 469  HOH H O   1 
HETATM 4049 O O   . HOH V 5 .   ? -9.084  8.279   19.163  1.00 41.16 ? 470  HOH H O   1 
HETATM 4050 O O   . HOH V 5 .   ? 7.483   29.607  29.698  1.00 21.48 ? 471  HOH H O   1 
HETATM 4051 O O   . HOH V 5 .   ? -3.526  34.179  40.885  1.00 31.03 ? 472  HOH H O   1 
HETATM 4052 O O   . HOH V 5 .   ? 19.839  37.557  8.522   1.00 45.67 ? 473  HOH H O   1 
HETATM 4053 O O   . HOH V 5 .   ? 23.574  13.889  19.189  1.00 28.17 ? 474  HOH H O   1 
HETATM 4054 O O   . HOH V 5 .   ? 11.068  14.231  25.564  1.00 33.06 ? 475  HOH H O   1 
HETATM 4055 O O   . HOH V 5 .   ? 19.530  6.588   8.463   1.00 33.98 ? 476  HOH H O   1 
HETATM 4056 O O   . HOH V 5 .   ? 20.516  21.579  -3.431  1.00 29.30 ? 477  HOH H O   1 
HETATM 4057 O O   . HOH V 5 .   ? -3.505  43.256  24.546  1.00 40.25 ? 478  HOH H O   1 
HETATM 4058 O O   . HOH V 5 .   ? -10.812 14.573  24.320  1.00 38.85 ? 479  HOH H O   1 
HETATM 4059 O O   . HOH V 5 .   ? 11.166  13.626  18.060  1.00 17.36 ? 480  HOH H O   1 
HETATM 4060 O O   . HOH V 5 .   ? 6.378   9.297   6.377   1.00 28.25 ? 481  HOH H O   1 
HETATM 4061 O O   . HOH V 5 .   ? 16.938  10.584  7.338   1.00 20.67 ? 482  HOH H O   1 
HETATM 4062 O O   . HOH V 5 .   ? 2.359   31.610  -1.992  1.00 35.12 ? 483  HOH H O   1 
HETATM 4063 O O   . HOH V 5 .   ? 13.844  39.828  4.900   1.00 35.91 ? 484  HOH H O   1 
HETATM 4064 O O   . HOH V 5 .   ? 9.568   30.144  23.910  1.00 34.30 ? 485  HOH H O   1 
HETATM 4065 O O   . HOH V 5 .   ? -3.277  17.936  24.428  1.00 17.52 ? 486  HOH H O   1 
HETATM 4066 O O   . HOH V 5 .   ? -3.239  6.659   22.099  1.00 30.12 ? 487  HOH H O   1 
HETATM 4067 O O   . HOH V 5 .   ? -5.477  23.758  11.012  1.00 27.06 ? 488  HOH H O   1 
HETATM 4068 O O   . HOH V 5 .   ? 14.829  19.570  25.836  1.00 37.24 ? 489  HOH H O   1 
HETATM 4069 O O   . HOH V 5 .   ? 18.137  38.479  -0.657  1.00 45.19 ? 490  HOH H O   1 
HETATM 4070 O O   . HOH V 5 .   ? 10.839  37.479  22.578  1.00 52.45 ? 491  HOH H O   1 
HETATM 4071 O O   . HOH V 5 .   ? 5.944   35.466  37.108  1.00 20.88 ? 492  HOH H O   1 
HETATM 4072 O O   . HOH V 5 .   ? 15.770  17.440  20.800  1.00 35.06 ? 493  HOH H O   1 
HETATM 4073 O O   . HOH V 5 .   ? 0.242   22.684  7.606   1.00 18.47 ? 494  HOH H O   1 
HETATM 4074 O O   . HOH V 5 .   ? 24.928  23.724  12.622  1.00 33.77 ? 495  HOH H O   1 
HETATM 4075 O O   . HOH V 5 .   ? 9.863   27.791  35.366  1.00 24.62 ? 496  HOH H O   1 
HETATM 4076 O O   . HOH V 5 .   ? 12.519  22.288  27.099  1.00 30.43 ? 497  HOH H O   1 
HETATM 4077 O O   . HOH V 5 .   ? -1.283  23.026  5.377   1.00 21.09 ? 498  HOH H O   1 
HETATM 4078 O O   . HOH V 5 .   ? -3.530  32.355  12.762  1.00 42.37 ? 499  HOH H O   1 
HETATM 4079 O O   . HOH V 5 .   ? 11.195  28.465  33.080  1.00 30.30 ? 500  HOH H O   1 
HETATM 4080 O O   . HOH V 5 .   ? 24.801  11.092  8.154   1.00 28.29 ? 501  HOH H O   1 
HETATM 4081 O O   . HOH V 5 .   ? -1.002  39.088  37.399  1.00 34.39 ? 502  HOH H O   1 
HETATM 4082 O O   . HOH V 5 .   ? 8.307   33.989  -11.811 1.00 41.96 ? 503  HOH H O   1 
HETATM 4083 O O   . HOH V 5 .   ? 15.613  34.158  -8.705  1.00 36.67 ? 504  HOH H O   1 
HETATM 4084 O O   . HOH V 5 .   ? 3.036   27.221  -8.328  1.00 18.76 ? 505  HOH H O   1 
HETATM 4085 O O   . HOH V 5 .   ? 10.202  10.840  21.363  1.00 27.09 ? 506  HOH H O   1 
HETATM 4086 O O   . HOH V 5 .   ? 23.837  14.497  -0.831  1.00 40.89 ? 507  HOH H O   1 
HETATM 4087 O O   . HOH V 5 .   ? 11.126  10.724  -2.062  1.00 35.24 ? 508  HOH H O   1 
HETATM 4088 O O   . HOH V 5 .   ? -8.359  28.216  21.928  1.00 28.29 ? 509  HOH H O   1 
HETATM 4089 O O   . HOH V 5 .   ? -5.679  22.004  7.319   1.00 28.26 ? 510  HOH H O   1 
HETATM 4090 O O   . HOH V 5 .   ? 4.714   14.338  31.211  1.00 24.13 ? 511  HOH H O   1 
HETATM 4091 O O   . HOH V 5 .   ? -0.814  10.384  6.418   1.00 33.27 ? 512  HOH H O   1 
HETATM 4092 O O   . HOH V 5 .   ? -6.996  26.621  11.694  1.00 35.83 ? 513  HOH H O   1 
HETATM 4093 O O   . HOH V 5 .   ? -1.125  24.302  9.440   1.00 18.40 ? 514  HOH H O   1 
HETATM 4094 O O   . HOH V 5 .   ? 3.044   36.791  20.572  1.00 50.77 ? 515  HOH H O   1 
HETATM 4095 O O   . HOH V 5 .   ? -0.636  16.990  1.375   1.00 22.70 ? 516  HOH H O   1 
HETATM 4096 O O   . HOH V 5 .   ? -9.427  19.245  -1.965  1.00 42.05 ? 517  HOH H O   1 
HETATM 4097 O O   . HOH V 5 .   ? -2.848  32.726  -3.570  1.00 34.36 ? 518  HOH H O   1 
HETATM 4098 O O   . HOH V 5 .   ? -2.687  8.472   18.264  1.00 27.02 ? 519  HOH H O   1 
HETATM 4099 O O   . HOH V 5 .   ? 9.608   31.095  29.288  1.00 34.61 ? 520  HOH H O   1 
HETATM 4100 O O   . HOH V 5 .   ? -3.426  40.517  36.402  1.00 40.80 ? 521  HOH H O   1 
HETATM 4101 O O   . HOH V 5 .   ? -3.020  26.801  39.058  1.00 27.49 ? 522  HOH H O   1 
HETATM 4102 O O   . HOH V 5 .   ? 19.974  34.331  11.241  1.00 44.22 ? 523  HOH H O   1 
HETATM 4103 O O   . HOH V 5 .   ? -7.221  29.999  38.059  1.00 37.98 ? 524  HOH H O   1 
HETATM 4104 O O   . HOH V 5 .   ? 2.110   30.492  8.132   1.00 38.24 ? 525  HOH H O   1 
HETATM 4105 O O   . HOH V 5 .   ? -4.407  28.477  40.298  1.00 43.97 ? 526  HOH H O   1 
HETATM 4106 O O   . HOH V 5 .   ? 12.000  24.841  28.836  1.00 38.72 ? 527  HOH H O   1 
HETATM 4107 O O   . HOH V 5 .   ? 5.471   41.351  1.642   1.00 50.31 ? 528  HOH H O   1 
HETATM 4108 O O   . HOH V 5 .   ? -9.215  18.237  26.170  1.00 36.73 ? 529  HOH H O   1 
HETATM 4109 O O   . HOH V 5 .   ? 26.416  13.462  10.191  1.00 34.62 ? 530  HOH H O   1 
HETATM 4110 O O   . HOH V 5 .   ? 3.239   39.642  -5.091  1.00 35.27 ? 531  HOH H O   1 
HETATM 4111 O O   . HOH V 5 .   ? 2.394   14.427  -0.919  1.00 41.70 ? 532  HOH H O   1 
HETATM 4112 O O   . HOH V 5 .   ? 7.014   39.474  36.548  1.00 37.06 ? 533  HOH H O   1 
HETATM 4113 O O   . HOH V 5 .   ? 22.504  11.019  15.880  1.00 27.52 ? 534  HOH H O   1 
HETATM 4114 O O   . HOH V 5 .   ? -9.512  35.940  28.190  1.00 35.34 ? 535  HOH H O   1 
HETATM 4115 O O   . HOH V 5 .   ? 5.208   14.361  -1.635  1.00 19.60 ? 536  HOH H O   1 
HETATM 4116 O O   . HOH V 5 .   ? -12.784 14.057  21.707  1.00 40.66 ? 537  HOH H O   1 
HETATM 4117 O O   . HOH V 5 .   ? 1.687   28.823  -2.329  1.00 35.50 ? 538  HOH H O   1 
HETATM 4118 O O   . HOH V 5 .   ? -10.854 25.444  20.540  1.00 38.28 ? 539  HOH H O   1 
HETATM 4119 O O   . HOH V 5 .   ? -6.980  42.078  28.925  1.00 40.26 ? 540  HOH H O   1 
HETATM 4120 O O   . HOH V 5 .   ? 23.499  33.379  4.904   1.00 41.00 ? 541  HOH H O   1 
HETATM 4121 O O   . HOH V 5 .   ? -3.361  8.946   15.375  1.00 38.96 ? 542  HOH H O   1 
HETATM 4122 O O   . HOH V 5 .   ? 8.141   34.713  35.145  1.00 27.07 ? 543  HOH H O   1 
HETATM 4123 O O   . HOH V 5 .   ? 1.310   15.661  2.753   1.00 28.47 ? 544  HOH H O   1 
HETATM 4124 O O   . HOH V 5 .   ? 18.760  16.214  -2.420  1.00 25.39 ? 545  HOH H O   1 
HETATM 4125 O O   . HOH V 5 .   ? -6.551  32.186  33.664  1.00 32.73 ? 546  HOH H O   1 
HETATM 4126 O O   . HOH V 5 .   ? 2.735   18.056  36.440  1.00 30.24 ? 547  HOH H O   1 
HETATM 4127 O O   . HOH V 5 .   ? 8.813   32.353  36.313  1.00 33.18 ? 548  HOH H O   1 
HETATM 4128 O O   . HOH V 5 .   ? 7.796   9.911   20.579  1.00 27.12 ? 549  HOH H O   1 
HETATM 4129 O O   . HOH V 5 .   ? -8.149  29.640  30.882  1.00 35.46 ? 550  HOH H O   1 
HETATM 4130 O O   . HOH V 5 .   ? 18.710  32.462  -2.664  1.00 33.51 ? 551  HOH H O   1 
HETATM 4131 O O   . HOH V 5 .   ? 16.633  35.795  8.848   1.00 28.12 ? 552  HOH H O   1 
HETATM 4132 O O   . HOH V 5 .   ? -5.447  12.948  28.516  1.00 25.06 ? 553  HOH H O   1 
HETATM 4133 O O   . HOH V 5 .   ? 12.843  25.244  -7.521  1.00 41.67 ? 554  HOH H O   1 
HETATM 4134 O O   . HOH V 5 .   ? 6.438   46.562  -0.649  1.00 47.93 ? 555  HOH H O   1 
HETATM 4135 O O   . HOH V 5 .   ? 19.810  25.692  16.465  1.00 37.93 ? 556  HOH H O   1 
HETATM 4136 O O   . HOH V 5 .   ? -3.143  19.825  -5.758  1.00 38.91 ? 557  HOH H O   1 
HETATM 4137 O O   . HOH V 5 .   ? 3.885   40.663  21.830  1.00 54.35 ? 558  HOH H O   1 
HETATM 4138 O O   . HOH V 5 .   ? 8.559   33.801  13.613  1.00 26.69 ? 559  HOH H O   1 
HETATM 4139 O O   . HOH V 5 .   ? -10.237 35.611  21.322  1.00 33.59 ? 560  HOH H O   1 
HETATM 4140 O O   . HOH V 5 .   ? 16.286  23.154  -5.210  1.00 32.43 ? 561  HOH H O   1 
HETATM 4141 O O   . HOH V 5 .   ? 5.076   35.520  40.896  1.00 37.98 ? 562  HOH H O   1 
HETATM 4142 O O   . HOH V 5 .   ? 23.533  25.229  -3.021  1.00 45.74 ? 563  HOH H O   1 
HETATM 4143 O O   . HOH V 5 .   ? -8.519  10.821  27.162  1.00 34.56 ? 564  HOH H O   1 
HETATM 4144 O O   . HOH V 5 .   ? -3.563  27.603  10.984  1.00 42.72 ? 565  HOH H O   1 
HETATM 4145 O O   . HOH V 5 .   ? -5.092  14.303  2.772   1.00 46.84 ? 566  HOH H O   1 
HETATM 4146 O O   . HOH V 5 .   ? 20.928  32.709  -1.879  1.00 48.07 ? 567  HOH H O   1 
HETATM 4147 O O   . HOH V 5 .   ? 16.393  30.133  18.043  1.00 50.09 ? 568  HOH H O   1 
HETATM 4148 O O   . HOH V 5 .   ? -7.702  22.262  5.417   1.00 38.65 ? 569  HOH H O   1 
HETATM 4149 O O   . HOH V 5 .   ? -9.775  24.484  1.598   1.00 57.92 ? 570  HOH H O   1 
HETATM 4150 O O   . HOH V 5 .   ? 22.288  4.308   12.184  1.00 53.50 ? 571  HOH H O   1 
HETATM 4151 O O   . HOH V 5 .   ? -4.787  23.367  -7.028  1.00 36.83 ? 572  HOH H O   1 
HETATM 4152 O O   . HOH V 5 .   ? 24.062  30.035  6.858   1.00 54.17 ? 573  HOH H O   1 
HETATM 4153 O O   . HOH V 5 .   ? 17.512  30.666  -5.733  1.00 37.50 ? 574  HOH H O   1 
HETATM 4154 O O   . HOH V 5 .   ? 19.435  34.602  -3.497  1.00 37.21 ? 575  HOH H O   1 
HETATM 4155 O O   . HOH V 5 .   ? 0.223   12.858  32.148  1.00 39.50 ? 576  HOH H O   1 
HETATM 4156 O O   . HOH V 5 .   ? 0.743   28.105  0.005   1.00 34.54 ? 577  HOH H O   1 
HETATM 4157 O O   . HOH V 5 .   ? -1.421  25.788  40.958  1.00 30.10 ? 578  HOH H O   1 
HETATM 4158 O O   . HOH V 5 .   ? 17.303  18.363  22.683  1.00 35.39 ? 579  HOH H O   1 
HETATM 4159 O O   . HOH V 5 .   ? 7.602   38.011  7.715   1.00 39.31 ? 580  HOH H O   1 
HETATM 4160 O O   . HOH V 5 .   ? -4.222  20.025  37.589  1.00 51.15 ? 581  HOH H O   1 
HETATM 4161 O O   . HOH V 5 .   ? 8.650   27.382  29.187  1.00 37.57 ? 582  HOH H O   1 
HETATM 4162 O O   . HOH V 5 .   ? 22.117  20.360  -2.330  1.00 46.56 ? 583  HOH H O   1 
HETATM 4163 O O   . HOH V 5 .   ? 13.418  36.954  -11.429 1.00 49.57 ? 584  HOH H O   1 
HETATM 4164 O O   . HOH V 5 .   ? 19.052  7.714   15.962  1.00 18.69 ? 585  HOH H O   1 
HETATM 4165 O O   . HOH V 5 .   ? 2.289   39.766  26.543  1.00 36.25 ? 586  HOH H O   1 
HETATM 4166 O O   . HOH V 5 .   ? -2.015  33.098  43.042  1.00 27.37 ? 587  HOH H O   1 
HETATM 4167 O O   . HOH V 5 .   ? -0.812  15.211  32.805  1.00 45.12 ? 588  HOH H O   1 
HETATM 4168 O O   . HOH V 5 .   ? 15.984  17.838  24.703  1.00 39.50 ? 589  HOH H O   1 
HETATM 4169 O O   . HOH V 5 .   ? 17.999  23.220  23.451  1.00 47.77 ? 590  HOH H O   1 
HETATM 4170 O O   . HOH V 5 .   ? 16.292  15.427  -4.130  1.00 37.24 ? 591  HOH H O   1 
HETATM 4171 O O   . HOH V 5 .   ? 29.514  12.807  6.562   1.00 54.80 ? 592  HOH H O   1 
HETATM 4172 O O   . HOH V 5 .   ? 26.699  11.676  16.976  1.00 45.72 ? 593  HOH H O   1 
HETATM 4173 O O   . HOH V 5 .   ? -8.405  28.519  12.840  1.00 50.39 ? 594  HOH H O   1 
HETATM 4174 O O   . HOH V 5 .   ? 8.564   37.888  24.295  1.00 45.04 ? 595  HOH H O   1 
HETATM 4175 O O   . HOH V 5 .   ? -5.537  24.121  8.429   1.00 39.63 ? 596  HOH H O   1 
HETATM 4176 O O   . HOH V 5 .   ? 11.056  26.093  26.087  1.00 59.02 ? 597  HOH H O   1 
HETATM 4177 O O   . HOH V 5 .   ? 14.579  42.715  -10.755 1.00 44.80 ? 598  HOH H O   1 
HETATM 4178 O O   . HOH V 5 .   ? -3.032  25.094  8.074   1.00 41.19 ? 599  HOH H O   1 
HETATM 4179 O O   . HOH V 5 .   ? 10.752  14.482  -4.692  1.00 28.03 ? 600  HOH H O   1 
HETATM 4180 O O   . HOH V 5 .   ? 15.362  18.525  -6.579  1.00 29.40 ? 601  HOH H O   1 
HETATM 4181 O O   . HOH V 5 .   ? 3.930   47.444  -0.978  1.00 52.33 ? 602  HOH H O   1 
HETATM 4182 O O   . HOH V 5 .   ? 4.134   40.742  32.480  1.00 44.99 ? 603  HOH H O   1 
HETATM 4183 O O   . HOH V 5 .   ? 25.610  6.158   10.220  1.00 43.82 ? 604  HOH H O   1 
HETATM 4184 O O   . HOH V 5 .   ? 4.690   39.966  26.241  1.00 52.08 ? 605  HOH H O   1 
HETATM 4185 O O   . HOH V 5 .   ? 16.355  20.834  -6.899  1.00 42.92 ? 606  HOH H O   1 
HETATM 4186 O O   . HOH V 5 .   ? -15.712 7.914   18.425  1.00 46.95 ? 607  HOH H O   1 
HETATM 4187 O O   . HOH W 5 .   ? 23.274  10.069  26.915  1.00 30.09 ? 201  HOH M O   1 
HETATM 4188 O O   . HOH W 5 .   ? 14.255  10.820  32.601  1.00 42.90 ? 202  HOH M O   1 
HETATM 4189 O O   . HOH W 5 .   ? 12.289  8.435   21.147  1.00 27.03 ? 203  HOH M O   1 
HETATM 4190 O O   . HOH W 5 .   ? 8.593   7.477   24.748  1.00 20.69 ? 204  HOH M O   1 
HETATM 4191 O O   . HOH W 5 .   ? 21.472  12.356  27.507  1.00 37.54 ? 205  HOH M O   1 
HETATM 4192 O O   . HOH W 5 .   ? 17.110  10.140  22.462  1.00 20.56 ? 206  HOH M O   1 
HETATM 4193 O O   . HOH W 5 .   ? 7.683   8.401   35.420  1.00 39.12 ? 207  HOH M O   1 
HETATM 4194 O O   . HOH W 5 .   ? 8.325   11.715  30.500  1.00 25.13 ? 208  HOH M O   1 
HETATM 4195 O O   . HOH W 5 .   ? 12.201  5.901   22.455  1.00 22.19 ? 209  HOH M O   1 
HETATM 4196 O O   . HOH W 5 .   ? 18.508  13.541  31.686  1.00 34.92 ? 210  HOH M O   1 
HETATM 4197 O O   . HOH W 5 .   ? 12.822  10.904  30.353  1.00 28.63 ? 211  HOH M O   1 
HETATM 4198 O O   . HOH W 5 .   ? 10.397  8.895   35.021  1.00 41.67 ? 212  HOH M O   1 
HETATM 4199 O O   . HOH W 5 .   ? 14.556  8.546   29.570  1.00 4.68  ? 213  HOH M O   1 
HETATM 4200 O O   . HOH X 5 .   ? 17.361  6.774   7.262   1.00 32.49 ? 201  HOH N O   1 
HETATM 4201 O O   . HOH X 5 .   ? -0.525  6.168   10.918  1.00 45.79 ? 202  HOH N O   1 
HETATM 4202 O O   . HOH X 5 .   ? 6.586   6.246   7.560   1.00 41.83 ? 203  HOH N O   1 
HETATM 4203 O O   . HOH X 5 .   ? 10.755  11.087  16.982  1.00 23.84 ? 204  HOH N O   1 
HETATM 4204 O O   . HOH X 5 .   ? 6.393   9.619   17.217  1.00 32.85 ? 205  HOH N O   1 
HETATM 4205 O O   . HOH X 5 .   ? 14.594  6.686   14.309  1.00 19.74 ? 206  HOH N O   1 
HETATM 4206 O O   . HOH X 5 .   ? 11.260  8.595   18.129  1.00 29.93 ? 207  HOH N O   1 
HETATM 4207 O O   . HOH X 5 .   ? 2.733   5.355   12.661  1.00 26.08 ? 208  HOH N O   1 
HETATM 4208 O O   . HOH X 5 .   ? 6.469   6.055   10.158  1.00 31.94 ? 209  HOH N O   1 
HETATM 4209 O O   . HOH X 5 .   ? 10.665  3.200   5.733   1.00 37.64 ? 210  HOH N O   1 
HETATM 4210 O O   . HOH X 5 .   ? 8.586   8.475   9.847   1.00 5.82  ? 211  HOH N O   1 
HETATM 4211 O O   . HOH X 5 .   ? 12.755  1.545   9.906   1.00 45.78 ? 212  HOH N O   1 
HETATM 4212 O O   . HOH X 5 .   ? 2.289   5.413   8.344   1.00 50.16 ? 213  HOH N O   1 
HETATM 4213 O O   . HOH X 5 .   ? 11.338  1.514   7.874   1.00 39.85 ? 214  HOH N 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 1   ? 0.5082 0.6009 0.5020 0.0320  -0.0139 0.0139  1    GLN A N   
2    C CA  . GLN A 1   ? 0.4606 0.5599 0.4569 0.0314  -0.0104 0.0158  1    GLN A CA  
3    C C   . GLN A 1   ? 0.3651 0.4657 0.3680 0.0269  -0.0095 0.0163  1    GLN A C   
4    O O   . GLN A 1   ? 0.3360 0.4407 0.3404 0.0268  -0.0080 0.0166  1    GLN A O   
5    C CB  . GLN A 1   ? 0.5123 0.6153 0.5066 0.0323  -0.0078 0.0183  1    GLN A CB  
6    C CG  . GLN A 1   ? 0.5527 0.6611 0.5521 0.0286  -0.0047 0.0210  1    GLN A CG  
7    C CD  . GLN A 1   ? 0.6404 0.7537 0.6375 0.0298  -0.0017 0.0237  1    GLN A CD  
8    O OE1 . GLN A 1   ? 0.7214 0.8338 0.7129 0.0334  -0.0019 0.0238  1    GLN A OE1 
9    N NE2 . GLN A 1   ? 0.6708 0.7897 0.6721 0.0267  0.0009  0.0259  1    GLN A NE2 
10   N N   . VAL A 2   ? 0.2987 0.3958 0.3050 0.0237  -0.0107 0.0160  2    VAL A N   
11   C CA  . VAL A 2   ? 0.2594 0.3566 0.2706 0.0204  -0.0105 0.0155  2    VAL A CA  
12   C C   . VAL A 2   ? 0.2438 0.3387 0.2534 0.0218  -0.0123 0.0134  2    VAL A C   
13   O O   . VAL A 2   ? 0.2243 0.3146 0.2309 0.0234  -0.0149 0.0118  2    VAL A O   
14   C CB  . VAL A 2   ? 0.2615 0.3558 0.2764 0.0173  -0.0111 0.0156  2    VAL A CB  
15   C CG1 . VAL A 2   ? 0.2525 0.3461 0.2711 0.0146  -0.0112 0.0147  2    VAL A CG1 
16   C CG2 . VAL A 2   ? 0.2673 0.3632 0.2837 0.0156  -0.0090 0.0178  2    VAL A CG2 
17   N N   . GLN A 3   ? 0.2451 0.3426 0.2566 0.0210  -0.0113 0.0134  3    GLN A N   
18   C CA  . GLN A 3   ? 0.2476 0.3425 0.2573 0.0224  -0.0129 0.0117  3    GLN A CA  
19   C C   . GLN A 3   ? 0.2126 0.3087 0.2262 0.0195  -0.0120 0.0119  3    GLN A C   
20   O O   . GLN A 3   ? 0.2050 0.3060 0.2216 0.0178  -0.0100 0.0133  3    GLN A O   
21   C CB  . GLN A 3   ? 0.2969 0.3943 0.3023 0.0268  -0.0125 0.0114  3    GLN A CB  
22   C CG  . GLN A 3   ? 0.3682 0.4637 0.3683 0.0304  -0.0134 0.0110  3    GLN A CG  
23   C CD  . GLN A 3   ? 0.4397 0.5275 0.4361 0.0313  -0.0168 0.0088  3    GLN A CD  
24   O OE1 . GLN A 3   ? 0.5656 0.6500 0.5639 0.0287  -0.0183 0.0085  3    GLN A OE1 
25   N NE2 . GLN A 3   ? 0.5386 0.6233 0.5294 0.0352  -0.0182 0.0072  3    GLN A NE2 
26   N N   . LEU A 4   ? 0.2196 0.3112 0.2330 0.0187  -0.0137 0.0105  4    LEU A N   
27   C CA  . LEU A 4   ? 0.2083 0.3003 0.2239 0.0167  -0.0133 0.0104  4    LEU A CA  
28   C C   . LEU A 4   ? 0.2259 0.3144 0.2373 0.0194  -0.0150 0.0091  4    LEU A C   
29   O O   . LEU A 4   ? 0.2416 0.3239 0.2510 0.0191  -0.0171 0.0079  4    LEU A O   
30   C CB  . LEU A 4   ? 0.2040 0.2933 0.2231 0.0128  -0.0133 0.0104  4    LEU A CB  
31   C CG  . LEU A 4   ? 0.2010 0.2925 0.2238 0.0103  -0.0117 0.0116  4    LEU A CG  
32   C CD1 . LEU A 4   ? 0.2026 0.2912 0.2283 0.0074  -0.0118 0.0112  4    LEU A CD1 
33   C CD2 . LEU A 4   ? 0.1957 0.2922 0.2203 0.0093  -0.0097 0.0128  4    LEU A CD2 
34   N N   . GLN A 5   ? 0.2141 0.3063 0.2242 0.0219  -0.0143 0.0093  5    GLN A N   
35   C CA  . GLN A 5   ? 0.2324 0.3211 0.2374 0.0256  -0.0160 0.0080  5    GLN A CA  
36   C C   . GLN A 5   ? 0.2144 0.3027 0.2206 0.0242  -0.0160 0.0081  5    GLN A C   
37   O O   . GLN A 5   ? 0.2153 0.3102 0.2242 0.0240  -0.0145 0.0091  5    GLN A O   
38   C CB  . GLN A 5   ? 0.2691 0.3627 0.2714 0.0304  -0.0152 0.0082  5    GLN A CB  
39   C CG  . GLN A 5   ? 0.3438 0.4334 0.3403 0.0349  -0.0169 0.0069  5    GLN A CG  
40   C CD  . GLN A 5   ? 0.4209 0.5009 0.4119 0.0361  -0.0196 0.0051  5    GLN A CD  
41   O OE1 . GLN A 5   ? 0.4802 0.5576 0.4716 0.0342  -0.0203 0.0049  5    GLN A OE1 
42   N NE2 . GLN A 5   ? 0.5271 0.6015 0.5126 0.0393  -0.0214 0.0039  5    GLN A NE2 
43   N N   . GLN A 6   ? 0.2033 0.2843 0.2071 0.0233  -0.0178 0.0071  6    GLN A N   
44   C CA  . GLN A 6   ? 0.2060 0.2856 0.2100 0.0221  -0.0179 0.0073  6    GLN A CA  
45   C C   . GLN A 6   ? 0.2236 0.3012 0.2223 0.0267  -0.0192 0.0066  6    GLN A C   
46   O O   . GLN A 6   ? 0.2443 0.3189 0.2383 0.0306  -0.0205 0.0056  6    GLN A O   
47   C CB  . GLN A 6   ? 0.1952 0.2683 0.1996 0.0184  -0.0188 0.0070  6    GLN A CB  
48   C CG  . GLN A 6   ? 0.1805 0.2558 0.1900 0.0146  -0.0175 0.0076  6    GLN A CG  
49   C CD  . GLN A 6   ? 0.1767 0.2473 0.1874 0.0110  -0.0179 0.0076  6    GLN A CD  
50   O OE1 . GLN A 6   ? 0.1647 0.2345 0.1779 0.0090  -0.0181 0.0075  6    GLN A OE1 
51   N NE2 . GLN A 6   ? 0.1826 0.2502 0.1916 0.0103  -0.0181 0.0077  6    GLN A NE2 
52   N N   . SER A 7   ? 0.2352 0.3138 0.2341 0.0265  -0.0190 0.0070  7    SER A N   
53   C CA  . SER A 7   ? 0.2501 0.3262 0.2439 0.0308  -0.0204 0.0065  7    SER A CA  
54   C C   . SER A 7   ? 0.2625 0.3273 0.2504 0.0312  -0.0227 0.0055  7    SER A C   
55   O O   . SER A 7   ? 0.2492 0.3090 0.2381 0.0272  -0.0231 0.0054  7    SER A O   
56   C CB  . SER A 7   ? 0.2382 0.3188 0.2341 0.0302  -0.0198 0.0073  7    SER A CB  
57   O OG  . SER A 7   ? 0.2234 0.3024 0.2222 0.0251  -0.0192 0.0078  7    SER A OG  
58   N N   . ASP A 8   ? 0.2818 0.3430 0.2638 0.0360  -0.0242 0.0049  8    ASP A N   
59   C CA  . ASP A 8   ? 0.3092 0.3587 0.2838 0.0375  -0.0267 0.0038  8    ASP A CA  
60   C C   . ASP A 8   ? 0.3002 0.3438 0.2745 0.0334  -0.0272 0.0046  8    ASP A C   
61   O O   . ASP A 8   ? 0.2935 0.3423 0.2718 0.0312  -0.0257 0.0057  8    ASP A O   
62   C CB  . ASP A 8   ? 0.3460 0.3943 0.3144 0.0445  -0.0279 0.0031  8    ASP A CB  
63   C CG  . ASP A 8   ? 0.3895 0.4416 0.3565 0.0490  -0.0276 0.0022  8    ASP A CG  
64   O OD1 . ASP A 8   ? 0.3902 0.4437 0.3598 0.0467  -0.0270 0.0020  8    ASP A OD1 
65   O OD2 . ASP A 8   ? 0.4600 0.5133 0.4226 0.0554  -0.0280 0.0017  8    ASP A OD2 
66   N N   . ALA A 9   ? 0.3080 0.3407 0.2772 0.0324  -0.0292 0.0040  9    ALA A N   
67   C CA  . ALA A 9   ? 0.3271 0.3523 0.2943 0.0288  -0.0298 0.0048  9    ALA A CA  
68   C C   . ALA A 9   ? 0.3292 0.3552 0.2940 0.0314  -0.0297 0.0055  9    ALA A C   
69   O O   . ALA A 9   ? 0.3227 0.3507 0.2842 0.0371  -0.0303 0.0050  9    ALA A O   
70   C CB  . ALA A 9   ? 0.3517 0.3647 0.3122 0.0287  -0.0326 0.0039  9    ALA A CB  
71   N N   . GLU A 10  ? 0.3311 0.3562 0.2974 0.0275  -0.0287 0.0068  10   GLU A N   
72   C CA  . GLU A 10  ? 0.3652 0.3912 0.3295 0.0291  -0.0286 0.0077  10   GLU A CA  
73   C C   . GLU A 10  ? 0.3736 0.3885 0.3320 0.0271  -0.0297 0.0086  10   GLU A C   
74   O O   . GLU A 10  ? 0.3461 0.3573 0.3062 0.0219  -0.0291 0.0091  10   GLU A O   
75   C CB  . GLU A 10  ? 0.3793 0.4147 0.3504 0.0260  -0.0262 0.0085  10   GLU A CB  
76   C CG  . GLU A 10  ? 0.4044 0.4507 0.3816 0.0271  -0.0250 0.0081  10   GLU A CG  
77   C CD  . GLU A 10  ? 0.4462 0.5004 0.4241 0.0309  -0.0250 0.0082  10   GLU A CD  
78   O OE1 . GLU A 10  ? 0.4393 0.4900 0.4120 0.0343  -0.0264 0.0084  10   GLU A OE1 
79   O OE2 . GLU A 10  ? 0.4478 0.5118 0.4315 0.0305  -0.0236 0.0082  10   GLU A OE2 
80   N N   . LEU A 11  ? 0.3766 0.3865 0.3282 0.0314  -0.0312 0.0087  11   LEU A N   
81   C CA  . LEU A 11  ? 0.4176 0.4161 0.3623 0.0302  -0.0324 0.0098  11   LEU A CA  
82   C C   . LEU A 11  ? 0.4032 0.4053 0.3469 0.0321  -0.0319 0.0109  11   LEU A C   
83   O O   . LEU A 11  ? 0.3789 0.3849 0.3209 0.0379  -0.0329 0.0103  11   LEU A O   
84   C CB  . LEU A 11  ? 0.4621 0.4497 0.3979 0.0347  -0.0352 0.0089  11   LEU A CB  
85   C CG  . LEU A 11  ? 0.5442 0.5175 0.4735 0.0314  -0.0368 0.0096  11   LEU A CG  
86   C CD1 . LEU A 11  ? 0.5185 0.4899 0.4486 0.0261  -0.0353 0.0118  11   LEU A CD1 
87   C CD2 . LEU A 11  ? 0.5723 0.5428 0.5037 0.0280  -0.0374 0.0086  11   LEU A CD2 
88   N N   . VAL A 12  ? 0.3989 0.4009 0.3442 0.0275  -0.0304 0.0123  12   VAL A N   
89   C CA  . VAL A 12  ? 0.4169 0.4232 0.3616 0.0289  -0.0300 0.0131  12   VAL A CA  
90   C C   . VAL A 12  ? 0.4106 0.4079 0.3500 0.0258  -0.0297 0.0149  12   VAL A C   
91   O O   . VAL A 12  ? 0.3687 0.3589 0.3070 0.0216  -0.0292 0.0156  12   VAL A O   
92   C CB  . VAL A 12  ? 0.4103 0.4292 0.3635 0.0266  -0.0279 0.0129  12   VAL A CB  
93   C CG1 . VAL A 12  ? 0.4187 0.4473 0.3769 0.0298  -0.0280 0.0115  12   VAL A CG1 
94   C CG2 . VAL A 12  ? 0.4014 0.4207 0.3596 0.0202  -0.0256 0.0133  12   VAL A CG2 
95   N N   . LYS A 13  ? 0.4385 0.4369 0.3747 0.0282  -0.0302 0.0157  13   LYS A N   
96   C CA  . LYS A 13  ? 0.4711 0.4623 0.4016 0.0261  -0.0298 0.0175  13   LYS A CA  
97   C C   . LYS A 13  ? 0.4259 0.4232 0.3623 0.0207  -0.0269 0.0181  13   LYS A C   
98   O O   . LYS A 13  ? 0.3943 0.4021 0.3374 0.0204  -0.0259 0.0171  13   LYS A O   
99   C CB  . LYS A 13  ? 0.5135 0.5050 0.4385 0.0315  -0.0317 0.0179  13   LYS A CB  
100  C CG  . LYS A 13  ? 0.5778 0.5624 0.4957 0.0379  -0.0346 0.0174  13   LYS A CG  
101  C CD  . LYS A 13  ? 0.6400 0.6121 0.5474 0.0394  -0.0361 0.0192  13   LYS A CD  
102  C CE  . LYS A 13  ? 0.6769 0.6449 0.5770 0.0473  -0.0392 0.0188  13   LYS A CE  
103  N NZ  . LYS A 13  ? 0.7084 0.6676 0.6046 0.0493  -0.0406 0.0178  13   LYS A NZ  
104  N N   . PRO A 14  ? 0.4169 0.4074 0.3502 0.0164  -0.0254 0.0198  14   PRO A N   
105  C CA  . PRO A 14  ? 0.4124 0.4076 0.3491 0.0124  -0.0227 0.0205  14   PRO A CA  
106  C C   . PRO A 14  ? 0.3930 0.3953 0.3298 0.0155  -0.0234 0.0199  14   PRO A C   
107  O O   . PRO A 14  ? 0.4248 0.4247 0.3561 0.0201  -0.0257 0.0200  14   PRO A O   
108  C CB  . PRO A 14  ? 0.4268 0.4120 0.3571 0.0092  -0.0216 0.0229  14   PRO A CB  
109  C CG  . PRO A 14  ? 0.4425 0.4177 0.3684 0.0096  -0.0235 0.0233  14   PRO A CG  
110  C CD  . PRO A 14  ? 0.4535 0.4312 0.3797 0.0152  -0.0262 0.0213  14   PRO A CD  
111  N N   . GLY A 15  ? 0.3823 0.3933 0.3254 0.0131  -0.0215 0.0192  15   GLY A N   
112  C CA  . GLY A 15  ? 0.3641 0.3822 0.3079 0.0149  -0.0221 0.0185  15   GLY A CA  
113  C C   . GLY A 15  ? 0.3537 0.3811 0.3032 0.0177  -0.0236 0.0168  15   GLY A C   
114  O O   . GLY A 15  ? 0.3605 0.3954 0.3128 0.0179  -0.0238 0.0160  15   GLY A O   
115  N N   . ALA A 16  ? 0.3304 0.3577 0.2816 0.0196  -0.0244 0.0162  16   ALA A N   
116  C CA  . ALA A 16  ? 0.3271 0.3638 0.2837 0.0224  -0.0254 0.0148  16   ALA A CA  
117  C C   . ALA A 16  ? 0.2941 0.3378 0.2589 0.0183  -0.0232 0.0140  16   ALA A C   
118  O O   . ALA A 16  ? 0.2719 0.3131 0.2381 0.0139  -0.0211 0.0144  16   ALA A O   
119  C CB  . ALA A 16  ? 0.3347 0.3681 0.2892 0.0264  -0.0271 0.0144  16   ALA A CB  
120  N N   . SER A 17  ? 0.2887 0.3413 0.2588 0.0198  -0.0237 0.0130  17   SER A N   
121  C CA  . SER A 17  ? 0.2787 0.3377 0.2563 0.0168  -0.0219 0.0122  17   SER A CA  
122  C C   . SER A 17  ? 0.2805 0.3409 0.2602 0.0192  -0.0224 0.0117  17   SER A C   
123  O O   . SER A 17  ? 0.2807 0.3402 0.2569 0.0238  -0.0242 0.0116  17   SER A O   
124  C CB  . SER A 17  ? 0.2718 0.3399 0.2535 0.0161  -0.0221 0.0118  17   SER A CB  
125  O OG  . SER A 17  ? 0.2874 0.3534 0.2673 0.0133  -0.0213 0.0120  17   SER A OG  
126  N N   . VAL A 18  ? 0.2671 0.3303 0.2521 0.0165  -0.0208 0.0113  18   VAL A N   
127  C CA  . VAL A 18  ? 0.2662 0.3320 0.2534 0.0187  -0.0211 0.0107  18   VAL A CA  
128  C C   . VAL A 18  ? 0.2512 0.3249 0.2454 0.0160  -0.0195 0.0104  18   VAL A C   
129  O O   . VAL A 18  ? 0.2433 0.3173 0.2399 0.0121  -0.0180 0.0105  18   VAL A O   
130  C CB  . VAL A 18  ? 0.2785 0.3363 0.2633 0.0184  -0.0212 0.0106  18   VAL A CB  
131  C CG1 . VAL A 18  ? 0.3153 0.3642 0.2925 0.0211  -0.0230 0.0109  18   VAL A CG1 
132  C CG2 . VAL A 18  ? 0.2736 0.3289 0.2612 0.0133  -0.0194 0.0109  18   VAL A CG2 
133  N N   . LYS A 19  ? 0.2536 0.3334 0.2505 0.0184  -0.0197 0.0101  19   LYS A N   
134  C CA  . LYS A 19  ? 0.2451 0.3315 0.2480 0.0160  -0.0181 0.0100  19   LYS A CA  
135  C C   . LYS A 19  ? 0.2538 0.3393 0.2571 0.0176  -0.0180 0.0097  19   LYS A C   
136  O O   . LYS A 19  ? 0.2507 0.3373 0.2517 0.0221  -0.0190 0.0095  19   LYS A O   
137  C CB  . LYS A 19  ? 0.2687 0.3648 0.2748 0.0171  -0.0184 0.0103  19   LYS A CB  
138  C CG  . LYS A 19  ? 0.2686 0.3709 0.2805 0.0137  -0.0169 0.0105  19   LYS A CG  
139  C CD  . LYS A 19  ? 0.3131 0.4248 0.3280 0.0143  -0.0174 0.0109  19   LYS A CD  
140  C CE  . LYS A 19  ? 0.3166 0.4333 0.3365 0.0100  -0.0163 0.0112  19   LYS A CE  
141  N NZ  . LYS A 19  ? 0.3249 0.4493 0.3470 0.0094  -0.0174 0.0115  19   LYS A NZ  
142  N N   . ILE A 20  ? 0.2292 0.3120 0.2345 0.0145  -0.0169 0.0097  20   ILE A N   
143  C CA  . ILE A 20  ? 0.2352 0.3163 0.2408 0.0154  -0.0169 0.0093  20   ILE A CA  
144  C C   . ILE A 20  ? 0.2098 0.2983 0.2203 0.0144  -0.0155 0.0096  20   ILE A C   
145  O O   . ILE A 20  ? 0.2127 0.3042 0.2266 0.0112  -0.0143 0.0100  20   ILE A O   
146  C CB  . ILE A 20  ? 0.2466 0.3207 0.2517 0.0124  -0.0167 0.0092  20   ILE A CB  
147  C CG1 . ILE A 20  ? 0.2608 0.3273 0.2609 0.0126  -0.0178 0.0092  20   ILE A CG1 
148  C CG2 . ILE A 20  ? 0.2854 0.3582 0.2909 0.0131  -0.0171 0.0087  20   ILE A CG2 
149  C CD1 . ILE A 20  ? 0.2661 0.3271 0.2668 0.0089  -0.0173 0.0095  20   ILE A CD1 
150  N N   . SER A 21  ? 0.2069 0.2982 0.2171 0.0174  -0.0156 0.0095  21   SER A N   
151  C CA  . SER A 21  ? 0.2005 0.2988 0.2149 0.0167  -0.0142 0.0101  21   SER A CA  
152  C C   . SER A 21  ? 0.1978 0.2929 0.2123 0.0160  -0.0139 0.0099  21   SER A C   
153  O O   . SER A 21  ? 0.1899 0.2789 0.2010 0.0175  -0.0152 0.0091  21   SER A O   
154  C CB  . SER A 21  ? 0.2169 0.3224 0.2311 0.0206  -0.0142 0.0104  21   SER A CB  
155  O OG  . SER A 21  ? 0.2233 0.3255 0.2331 0.0251  -0.0152 0.0097  21   SER A OG  
156  N N   . CYS A 22  ? 0.1905 0.2900 0.2088 0.0141  -0.0125 0.0106  22   CYS A N   
157  C CA  . CYS A 22  ? 0.2069 0.3046 0.2259 0.0133  -0.0121 0.0106  22   CYS A CA  
158  C C   . CYS A 22  ? 0.1885 0.2931 0.2095 0.0140  -0.0107 0.0117  22   CYS A C   
159  O O   . CYS A 22  ? 0.1783 0.2862 0.2027 0.0109  -0.0094 0.0126  22   CYS A O   
160  C CB  . CYS A 22  ? 0.2015 0.2961 0.2230 0.0093  -0.0115 0.0107  22   CYS A CB  
161  S SG  . CYS A 22  ? 0.2430 0.3364 0.2661 0.0084  -0.0111 0.0110  22   CYS A SG  
162  N N   . LYS A 23  ? 0.2017 0.3082 0.2203 0.0178  -0.0109 0.0116  23   LYS A N   
163  C CA  . LYS A 23  ? 0.2141 0.3276 0.2343 0.0186  -0.0093 0.0129  23   LYS A CA  
164  C C   . LYS A 23  ? 0.2078 0.3194 0.2282 0.0175  -0.0086 0.0134  23   LYS A C   
165  O O   . LYS A 23  ? 0.1943 0.3014 0.2112 0.0198  -0.0098 0.0125  23   LYS A O   
166  C CB  . LYS A 23  ? 0.2621 0.3790 0.2792 0.0237  -0.0094 0.0127  23   LYS A CB  
167  C CG  . LYS A 23  ? 0.3305 0.4552 0.3491 0.0248  -0.0074 0.0143  23   LYS A CG  
168  C CD  . LYS A 23  ? 0.3408 0.4724 0.3649 0.0206  -0.0057 0.0161  23   LYS A CD  
169  C CE  . LYS A 23  ? 0.3526 0.4898 0.3779 0.0203  -0.0036 0.0179  23   LYS A CE  
170  N NZ  . LYS A 23  ? 0.4230 0.5638 0.4450 0.0259  -0.0031 0.0179  23   LYS A NZ  
171  N N   . ALA A 24  ? 0.1904 0.3052 0.2142 0.0143  -0.0070 0.0149  24   ALA A N   
172  C CA  . ALA A 24  ? 0.1950 0.3077 0.2190 0.0131  -0.0065 0.0156  24   ALA A CA  
173  C C   . ALA A 24  ? 0.2076 0.3255 0.2307 0.0151  -0.0051 0.0170  24   ALA A C   
174  O O   . ALA A 24  ? 0.2021 0.3271 0.2271 0.0150  -0.0036 0.0182  24   ALA A O   
175  C CB  . ALA A 24  ? 0.1970 0.3089 0.2244 0.0086  -0.0056 0.0163  24   ALA A CB  
176  N N   . SER A 25  ? 0.2012 0.3163 0.2214 0.0170  -0.0054 0.0169  25   SER A N   
177  C CA  . SER A 25  ? 0.2087 0.3283 0.2276 0.0185  -0.0037 0.0186  25   SER A CA  
178  C C   . SER A 25  ? 0.2002 0.3155 0.2178 0.0178  -0.0038 0.0192  25   SER A C   
179  O O   . SER A 25  ? 0.1798 0.2891 0.1971 0.0171  -0.0056 0.0179  25   SER A O   
180  C CB  . SER A 25  ? 0.2472 0.3691 0.2622 0.0236  -0.0039 0.0179  25   SER A CB  
181  O OG  . SER A 25  ? 0.2717 0.3866 0.2824 0.0263  -0.0063 0.0158  25   SER A OG  
182  N N   . GLY A 26  ? 0.1916 0.3104 0.2085 0.0179  -0.0019 0.0213  26   GLY A N   
183  C CA  . GLY A 26  ? 0.2037 0.3191 0.2178 0.0186  -0.0020 0.0220  26   GLY A CA  
184  C C   . GLY A 26  ? 0.2083 0.3208 0.2252 0.0146  -0.0016 0.0231  26   GLY A C   
185  O O   . GLY A 26  ? 0.2285 0.3372 0.2433 0.0151  -0.0021 0.0237  26   GLY A O   
186  N N   . TYR A 27  ? 0.1906 0.3046 0.2115 0.0109  -0.0008 0.0236  27   TYR A N   
187  C CA  . TYR A 27  ? 0.1912 0.3021 0.2143 0.0071  -0.0002 0.0247  27   TYR A CA  
188  C C   . TYR A 27  ? 0.1899 0.3047 0.2165 0.0034  0.0010  0.0256  27   TYR A C   
189  O O   . TYR A 27  ? 0.1948 0.3145 0.2226 0.0040  0.0011  0.0251  27   TYR A O   
190  C CB  . TYR A 27  ? 0.1859 0.2906 0.2096 0.0068  -0.0022 0.0229  27   TYR A CB  
191  C CG  . TYR A 27  ? 0.1815 0.2859 0.2076 0.0057  -0.0031 0.0210  27   TYR A CG  
192  C CD1 . TYR A 27  ? 0.1849 0.2892 0.2099 0.0082  -0.0045 0.0192  27   TYR A CD1 
193  C CD2 . TYR A 27  ? 0.1849 0.2885 0.2137 0.0023  -0.0024 0.0211  27   TYR A CD2 
194  C CE1 . TYR A 27  ? 0.1858 0.2894 0.2125 0.0071  -0.0053 0.0178  27   TYR A CE1 
195  C CE2 . TYR A 27  ? 0.1753 0.2784 0.2058 0.0014  -0.0032 0.0195  27   TYR A CE2 
196  C CZ  . TYR A 27  ? 0.1759 0.2792 0.2053 0.0038  -0.0045 0.0180  27   TYR A CZ  
197  O OH  . TYR A 27  ? 0.1780 0.2805 0.2086 0.0028  -0.0051 0.0167  27   TYR A OH  
198  N N   . ILE A 28  ? 0.1948 0.3067 0.2226 -0.0002 0.0017  0.0267  28   ILE A N   
199  C CA  . ILE A 28  ? 0.2078 0.3225 0.2386 -0.0043 0.0026  0.0275  28   ILE A CA  
200  C C   . ILE A 28  ? 0.1991 0.3116 0.2316 -0.0050 0.0011  0.0252  28   ILE A C   
201  O O   . ILE A 28  ? 0.1753 0.2817 0.2076 -0.0056 0.0004  0.0242  28   ILE A O   
202  C CB  . ILE A 28  ? 0.2273 0.3385 0.2578 -0.0079 0.0036  0.0295  28   ILE A CB  
203  C CG1 . ILE A 28  ? 0.2617 0.3750 0.2899 -0.0071 0.0052  0.0321  28   ILE A CG1 
204  C CG2 . ILE A 28  ? 0.2277 0.3412 0.2611 -0.0126 0.0040  0.0300  28   ILE A CG2 
205  C CD1 . ILE A 28  ? 0.2947 0.4035 0.3218 -0.0105 0.0062  0.0343  28   ILE A CD1 
206  N N   . PHE A 29  ? 0.1858 0.3036 0.2201 -0.0051 0.0009  0.0246  29   PHE A N   
207  C CA  . PHE A 29  ? 0.1879 0.3041 0.2232 -0.0052 -0.0003 0.0225  29   PHE A CA  
208  C C   . PHE A 29  ? 0.1950 0.3061 0.2311 -0.0089 -0.0005 0.0221  29   PHE A C   
209  O O   . PHE A 29  ? 0.1893 0.2959 0.2251 -0.0085 -0.0014 0.0204  29   PHE A O   
210  C CB  . PHE A 29  ? 0.1886 0.3118 0.2255 -0.0048 -0.0004 0.0224  29   PHE A CB  
211  C CG  . PHE A 29  ? 0.1911 0.3126 0.2282 -0.0044 -0.0019 0.0204  29   PHE A CG  
212  C CD1 . PHE A 29  ? 0.1800 0.2979 0.2151 -0.0013 -0.0030 0.0188  29   PHE A CD1 
213  C CD2 . PHE A 29  ? 0.1943 0.3186 0.2333 -0.0071 -0.0022 0.0203  29   PHE A CD2 
214  C CE1 . PHE A 29  ? 0.1982 0.3142 0.2329 -0.0010 -0.0042 0.0172  29   PHE A CE1 
215  C CE2 . PHE A 29  ? 0.1922 0.3149 0.2307 -0.0064 -0.0035 0.0186  29   PHE A CE2 
216  C CZ  . PHE A 29  ? 0.1907 0.3091 0.2270 -0.0034 -0.0044 0.0172  29   PHE A CZ  
217  N N   . ALA A 30  ? 0.2041 0.3159 0.2410 -0.0124 0.0004  0.0237  30   ALA A N   
218  C CA  . ALA A 30  ? 0.2105 0.3173 0.2476 -0.0161 0.0002  0.0234  30   ALA A CA  
219  C C   . ALA A 30  ? 0.1985 0.2974 0.2336 -0.0152 0.0002  0.0228  30   ALA A C   
220  O O   . ALA A 30  ? 0.2156 0.3097 0.2502 -0.0173 0.0000  0.0221  30   ALA A O   
221  C CB  . ALA A 30  ? 0.2262 0.3352 0.2641 -0.0201 0.0011  0.0255  30   ALA A CB  
222  N N   . ASP A 31  ? 0.1882 0.2860 0.2221 -0.0123 0.0003  0.0232  31   ASP A N   
223  C CA  . ASP A 31  ? 0.1892 0.2804 0.2215 -0.0115 0.0003  0.0233  31   ASP A CA  
224  C C   . ASP A 31  ? 0.1678 0.2563 0.2005 -0.0091 -0.0006 0.0212  31   ASP A C   
225  O O   . ASP A 31  ? 0.1721 0.2562 0.2041 -0.0081 -0.0007 0.0210  31   ASP A O   
226  C CB  . ASP A 31  ? 0.2197 0.3113 0.2503 -0.0102 0.0009  0.0253  31   ASP A CB  
227  C CG  . ASP A 31  ? 0.2270 0.3192 0.2570 -0.0137 0.0022  0.0277  31   ASP A CG  
228  O OD1 . ASP A 31  ? 0.2678 0.3602 0.2989 -0.0173 0.0023  0.0276  31   ASP A OD1 
229  O OD2 . ASP A 31  ? 0.2591 0.3513 0.2873 -0.0129 0.0029  0.0295  31   ASP A OD2 
230  N N   . HIS A 32  ? 0.1549 0.2463 0.1888 -0.0082 -0.0013 0.0197  32   HIS A N   
231  C CA  . HIS A 32  ? 0.1516 0.2406 0.1860 -0.0064 -0.0021 0.0180  32   HIS A CA  
232  C C   . HIS A 32  ? 0.1384 0.2284 0.1735 -0.0072 -0.0025 0.0167  32   HIS A C   
233  O O   . HIS A 32  ? 0.1466 0.2406 0.1818 -0.0073 -0.0027 0.0167  32   HIS A O   
234  C CB  . HIS A 32  ? 0.1435 0.2338 0.1774 -0.0034 -0.0031 0.0178  32   HIS A CB  
235  C CG  . HIS A 32  ? 0.1433 0.2324 0.1761 -0.0021 -0.0031 0.0191  32   HIS A CG  
236  N ND1 . HIS A 32  ? 0.1433 0.2286 0.1763 -0.0015 -0.0033 0.0190  32   HIS A ND1 
237  C CD2 . HIS A 32  ? 0.1483 0.2394 0.1794 -0.0013 -0.0027 0.0206  32   HIS A CD2 
238  C CE1 . HIS A 32  ? 0.1489 0.2333 0.1801 -0.0004 -0.0032 0.0205  32   HIS A CE1 
239  N NE2 . HIS A 32  ? 0.1498 0.2378 0.1796 -0.0002 -0.0028 0.0215  32   HIS A NE2 
240  N N   . ALA A 33  ? 0.1443 0.2312 0.1798 -0.0076 -0.0024 0.0155  33   ALA A N   
241  C CA  . ALA A 33  ? 0.1362 0.2234 0.1718 -0.0079 -0.0027 0.0143  33   ALA A CA  
242  C C   . ALA A 33  ? 0.1295 0.2183 0.1652 -0.0058 -0.0038 0.0138  33   ALA A C   
243  O O   . ALA A 33  ? 0.1311 0.2194 0.1670 -0.0041 -0.0044 0.0138  33   ALA A O   
244  C CB  . ALA A 33  ? 0.1386 0.2220 0.1743 -0.0087 -0.0020 0.0134  33   ALA A CB  
245  N N   . ILE A 34  ? 0.1377 0.2278 0.1727 -0.0058 -0.0043 0.0132  34   ILE A N   
246  C CA  . ILE A 34  ? 0.1380 0.2282 0.1722 -0.0040 -0.0054 0.0125  34   ILE A CA  
247  C C   . ILE A 34  ? 0.1325 0.2199 0.1665 -0.0050 -0.0053 0.0117  34   ILE A C   
248  O O   . ILE A 34  ? 0.1364 0.2236 0.1697 -0.0064 -0.0047 0.0114  34   ILE A O   
249  C CB  . ILE A 34  ? 0.1440 0.2376 0.1769 -0.0029 -0.0061 0.0127  34   ILE A CB  
250  C CG1 . ILE A 34  ? 0.1564 0.2533 0.1894 -0.0018 -0.0059 0.0137  34   ILE A CG1 
251  C CG2 . ILE A 34  ? 0.1487 0.2406 0.1797 -0.0010 -0.0074 0.0119  34   ILE A CG2 
252  C CD1 . ILE A 34  ? 0.1673 0.2632 0.1992 0.0005  -0.0067 0.0136  34   ILE A CD1 
253  N N   . HIS A 35  ? 0.1288 0.2143 0.1634 -0.0044 -0.0057 0.0113  35   HIS A N   
254  C CA  . HIS A 35  ? 0.1247 0.2079 0.1594 -0.0054 -0.0053 0.0109  35   HIS A CA  
255  C C   . HIS A 35  ? 0.1295 0.2117 0.1621 -0.0046 -0.0067 0.0106  35   HIS A C   
256  O O   . HIS A 35  ? 0.1423 0.2248 0.1740 -0.0029 -0.0081 0.0105  35   HIS A O   
257  C CB  . HIS A 35  ? 0.1165 0.1990 0.1538 -0.0056 -0.0049 0.0109  35   HIS A CB  
258  C CG  . HIS A 35  ? 0.1218 0.2044 0.1606 -0.0059 -0.0035 0.0111  35   HIS A CG  
259  N ND1 . HIS A 35  ? 0.1178 0.1991 0.1573 -0.0067 -0.0019 0.0108  35   HIS A ND1 
260  C CD2 . HIS A 35  ? 0.1215 0.2046 0.1605 -0.0053 -0.0035 0.0116  35   HIS A CD2 
261  C CE1 . HIS A 35  ? 0.1203 0.2010 0.1602 -0.0065 -0.0012 0.0110  35   HIS A CE1 
262  N NE2 . HIS A 35  ? 0.1164 0.1980 0.1559 -0.0059 -0.0021 0.0116  35   HIS A NE2 
263  N N   . TRP A 36  ? 0.1413 0.2215 0.1729 -0.0056 -0.0062 0.0104  36   TRP A N   
264  C CA  . TRP A 36  ? 0.1455 0.2233 0.1746 -0.0051 -0.0075 0.0103  36   TRP A CA  
265  C C   . TRP A 36  ? 0.1460 0.2214 0.1761 -0.0067 -0.0070 0.0105  36   TRP A C   
266  O O   . TRP A 36  ? 0.1304 0.2063 0.1621 -0.0080 -0.0052 0.0106  36   TRP A O   
267  C CB  . TRP A 36  ? 0.1489 0.2266 0.1750 -0.0047 -0.0076 0.0102  36   TRP A CB  
268  C CG  . TRP A 36  ? 0.1473 0.2282 0.1727 -0.0030 -0.0084 0.0102  36   TRP A CG  
269  C CD1 . TRP A 36  ? 0.1593 0.2437 0.1862 -0.0036 -0.0076 0.0104  36   TRP A CD1 
270  C CD2 . TRP A 36  ? 0.1597 0.2410 0.1828 -0.0004 -0.0100 0.0101  36   TRP A CD2 
271  N NE1 . TRP A 36  ? 0.1612 0.2490 0.1874 -0.0018 -0.0085 0.0106  36   TRP A NE1 
272  C CE2 . TRP A 36  ? 0.1622 0.2484 0.1861 0.0004  -0.0098 0.0103  36   TRP A CE2 
273  C CE3 . TRP A 36  ? 0.1762 0.2541 0.1964 0.0012  -0.0115 0.0098  36   TRP A CE3 
274  C CZ2 . TRP A 36  ? 0.1709 0.2594 0.1931 0.0033  -0.0109 0.0103  36   TRP A CZ2 
275  C CZ3 . TRP A 36  ? 0.1959 0.2748 0.2137 0.0043  -0.0128 0.0096  36   TRP A CZ3 
276  C CH2 . TRP A 36  ? 0.1801 0.2648 0.1990 0.0055  -0.0123 0.0099  36   TRP A CH2 
277  N N   . VAL A 37  ? 0.1651 0.2383 0.1944 -0.0065 -0.0086 0.0104  37   VAL A N   
278  C CA  . VAL A 37  ? 0.1807 0.2521 0.2116 -0.0085 -0.0085 0.0108  37   VAL A CA  
279  C C   . VAL A 37  ? 0.1994 0.2661 0.2263 -0.0087 -0.0100 0.0109  37   VAL A C   
280  O O   . VAL A 37  ? 0.2361 0.3008 0.2596 -0.0067 -0.0120 0.0104  37   VAL A O   
281  C CB  . VAL A 37  ? 0.1802 0.2534 0.2146 -0.0084 -0.0095 0.0106  37   VAL A CB  
282  C CG1 . VAL A 37  ? 0.2002 0.2727 0.2370 -0.0107 -0.0099 0.0110  37   VAL A CG1 
283  C CG2 . VAL A 37  ? 0.1714 0.2484 0.2091 -0.0080 -0.0080 0.0107  37   VAL A CG2 
284  N N   . LYS A 38  ? 0.2053 0.2700 0.2320 -0.0110 -0.0090 0.0117  38   LYS A N   
285  C CA  . LYS A 38  ? 0.2240 0.2832 0.2465 -0.0117 -0.0103 0.0121  38   LYS A CA  
286  C C   . LYS A 38  ? 0.2510 0.3089 0.2760 -0.0143 -0.0112 0.0126  38   LYS A C   
287  O O   . LYS A 38  ? 0.2360 0.2974 0.2657 -0.0164 -0.0094 0.0132  38   LYS A O   
288  C CB  . LYS A 38  ? 0.2296 0.2874 0.2499 -0.0129 -0.0083 0.0130  38   LYS A CB  
289  C CG  . LYS A 38  ? 0.2434 0.2949 0.2587 -0.0137 -0.0092 0.0138  38   LYS A CG  
290  C CD  . LYS A 38  ? 0.2452 0.2959 0.2584 -0.0149 -0.0070 0.0148  38   LYS A CD  
291  C CE  . LYS A 38  ? 0.2619 0.3058 0.2698 -0.0160 -0.0077 0.0160  38   LYS A CE  
292  N NZ  . LYS A 38  ? 0.2620 0.3052 0.2671 -0.0167 -0.0054 0.0170  38   LYS A NZ  
293  N N   . ARG A 39  ? 0.2946 0.3476 0.3164 -0.0140 -0.0140 0.0122  39   ARG A N   
294  C CA  . ARG A 39  ? 0.3548 0.4052 0.3780 -0.0171 -0.0155 0.0126  39   ARG A CA  
295  C C   . ARG A 39  ? 0.3545 0.3970 0.3718 -0.0184 -0.0166 0.0134  39   ARG A C   
296  O O   . ARG A 39  ? 0.3030 0.3404 0.3146 -0.0157 -0.0188 0.0125  39   ARG A O   
297  C CB  . ARG A 39  ? 0.3947 0.4451 0.4184 -0.0157 -0.0183 0.0114  39   ARG A CB  
298  C CG  . ARG A 39  ? 0.4858 0.5388 0.5150 -0.0188 -0.0191 0.0116  39   ARG A CG  
299  C CD  . ARG A 39  ? 0.5568 0.6061 0.5840 -0.0186 -0.0229 0.0105  39   ARG A CD  
300  N NE  . ARG A 39  ? 0.5511 0.6021 0.5832 -0.0225 -0.0240 0.0111  39   ARG A NE  
301  C CZ  . ARG A 39  ? 0.5894 0.6391 0.6229 -0.0266 -0.0232 0.0125  39   ARG A CZ  
302  N NH1 . ARG A 39  ? 0.6708 0.7232 0.7095 -0.0304 -0.0243 0.0131  39   ARG A NH1 
303  N NH2 . ARG A 39  ? 0.6526 0.6985 0.6822 -0.0270 -0.0214 0.0135  39   ARG A NH2 
304  N N   . LYS A 40  ? 0.3927 0.4342 0.4113 -0.0222 -0.0154 0.0149  40   LYS A N   
305  C CA  . LYS A 40  ? 0.4571 0.4902 0.4704 -0.0244 -0.0167 0.0159  40   LYS A CA  
306  C C   . LYS A 40  ? 0.4872 0.5179 0.5023 -0.0275 -0.0194 0.0158  40   LYS A C   
307  O O   . LYS A 40  ? 0.4866 0.5239 0.5089 -0.0296 -0.0188 0.0159  40   LYS A O   
308  C CB  . LYS A 40  ? 0.4723 0.5051 0.4855 -0.0274 -0.0138 0.0180  40   LYS A CB  
309  C CG  . LYS A 40  ? 0.4727 0.5016 0.4794 -0.0249 -0.0129 0.0183  40   LYS A CG  
310  C CD  . LYS A 40  ? 0.5083 0.5345 0.5128 -0.0279 -0.0106 0.0205  40   LYS A CD  
311  C CE  . LYS A 40  ? 0.5215 0.5452 0.5200 -0.0251 -0.0095 0.0208  40   LYS A CE  
312  N NZ  . LYS A 40  ? 0.5231 0.5372 0.5132 -0.0232 -0.0124 0.0208  40   LYS A NZ  
313  N N   . PRO A 41  ? 0.5797 0.6013 0.5884 -0.0274 -0.0227 0.0153  41   PRO A N   
314  C CA  . PRO A 41  ? 0.6103 0.6279 0.6194 -0.0306 -0.0259 0.0151  41   PRO A CA  
315  C C   . PRO A 41  ? 0.5997 0.6225 0.6163 -0.0364 -0.0246 0.0167  41   PRO A C   
316  O O   . PRO A 41  ? 0.5989 0.6215 0.6159 -0.0392 -0.0221 0.0188  41   PRO A O   
317  C CB  . PRO A 41  ? 0.6277 0.6331 0.6277 -0.0310 -0.0281 0.0154  41   PRO A CB  
318  C CG  . PRO A 41  ? 0.6343 0.6379 0.6285 -0.0252 -0.0275 0.0146  41   PRO A CG  
319  C CD  . PRO A 41  ? 0.6190 0.6330 0.6191 -0.0238 -0.0238 0.0149  41   PRO A CD  
320  N N   . GLU A 42  ? 0.6613 0.6890 0.6837 -0.0377 -0.0263 0.0159  42   GLU A N   
321  C CA  . GLU A 42  ? 0.6656 0.6989 0.6959 -0.0432 -0.0260 0.0173  42   GLU A CA  
322  C C   . GLU A 42  ? 0.6271 0.6711 0.6647 -0.0432 -0.0213 0.0186  42   GLU A C   
323  O O   . GLU A 42  ? 0.6348 0.6849 0.6793 -0.0473 -0.0201 0.0200  42   GLU A O   
324  C CB  . GLU A 42  ? 0.7487 0.7752 0.7765 -0.0487 -0.0267 0.0193  42   GLU A CB  
325  C CG  . GLU A 42  ? 0.8102 0.8229 0.8276 -0.0483 -0.0301 0.0186  42   GLU A CG  
326  C CD  . GLU A 42  ? 0.8456 0.8513 0.8586 -0.0519 -0.0288 0.0211  42   GLU A CD  
327  O OE1 . GLU A 42  ? 0.8522 0.8482 0.8559 -0.0491 -0.0295 0.0208  42   GLU A OE1 
328  O OE2 . GLU A 42  ? 0.8522 0.8625 0.8710 -0.0574 -0.0268 0.0234  42   GLU A OE2 
329  N N   . GLN A 43  ? 0.5886 0.6344 0.6242 -0.0389 -0.0187 0.0181  43   GLN A N   
330  C CA  . GLN A 43  ? 0.5610 0.6146 0.6014 -0.0387 -0.0141 0.0193  43   GLN A CA  
331  C C   . GLN A 43  ? 0.4898 0.5492 0.5326 -0.0343 -0.0133 0.0177  43   GLN A C   
332  O O   . GLN A 43  ? 0.5035 0.5607 0.5438 -0.0313 -0.0160 0.0160  43   GLN A O   
333  C CB  . GLN A 43  ? 0.5952 0.6442 0.6298 -0.0385 -0.0116 0.0205  43   GLN A CB  
334  C CG  . GLN A 43  ? 0.6617 0.7033 0.6925 -0.0427 -0.0127 0.0221  43   GLN A CG  
335  C CD  . GLN A 43  ? 0.7324 0.7709 0.7586 -0.0430 -0.0097 0.0239  43   GLN A CD  
336  O OE1 . GLN A 43  ? 0.7787 0.8213 0.8051 -0.0404 -0.0067 0.0238  43   GLN A OE1 
337  N NE2 . GLN A 43  ? 0.7929 0.8236 0.8144 -0.0464 -0.0105 0.0255  43   GLN A NE2 
338  N N   . GLY A 44  ? 0.4132 0.4796 0.4606 -0.0339 -0.0096 0.0184  44   GLY A N   
339  C CA  . GLY A 44  ? 0.3955 0.4684 0.4470 -0.0308 -0.0086 0.0174  44   GLY A CA  
340  C C   . GLY A 44  ? 0.3482 0.4181 0.3944 -0.0267 -0.0087 0.0160  44   GLY A C   
341  O O   . GLY A 44  ? 0.4156 0.4795 0.4557 -0.0262 -0.0093 0.0160  44   GLY A O   
342  N N   . LEU A 45  ? 0.2746 0.3486 0.3232 -0.0239 -0.0086 0.0150  45   LEU A N   
343  C CA  . LEU A 45  ? 0.2570 0.3298 0.3019 -0.0203 -0.0084 0.0139  45   LEU A CA  
344  C C   . LEU A 45  ? 0.2169 0.2920 0.2621 -0.0199 -0.0048 0.0144  45   LEU A C   
345  O O   . LEU A 45  ? 0.1941 0.2734 0.2437 -0.0212 -0.0026 0.0152  45   LEU A O   
346  C CB  . LEU A 45  ? 0.2585 0.3345 0.3061 -0.0181 -0.0098 0.0129  45   LEU A CB  
347  C CG  . LEU A 45  ? 0.3170 0.3900 0.3629 -0.0179 -0.0136 0.0121  45   LEU A CG  
348  C CD1 . LEU A 45  ? 0.3297 0.4070 0.3799 -0.0169 -0.0148 0.0116  45   LEU A CD1 
349  C CD2 . LEU A 45  ? 0.3248 0.3934 0.3645 -0.0152 -0.0147 0.0113  45   LEU A CD2 
350  N N   . GLU A 46  ? 0.1881 0.2607 0.2287 -0.0180 -0.0044 0.0139  46   GLU A N   
351  C CA  . GLU A 46  ? 0.2005 0.2745 0.2404 -0.0173 -0.0014 0.0140  46   GLU A CA  
352  C C   . GLU A 46  ? 0.1816 0.2558 0.2196 -0.0147 -0.0020 0.0129  46   GLU A C   
353  O O   . GLU A 46  ? 0.1968 0.2685 0.2316 -0.0135 -0.0041 0.0124  46   GLU A O   
354  C CB  . GLU A 46  ? 0.2294 0.2995 0.2644 -0.0182 -0.0005 0.0147  46   GLU A CB  
355  C CG  . GLU A 46  ? 0.2721 0.3419 0.3081 -0.0210 0.0008  0.0161  46   GLU A CG  
356  C CD  . GLU A 46  ? 0.3104 0.3759 0.3405 -0.0214 0.0020  0.0168  46   GLU A CD  
357  O OE1 . GLU A 46  ? 0.3309 0.3914 0.3563 -0.0211 0.0000  0.0169  46   GLU A OE1 
358  O OE2 . GLU A 46  ? 0.3546 0.4218 0.3844 -0.0213 0.0048  0.0171  46   GLU A OE2 
359  N N   . TRP A 47  ? 0.1714 0.2482 0.2112 -0.0138 -0.0001 0.0126  47   TRP A N   
360  C CA  . TRP A 47  ? 0.1666 0.2437 0.2050 -0.0120 -0.0005 0.0117  47   TRP A CA  
361  C C   . TRP A 47  ? 0.1623 0.2372 0.1961 -0.0119 0.0002  0.0115  47   TRP A C   
362  O O   . TRP A 47  ? 0.1828 0.2571 0.2157 -0.0127 0.0022  0.0118  47   TRP A O   
363  C CB  . TRP A 47  ? 0.1561 0.2360 0.1979 -0.0112 0.0008  0.0115  47   TRP A CB  
364  C CG  . TRP A 47  ? 0.1541 0.2337 0.1944 -0.0099 0.0007  0.0109  47   TRP A CG  
365  C CD1 . TRP A 47  ? 0.1522 0.2322 0.1923 -0.0089 -0.0009 0.0107  47   TRP A CD1 
366  C CD2 . TRP A 47  ? 0.1496 0.2280 0.1878 -0.0098 0.0023  0.0104  47   TRP A CD2 
367  N NE1 . TRP A 47  ? 0.1499 0.2295 0.1887 -0.0085 -0.0003 0.0104  47   TRP A NE1 
368  C CE2 . TRP A 47  ? 0.1492 0.2276 0.1866 -0.0091 0.0014  0.0101  47   TRP A CE2 
369  C CE3 . TRP A 47  ? 0.1550 0.2323 0.1915 -0.0103 0.0044  0.0103  47   TRP A CE3 
370  C CZ2 . TRP A 47  ? 0.1498 0.2267 0.1850 -0.0093 0.0023  0.0096  47   TRP A CZ2 
371  C CZ3 . TRP A 47  ? 0.1485 0.2240 0.1823 -0.0100 0.0052  0.0095  47   TRP A CZ3 
372  C CH2 . TRP A 47  ? 0.1513 0.2265 0.1846 -0.0097 0.0040  0.0092  47   TRP A CH2 
373  N N   . ILE A 48  ? 0.1555 0.2296 0.1867 -0.0108 -0.0013 0.0111  48   ILE A N   
374  C CA  . ILE A 48  ? 0.1531 0.2257 0.1802 -0.0106 -0.0012 0.0109  48   ILE A CA  
375  C C   . ILE A 48  ? 0.1492 0.2232 0.1764 -0.0104 -0.0004 0.0102  48   ILE A C   
376  O O   . ILE A 48  ? 0.1535 0.2262 0.1781 -0.0110 0.0005  0.0099  48   ILE A O   
377  C CB  . ILE A 48  ? 0.1551 0.2268 0.1794 -0.0094 -0.0036 0.0108  48   ILE A CB  
378  C CG1 . ILE A 48  ? 0.1555 0.2240 0.1784 -0.0098 -0.0044 0.0114  48   ILE A CG1 
379  C CG2 . ILE A 48  ? 0.1504 0.2218 0.1712 -0.0089 -0.0038 0.0106  48   ILE A CG2 
380  C CD1 . ILE A 48  ? 0.1575 0.2244 0.1777 -0.0080 -0.0069 0.0113  48   ILE A CD1 
381  N N   . GLY A 49  ? 0.1512 0.2272 0.1805 -0.0098 -0.0011 0.0100  49   GLY A N   
382  C CA  . GLY A 49  ? 0.1371 0.2138 0.1663 -0.0100 -0.0007 0.0096  49   GLY A CA  
383  C C   . GLY A 49  ? 0.1344 0.2133 0.1655 -0.0093 -0.0018 0.0098  49   GLY A C   
384  O O   . GLY A 49  ? 0.1269 0.2067 0.1590 -0.0083 -0.0029 0.0102  49   GLY A O   
385  N N   . TYR A 50  ? 0.1272 0.2065 0.1582 -0.0098 -0.0015 0.0097  50   TYR A N   
386  C CA  . TYR A 50  ? 0.1306 0.2121 0.1629 -0.0095 -0.0023 0.0102  50   TYR A CA  
387  C C   . TYR A 50  ? 0.1410 0.2238 0.1719 -0.0107 -0.0028 0.0102  50   TYR A C   
388  O O   . TYR A 50  ? 0.1579 0.2388 0.1870 -0.0120 -0.0024 0.0096  50   TYR A O   
389  C CB  . TYR A 50  ? 0.1314 0.2121 0.1656 -0.0091 -0.0016 0.0106  50   TYR A CB  
390  C CG  . TYR A 50  ? 0.1331 0.2112 0.1666 -0.0102 -0.0004 0.0103  50   TYR A CG  
391  C CD1 . TYR A 50  ? 0.1441 0.2220 0.1764 -0.0116 -0.0007 0.0105  50   TYR A CD1 
392  C CD2 . TYR A 50  ? 0.1358 0.2116 0.1696 -0.0097 0.0008  0.0098  50   TYR A CD2 
393  C CE1 . TYR A 50  ? 0.1460 0.2201 0.1767 -0.0127 0.0000  0.0101  50   TYR A CE1 
394  C CE2 . TYR A 50  ? 0.1461 0.2186 0.1785 -0.0101 0.0018  0.0094  50   TYR A CE2 
395  C CZ  . TYR A 50  ? 0.1506 0.2216 0.1810 -0.0117 0.0013  0.0094  50   TYR A CZ  
396  O OH  . TYR A 50  ? 0.1660 0.2324 0.1941 -0.0121 0.0021  0.0089  50   TYR A OH  
397  N N   . ILE A 51  ? 0.1540 0.2402 0.1858 -0.0103 -0.0036 0.0109  51   ILE A N   
398  C CA  . ILE A 51  ? 0.1496 0.2381 0.1814 -0.0120 -0.0039 0.0113  51   ILE A CA  
399  C C   . ILE A 51  ? 0.1489 0.2381 0.1822 -0.0122 -0.0034 0.0123  51   ILE A C   
400  O O   . ILE A 51  ? 0.1626 0.2533 0.1967 -0.0102 -0.0036 0.0129  51   ILE A O   
401  C CB  . ILE A 51  ? 0.1561 0.2489 0.1875 -0.0114 -0.0051 0.0115  51   ILE A CB  
402  C CG1 . ILE A 51  ? 0.1656 0.2619 0.1979 -0.0136 -0.0054 0.0120  51   ILE A CG1 
403  C CG2 . ILE A 51  ? 0.1591 0.2545 0.1911 -0.0087 -0.0056 0.0120  51   ILE A CG2 
404  C CD1 . ILE A 51  ? 0.1731 0.2736 0.2050 -0.0135 -0.0067 0.0118  51   ILE A CD1 
405  N N   . SER A 52  ? 0.1357 0.2231 0.1686 -0.0144 -0.0029 0.0126  52   SER A N   
406  C CA  . SER A 52  ? 0.1434 0.2306 0.1770 -0.0151 -0.0024 0.0138  52   SER A CA  
407  C C   . SER A 52  ? 0.1582 0.2497 0.1925 -0.0174 -0.0029 0.0148  52   SER A C   
408  O O   . SER A 52  ? 0.1818 0.2721 0.2153 -0.0202 -0.0032 0.0145  52   SER A O   
409  C CB  . SER A 52  ? 0.1400 0.2213 0.1723 -0.0161 -0.0016 0.0135  52   SER A CB  
410  O OG  . SER A 52  ? 0.1330 0.2130 0.1654 -0.0164 -0.0012 0.0148  52   SER A OG  
411  N N   . PRO A 53  ? 0.1683 0.2655 0.2040 -0.0161 -0.0030 0.0158  53   PRO A N   
412  C CA  . PRO A 53  ? 0.1823 0.2854 0.2194 -0.0180 -0.0034 0.0168  53   PRO A CA  
413  C C   . PRO A 53  ? 0.1984 0.3007 0.2358 -0.0216 -0.0028 0.0182  53   PRO A C   
414  O O   . PRO A 53  ? 0.2456 0.3516 0.2842 -0.0245 -0.0034 0.0187  53   PRO A O   
415  C CB  . PRO A 53  ? 0.1849 0.2938 0.2230 -0.0150 -0.0033 0.0176  53   PRO A CB  
416  C CG  . PRO A 53  ? 0.1855 0.2908 0.2225 -0.0119 -0.0031 0.0171  53   PRO A CG  
417  C CD  . PRO A 53  ? 0.1731 0.2715 0.2090 -0.0127 -0.0030 0.0161  53   PRO A CD  
418  N N   . GLY A 54  ? 0.1971 0.2949 0.2335 -0.0215 -0.0019 0.0190  54   GLY A N   
419  C CA  . GLY A 54  ? 0.2107 0.3064 0.2466 -0.0247 -0.0013 0.0206  54   GLY A CA  
420  C C   . GLY A 54  ? 0.2179 0.3081 0.2521 -0.0282 -0.0020 0.0197  54   GLY A C   
421  O O   . GLY A 54  ? 0.2455 0.3351 0.2796 -0.0320 -0.0020 0.0210  54   GLY A O   
422  N N   . ASN A 55  ? 0.2086 0.2946 0.2413 -0.0273 -0.0025 0.0175  55   ASN A N   
423  C CA  . ASN A 55  ? 0.2115 0.2912 0.2415 -0.0302 -0.0031 0.0164  55   ASN A CA  
424  C C   . ASN A 55  ? 0.2163 0.2973 0.2458 -0.0301 -0.0042 0.0145  55   ASN A C   
425  O O   . ASN A 55  ? 0.2161 0.2911 0.2425 -0.0316 -0.0047 0.0131  55   ASN A O   
426  C CB  . ASN A 55  ? 0.2153 0.2862 0.2423 -0.0288 -0.0022 0.0159  55   ASN A CB  
427  C CG  . ASN A 55  ? 0.2095 0.2797 0.2368 -0.0246 -0.0016 0.0147  55   ASN A CG  
428  O OD1 . ASN A 55  ? 0.1984 0.2740 0.2277 -0.0228 -0.0018 0.0145  55   ASN A OD1 
429  N ND2 . ASN A 55  ? 0.2130 0.2767 0.2381 -0.0230 -0.0009 0.0138  55   ASN A ND2 
430  N N   . ASP A 56  ? 0.2182 0.3060 0.2500 -0.0280 -0.0045 0.0144  56   ASP A N   
431  C CA  . ASP A 56  ? 0.2257 0.3155 0.2569 -0.0274 -0.0056 0.0130  56   ASP A CA  
432  C C   . ASP A 56  ? 0.2198 0.3027 0.2479 -0.0261 -0.0052 0.0112  56   ASP A C   
433  O O   . ASP A 56  ? 0.2497 0.3313 0.2757 -0.0269 -0.0061 0.0099  56   ASP A O   
434  C CB  . ASP A 56  ? 0.2697 0.3619 0.3010 -0.0311 -0.0073 0.0129  56   ASP A CB  
435  C CG  . ASP A 56  ? 0.3092 0.4091 0.3442 -0.0330 -0.0075 0.0148  56   ASP A CG  
436  O OD1 . ASP A 56  ? 0.3970 0.4965 0.4322 -0.0372 -0.0081 0.0155  56   ASP A OD1 
437  O OD2 . ASP A 56  ? 0.3608 0.4671 0.3982 -0.0302 -0.0070 0.0157  56   ASP A OD2 
438  N N   . ASP A 57  A 0.1947 0.2739 0.2224 -0.0238 -0.0038 0.0112  56   ASP A N   
439  C CA  . ASP A 57  A 0.1912 0.2652 0.2166 -0.0221 -0.0030 0.0098  56   ASP A CA  
440  C C   . ASP A 57  A 0.1925 0.2696 0.2190 -0.0194 -0.0029 0.0096  56   ASP A C   
441  O O   . ASP A 57  A 0.2095 0.2900 0.2384 -0.0177 -0.0028 0.0105  56   ASP A O   
442  C CB  . ASP A 57  A 0.1925 0.2618 0.2176 -0.0210 -0.0017 0.0102  56   ASP A CB  
443  C CG  . ASP A 57  A 0.2038 0.2691 0.2276 -0.0187 -0.0005 0.0089  56   ASP A CG  
444  O OD1 . ASP A 57  A 0.2279 0.2913 0.2492 -0.0191 -0.0005 0.0077  56   ASP A OD1 
445  O OD2 . ASP A 57  A 0.1805 0.2448 0.2055 -0.0166 0.0004  0.0093  56   ASP A OD2 
446  N N   . ILE A 58  ? 0.1863 0.2621 0.2107 -0.0191 -0.0030 0.0084  57   ILE A N   
447  C CA  . ILE A 58  ? 0.1827 0.2603 0.2074 -0.0170 -0.0029 0.0083  57   ILE A CA  
448  C C   . ILE A 58  ? 0.1923 0.2653 0.2149 -0.0161 -0.0014 0.0074  57   ILE A C   
449  O O   . ILE A 58  ? 0.2094 0.2787 0.2290 -0.0172 -0.0011 0.0064  57   ILE A O   
450  C CB  . ILE A 58  ? 0.1792 0.2603 0.2030 -0.0172 -0.0045 0.0082  57   ILE A CB  
451  C CG1 . ILE A 58  ? 0.1941 0.2807 0.2202 -0.0181 -0.0057 0.0091  57   ILE A CG1 
452  C CG2 . ILE A 58  ? 0.1874 0.2691 0.2106 -0.0150 -0.0045 0.0082  57   ILE A CG2 
453  C CD1 . ILE A 58  ? 0.2007 0.2913 0.2261 -0.0183 -0.0074 0.0090  57   ILE A CD1 
454  N N   . LYS A 59  ? 0.1734 0.2468 0.1976 -0.0143 -0.0005 0.0078  58   LYS A N   
455  C CA  . LYS A 59  ? 0.1765 0.2469 0.1996 -0.0134 0.0011  0.0072  58   LYS A CA  
456  C C   . LYS A 59  ? 0.1715 0.2435 0.1951 -0.0125 0.0011  0.0076  58   LYS A C   
457  O O   . LYS A 59  ? 0.1806 0.2551 0.2068 -0.0117 0.0004  0.0084  58   LYS A O   
458  C CB  . LYS A 59  ? 0.1913 0.2602 0.2162 -0.0124 0.0025  0.0073  58   LYS A CB  
459  C CG  . LYS A 59  ? 0.2128 0.2799 0.2372 -0.0112 0.0046  0.0069  58   LYS A CG  
460  C CD  . LYS A 59  ? 0.2582 0.3235 0.2838 -0.0099 0.0058  0.0067  58   LYS A CD  
461  C CE  . LYS A 59  ? 0.3047 0.3685 0.3293 -0.0085 0.0081  0.0061  58   LYS A CE  
462  N NZ  . LYS A 59  ? 0.3374 0.3968 0.3566 -0.0090 0.0087  0.0048  58   LYS A NZ  
463  N N   . TYR A 60  ? 0.1671 0.2371 0.1878 -0.0125 0.0021  0.0072  59   TYR A N   
464  C CA  . TYR A 60  ? 0.1698 0.2402 0.1901 -0.0121 0.0023  0.0078  59   TYR A CA  
465  C C   . TYR A 60  ? 0.1687 0.2382 0.1900 -0.0117 0.0046  0.0080  59   TYR A C   
466  O O   . TYR A 60  ? 0.1796 0.2474 0.1999 -0.0114 0.0064  0.0074  59   TYR A O   
467  C CB  . TYR A 60  ? 0.1715 0.2405 0.1873 -0.0124 0.0016  0.0075  59   TYR A CB  
468  C CG  . TYR A 60  ? 0.1625 0.2338 0.1780 -0.0126 -0.0008 0.0075  59   TYR A CG  
469  C CD1 . TYR A 60  ? 0.1708 0.2425 0.1853 -0.0137 -0.0017 0.0068  59   TYR A CD1 
470  C CD2 . TYR A 60  ? 0.1599 0.2331 0.1762 -0.0116 -0.0021 0.0082  59   TYR A CD2 
471  C CE1 . TYR A 60  ? 0.1646 0.2398 0.1797 -0.0139 -0.0038 0.0070  59   TYR A CE1 
472  C CE2 . TYR A 60  ? 0.1603 0.2365 0.1766 -0.0112 -0.0042 0.0083  59   TYR A CE2 
473  C CZ  . TYR A 60  ? 0.1552 0.2330 0.1711 -0.0124 -0.0050 0.0077  59   TYR A CZ  
474  O OH  . TYR A 60  ? 0.1412 0.2232 0.1579 -0.0122 -0.0068 0.0079  59   TYR A OH  
475  N N   . ASN A 61  ? 0.1684 0.2391 0.1915 -0.0116 0.0046  0.0089  60   ASN A N   
476  C CA  . ASN A 61  ? 0.1711 0.2415 0.1946 -0.0118 0.0068  0.0095  60   ASN A CA  
477  C C   . ASN A 61  ? 0.1804 0.2481 0.1985 -0.0122 0.0074  0.0094  60   ASN A C   
478  O O   . ASN A 61  ? 0.1687 0.2354 0.1841 -0.0124 0.0056  0.0096  60   ASN A O   
479  C CB  . ASN A 61  ? 0.1622 0.2339 0.1884 -0.0123 0.0060  0.0106  60   ASN A CB  
480  C CG  . ASN A 61  ? 0.1606 0.2332 0.1886 -0.0131 0.0083  0.0115  60   ASN A CG  
481  O OD1 . ASN A 61  ? 0.1619 0.2338 0.1878 -0.0130 0.0106  0.0115  60   ASN A OD1 
482  N ND2 . ASN A 61  ? 0.1606 0.2348 0.1922 -0.0138 0.0075  0.0124  60   ASN A ND2 
483  N N   . GLU A 62  ? 0.1923 0.2587 0.2083 -0.0119 0.0099  0.0090  61   GLU A N   
484  C CA  . GLU A 62  ? 0.2190 0.2825 0.2291 -0.0121 0.0108  0.0089  61   GLU A CA  
485  C C   . GLU A 62  ? 0.2183 0.2812 0.2270 -0.0128 0.0103  0.0103  61   GLU A C   
486  O O   . GLU A 62  ? 0.2239 0.2843 0.2276 -0.0128 0.0093  0.0103  61   GLU A O   
487  C CB  . GLU A 62  ? 0.2556 0.3185 0.2647 -0.0113 0.0140  0.0086  61   GLU A CB  
488  C CG  . GLU A 62  ? 0.3194 0.3788 0.3216 -0.0110 0.0151  0.0080  61   GLU A CG  
489  C CD  . GLU A 62  ? 0.3475 0.4039 0.3453 -0.0108 0.0133  0.0062  61   GLU A CD  
490  O OE1 . GLU A 62  ? 0.3622 0.4186 0.3622 -0.0106 0.0124  0.0052  61   GLU A OE1 
491  O OE2 . GLU A 62  ? 0.3972 0.4507 0.3889 -0.0109 0.0128  0.0059  61   GLU A OE2 
492  N N   . LYS A 63  ? 0.2099 0.2746 0.2228 -0.0135 0.0107  0.0116  62   LYS A N   
493  C CA  . LYS A 63  ? 0.2326 0.2958 0.2441 -0.0146 0.0103  0.0131  62   LYS A CA  
494  C C   . LYS A 63  ? 0.2076 0.2688 0.2161 -0.0141 0.0071  0.0128  62   LYS A C   
495  O O   . LYS A 63  ? 0.2054 0.2636 0.2099 -0.0144 0.0066  0.0138  62   LYS A O   
496  C CB  . LYS A 63  ? 0.2534 0.3193 0.2707 -0.0157 0.0106  0.0140  62   LYS A CB  
497  C CG  . LYS A 63  ? 0.3010 0.3648 0.3175 -0.0173 0.0098  0.0156  62   LYS A CG  
498  C CD  . LYS A 63  ? 0.3160 0.3832 0.3387 -0.0189 0.0107  0.0166  62   LYS A CD  
499  C CE  . LYS A 63  ? 0.3776 0.4429 0.3999 -0.0215 0.0110  0.0185  62   LYS A CE  
500  N NZ  . LYS A 63  ? 0.4405 0.5005 0.4584 -0.0215 0.0079  0.0186  62   LYS A NZ  
501  N N   . PHE A 64  ? 0.1980 0.2610 0.2085 -0.0132 0.0050  0.0118  63   PHE A N   
502  C CA  . PHE A 64  ? 0.1926 0.2550 0.2011 -0.0122 0.0021  0.0116  63   PHE A CA  
503  C C   . PHE A 64  ? 0.1869 0.2494 0.1921 -0.0115 0.0010  0.0106  63   PHE A C   
504  O O   . PHE A 64  ? 0.1843 0.2474 0.1882 -0.0105 -0.0013 0.0105  63   PHE A O   
505  C CB  . PHE A 64  ? 0.1899 0.2547 0.2028 -0.0117 0.0005  0.0114  63   PHE A CB  
506  C CG  . PHE A 64  ? 0.1947 0.2586 0.2096 -0.0123 0.0003  0.0124  63   PHE A CG  
507  C CD1 . PHE A 64  ? 0.2023 0.2680 0.2216 -0.0135 0.0020  0.0127  63   PHE A CD1 
508  C CD2 . PHE A 64  ? 0.2111 0.2721 0.2232 -0.0118 -0.0015 0.0129  63   PHE A CD2 
509  C CE1 . PHE A 64  ? 0.2030 0.2680 0.2243 -0.0146 0.0015  0.0136  63   PHE A CE1 
510  C CE2 . PHE A 64  ? 0.2087 0.2678 0.2220 -0.0129 -0.0019 0.0137  63   PHE A CE2 
511  C CZ  . PHE A 64  ? 0.2185 0.2800 0.2367 -0.0145 -0.0005 0.0140  63   PHE A CZ  
512  N N   . LYS A 65  ? 0.1967 0.2588 0.2006 -0.0120 0.0025  0.0098  64   LYS A N   
513  C CA  . LYS A 65  ? 0.1996 0.2613 0.1997 -0.0117 0.0011  0.0088  64   LYS A CA  
514  C C   . LYS A 65  ? 0.2003 0.2594 0.1948 -0.0111 0.0001  0.0094  64   LYS A C   
515  O O   . LYS A 65  ? 0.1851 0.2414 0.1770 -0.0113 0.0018  0.0104  64   LYS A O   
516  C CB  . LYS A 65  ? 0.2134 0.2737 0.2119 -0.0123 0.0028  0.0077  64   LYS A CB  
517  C CG  . LYS A 65  ? 0.2328 0.2948 0.2357 -0.0126 0.0033  0.0070  64   LYS A CG  
518  C CD  . LYS A 65  ? 0.2746 0.3340 0.2748 -0.0128 0.0048  0.0057  64   LYS A CD  
519  C CE  . LYS A 65  ? 0.3173 0.3770 0.3195 -0.0134 0.0038  0.0047  64   LYS A CE  
520  N NZ  . LYS A 65  ? 0.3557 0.4120 0.3557 -0.0130 0.0058  0.0035  64   LYS A NZ  
521  N N   . GLY A 66  ? 0.2027 0.2631 0.1956 -0.0103 -0.0025 0.0091  65   GLY A N   
522  C CA  . GLY A 66  ? 0.2105 0.2685 0.1980 -0.0091 -0.0039 0.0098  65   GLY A CA  
523  C C   . GLY A 66  ? 0.2167 0.2741 0.2048 -0.0079 -0.0050 0.0109  65   GLY A C   
524  O O   . GLY A 66  ? 0.2349 0.2898 0.2183 -0.0065 -0.0064 0.0116  65   GLY A O   
525  N N   . LYS A 67  ? 0.2075 0.2667 0.2006 -0.0081 -0.0048 0.0111  66   LYS A N   
526  C CA  . LYS A 67  ? 0.2098 0.2677 0.2033 -0.0068 -0.0060 0.0119  66   LYS A CA  
527  C C   . LYS A 67  ? 0.2023 0.2648 0.2002 -0.0057 -0.0075 0.0112  66   LYS A C   
528  O O   . LYS A 67  ? 0.2129 0.2752 0.2096 -0.0036 -0.0094 0.0115  66   LYS A O   
529  C CB  . LYS A 67  ? 0.2266 0.2816 0.2213 -0.0084 -0.0041 0.0129  66   LYS A CB  
530  C CG  . LYS A 67  ? 0.2425 0.2955 0.2377 -0.0077 -0.0055 0.0135  66   LYS A CG  
531  C CD  . LYS A 67  ? 0.2622 0.3106 0.2514 -0.0059 -0.0073 0.0142  66   LYS A CD  
532  C CE  . LYS A 67  ? 0.2689 0.3126 0.2530 -0.0071 -0.0060 0.0154  66   LYS A CE  
533  N NZ  . LYS A 67  ? 0.2798 0.3175 0.2580 -0.0057 -0.0077 0.0165  66   LYS A NZ  
534  N N   . ALA A 68  ? 0.1799 0.2456 0.1823 -0.0069 -0.0065 0.0106  67   ALA A N   
535  C CA  . ALA A 68  ? 0.1852 0.2552 0.1918 -0.0061 -0.0075 0.0102  67   ALA A CA  
536  C C   . ALA A 68  ? 0.1769 0.2512 0.1852 -0.0067 -0.0079 0.0095  67   ALA A C   
537  O O   . ALA A 68  ? 0.1849 0.2585 0.1928 -0.0084 -0.0068 0.0090  67   ALA A O   
538  C CB  . ALA A 68  ? 0.1778 0.2476 0.1883 -0.0071 -0.0062 0.0104  67   ALA A CB  
539  N N   . THR A 69  ? 0.1864 0.2650 0.1963 -0.0054 -0.0095 0.0095  68   THR A N   
540  C CA  . THR A 69  ? 0.1871 0.2705 0.1996 -0.0065 -0.0099 0.0090  68   THR A CA  
541  C C   . THR A 69  ? 0.1726 0.2600 0.1892 -0.0059 -0.0099 0.0094  68   THR A C   
542  O O   . THR A 69  ? 0.1762 0.2652 0.1927 -0.0035 -0.0109 0.0097  68   THR A O   
543  C CB  . THR A 69  ? 0.2049 0.2914 0.2155 -0.0059 -0.0118 0.0089  68   THR A CB  
544  O OG1 . THR A 69  ? 0.2105 0.2928 0.2165 -0.0062 -0.0119 0.0086  68   THR A OG1 
545  C CG2 . THR A 69  ? 0.2021 0.2934 0.2155 -0.0079 -0.0124 0.0085  68   THR A CG2 
546  N N   . LEU A 70  ? 0.1756 0.2638 0.1951 -0.0078 -0.0088 0.0093  69   LEU A N   
547  C CA  . LEU A 70  ? 0.1674 0.2590 0.1903 -0.0073 -0.0086 0.0098  69   LEU A CA  
548  C C   . LEU A 70  ? 0.1649 0.2620 0.1898 -0.0085 -0.0092 0.0101  69   LEU A C   
549  O O   . LEU A 70  ? 0.1873 0.2841 0.2121 -0.0111 -0.0092 0.0097  69   LEU A O   
550  C CB  . LEU A 70  ? 0.1559 0.2448 0.1806 -0.0085 -0.0070 0.0098  69   LEU A CB  
551  C CG  . LEU A 70  ? 0.1587 0.2429 0.1823 -0.0082 -0.0061 0.0096  69   LEU A CG  
552  C CD1 . LEU A 70  ? 0.1733 0.2560 0.1993 -0.0090 -0.0047 0.0097  69   LEU A CD1 
553  C CD2 . LEU A 70  ? 0.1628 0.2462 0.1852 -0.0061 -0.0072 0.0099  69   LEU A CD2 
554  N N   . THR A 71  ? 0.1746 0.2767 0.2013 -0.0068 -0.0098 0.0107  70   THR A N   
555  C CA  . THR A 71  ? 0.1760 0.2846 0.2055 -0.0081 -0.0101 0.0114  70   THR A CA  
556  C C   . THR A 71  ? 0.1741 0.2853 0.2057 -0.0068 -0.0092 0.0123  70   THR A C   
557  O O   . THR A 71  ? 0.1638 0.2721 0.1943 -0.0045 -0.0089 0.0122  70   THR A O   
558  C CB  . THR A 71  ? 0.1838 0.2979 0.2131 -0.0068 -0.0117 0.0114  70   THR A CB  
559  O OG1 . THR A 71  ? 0.1734 0.2877 0.2011 -0.0027 -0.0122 0.0115  70   THR A OG1 
560  C CG2 . THR A 71  ? 0.2042 0.3158 0.2310 -0.0081 -0.0128 0.0106  70   THR A CG2 
561  N N   . ALA A 72  ? 0.1799 0.2966 0.2144 -0.0085 -0.0089 0.0133  71   ALA A N   
562  C CA  . ALA A 72  ? 0.1755 0.2954 0.2116 -0.0072 -0.0079 0.0144  71   ALA A CA  
563  C C   . ALA A 72  ? 0.1913 0.3201 0.2305 -0.0081 -0.0079 0.0156  71   ALA A C   
564  O O   . ALA A 72  ? 0.1891 0.3200 0.2298 -0.0115 -0.0084 0.0158  71   ALA A O   
565  C CB  . ALA A 72  ? 0.1775 0.2930 0.2140 -0.0091 -0.0066 0.0147  71   ALA A CB  
566  N N   . ASP A 73  ? 0.1914 0.3253 0.2312 -0.0049 -0.0076 0.0164  72   ASP A N   
567  C CA  . ASP A 73  ? 0.2058 0.3497 0.2489 -0.0051 -0.0073 0.0178  72   ASP A CA  
568  C C   . ASP A 73  ? 0.1902 0.3356 0.2345 -0.0060 -0.0054 0.0194  72   ASP A C   
569  O O   . ASP A 73  ? 0.1738 0.3184 0.2164 -0.0024 -0.0047 0.0194  72   ASP A O   
570  C CB  . ASP A 73  ? 0.2512 0.3997 0.2933 0.0000  -0.0080 0.0175  72   ASP A CB  
571  C CG  . ASP A 73  ? 0.2984 0.4586 0.3443 0.0006  -0.0075 0.0190  72   ASP A CG  
572  O OD1 . ASP A 73  ? 0.3268 0.4910 0.3759 -0.0031 -0.0063 0.0205  72   ASP A OD1 
573  O OD2 . ASP A 73  ? 0.3704 0.5351 0.4156 0.0051  -0.0083 0.0186  72   ASP A OD2 
574  N N   . LYS A 74  ? 0.1847 0.3307 0.2311 -0.0106 -0.0047 0.0205  73   LYS A N   
575  C CA  . LYS A 74  ? 0.2147 0.3614 0.2617 -0.0114 -0.0028 0.0223  73   LYS A CA  
576  C C   . LYS A 74  ? 0.1940 0.3506 0.2428 -0.0088 -0.0017 0.0238  73   LYS A C   
577  O O   . LYS A 74  ? 0.1919 0.3483 0.2396 -0.0073 -0.0002 0.0249  73   LYS A O   
578  C CB  . LYS A 74  ? 0.2701 0.4155 0.3187 -0.0172 -0.0023 0.0235  73   LYS A CB  
579  C CG  . LYS A 74  ? 0.3205 0.4550 0.3663 -0.0190 -0.0027 0.0223  73   LYS A CG  
580  C CD  . LYS A 74  ? 0.4177 0.5493 0.4635 -0.0226 -0.0040 0.0212  73   LYS A CD  
581  C CE  . LYS A 74  ? 0.4600 0.5902 0.5067 -0.0280 -0.0038 0.0224  73   LYS A CE  
582  N NZ  . LYS A 74  ? 0.5218 0.6416 0.5653 -0.0297 -0.0042 0.0210  73   LYS A NZ  
583  N N   . SER A 75  ? 0.1689 0.3338 0.2202 -0.0079 -0.0025 0.0239  74   SER A N   
584  C CA  . SER A 75  ? 0.1535 0.3292 0.2070 -0.0051 -0.0012 0.0255  74   SER A CA  
585  C C   . SER A 75  ? 0.1539 0.3274 0.2035 0.0012  -0.0007 0.0246  74   SER A C   
586  O O   . SER A 75  ? 0.1452 0.3250 0.1952 0.0037  0.0009  0.0261  74   SER A O   
587  C CB  . SER A 75  ? 0.1519 0.3375 0.2093 -0.0053 -0.0023 0.0257  74   SER A CB  
588  O OG  . SER A 75  ? 0.1438 0.3276 0.1989 -0.0010 -0.0042 0.0236  74   SER A OG  
589  N N   . SER A 76  ? 0.1509 0.3156 0.1966 0.0037  -0.0022 0.0225  75   SER A N   
590  C CA  . SER A 76  ? 0.1567 0.3181 0.1980 0.0095  -0.0025 0.0213  75   SER A CA  
591  C C   . SER A 76  ? 0.1681 0.3189 0.2060 0.0091  -0.0027 0.0204  75   SER A C   
592  O O   . SER A 76  ? 0.1730 0.3197 0.2070 0.0133  -0.0033 0.0193  75   SER A O   
593  C CB  . SER A 76  ? 0.1658 0.3263 0.2053 0.0130  -0.0044 0.0196  75   SER A CB  
594  O OG  . SER A 76  ? 0.1531 0.3057 0.1915 0.0103  -0.0059 0.0183  75   SER A OG  
595  N N   . SER A 77  ? 0.1578 0.3045 0.1971 0.0044  -0.0024 0.0208  76   SER A N   
596  C CA  . SER A 77  ? 0.1729 0.3100 0.2096 0.0038  -0.0027 0.0200  76   SER A CA  
597  C C   . SER A 77  ? 0.1659 0.2970 0.1998 0.0063  -0.0044 0.0179  76   SER A C   
598  O O   . SER A 77  ? 0.1666 0.2922 0.1976 0.0084  -0.0050 0.0170  76   SER A O   
599  C CB  . SER A 77  ? 0.1928 0.3295 0.2278 0.0055  -0.0015 0.0209  76   SER A CB  
600  O OG  . SER A 77  ? 0.2126 0.3543 0.2500 0.0027  0.0002  0.0232  76   SER A OG  
601  N N   . THR A 78  ? 0.1696 0.3014 0.2041 0.0058  -0.0055 0.0171  77   THR A N   
602  C CA  . THR A 78  ? 0.1694 0.2955 0.2009 0.0080  -0.0071 0.0153  77   THR A CA  
603  C C   . THR A 78  ? 0.1639 0.2854 0.1960 0.0044  -0.0076 0.0147  77   THR A C   
604  O O   . THR A 78  ? 0.1573 0.2822 0.1916 0.0016  -0.0076 0.0151  77   THR A O   
605  C CB  . THR A 78  ? 0.1805 0.3105 0.2105 0.0120  -0.0081 0.0149  77   THR A CB  
606  O OG1 . THR A 78  ? 0.1888 0.3227 0.2177 0.0157  -0.0073 0.0155  77   THR A OG1 
607  C CG2 . THR A 78  ? 0.1834 0.3064 0.2094 0.0143  -0.0098 0.0134  77   THR A CG2 
608  N N   . ALA A 79  ? 0.1531 0.2673 0.1832 0.0045  -0.0082 0.0137  78   ALA A N   
609  C CA  . ALA A 79  ? 0.1563 0.2657 0.1861 0.0020  -0.0085 0.0129  78   ALA A CA  
610  C C   . ALA A 79  ? 0.1604 0.2674 0.1872 0.0043  -0.0099 0.0120  78   ALA A C   
611  O O   . ALA A 79  ? 0.1824 0.2878 0.2067 0.0077  -0.0107 0.0117  78   ALA A O   
612  C CB  . ALA A 79  ? 0.1561 0.2598 0.1860 0.0006  -0.0080 0.0126  78   ALA A CB  
613  N N   . TYR A 80  ? 0.1685 0.2745 0.1949 0.0027  -0.0103 0.0117  79   TYR A N   
614  C CA  . TYR A 80  ? 0.1627 0.2658 0.1857 0.0046  -0.0116 0.0111  79   TYR A CA  
615  C C   . TYR A 80  ? 0.1620 0.2591 0.1838 0.0021  -0.0113 0.0107  79   TYR A C   
616  O O   . TYR A 80  ? 0.1741 0.2712 0.1976 -0.0008 -0.0104 0.0107  79   TYR A O   
617  C CB  . TYR A 80  ? 0.1677 0.2766 0.1911 0.0055  -0.0125 0.0113  79   TYR A CB  
618  C CG  . TYR A 80  ? 0.1838 0.2999 0.2086 0.0083  -0.0126 0.0119  79   TYR A CG  
619  C CD1 . TYR A 80  ? 0.1946 0.3178 0.2235 0.0064  -0.0116 0.0128  79   TYR A CD1 
620  C CD2 . TYR A 80  ? 0.1998 0.3154 0.2215 0.0129  -0.0135 0.0116  79   TYR A CD2 
621  C CE1 . TYR A 80  ? 0.1995 0.3302 0.2299 0.0090  -0.0114 0.0136  79   TYR A CE1 
622  C CE2 . TYR A 80  ? 0.2020 0.3245 0.2247 0.0161  -0.0134 0.0121  79   TYR A CE2 
623  C CZ  . TYR A 80  ? 0.1948 0.3254 0.2221 0.0141  -0.0121 0.0132  79   TYR A CZ  
624  O OH  . TYR A 80  ? 0.1888 0.3269 0.2171 0.0175  -0.0117 0.0139  79   TYR A OH  
625  N N   . MET A 81  ? 0.1712 0.2630 0.1897 0.0035  -0.0120 0.0103  80   MET A N   
626  C CA  . MET A 81  ? 0.1781 0.2647 0.1947 0.0016  -0.0117 0.0101  80   MET A CA  
627  C C   . MET A 81  ? 0.1836 0.2681 0.1959 0.0037  -0.0131 0.0101  80   MET A C   
628  O O   . MET A 81  ? 0.1720 0.2538 0.1815 0.0064  -0.0143 0.0101  80   MET A O   
629  C CB  . MET A 81  ? 0.1836 0.2649 0.2001 0.0007  -0.0111 0.0101  80   MET A CB  
630  C CG  . MET A 81  ? 0.2046 0.2816 0.2193 -0.0010 -0.0105 0.0102  80   MET A CG  
631  S SD  . MET A 81  ? 0.2438 0.3165 0.2598 -0.0028 -0.0095 0.0103  80   MET A SD  
632  C CE  . MET A 81  ? 0.2326 0.3016 0.2455 -0.0004 -0.0116 0.0103  80   MET A CE  
633  N N   . GLN A 82  ? 0.2069 0.2924 0.2183 0.0026  -0.0132 0.0101  81   GLN A N   
634  C CA  . GLN A 82  ? 0.2179 0.3009 0.2247 0.0045  -0.0146 0.0102  81   GLN A CA  
635  C C   . GLN A 82  ? 0.2044 0.2804 0.2082 0.0026  -0.0137 0.0104  81   GLN A C   
636  O O   . GLN A 82  ? 0.2030 0.2789 0.2083 -0.0002 -0.0122 0.0103  81   GLN A O   
637  C CB  . GLN A 82  ? 0.2494 0.3379 0.2566 0.0046  -0.0156 0.0101  81   GLN A CB  
638  C CG  . GLN A 82  ? 0.3068 0.3932 0.3091 0.0073  -0.0173 0.0103  81   GLN A CG  
639  C CD  . GLN A 82  ? 0.4010 0.4938 0.4042 0.0075  -0.0187 0.0102  81   GLN A CD  
640  O OE1 . GLN A 82  ? 0.4870 0.5855 0.4944 0.0052  -0.0184 0.0099  81   GLN A OE1 
641  N NE2 . GLN A 82  ? 0.4576 0.5492 0.4564 0.0101  -0.0205 0.0103  81   GLN A NE2 
642  N N   . LEU A 83  ? 0.2026 0.2730 0.2022 0.0041  -0.0145 0.0108  82   LEU A N   
643  C CA  . LEU A 83  ? 0.2115 0.2754 0.2077 0.0024  -0.0137 0.0114  82   LEU A CA  
644  C C   . LEU A 83  ? 0.2174 0.2789 0.2080 0.0042  -0.0150 0.0118  82   LEU A C   
645  O O   . LEU A 83  ? 0.2413 0.3021 0.2293 0.0076  -0.0169 0.0118  82   LEU A O   
646  C CB  . LEU A 83  ? 0.2139 0.2725 0.2093 0.0022  -0.0137 0.0117  82   LEU A CB  
647  C CG  . LEU A 83  ? 0.2168 0.2775 0.2174 0.0005  -0.0126 0.0114  82   LEU A CG  
648  C CD1 . LEU A 83  ? 0.2313 0.2871 0.2306 0.0009  -0.0136 0.0115  82   LEU A CD1 
649  C CD2 . LEU A 83  ? 0.2198 0.2812 0.2231 -0.0028 -0.0102 0.0116  82   LEU A CD2 
650  N N   . ASN A 84  A 0.2200 0.2803 0.2088 0.0024  -0.0141 0.0120  82   ASN A N   
651  C CA  . ASN A 84  A 0.2316 0.2902 0.2148 0.0041  -0.0155 0.0123  82   ASN A CA  
652  C C   . ASN A 84  A 0.2396 0.2900 0.2173 0.0033  -0.0147 0.0135  82   ASN A C   
653  O O   . ASN A 84  A 0.2366 0.2843 0.2158 0.0005  -0.0126 0.0139  82   ASN A O   
654  C CB  . ASN A 84  A 0.2389 0.3019 0.2227 0.0030  -0.0156 0.0116  82   ASN A CB  
655  C CG  . ASN A 84  A 0.2334 0.2949 0.2182 -0.0004 -0.0131 0.0114  82   ASN A CG  
656  O OD1 . ASN A 84  A 0.2466 0.3039 0.2268 -0.0012 -0.0122 0.0119  82   ASN A OD1 
657  N ND2 . ASN A 84  A 0.2146 0.2796 0.2048 -0.0022 -0.0119 0.0108  82   ASN A ND2 
658  N N   . SER A 85  B 0.2392 0.2862 0.2108 0.0056  -0.0163 0.0141  82   SER A N   
659  C CA  . SER A 85  B 0.2476 0.2870 0.2128 0.0047  -0.0155 0.0155  82   SER A CA  
660  C C   . SER A 85  B 0.2472 0.2805 0.2120 0.0031  -0.0144 0.0165  82   SER A C   
661  O O   . SER A 85  B 0.2410 0.2713 0.2057 0.0000  -0.0120 0.0174  82   SER A O   
662  C CB  . SER A 85  B 0.2477 0.2882 0.2127 0.0020  -0.0135 0.0154  82   SER A CB  
663  O OG  . SER A 85  B 0.2432 0.2898 0.2096 0.0028  -0.0148 0.0141  82   SER A OG  
664  N N   . LEU A 86  C 0.2484 0.2797 0.2128 0.0054  -0.0162 0.0164  82   LEU A N   
665  C CA  . LEU A 86  C 0.2622 0.2891 0.2279 0.0035  -0.0157 0.0168  82   LEU A CA  
666  C C   . LEU A 86  C 0.2777 0.2951 0.2373 0.0019  -0.0153 0.0187  82   LEU A C   
667  O O   . LEU A 86  C 0.3112 0.3236 0.2638 0.0040  -0.0165 0.0195  82   LEU A O   
668  C CB  . LEU A 86  C 0.2721 0.2995 0.2385 0.0067  -0.0179 0.0159  82   LEU A CB  
669  C CG  . LEU A 86  C 0.2678 0.3045 0.2412 0.0074  -0.0178 0.0144  82   LEU A CG  
670  C CD1 . LEU A 86  C 0.2721 0.3090 0.2446 0.0115  -0.0200 0.0136  82   LEU A CD1 
671  C CD2 . LEU A 86  C 0.2738 0.3130 0.2533 0.0036  -0.0157 0.0141  82   LEU A CD2 
672  N N   . THR A 87  ? 0.2868 0.3022 0.2490 -0.0019 -0.0135 0.0194  83   THR A N   
673  C CA  . THR A 87  ? 0.3267 0.3333 0.2843 -0.0045 -0.0130 0.0214  83   THR A CA  
674  C C   . THR A 87  ? 0.3222 0.3264 0.2828 -0.0063 -0.0138 0.0212  83   THR A C   
675  O O   . THR A 87  ? 0.2998 0.3098 0.2663 -0.0057 -0.0143 0.0196  83   THR A O   
676  C CB  . THR A 87  ? 0.3218 0.3294 0.2804 -0.0084 -0.0096 0.0228  83   THR A CB  
677  O OG1 . THR A 87  ? 0.3376 0.3511 0.3043 -0.0113 -0.0077 0.0222  83   THR A OG1 
678  C CG2 . THR A 87  ? 0.3184 0.3297 0.2752 -0.0069 -0.0087 0.0224  83   THR A CG2 
679  N N   . SER A 88  ? 0.3461 0.3420 0.3027 -0.0089 -0.0140 0.0229  84   SER A N   
680  C CA  . SER A 88  ? 0.3476 0.3404 0.3067 -0.0115 -0.0149 0.0228  84   SER A CA  
681  C C   . SER A 88  ? 0.3362 0.3378 0.3048 -0.0147 -0.0127 0.0223  84   SER A C   
682  O O   . SER A 88  ? 0.3119 0.3142 0.2842 -0.0156 -0.0141 0.0213  84   SER A O   
683  C CB  . SER A 88  ? 0.3925 0.3755 0.3462 -0.0149 -0.0150 0.0251  84   SER A CB  
684  O OG  . SER A 88  ? 0.4283 0.4133 0.3828 -0.0183 -0.0116 0.0271  84   SER A OG  
685  N N   . GLU A 89  ? 0.3513 0.3588 0.3232 -0.0163 -0.0096 0.0228  85   GLU A N   
686  C CA  . GLU A 89  ? 0.3519 0.3675 0.3324 -0.0190 -0.0073 0.0224  85   GLU A CA  
687  C C   . GLU A 89  ? 0.3087 0.3306 0.2938 -0.0161 -0.0085 0.0201  85   GLU A C   
688  O O   . GLU A 89  ? 0.3193 0.3466 0.3113 -0.0178 -0.0076 0.0196  85   GLU A O   
689  C CB  . GLU A 89  ? 0.4109 0.4304 0.3925 -0.0205 -0.0036 0.0234  85   GLU A CB  
690  C CG  . GLU A 89  ? 0.4829 0.4977 0.4617 -0.0243 -0.0016 0.0261  85   GLU A CG  
691  C CD  . GLU A 89  ? 0.5791 0.5960 0.5562 -0.0250 0.0018  0.0273  85   GLU A CD  
692  O OE1 . GLU A 89  ? 0.6530 0.6696 0.6310 -0.0288 0.0045  0.0294  85   GLU A OE1 
693  O OE2 . GLU A 89  ? 0.6720 0.6910 0.6469 -0.0220 0.0020  0.0261  85   GLU A OE2 
694  N N   . ASP A 90  ? 0.2724 0.2938 0.2542 -0.0120 -0.0106 0.0189  86   ASP A N   
695  C CA  . ASP A 90  ? 0.2614 0.2888 0.2471 -0.0092 -0.0117 0.0170  86   ASP A CA  
696  C C   . ASP A 90  ? 0.2630 0.2875 0.2484 -0.0079 -0.0144 0.0161  86   ASP A C   
697  O O   . ASP A 90  ? 0.2567 0.2862 0.2458 -0.0063 -0.0149 0.0148  86   ASP A O   
698  C CB  . ASP A 90  ? 0.2560 0.2857 0.2389 -0.0055 -0.0124 0.0163  86   ASP A CB  
699  C CG  . ASP A 90  ? 0.2579 0.2908 0.2412 -0.0068 -0.0100 0.0167  86   ASP A CG  
700  O OD1 . ASP A 90  ? 0.2581 0.2953 0.2465 -0.0091 -0.0077 0.0166  86   ASP A OD1 
701  O OD2 . ASP A 90  ? 0.2664 0.2967 0.2444 -0.0054 -0.0104 0.0172  86   ASP A OD2 
702  N N   . SER A 91  ? 0.2757 0.2917 0.2560 -0.0086 -0.0161 0.0169  87   SER A N   
703  C CA  . SER A 91  ? 0.2760 0.2878 0.2552 -0.0078 -0.0188 0.0159  87   SER A CA  
704  C C   . SER A 91  ? 0.2701 0.2870 0.2567 -0.0107 -0.0182 0.0154  87   SER A C   
705  O O   . SER A 91  ? 0.2866 0.3045 0.2767 -0.0149 -0.0165 0.0166  87   SER A O   
706  C CB  . SER A 91  ? 0.3034 0.3042 0.2757 -0.0091 -0.0205 0.0171  87   SER A CB  
707  O OG  . SER A 91  ? 0.3154 0.3117 0.2806 -0.0055 -0.0213 0.0174  87   SER A OG  
708  N N   . ALA A 92  ? 0.2699 0.2906 0.2589 -0.0082 -0.0193 0.0138  88   ALA A N   
709  C CA  . ALA A 92  ? 0.2585 0.2846 0.2542 -0.0100 -0.0190 0.0132  88   ALA A CA  
710  C C   . ALA A 92  ? 0.2513 0.2795 0.2469 -0.0062 -0.0208 0.0115  88   ALA A C   
711  O O   . ALA A 92  ? 0.2605 0.2869 0.2514 -0.0022 -0.0219 0.0109  88   ALA A O   
712  C CB  . ALA A 92  ? 0.2545 0.2884 0.2563 -0.0117 -0.0159 0.0137  88   ALA A CB  
713  N N   . VAL A 93  ? 0.2316 0.2638 0.2323 -0.0074 -0.0210 0.0109  89   VAL A N   
714  C CA  . VAL A 93  ? 0.2228 0.2589 0.2245 -0.0041 -0.0218 0.0096  89   VAL A CA  
715  C C   . VAL A 93  ? 0.2135 0.2582 0.2210 -0.0044 -0.0191 0.0098  89   VAL A C   
716  O O   . VAL A 93  ? 0.2192 0.2665 0.2312 -0.0075 -0.0174 0.0106  89   VAL A O   
717  C CB  . VAL A 93  ? 0.2315 0.2659 0.2342 -0.0049 -0.0241 0.0087  89   VAL A CB  
718  C CG1 . VAL A 93  ? 0.2293 0.2677 0.2325 -0.0014 -0.0246 0.0075  89   VAL A CG1 
719  C CG2 . VAL A 93  ? 0.2442 0.2687 0.2404 -0.0052 -0.0270 0.0084  89   VAL A CG2 
720  N N   . TYR A 94  ? 0.2007 0.2491 0.2075 -0.0011 -0.0187 0.0093  90   TYR A N   
721  C CA  . TYR A 94  ? 0.1902 0.2459 0.2016 -0.0011 -0.0165 0.0095  90   TYR A CA  
722  C C   . TYR A 94  ? 0.1891 0.2484 0.2023 0.0006  -0.0171 0.0088  90   TYR A C   
723  O O   . TYR A 94  ? 0.1946 0.2532 0.2044 0.0039  -0.0185 0.0081  90   TYR A O   
724  C CB  . TYR A 94  ? 0.1852 0.2427 0.1946 0.0003  -0.0156 0.0097  90   TYR A CB  
725  C CG  . TYR A 94  ? 0.1927 0.2468 0.2001 -0.0016 -0.0148 0.0106  90   TYR A CG  
726  C CD1 . TYR A 94  ? 0.1868 0.2434 0.1973 -0.0042 -0.0125 0.0111  90   TYR A CD1 
727  C CD2 . TYR A 94  ? 0.2130 0.2607 0.2148 -0.0007 -0.0162 0.0108  90   TYR A CD2 
728  C CE1 . TYR A 94  ? 0.1872 0.2407 0.1953 -0.0058 -0.0115 0.0120  90   TYR A CE1 
729  C CE2 . TYR A 94  ? 0.2103 0.2543 0.2098 -0.0026 -0.0154 0.0118  90   TYR A CE2 
730  C CZ  . TYR A 94  ? 0.2027 0.2499 0.2053 -0.0052 -0.0129 0.0125  90   TYR A CZ  
731  O OH  . TYR A 94  ? 0.2091 0.2530 0.2088 -0.0068 -0.0118 0.0135  90   TYR A OH  
732  N N   . PHE A 95  ? 0.1809 0.2443 0.1991 -0.0009 -0.0158 0.0090  91   PHE A N   
733  C CA  . PHE A 95  ? 0.1714 0.2386 0.1915 0.0005  -0.0159 0.0087  91   PHE A CA  
734  C C   . PHE A 95  ? 0.1698 0.2422 0.1924 0.0005  -0.0138 0.0092  91   PHE A C   
735  O O   . PHE A 95  ? 0.1542 0.2277 0.1793 -0.0016 -0.0121 0.0096  91   PHE A O   
736  C CB  . PHE A 95  ? 0.1728 0.2399 0.1962 -0.0012 -0.0165 0.0086  91   PHE A CB  
737  C CG  . PHE A 95  ? 0.1837 0.2458 0.2046 -0.0014 -0.0191 0.0080  91   PHE A CG  
738  C CD1 . PHE A 95  ? 0.2075 0.2679 0.2251 0.0012  -0.0212 0.0071  91   PHE A CD1 
739  C CD2 . PHE A 95  ? 0.1994 0.2580 0.2206 -0.0044 -0.0195 0.0084  91   PHE A CD2 
740  C CE1 . PHE A 95  ? 0.2089 0.2637 0.2235 0.0009  -0.0241 0.0063  91   PHE A CE1 
741  C CE2 . PHE A 95  ? 0.1996 0.2530 0.2184 -0.0051 -0.0223 0.0078  91   PHE A CE2 
742  C CZ  . PHE A 95  ? 0.2134 0.2645 0.2286 -0.0024 -0.0247 0.0067  91   PHE A CZ  
743  N N   . CYS A 96  ? 0.1668 0.2424 0.1891 0.0027  -0.0138 0.0091  92   CYS A N   
744  C CA  . CYS A 96  ? 0.1630 0.2432 0.1884 0.0020  -0.0121 0.0097  92   CYS A CA  
745  C C   . CYS A 96  ? 0.1583 0.2392 0.1857 0.0021  -0.0123 0.0098  92   CYS A C   
746  O O   . CYS A 96  ? 0.1730 0.2518 0.1986 0.0035  -0.0141 0.0093  92   CYS A O   
747  C CB  . CYS A 96  ? 0.1818 0.2658 0.2061 0.0038  -0.0116 0.0100  92   CYS A CB  
748  S SG  . CYS A 96  ? 0.2252 0.3102 0.2467 0.0075  -0.0130 0.0097  92   CYS A SG  
749  N N   . LYS A 97  ? 0.1473 0.2303 0.1777 0.0007  -0.0108 0.0104  93   LYS A N   
750  C CA  . LYS A 97  ? 0.1492 0.2328 0.1813 0.0011  -0.0110 0.0106  93   LYS A CA  
751  C C   . LYS A 97  ? 0.1480 0.2339 0.1819 0.0003  -0.0093 0.0115  93   LYS A C   
752  O O   . LYS A 97  ? 0.1418 0.2281 0.1764 -0.0011 -0.0079 0.0116  93   LYS A O   
753  C CB  . LYS A 97  ? 0.1457 0.2275 0.1800 0.0000  -0.0119 0.0102  93   LYS A CB  
754  C CG  . LYS A 97  ? 0.1483 0.2303 0.1858 -0.0022 -0.0103 0.0105  93   LYS A CG  
755  C CD  . LYS A 97  ? 0.1610 0.2447 0.2010 -0.0022 -0.0090 0.0110  93   LYS A CD  
756  C CE  . LYS A 97  ? 0.1612 0.2455 0.2032 -0.0014 -0.0103 0.0111  93   LYS A CE  
757  N NZ  . LYS A 97  ? 0.1684 0.2538 0.2122 -0.0008 -0.0093 0.0117  93   LYS A NZ  
758  N N   . ARG A 98  ? 0.1462 0.2329 0.1803 0.0014  -0.0095 0.0120  94   ARG A N   
759  C CA  . ARG A 98  ? 0.1539 0.2418 0.1888 0.0008  -0.0080 0.0130  94   ARG A CA  
760  C C   . ARG A 98  ? 0.1437 0.2301 0.1811 0.0000  -0.0075 0.0131  94   ARG A C   
761  O O   . ARG A 98  ? 0.1296 0.2155 0.1682 0.0008  -0.0086 0.0128  94   ARG A O   
762  C CB  . ARG A 98  ? 0.1586 0.2480 0.1916 0.0026  -0.0083 0.0138  94   ARG A CB  
763  C CG  . ARG A 98  ? 0.1651 0.2556 0.1983 0.0017  -0.0067 0.0152  94   ARG A CG  
764  C CD  . ARG A 98  ? 0.1677 0.2599 0.1987 0.0036  -0.0069 0.0162  94   ARG A CD  
765  N NE  . ARG A 98  ? 0.1709 0.2614 0.2008 0.0056  -0.0082 0.0161  94   ARG A NE  
766  C CZ  . ARG A 98  ? 0.1771 0.2681 0.2047 0.0072  -0.0082 0.0172  94   ARG A CZ  
767  N NH1 . ARG A 98  ? 0.1753 0.2689 0.2016 0.0070  -0.0066 0.0187  94   ARG A NH1 
768  N NH2 . ARG A 98  ? 0.1784 0.2676 0.2049 0.0090  -0.0098 0.0169  94   ARG A NH2 
769  N N   . SER A 99  ? 0.1319 0.2178 0.1699 -0.0015 -0.0058 0.0135  95   SER A N   
770  C CA  . SER A 99  ? 0.1274 0.2116 0.1668 -0.0017 -0.0050 0.0138  95   SER A CA  
771  C C   . SER A 99  ? 0.1217 0.2054 0.1636 -0.0018 -0.0049 0.0130  95   SER A C   
772  O O   . SER A 99  ? 0.1196 0.2039 0.1620 -0.0023 -0.0054 0.0123  95   SER A O   
773  C CB  . SER A 99  ? 0.1349 0.2190 0.1737 0.0000  -0.0056 0.0147  95   SER A CB  
774  O OG  . SER A 99  ? 0.1423 0.2243 0.1815 0.0000  -0.0046 0.0153  95   SER A OG  
775  N N   . LEU A 100 ? 0.1293 0.2121 0.1726 -0.0012 -0.0042 0.0132  96   LEU A N   
776  C CA  . LEU A 100 ? 0.1326 0.2163 0.1791 -0.0007 -0.0041 0.0127  96   LEU A CA  
777  C C   . LEU A 100 ? 0.1384 0.2239 0.1865 0.0006  -0.0062 0.0129  96   LEU A C   
778  O O   . LEU A 100 ? 0.1461 0.2314 0.1922 0.0015  -0.0074 0.0133  96   LEU A O   
779  C CB  . LEU A 100 ? 0.1380 0.2200 0.1849 -0.0001 -0.0025 0.0128  96   LEU A CB  
780  C CG  . LEU A 100 ? 0.1474 0.2269 0.1923 -0.0015 -0.0006 0.0124  96   LEU A CG  
781  C CD1 . LEU A 100 ? 0.1513 0.2279 0.1956 -0.0003 0.0006  0.0124  96   LEU A CD1 
782  C CD2 . LEU A 100 ? 0.1478 0.2285 0.1936 -0.0027 0.0000  0.0116  96   LEU A CD2 
783  N N   . PRO A 101 ? 0.1388 0.2265 0.1905 0.0006  -0.0067 0.0125  97   PRO A N   
784  C CA  . PRO A 101 ? 0.1399 0.2295 0.1934 0.0018  -0.0090 0.0126  97   PRO A CA  
785  C C   . PRO A 101 ? 0.1488 0.2376 0.2015 0.0041  -0.0092 0.0133  97   PRO A C   
786  O O   . PRO A 101 ? 0.1547 0.2424 0.2075 0.0048  -0.0075 0.0137  97   PRO A O   
787  C CB  . PRO A 101 ? 0.1380 0.2307 0.1964 0.0010  -0.0088 0.0123  97   PRO A CB  
788  C CG  . PRO A 101 ? 0.1410 0.2328 0.1988 -0.0008 -0.0069 0.0121  97   PRO A CG  
789  C CD  . PRO A 101 ? 0.1423 0.2311 0.1966 -0.0003 -0.0051 0.0122  97   PRO A CD  
790  N N   . GLY A 102 ? 0.1440 0.2327 0.1949 0.0053  -0.0113 0.0136  98   GLY A N   
791  C CA  . GLY A 102 ? 0.1422 0.2297 0.1912 0.0075  -0.0117 0.0145  98   GLY A CA  
792  C C   . GLY A 102 ? 0.1470 0.2335 0.1919 0.0081  -0.0129 0.0148  98   GLY A C   
793  O O   . GLY A 102 ? 0.1332 0.2202 0.1774 0.0073  -0.0141 0.0140  98   GLY A O   
794  N N   . THR A 103 ? 0.1612 0.2460 0.2032 0.0096  -0.0127 0.0160  99   THR A N   
795  C CA  . THR A 103 ? 0.1858 0.2700 0.2237 0.0108  -0.0140 0.0165  99   THR A CA  
796  C C   . THR A 103 ? 0.1611 0.2455 0.1966 0.0096  -0.0131 0.0163  99   THR A C   
797  O O   . THR A 103 ? 0.1579 0.2426 0.1906 0.0109  -0.0146 0.0160  99   THR A O   
798  C CB  . THR A 103 ? 0.2339 0.3161 0.2690 0.0127  -0.0138 0.0181  99   THR A CB  
799  O OG1 . THR A 103 ? 0.3176 0.4003 0.3498 0.0144  -0.0159 0.0180  99   THR A OG1 
800  C CG2 . THR A 103 ? 0.2544 0.3345 0.2869 0.0115  -0.0112 0.0195  99   THR A CG2 
801  N N   . PHE A 104 ? 0.1510 0.2353 0.1874 0.0075  -0.0111 0.0162  100  PHE A N   
802  C CA  . PHE A 104 ? 0.1484 0.2336 0.1827 0.0067  -0.0103 0.0162  100  PHE A CA  
803  C C   . PHE A 104 ? 0.1522 0.2381 0.1876 0.0060  -0.0113 0.0146  100  PHE A C   
804  O O   . PHE A 104 ? 0.1461 0.2328 0.1799 0.0056  -0.0108 0.0144  100  PHE A O   
805  C CB  . PHE A 104 ? 0.1493 0.2340 0.1834 0.0048  -0.0079 0.0171  100  PHE A CB  
806  C CG  . PHE A 104 ? 0.1477 0.2308 0.1799 0.0051  -0.0070 0.0188  100  PHE A CG  
807  C CD1 . PHE A 104 ? 0.1501 0.2341 0.1792 0.0060  -0.0068 0.0201  100  PHE A CD1 
808  C CD2 . PHE A 104 ? 0.1511 0.2313 0.1842 0.0048  -0.0063 0.0192  100  PHE A CD2 
809  C CE1 . PHE A 104 ? 0.1562 0.2382 0.1832 0.0060  -0.0058 0.0220  100  PHE A CE1 
810  C CE2 . PHE A 104 ? 0.1577 0.2352 0.1883 0.0051  -0.0055 0.0210  100  PHE A CE2 
811  C CZ  . PHE A 104 ? 0.1556 0.2340 0.1831 0.0055  -0.0053 0.0225  100  PHE A CZ  
812  N N   . ASP A 105 ? 0.1423 0.2282 0.1806 0.0057  -0.0125 0.0137  101  ASP A N   
813  C CA  . ASP A 105 ? 0.1411 0.2269 0.1802 0.0045  -0.0134 0.0125  101  ASP A CA  
814  C C   . ASP A 105 ? 0.1462 0.2312 0.1814 0.0059  -0.0150 0.0119  101  ASP A C   
815  O O   . ASP A 105 ? 0.1338 0.2185 0.1670 0.0077  -0.0167 0.0119  101  ASP A O   
816  C CB  . ASP A 105 ? 0.1398 0.2263 0.1826 0.0039  -0.0148 0.0119  101  ASP A CB  
817  C CG  . ASP A 105 ? 0.1352 0.2213 0.1793 0.0020  -0.0152 0.0111  101  ASP A CG  
818  O OD1 . ASP A 105 ? 0.1643 0.2510 0.2109 0.0005  -0.0134 0.0112  101  ASP A OD1 
819  O OD2 . ASP A 105 ? 0.1398 0.2245 0.1821 0.0021  -0.0174 0.0103  101  ASP A OD2 
820  N N   . TYR A 106 ? 0.1447 0.2293 0.1784 0.0054  -0.0146 0.0115  102  TYR A N   
821  C CA  . TYR A 106 ? 0.1634 0.2470 0.1929 0.0072  -0.0159 0.0108  102  TYR A CA  
822  C C   . TYR A 106 ? 0.1622 0.2448 0.1913 0.0061  -0.0156 0.0102  102  TYR A C   
823  O O   . TYR A 106 ? 0.1564 0.2403 0.1873 0.0046  -0.0136 0.0107  102  TYR A O   
824  C CB  . TYR A 106 ? 0.2044 0.2900 0.2310 0.0092  -0.0148 0.0117  102  TYR A CB  
825  C CG  . TYR A 106 ? 0.2562 0.3407 0.2781 0.0120  -0.0164 0.0110  102  TYR A CG  
826  C CD1 . TYR A 106 ? 0.3406 0.4241 0.3597 0.0142  -0.0181 0.0107  102  TYR A CD1 
827  C CD2 . TYR A 106 ? 0.3099 0.3943 0.3297 0.0128  -0.0162 0.0104  102  TYR A CD2 
828  C CE1 . TYR A 106 ? 0.3672 0.4490 0.3811 0.0171  -0.0196 0.0097  102  TYR A CE1 
829  C CE2 . TYR A 106 ? 0.3532 0.4360 0.3683 0.0158  -0.0178 0.0094  102  TYR A CE2 
830  C CZ  . TYR A 106 ? 0.3514 0.4328 0.3632 0.0180  -0.0193 0.0091  102  TYR A CZ  
831  O OH  . TYR A 106 ? 0.4349 0.5142 0.4413 0.0213  -0.0206 0.0079  102  TYR A OH  
832  N N   . TRP A 107 ? 0.1653 0.2451 0.1917 0.0069  -0.0176 0.0091  103  TRP A N   
833  C CA  . TRP A 107 ? 0.1707 0.2482 0.1960 0.0060  -0.0178 0.0086  103  TRP A CA  
834  C C   . TRP A 107 ? 0.1878 0.2641 0.2081 0.0088  -0.0186 0.0080  103  TRP A C   
835  O O   . TRP A 107 ? 0.1873 0.2624 0.2042 0.0114  -0.0200 0.0074  103  TRP A O   
836  C CB  . TRP A 107 ? 0.1807 0.2551 0.2072 0.0040  -0.0196 0.0079  103  TRP A CB  
837  C CG  . TRP A 107 ? 0.1775 0.2539 0.2092 0.0015  -0.0186 0.0085  103  TRP A CG  
838  C CD1 . TRP A 107 ? 0.1729 0.2518 0.2076 0.0017  -0.0185 0.0089  103  TRP A CD1 
839  C CD2 . TRP A 107 ? 0.1805 0.2568 0.2150 -0.0010 -0.0174 0.0088  103  TRP A CD2 
840  N NE1 . TRP A 107 ? 0.1715 0.2522 0.2108 -0.0004 -0.0173 0.0094  103  TRP A NE1 
841  C CE2 . TRP A 107 ? 0.1771 0.2563 0.2164 -0.0022 -0.0165 0.0093  103  TRP A CE2 
842  C CE3 . TRP A 107 ? 0.1857 0.2598 0.2188 -0.0023 -0.0168 0.0088  103  TRP A CE3 
843  C CZ2 . TRP A 107 ? 0.1730 0.2534 0.2158 -0.0045 -0.0148 0.0098  103  TRP A CZ2 
844  C CZ3 . TRP A 107 ? 0.1813 0.2560 0.2176 -0.0049 -0.0154 0.0093  103  TRP A CZ3 
845  C CH2 . TRP A 107 ? 0.1923 0.2704 0.2335 -0.0059 -0.0143 0.0098  103  TRP A CH2 
846  N N   . GLY A 108 ? 0.1914 0.2678 0.2109 0.0087  -0.0176 0.0081  104  GLY A N   
847  C CA  . GLY A 108 ? 0.2079 0.2822 0.2225 0.0115  -0.0186 0.0074  104  GLY A CA  
848  C C   . GLY A 108 ? 0.2096 0.2774 0.2210 0.0115  -0.0213 0.0062  104  GLY A C   
849  O O   . GLY A 108 ? 0.2007 0.2666 0.2147 0.0087  -0.0221 0.0062  104  GLY A O   
850  N N   . GLN A 109 ? 0.2156 0.2800 0.2215 0.0146  -0.0227 0.0054  105  GLN A N   
851  C CA  . GLN A 109 ? 0.2272 0.2838 0.2286 0.0149  -0.0257 0.0041  105  GLN A CA  
852  C C   . GLN A 109 ? 0.2233 0.2760 0.2247 0.0123  -0.0258 0.0044  105  GLN A C   
853  O O   . GLN A 109 ? 0.2263 0.2721 0.2245 0.0113  -0.0282 0.0037  105  GLN A O   
854  C CB  . GLN A 109 ? 0.2384 0.2922 0.2329 0.0199  -0.0271 0.0029  105  GLN A CB  
855  C CG  . GLN A 109 ? 0.2506 0.3030 0.2415 0.0225  -0.0268 0.0029  105  GLN A CG  
856  C CD  . GLN A 109 ? 0.2408 0.3015 0.2342 0.0243  -0.0241 0.0039  105  GLN A CD  
857  O OE1 . GLN A 109 ? 0.2277 0.2949 0.2264 0.0224  -0.0220 0.0050  105  GLN A OE1 
858  N NE2 . GLN A 109 ? 0.2423 0.3026 0.2318 0.0280  -0.0242 0.0037  105  GLN A NE2 
859  N N   . GLY A 110 ? 0.2051 0.2618 0.2097 0.0110  -0.0234 0.0055  106  GLY A N   
860  C CA  . GLY A 110 ? 0.2230 0.2760 0.2270 0.0087  -0.0233 0.0059  106  GLY A CA  
861  C C   . GLY A 110 ? 0.2282 0.2779 0.2265 0.0120  -0.0240 0.0056  106  GLY A C   
862  O O   . GLY A 110 ? 0.2291 0.2775 0.2229 0.0162  -0.0253 0.0047  106  GLY A O   
863  N N   . THR A 111 ? 0.2164 0.2653 0.2148 0.0105  -0.0231 0.0064  107  THR A N   
864  C CA  . THR A 111 ? 0.2383 0.2840 0.2313 0.0135  -0.0237 0.0064  107  THR A CA  
865  C C   . THR A 111 ? 0.2375 0.2763 0.2285 0.0104  -0.0242 0.0070  107  THR A C   
866  O O   . THR A 111 ? 0.2206 0.2617 0.2157 0.0067  -0.0224 0.0080  107  THR A O   
867  C CB  . THR A 111 ? 0.2300 0.2831 0.2253 0.0149  -0.0218 0.0070  107  THR A CB  
868  O OG1 . THR A 111 ? 0.2220 0.2817 0.2192 0.0174  -0.0212 0.0067  107  THR A OG1 
869  C CG2 . THR A 111 ? 0.2362 0.2866 0.2266 0.0177  -0.0226 0.0071  107  THR A CG2 
870  N N   . THR A 112 ? 0.2698 0.3001 0.2543 0.0119  -0.0265 0.0065  108  THR A N   
871  C CA  . THR A 112 ? 0.2813 0.3040 0.2627 0.0091  -0.0271 0.0074  108  THR A CA  
872  C C   . THR A 112 ? 0.2857 0.3087 0.2644 0.0111  -0.0263 0.0081  108  THR A C   
873  O O   . THR A 112 ? 0.3166 0.3395 0.2913 0.0160  -0.0273 0.0075  108  THR A O   
874  C CB  . THR A 112 ? 0.3234 0.3355 0.2982 0.0097  -0.0302 0.0066  108  THR A CB  
875  O OG1 . THR A 112 ? 0.3067 0.3200 0.2848 0.0078  -0.0311 0.0058  108  THR A OG1 
876  C CG2 . THR A 112 ? 0.3308 0.3348 0.3023 0.0064  -0.0307 0.0078  108  THR A CG2 
877  N N   . LEU A 113 ? 0.2724 0.2962 0.2532 0.0076  -0.0245 0.0095  109  LEU A N   
878  C CA  . LEU A 113 ? 0.2869 0.3091 0.2639 0.0090  -0.0242 0.0103  109  LEU A CA  
879  C C   . LEU A 113 ? 0.3003 0.3123 0.2721 0.0067  -0.0251 0.0114  109  LEU A C   
880  O O   . LEU A 113 ? 0.3095 0.3204 0.2842 0.0018  -0.0241 0.0122  109  LEU A O   
881  C CB  . LEU A 113 ? 0.2756 0.3057 0.2579 0.0071  -0.0215 0.0110  109  LEU A CB  
882  C CG  . LEU A 113 ? 0.2831 0.3113 0.2616 0.0076  -0.0211 0.0120  109  LEU A CG  
883  C CD1 . LEU A 113 ? 0.2840 0.3129 0.2583 0.0131  -0.0228 0.0114  109  LEU A CD1 
884  C CD2 . LEU A 113 ? 0.2751 0.3099 0.2583 0.0050  -0.0186 0.0125  109  LEU A CD2 
885  N N   . THR A 114 ? 0.3225 0.3274 0.2867 0.0101  -0.0270 0.0114  110  THR A N   
886  C CA  . THR A 114 ? 0.3334 0.3278 0.2914 0.0081  -0.0278 0.0127  110  THR A CA  
887  C C   . THR A 114 ? 0.3357 0.3302 0.2902 0.0102  -0.0271 0.0138  110  THR A C   
888  O O   . THR A 114 ? 0.3466 0.3425 0.2981 0.0155  -0.0283 0.0130  110  THR A O   
889  C CB  . THR A 114 ? 0.3482 0.3318 0.2985 0.0107  -0.0310 0.0119  110  THR A CB  
890  O OG1 . THR A 114 ? 0.3603 0.3450 0.3142 0.0090  -0.0318 0.0107  110  THR A OG1 
891  C CG2 . THR A 114 ? 0.3604 0.3323 0.3041 0.0081  -0.0320 0.0135  110  THR A CG2 
892  N N   . VAL A 115 ? 0.3394 0.3332 0.2945 0.0062  -0.0252 0.0155  111  VAL A N   
893  C CA  . VAL A 115 ? 0.3561 0.3480 0.3065 0.0075  -0.0248 0.0167  111  VAL A CA  
894  C C   . VAL A 115 ? 0.4044 0.3832 0.3461 0.0070  -0.0263 0.0181  111  VAL A C   
895  O O   . VAL A 115 ? 0.4168 0.3913 0.3592 0.0017  -0.0254 0.0194  111  VAL A O   
896  C CB  . VAL A 115 ? 0.3520 0.3505 0.3074 0.0038  -0.0216 0.0177  111  VAL A CB  
897  C CG1 . VAL A 115 ? 0.3697 0.3671 0.3202 0.0055  -0.0214 0.0187  111  VAL A CG1 
898  C CG2 . VAL A 115 ? 0.3365 0.3463 0.3000 0.0039  -0.0203 0.0163  111  VAL A CG2 
899  N N   . SER A 116 ? 0.4531 0.4259 0.3870 0.0122  -0.0286 0.0180  112  SER A N   
900  C CA  . SER A 116 ? 0.5080 0.4675 0.4319 0.0125  -0.0302 0.0196  112  SER A CA  
901  C C   . SER A 116 ? 0.5159 0.4728 0.4398 0.0065  -0.0277 0.0221  112  SER A C   
902  O O   . SER A 116 ? 0.6277 0.5759 0.5490 0.0028  -0.0283 0.0231  112  SER A O   
903  C CB  . SER A 116 ? 0.5203 0.4779 0.4375 0.0188  -0.0318 0.0197  112  SER A CB  
904  O OG  . SER A 116 ? 0.5656 0.5284 0.4838 0.0247  -0.0334 0.0176  112  SER A OG  
905  N N   . GLY A 125 ? 0.5599 0.6496 0.6548 -0.1058 -0.1119 0.0898  121  GLY A N   
906  C CA  . GLY A 125 ? 0.5200 0.6183 0.6034 -0.1064 -0.1046 0.0863  121  GLY A CA  
907  C C   . GLY A 125 ? 0.4813 0.5901 0.5555 -0.1047 -0.0959 0.0809  121  GLY A C   
908  O O   . GLY A 125 ? 0.4108 0.5235 0.4824 -0.1084 -0.0981 0.0835  121  GLY A O   
909  N N   . GLY A 126 ? 0.4110 0.5234 0.4809 -0.0993 -0.0870 0.0738  122  GLY A N   
910  C CA  . GLY A 126 ? 0.3950 0.5168 0.4560 -0.0965 -0.0782 0.0674  122  GLY A CA  
911  C C   . GLY A 126 ? 0.3767 0.4958 0.4415 -0.0910 -0.0752 0.0631  122  GLY A C   
912  O O   . GLY A 126 ? 0.3718 0.4985 0.4283 -0.0914 -0.0711 0.0600  122  GLY A O   
913  N N   . GLY A 127 ? 0.3403 0.4493 0.4170 -0.0863 -0.0776 0.0627  123  GLY A N   
914  C CA  . GLY A 127 ? 0.3067 0.4134 0.3880 -0.0811 -0.0747 0.0587  123  GLY A CA  
915  C C   . GLY A 127 ? 0.3003 0.4060 0.3819 -0.0728 -0.0659 0.0502  123  GLY A C   
916  O O   . GLY A 127 ? 0.2782 0.3831 0.3618 -0.0687 -0.0627 0.0465  123  GLY A O   
917  N N   . GLY A 128 ? 0.2988 0.4045 0.3785 -0.0705 -0.0622 0.0474  124  GLY A N   
918  C CA  . GLY A 128 ? 0.3023 0.4072 0.3817 -0.0633 -0.0542 0.0397  124  GLY A CA  
919  C C   . GLY A 128 ? 0.3149 0.4277 0.3833 -0.0631 -0.0488 0.0358  124  GLY A C   
920  O O   . GLY A 128 ? 0.2956 0.4158 0.3559 -0.0688 -0.0508 0.0387  124  GLY A O   
921  N N   . GLY A 129 ? 0.3082 0.4198 0.3761 -0.0571 -0.0426 0.0294  125  GLY A N   
922  C CA  . GLY A 129 ? 0.3066 0.4244 0.3649 -0.0559 -0.0379 0.0249  125  GLY A CA  
923  C C   . GLY A 129 ? 0.3207 0.4448 0.3721 -0.0569 -0.0353 0.0237  125  GLY A C   
924  O O   . GLY A 129 ? 0.3266 0.4485 0.3811 -0.0576 -0.0363 0.0257  125  GLY A O   
925  N N   . SER A 130 ? 0.3317 0.4633 0.3744 -0.0567 -0.0322 0.0203  126  SER A N   
926  C CA  . SER A 130 ? 0.3361 0.4753 0.3725 -0.0565 -0.0287 0.0178  126  SER A CA  
927  C C   . SER A 130 ? 0.3356 0.4740 0.3697 -0.0501 -0.0233 0.0106  126  SER A C   
928  O O   . SER A 130 ? 0.3461 0.4812 0.3802 -0.0477 -0.0229 0.0081  126  SER A O   
929  C CB  . SER A 130 ? 0.3536 0.5040 0.3820 -0.0621 -0.0301 0.0197  126  SER A CB  
930  O OG  . SER A 130 ? 0.4047 0.5554 0.4350 -0.0688 -0.0359 0.0270  126  SER A OG  
931  N N   . SER A 131 ? 0.3524 0.4939 0.3844 -0.0479 -0.0199 0.0079  127  SER A N   
932  C CA  . SER A 131 ? 0.3393 0.4818 0.3681 -0.0424 -0.0155 0.0013  127  SER A CA  
933  C C   . SER A 131 ? 0.3578 0.5088 0.3794 -0.0428 -0.0149 -0.0017 127  SER A C   
934  O O   . SER A 131 ? 0.3800 0.5395 0.3978 -0.0480 -0.0169 0.0011  127  SER A O   
935  C CB  . SER A 131 ? 0.3451 0.4902 0.3734 -0.0410 -0.0129 0.0002  127  SER A CB  
936  O OG  . SER A 131 ? 0.3346 0.4719 0.3690 -0.0411 -0.0136 0.0028  127  SER A OG  
937  N N   . GLY A 132 ? 0.3407 0.4895 0.3603 -0.0377 -0.0127 -0.0076 128  GLY A N   
938  C CA  . GLY A 132 ? 0.3437 0.5000 0.3566 -0.0363 -0.0117 -0.0126 128  GLY A CA  
939  C C   . GLY A 132 ? 0.3582 0.5250 0.3679 -0.0353 -0.0089 -0.0154 128  GLY A C   
940  O O   . GLY A 132 ? 0.3199 0.4850 0.3326 -0.0332 -0.0071 -0.0154 128  GLY A O   
941  N N   . SER A 133 ? 0.3449 0.5231 0.3487 -0.0365 -0.0084 -0.0183 129  SER A N   
942  C CA  . SER A 133 ? 0.3808 0.5715 0.3817 -0.0351 -0.0055 -0.0220 129  SER A CA  
943  C C   . SER A 133 ? 0.3515 0.5377 0.3538 -0.0273 -0.0032 -0.0286 129  SER A C   
944  O O   . SER A 133 ? 0.3763 0.5697 0.3790 -0.0252 -0.0010 -0.0309 129  SER A O   
945  C CB  . SER A 133 ? 0.4011 0.6053 0.3955 -0.0381 -0.0054 -0.0242 129  SER A CB  
946  O OG  . SER A 133 ? 0.4440 0.6444 0.4354 -0.0342 -0.0056 -0.0302 129  SER A OG  
947  N N   . SER A 134 ? 0.3413 0.5156 0.3449 -0.0236 -0.0043 -0.0309 130  SER A N   
948  C CA  . SER A 134 ? 0.3484 0.5156 0.3532 -0.0168 -0.0035 -0.0366 130  SER A CA  
949  C C   . SER A 134 ? 0.3021 0.4602 0.3121 -0.0155 -0.0029 -0.0338 130  SER A C   
950  O O   . SER A 134 ? 0.3097 0.4637 0.3207 -0.0106 -0.0023 -0.0378 130  SER A O   
951  C CB  . SER A 134 ? 0.4176 0.5762 0.4207 -0.0152 -0.0057 -0.0389 130  SER A CB  
952  O OG  . SER A 134 ? 0.4976 0.6465 0.5024 -0.0098 -0.0062 -0.0427 130  SER A OG  
953  N N   . ASP A 135 ? 0.2516 0.4061 0.2649 -0.0197 -0.0035 -0.0276 1001 ASP A N   
954  C CA  . ASP A 135 ? 0.2260 0.3712 0.2440 -0.0186 -0.0029 -0.0255 1001 ASP A CA  
955  C C   . ASP A 135 ? 0.2116 0.3616 0.2299 -0.0169 -0.0008 -0.0267 1001 ASP A C   
956  O O   . ASP A 135 ? 0.2010 0.3621 0.2175 -0.0188 0.0000  -0.0262 1001 ASP A O   
957  C CB  . ASP A 135 ? 0.2100 0.3511 0.2318 -0.0231 -0.0041 -0.0193 1001 ASP A CB  
958  C CG  . ASP A 135 ? 0.2063 0.3426 0.2292 -0.0249 -0.0064 -0.0175 1001 ASP A CG  
959  O OD1 . ASP A 135 ? 0.2150 0.3491 0.2414 -0.0285 -0.0080 -0.0126 1001 ASP A OD1 
960  O OD2 . ASP A 135 ? 0.1982 0.3328 0.2182 -0.0227 -0.0071 -0.0210 1001 ASP A OD2 
961  N N   . VAL A 136 ? 0.2018 0.3442 0.2224 -0.0140 -0.0001 -0.0279 1002 VAL A N   
962  C CA  . VAL A 136 ? 0.1913 0.3375 0.2125 -0.0128 0.0014  -0.0285 1002 VAL A CA  
963  C C   . VAL A 136 ? 0.1792 0.3265 0.2024 -0.0174 0.0017  -0.0229 1002 VAL A C   
964  O O   . VAL A 136 ? 0.1852 0.3243 0.2111 -0.0195 0.0009  -0.0198 1002 VAL A O   
965  C CB  . VAL A 136 ? 0.1930 0.3303 0.2155 -0.0091 0.0016  -0.0308 1002 VAL A CB  
966  C CG1 . VAL A 136 ? 0.1886 0.3302 0.2116 -0.0082 0.0028  -0.0310 1002 VAL A CG1 
967  C CG2 . VAL A 136 ? 0.2006 0.3346 0.2215 -0.0047 0.0002  -0.0358 1002 VAL A CG2 
968  N N   . VAL A 137 ? 0.1766 0.3336 0.1987 -0.0190 0.0024  -0.0219 1003 VAL A N   
969  C CA  . VAL A 137 ? 0.1841 0.3419 0.2075 -0.0235 0.0021  -0.0168 1003 VAL A CA  
970  C C   . VAL A 137 ? 0.1753 0.3306 0.1998 -0.0216 0.0034  -0.0177 1003 VAL A C   
971  O O   . VAL A 137 ? 0.1704 0.3324 0.1939 -0.0187 0.0045  -0.0209 1003 VAL A O   
972  C CB  . VAL A 137 ? 0.2028 0.3737 0.2239 -0.0280 0.0015  -0.0140 1003 VAL A CB  
973  C CG1 . VAL A 137 ? 0.1992 0.3691 0.2217 -0.0329 0.0002  -0.0084 1003 VAL A CG1 
974  C CG2 . VAL A 137 ? 0.2107 0.3852 0.2299 -0.0303 0.0001  -0.0134 1003 VAL A CG2 
975  N N   . MET A 138 ? 0.1813 0.3279 0.2080 -0.0233 0.0032  -0.0149 1004 MET A N   
976  C CA  . MET A 138 ? 0.1893 0.3329 0.2165 -0.0226 0.0042  -0.0151 1004 MET A CA  
977  C C   . MET A 138 ? 0.2095 0.3565 0.2367 -0.0273 0.0033  -0.0106 1004 MET A C   
978  O O   . MET A 138 ? 0.2293 0.3712 0.2580 -0.0303 0.0018  -0.0074 1004 MET A O   
979  C CB  . MET A 138 ? 0.1860 0.3171 0.2151 -0.0213 0.0047  -0.0159 1004 MET A CB  
980  C CG  . MET A 138 ? 0.1898 0.3166 0.2186 -0.0175 0.0049  -0.0195 1004 MET A CG  
981  S SD  . MET A 138 ? 0.2087 0.3394 0.2356 -0.0131 0.0051  -0.0238 1004 MET A SD  
982  C CE  . MET A 138 ? 0.2147 0.3396 0.2418 -0.0135 0.0058  -0.0232 1004 MET A CE  
983  N N   . THR A 139 ? 0.2146 0.3707 0.2403 -0.0279 0.0037  -0.0103 1005 THR A N   
984  C CA  . THR A 139 ? 0.2091 0.3703 0.2340 -0.0331 0.0023  -0.0056 1005 THR A CA  
985  C C   . THR A 139 ? 0.2122 0.3682 0.2374 -0.0334 0.0027  -0.0049 1005 THR A C   
986  O O   . THR A 139 ? 0.2313 0.3914 0.2560 -0.0309 0.0039  -0.0072 1005 THR A O   
987  C CB  . THR A 139 ? 0.2234 0.4007 0.2465 -0.0348 0.0024  -0.0051 1005 THR A CB  
988  O OG1 . THR A 139 ? 0.2539 0.4350 0.2761 -0.0347 0.0021  -0.0061 1005 THR A OG1 
989  C CG2 . THR A 139 ? 0.2277 0.4099 0.2498 -0.0410 0.0004  0.0005  1005 THR A CG2 
990  N N   . GLN A 140 ? 0.2121 0.3594 0.2380 -0.0365 0.0012  -0.0019 1006 GLN A N   
991  C CA  . GLN A 140 ? 0.2274 0.3709 0.2526 -0.0382 0.0010  -0.0006 1006 GLN A CA  
992  C C   . GLN A 140 ? 0.2732 0.4245 0.2970 -0.0437 -0.0014 0.0042  1006 GLN A C   
993  O O   . GLN A 140 ? 0.2954 0.4439 0.3198 -0.0473 -0.0040 0.0076  1006 GLN A O   
994  C CB  . GLN A 140 ? 0.2227 0.3523 0.2493 -0.0382 0.0008  -0.0011 1006 GLN A CB  
995  C CG  . GLN A 140 ? 0.2186 0.3421 0.2460 -0.0336 0.0033  -0.0056 1006 GLN A CG  
996  C CD  . GLN A 140 ? 0.2104 0.3222 0.2396 -0.0335 0.0038  -0.0068 1006 GLN A CD  
997  O OE1 . GLN A 140 ? 0.2125 0.3204 0.2440 -0.0316 0.0044  -0.0084 1006 GLN A OE1 
998  N NE2 . GLN A 140 ? 0.2083 0.3149 0.2364 -0.0354 0.0037  -0.0063 1006 GLN A NE2 
999  N N   . SER A 141 ? 0.3283 0.4895 0.3507 -0.0445 -0.0009 0.0048  1007 SER A N   
1000 C CA  . SER A 141 ? 0.4032 0.5748 0.4239 -0.0502 -0.0031 0.0098  1007 SER A CA  
1001 C C   . SER A 141 ? 0.3996 0.5621 0.4196 -0.0555 -0.0065 0.0144  1007 SER A C   
1002 O O   . SER A 141 ? 0.4393 0.6064 0.4584 -0.0611 -0.0098 0.0193  1007 SER A O   
1003 C CB  . SER A 141 ? 0.4179 0.6005 0.4381 -0.0493 -0.0017 0.0090  1007 SER A CB  
1004 O OG  . SER A 141 ? 0.5234 0.6967 0.5437 -0.0471 -0.0009 0.0073  1007 SER A OG  
1005 N N   . HIS A 142 ? 0.3415 0.4911 0.3618 -0.0540 -0.0062 0.0128  1008 HIS A N   
1006 C CA  . HIS A 142 ? 0.3282 0.4682 0.3477 -0.0585 -0.0097 0.0162  1008 HIS A CA  
1007 C C   . HIS A 142 ? 0.2979 0.4241 0.3200 -0.0568 -0.0104 0.0144  1008 HIS A C   
1008 O O   . HIS A 142 ? 0.2933 0.4124 0.3164 -0.0524 -0.0074 0.0098  1008 HIS A O   
1009 C CB  . HIS A 142 ? 0.3434 0.4809 0.3608 -0.0589 -0.0091 0.0158  1008 HIS A CB  
1010 C CG  . HIS A 142 ? 0.3829 0.5348 0.3989 -0.0605 -0.0087 0.0177  1008 HIS A CG  
1011 N ND1 . HIS A 142 ? 0.4194 0.5843 0.4349 -0.0648 -0.0106 0.0220  1008 HIS A ND1 
1012 C CD2 . HIS A 142 ? 0.4057 0.5625 0.4212 -0.0585 -0.0067 0.0160  1008 HIS A CD2 
1013 C CE1 . HIS A 142 ? 0.4242 0.6019 0.4392 -0.0651 -0.0095 0.0225  1008 HIS A CE1 
1014 N NE2 . HIS A 142 ? 0.3994 0.5718 0.4147 -0.0611 -0.0074 0.0189  1008 HIS A NE2 
1015 N N   . LYS A 143 ? 0.2735 0.3960 0.2967 -0.0606 -0.0146 0.0181  1009 LYS A N   
1016 C CA  . LYS A 143 ? 0.2941 0.4034 0.3209 -0.0590 -0.0161 0.0165  1009 LYS A CA  
1017 C C   . LYS A 143 ? 0.2550 0.3528 0.2813 -0.0594 -0.0170 0.0152  1009 LYS A C   
1018 O O   . LYS A 143 ? 0.2360 0.3234 0.2653 -0.0562 -0.0161 0.0112  1009 LYS A O   
1019 C CB  . LYS A 143 ? 0.3400 0.4492 0.3687 -0.0632 -0.0214 0.0215  1009 LYS A CB  
1020 C CG  . LYS A 143 ? 0.4270 0.5497 0.4545 -0.0652 -0.0215 0.0243  1009 LYS A CG  
1021 C CD  . LYS A 143 ? 0.5167 0.6513 0.5401 -0.0719 -0.0244 0.0302  1009 LYS A CD  
1022 C CE  . LYS A 143 ? 0.5229 0.6743 0.5440 -0.0711 -0.0206 0.0291  1009 LYS A CE  
1023 N NZ  . LYS A 143 ? 0.5314 0.6872 0.5536 -0.0694 -0.0197 0.0279  1009 LYS A NZ  
1024 N N   . PHE A 144 ? 0.2624 0.3627 0.2850 -0.0636 -0.0189 0.0183  1010 PHE A N   
1025 C CA  . PHE A 144 ? 0.2809 0.3710 0.3018 -0.0648 -0.0201 0.0172  1010 PHE A CA  
1026 C C   . PHE A 144 ? 0.2681 0.3641 0.2847 -0.0657 -0.0179 0.0173  1010 PHE A C   
1027 O O   . PHE A 144 ? 0.2417 0.3495 0.2565 -0.0687 -0.0187 0.0212  1010 PHE A O   
1028 C CB  . PHE A 144 ? 0.3145 0.3989 0.3350 -0.0704 -0.0268 0.0222  1010 PHE A CB  
1029 C CG  . PHE A 144 ? 0.3200 0.3972 0.3455 -0.0696 -0.0301 0.0224  1010 PHE A CG  
1030 C CD1 . PHE A 144 ? 0.3390 0.4034 0.3681 -0.0660 -0.0300 0.0176  1010 PHE A CD1 
1031 C CD2 . PHE A 144 ? 0.3559 0.4401 0.3827 -0.0725 -0.0332 0.0271  1010 PHE A CD2 
1032 C CE1 . PHE A 144 ? 0.3649 0.4230 0.3997 -0.0647 -0.0332 0.0175  1010 PHE A CE1 
1033 C CE2 . PHE A 144 ? 0.3687 0.4461 0.4005 -0.0717 -0.0366 0.0275  1010 PHE A CE2 
1034 C CZ  . PHE A 144 ? 0.3599 0.4242 0.3962 -0.0676 -0.0367 0.0227  1010 PHE A CZ  
1035 N N   . MET A 145 ? 0.2661 0.3542 0.2811 -0.0638 -0.0156 0.0133  1011 MET A N   
1036 C CA  . MET A 145 ? 0.2894 0.3815 0.3003 -0.0651 -0.0143 0.0137  1011 MET A CA  
1037 C C   . MET A 145 ? 0.2863 0.3663 0.2944 -0.0671 -0.0157 0.0121  1011 MET A C   
1038 O O   . MET A 145 ? 0.2688 0.3384 0.2785 -0.0645 -0.0147 0.0078  1011 MET A O   
1039 C CB  . MET A 145 ? 0.3088 0.4054 0.3200 -0.0603 -0.0092 0.0096  1011 MET A CB  
1040 C CG  . MET A 145 ? 0.3681 0.4715 0.3764 -0.0611 -0.0081 0.0105  1011 MET A CG  
1041 S SD  . MET A 145 ? 0.4349 0.5427 0.4448 -0.0548 -0.0033 0.0058  1011 MET A SD  
1042 C CE  . MET A 145 ? 0.3113 0.4275 0.3252 -0.0523 -0.0030 0.0062  1011 MET A CE  
1043 N N   . SER A 146 ? 0.2781 0.3603 0.2821 -0.0716 -0.0179 0.0156  1012 SER A N   
1044 C CA  . SER A 146 ? 0.3204 0.3919 0.3205 -0.0743 -0.0198 0.0146  1012 SER A CA  
1045 C C   . SER A 146 ? 0.3063 0.3799 0.3027 -0.0736 -0.0164 0.0126  1012 SER A C   
1046 O O   . SER A 146 ? 0.2889 0.3744 0.2855 -0.0734 -0.0152 0.0149  1012 SER A O   
1047 C CB  . SER A 146 ? 0.3537 0.4256 0.3514 -0.0808 -0.0257 0.0208  1012 SER A CB  
1048 O OG  . SER A 146 ? 0.4325 0.4947 0.4323 -0.0817 -0.0299 0.0210  1012 SER A OG  
1049 N N   . THR A 147 ? 0.3066 0.3699 0.3001 -0.0733 -0.0151 0.0083  1013 THR A N   
1050 C CA  . THR A 147 ? 0.3194 0.3836 0.3084 -0.0741 -0.0129 0.0072  1013 THR A CA  
1051 C C   . THR A 147 ? 0.3103 0.3629 0.2940 -0.0775 -0.0146 0.0054  1013 THR A C   
1052 O O   . THR A 147 ? 0.3363 0.3793 0.3206 -0.0779 -0.0168 0.0035  1013 THR A O   
1053 C CB  . THR A 147 ? 0.3438 0.4058 0.3326 -0.0700 -0.0079 0.0017  1013 THR A CB  
1054 O OG1 . THR A 147 ? 0.3891 0.4476 0.3821 -0.0658 -0.0054 -0.0024 1013 THR A OG1 
1055 C CG2 . THR A 147 ? 0.3242 0.3952 0.3124 -0.0692 -0.0062 0.0030  1013 THR A CG2 
1056 N N   . SER A 148 ? 0.3062 0.3592 0.2851 -0.0794 -0.0135 0.0052  1014 SER A N   
1057 C CA  . SER A 148 ? 0.3045 0.3468 0.2773 -0.0825 -0.0140 0.0022  1014 SER A CA  
1058 C C   . SER A 148 ? 0.2956 0.3364 0.2663 -0.0801 -0.0091 -0.0028 1014 SER A C   
1059 O O   . SER A 148 ? 0.2877 0.3367 0.2598 -0.0783 -0.0069 -0.0016 1014 SER A O   
1060 C CB  . SER A 148 ? 0.3182 0.3623 0.2862 -0.0882 -0.0178 0.0072  1014 SER A CB  
1061 O OG  . SER A 148 ? 0.3421 0.3899 0.3122 -0.0909 -0.0223 0.0128  1014 SER A OG  
1062 N N   . VAL A 149 ? 0.3085 0.3396 0.2760 -0.0804 -0.0075 -0.0085 1015 VAL A N   
1063 C CA  . VAL A 149 ? 0.3151 0.3453 0.2792 -0.0798 -0.0030 -0.0130 1015 VAL A CA  
1064 C C   . VAL A 149 ? 0.3101 0.3458 0.2698 -0.0830 -0.0037 -0.0089 1015 VAL A C   
1065 O O   . VAL A 149 ? 0.3208 0.3558 0.2764 -0.0876 -0.0073 -0.0050 1015 VAL A O   
1066 C CB  . VAL A 149 ? 0.3376 0.3574 0.2974 -0.0810 -0.0017 -0.0196 1015 VAL A CB  
1067 C CG1 . VAL A 149 ? 0.3495 0.3694 0.3041 -0.0822 0.0023  -0.0233 1015 VAL A CG1 
1068 C CG2 . VAL A 149 ? 0.3363 0.3516 0.3022 -0.0765 -0.0007 -0.0244 1015 VAL A CG2 
1069 N N   . GLY A 150 ? 0.2988 0.3397 0.2596 -0.0809 -0.0008 -0.0095 1016 GLY A N   
1070 C CA  . GLY A 150 ? 0.2993 0.3451 0.2570 -0.0832 -0.0016 -0.0061 1016 GLY A CA  
1071 C C   . GLY A 150 ? 0.2928 0.3489 0.2561 -0.0808 -0.0034 -0.0011 1016 GLY A C   
1072 O O   . GLY A 150 ? 0.2789 0.3396 0.2418 -0.0810 -0.0040 0.0009  1016 GLY A O   
1073 N N   . ASP A 151 ? 0.2847 0.3448 0.2535 -0.0784 -0.0045 0.0004  1017 ASP A N   
1074 C CA  . ASP A 151 ? 0.3013 0.3728 0.2755 -0.0760 -0.0057 0.0045  1017 ASP A CA  
1075 C C   . ASP A 151 ? 0.2891 0.3645 0.2678 -0.0706 -0.0030 0.0021  1017 ASP A C   
1076 O O   . ASP A 151 ? 0.2751 0.3445 0.2534 -0.0688 -0.0001 -0.0022 1017 ASP A O   
1077 C CB  . ASP A 151 ? 0.3335 0.4082 0.3109 -0.0763 -0.0079 0.0072  1017 ASP A CB  
1078 C CG  . ASP A 151 ? 0.3892 0.4632 0.3628 -0.0821 -0.0119 0.0114  1017 ASP A CG  
1079 O OD1 . ASP A 151 ? 0.3748 0.4465 0.3436 -0.0854 -0.0127 0.0122  1017 ASP A OD1 
1080 O OD2 . ASP A 151 ? 0.4453 0.5203 0.4203 -0.0837 -0.0144 0.0140  1017 ASP A OD2 
1081 N N   . ARG A 152 ? 0.2895 0.3750 0.2725 -0.0680 -0.0039 0.0046  1018 ARG A N   
1082 C CA  . ARG A 152 ? 0.2849 0.3744 0.2727 -0.0625 -0.0020 0.0024  1018 ARG A CA  
1083 C C   . ARG A 152 ? 0.2818 0.3757 0.2741 -0.0601 -0.0016 0.0026  1018 ARG A C   
1084 O O   . ARG A 152 ? 0.2787 0.3795 0.2725 -0.0617 -0.0036 0.0061  1018 ARG A O   
1085 C CB  . ARG A 152 ? 0.3244 0.4217 0.3146 -0.0605 -0.0035 0.0041  1018 ARG A CB  
1086 C CG  . ARG A 152 ? 0.3604 0.4616 0.3554 -0.0548 -0.0023 0.0018  1018 ARG A CG  
1087 C CD  . ARG A 152 ? 0.4410 0.5460 0.4377 -0.0527 -0.0043 0.0023  1018 ARG A CD  
1088 N NE  . ARG A 152 ? 0.5216 0.6172 0.5129 -0.0560 -0.0045 0.0017  1018 ARG A NE  
1089 C CZ  . ARG A 152 ? 0.5791 0.6738 0.5678 -0.0590 -0.0071 0.0040  1018 ARG A CZ  
1090 N NH1 . ARG A 152 ? 0.6592 0.7622 0.6512 -0.0583 -0.0099 0.0069  1018 ARG A NH1 
1091 N NH2 . ARG A 152 ? 0.5859 0.6720 0.5687 -0.0628 -0.0069 0.0034  1018 ARG A NH2 
1092 N N   . VAL A 153 ? 0.2386 0.3296 0.2332 -0.0567 0.0006  -0.0006 1019 VAL A N   
1093 C CA  . VAL A 153 ? 0.2501 0.3446 0.2490 -0.0544 0.0009  -0.0006 1019 VAL A CA  
1094 C C   . VAL A 153 ? 0.2246 0.3259 0.2274 -0.0495 0.0020  -0.0018 1019 VAL A C   
1095 O O   . VAL A 153 ? 0.2071 0.3046 0.2093 -0.0477 0.0032  -0.0043 1019 VAL A O   
1096 C CB  . VAL A 153 ? 0.2658 0.3508 0.2645 -0.0543 0.0025  -0.0036 1019 VAL A CB  
1097 C CG1 . VAL A 153 ? 0.2696 0.3574 0.2732 -0.0515 0.0028  -0.0040 1019 VAL A CG1 
1098 C CG2 . VAL A 153 ? 0.2837 0.3619 0.2791 -0.0587 0.0008  -0.0028 1019 VAL A CG2 
1099 N N   . SER A 154 ? 0.2152 0.3265 0.2215 -0.0479 0.0012  -0.0002 1020 SER A N   
1100 C CA  . SER A 154 ? 0.2143 0.3318 0.2243 -0.0429 0.0021  -0.0022 1020 SER A CA  
1101 C C   . SER A 154 ? 0.1953 0.3151 0.2078 -0.0422 0.0026  -0.0021 1020 SER A C   
1102 O O   . SER A 154 ? 0.2025 0.3281 0.2154 -0.0448 0.0012  0.0008  1020 SER A O   
1103 C CB  . SER A 154 ? 0.2516 0.3808 0.2639 -0.0412 0.0009  -0.0011 1020 SER A CB  
1104 O OG  . SER A 154 ? 0.3305 0.4572 0.3410 -0.0421 -0.0001 -0.0006 1020 SER A OG  
1105 N N   . ILE A 155 ? 0.1825 0.2981 0.1965 -0.0391 0.0041  -0.0050 1021 ILE A N   
1106 C CA  . ILE A 155 ? 0.1798 0.2967 0.1961 -0.0385 0.0043  -0.0049 1021 ILE A CA  
1107 C C   . ILE A 155 ? 0.1789 0.3024 0.1975 -0.0340 0.0050  -0.0071 1021 ILE A C   
1108 O O   . ILE A 155 ? 0.1647 0.2837 0.1834 -0.0311 0.0059  -0.0100 1021 ILE A O   
1109 C CB  . ILE A 155 ? 0.2006 0.3067 0.2172 -0.0388 0.0053  -0.0067 1021 ILE A CB  
1110 C CG1 . ILE A 155 ? 0.2204 0.3198 0.2349 -0.0428 0.0043  -0.0054 1021 ILE A CG1 
1111 C CG2 . ILE A 155 ? 0.2056 0.3135 0.2253 -0.0377 0.0050  -0.0065 1021 ILE A CG2 
1112 C CD1 . ILE A 155 ? 0.2278 0.3173 0.2430 -0.0425 0.0056  -0.0082 1021 ILE A CD1 
1113 N N   . THR A 156 ? 0.1798 0.3134 0.2000 -0.0338 0.0044  -0.0059 1022 THR A N   
1114 C CA  . THR A 156 ? 0.1870 0.3278 0.2090 -0.0294 0.0049  -0.0086 1022 THR A CA  
1115 C C   . THR A 156 ? 0.2006 0.3419 0.2238 -0.0287 0.0053  -0.0092 1022 THR A C   
1116 O O   . THR A 156 ? 0.2098 0.3507 0.2329 -0.0322 0.0044  -0.0063 1022 THR A O   
1117 C CB  . THR A 156 ? 0.2162 0.3709 0.2391 -0.0290 0.0044  -0.0079 1022 THR A CB  
1118 O OG1 . THR A 156 ? 0.3209 0.4806 0.3431 -0.0338 0.0035  -0.0039 1022 THR A OG1 
1119 C CG2 . THR A 156 ? 0.1906 0.3447 0.2132 -0.0287 0.0037  -0.0078 1022 THR A CG2 
1120 N N   . CYS A 157 ? 0.2183 0.3604 0.2425 -0.0244 0.0059  -0.0127 1023 CYS A N   
1121 C CA  . CYS A 157 ? 0.2267 0.3688 0.2517 -0.0232 0.0061  -0.0137 1023 CYS A CA  
1122 C C   . CYS A 157 ? 0.2216 0.3731 0.2473 -0.0192 0.0062  -0.0170 1023 CYS A C   
1123 O O   . CYS A 157 ? 0.2125 0.3630 0.2386 -0.0156 0.0059  -0.0198 1023 CYS A O   
1124 C CB  . CYS A 157 ? 0.2870 0.4170 0.3124 -0.0223 0.0066  -0.0152 1023 CYS A CB  
1125 S SG  . CYS A 157 ? 0.4368 0.5671 0.4636 -0.0217 0.0064  -0.0156 1023 CYS A SG  
1126 N N   . LYS A 158 ? 0.2161 0.3773 0.2417 -0.0201 0.0061  -0.0165 1024 LYS A N   
1127 C CA  . LYS A 158 ? 0.2260 0.3967 0.2520 -0.0161 0.0065  -0.0206 1024 LYS A CA  
1128 C C   . LYS A 158 ? 0.2174 0.3843 0.2429 -0.0151 0.0064  -0.0222 1024 LYS A C   
1129 O O   . LYS A 158 ? 0.2092 0.3755 0.2341 -0.0190 0.0060  -0.0190 1024 LYS A O   
1130 C CB  . LYS A 158 ? 0.2717 0.4587 0.2974 -0.0183 0.0069  -0.0193 1024 LYS A CB  
1131 C CG  . LYS A 158 ? 0.3221 0.5208 0.3488 -0.0136 0.0076  -0.0246 1024 LYS A CG  
1132 C CD  . LYS A 158 ? 0.3805 0.5943 0.4086 -0.0139 0.0082  -0.0245 1024 LYS A CD  
1133 C CE  . LYS A 158 ? 0.4164 0.6432 0.4465 -0.0084 0.0091  -0.0307 1024 LYS A CE  
1134 N NZ  . LYS A 158 ? 0.4287 0.6486 0.4616 -0.0016 0.0081  -0.0356 1024 LYS A NZ  
1135 N N   . ALA A 159 ? 0.1871 0.3521 0.2129 -0.0101 0.0061  -0.0269 1025 ALA A N   
1136 C CA  . ALA A 159 ? 0.1877 0.3494 0.2126 -0.0088 0.0057  -0.0290 1025 ALA A CA  
1137 C C   . ALA A 159 ? 0.1858 0.3612 0.2096 -0.0076 0.0061  -0.0318 1025 ALA A C   
1138 O O   . ALA A 159 ? 0.1934 0.3776 0.2182 -0.0046 0.0066  -0.0348 1025 ALA A O   
1139 C CB  . ALA A 159 ? 0.1822 0.3337 0.2074 -0.0045 0.0046  -0.0325 1025 ALA A CB  
1140 N N   . SER A 160 ? 0.1752 0.3521 0.1973 -0.0096 0.0059  -0.0312 1026 SER A N   
1141 C CA  . SER A 160 ? 0.1974 0.3877 0.2176 -0.0092 0.0064  -0.0341 1026 SER A CA  
1142 C C   . SER A 160 ? 0.2013 0.3908 0.2213 -0.0027 0.0060  -0.0412 1026 SER A C   
1143 O O   . SER A 160 ? 0.2062 0.4075 0.2248 -0.0011 0.0068  -0.0452 1026 SER A O   
1144 C CB  . SER A 160 ? 0.1943 0.3853 0.2123 -0.0142 0.0057  -0.0305 1026 SER A CB  
1145 O OG  . SER A 160 ? 0.1782 0.3568 0.1963 -0.0130 0.0045  -0.0311 1026 SER A OG  
1146 N N   . GLN A 161 ? 0.2063 0.3824 0.2274 0.0007  0.0046  -0.0430 1027 GLN A N   
1147 C CA  . GLN A 161 ? 0.2303 0.4039 0.2515 0.0071  0.0031  -0.0497 1027 GLN A CA  
1148 C C   . GLN A 161 ? 0.2080 0.3699 0.2314 0.0099  0.0014  -0.0499 1027 GLN A C   
1149 O O   . GLN A 161 ? 0.1833 0.3385 0.2073 0.0063  0.0018  -0.0449 1027 GLN A O   
1150 C CB  . GLN A 161 ? 0.2772 0.4453 0.2958 0.0079  0.0017  -0.0521 1027 GLN A CB  
1151 C CG  . GLN A 161 ? 0.3051 0.4642 0.3229 0.0031  0.0013  -0.0468 1027 GLN A CG  
1152 C CD  . GLN A 161 ? 0.3250 0.4838 0.3398 0.0027  0.0002  -0.0487 1027 GLN A CD  
1153 O OE1 . GLN A 161 ? 0.3375 0.4901 0.3512 0.0064  -0.0017 -0.0530 1027 GLN A OE1 
1154 N NE2 . GLN A 161 ? 0.3137 0.4777 0.3271 -0.0023 0.0008  -0.0448 1027 GLN A NE2 
1155 N N   . ASP A 162 ? 0.1998 0.3599 0.2242 0.0157  -0.0006 -0.0556 1028 ASP A N   
1156 C CA  . ASP A 162 ? 0.2086 0.3570 0.2348 0.0183  -0.0033 -0.0559 1028 ASP A CA  
1157 C C   . ASP A 162 ? 0.2010 0.3350 0.2254 0.0151  -0.0045 -0.0522 1028 ASP A C   
1158 O O   . ASP A 162 ? 0.2009 0.3301 0.2235 0.0158  -0.0059 -0.0540 1028 ASP A O   
1159 C CB  . ASP A 162 ? 0.2315 0.3793 0.2590 0.0253  -0.0065 -0.0629 1028 ASP A CB  
1160 C CG  . ASP A 162 ? 0.2622 0.3989 0.2917 0.0279  -0.0103 -0.0632 1028 ASP A CG  
1161 O OD1 . ASP A 162 ? 0.2440 0.3735 0.2733 0.0240  -0.0102 -0.0580 1028 ASP A OD1 
1162 O OD2 . ASP A 162 ? 0.3040 0.4399 0.3355 0.0341  -0.0137 -0.0691 1028 ASP A OD2 
1163 N N   . VAL A 163 ? 0.1837 0.3116 0.2087 0.0117  -0.0039 -0.0476 1029 VAL A N   
1164 C CA  . VAL A 163 ? 0.1754 0.2910 0.1994 0.0085  -0.0047 -0.0444 1029 VAL A CA  
1165 C C   . VAL A 163 ? 0.1737 0.2800 0.1980 0.0097  -0.0075 -0.0445 1029 VAL A C   
1166 O O   . VAL A 163 ? 0.1755 0.2731 0.1989 0.0062  -0.0076 -0.0413 1029 VAL A O   
1167 C CB  . VAL A 163 ? 0.1643 0.2805 0.1885 0.0032  -0.0016 -0.0393 1029 VAL A CB  
1168 C CG1 . VAL A 163 ? 0.1662 0.2893 0.1899 0.0014  -0.0001 -0.0385 1029 VAL A CG1 
1169 C CG2 . VAL A 163 ? 0.1575 0.2779 0.1827 0.0017  -0.0001 -0.0371 1029 VAL A CG2 
1170 N N   . GLY A 164 ? 0.1601 0.2686 0.1858 0.0141  -0.0098 -0.0479 1030 GLY A N   
1171 C CA  . GLY A 164 ? 0.1647 0.2638 0.1907 0.0150  -0.0137 -0.0477 1030 GLY A CA  
1172 C C   . GLY A 164 ? 0.1595 0.2567 0.1852 0.0104  -0.0119 -0.0429 1030 GLY A C   
1173 O O   . GLY A 164 ? 0.1471 0.2530 0.1741 0.0098  -0.0094 -0.0419 1030 GLY A O   
1174 N N   . THR A 165 ? 0.1561 0.2431 0.1799 0.0067  -0.0131 -0.0399 1031 THR A N   
1175 C CA  . THR A 165 ? 0.1584 0.2435 0.1812 0.0018  -0.0110 -0.0358 1031 THR A CA  
1176 C C   . THR A 165 ? 0.1557 0.2370 0.1770 -0.0026 -0.0082 -0.0332 1031 THR A C   
1177 O O   . THR A 165 ? 0.1540 0.2322 0.1741 -0.0067 -0.0067 -0.0305 1031 THR A O   
1178 C CB  . THR A 165 ? 0.1710 0.2492 0.1930 0.0013  -0.0150 -0.0348 1031 THR A CB  
1179 O OG1 . THR A 165 ? 0.1752 0.2442 0.1957 0.0013  -0.0189 -0.0353 1031 THR A OG1 
1180 C CG2 . THR A 165 ? 0.1802 0.2635 0.2050 0.0059  -0.0175 -0.0372 1031 THR A CG2 
1181 N N   . ALA A 166 ? 0.1652 0.2480 0.1870 -0.0019 -0.0072 -0.0342 1032 ALA A N   
1182 C CA  . ALA A 166 ? 0.1640 0.2438 0.1858 -0.0056 -0.0049 -0.0320 1032 ALA A CA  
1183 C C   . ALA A 166 ? 0.1548 0.2406 0.1780 -0.0076 -0.0009 -0.0303 1032 ALA A C   
1184 O O   . ALA A 166 ? 0.1459 0.2354 0.1704 -0.0076 0.0003  -0.0301 1032 ALA A O   
1185 C CB  . ALA A 166 ? 0.1748 0.2520 0.1964 -0.0041 -0.0069 -0.0335 1032 ALA A CB  
1186 N N   . VAL A 167 ? 0.1541 0.2401 0.1768 -0.0098 0.0005  -0.0287 1033 VAL A N   
1187 C CA  . VAL A 167 ? 0.1530 0.2435 0.1768 -0.0120 0.0035  -0.0269 1033 VAL A CA  
1188 C C   . VAL A 167 ? 0.1545 0.2399 0.1774 -0.0157 0.0052  -0.0254 1033 VAL A C   
1189 O O   . VAL A 167 ? 0.1520 0.2335 0.1727 -0.0168 0.0041  -0.0252 1033 VAL A O   
1190 C CB  . VAL A 167 ? 0.1623 0.2602 0.1862 -0.0107 0.0035  -0.0269 1033 VAL A CB  
1191 C CG1 . VAL A 167 ? 0.1696 0.2699 0.1938 -0.0139 0.0057  -0.0245 1033 VAL A CG1 
1192 C CG2 . VAL A 167 ? 0.1695 0.2744 0.1944 -0.0077 0.0028  -0.0287 1033 VAL A CG2 
1193 N N   . ALA A 168 ? 0.1393 0.2251 0.1641 -0.0177 0.0076  -0.0244 1034 ALA A N   
1194 C CA  . ALA A 168 ? 0.1356 0.2179 0.1601 -0.0209 0.0098  -0.0239 1034 ALA A CA  
1195 C C   . ALA A 168 ? 0.1327 0.2176 0.1578 -0.0222 0.0111  -0.0228 1034 ALA A C   
1196 O O   . ALA A 168 ? 0.1425 0.2318 0.1694 -0.0211 0.0106  -0.0220 1034 ALA A O   
1197 C CB  . ALA A 168 ? 0.1382 0.2179 0.1650 -0.0217 0.0109  -0.0244 1034 ALA A CB  
1198 N N   . TRP A 169 ? 0.1339 0.2159 0.1575 -0.0248 0.0127  -0.0228 1035 TRP A N   
1199 C CA  . TRP A 169 ? 0.1451 0.2274 0.1693 -0.0266 0.0137  -0.0221 1035 TRP A CA  
1200 C C   . TRP A 169 ? 0.1572 0.2355 0.1830 -0.0282 0.0161  -0.0237 1035 TRP A C   
1201 O O   . TRP A 169 ? 0.1658 0.2416 0.1896 -0.0297 0.0174  -0.0250 1035 TRP A O   
1202 C CB  . TRP A 169 ? 0.1431 0.2260 0.1637 -0.0282 0.0131  -0.0211 1035 TRP A CB  
1203 C CG  . TRP A 169 ? 0.1446 0.2333 0.1649 -0.0263 0.0110  -0.0198 1035 TRP A CG  
1204 C CD1 . TRP A 169 ? 0.1465 0.2369 0.1657 -0.0244 0.0094  -0.0202 1035 TRP A CD1 
1205 C CD2 . TRP A 169 ? 0.1418 0.2363 0.1634 -0.0263 0.0102  -0.0180 1035 TRP A CD2 
1206 N NE1 . TRP A 169 ? 0.1420 0.2395 0.1620 -0.0227 0.0081  -0.0195 1035 TRP A NE1 
1207 C CE2 . TRP A 169 ? 0.1419 0.2425 0.1630 -0.0242 0.0087  -0.0179 1035 TRP A CE2 
1208 C CE3 . TRP A 169 ? 0.1424 0.2372 0.1654 -0.0282 0.0102  -0.0165 1035 TRP A CE3 
1209 C CZ2 . TRP A 169 ? 0.1376 0.2463 0.1595 -0.0243 0.0079  -0.0163 1035 TRP A CZ2 
1210 C CZ3 . TRP A 169 ? 0.1478 0.2495 0.1711 -0.0288 0.0088  -0.0142 1035 TRP A CZ3 
1211 C CH2 . TRP A 169 ? 0.1341 0.2433 0.1567 -0.0271 0.0080  -0.0141 1035 TRP A CH2 
1212 N N   . TYR A 170 ? 0.1608 0.2391 0.1902 -0.0281 0.0162  -0.0235 1036 TYR A N   
1213 C CA  . TYR A 170 ? 0.1638 0.2388 0.1963 -0.0289 0.0181  -0.0256 1036 TYR A CA  
1214 C C   . TYR A 170 ? 0.1651 0.2380 0.1970 -0.0304 0.0175  -0.0254 1036 TYR A C   
1215 O O   . TYR A 170 ? 0.1721 0.2468 0.2033 -0.0308 0.0152  -0.0227 1036 TYR A O   
1216 C CB  . TYR A 170 ? 0.1528 0.2287 0.1913 -0.0270 0.0175  -0.0256 1036 TYR A CB  
1217 C CG  . TYR A 170 ? 0.1465 0.2234 0.1857 -0.0260 0.0181  -0.0262 1036 TYR A CG  
1218 C CD1 . TYR A 170 ? 0.1471 0.2231 0.1879 -0.0266 0.0206  -0.0286 1036 TYR A CD1 
1219 C CD2 . TYR A 170 ? 0.1514 0.2308 0.1899 -0.0245 0.0162  -0.0245 1036 TYR A CD2 
1220 C CE1 . TYR A 170 ? 0.1429 0.2200 0.1844 -0.0263 0.0206  -0.0286 1036 TYR A CE1 
1221 C CE2 . TYR A 170 ? 0.1525 0.2319 0.1913 -0.0238 0.0161  -0.0250 1036 TYR A CE2 
1222 C CZ  . TYR A 170 ? 0.1469 0.2250 0.1873 -0.0250 0.0182  -0.0267 1036 TYR A CZ  
1223 O OH  . TYR A 170 ? 0.1622 0.2403 0.2024 -0.0250 0.0176  -0.0266 1036 TYR A OH  
1224 N N   . GLN A 171 ? 0.1725 0.2419 0.2042 -0.0316 0.0196  -0.0283 1037 GLN A N   
1225 C CA  . GLN A 171 ? 0.1949 0.2605 0.2273 -0.0327 0.0190  -0.0292 1037 GLN A CA  
1226 C C   . GLN A 171 ? 0.2046 0.2683 0.2442 -0.0306 0.0192  -0.0316 1037 GLN A C   
1227 O O   . GLN A 171 ? 0.1855 0.2506 0.2280 -0.0294 0.0217  -0.0342 1037 GLN A O   
1228 C CB  . GLN A 171 ? 0.2149 0.2779 0.2425 -0.0350 0.0215  -0.0322 1037 GLN A CB  
1229 C CG  . GLN A 171 ? 0.2234 0.2816 0.2500 -0.0365 0.0206  -0.0335 1037 GLN A CG  
1230 C CD  . GLN A 171 ? 0.2464 0.3025 0.2674 -0.0391 0.0232  -0.0366 1037 GLN A CD  
1231 O OE1 . GLN A 171 ? 0.3010 0.3555 0.3162 -0.0419 0.0221  -0.0352 1037 GLN A OE1 
1232 N NE2 . GLN A 171 ? 0.2338 0.2906 0.2563 -0.0387 0.0267  -0.0410 1037 GLN A NE2 
1233 N N   . GLN A 172 ? 0.2294 0.2902 0.2722 -0.0305 0.0163  -0.0305 1038 GLN A N   
1234 C CA  . GLN A 172 ? 0.2553 0.3130 0.3056 -0.0284 0.0159  -0.0334 1038 GLN A CA  
1235 C C   . GLN A 172 ? 0.2668 0.3181 0.3174 -0.0292 0.0136  -0.0346 1038 GLN A C   
1236 O O   . GLN A 172 ? 0.2693 0.3193 0.3176 -0.0312 0.0099  -0.0306 1038 GLN A O   
1237 C CB  . GLN A 172 ? 0.2541 0.3135 0.3105 -0.0266 0.0132  -0.0307 1038 GLN A CB  
1238 C CG  . GLN A 172 ? 0.2533 0.3109 0.3184 -0.0239 0.0136  -0.0343 1038 GLN A CG  
1239 C CD  . GLN A 172 ? 0.2694 0.3280 0.3406 -0.0227 0.0100  -0.0310 1038 GLN A CD  
1240 O OE1 . GLN A 172 ? 0.2979 0.3563 0.3771 -0.0203 0.0098  -0.0329 1038 GLN A OE1 
1241 N NE2 . GLN A 172 ? 0.2616 0.3222 0.3294 -0.0245 0.0072  -0.0259 1038 GLN A NE2 
1242 N N   . LYS A 173 ? 0.3008 0.3490 0.3547 -0.0278 0.0156  -0.0403 1039 LYS A N   
1243 C CA  . LYS A 173 ? 0.3256 0.3665 0.3813 -0.0276 0.0131  -0.0429 1039 LYS A CA  
1244 C C   . LYS A 173 ? 0.3507 0.3890 0.4168 -0.0243 0.0101  -0.0440 1039 LYS A C   
1245 O O   . LYS A 173 ? 0.3072 0.3496 0.3793 -0.0218 0.0118  -0.0451 1039 LYS A O   
1246 C CB  . LYS A 173 ? 0.3382 0.3776 0.3902 -0.0282 0.0173  -0.0491 1039 LYS A CB  
1247 C CG  . LYS A 173 ? 0.3355 0.3773 0.3775 -0.0319 0.0194  -0.0472 1039 LYS A CG  
1248 C CD  . LYS A 173 ? 0.3617 0.4003 0.3985 -0.0337 0.0220  -0.0524 1039 LYS A CD  
1249 C CE  . LYS A 173 ? 0.3731 0.4149 0.4007 -0.0375 0.0242  -0.0504 1039 LYS A CE  
1250 N NZ  . LYS A 173 ? 0.3883 0.4273 0.4101 -0.0399 0.0267  -0.0553 1039 LYS A NZ  
1251 N N   . PRO A 174 ? 0.3952 0.4260 0.4640 -0.0243 0.0051  -0.0438 1040 PRO A N   
1252 C CA  . PRO A 174 ? 0.3966 0.4240 0.4757 -0.0212 0.0009  -0.0442 1040 PRO A CA  
1253 C C   . PRO A 174 ? 0.3775 0.4070 0.4646 -0.0167 0.0050  -0.0516 1040 PRO A C   
1254 O O   . PRO A 174 ? 0.3907 0.4205 0.4757 -0.0160 0.0095  -0.0579 1040 PRO A O   
1255 C CB  . PRO A 174 ? 0.4398 0.4575 0.5184 -0.0227 -0.0049 -0.0437 1040 PRO A CB  
1256 C CG  . PRO A 174 ? 0.4236 0.4423 0.4911 -0.0276 -0.0049 -0.0392 1040 PRO A CG  
1257 C CD  . PRO A 174 ? 0.4268 0.4519 0.4889 -0.0275 0.0024  -0.0427 1040 PRO A CD  
1258 N N   . GLY A 175 ? 0.3834 0.4157 0.4791 -0.0141 0.0037  -0.0505 1041 GLY A N   
1259 C CA  . GLY A 175 ? 0.3902 0.4264 0.4952 -0.0098 0.0071  -0.0565 1041 GLY A CA  
1260 C C   . GLY A 175 ? 0.4011 0.4461 0.5022 -0.0103 0.0146  -0.0592 1041 GLY A C   
1261 O O   . GLY A 175 ? 0.4190 0.4687 0.5272 -0.0072 0.0183  -0.0649 1041 GLY A O   
1262 N N   . GLN A 176 ? 0.3372 0.3850 0.4279 -0.0141 0.0167  -0.0554 1042 GLN A N   
1263 C CA  . GLN A 176 ? 0.3327 0.3879 0.4188 -0.0154 0.0228  -0.0572 1042 GLN A CA  
1264 C C   . GLN A 176 ? 0.2839 0.3434 0.3680 -0.0167 0.0221  -0.0511 1042 GLN A C   
1265 O O   . GLN A 176 ? 0.3011 0.3583 0.3845 -0.0174 0.0176  -0.0457 1042 GLN A O   
1266 C CB  . GLN A 176 ? 0.3259 0.3801 0.4016 -0.0187 0.0257  -0.0588 1042 GLN A CB  
1267 C CG  . GLN A 176 ? 0.3946 0.4445 0.4710 -0.0177 0.0269  -0.0658 1042 GLN A CG  
1268 C CD  . GLN A 176 ? 0.4260 0.4758 0.4915 -0.0216 0.0300  -0.0672 1042 GLN A CD  
1269 O OE1 . GLN A 176 ? 0.5349 0.5804 0.5983 -0.0218 0.0306  -0.0721 1042 GLN A OE1 
1270 N NE2 . GLN A 176 ? 0.4450 0.4987 0.5030 -0.0249 0.0316  -0.0629 1042 GLN A NE2 
1271 N N   . SER A 177 ? 0.2447 0.3105 0.3272 -0.0174 0.0261  -0.0519 1043 SER A N   
1272 C CA  . SER A 177 ? 0.2521 0.3214 0.3325 -0.0184 0.0252  -0.0467 1043 SER A CA  
1273 C C   . SER A 177 ? 0.2347 0.3033 0.3043 -0.0215 0.0253  -0.0436 1043 SER A C   
1274 O O   . SER A 177 ? 0.2179 0.2847 0.2818 -0.0233 0.0270  -0.0456 1043 SER A O   
1275 C CB  . SER A 177 ? 0.2810 0.3566 0.3654 -0.0178 0.0286  -0.0489 1043 SER A CB  
1276 O OG  . SER A 177 ? 0.3080 0.3863 0.3862 -0.0202 0.0331  -0.0519 1043 SER A OG  
1277 N N   . PRO A 178 ? 0.2171 0.2869 0.2839 -0.0221 0.0229  -0.0386 1044 PRO A N   
1278 C CA  . PRO A 178 ? 0.2185 0.2887 0.2764 -0.0244 0.0229  -0.0361 1044 PRO A CA  
1279 C C   . PRO A 178 ? 0.2093 0.2814 0.2624 -0.0263 0.0266  -0.0384 1044 PRO A C   
1280 O O   . PRO A 178 ? 0.2012 0.2763 0.2574 -0.0261 0.0291  -0.0407 1044 PRO A O   
1281 C CB  . PRO A 178 ? 0.2143 0.2870 0.2725 -0.0238 0.0204  -0.0321 1044 PRO A CB  
1282 C CG  . PRO A 178 ? 0.2175 0.2892 0.2832 -0.0221 0.0176  -0.0309 1044 PRO A CG  
1283 C CD  . PRO A 178 ? 0.2222 0.2935 0.2943 -0.0206 0.0200  -0.0355 1044 PRO A CD  
1284 N N   . LYS A 179 ? 0.1990 0.2698 0.2446 -0.0286 0.0267  -0.0375 1045 LYS A N   
1285 C CA  . LYS A 179 ? 0.2135 0.2855 0.2532 -0.0313 0.0292  -0.0388 1045 LYS A CA  
1286 C C   . LYS A 179 ? 0.1828 0.2549 0.2168 -0.0323 0.0270  -0.0350 1045 LYS A C   
1287 O O   . LYS A 179 ? 0.1733 0.2443 0.2049 -0.0322 0.0248  -0.0328 1045 LYS A O   
1288 C CB  . LYS A 179 ? 0.2577 0.3273 0.2937 -0.0334 0.0312  -0.0418 1045 LYS A CB  
1289 C CG  . LYS A 179 ? 0.3283 0.3983 0.3703 -0.0320 0.0337  -0.0470 1045 LYS A CG  
1290 C CD  . LYS A 179 ? 0.3760 0.4513 0.4204 -0.0326 0.0374  -0.0500 1045 LYS A CD  
1291 C CE  . LYS A 179 ? 0.4221 0.4995 0.4754 -0.0298 0.0395  -0.0550 1045 LYS A CE  
1292 N NZ  . LYS A 179 ? 0.4359 0.5083 0.4946 -0.0266 0.0366  -0.0554 1045 LYS A NZ  
1293 N N   . LEU A 180 ? 0.1773 0.2512 0.2095 -0.0333 0.0272  -0.0343 1046 LEU A N   
1294 C CA  . LEU A 180 ? 0.1689 0.2423 0.1966 -0.0335 0.0245  -0.0312 1046 LEU A CA  
1295 C C   . LEU A 180 ? 0.1673 0.2390 0.1885 -0.0362 0.0244  -0.0308 1046 LEU A C   
1296 O O   . LEU A 180 ? 0.1662 0.2376 0.1846 -0.0394 0.0267  -0.0326 1046 LEU A O   
1297 C CB  . LEU A 180 ? 0.1743 0.2486 0.2017 -0.0340 0.0239  -0.0305 1046 LEU A CB  
1298 C CG  . LEU A 180 ? 0.1738 0.2468 0.1973 -0.0337 0.0205  -0.0280 1046 LEU A CG  
1299 C CD1 . LEU A 180 ? 0.1607 0.2346 0.1862 -0.0300 0.0180  -0.0267 1046 LEU A CD1 
1300 C CD2 . LEU A 180 ? 0.1880 0.2606 0.2108 -0.0350 0.0194  -0.0274 1046 LEU A CD2 
1301 N N   . LEU A 181 ? 0.1660 0.2374 0.1851 -0.0353 0.0218  -0.0285 1047 LEU A N   
1302 C CA  . LEU A 181 ? 0.1672 0.2373 0.1804 -0.0379 0.0209  -0.0275 1047 LEU A CA  
1303 C C   . LEU A 181 ? 0.1641 0.2340 0.1746 -0.0378 0.0179  -0.0254 1047 LEU A C   
1304 O O   . LEU A 181 ? 0.1702 0.2382 0.1758 -0.0411 0.0173  -0.0248 1047 LEU A O   
1305 C CB  . LEU A 181 ? 0.1742 0.2448 0.1875 -0.0370 0.0196  -0.0261 1047 LEU A CB  
1306 C CG  . LEU A 181 ? 0.1884 0.2578 0.2044 -0.0371 0.0210  -0.0276 1047 LEU A CG  
1307 C CD1 . LEU A 181 ? 0.2107 0.2814 0.2267 -0.0366 0.0186  -0.0251 1047 LEU A CD1 
1308 C CD2 . LEU A 181 ? 0.2058 0.2724 0.2189 -0.0401 0.0237  -0.0306 1047 LEU A CD2 
1309 N N   . ILE A 182 ? 0.1528 0.2245 0.1660 -0.0341 0.0156  -0.0243 1048 ILE A N   
1310 C CA  . ILE A 182 ? 0.1547 0.2264 0.1664 -0.0327 0.0121  -0.0229 1048 ILE A CA  
1311 C C   . ILE A 182 ? 0.1457 0.2179 0.1603 -0.0297 0.0109  -0.0234 1048 ILE A C   
1312 O O   . ILE A 182 ? 0.1361 0.2107 0.1544 -0.0276 0.0120  -0.0239 1048 ILE A O   
1313 C CB  . ILE A 182 ? 0.1634 0.2383 0.1751 -0.0308 0.0104  -0.0218 1048 ILE A CB  
1314 C CG1 . ILE A 182 ? 0.1731 0.2472 0.1814 -0.0341 0.0110  -0.0209 1048 ILE A CG1 
1315 C CG2 . ILE A 182 ? 0.1697 0.2455 0.1816 -0.0279 0.0068  -0.0214 1048 ILE A CG2 
1316 C CD1 . ILE A 182 ? 0.1805 0.2511 0.1841 -0.0374 0.0095  -0.0200 1048 ILE A CD1 
1317 N N   . TYR A 183 ? 0.1470 0.2166 0.1600 -0.0297 0.0081  -0.0230 1049 TYR A N   
1318 C CA  . TYR A 183 ? 0.1482 0.2177 0.1635 -0.0264 0.0060  -0.0235 1049 TYR A CA  
1319 C C   . TYR A 183 ? 0.1567 0.2240 0.1703 -0.0246 0.0014  -0.0233 1049 TYR A C   
1320 O O   . TYR A 183 ? 0.1732 0.2387 0.1842 -0.0261 -0.0003 -0.0223 1049 TYR A O   
1321 C CB  . TYR A 183 ? 0.1440 0.2118 0.1603 -0.0283 0.0072  -0.0237 1049 TYR A CB  
1322 C CG  . TYR A 183 ? 0.1552 0.2194 0.1679 -0.0327 0.0065  -0.0228 1049 TYR A CG  
1323 C CD1 . TYR A 183 ? 0.1729 0.2332 0.1837 -0.0331 0.0022  -0.0217 1049 TYR A CD1 
1324 C CD2 . TYR A 183 ? 0.1576 0.2225 0.1683 -0.0367 0.0095  -0.0229 1049 TYR A CD2 
1325 C CE1 . TYR A 183 ? 0.1774 0.2346 0.1844 -0.0382 0.0009  -0.0201 1049 TYR A CE1 
1326 C CE2 . TYR A 183 ? 0.1655 0.2283 0.1722 -0.0417 0.0090  -0.0218 1049 TYR A CE2 
1327 C CZ  . TYR A 183 ? 0.1746 0.2337 0.1794 -0.0427 0.0045  -0.0201 1049 TYR A CZ  
1328 O OH  . TYR A 183 ? 0.2047 0.2619 0.2051 -0.0484 0.0033  -0.0183 1049 TYR A OH  
1329 N N   . TRP A 184 ? 0.1639 0.2314 0.1793 -0.0208 -0.0008 -0.0244 1050 TRP A N   
1330 C CA  . TRP A 184 ? 0.1842 0.2500 0.1991 -0.0176 -0.0055 -0.0252 1050 TRP A CA  
1331 C C   . TRP A 184 ? 0.1739 0.2440 0.1892 -0.0159 -0.0057 -0.0253 1050 TRP A C   
1332 O O   . TRP A 184 ? 0.1735 0.2411 0.1880 -0.0152 -0.0094 -0.0251 1050 TRP A O   
1333 C CB  . TRP A 184 ? 0.2096 0.2678 0.2217 -0.0203 -0.0095 -0.0240 1050 TRP A CB  
1334 C CG  . TRP A 184 ? 0.2542 0.3092 0.2665 -0.0205 -0.0107 -0.0242 1050 TRP A CG  
1335 C CD1 . TRP A 184 ? 0.2986 0.3508 0.3094 -0.0252 -0.0099 -0.0225 1050 TRP A CD1 
1336 C CD2 . TRP A 184 ? 0.2613 0.3160 0.2754 -0.0161 -0.0130 -0.0264 1050 TRP A CD2 
1337 N NE1 . TRP A 184 ? 0.3271 0.3770 0.3388 -0.0241 -0.0118 -0.0230 1050 TRP A NE1 
1338 C CE2 . TRP A 184 ? 0.2998 0.3509 0.3133 -0.0186 -0.0137 -0.0255 1050 TRP A CE2 
1339 C CE3 . TRP A 184 ? 0.2664 0.3243 0.2823 -0.0106 -0.0144 -0.0292 1050 TRP A CE3 
1340 C CZ2 . TRP A 184 ? 0.2948 0.3437 0.3089 -0.0157 -0.0165 -0.0271 1050 TRP A CZ2 
1341 C CZ3 . TRP A 184 ? 0.2897 0.3462 0.3061 -0.0075 -0.0167 -0.0314 1050 TRP A CZ3 
1342 C CH2 . TRP A 184 ? 0.2749 0.3264 0.2903 -0.0102 -0.0178 -0.0302 1050 TRP A CH2 
1343 N N   . ALA A 185 ? 0.1575 0.2338 0.1743 -0.0157 -0.0021 -0.0253 1051 ALA A N   
1344 C CA  . ALA A 185 ? 0.1566 0.2391 0.1743 -0.0146 -0.0017 -0.0250 1051 ALA A CA  
1345 C C   . ALA A 185 ? 0.1598 0.2400 0.1749 -0.0185 -0.0015 -0.0229 1051 ALA A C   
1346 O O   . ALA A 185 ? 0.1587 0.2432 0.1739 -0.0196 0.0003  -0.0220 1051 ALA A O   
1347 C CB  . ALA A 185 ? 0.1575 0.2440 0.1772 -0.0097 -0.0047 -0.0271 1051 ALA A CB  
1348 N N   . SER A 186 ? 0.1729 0.2466 0.1854 -0.0208 -0.0039 -0.0220 1052 SER A N   
1349 C CA  . SER A 186 ? 0.1822 0.2541 0.1917 -0.0245 -0.0047 -0.0199 1052 SER A CA  
1350 C C   . SER A 186 ? 0.1861 0.2517 0.1913 -0.0300 -0.0042 -0.0186 1052 SER A C   
1351 O O   . SER A 186 ? 0.1929 0.2569 0.1948 -0.0339 -0.0048 -0.0168 1052 SER A O   
1352 C CB  . SER A 186 ? 0.2002 0.2720 0.2108 -0.0219 -0.0097 -0.0197 1052 SER A CB  
1353 O OG  . SER A 186 ? 0.2007 0.2665 0.2111 -0.0207 -0.0138 -0.0203 1052 SER A OG  
1354 N N   . THR A 187 ? 0.1878 0.2511 0.1930 -0.0310 -0.0029 -0.0193 1053 THR A N   
1355 C CA  . THR A 187 ? 0.2068 0.2658 0.2080 -0.0367 -0.0024 -0.0181 1053 THR A CA  
1356 C C   . THR A 187 ? 0.2070 0.2685 0.2076 -0.0395 0.0032  -0.0190 1053 THR A C   
1357 O O   . THR A 187 ? 0.1809 0.2450 0.1850 -0.0374 0.0063  -0.0207 1053 THR A O   
1358 C CB  . THR A 187 ? 0.2298 0.2854 0.2313 -0.0368 -0.0045 -0.0181 1053 THR A CB  
1359 O OG1 . THR A 187 ? 0.2732 0.3255 0.2751 -0.0339 -0.0104 -0.0176 1053 THR A OG1 
1360 C CG2 . THR A 187 ? 0.2391 0.2923 0.2364 -0.0433 -0.0036 -0.0167 1053 THR A CG2 
1361 N N   . ARG A 188 ? 0.2110 0.2713 0.2072 -0.0444 0.0043  -0.0182 1054 ARG A N   
1362 C CA  A ARG A 188 ? 0.2151 0.2772 0.2105 -0.0471 0.0094  -0.0199 1054 ARG A CA  
1363 C CA  B ARG A 188 ? 0.2233 0.2855 0.2188 -0.0470 0.0094  -0.0199 1054 ARG A CA  
1364 C C   . ARG A 188 ? 0.2197 0.2819 0.2152 -0.0495 0.0118  -0.0212 1054 ARG A C   
1365 O O   . ARG A 188 ? 0.2326 0.2929 0.2249 -0.0531 0.0098  -0.0196 1054 ARG A O   
1366 C CB  A ARG A 188 ? 0.2229 0.2838 0.2130 -0.0516 0.0094  -0.0189 1054 ARG A CB  
1367 C CB  B ARG A 188 ? 0.2433 0.3043 0.2335 -0.0515 0.0095  -0.0190 1054 ARG A CB  
1368 C CG  A ARG A 188 ? 0.2267 0.2892 0.2166 -0.0526 0.0138  -0.0212 1054 ARG A CG  
1369 C CG  B ARG A 188 ? 0.2606 0.3232 0.2508 -0.0523 0.0139  -0.0212 1054 ARG A CG  
1370 C CD  A ARG A 188 ? 0.2286 0.2897 0.2127 -0.0573 0.0140  -0.0205 1054 ARG A CD  
1371 C CD  B ARG A 188 ? 0.2733 0.3344 0.2575 -0.0572 0.0140  -0.0206 1054 ARG A CD  
1372 N NE  A ARG A 188 ? 0.2338 0.2925 0.2125 -0.0619 0.0108  -0.0180 1054 ARG A NE  
1373 N NE  B ARG A 188 ? 0.2960 0.3571 0.2801 -0.0558 0.0104  -0.0180 1054 ARG A NE  
1374 C CZ  A ARG A 188 ? 0.2483 0.3064 0.2224 -0.0674 0.0121  -0.0183 1054 ARG A CZ  
1375 C CZ  B ARG A 188 ? 0.2946 0.3539 0.2755 -0.0581 0.0064  -0.0152 1054 ARG A CZ  
1376 N NH1 A ARG A 188 ? 0.2452 0.3057 0.2198 -0.0686 0.0170  -0.0217 1054 ARG A NH1 
1377 N NH1 B ARG A 188 ? 0.3087 0.3655 0.2857 -0.0624 0.0053  -0.0143 1054 ARG A NH1 
1378 N NH2 A ARG A 188 ? 0.2674 0.3231 0.2367 -0.0719 0.0082  -0.0151 1054 ARG A NH2 
1379 N NH2 B ARG A 188 ? 0.2856 0.3459 0.2675 -0.0564 0.0032  -0.0131 1054 ARG A NH2 
1380 N N   . HIS A 189 ? 0.2105 0.2754 0.2099 -0.0479 0.0158  -0.0236 1055 HIS A N   
1381 C CA  . HIS A 189 ? 0.2112 0.2781 0.2120 -0.0500 0.0189  -0.0254 1055 HIS A CA  
1382 C C   . HIS A 189 ? 0.2344 0.3022 0.2302 -0.0558 0.0217  -0.0265 1055 HIS A C   
1383 O O   . HIS A 189 ? 0.2165 0.2836 0.2092 -0.0572 0.0228  -0.0272 1055 HIS A O   
1384 C CB  . HIS A 189 ? 0.2093 0.2788 0.2166 -0.0460 0.0218  -0.0277 1055 HIS A CB  
1385 C CG  . HIS A 189 ? 0.2162 0.2886 0.2268 -0.0470 0.0246  -0.0296 1055 HIS A CG  
1386 N ND1 . HIS A 189 ? 0.2406 0.3134 0.2498 -0.0495 0.0233  -0.0281 1055 HIS A ND1 
1387 C CD2 . HIS A 189 ? 0.2269 0.3023 0.2425 -0.0457 0.0283  -0.0327 1055 HIS A CD2 
1388 C CE1 . HIS A 189 ? 0.2516 0.3287 0.2647 -0.0503 0.0266  -0.0302 1055 HIS A CE1 
1389 N NE2 . HIS A 189 ? 0.2452 0.3239 0.2626 -0.0476 0.0299  -0.0333 1055 HIS A NE2 
1390 N N   . THR A 190 ? 0.2552 0.3252 0.2498 -0.0595 0.0231  -0.0269 1056 THR A N   
1391 C CA  . THR A 190 ? 0.2813 0.3537 0.2706 -0.0659 0.0260  -0.0282 1056 THR A CA  
1392 C C   . THR A 190 ? 0.2811 0.3554 0.2717 -0.0647 0.0307  -0.0325 1056 THR A C   
1393 O O   . THR A 190 ? 0.2788 0.3550 0.2762 -0.0603 0.0331  -0.0353 1056 THR A O   
1394 C CB  . THR A 190 ? 0.2976 0.3745 0.2873 -0.0696 0.0276  -0.0284 1056 THR A CB  
1395 O OG1 . THR A 190 ? 0.2797 0.3537 0.2692 -0.0697 0.0225  -0.0244 1056 THR A OG1 
1396 C CG2 . THR A 190 ? 0.3239 0.4041 0.3067 -0.0771 0.0300  -0.0292 1056 THR A CG2 
1397 N N   . GLY A 191 ? 0.2906 0.3639 0.2749 -0.0687 0.0314  -0.0331 1057 GLY A N   
1398 C CA  . GLY A 191 ? 0.3056 0.3803 0.2902 -0.0685 0.0358  -0.0379 1057 GLY A CA  
1399 C C   . GLY A 191 ? 0.2981 0.3685 0.2839 -0.0648 0.0341  -0.0375 1057 GLY A C   
1400 O O   . GLY A 191 ? 0.3499 0.4196 0.3343 -0.0653 0.0366  -0.0410 1057 GLY A O   
1401 N N   . VAL A 192 ? 0.2611 0.3290 0.2492 -0.0612 0.0301  -0.0338 1058 VAL A N   
1402 C CA  . VAL A 192 ? 0.2535 0.3190 0.2435 -0.0578 0.0284  -0.0330 1058 VAL A CA  
1403 C C   . VAL A 192 ? 0.2501 0.3131 0.2330 -0.0618 0.0266  -0.0311 1058 VAL A C   
1404 O O   . VAL A 192 ? 0.2522 0.3146 0.2308 -0.0651 0.0241  -0.0282 1058 VAL A O   
1405 C CB  . VAL A 192 ? 0.2512 0.3166 0.2459 -0.0530 0.0251  -0.0300 1058 VAL A CB  
1406 C CG1 . VAL A 192 ? 0.2549 0.3194 0.2505 -0.0506 0.0228  -0.0283 1058 VAL A CG1 
1407 C CG2 . VAL A 192 ? 0.2479 0.3156 0.2493 -0.0495 0.0268  -0.0318 1058 VAL A CG2 
1408 N N   . PRO A 193 ? 0.2589 0.3200 0.2404 -0.0620 0.0271  -0.0323 1059 PRO A N   
1409 C CA  . PRO A 193 ? 0.2620 0.3209 0.2366 -0.0663 0.0252  -0.0303 1059 PRO A CA  
1410 C C   . PRO A 193 ? 0.2616 0.3202 0.2360 -0.0654 0.0204  -0.0252 1059 PRO A C   
1411 O O   . PRO A 193 ? 0.2472 0.3073 0.2273 -0.0605 0.0186  -0.0237 1059 PRO A O   
1412 C CB  . PRO A 193 ? 0.2635 0.3201 0.2379 -0.0658 0.0261  -0.0324 1059 PRO A CB  
1413 C CG  . PRO A 193 ? 0.2634 0.3208 0.2438 -0.0624 0.0296  -0.0371 1059 PRO A CG  
1414 C CD  . PRO A 193 ? 0.2535 0.3139 0.2395 -0.0590 0.0293  -0.0357 1059 PRO A CD  
1415 N N   . ASP A 194 ? 0.2644 0.3215 0.2325 -0.0702 0.0182  -0.0228 1060 ASP A N   
1416 C CA  . ASP A 194 ? 0.2886 0.3453 0.2564 -0.0698 0.0130  -0.0181 1060 ASP A CA  
1417 C C   . ASP A 194 ? 0.2483 0.3067 0.2206 -0.0655 0.0113  -0.0167 1060 ASP A C   
1418 O O   . ASP A 194 ? 0.2530 0.3132 0.2286 -0.0622 0.0078  -0.0142 1060 ASP A O   
1419 C CB  . ASP A 194 ? 0.3126 0.3671 0.2728 -0.0763 0.0107  -0.0157 1060 ASP A CB  
1420 C CG  . ASP A 194 ? 0.3521 0.4058 0.3069 -0.0819 0.0114  -0.0160 1060 ASP A CG  
1421 O OD1 . ASP A 194 ? 0.3551 0.4099 0.3131 -0.0801 0.0118  -0.0165 1060 ASP A OD1 
1422 O OD2 . ASP A 194 ? 0.3650 0.4174 0.3123 -0.0885 0.0113  -0.0154 1060 ASP A OD2 
1423 N N   . ARG A 195 ? 0.2442 0.3023 0.2164 -0.0655 0.0133  -0.0184 1061 ARG A N   
1424 C CA  . ARG A 195 ? 0.2263 0.2866 0.2017 -0.0628 0.0113  -0.0163 1061 ARG A CA  
1425 C C   . ARG A 195 ? 0.2213 0.2854 0.2040 -0.0569 0.0110  -0.0162 1061 ARG A C   
1426 O O   . ARG A 195 ? 0.2222 0.2898 0.2075 -0.0550 0.0092  -0.0141 1061 ARG A O   
1427 C CB  . ARG A 195 ? 0.2419 0.2997 0.2147 -0.0652 0.0127  -0.0178 1061 ARG A CB  
1428 C CG  . ARG A 195 ? 0.2388 0.2950 0.2147 -0.0631 0.0160  -0.0218 1061 ARG A CG  
1429 C CD  . ARG A 195 ? 0.2536 0.3058 0.2261 -0.0659 0.0166  -0.0236 1061 ARG A CD  
1430 N NE  . ARG A 195 ? 0.2481 0.2979 0.2236 -0.0641 0.0195  -0.0283 1061 ARG A NE  
1431 C CZ  . ARG A 195 ? 0.2516 0.2997 0.2250 -0.0655 0.0231  -0.0332 1061 ARG A CZ  
1432 N NH1 . ARG A 195 ? 0.2460 0.2948 0.2137 -0.0694 0.0243  -0.0336 1061 ARG A NH1 
1433 N NH2 . ARG A 195 ? 0.2590 0.3055 0.2366 -0.0629 0.0253  -0.0377 1061 ARG A NH2 
1434 N N   . PHE A 196 ? 0.2034 0.2674 0.1891 -0.0545 0.0129  -0.0184 1062 PHE A N   
1435 C CA  . PHE A 196 ? 0.2071 0.2746 0.1991 -0.0493 0.0126  -0.0184 1062 PHE A CA  
1436 C C   . PHE A 196 ? 0.1981 0.2674 0.1915 -0.0471 0.0097  -0.0168 1062 PHE A C   
1437 O O   . PHE A 196 ? 0.1965 0.2632 0.1879 -0.0485 0.0094  -0.0172 1062 PHE A O   
1438 C CB  . PHE A 196 ? 0.2075 0.2741 0.2026 -0.0477 0.0156  -0.0214 1062 PHE A CB  
1439 C CG  . PHE A 196 ? 0.2154 0.2802 0.2112 -0.0485 0.0178  -0.0234 1062 PHE A CG  
1440 C CD1 . PHE A 196 ? 0.2311 0.2924 0.2230 -0.0520 0.0201  -0.0261 1062 PHE A CD1 
1441 C CD2 . PHE A 196 ? 0.2105 0.2770 0.2109 -0.0458 0.0171  -0.0228 1062 PHE A CD2 
1442 C CE1 . PHE A 196 ? 0.2380 0.2969 0.2312 -0.0520 0.0215  -0.0286 1062 PHE A CE1 
1443 C CE2 . PHE A 196 ? 0.2207 0.2844 0.2222 -0.0464 0.0180  -0.0245 1062 PHE A CE2 
1444 C CZ  . PHE A 196 ? 0.2226 0.2820 0.2207 -0.0492 0.0201  -0.0276 1062 PHE A CZ  
1445 N N   . THR A 197 ? 0.1940 0.2679 0.1906 -0.0437 0.0074  -0.0152 1063 THR A N   
1446 C CA  . THR A 197 ? 0.2011 0.2768 0.2000 -0.0404 0.0043  -0.0146 1063 THR A CA  
1447 C C   . THR A 197 ? 0.1878 0.2689 0.1919 -0.0354 0.0044  -0.0155 1063 THR A C   
1448 O O   . THR A 197 ? 0.1908 0.2756 0.1966 -0.0349 0.0058  -0.0152 1063 THR A O   
1449 C CB  . THR A 197 ? 0.2154 0.2925 0.2131 -0.0411 0.0006  -0.0122 1063 THR A CB  
1450 O OG1 . THR A 197 ? 0.2054 0.2877 0.2042 -0.0411 0.0006  -0.0109 1063 THR A OG1 
1451 C CG2 . THR A 197 ? 0.2232 0.2948 0.2153 -0.0465 -0.0002 -0.0110 1063 THR A CG2 
1452 N N   . GLY A 198 ? 0.1764 0.2576 0.1827 -0.0320 0.0026  -0.0164 1064 GLY A N   
1453 C CA  . GLY A 198 ? 0.1694 0.2558 0.1800 -0.0273 0.0025  -0.0177 1064 GLY A CA  
1454 C C   . GLY A 198 ? 0.1635 0.2530 0.1762 -0.0235 -0.0010 -0.0181 1064 GLY A C   
1455 O O   . GLY A 198 ? 0.1448 0.2297 0.1561 -0.0240 -0.0040 -0.0177 1064 GLY A O   
1456 N N   . SER A 199 ? 0.1699 0.2673 0.1861 -0.0198 -0.0011 -0.0190 1065 SER A N   
1457 C CA  . SER A 199 ? 0.1795 0.2811 0.1988 -0.0150 -0.0043 -0.0207 1065 SER A CA  
1458 C C   . SER A 199 ? 0.1796 0.2880 0.2020 -0.0109 -0.0033 -0.0232 1065 SER A C   
1459 O O   . SER A 199 ? 0.1626 0.2744 0.1849 -0.0124 -0.0004 -0.0226 1065 SER A O   
1460 C CB  . SER A 199 ? 0.1980 0.3055 0.2184 -0.0155 -0.0057 -0.0190 1065 SER A CB  
1461 O OG  . SER A 199 ? 0.2207 0.3353 0.2412 -0.0174 -0.0029 -0.0176 1065 SER A OG  
1462 N N   . GLY A 200 ? 0.1897 0.3006 0.2149 -0.0059 -0.0061 -0.0260 1066 GLY A N   
1463 C CA  . GLY A 200 ? 0.2024 0.3221 0.2304 -0.0017 -0.0053 -0.0290 1066 GLY A CA  
1464 C C   . GLY A 200 ? 0.1992 0.3142 0.2276 0.0020  -0.0072 -0.0325 1066 GLY A C   
1465 O O   . GLY A 200 ? 0.2064 0.3111 0.2329 0.0009  -0.0090 -0.0321 1066 GLY A O   
1466 N N   . SER A 201 ? 0.2007 0.3239 0.2316 0.0065  -0.0072 -0.0360 1067 SER A N   
1467 C CA  . SER A 201 ? 0.2104 0.3305 0.2417 0.0105  -0.0090 -0.0400 1067 SER A CA  
1468 C C   . SER A 201 ? 0.2018 0.3343 0.2347 0.0135  -0.0071 -0.0433 1067 SER A C   
1469 O O   . SER A 201 ? 0.2004 0.3445 0.2352 0.0134  -0.0054 -0.0429 1067 SER A O   
1470 C CB  . SER A 201 ? 0.2524 0.3663 0.2854 0.0147  -0.0142 -0.0427 1067 SER A CB  
1471 O OG  . SER A 201 ? 0.3055 0.4293 0.3427 0.0190  -0.0152 -0.0453 1067 SER A OG  
1472 N N   . GLY A 202 ? 0.1892 0.3197 0.2211 0.0155  -0.0075 -0.0462 1068 GLY A N   
1473 C CA  . GLY A 202 ? 0.1916 0.3339 0.2243 0.0181  -0.0057 -0.0498 1068 GLY A CA  
1474 C C   . GLY A 202 ? 0.1789 0.3273 0.2097 0.0129  -0.0019 -0.0460 1068 GLY A C   
1475 O O   . GLY A 202 ? 0.1662 0.3083 0.1948 0.0103  -0.0013 -0.0443 1068 GLY A O   
1476 N N   . THR A 203 ? 0.1696 0.3302 0.2015 0.0113  0.0001  -0.0445 1069 THR A N   
1477 C CA  . THR A 203 ? 0.1716 0.3384 0.2018 0.0059  0.0029  -0.0405 1069 THR A CA  
1478 C C   . THR A 203 ? 0.1794 0.3456 0.2095 0.0012  0.0038  -0.0352 1069 THR A C   
1479 O O   . THR A 203 ? 0.1917 0.3601 0.2204 -0.0035 0.0052  -0.0314 1069 THR A O   
1480 C CB  . THR A 203 ? 0.1838 0.3668 0.2144 0.0070  0.0044  -0.0431 1069 THR A CB  
1481 O OG1 . THR A 203 ? 0.1939 0.3871 0.2275 0.0091  0.0044  -0.0443 1069 THR A OG1 
1482 C CG2 . THR A 203 ? 0.1915 0.3743 0.2214 0.0115  0.0034  -0.0488 1069 THR A CG2 
1483 N N   . ASP A 204 ? 0.1707 0.3328 0.2020 0.0021  0.0025  -0.0347 1070 ASP A N   
1484 C CA  A ASP A 204 ? 0.1664 0.3289 0.1972 -0.0025 0.0032  -0.0299 1070 ASP A CA  
1485 C CA  B ASP A 204 ? 0.1751 0.3376 0.2058 -0.0026 0.0033  -0.0298 1070 ASP A CA  
1486 C C   . ASP A 204 ? 0.1572 0.3052 0.1863 -0.0044 0.0024  -0.0280 1070 ASP A C   
1487 O O   . ASP A 204 ? 0.1370 0.2794 0.1669 -0.0014 0.0002  -0.0300 1070 ASP A O   
1488 C CB  A ASP A 204 ? 0.1743 0.3480 0.2078 -0.0010 0.0027  -0.0304 1070 ASP A CB  
1489 C CB  B ASP A 204 ? 0.1947 0.3689 0.2279 -0.0016 0.0030  -0.0300 1070 ASP A CB  
1490 C CG  A ASP A 204 ? 0.1776 0.3684 0.2126 -0.0002 0.0042  -0.0320 1070 ASP A CG  
1491 C CG  B ASP A 204 ? 0.2171 0.3870 0.2526 0.0019  0.0005  -0.0318 1070 ASP A CG  
1492 O OD1 A ASP A 204 ? 0.1782 0.3732 0.2111 -0.0045 0.0057  -0.0292 1070 ASP A OD1 
1493 O OD1 B ASP A 204 ? 0.2659 0.4312 0.3027 0.0068  -0.0014 -0.0359 1070 ASP A OD1 
1494 O OD2 A ASP A 204 ? 0.1957 0.3962 0.2342 0.0045  0.0036  -0.0360 1070 ASP A OD2 
1495 O OD2 B ASP A 204 ? 0.2123 0.3836 0.2483 -0.0002 0.0000  -0.0290 1070 ASP A OD2 
1496 N N   . PHE A 205 ? 0.1455 0.2885 0.1727 -0.0093 0.0037  -0.0243 1071 PHE A N   
1497 C CA  . PHE A 205 ? 0.1394 0.2699 0.1648 -0.0115 0.0035  -0.0229 1071 PHE A CA  
1498 C C   . PHE A 205 ? 0.1327 0.2625 0.1566 -0.0164 0.0044  -0.0192 1071 PHE A C   
1499 O O   . PHE A 205 ? 0.1348 0.2697 0.1588 -0.0188 0.0053  -0.0172 1071 PHE A O   
1500 C CB  . PHE A 205 ? 0.1378 0.2603 0.1625 -0.0118 0.0042  -0.0236 1071 PHE A CB  
1501 C CG  . PHE A 205 ? 0.1428 0.2651 0.1684 -0.0073 0.0028  -0.0272 1071 PHE A CG  
1502 C CD1 . PHE A 205 ? 0.1456 0.2602 0.1707 -0.0055 0.0007  -0.0288 1071 PHE A CD1 
1503 C CD2 . PHE A 205 ? 0.1481 0.2783 0.1746 -0.0054 0.0031  -0.0288 1071 PHE A CD2 
1504 C CE1 . PHE A 205 ? 0.1545 0.2683 0.1803 -0.0012 -0.0013 -0.0322 1071 PHE A CE1 
1505 C CE2 . PHE A 205 ? 0.1618 0.2918 0.1888 -0.0011 0.0016  -0.0327 1071 PHE A CE2 
1506 C CZ  . PHE A 205 ? 0.1589 0.2801 0.1857 0.0010  -0.0007 -0.0344 1071 PHE A CZ  
1507 N N   . THR A 206 ? 0.1366 0.2597 0.1588 -0.0180 0.0039  -0.0183 1072 THR A N   
1508 C CA  . THR A 206 ? 0.1359 0.2571 0.1561 -0.0227 0.0044  -0.0153 1072 THR A CA  
1509 C C   . THR A 206 ? 0.1439 0.2536 0.1613 -0.0251 0.0051  -0.0154 1072 THR A C   
1510 O O   . THR A 206 ? 0.1549 0.2600 0.1714 -0.0241 0.0039  -0.0165 1072 THR A O   
1511 C CB  . THR A 206 ? 0.1401 0.2676 0.1605 -0.0232 0.0029  -0.0138 1072 THR A CB  
1512 O OG1 . THR A 206 ? 0.1373 0.2770 0.1605 -0.0211 0.0029  -0.0141 1072 THR A OG1 
1513 C CG2 . THR A 206 ? 0.1510 0.2760 0.1687 -0.0283 0.0031  -0.0106 1072 THR A CG2 
1514 N N   . LEU A 207 ? 0.1417 0.2477 0.1578 -0.0285 0.0064  -0.0141 1073 LEU A N   
1515 C CA  . LEU A 207 ? 0.1587 0.2559 0.1719 -0.0316 0.0075  -0.0143 1073 LEU A CA  
1516 C C   . LEU A 207 ? 0.1666 0.2642 0.1771 -0.0351 0.0067  -0.0120 1073 LEU A C   
1517 O O   . LEU A 207 ? 0.1761 0.2779 0.1872 -0.0367 0.0062  -0.0100 1073 LEU A O   
1518 C CB  . LEU A 207 ? 0.1635 0.2561 0.1776 -0.0326 0.0093  -0.0152 1073 LEU A CB  
1519 C CG  . LEU A 207 ? 0.1662 0.2511 0.1776 -0.0357 0.0109  -0.0163 1073 LEU A CG  
1520 C CD1 . LEU A 207 ? 0.1697 0.2507 0.1796 -0.0354 0.0117  -0.0181 1073 LEU A CD1 
1521 C CD2 . LEU A 207 ? 0.1853 0.2670 0.1990 -0.0363 0.0122  -0.0172 1073 LEU A CD2 
1522 N N   . THR A 208 ? 0.1743 0.2682 0.1818 -0.0368 0.0060  -0.0120 1074 THR A N   
1523 C CA  . THR A 208 ? 0.1864 0.2797 0.1906 -0.0407 0.0050  -0.0098 1074 THR A CA  
1524 C C   . THR A 208 ? 0.2053 0.2899 0.2054 -0.0443 0.0067  -0.0111 1074 THR A C   
1525 O O   . THR A 208 ? 0.1955 0.2756 0.1942 -0.0443 0.0078  -0.0130 1074 THR A O   
1526 C CB  . THR A 208 ? 0.2042 0.3010 0.2082 -0.0400 0.0025  -0.0085 1074 THR A CB  
1527 O OG1 . THR A 208 ? 0.1908 0.2968 0.1994 -0.0360 0.0014  -0.0084 1074 THR A OG1 
1528 C CG2 . THR A 208 ? 0.2129 0.3098 0.2137 -0.0443 0.0011  -0.0058 1074 THR A CG2 
1529 N N   . ILE A 209 ? 0.2199 0.3026 0.2180 -0.0475 0.0069  -0.0102 1075 ILE A N   
1530 C CA  . ILE A 209 ? 0.2215 0.2964 0.2150 -0.0512 0.0083  -0.0119 1075 ILE A CA  
1531 C C   . ILE A 209 ? 0.2190 0.2938 0.2082 -0.0551 0.0063  -0.0094 1075 ILE A C   
1532 O O   . ILE A 209 ? 0.2432 0.3205 0.2328 -0.0564 0.0047  -0.0071 1075 ILE A O   
1533 C CB  . ILE A 209 ? 0.2334 0.3043 0.2282 -0.0515 0.0097  -0.0138 1075 ILE A CB  
1534 C CG1 . ILE A 209 ? 0.2436 0.3168 0.2441 -0.0475 0.0106  -0.0149 1075 ILE A CG1 
1535 C CG2 . ILE A 209 ? 0.2555 0.3194 0.2462 -0.0542 0.0119  -0.0172 1075 ILE A CG2 
1536 C CD1 . ILE A 209 ? 0.2466 0.3159 0.2494 -0.0476 0.0109  -0.0161 1075 ILE A CD1 
1537 N N   . SER A 210 ? 0.2282 0.3011 0.2137 -0.0571 0.0057  -0.0092 1076 SER A N   
1538 C CA  . SER A 210 ? 0.2255 0.2971 0.2060 -0.0616 0.0037  -0.0068 1076 SER A CA  
1539 C C   . SER A 210 ? 0.2306 0.2952 0.2058 -0.0659 0.0052  -0.0089 1076 SER A C   
1540 O O   . SER A 210 ? 0.2134 0.2735 0.1875 -0.0659 0.0083  -0.0128 1076 SER A O   
1541 C CB  . SER A 210 ? 0.2303 0.3018 0.2089 -0.0625 0.0019  -0.0057 1076 SER A CB  
1542 O OG  . SER A 210 ? 0.2446 0.3228 0.2290 -0.0578 0.0000  -0.0043 1076 SER A OG  
1543 N N   . ASN A 211 ? 0.2375 0.3011 0.2091 -0.0698 0.0032  -0.0066 1077 ASN A N   
1544 C CA  . ASN A 211 ? 0.2471 0.3030 0.2123 -0.0743 0.0043  -0.0091 1077 ASN A CA  
1545 C C   . ASN A 211 ? 0.2558 0.3077 0.2233 -0.0720 0.0071  -0.0136 1077 ASN A C   
1546 O O   . ASN A 211 ? 0.2506 0.2979 0.2154 -0.0730 0.0101  -0.0181 1077 ASN A O   
1547 C CB  . ASN A 211 ? 0.2580 0.3108 0.2171 -0.0779 0.0051  -0.0102 1077 ASN A CB  
1548 C CG  . ASN A 211 ? 0.2722 0.3184 0.2233 -0.0835 0.0056  -0.0122 1077 ASN A CG  
1549 O OD1 . ASN A 211 ? 0.3029 0.3465 0.2480 -0.0874 0.0067  -0.0137 1077 ASN A OD1 
1550 N ND2 . ASN A 211 ? 0.2588 0.3023 0.2094 -0.0844 0.0044  -0.0122 1077 ASN A ND2 
1551 N N   . VAL A 212 ? 0.2503 0.3045 0.2232 -0.0692 0.0060  -0.0123 1078 VAL A N   
1552 C CA  . VAL A 212 ? 0.2473 0.2987 0.2245 -0.0661 0.0078  -0.0158 1078 VAL A CA  
1553 C C   . VAL A 212 ? 0.2635 0.3065 0.2369 -0.0687 0.0085  -0.0198 1078 VAL A C   
1554 O O   . VAL A 212 ? 0.2607 0.3007 0.2294 -0.0727 0.0060  -0.0181 1078 VAL A O   
1555 C CB  . VAL A 212 ? 0.2487 0.3044 0.2315 -0.0638 0.0055  -0.0126 1078 VAL A CB  
1556 C CG1 . VAL A 212 ? 0.2577 0.3119 0.2384 -0.0674 0.0018  -0.0093 1078 VAL A CG1 
1557 C CG2 . VAL A 212 ? 0.2488 0.3025 0.2371 -0.0601 0.0071  -0.0157 1078 VAL A CG2 
1558 N N   . GLN A 213 ? 0.2548 0.2947 0.2303 -0.0664 0.0117  -0.0252 1079 GLN A N   
1559 C CA  . GLN A 213 ? 0.2662 0.2986 0.2394 -0.0675 0.0128  -0.0306 1079 GLN A CA  
1560 C C   . GLN A 213 ? 0.2761 0.3053 0.2561 -0.0640 0.0117  -0.0325 1079 GLN A C   
1561 O O   . GLN A 213 ? 0.2506 0.2839 0.2369 -0.0605 0.0115  -0.0307 1079 GLN A O   
1562 C CB  . GLN A 213 ? 0.2689 0.3015 0.2394 -0.0681 0.0175  -0.0358 1079 GLN A CB  
1563 C CG  . GLN A 213 ? 0.2729 0.3076 0.2360 -0.0726 0.0177  -0.0335 1079 GLN A CG  
1564 C CD  . GLN A 213 ? 0.2879 0.3184 0.2440 -0.0774 0.0149  -0.0318 1079 GLN A CD  
1565 O OE1 . GLN A 213 ? 0.3041 0.3286 0.2566 -0.0793 0.0154  -0.0360 1079 GLN A OE1 
1566 N NE2 . GLN A 213 ? 0.2879 0.3217 0.2424 -0.0794 0.0118  -0.0257 1079 GLN A NE2 
1567 N N   . SER A 214 ? 0.3026 0.3241 0.2814 -0.0646 0.0112  -0.0370 1080 SER A N   
1568 C CA  . SER A 214 ? 0.3094 0.3263 0.2951 -0.0612 0.0092  -0.0392 1080 SER A CA  
1569 C C   . SER A 214 ? 0.3044 0.3250 0.2972 -0.0564 0.0130  -0.0428 1080 SER A C   
1570 O O   . SER A 214 ? 0.2876 0.3082 0.2878 -0.0532 0.0109  -0.0415 1080 SER A O   
1571 C CB  . SER A 214 ? 0.3371 0.3443 0.3198 -0.0627 0.0075  -0.0439 1080 SER A CB  
1572 O OG  . SER A 214 ? 0.3791 0.3855 0.3592 -0.0625 0.0125  -0.0513 1080 SER A OG  
1573 N N   . GLU A 215 ? 0.2990 0.3235 0.2901 -0.0562 0.0179  -0.0464 1081 GLU A N   
1574 C CA  . GLU A 215 ? 0.2975 0.3260 0.2956 -0.0520 0.0213  -0.0497 1081 GLU A CA  
1575 C C   . GLU A 215 ? 0.2752 0.3096 0.2774 -0.0501 0.0201  -0.0439 1081 GLU A C   
1576 O O   . GLU A 215 ? 0.2827 0.3203 0.2912 -0.0466 0.0219  -0.0454 1081 GLU A O   
1577 C CB  . GLU A 215 ? 0.3211 0.3530 0.3157 -0.0532 0.0268  -0.0547 1081 GLU A CB  
1578 C CG  . GLU A 215 ? 0.3344 0.3709 0.3226 -0.0568 0.0275  -0.0504 1081 GLU A CG  
1579 C CD  . GLU A 215 ? 0.3784 0.4193 0.3635 -0.0586 0.0322  -0.0539 1081 GLU A CD  
1580 O OE1 . GLU A 215 ? 0.4291 0.4708 0.4064 -0.0633 0.0325  -0.0521 1081 GLU A OE1 
1581 O OE2 . GLU A 215 ? 0.3999 0.4440 0.3907 -0.0557 0.0353  -0.0578 1081 GLU A OE2 
1582 N N   . ASP A 216 ? 0.2615 0.2982 0.2601 -0.0523 0.0174  -0.0378 1082 ASP A N   
1583 C CA  . ASP A 216 ? 0.2503 0.2935 0.2520 -0.0506 0.0163  -0.0328 1082 ASP A CA  
1584 C C   . ASP A 216 ? 0.2543 0.2971 0.2612 -0.0491 0.0123  -0.0294 1082 ASP A C   
1585 O O   . ASP A 216 ? 0.2430 0.2914 0.2528 -0.0475 0.0114  -0.0259 1082 ASP A O   
1586 C CB  . ASP A 216 ? 0.2456 0.2926 0.2418 -0.0533 0.0153  -0.0285 1082 ASP A CB  
1587 C CG  . ASP A 216 ? 0.2485 0.2959 0.2391 -0.0556 0.0181  -0.0304 1082 ASP A CG  
1588 O OD1 . ASP A 216 ? 0.2425 0.2897 0.2341 -0.0547 0.0216  -0.0348 1082 ASP A OD1 
1589 O OD2 . ASP A 216 ? 0.2529 0.3010 0.2381 -0.0588 0.0166  -0.0275 1082 ASP A OD2 
1590 N N   . LEU A 217 ? 0.2551 0.2914 0.2627 -0.0500 0.0096  -0.0303 1083 LEU A N   
1591 C CA  . LEU A 217 ? 0.2756 0.3109 0.2881 -0.0493 0.0050  -0.0268 1083 LEU A CA  
1592 C C   . LEU A 217 ? 0.2747 0.3107 0.2950 -0.0450 0.0062  -0.0292 1083 LEU A C   
1593 O O   . LEU A 217 ? 0.2867 0.3192 0.3097 -0.0428 0.0088  -0.0351 1083 LEU A O   
1594 C CB  . LEU A 217 ? 0.3073 0.3339 0.3183 -0.0516 0.0011  -0.0274 1083 LEU A CB  
1595 C CG  . LEU A 217 ? 0.3336 0.3591 0.3366 -0.0563 -0.0001 -0.0251 1083 LEU A CG  
1596 C CD1 . LEU A 217 ? 0.3694 0.3849 0.3708 -0.0585 -0.0042 -0.0265 1083 LEU A CD1 
1597 C CD2 . LEU A 217 ? 0.3414 0.3749 0.3428 -0.0585 -0.0023 -0.0180 1083 LEU A CD2 
1598 N N   . ALA A 218 ? 0.2649 0.3065 0.2885 -0.0439 0.0049  -0.0251 1084 ALA A N   
1599 C CA  . ALA A 218 ? 0.2598 0.3039 0.2901 -0.0402 0.0063  -0.0265 1084 ALA A CA  
1600 C C   . ALA A 218 ? 0.2387 0.2894 0.2702 -0.0404 0.0041  -0.0209 1084 ALA A C   
1601 O O   . ALA A 218 ? 0.2251 0.2792 0.2523 -0.0432 0.0022  -0.0167 1084 ALA A O   
1602 C CB  . ALA A 218 ? 0.2712 0.3184 0.3004 -0.0386 0.0116  -0.0303 1084 ALA A CB  
1603 N N   . ASP A 219 ? 0.2364 0.2895 0.2733 -0.0377 0.0045  -0.0210 1085 ASP A N   
1604 C CA  . ASP A 219 ? 0.2514 0.3118 0.2888 -0.0376 0.0034  -0.0168 1085 ASP A CA  
1605 C C   . ASP A 219 ? 0.2344 0.3000 0.2692 -0.0360 0.0072  -0.0182 1085 ASP A C   
1606 O O   . ASP A 219 ? 0.2289 0.2924 0.2642 -0.0345 0.0106  -0.0223 1085 ASP A O   
1607 C CB  . ASP A 219 ? 0.2781 0.3386 0.3222 -0.0356 0.0017  -0.0162 1085 ASP A CB  
1608 C CG  . ASP A 219 ? 0.3350 0.3907 0.3830 -0.0371 -0.0034 -0.0138 1085 ASP A CG  
1609 O OD1 . ASP A 219 ? 0.3520 0.4043 0.3971 -0.0400 -0.0063 -0.0120 1085 ASP A OD1 
1610 O OD2 . ASP A 219 ? 0.3520 0.4071 0.4060 -0.0354 -0.0049 -0.0136 1085 ASP A OD2 
1611 N N   . TYR A 220 ? 0.2059 0.2782 0.2379 -0.0366 0.0066  -0.0150 1086 TYR A N   
1612 C CA  . TYR A 220 ? 0.1916 0.2684 0.2216 -0.0348 0.0091  -0.0160 1086 TYR A CA  
1613 C C   . TYR A 220 ? 0.1906 0.2734 0.2227 -0.0333 0.0079  -0.0140 1086 TYR A C   
1614 O O   . TYR A 220 ? 0.1914 0.2785 0.2235 -0.0350 0.0053  -0.0106 1086 TYR A O   
1615 C CB  . TYR A 220 ? 0.2003 0.2795 0.2249 -0.0365 0.0093  -0.0150 1086 TYR A CB  
1616 C CG  . TYR A 220 ? 0.1987 0.2720 0.2203 -0.0382 0.0106  -0.0172 1086 TYR A CG  
1617 C CD1 . TYR A 220 ? 0.2066 0.2759 0.2270 -0.0409 0.0089  -0.0164 1086 TYR A CD1 
1618 C CD2 . TYR A 220 ? 0.1913 0.2625 0.2110 -0.0377 0.0135  -0.0203 1086 TYR A CD2 
1619 C CE1 . TYR A 220 ? 0.2121 0.2755 0.2292 -0.0426 0.0102  -0.0192 1086 TYR A CE1 
1620 C CE2 . TYR A 220 ? 0.2047 0.2711 0.2212 -0.0398 0.0150  -0.0227 1086 TYR A CE2 
1621 C CZ  . TYR A 220 ? 0.2147 0.2773 0.2297 -0.0421 0.0135  -0.0224 1086 TYR A CZ  
1622 O OH  . TYR A 220 ? 0.2312 0.2890 0.2424 -0.0442 0.0152  -0.0254 1086 TYR A OH  
1623 N N   . PHE A 221 ? 0.1846 0.2684 0.2180 -0.0308 0.0096  -0.0159 1087 PHE A N   
1624 C CA  . PHE A 221 ? 0.1833 0.2721 0.2184 -0.0292 0.0087  -0.0149 1087 PHE A CA  
1625 C C   . PHE A 221 ? 0.1689 0.2600 0.2014 -0.0270 0.0101  -0.0166 1087 PHE A C   
1626 O O   . PHE A 221 ? 0.1545 0.2415 0.1864 -0.0265 0.0119  -0.0189 1087 PHE A O   
1627 C CB  . PHE A 221 ? 0.2262 0.3118 0.2664 -0.0280 0.0087  -0.0158 1087 PHE A CB  
1628 C CG  . PHE A 221 ? 0.2816 0.3647 0.3256 -0.0294 0.0062  -0.0139 1087 PHE A CG  
1629 C CD1 . PHE A 221 ? 0.3147 0.3915 0.3617 -0.0295 0.0066  -0.0159 1087 PHE A CD1 
1630 C CD2 . PHE A 221 ? 0.3083 0.3954 0.3534 -0.0308 0.0031  -0.0104 1087 PHE A CD2 
1631 C CE1 . PHE A 221 ? 0.3272 0.4006 0.3783 -0.0305 0.0034  -0.0143 1087 PHE A CE1 
1632 C CE2 . PHE A 221 ? 0.2945 0.3783 0.3431 -0.0327 -0.0002 -0.0081 1087 PHE A CE2 
1633 C CZ  . PHE A 221 ? 0.2748 0.3513 0.3266 -0.0323 -0.0003 -0.0100 1087 PHE A CZ  
1634 N N   . CYS A 222 ? 0.1629 0.2604 0.1943 -0.0259 0.0090  -0.0157 1088 CYS A N   
1635 C CA  . CYS A 222 ? 0.1756 0.2747 0.2055 -0.0232 0.0093  -0.0177 1088 CYS A CA  
1636 C C   . CYS A 222 ? 0.1694 0.2681 0.2018 -0.0217 0.0089  -0.0183 1088 CYS A C   
1637 O O   . CYS A 222 ? 0.1811 0.2806 0.2162 -0.0228 0.0081  -0.0167 1088 CYS A O   
1638 C CB  . CYS A 222 ? 0.2239 0.3306 0.2517 -0.0220 0.0083  -0.0175 1088 CYS A CB  
1639 S SG  . CYS A 222 ? 0.3212 0.4366 0.3500 -0.0231 0.0070  -0.0152 1088 CYS A SG  
1640 N N   . GLN A 223 ? 0.1487 0.2454 0.1803 -0.0197 0.0091  -0.0204 1089 GLN A N   
1641 C CA  . GLN A 223 ? 0.1466 0.2429 0.1799 -0.0184 0.0083  -0.0210 1089 GLN A CA  
1642 C C   . GLN A 223 ? 0.1459 0.2431 0.1766 -0.0157 0.0071  -0.0231 1089 GLN A C   
1643 O O   . GLN A 223 ? 0.1553 0.2491 0.1841 -0.0153 0.0071  -0.0241 1089 GLN A O   
1644 C CB  . GLN A 223 ? 0.1533 0.2437 0.1893 -0.0192 0.0095  -0.0215 1089 GLN A CB  
1645 C CG  . GLN A 223 ? 0.1561 0.2463 0.1941 -0.0183 0.0084  -0.0216 1089 GLN A CG  
1646 C CD  . GLN A 223 ? 0.1827 0.2687 0.2234 -0.0189 0.0094  -0.0222 1089 GLN A CD  
1647 O OE1 . GLN A 223 ? 0.1856 0.2689 0.2264 -0.0200 0.0112  -0.0230 1089 GLN A OE1 
1648 N NE2 . GLN A 223 ? 0.2212 0.3075 0.2645 -0.0186 0.0082  -0.0216 1089 GLN A NE2 
1649 N N   . GLN A 224 ? 0.1444 0.2450 0.1749 -0.0141 0.0058  -0.0238 1090 GLN A N   
1650 C CA  . GLN A 224 ? 0.1414 0.2412 0.1699 -0.0111 0.0041  -0.0265 1090 GLN A CA  
1651 C C   . GLN A 224 ? 0.1447 0.2390 0.1742 -0.0114 0.0034  -0.0267 1090 GLN A C   
1652 O O   . GLN A 224 ? 0.1506 0.2452 0.1825 -0.0129 0.0038  -0.0251 1090 GLN A O   
1653 C CB  . GLN A 224 ? 0.1380 0.2458 0.1652 -0.0090 0.0032  -0.0281 1090 GLN A CB  
1654 C CG  . GLN A 224 ? 0.1466 0.2581 0.1744 -0.0100 0.0029  -0.0272 1090 GLN A CG  
1655 C CD  . GLN A 224 ? 0.1424 0.2499 0.1696 -0.0086 0.0012  -0.0290 1090 GLN A CD  
1656 O OE1 . GLN A 224 ? 0.1469 0.2498 0.1728 -0.0062 -0.0002 -0.0315 1090 GLN A OE1 
1657 N NE2 . GLN A 224 ? 0.1451 0.2537 0.1733 -0.0105 0.0008  -0.0272 1090 GLN A NE2 
1658 N N   . TYR A 225 ? 0.1426 0.2316 0.1705 -0.0103 0.0019  -0.0281 1091 TYR A N   
1659 C CA  . TYR A 225 ? 0.1396 0.2236 0.1677 -0.0106 0.0003  -0.0283 1091 TYR A CA  
1660 C C   . TYR A 225 ? 0.1427 0.2244 0.1680 -0.0076 -0.0030 -0.0310 1091 TYR A C   
1661 O O   . TYR A 225 ? 0.1546 0.2300 0.1789 -0.0081 -0.0053 -0.0312 1091 TYR A O   
1662 C CB  . TYR A 225 ? 0.1416 0.2208 0.1709 -0.0135 0.0016  -0.0268 1091 TYR A CB  
1663 C CG  . TYR A 225 ? 0.1388 0.2147 0.1656 -0.0142 0.0013  -0.0271 1091 TYR A CG  
1664 C CD1 . TYR A 225 ? 0.1465 0.2168 0.1710 -0.0146 -0.0014 -0.0273 1091 TYR A CD1 
1665 C CD2 . TYR A 225 ? 0.1444 0.2225 0.1710 -0.0151 0.0034  -0.0265 1091 TYR A CD2 
1666 C CE1 . TYR A 225 ? 0.1485 0.2157 0.1706 -0.0160 -0.0022 -0.0269 1091 TYR A CE1 
1667 C CE2 . TYR A 225 ? 0.1451 0.2202 0.1692 -0.0162 0.0028  -0.0264 1091 TYR A CE2 
1668 C CZ  . TYR A 225 ? 0.1528 0.2226 0.1747 -0.0169 0.0001  -0.0264 1091 TYR A CZ  
1669 O OH  . TYR A 225 ? 0.1551 0.2219 0.1743 -0.0187 -0.0008 -0.0258 1091 TYR A OH  
1670 N N   . SER A 226 ? 0.1542 0.2413 0.1784 -0.0046 -0.0036 -0.0333 1092 SER A N   
1671 C CA  . SER A 226 ? 0.1660 0.2525 0.1882 -0.0008 -0.0068 -0.0371 1092 SER A CA  
1672 C C   . SER A 226 ? 0.1799 0.2658 0.2015 -0.0010 -0.0079 -0.0376 1092 SER A C   
1673 O O   . SER A 226 ? 0.1927 0.2731 0.2124 0.0007  -0.0113 -0.0398 1092 SER A O   
1674 C CB  . SER A 226 ? 0.1725 0.2676 0.1945 0.0021  -0.0061 -0.0396 1092 SER A CB  
1675 O OG  . SER A 226 ? 0.1893 0.2843 0.2099 0.0064  -0.0091 -0.0441 1092 SER A OG  
1676 N N   . SER A 227 ? 0.1708 0.2620 0.1935 -0.0030 -0.0058 -0.0357 1093 SER A N   
1677 C CA  . SER A 227 ? 0.1880 0.2797 0.2097 -0.0034 -0.0072 -0.0362 1093 SER A CA  
1678 C C   . SER A 227 ? 0.1731 0.2667 0.1979 -0.0072 -0.0054 -0.0320 1093 SER A C   
1679 O O   . SER A 227 ? 0.1512 0.2476 0.1783 -0.0089 -0.0031 -0.0297 1093 SER A O   
1680 C CB  . SER A 227 ? 0.2042 0.3036 0.2234 -0.0007 -0.0076 -0.0399 1093 SER A CB  
1681 O OG  . SER A 227 ? 0.2328 0.3412 0.2530 -0.0020 -0.0049 -0.0384 1093 SER A OG  
1682 N N   . TYR A 228 ? 0.1617 0.2528 0.1867 -0.0086 -0.0070 -0.0310 1094 TYR A N   
1683 C CA  . TYR A 228 ? 0.1654 0.2585 0.1939 -0.0119 -0.0062 -0.0272 1094 TYR A CA  
1684 C C   . TYR A 228 ? 0.1655 0.2664 0.1923 -0.0127 -0.0064 -0.0270 1094 TYR A C   
1685 O O   . TYR A 228 ? 0.1711 0.2748 0.1938 -0.0110 -0.0076 -0.0301 1094 TYR A O   
1686 C CB  . TYR A 228 ? 0.1642 0.2517 0.1943 -0.0134 -0.0081 -0.0259 1094 TYR A CB  
1687 C CG  . TYR A 228 ? 0.1583 0.2400 0.1906 -0.0140 -0.0075 -0.0251 1094 TYR A CG  
1688 C CD1 . TYR A 228 ? 0.1780 0.2539 0.2072 -0.0129 -0.0097 -0.0270 1094 TYR A CD1 
1689 C CD2 . TYR A 228 ? 0.1542 0.2365 0.1914 -0.0158 -0.0050 -0.0227 1094 TYR A CD2 
1690 C CE1 . TYR A 228 ? 0.1758 0.2473 0.2065 -0.0145 -0.0093 -0.0258 1094 TYR A CE1 
1691 C CE2 . TYR A 228 ? 0.1608 0.2393 0.1998 -0.0169 -0.0041 -0.0223 1094 TYR A CE2 
1692 C CZ  . TYR A 228 ? 0.1671 0.2406 0.2023 -0.0165 -0.0060 -0.0237 1094 TYR A CZ  
1693 O OH  . TYR A 228 ? 0.1860 0.2568 0.2223 -0.0184 -0.0051 -0.0229 1094 TYR A OH  
1694 N N   . PRO A 229 ? 0.1611 0.2656 0.1910 -0.0156 -0.0056 -0.0234 1095 PRO A N   
1695 C CA  . PRO A 229 ? 0.1581 0.2592 0.1933 -0.0171 -0.0043 -0.0204 1095 PRO A CA  
1696 C C   . PRO A 229 ? 0.1471 0.2483 0.1823 -0.0160 -0.0020 -0.0213 1095 PRO A C   
1697 O O   . PRO A 229 ? 0.1379 0.2443 0.1701 -0.0151 -0.0014 -0.0226 1095 PRO A O   
1698 C CB  . PRO A 229 ? 0.1651 0.2701 0.2031 -0.0203 -0.0052 -0.0166 1095 PRO A CB  
1699 C CG  . PRO A 229 ? 0.1720 0.2849 0.2048 -0.0207 -0.0058 -0.0175 1095 PRO A CG  
1700 C CD  . PRO A 229 ? 0.1671 0.2794 0.1952 -0.0177 -0.0062 -0.0220 1095 PRO A CD  
1701 N N   . LEU A 230 ? 0.1414 0.2377 0.1798 -0.0163 -0.0006 -0.0207 1096 LEU A N   
1702 C CA  . LEU A 230 ? 0.1468 0.2424 0.1850 -0.0159 0.0014  -0.0212 1096 LEU A CA  
1703 C C   . LEU A 230 ? 0.1445 0.2446 0.1843 -0.0177 0.0017  -0.0189 1096 LEU A C   
1704 O O   . LEU A 230 ? 0.1443 0.2448 0.1874 -0.0195 0.0006  -0.0164 1096 LEU A O   
1705 C CB  . LEU A 230 ? 0.1474 0.2376 0.1888 -0.0166 0.0028  -0.0211 1096 LEU A CB  
1706 C CG  . LEU A 230 ? 0.1558 0.2418 0.1965 -0.0163 0.0018  -0.0221 1096 LEU A CG  
1707 C CD1 . LEU A 230 ? 0.1620 0.2448 0.2055 -0.0177 0.0038  -0.0219 1096 LEU A CD1 
1708 C CD2 . LEU A 230 ? 0.1558 0.2405 0.1911 -0.0141 0.0002  -0.0245 1096 LEU A CD2 
1709 N N   . THR A 231 ? 0.1438 0.2473 0.1811 -0.0173 0.0026  -0.0194 1097 THR A N   
1710 C CA  . THR A 231 ? 0.1452 0.2532 0.1831 -0.0197 0.0024  -0.0167 1097 THR A CA  
1711 C C   . THR A 231 ? 0.1307 0.2374 0.1683 -0.0199 0.0040  -0.0168 1097 THR A C   
1712 O O   . THR A 231 ? 0.1360 0.2414 0.1714 -0.0181 0.0051  -0.0191 1097 THR A O   
1713 C CB  . THR A 231 ? 0.1491 0.2658 0.1836 -0.0202 0.0013  -0.0165 1097 THR A CB  
1714 O OG1 . THR A 231 ? 0.1672 0.2866 0.1983 -0.0171 0.0021  -0.0201 1097 THR A OG1 
1715 C CG2 . THR A 231 ? 0.1576 0.2756 0.1921 -0.0211 -0.0005 -0.0158 1097 THR A CG2 
1716 N N   . PHE A 232 ? 0.1353 0.2420 0.1750 -0.0224 0.0035  -0.0142 1098 PHE A N   
1717 C CA  . PHE A 232 ? 0.1368 0.2413 0.1766 -0.0234 0.0046  -0.0138 1098 PHE A CA  
1718 C C   . PHE A 232 ? 0.1477 0.2588 0.1852 -0.0257 0.0034  -0.0113 1098 PHE A C   
1719 O O   . PHE A 232 ? 0.1535 0.2696 0.1910 -0.0277 0.0014  -0.0089 1098 PHE A O   
1720 C CB  . PHE A 232 ? 0.1416 0.2398 0.1859 -0.0245 0.0045  -0.0129 1098 PHE A CB  
1721 C CG  . PHE A 232 ? 0.1477 0.2407 0.1950 -0.0229 0.0060  -0.0152 1098 PHE A CG  
1722 C CD1 . PHE A 232 ? 0.1377 0.2304 0.1884 -0.0224 0.0049  -0.0148 1098 PHE A CD1 
1723 C CD2 . PHE A 232 ? 0.1563 0.2456 0.2029 -0.0223 0.0084  -0.0176 1098 PHE A CD2 
1724 C CE1 . PHE A 232 ? 0.1455 0.2345 0.1994 -0.0214 0.0063  -0.0166 1098 PHE A CE1 
1725 C CE2 . PHE A 232 ? 0.1513 0.2373 0.2006 -0.0216 0.0099  -0.0195 1098 PHE A CE2 
1726 C CZ  . PHE A 232 ? 0.1540 0.2402 0.2071 -0.0210 0.0089  -0.0190 1098 PHE A CZ  
1727 N N   . GLY A 233 ? 0.1552 0.2666 0.1907 -0.0261 0.0043  -0.0115 1099 GLY A N   
1728 C CA  . GLY A 233 ? 0.1712 0.2882 0.2052 -0.0291 0.0030  -0.0085 1099 GLY A CA  
1729 C C   . GLY A 233 ? 0.1807 0.2932 0.2175 -0.0323 0.0007  -0.0053 1099 GLY A C   
1730 O O   . GLY A 233 ? 0.1826 0.2876 0.2230 -0.0314 0.0008  -0.0063 1099 GLY A O   
1731 N N   . GLY A 234 ? 0.1856 0.3029 0.2210 -0.0361 -0.0015 -0.0016 1100 GLY A N   
1732 C CA  . GLY A 234 ? 0.2117 0.3246 0.2497 -0.0396 -0.0050 0.0020  1100 GLY A CA  
1733 C C   . GLY A 234 ? 0.2256 0.3294 0.2648 -0.0398 -0.0049 0.0011  1100 GLY A C   
1734 O O   . GLY A 234 ? 0.2216 0.3195 0.2639 -0.0417 -0.0080 0.0031  1100 GLY A O   
1735 N N   . GLY A 235 ? 0.2183 0.3210 0.2552 -0.0379 -0.0019 -0.0017 1101 GLY A N   
1736 C CA  . GLY A 235 ? 0.2148 0.3092 0.2519 -0.0383 -0.0015 -0.0031 1101 GLY A CA  
1737 C C   . GLY A 235 ? 0.2140 0.3106 0.2476 -0.0419 -0.0033 -0.0002 1101 GLY A C   
1738 O O   . GLY A 235 ? 0.1984 0.3018 0.2307 -0.0450 -0.0059 0.0037  1101 GLY A O   
1739 N N   . THR A 236 ? 0.2087 0.3006 0.2403 -0.0417 -0.0017 -0.0023 1102 THR A N   
1740 C CA  . THR A 236 ? 0.2238 0.3152 0.2520 -0.0453 -0.0035 0.0000  1102 THR A CA  
1741 C C   . THR A 236 ? 0.2151 0.2952 0.2441 -0.0454 -0.0037 -0.0025 1102 THR A C   
1742 O O   . THR A 236 ? 0.2288 0.3051 0.2580 -0.0428 -0.0003 -0.0068 1102 THR A O   
1743 C CB  . THR A 236 ? 0.2216 0.3196 0.2458 -0.0450 -0.0014 -0.0003 1102 THR A CB  
1744 O OG1 . THR A 236 ? 0.2123 0.3213 0.2365 -0.0444 -0.0013 0.0012  1102 THR A OG1 
1745 C CG2 . THR A 236 ? 0.2328 0.3301 0.2536 -0.0490 -0.0033 0.0021  1102 THR A CG2 
1746 N N   . LYS A 237 ? 0.2224 0.2978 0.2519 -0.0487 -0.0079 0.0001  1103 LYS A N   
1747 C CA  . LYS A 237 ? 0.2396 0.3041 0.2695 -0.0490 -0.0087 -0.0026 1103 LYS A CA  
1748 C C   . LYS A 237 ? 0.2460 0.3105 0.2700 -0.0520 -0.0088 -0.0016 1103 LYS A C   
1749 O O   . LYS A 237 ? 0.2244 0.2929 0.2460 -0.0561 -0.0123 0.0033  1103 LYS A O   
1750 C CB  . LYS A 237 ? 0.2737 0.3317 0.3074 -0.0508 -0.0141 -0.0003 1103 LYS A CB  
1751 C CG  . LYS A 237 ? 0.3118 0.3581 0.3470 -0.0499 -0.0150 -0.0045 1103 LYS A CG  
1752 C CD  . LYS A 237 ? 0.3670 0.4059 0.4067 -0.0514 -0.0215 -0.0022 1103 LYS A CD  
1753 C CE  . LYS A 237 ? 0.4280 0.4551 0.4680 -0.0513 -0.0235 -0.0061 1103 LYS A CE  
1754 N NZ  . LYS A 237 ? 0.4687 0.4922 0.5136 -0.0458 -0.0192 -0.0136 1103 LYS A NZ  
1755 N N   . LEU A 238 ? 0.2446 0.3056 0.2661 -0.0505 -0.0052 -0.0059 1104 LEU A N   
1756 C CA  . LEU A 238 ? 0.2395 0.2999 0.2552 -0.0535 -0.0052 -0.0053 1104 LEU A CA  
1757 C C   . LEU A 238 ? 0.2609 0.3103 0.2757 -0.0554 -0.0077 -0.0071 1104 LEU A C   
1758 O O   . LEU A 238 ? 0.2546 0.2972 0.2719 -0.0526 -0.0057 -0.0125 1104 LEU A O   
1759 C CB  . LEU A 238 ? 0.2380 0.3003 0.2512 -0.0514 -0.0004 -0.0087 1104 LEU A CB  
1760 C CG  . LEU A 238 ? 0.2437 0.3054 0.2510 -0.0544 -0.0003 -0.0082 1104 LEU A CG  
1761 C CD1 . LEU A 238 ? 0.2489 0.3195 0.2545 -0.0570 -0.0028 -0.0027 1104 LEU A CD1 
1762 C CD2 . LEU A 238 ? 0.2503 0.3122 0.2553 -0.0527 0.0037  -0.0118 1104 LEU A CD2 
1763 N N   . GLU A 239 ? 0.2832 0.3313 0.2947 -0.0599 -0.0119 -0.0031 1105 GLU A N   
1764 C CA  . GLU A 239 ? 0.3191 0.3558 0.3295 -0.0621 -0.0156 -0.0044 1105 GLU A CA  
1765 C C   . GLU A 239 ? 0.3232 0.3588 0.3266 -0.0663 -0.0165 -0.0029 1105 GLU A C   
1766 O O   . GLU A 239 ? 0.2891 0.3340 0.2898 -0.0681 -0.0156 0.0007  1105 GLU A O   
1767 C CB  . GLU A 239 ? 0.3577 0.3920 0.3712 -0.0647 -0.0221 0.0004  1105 GLU A CB  
1768 C CG  . GLU A 239 ? 0.3904 0.4267 0.4106 -0.0615 -0.0223 0.0004  1105 GLU A CG  
1769 C CD  . GLU A 239 ? 0.4221 0.4573 0.4446 -0.0652 -0.0294 0.0065  1105 GLU A CD  
1770 O OE1 . GLU A 239 ? 0.4654 0.4918 0.4929 -0.0637 -0.0328 0.0048  1105 GLU A OE1 
1771 O OE2 . GLU A 239 ? 0.4774 0.5209 0.4969 -0.0698 -0.0319 0.0129  1105 GLU A OE2 
1772 N N   . MET A 240 ? 0.3627 0.3873 0.3639 -0.0680 -0.0189 -0.0056 1106 MET A N   
1773 C CA  . MET A 240 ? 0.4362 0.4578 0.4302 -0.0728 -0.0208 -0.0040 1106 MET A CA  
1774 C C   . MET A 240 ? 0.4066 0.4313 0.3994 -0.0781 -0.0270 0.0039  1106 MET A C   
1775 O O   . MET A 240 ? 0.3644 0.3843 0.3605 -0.0789 -0.0317 0.0057  1106 MET A O   
1776 C CB  . MET A 240 ? 0.5085 0.5164 0.5006 -0.0729 -0.0222 -0.0096 1106 MET A CB  
1777 C CG  . MET A 240 ? 0.6060 0.6121 0.5957 -0.0702 -0.0162 -0.0168 1106 MET A CG  
1778 S SD  . MET A 240 ? 0.7308 0.7413 0.7114 -0.0749 -0.0144 -0.0145 1106 MET A SD  
1779 C CE  . MET A 240 ? 0.6482 0.6715 0.6313 -0.0715 -0.0088 -0.0136 1106 MET A CE  
1780 N N   . LYS A 241 ? 0.4411 0.4736 0.4294 -0.0819 -0.0271 0.0083  1107 LYS A N   
1781 C CA  . LYS A 241 ? 0.4892 0.5236 0.4746 -0.0884 -0.0333 0.0156  1107 LYS A CA  
1782 C C   . LYS A 241 ? 0.5237 0.5430 0.5063 -0.0915 -0.0386 0.0143  1107 LYS A C   
1783 O O   . LYS A 241 ? 0.5273 0.5388 0.5058 -0.0909 -0.0366 0.0092  1107 LYS A O   
1784 C CB  . LYS A 241 ? 0.5331 0.5771 0.5142 -0.0916 -0.0321 0.0191  1107 LYS A CB  
1785 C CG  . LYS A 241 ? 0.5969 0.6574 0.5812 -0.0906 -0.0301 0.0230  1107 LYS A CG  
1786 C CD  . LYS A 241 ? 0.6495 0.7208 0.6310 -0.0934 -0.0297 0.0267  1107 LYS A CD  
1787 C CE  . LYS A 241 ? 0.6803 0.7673 0.6662 -0.0899 -0.0261 0.0276  1107 LYS A CE  
1788 N NZ  . LYS A 241 ? 0.7171 0.8112 0.7016 -0.0891 -0.0235 0.0273  1107 LYS A NZ  
1789 N N   . GLN B 1   ? 0.5724 0.6577 0.5067 -0.1043 -0.0818 0.0671  1    GLN H N   
1790 C CA  . GLN B 1   ? 0.5860 0.6488 0.5024 -0.1112 -0.0849 0.0644  1    GLN H CA  
1791 C C   . GLN B 1   ? 0.5443 0.6074 0.4666 -0.1017 -0.0827 0.0605  1    GLN H C   
1792 O O   . GLN B 1   ? 0.5494 0.6278 0.4744 -0.1042 -0.0841 0.0660  1    GLN H O   
1793 C CB  . GLN B 1   ? 0.6359 0.7003 0.5367 -0.1293 -0.0912 0.0732  1    GLN H CB  
1794 C CG  . GLN B 1   ? 0.6956 0.7262 0.5714 -0.1373 -0.0944 0.0689  1    GLN H CG  
1795 C CD  . GLN B 1   ? 0.7378 0.7424 0.6088 -0.1276 -0.0907 0.0586  1    GLN H CD  
1796 O OE1 . GLN B 1   ? 0.7683 0.7783 0.6518 -0.1192 -0.0871 0.0556  1    GLN H OE1 
1797 N NE2 . GLN B 1   ? 0.7931 0.7693 0.6453 -0.1282 -0.0914 0.0535  1    GLN H NE2 
1798 N N   . VAL B 2   ? 0.4793 0.5253 0.4028 -0.0912 -0.0793 0.0511  2    VAL H N   
1799 C CA  . VAL B 2   ? 0.4716 0.5152 0.4007 -0.0812 -0.0769 0.0461  2    VAL H CA  
1800 C C   . VAL B 2   ? 0.4697 0.4944 0.3803 -0.0887 -0.0801 0.0454  2    VAL H C   
1801 O O   . VAL B 2   ? 0.4700 0.4728 0.3634 -0.0950 -0.0819 0.0435  2    VAL H O   
1802 C CB  . VAL B 2   ? 0.4456 0.4788 0.3821 -0.0684 -0.0725 0.0373  2    VAL H CB  
1803 C CG1 . VAL B 2   ? 0.4434 0.4686 0.3808 -0.0603 -0.0709 0.0317  2    VAL H CG1 
1804 C CG2 . VAL B 2   ? 0.4412 0.4923 0.3946 -0.0610 -0.0695 0.0382  2    VAL H CG2 
1805 N N   . GLN B 3   ? 0.4645 0.4956 0.3773 -0.0870 -0.0805 0.0465  3    GLN H N   
1806 C CA  . GLN B 3   ? 0.4893 0.5008 0.3846 -0.0922 -0.0830 0.0448  3    GLN H CA  
1807 C C   . GLN B 3   ? 0.4436 0.4556 0.3466 -0.0813 -0.0804 0.0400  3    GLN H C   
1808 O O   . GLN B 3   ? 0.4360 0.4691 0.3552 -0.0749 -0.0785 0.0420  3    GLN H O   
1809 C CB  . GLN B 3   ? 0.5432 0.5638 0.4290 -0.1072 -0.0883 0.0542  3    GLN H CB  
1810 C CG  . GLN B 3   ? 0.6345 0.6278 0.4951 -0.1167 -0.0921 0.0530  3    GLN H CG  
1811 C CD  . GLN B 3   ? 0.6654 0.6524 0.5083 -0.1339 -0.0975 0.0597  3    GLN H CD  
1812 O OE1 . GLN B 3   ? 0.7290 0.7167 0.5727 -0.1362 -0.0974 0.0605  3    GLN H OE1 
1813 N NE2 . GLN B 3   ? 0.7227 0.7037 0.5490 -0.1467 -0.1025 0.0648  3    GLN H NE2 
1814 N N   . LEU B 4   ? 0.4426 0.4310 0.3328 -0.0790 -0.0801 0.0342  4    LEU H N   
1815 C CA  . LEU B 4   ? 0.4305 0.4164 0.3233 -0.0714 -0.0787 0.0305  4    LEU H CA  
1816 C C   . LEU B 4   ? 0.4473 0.4154 0.3183 -0.0809 -0.0824 0.0321  4    LEU H C   
1817 O O   . LEU B 4   ? 0.4413 0.3836 0.2942 -0.0821 -0.0827 0.0284  4    LEU H O   
1818 C CB  . LEU B 4   ? 0.4313 0.4065 0.3296 -0.0583 -0.0745 0.0220  4    LEU H CB  
1819 C CG  . LEU B 4   ? 0.4211 0.4114 0.3393 -0.0490 -0.0711 0.0200  4    LEU H CG  
1820 C CD1 . LEU B 4   ? 0.4238 0.4035 0.3455 -0.0380 -0.0678 0.0126  4    LEU H CD1 
1821 C CD2 . LEU B 4   ? 0.4035 0.4170 0.3373 -0.0453 -0.0705 0.0233  4    LEU H CD2 
1822 N N   . GLN B 5   ? 0.4534 0.4346 0.3251 -0.0870 -0.0851 0.0378  5    GLN H N   
1823 C CA  . GLN B 5   ? 0.4881 0.4547 0.3385 -0.0987 -0.0896 0.0410  5    GLN H CA  
1824 C C   . GLN B 5   ? 0.4602 0.4212 0.3110 -0.0909 -0.0880 0.0367  5    GLN H C   
1825 O O   . GLN B 5   ? 0.4521 0.4346 0.3191 -0.0860 -0.0869 0.0387  5    GLN H O   
1826 C CB  . GLN B 5   ? 0.5176 0.5053 0.3688 -0.1122 -0.0940 0.0515  5    GLN H CB  
1827 C CG  . GLN B 5   ? 0.5753 0.5503 0.4049 -0.1257 -0.0993 0.0558  5    GLN H CG  
1828 C CD  . GLN B 5   ? 0.6592 0.6003 0.4602 -0.1349 -0.1023 0.0538  5    GLN H CD  
1829 O OE1 . GLN B 5   ? 0.6691 0.6013 0.4667 -0.1348 -0.1015 0.0518  5    GLN H OE1 
1830 N NE2 . GLN B 5   ? 0.6928 0.6129 0.4714 -0.1426 -0.1056 0.0541  5    GLN H NE2 
1831 N N   . GLN B 6   ? 0.4468 0.3797 0.2799 -0.0886 -0.0876 0.0312  6    GLN H N   
1832 C CA  . GLN B 6   ? 0.4456 0.3718 0.2776 -0.0811 -0.0862 0.0272  6    GLN H CA  
1833 C C   . GLN B 6   ? 0.4675 0.3855 0.2812 -0.0932 -0.0909 0.0320  6    GLN H C   
1834 O O   . GLN B 6   ? 0.4861 0.3940 0.2813 -0.1076 -0.0954 0.0370  6    GLN H O   
1835 C CB  . GLN B 6   ? 0.4405 0.3437 0.2645 -0.0702 -0.0827 0.0193  6    GLN H CB  
1836 C CG  . GLN B 6   ? 0.4344 0.3470 0.2763 -0.0596 -0.0785 0.0153  6    GLN H CG  
1837 C CD  . GLN B 6   ? 0.4361 0.3307 0.2723 -0.0482 -0.0749 0.0086  6    GLN H CD  
1838 O OE1 . GLN B 6   ? 0.4234 0.3128 0.2604 -0.0439 -0.0726 0.0063  6    GLN H OE1 
1839 N NE2 . GLN B 6   ? 0.4351 0.3209 0.2654 -0.0431 -0.0741 0.0061  6    GLN H NE2 
1840 N N   . SER B 7   ? 0.4807 0.4013 0.2982 -0.0877 -0.0900 0.0303  7    SER H N   
1841 C CA  . SER B 7   ? 0.5008 0.4124 0.3012 -0.0976 -0.0941 0.0340  7    SER H CA  
1842 C C   . SER B 7   ? 0.5410 0.4149 0.3115 -0.0996 -0.0950 0.0300  7    SER H C   
1843 O O   . SER B 7   ? 0.5346 0.3916 0.3006 -0.0903 -0.0915 0.0239  7    SER H O   
1844 C CB  . SER B 7   ? 0.4698 0.3975 0.2851 -0.0900 -0.0924 0.0334  7    SER H CB  
1845 O OG  . SER B 7   ? 0.4409 0.3645 0.2666 -0.0740 -0.0875 0.0253  7    SER H OG  
1846 N N   . ASP B 8   ? 0.5802 0.4412 0.3303 -0.1107 -0.0994 0.0337  8    ASP H N   
1847 C CA  . ASP B 8   ? 0.6319 0.4545 0.3468 -0.1171 -0.1018 0.0322  8    ASP H CA  
1848 C C   . ASP B 8   ? 0.6324 0.4355 0.3415 -0.1016 -0.0972 0.0243  8    ASP H C   
1849 O O   . ASP B 8   ? 0.6059 0.4274 0.3371 -0.0901 -0.0938 0.0214  8    ASP H O   
1850 C CB  . ASP B 8   ? 0.6823 0.5012 0.3794 -0.1344 -0.1083 0.0395  8    ASP H CB  
1851 C CG  . ASP B 8   ? 0.7328 0.5659 0.4282 -0.1524 -0.1139 0.0487  8    ASP H CG  
1852 O OD1 . ASP B 8   ? 0.7395 0.5775 0.4411 -0.1524 -0.1130 0.0488  8    ASP H OD1 
1853 O OD2 . ASP B 8   ? 0.7822 0.6222 0.4700 -0.1668 -0.1193 0.0561  8    ASP H OD2 
1854 N N   . ALA B 9   ? 0.6675 0.4342 0.3461 -0.1015 -0.0971 0.0214  9    ALA H N   
1855 C CA  . ALA B 9   ? 0.7037 0.4471 0.3690 -0.0883 -0.0932 0.0152  9    ALA H CA  
1856 C C   . ALA B 9   ? 0.6889 0.4405 0.3592 -0.0878 -0.0942 0.0158  9    ALA H C   
1857 O O   . ALA B 9   ? 0.6818 0.4414 0.3489 -0.1021 -0.0994 0.0218  9    ALA H O   
1858 C CB  . ALA B 9   ? 0.7498 0.4507 0.3748 -0.0922 -0.0945 0.0144  9    ALA H CB  
1859 N N   . GLU B 10  ? 0.6796 0.4317 0.3589 -0.0719 -0.0894 0.0103  10   GLU H N   
1860 C CA  . GLU B 10  ? 0.6909 0.4520 0.3781 -0.0682 -0.0892 0.0097  10   GLU H CA  
1861 C C   . GLU B 10  ? 0.7028 0.4334 0.3662 -0.0589 -0.0867 0.0054  10   GLU H C   
1862 O O   . GLU B 10  ? 0.6677 0.3875 0.3283 -0.0461 -0.0820 0.0011  10   GLU H O   
1863 C CB  . GLU B 10  ? 0.6903 0.4839 0.4136 -0.0563 -0.0855 0.0072  10   GLU H CB  
1864 C CG  . GLU B 10  ? 0.7071 0.5314 0.4539 -0.0632 -0.0873 0.0116  10   GLU H CG  
1865 C CD  . GLU B 10  ? 0.7376 0.5844 0.4974 -0.0685 -0.0897 0.0160  10   GLU H CD  
1866 O OE1 . GLU B 10  ? 0.7371 0.5733 0.4844 -0.0705 -0.0912 0.0162  10   GLU H OE1 
1867 O OE2 . GLU B 10  ? 0.7630 0.6377 0.5448 -0.0701 -0.0899 0.0193  10   GLU H OE2 
1868 N N   . LEU B 11  ? 0.7314 0.4510 0.3797 -0.0643 -0.0894 0.0069  11   LEU H N   
1869 C CA  . LEU B 11  ? 0.7676 0.4583 0.3920 -0.0557 -0.0872 0.0034  11   LEU H CA  
1870 C C   . LEU B 11  ? 0.7356 0.4444 0.3769 -0.0514 -0.0869 0.0028  11   LEU H C   
1871 O O   . LEU B 11  ? 0.7209 0.4407 0.3648 -0.0640 -0.0914 0.0073  11   LEU H O   
1872 C CB  . LEU B 11  ? 0.8347 0.4898 0.4185 -0.0699 -0.0921 0.0066  11   LEU H CB  
1873 C CG  . LEU B 11  ? 0.9021 0.5144 0.4488 -0.0617 -0.0894 0.0032  11   LEU H CG  
1874 C CD1 . LEU B 11  ? 0.8749 0.4889 0.4305 -0.0409 -0.0829 -0.0019 11   LEU H CD1 
1875 C CD2 . LEU B 11  ? 0.9368 0.5297 0.4665 -0.0623 -0.0886 0.0029  11   LEU H CD2 
1876 N N   . VAL B 12  ? 0.7366 0.4517 0.3911 -0.0346 -0.0818 -0.0019 12   VAL H N   
1877 C CA  . VAL B 12  ? 0.7309 0.4669 0.4058 -0.0294 -0.0811 -0.0028 12   VAL H CA  
1878 C C   . VAL B 12  ? 0.7527 0.4729 0.4176 -0.0147 -0.0770 -0.0071 12   VAL H C   
1879 O O   . VAL B 12  ? 0.7550 0.4551 0.4042 -0.0055 -0.0735 -0.0095 12   VAL H O   
1880 C CB  . VAL B 12  ? 0.7138 0.4868 0.4267 -0.0245 -0.0795 -0.0034 12   VAL H CB  
1881 C CG1 . VAL B 12  ? 0.6941 0.4870 0.4194 -0.0377 -0.0832 0.0016  12   VAL H CG1 
1882 C CG2 . VAL B 12  ? 0.7033 0.4802 0.4278 -0.0112 -0.0746 -0.0074 12   VAL H CG2 
1883 N N   . LYS B 13  ? 0.7812 0.5116 0.4551 -0.0123 -0.0773 -0.0075 13   LYS H N   
1884 C CA  . LYS B 13  ? 0.7943 0.5162 0.4634 0.0012  -0.0738 -0.0110 13   LYS H CA  
1885 C C   . LYS B 13  ? 0.7281 0.4740 0.4259 0.0153  -0.0694 -0.0142 13   LYS H C   
1886 O O   . LYS B 13  ? 0.6864 0.4597 0.4113 0.0131  -0.0702 -0.0137 13   LYS H O   
1887 C CB  . LYS B 13  ? 0.8161 0.5429 0.4862 -0.0035 -0.0765 -0.0097 13   LYS H CB  
1888 C CG  . LYS B 13  ? 0.8997 0.5957 0.5350 -0.0132 -0.0799 -0.0075 13   LYS H CG  
1889 C CD  . LYS B 13  ? 0.9704 0.6348 0.5782 -0.0014 -0.0763 -0.0105 13   LYS H CD  
1890 C CE  . LYS B 13  ? 1.0104 0.6546 0.5951 -0.0053 -0.0785 -0.0097 13   LYS H CE  
1891 N NZ  . LYS B 13  ? 1.0494 0.6661 0.6018 -0.0221 -0.0837 -0.0060 13   LYS H NZ  
1892 N N   . PRO B 14  ? 0.7310 0.4670 0.4222 0.0299  -0.0649 -0.0169 14   PRO H N   
1893 C CA  . PRO B 14  ? 0.6846 0.4440 0.4017 0.0424  -0.0615 -0.0192 14   PRO H CA  
1894 C C   . PRO B 14  ? 0.6315 0.4148 0.3714 0.0392  -0.0637 -0.0192 14   PRO H C   
1895 O O   . PRO B 14  ? 0.6131 0.3892 0.3432 0.0331  -0.0663 -0.0181 14   PRO H O   
1896 C CB  . PRO B 14  ? 0.7272 0.4700 0.4279 0.0567  -0.0572 -0.0207 14   PRO H CB  
1897 C CG  . PRO B 14  ? 0.7725 0.4790 0.4360 0.0536  -0.0572 -0.0197 14   PRO H CG  
1898 C CD  . PRO B 14  ? 0.7871 0.4886 0.4438 0.0352  -0.0629 -0.0174 14   PRO H CD  
1899 N N   . GLY B 15  ? 0.5715 0.3814 0.3398 0.0423  -0.0631 -0.0201 15   GLY H N   
1900 C CA  . GLY B 15  ? 0.5364 0.3690 0.3267 0.0410  -0.0647 -0.0203 15   GLY H CA  
1901 C C   . GLY B 15  ? 0.5228 0.3684 0.3231 0.0294  -0.0680 -0.0177 15   GLY H C   
1902 O O   . GLY B 15  ? 0.5322 0.3983 0.3524 0.0296  -0.0687 -0.0176 15   GLY H O   
1903 N N   . ALA B 16  ? 0.5393 0.3738 0.3258 0.0194  -0.0700 -0.0150 16   ALA H N   
1904 C CA  . ALA B 16  ? 0.5166 0.3666 0.3134 0.0084  -0.0730 -0.0114 16   ALA H CA  
1905 C C   . ALA B 16  ? 0.4972 0.3648 0.3143 0.0110  -0.0716 -0.0120 16   ALA H C   
1906 O O   . ALA B 16  ? 0.4628 0.3302 0.2855 0.0204  -0.0686 -0.0152 16   ALA H O   
1907 C CB  . ALA B 16  ? 0.5486 0.3817 0.3231 -0.0043 -0.0763 -0.0076 16   ALA H CB  
1908 N N   . SER B 17  ? 0.4696 0.3534 0.2976 0.0032  -0.0737 -0.0085 17   SER H N   
1909 C CA  . SER B 17  ? 0.4637 0.3630 0.3083 0.0034  -0.0729 -0.0081 17   SER H CA  
1910 C C   . SER B 17  ? 0.4637 0.3590 0.2987 -0.0079 -0.0752 -0.0039 17   SER H C   
1911 O O   . SER B 17  ? 0.4961 0.3826 0.3156 -0.0174 -0.0781 -0.0003 17   SER H O   
1912 C CB  . SER B 17  ? 0.4370 0.3598 0.3026 0.0058  -0.0728 -0.0073 17   SER H CB  
1913 O OG  . SER B 17  ? 0.4604 0.3856 0.3343 0.0161  -0.0709 -0.0115 17   SER H OG  
1914 N N   . VAL B 18  ? 0.4410 0.3425 0.2841 -0.0079 -0.0742 -0.0039 18   VAL H N   
1915 C CA  . VAL B 18  ? 0.4614 0.3628 0.2982 -0.0192 -0.0766 0.0005  18   VAL H CA  
1916 C C   . VAL B 18  ? 0.4182 0.3413 0.2764 -0.0170 -0.0754 0.0013  18   VAL H C   
1917 O O   . VAL B 18  ? 0.3874 0.3166 0.2588 -0.0072 -0.0727 -0.0026 18   VAL H O   
1918 C CB  . VAL B 18  ? 0.4990 0.3759 0.3145 -0.0223 -0.0767 -0.0002 18   VAL H CB  
1919 C CG1 . VAL B 18  ? 0.5414 0.3932 0.3314 -0.0248 -0.0780 -0.0006 18   VAL H CG1 
1920 C CG2 . VAL B 18  ? 0.4787 0.3527 0.3004 -0.0116 -0.0729 -0.0048 18   VAL H CG2 
1921 N N   . LYS B 19  ? 0.4271 0.3620 0.2877 -0.0262 -0.0777 0.0069  19   LYS H N   
1922 C CA  . LYS B 19  ? 0.4357 0.3890 0.3127 -0.0254 -0.0767 0.0086  19   LYS H CA  
1923 C C   . LYS B 19  ? 0.4426 0.3898 0.3096 -0.0352 -0.0785 0.0119  19   LYS H C   
1924 O O   . LYS B 19  ? 0.4472 0.3934 0.3030 -0.0468 -0.0820 0.0175  19   LYS H O   
1925 C CB  . LYS B 19  ? 0.4537 0.4301 0.3433 -0.0266 -0.0773 0.0136  19   LYS H CB  
1926 C CG  . LYS B 19  ? 0.4558 0.4516 0.3629 -0.0223 -0.0755 0.0150  19   LYS H CG  
1927 C CD  . LYS B 19  ? 0.4718 0.4855 0.3906 -0.0167 -0.0745 0.0172  19   LYS H CD  
1928 C CE  . LYS B 19  ? 0.4959 0.5307 0.4267 -0.0157 -0.0734 0.0222  19   LYS H CE  
1929 N NZ  . LYS B 19  ? 0.4941 0.5435 0.4336 -0.0085 -0.0719 0.0241  19   LYS H NZ  
1930 N N   . ILE B 20  ? 0.4314 0.3746 0.3020 -0.0310 -0.0765 0.0088  20   ILE H N   
1931 C CA  . ILE B 20  ? 0.4468 0.3833 0.3089 -0.0387 -0.0777 0.0110  20   ILE H CA  
1932 C C   . ILE B 20  ? 0.4062 0.3664 0.2865 -0.0393 -0.0773 0.0145  20   ILE H C   
1933 O O   . ILE B 20  ? 0.3850 0.3580 0.2824 -0.0296 -0.0746 0.0119  20   ILE H O   
1934 C CB  . ILE B 20  ? 0.4692 0.3874 0.3244 -0.0320 -0.0752 0.0055  20   ILE H CB  
1935 C CG1 . ILE B 20  ? 0.5240 0.4187 0.3600 -0.0295 -0.0750 0.0025  20   ILE H CG1 
1936 C CG2 . ILE B 20  ? 0.5112 0.4227 0.3584 -0.0389 -0.0761 0.0074  20   ILE H CG2 
1937 C CD1 . ILE B 20  ? 0.5309 0.4110 0.3620 -0.0195 -0.0715 -0.0024 20   ILE H CD1 
1938 N N   . SER B 21  ? 0.3954 0.3614 0.2711 -0.0503 -0.0800 0.0206  21   SER H N   
1939 C CA  . SER B 21  ? 0.3782 0.3671 0.2696 -0.0509 -0.0795 0.0249  21   SER H CA  
1940 C C   . SER B 21  ? 0.3912 0.3729 0.2796 -0.0534 -0.0792 0.0240  21   SER H C   
1941 O O   . SER B 21  ? 0.4037 0.3642 0.2742 -0.0591 -0.0807 0.0228  21   SER H O   
1942 C CB  . SER B 21  ? 0.3864 0.3934 0.2782 -0.0605 -0.0825 0.0338  21   SER H CB  
1943 O OG  . SER B 21  ? 0.4061 0.4025 0.2799 -0.0749 -0.0868 0.0383  21   SER H OG  
1944 N N   . CYS B 22  ? 0.3906 0.3890 0.2950 -0.0489 -0.0772 0.0248  22   CYS H N   
1945 C CA  . CYS B 22  ? 0.4051 0.4013 0.3106 -0.0502 -0.0765 0.0243  22   CYS H CA  
1946 C C   . CYS B 22  ? 0.3866 0.4072 0.3041 -0.0531 -0.0768 0.0310  22   CYS H C   
1947 O O   . CYS B 22  ? 0.3924 0.4272 0.3250 -0.0439 -0.0740 0.0302  22   CYS H O   
1948 C CB  . CYS B 22  ? 0.3977 0.3877 0.3116 -0.0384 -0.0727 0.0169  22   CYS H CB  
1949 S SG  . CYS B 22  ? 0.4354 0.4245 0.3522 -0.0392 -0.0716 0.0164  22   CYS H SG  
1950 N N   . LYS B 23  ? 0.4003 0.4253 0.3097 -0.0655 -0.0802 0.0380  23   LYS H N   
1951 C CA  . LYS B 23  ? 0.4044 0.4561 0.3249 -0.0685 -0.0806 0.0462  23   LYS H CA  
1952 C C   . LYS B 23  ? 0.3726 0.4257 0.2979 -0.0679 -0.0793 0.0456  23   LYS H C   
1953 O O   . LYS B 23  ? 0.3641 0.4027 0.2769 -0.0762 -0.0815 0.0454  23   LYS H O   
1954 C CB  . LYS B 23  ? 0.4435 0.5032 0.3539 -0.0832 -0.0854 0.0554  23   LYS H CB  
1955 C CG  . LYS B 23  ? 0.4903 0.5770 0.4093 -0.0886 -0.0863 0.0652  23   LYS H CG  
1956 C CD  . LYS B 23  ? 0.5039 0.6162 0.4425 -0.0761 -0.0821 0.0676  23   LYS H CD  
1957 C CE  . LYS B 23  ? 0.5575 0.6983 0.5001 -0.0819 -0.0839 0.0795  23   LYS H CE  
1958 N NZ  . LYS B 23  ? 0.5817 0.7376 0.5233 -0.0930 -0.0867 0.0885  23   LYS H NZ  
1959 N N   . ALA B 24  ? 0.3476 0.4166 0.2890 -0.0582 -0.0758 0.0454  24   ALA H N   
1960 C CA  . ALA B 24  ? 0.3656 0.4358 0.3128 -0.0559 -0.0741 0.0442  24   ALA H CA  
1961 C C   . ALA B 24  ? 0.3652 0.4578 0.3167 -0.0624 -0.0754 0.0538  24   ALA H C   
1962 O O   . ALA B 24  ? 0.3800 0.4932 0.3382 -0.0608 -0.0751 0.0601  24   ALA H O   
1963 C CB  . ALA B 24  ? 0.3555 0.4274 0.3155 -0.0417 -0.0698 0.0383  24   ALA H CB  
1964 N N   . SER B 25  ? 0.3844 0.4742 0.3322 -0.0690 -0.0766 0.0554  25   SER H N   
1965 C CA  . SER B 25  ? 0.3616 0.4747 0.3150 -0.0743 -0.0775 0.0648  25   SER H CA  
1966 C C   . SER B 25  ? 0.3527 0.4610 0.3089 -0.0728 -0.0760 0.0621  25   SER H C   
1967 O O   . SER B 25  ? 0.3467 0.4320 0.2961 -0.0720 -0.0757 0.0544  25   SER H O   
1968 C CB  . SER B 25  ? 0.3998 0.5185 0.3416 -0.0907 -0.0829 0.0736  25   SER H CB  
1969 O OG  . SER B 25  ? 0.4256 0.5181 0.3495 -0.1010 -0.0863 0.0701  25   SER H OG  
1970 N N   . GLY B 26  ? 0.3469 0.4773 0.3118 -0.0729 -0.0753 0.0692  26   GLY H N   
1971 C CA  . GLY B 26  ? 0.3436 0.4732 0.3107 -0.0736 -0.0745 0.0688  26   GLY H CA  
1972 C C   . GLY B 26  ? 0.3156 0.4416 0.2935 -0.0590 -0.0695 0.0617  26   GLY H C   
1973 O O   . GLY B 26  ? 0.2968 0.4188 0.2761 -0.0589 -0.0686 0.0600  26   GLY H O   
1974 N N   . TYR B 27  ? 0.2958 0.4246 0.2807 -0.0476 -0.0665 0.0587  27   TYR H N   
1975 C CA  . TYR B 27  ? 0.2852 0.4109 0.2788 -0.0343 -0.0622 0.0529  27   TYR H CA  
1976 C C   . TYR B 27  ? 0.2963 0.4316 0.2955 -0.0238 -0.0597 0.0537  27   TYR H C   
1977 O O   . TYR B 27  ? 0.2923 0.4346 0.2890 -0.0269 -0.0612 0.0576  27   TYR H O   
1978 C CB  . TYR B 27  ? 0.2875 0.3886 0.2774 -0.0327 -0.0619 0.0429  27   TYR H CB  
1979 C CG  . TYR B 27  ? 0.2836 0.3716 0.2693 -0.0306 -0.0624 0.0375  27   TYR H CG  
1980 C CD1 . TYR B 27  ? 0.2910 0.3681 0.2654 -0.0395 -0.0655 0.0374  27   TYR H CD1 
1981 C CD2 . TYR B 27  ? 0.2796 0.3658 0.2712 -0.0199 -0.0599 0.0329  27   TYR H CD2 
1982 C CE1 . TYR B 27  ? 0.3007 0.3661 0.2710 -0.0369 -0.0657 0.0328  27   TYR H CE1 
1983 C CE2 . TYR B 27  ? 0.2839 0.3593 0.2720 -0.0179 -0.0604 0.0284  27   TYR H CE2 
1984 C CZ  . TYR B 27  ? 0.2928 0.3585 0.2708 -0.0261 -0.0632 0.0283  27   TYR H CZ  
1985 O OH  . TYR B 27  ? 0.3051 0.3607 0.2796 -0.0234 -0.0634 0.0241  27   TYR H OH  
1986 N N   . ILE B 28  ? 0.2686 0.4024 0.2736 -0.0121 -0.0561 0.0500  28   ILE H N   
1987 C CA  . ILE B 28  ? 0.2661 0.4062 0.2740 -0.0010 -0.0534 0.0506  28   ILE H CA  
1988 C C   . ILE B 28  ? 0.2640 0.3868 0.2688 0.0004  -0.0543 0.0428  28   ILE H C   
1989 O O   . ILE B 28  ? 0.2316 0.3380 0.2362 0.0028  -0.0539 0.0352  28   ILE H O   
1990 C CB  . ILE B 28  ? 0.2772 0.4198 0.2890 0.0106  -0.0495 0.0501  28   ILE H CB  
1991 C CG1 . ILE B 28  ? 0.3008 0.4627 0.3156 0.0093  -0.0485 0.0589  28   ILE H CG1 
1992 C CG2 . ILE B 28  ? 0.2889 0.4333 0.3001 0.0221  -0.0468 0.0501  28   ILE H CG2 
1993 C CD1 . ILE B 28  ? 0.3175 0.4778 0.3341 0.0196  -0.0448 0.0577  28   ILE H CD1 
1994 N N   . PHE B 29  ? 0.2509 0.3791 0.2535 -0.0009 -0.0554 0.0456  29   PHE H N   
1995 C CA  . PHE B 29  ? 0.2633 0.3765 0.2623 -0.0005 -0.0565 0.0391  29   PHE H CA  
1996 C C   . PHE B 29  ? 0.2469 0.3487 0.2481 0.0101  -0.0541 0.0320  29   PHE H C   
1997 O O   . PHE B 29  ? 0.2511 0.3369 0.2503 0.0096  -0.0551 0.0250  29   PHE H O   
1998 C CB  . PHE B 29  ? 0.2831 0.4074 0.2803 -0.0018 -0.0575 0.0444  29   PHE H CB  
1999 C CG  . PHE B 29  ? 0.2860 0.3961 0.2786 -0.0026 -0.0589 0.0388  29   PHE H CG  
2000 C CD1 . PHE B 29  ? 0.3010 0.3962 0.2868 -0.0111 -0.0617 0.0352  29   PHE H CD1 
2001 C CD2 . PHE B 29  ? 0.3009 0.4130 0.2947 0.0052  -0.0575 0.0380  29   PHE H CD2 
2002 C CE1 . PHE B 29  ? 0.3092 0.3921 0.2900 -0.0112 -0.0628 0.0307  29   PHE H CE1 
2003 C CE2 . PHE B 29  ? 0.2920 0.3922 0.2816 0.0043  -0.0590 0.0334  29   PHE H CE2 
2004 C CZ  . PHE B 29  ? 0.3042 0.3901 0.2878 -0.0036 -0.0615 0.0296  29   PHE H CZ  
2005 N N   . ALA B 30  ? 0.2409 0.3506 0.2447 0.0196  -0.0512 0.0344  30   ALA H N   
2006 C CA  . ALA B 30  ? 0.2489 0.3473 0.2521 0.0296  -0.0492 0.0288  30   ALA H CA  
2007 C C   . ALA B 30  ? 0.2448 0.3289 0.2488 0.0282  -0.0496 0.0223  30   ALA H C   
2008 O O   . ALA B 30  ? 0.2599 0.3326 0.2624 0.0339  -0.0490 0.0173  30   ALA H O   
2009 C CB  . ALA B 30  ? 0.2605 0.3692 0.2632 0.0397  -0.0458 0.0338  30   ALA H CB  
2010 N N   . ASP B 31  ? 0.2416 0.3275 0.2474 0.0214  -0.0504 0.0235  31   ASP H N   
2011 C CA  . ASP B 31  ? 0.2440 0.3201 0.2513 0.0217  -0.0500 0.0190  31   ASP H CA  
2012 C C   . ASP B 31  ? 0.2313 0.2939 0.2378 0.0164  -0.0519 0.0129  31   ASP H C   
2013 O O   . ASP B 31  ? 0.2206 0.2759 0.2286 0.0165  -0.0516 0.0095  31   ASP H O   
2014 C CB  . ASP B 31  ? 0.2660 0.3522 0.2754 0.0199  -0.0489 0.0240  31   ASP H CB  
2015 C CG  . ASP B 31  ? 0.2667 0.3631 0.2761 0.0290  -0.0459 0.0288  31   ASP H CG  
2016 O OD1 . ASP B 31  ? 0.3138 0.4078 0.3203 0.0369  -0.0446 0.0281  31   ASP H OD1 
2017 O OD2 . ASP B 31  ? 0.3115 0.4168 0.3227 0.0286  -0.0448 0.0331  31   ASP H OD2 
2018 N N   . HIS B 32  ? 0.2232 0.2822 0.2270 0.0127  -0.0536 0.0118  32   HIS H N   
2019 C CA  . HIS B 32  ? 0.2187 0.2649 0.2205 0.0096  -0.0548 0.0065  32   HIS H CA  
2020 C C   . HIS B 32  ? 0.2218 0.2634 0.2205 0.0106  -0.0558 0.0045  32   HIS H C   
2021 O O   . HIS B 32  ? 0.2238 0.2715 0.2201 0.0088  -0.0565 0.0080  32   HIS H O   
2022 C CB  . HIS B 32  ? 0.2131 0.2567 0.2107 0.0015  -0.0560 0.0081  32   HIS H CB  
2023 C CG  . HIS B 32  ? 0.2137 0.2617 0.2139 -0.0002 -0.0552 0.0102  32   HIS H CG  
2024 N ND1 . HIS B 32  ? 0.2125 0.2545 0.2158 0.0019  -0.0542 0.0066  32   HIS H ND1 
2025 C CD2 . HIS B 32  ? 0.2108 0.2704 0.2118 -0.0034 -0.0552 0.0161  32   HIS H CD2 
2026 C CE1 . HIS B 32  ? 0.2023 0.2505 0.2078 0.0004  -0.0535 0.0096  32   HIS H CE1 
2027 N NE2 . HIS B 32  ? 0.1967 0.2562 0.2009 -0.0028 -0.0540 0.0156  32   HIS H NE2 
2028 N N   . ALA B 33  ? 0.2178 0.2499 0.2168 0.0129  -0.0561 -0.0005 33   ALA H N   
2029 C CA  . ALA B 33  ? 0.2222 0.2486 0.2181 0.0136  -0.0570 -0.0030 33   ALA H CA  
2030 C C   . ALA B 33  ? 0.2255 0.2465 0.2142 0.0077  -0.0580 -0.0021 33   ALA H C   
2031 O O   . ALA B 33  ? 0.2210 0.2380 0.2070 0.0040  -0.0579 -0.0018 33   ALA H O   
2032 C CB  . ALA B 33  ? 0.2226 0.2424 0.2209 0.0174  -0.0570 -0.0076 33   ALA H CB  
2033 N N   . ILE B 34  ? 0.2277 0.2464 0.2117 0.0072  -0.0589 -0.0020 34   ILE H N   
2034 C CA  . ILE B 34  ? 0.2402 0.2498 0.2140 0.0022  -0.0600 -0.0017 34   ILE H CA  
2035 C C   . ILE B 34  ? 0.2395 0.2401 0.2114 0.0069  -0.0597 -0.0061 34   ILE H C   
2036 O O   . ILE B 34  ? 0.2331 0.2366 0.2089 0.0113  -0.0598 -0.0076 34   ILE H O   
2037 C CB  . ILE B 34  ? 0.2614 0.2763 0.2305 -0.0023 -0.0616 0.0026  34   ILE H CB  
2038 C CG1 . ILE B 34  ? 0.2664 0.2933 0.2378 -0.0071 -0.0620 0.0083  34   ILE H CG1 
2039 C CG2 . ILE B 34  ? 0.2655 0.2674 0.2216 -0.0071 -0.0631 0.0023  34   ILE H CG2 
2040 C CD1 . ILE B 34  ? 0.2963 0.3167 0.2606 -0.0144 -0.0630 0.0097  34   ILE H CD1 
2041 N N   . HIS B 35  ? 0.2419 0.2323 0.2076 0.0065  -0.0591 -0.0078 35   HIS H N   
2042 C CA  . HIS B 35  ? 0.2442 0.2265 0.2068 0.0114  -0.0583 -0.0110 35   HIS H CA  
2043 C C   . HIS B 35  ? 0.2701 0.2405 0.2182 0.0088  -0.0589 -0.0104 35   HIS H C   
2044 O O   . HIS B 35  ? 0.2824 0.2471 0.2206 0.0020  -0.0601 -0.0077 35   HIS H O   
2045 C CB  . HIS B 35  ? 0.2426 0.2221 0.2071 0.0143  -0.0566 -0.0126 35   HIS H CB  
2046 C CG  . HIS B 35  ? 0.2266 0.2161 0.2040 0.0167  -0.0563 -0.0134 35   HIS H CG  
2047 N ND1 . HIS B 35  ? 0.2271 0.2234 0.2100 0.0139  -0.0566 -0.0119 35   HIS H ND1 
2048 C CD2 . HIS B 35  ? 0.2098 0.2028 0.1940 0.0209  -0.0559 -0.0152 35   HIS H CD2 
2049 C CE1 . HIS B 35  ? 0.2037 0.2052 0.1952 0.0166  -0.0563 -0.0131 35   HIS H CE1 
2050 N NE2 . HIS B 35  ? 0.2274 0.2272 0.2200 0.0201  -0.0562 -0.0150 35   HIS H NE2 
2051 N N   . TRP B 36  ? 0.2818 0.2471 0.2270 0.0140  -0.0584 -0.0126 36   TRP H N   
2052 C CA  . TRP B 36  ? 0.2982 0.2491 0.2273 0.0130  -0.0586 -0.0125 36   TRP H CA  
2053 C C   . TRP B 36  ? 0.3100 0.2518 0.2332 0.0199  -0.0562 -0.0145 36   TRP H C   
2054 O O   . TRP B 36  ? 0.2986 0.2485 0.2322 0.0260  -0.0551 -0.0160 36   TRP H O   
2055 C CB  . TRP B 36  ? 0.2995 0.2530 0.2284 0.0127  -0.0600 -0.0123 36   TRP H CB  
2056 C CG  . TRP B 36  ? 0.2971 0.2592 0.2286 0.0058  -0.0621 -0.0089 36   TRP H CG  
2057 C CD1 . TRP B 36  ? 0.2982 0.2754 0.2431 0.0068  -0.0623 -0.0080 36   TRP H CD1 
2058 C CD2 . TRP B 36  ? 0.3172 0.2741 0.2367 -0.0026 -0.0642 -0.0053 36   TRP H CD2 
2059 N NE1 . TRP B 36  ? 0.3001 0.2841 0.2434 0.0007  -0.0639 -0.0037 36   TRP H NE1 
2060 C CE2 . TRP B 36  ? 0.3154 0.2882 0.2440 -0.0059 -0.0655 -0.0018 36   TRP H CE2 
2061 C CE3 . TRP B 36  ? 0.3431 0.2830 0.2437 -0.0077 -0.0654 -0.0044 36   TRP H CE3 
2062 C CZ2 . TRP B 36  ? 0.3363 0.3117 0.2577 -0.0148 -0.0679 0.0031  36   TRP H CZ2 
2063 C CZ3 . TRP B 36  ? 0.3683 0.3078 0.2601 -0.0177 -0.0684 0.0000  36   TRP H CZ3 
2064 C CH2 . TRP B 36  ? 0.3524 0.3112 0.2556 -0.0214 -0.0697 0.0041  36   TRP H CH2 
2065 N N   . VAL B 37  ? 0.3360 0.2609 0.2413 0.0186  -0.0556 -0.0138 37   VAL H N   
2066 C CA  . VAL B 37  ? 0.3672 0.2806 0.2624 0.0259  -0.0527 -0.0147 37   VAL H CA  
2067 C C   . VAL B 37  ? 0.3885 0.2817 0.2614 0.0264  -0.0526 -0.0146 37   VAL H C   
2068 O O   . VAL B 37  ? 0.3959 0.2787 0.2562 0.0180  -0.0550 -0.0132 37   VAL H O   
2069 C CB  . VAL B 37  ? 0.3766 0.2869 0.2697 0.0243  -0.0516 -0.0139 37   VAL H CB  
2070 C CG1 . VAL B 37  ? 0.3903 0.2870 0.2695 0.0320  -0.0482 -0.0140 37   VAL H CG1 
2071 C CG2 . VAL B 37  ? 0.3604 0.2901 0.2748 0.0245  -0.0516 -0.0142 37   VAL H CG2 
2072 N N   . LYS B 38  ? 0.4043 0.2923 0.2718 0.0360  -0.0499 -0.0156 38   LYS H N   
2073 C CA  . LYS B 38  ? 0.4282 0.2952 0.2729 0.0391  -0.0491 -0.0156 38   LYS H CA  
2074 C C   . LYS B 38  ? 0.4665 0.3167 0.2937 0.0456  -0.0456 -0.0151 38   LYS H C   
2075 O O   . LYS B 38  ? 0.4388 0.2996 0.2761 0.0537  -0.0427 -0.0149 38   LYS H O   
2076 C CB  . LYS B 38  ? 0.4244 0.2994 0.2762 0.0471  -0.0480 -0.0167 38   LYS H CB  
2077 C CG  . LYS B 38  ? 0.4419 0.2972 0.2719 0.0523  -0.0466 -0.0168 38   LYS H CG  
2078 C CD  . LYS B 38  ? 0.4333 0.3000 0.2731 0.0605  -0.0454 -0.0174 38   LYS H CD  
2079 C CE  . LYS B 38  ? 0.4566 0.3031 0.2737 0.0667  -0.0437 -0.0174 38   LYS H CE  
2080 N NZ  . LYS B 38  ? 0.4373 0.2969 0.2653 0.0739  -0.0429 -0.0178 38   LYS H NZ  
2081 N N   . ARG B 39  ? 0.5170 0.3417 0.3178 0.0416  -0.0462 -0.0144 39   ARG H N   
2082 C CA  . ARG B 39  ? 0.5745 0.3767 0.3517 0.0483  -0.0428 -0.0138 39   ARG H CA  
2083 C C   . ARG B 39  ? 0.6028 0.3807 0.3536 0.0534  -0.0416 -0.0140 39   ARG H C   
2084 O O   . ARG B 39  ? 0.5800 0.3402 0.3129 0.0438  -0.0450 -0.0137 39   ARG H O   
2085 C CB  . ARG B 39  ? 0.6140 0.4040 0.3799 0.0379  -0.0450 -0.0128 39   ARG H CB  
2086 C CG  . ARG B 39  ? 0.6735 0.4553 0.4312 0.0450  -0.0412 -0.0123 39   ARG H CG  
2087 C CD  . ARG B 39  ? 0.7553 0.5031 0.4772 0.0499  -0.0390 -0.0118 39   ARG H CD  
2088 N NE  . ARG B 39  ? 0.7654 0.5078 0.4804 0.0619  -0.0338 -0.0110 39   ARG H NE  
2089 C CZ  . ARG B 39  ? 0.8096 0.5519 0.5207 0.0777  -0.0286 -0.0104 39   ARG H CZ  
2090 N NH1 . ARG B 39  ? 0.8585 0.5945 0.5605 0.0882  -0.0238 -0.0089 39   ARG H NH1 
2091 N NH2 . ARG B 39  ? 0.8287 0.5768 0.5436 0.0835  -0.0279 -0.0107 39   ARG H NH2 
2092 N N   . LYS B 40  ? 0.6339 0.4138 0.3842 0.0677  -0.0372 -0.0139 40   LYS H N   
2093 C CA  . LYS B 40  ? 0.7151 0.4744 0.4421 0.0752  -0.0353 -0.0140 40   LYS H CA  
2094 C C   . LYS B 40  ? 0.7998 0.5347 0.4995 0.0856  -0.0306 -0.0127 40   LYS H C   
2095 O O   . LYS B 40  ? 0.7924 0.5406 0.5028 0.0955  -0.0266 -0.0114 40   LYS H O   
2096 C CB  . LYS B 40  ? 0.7064 0.4862 0.4513 0.0846  -0.0335 -0.0141 40   LYS H CB  
2097 C CG  . LYS B 40  ? 0.7471 0.5082 0.4706 0.0910  -0.0323 -0.0142 40   LYS H CG  
2098 C CD  . LYS B 40  ? 0.7398 0.5218 0.4809 0.1002  -0.0306 -0.0140 40   LYS H CD  
2099 C CE  . LYS B 40  ? 0.7738 0.5364 0.4930 0.1062  -0.0294 -0.0141 40   LYS H CE  
2100 N NZ  . LYS B 40  ? 0.7531 0.4969 0.4575 0.0929  -0.0342 -0.0157 40   LYS H NZ  
2101 N N   . PRO B 41  ? 0.8941 0.5930 0.5577 0.0836  -0.0310 -0.0127 41   PRO H N   
2102 C CA  . PRO B 41  ? 0.9846 0.6538 0.6163 0.0918  -0.0271 -0.0116 41   PRO H CA  
2103 C C   . PRO B 41  ? 1.0245 0.7027 0.6594 0.1114  -0.0199 -0.0097 41   PRO H C   
2104 O O   . PRO B 41  ? 1.1020 0.7831 0.7392 0.1141  -0.0177 -0.0086 41   PRO H O   
2105 C CB  . PRO B 41  ? 1.0066 0.6389 0.6006 0.0914  -0.0278 -0.0119 41   PRO H CB  
2106 C CG  . PRO B 41  ? 0.9933 0.6401 0.6031 0.0832  -0.0321 -0.0131 41   PRO H CG  
2107 C CD  . PRO B 41  ? 0.9286 0.6117 0.5776 0.0732  -0.0355 -0.0136 41   PRO H CD  
2108 N N   . GLU B 42  ? 1.1081 0.7914 0.7431 0.1245  -0.0163 -0.0087 42   GLU H N   
2109 C CA  . GLU B 42  ? 1.1614 0.8499 0.7929 0.1449  -0.0088 -0.0055 42   GLU H CA  
2110 C C   . GLU B 42  ? 1.0491 0.7805 0.7208 0.1472  -0.0081 -0.0039 42   GLU H C   
2111 O O   . GLU B 42  ? 1.1393 0.8843 0.8154 0.1628  -0.0026 -0.0003 42   GLU H O   
2112 C CB  . GLU B 42  ? 1.2180 0.8961 0.8332 0.1580  -0.0053 -0.0044 42   GLU H CB  
2113 C CG  . GLU B 42  ? 1.3131 0.9479 0.8881 0.1540  -0.0069 -0.0062 42   GLU H CG  
2114 C CD  . GLU B 42  ? 1.3991 0.9968 0.9388 0.1523  -0.0061 -0.0061 42   GLU H CD  
2115 O OE1 . GLU B 42  ? 1.4369 1.0363 0.9738 0.1635  -0.0011 -0.0038 42   GLU H OE1 
2116 O OE2 . GLU B 42  ? 1.4422 1.0089 0.9561 0.1395  -0.0107 -0.0081 42   GLU H OE2 
2117 N N   . GLN B 43  ? 0.9700 0.7222 0.6690 0.1323  -0.0136 -0.0060 43   GLN H N   
2118 C CA  . GLN B 43  ? 0.8694 0.6587 0.6042 0.1315  -0.0139 -0.0049 43   GLN H CA  
2119 C C   . GLN B 43  ? 0.8515 0.6395 0.5901 0.1220  -0.0158 -0.0056 43   GLN H C   
2120 O O   . GLN B 43  ? 0.8559 0.6161 0.5669 0.1239  -0.0138 -0.0053 43   GLN H O   
2121 C CB  . GLN B 43  ? 0.9022 0.7141 0.6626 0.1235  -0.0184 -0.0067 43   GLN H CB  
2122 C CG  . GLN B 43  ? 0.9007 0.7482 0.6910 0.1293  -0.0173 -0.0043 43   GLN H CG  
2123 C CD  . GLN B 43  ? 0.8640 0.7359 0.6844 0.1167  -0.0224 -0.0061 43   GLN H CD  
2124 O OE1 . GLN B 43  ? 0.8069 0.7017 0.6481 0.1166  -0.0239 -0.0057 43   GLN H OE1 
2125 N NE2 . GLN B 43  ? 0.7957 0.6620 0.6171 0.1061  -0.0249 -0.0079 43   GLN H NE2 
2126 N N   . GLY B 44  ? 0.6931 0.5091 0.4630 0.1134  -0.0190 -0.0063 44   GLY H N   
2127 C CA  . GLY B 44  ? 0.6439 0.4646 0.4243 0.1015  -0.0222 -0.0076 44   GLY H CA  
2128 C C   . GLY B 44  ? 0.5795 0.4150 0.3807 0.0875  -0.0280 -0.0100 44   GLY H C   
2129 O O   . GLY B 44  ? 0.5572 0.3779 0.3464 0.0801  -0.0311 -0.0116 44   GLY H O   
2130 N N   . LEU B 45  ? 0.5121 0.3735 0.3407 0.0835  -0.0295 -0.0099 45   LEU H N   
2131 C CA  . LEU B 45  ? 0.4529 0.3273 0.2999 0.0709  -0.0345 -0.0118 45   LEU H CA  
2132 C C   . LEU B 45  ? 0.4223 0.3222 0.2937 0.0727  -0.0356 -0.0119 45   LEU H C   
2133 O O   . LEU B 45  ? 0.4014 0.3160 0.2832 0.0802  -0.0332 -0.0100 45   LEU H O   
2134 C CB  . LEU B 45  ? 0.4389 0.3179 0.2937 0.0633  -0.0358 -0.0118 45   LEU H CB  
2135 C CG  . LEU B 45  ? 0.4659 0.3207 0.2979 0.0579  -0.0362 -0.0117 45   LEU H CG  
2136 C CD1 . LEU B 45  ? 0.4584 0.3196 0.2983 0.0552  -0.0358 -0.0110 45   LEU H CD1 
2137 C CD2 . LEU B 45  ? 0.4791 0.3263 0.3057 0.0456  -0.0409 -0.0125 45   LEU H CD2 
2138 N N   . GLU B 46  ? 0.3945 0.2991 0.2736 0.0654  -0.0392 -0.0136 46   GLU H N   
2139 C CA  . GLU B 46  ? 0.3850 0.3108 0.2850 0.0657  -0.0409 -0.0141 46   GLU H CA  
2140 C C   . GLU B 46  ? 0.3517 0.2851 0.2641 0.0552  -0.0448 -0.0155 46   GLU H C   
2141 O O   . GLU B 46  ? 0.3533 0.2758 0.2564 0.0485  -0.0467 -0.0161 46   GLU H O   
2142 C CB  . GLU B 46  ? 0.4168 0.3399 0.3119 0.0700  -0.0409 -0.0145 46   GLU H CB  
2143 C CG  . GLU B 46  ? 0.4758 0.3934 0.3592 0.0820  -0.0368 -0.0125 46   GLU H CG  
2144 C CD  . GLU B 46  ? 0.5176 0.4310 0.3942 0.0867  -0.0366 -0.0129 46   GLU H CD  
2145 O OE1 . GLU B 46  ? 0.6055 0.4962 0.4594 0.0886  -0.0355 -0.0133 46   GLU H OE1 
2146 O OE2 . GLU B 46  ? 0.5670 0.4988 0.4595 0.0888  -0.0375 -0.0123 46   GLU H OE2 
2147 N N   . TRP B 47  ? 0.3178 0.2695 0.2493 0.0540  -0.0460 -0.0156 47   TRP H N   
2148 C CA  . TRP B 47  ? 0.2929 0.2524 0.2358 0.0461  -0.0491 -0.0167 47   TRP H CA  
2149 C C   . TRP B 47  ? 0.2911 0.2554 0.2387 0.0459  -0.0511 -0.0178 47   TRP H C   
2150 O O   . TRP B 47  ? 0.2752 0.2469 0.2280 0.0511  -0.0507 -0.0176 47   TRP H O   
2151 C CB  . TRP B 47  ? 0.2835 0.2563 0.2409 0.0449  -0.0494 -0.0162 47   TRP H CB  
2152 C CG  . TRP B 47  ? 0.2685 0.2487 0.2364 0.0388  -0.0520 -0.0171 47   TRP H CG  
2153 C CD1 . TRP B 47  ? 0.2765 0.2539 0.2430 0.0328  -0.0530 -0.0169 47   TRP H CD1 
2154 C CD2 . TRP B 47  ? 0.2638 0.2548 0.2432 0.0386  -0.0540 -0.0178 47   TRP H CD2 
2155 N NE1 . TRP B 47  ? 0.2676 0.2540 0.2445 0.0302  -0.0549 -0.0174 47   TRP H NE1 
2156 C CE2 . TRP B 47  ? 0.2572 0.2503 0.2409 0.0335  -0.0556 -0.0182 47   TRP H CE2 
2157 C CE3 . TRP B 47  ? 0.2539 0.2528 0.2393 0.0420  -0.0547 -0.0178 47   TRP H CE3 
2158 C CZ2 . TRP B 47  ? 0.2507 0.2505 0.2424 0.0326  -0.0576 -0.0190 47   TRP H CZ2 
2159 C CZ3 . TRP B 47  ? 0.2477 0.2534 0.2415 0.0396  -0.0573 -0.0187 47   TRP H CZ3 
2160 C CH2 . TRP B 47  ? 0.2435 0.2482 0.2393 0.0354  -0.0586 -0.0195 47   TRP H CH2 
2161 N N   . ILE B 48  ? 0.2922 0.2538 0.2382 0.0401  -0.0532 -0.0183 48   ILE H N   
2162 C CA  . ILE B 48  ? 0.2850 0.2494 0.2334 0.0400  -0.0549 -0.0192 48   ILE H CA  
2163 C C   . ILE B 48  ? 0.2716 0.2487 0.2344 0.0377  -0.0568 -0.0197 48   ILE H C   
2164 O O   . ILE B 48  ? 0.2570 0.2402 0.2258 0.0402  -0.0578 -0.0206 48   ILE H O   
2165 C CB  . ILE B 48  ? 0.2966 0.2501 0.2325 0.0352  -0.0559 -0.0186 48   ILE H CB  
2166 C CG1 . ILE B 48  ? 0.3093 0.2461 0.2270 0.0379  -0.0542 -0.0183 48   ILE H CG1 
2167 C CG2 . ILE B 48  ? 0.2959 0.2542 0.2356 0.0344  -0.0577 -0.0191 48   ILE H CG2 
2168 C CD1 . ILE B 48  ? 0.3244 0.2482 0.2272 0.0309  -0.0558 -0.0171 48   ILE H CD1 
2169 N N   . GLY B 49  ? 0.2765 0.2565 0.2432 0.0331  -0.0573 -0.0190 49   GLY H N   
2170 C CA  . GLY B 49  ? 0.2593 0.2485 0.2363 0.0315  -0.0587 -0.0192 49   GLY H CA  
2171 C C   . GLY B 49  ? 0.2470 0.2375 0.2244 0.0268  -0.0588 -0.0176 49   GLY H C   
2172 O O   . GLY B 49  ? 0.2469 0.2312 0.2164 0.0237  -0.0582 -0.0162 49   GLY H O   
2173 N N   . TYR B 50  ? 0.2369 0.2344 0.2215 0.0265  -0.0595 -0.0173 50   TYR H N   
2174 C CA  . TYR B 50  ? 0.2345 0.2357 0.2199 0.0230  -0.0594 -0.0150 50   TYR H CA  
2175 C C   . TYR B 50  ? 0.2392 0.2459 0.2268 0.0244  -0.0600 -0.0140 50   TYR H C   
2176 O O   . TYR B 50  ? 0.2429 0.2497 0.2328 0.0280  -0.0606 -0.0158 50   TYR H O   
2177 C CB  . TYR B 50  ? 0.2342 0.2378 0.2247 0.0223  -0.0587 -0.0149 50   TYR H CB  
2178 C CG  . TYR B 50  ? 0.2244 0.2315 0.2214 0.0250  -0.0592 -0.0163 50   TYR H CG  
2179 C CD1 . TYR B 50  ? 0.2229 0.2333 0.2213 0.0263  -0.0594 -0.0154 50   TYR H CD1 
2180 C CD2 . TYR B 50  ? 0.2297 0.2363 0.2301 0.0261  -0.0595 -0.0179 50   TYR H CD2 
2181 C CE1 . TYR B 50  ? 0.2257 0.2353 0.2265 0.0284  -0.0601 -0.0168 50   TYR H CE1 
2182 C CE2 . TYR B 50  ? 0.2225 0.2306 0.2268 0.0269  -0.0606 -0.0189 50   TYR H CE2 
2183 C CZ  . TYR B 50  ? 0.2287 0.2366 0.2322 0.0279  -0.0610 -0.0186 50   TYR H CZ  
2184 O OH  . TYR B 50  ? 0.2335 0.2391 0.2373 0.0285  -0.0624 -0.0196 50   TYR H OH  
2185 N N   . ILE B 51  ? 0.2307 0.2423 0.2172 0.0217  -0.0598 -0.0106 51   ILE H N   
2186 C CA  . ILE B 51  ? 0.2347 0.2540 0.2238 0.0242  -0.0595 -0.0083 51   ILE H CA  
2187 C C   . ILE B 51  ? 0.2301 0.2551 0.2222 0.0233  -0.0585 -0.0057 51   ILE H C   
2188 O O   . ILE B 51  ? 0.2359 0.2629 0.2266 0.0181  -0.0585 -0.0032 51   ILE H O   
2189 C CB  . ILE B 51  ? 0.2328 0.2561 0.2179 0.0226  -0.0600 -0.0052 51   ILE H CB  
2190 C CG1 . ILE B 51  ? 0.2388 0.2710 0.2262 0.0269  -0.0591 -0.0023 51   ILE H CG1 
2191 C CG2 . ILE B 51  ? 0.2431 0.2671 0.2233 0.0154  -0.0607 -0.0018 51   ILE H CG2 
2192 C CD1 . ILE B 51  ? 0.2449 0.2812 0.2292 0.0275  -0.0596 0.0000  51   ILE H CD1 
2193 N N   . SER B 52  ? 0.2223 0.2488 0.2171 0.0281  -0.0577 -0.0062 52   SER H N   
2194 C CA  . SER B 52  ? 0.2328 0.2641 0.2296 0.0291  -0.0564 -0.0038 52   SER H CA  
2195 C C   . SER B 52  ? 0.2362 0.2764 0.2316 0.0333  -0.0551 0.0006  52   SER H C   
2196 O O   . SER B 52  ? 0.2441 0.2814 0.2373 0.0394  -0.0545 -0.0003 52   SER H O   
2197 C CB  . SER B 52  ? 0.2353 0.2599 0.2334 0.0317  -0.0565 -0.0072 52   SER H CB  
2198 O OG  . SER B 52  ? 0.2383 0.2658 0.2373 0.0328  -0.0551 -0.0052 52   SER H OG  
2199 N N   . PRO B 53  ? 0.2550 0.3060 0.2507 0.0299  -0.0548 0.0060  53   PRO H N   
2200 C CA  . PRO B 53  ? 0.2726 0.3352 0.2673 0.0340  -0.0534 0.0115  53   PRO H CA  
2201 C C   . PRO B 53  ? 0.2868 0.3531 0.2812 0.0420  -0.0508 0.0138  53   PRO H C   
2202 O O   . PRO B 53  ? 0.3133 0.3848 0.3050 0.0488  -0.0492 0.0167  53   PRO H O   
2203 C CB  . PRO B 53  ? 0.2845 0.3594 0.2797 0.0268  -0.0542 0.0177  53   PRO H CB  
2204 C CG  . PRO B 53  ? 0.2828 0.3498 0.2775 0.0188  -0.0559 0.0150  53   PRO H CG  
2205 C CD  . PRO B 53  ? 0.2625 0.3155 0.2581 0.0216  -0.0559 0.0079  53   PRO H CD  
2206 N N   . GLY B 54  ? 0.2740 0.3366 0.2698 0.0417  -0.0503 0.0124  54   GLY H N   
2207 C CA  . GLY B 54  ? 0.2865 0.3503 0.2799 0.0495  -0.0476 0.0145  54   GLY H CA  
2208 C C   . GLY B 54  ? 0.2951 0.3457 0.2819 0.0573  -0.0471 0.0105  54   GLY H C   
2209 O O   . GLY B 54  ? 0.3000 0.3511 0.2811 0.0659  -0.0445 0.0134  54   GLY H O   
2210 N N   . ASN B 55  ? 0.2757 0.3139 0.2617 0.0546  -0.0495 0.0045  55   ASN H N   
2211 C CA  . ASN B 55  ? 0.2931 0.3168 0.2715 0.0602  -0.0498 0.0005  55   ASN H CA  
2212 C C   . ASN B 55  ? 0.2966 0.3169 0.2741 0.0594  -0.0517 -0.0020 55   ASN H C   
2213 O O   . ASN B 55  ? 0.3114 0.3190 0.2828 0.0618  -0.0529 -0.0057 55   ASN H O   
2214 C CB  . ASN B 55  ? 0.2840 0.2958 0.2614 0.0572  -0.0513 -0.0036 55   ASN H CB  
2215 C CG  . ASN B 55  ? 0.2757 0.2867 0.2604 0.0488  -0.0539 -0.0072 55   ASN H CG  
2216 O OD1 . ASN B 55  ? 0.2935 0.2965 0.2782 0.0459  -0.0555 -0.0104 55   ASN H OD1 
2217 N ND2 . ASN B 55  ? 0.2632 0.2817 0.2529 0.0450  -0.0544 -0.0063 55   ASN H ND2 
2218 N N   . ASP B 56  ? 0.3077 0.3380 0.2900 0.0559  -0.0520 0.0000  56   ASP H N   
2219 C CA  . ASP B 56  ? 0.3332 0.3613 0.3148 0.0550  -0.0536 -0.0019 56   ASP H CA  
2220 C C   . ASP B 56  ? 0.3349 0.3513 0.3168 0.0517  -0.0562 -0.0079 56   ASP H C   
2221 O O   . ASP B 56  ? 0.3670 0.3778 0.3459 0.0535  -0.0574 -0.0102 56   ASP H O   
2222 C CB  . ASP B 56  ? 0.3671 0.3940 0.3418 0.0634  -0.0522 -0.0003 56   ASP H CB  
2223 C CG  . ASP B 56  ? 0.4005 0.4424 0.3753 0.0677  -0.0492 0.0069  56   ASP H CG  
2224 O OD1 . ASP B 56  ? 0.4087 0.4630 0.3894 0.0620  -0.0493 0.0106  56   ASP H OD1 
2225 O OD2 . ASP B 56  ? 0.4916 0.5326 0.4594 0.0768  -0.0469 0.0092  56   ASP H OD2 
2226 N N   . ASP B 57  A 0.3079 0.3220 0.2937 0.0469  -0.0571 -0.0098 56   ASP H N   
2227 C CA  . ASP B 57  A 0.3041 0.3106 0.2913 0.0436  -0.0595 -0.0143 56   ASP H CA  
2228 C C   . ASP B 57  A 0.3024 0.3125 0.2933 0.0394  -0.0601 -0.0147 56   ASP H C   
2229 O O   . ASP B 57  A 0.3033 0.3185 0.2964 0.0360  -0.0593 -0.0126 56   ASP H O   
2230 C CB  . ASP B 57  A 0.2978 0.3012 0.2867 0.0414  -0.0597 -0.0152 56   ASP H CB  
2231 C CG  . ASP B 57  A 0.3108 0.3104 0.3026 0.0374  -0.0619 -0.0183 56   ASP H CG  
2232 O OD1 . ASP B 57  A 0.2995 0.2957 0.2897 0.0377  -0.0637 -0.0202 56   ASP H OD1 
2233 O OD2 . ASP B 57  A 0.2745 0.2758 0.2703 0.0341  -0.0617 -0.0183 56   ASP H OD2 
2234 N N   . ILE B 58  ? 0.2899 0.2965 0.2801 0.0395  -0.0616 -0.0171 57   ILE H N   
2235 C CA  . ILE B 58  ? 0.2846 0.2923 0.2759 0.0368  -0.0620 -0.0176 57   ILE H CA  
2236 C C   . ILE B 58  ? 0.2862 0.2902 0.2793 0.0361  -0.0634 -0.0204 57   ILE H C   
2237 O O   . ILE B 58  ? 0.2825 0.2834 0.2747 0.0377  -0.0650 -0.0220 57   ILE H O   
2238 C CB  . ILE B 58  ? 0.2883 0.2974 0.2763 0.0383  -0.0620 -0.0166 57   ILE H CB  
2239 C CG1 . ILE B 58  ? 0.3011 0.3170 0.2879 0.0389  -0.0606 -0.0125 57   ILE H CG1 
2240 C CG2 . ILE B 58  ? 0.2758 0.2831 0.2623 0.0357  -0.0624 -0.0171 57   ILE H CG2 
2241 C CD1 . ILE B 58  ? 0.3089 0.3275 0.2926 0.0410  -0.0607 -0.0109 57   ILE H CD1 
2242 N N   . LYS B 59  ? 0.2688 0.2733 0.2636 0.0339  -0.0630 -0.0205 58   LYS H N   
2243 C CA  . LYS B 59  ? 0.2738 0.2780 0.2710 0.0340  -0.0640 -0.0220 58   LYS H CA  
2244 C C   . LYS B 59  ? 0.2640 0.2671 0.2585 0.0346  -0.0630 -0.0219 58   LYS H C   
2245 O O   . LYS B 59  ? 0.2568 0.2581 0.2484 0.0329  -0.0615 -0.0207 58   LYS H O   
2246 C CB  . LYS B 59  ? 0.2883 0.2941 0.2893 0.0320  -0.0640 -0.0218 58   LYS H CB  
2247 C CG  . LYS B 59  ? 0.3358 0.3445 0.3400 0.0319  -0.0651 -0.0221 58   LYS H CG  
2248 C CD  . LYS B 59  ? 0.3713 0.3823 0.3793 0.0292  -0.0659 -0.0215 58   LYS H CD  
2249 C CE  . LYS B 59  ? 0.4252 0.4360 0.4334 0.0273  -0.0691 -0.0219 58   LYS H CE  
2250 N NZ  . LYS B 59  ? 0.4510 0.4548 0.4548 0.0268  -0.0700 -0.0227 58   LYS H NZ  
2251 N N   . TYR B 60  ? 0.2463 0.2497 0.2406 0.0368  -0.0639 -0.0228 59   TYR H N   
2252 C CA  . TYR B 60  ? 0.2439 0.2449 0.2339 0.0389  -0.0627 -0.0226 59   TYR H CA  
2253 C C   . TYR B 60  ? 0.2413 0.2466 0.2345 0.0408  -0.0622 -0.0220 59   TYR H C   
2254 O O   . TYR B 60  ? 0.2412 0.2523 0.2402 0.0400  -0.0640 -0.0219 59   TYR H O   
2255 C CB  . TYR B 60  ? 0.2493 0.2488 0.2363 0.0412  -0.0635 -0.0235 59   TYR H CB  
2256 C CG  . TYR B 60  ? 0.2405 0.2374 0.2241 0.0398  -0.0637 -0.0232 59   TYR H CG  
2257 C CD1 . TYR B 60  ? 0.2363 0.2353 0.2222 0.0399  -0.0649 -0.0235 59   TYR H CD1 
2258 C CD2 . TYR B 60  ? 0.2494 0.2417 0.2261 0.0384  -0.0627 -0.0222 59   TYR H CD2 
2259 C CE1 . TYR B 60  ? 0.2460 0.2450 0.2289 0.0397  -0.0646 -0.0223 59   TYR H CE1 
2260 C CE2 . TYR B 60  ? 0.2494 0.2422 0.2236 0.0363  -0.0630 -0.0208 59   TYR H CE2 
2261 C CZ  . TYR B 60  ? 0.2397 0.2371 0.2177 0.0375  -0.0638 -0.0207 59   TYR H CZ  
2262 O OH  . TYR B 60  ? 0.2387 0.2390 0.2145 0.0363  -0.0637 -0.0183 59   TYR H OH  
2263 N N   . ASN B 61  ? 0.2454 0.2471 0.2332 0.0432  -0.0600 -0.0211 60   ASN H N   
2264 C CA  . ASN B 61  ? 0.2542 0.2600 0.2422 0.0478  -0.0588 -0.0198 60   ASN H CA  
2265 C C   . ASN B 61  ? 0.2678 0.2760 0.2558 0.0504  -0.0601 -0.0202 60   ASN H C   
2266 O O   . ASN B 61  ? 0.2699 0.2704 0.2509 0.0512  -0.0598 -0.0213 60   ASN H O   
2267 C CB  . ASN B 61  ? 0.2600 0.2574 0.2380 0.0510  -0.0557 -0.0189 60   ASN H CB  
2268 C CG  . ASN B 61  ? 0.2631 0.2656 0.2407 0.0573  -0.0536 -0.0166 60   ASN H CG  
2269 O OD1 . ASN B 61  ? 0.2682 0.2816 0.2526 0.0594  -0.0546 -0.0153 60   ASN H OD1 
2270 N ND2 . ASN B 61  ? 0.2791 0.2735 0.2471 0.0607  -0.0505 -0.0155 60   ASN H ND2 
2271 N N   . GLU B 62  ? 0.2836 0.3020 0.2785 0.0510  -0.0617 -0.0189 61   GLU H N   
2272 C CA  . GLU B 62  ? 0.3099 0.3321 0.3052 0.0535  -0.0631 -0.0188 61   GLU H CA  
2273 C C   . GLU B 62  ? 0.3216 0.3378 0.3080 0.0596  -0.0604 -0.0185 61   GLU H C   
2274 O O   . GLU B 62  ? 0.3111 0.3238 0.2942 0.0606  -0.0613 -0.0197 61   GLU H O   
2275 C CB  . GLU B 62  ? 0.3510 0.3871 0.3541 0.0532  -0.0648 -0.0159 61   GLU H CB  
2276 C CG  . GLU B 62  ? 0.3844 0.4259 0.3896 0.0527  -0.0678 -0.0155 61   GLU H CG  
2277 C CD  . GLU B 62  ? 0.4205 0.4559 0.4253 0.0477  -0.0712 -0.0184 61   GLU H CD  
2278 O OE1 . GLU B 62  ? 0.4251 0.4562 0.4306 0.0434  -0.0722 -0.0197 61   GLU H OE1 
2279 O OE2 . GLU B 62  ? 0.5246 0.5594 0.5275 0.0487  -0.0727 -0.0191 61   GLU H OE2 
2280 N N   . LYS B 63  ? 0.3127 0.3257 0.2934 0.0636  -0.0571 -0.0169 62   LYS H N   
2281 C CA  . LYS B 63  ? 0.3342 0.3381 0.3027 0.0702  -0.0541 -0.0164 62   LYS H CA  
2282 C C   . LYS B 63  ? 0.3203 0.3102 0.2799 0.0674  -0.0548 -0.0191 62   LYS H C   
2283 O O   . LYS B 63  ? 0.3085 0.2909 0.2584 0.0716  -0.0536 -0.0192 62   LYS H O   
2284 C CB  . LYS B 63  ? 0.3602 0.3600 0.3223 0.0742  -0.0506 -0.0145 62   LYS H CB  
2285 C CG  . LYS B 63  ? 0.4122 0.3973 0.3571 0.0811  -0.0471 -0.0140 62   LYS H CG  
2286 C CD  . LYS B 63  ? 0.4398 0.4222 0.3773 0.0876  -0.0431 -0.0113 62   LYS H CD  
2287 C CE  . LYS B 63  ? 0.4765 0.4421 0.3939 0.0959  -0.0396 -0.0106 62   LYS H CE  
2288 N NZ  . LYS B 63  ? 0.5140 0.4799 0.4245 0.1053  -0.0351 -0.0070 62   LYS H NZ  
2289 N N   . PHE B 64  ? 0.2924 0.2786 0.2534 0.0608  -0.0562 -0.0207 63   PHE H N   
2290 C CA  . PHE B 64  ? 0.3030 0.2781 0.2554 0.0572  -0.0568 -0.0220 63   PHE H CA  
2291 C C   . PHE B 64  ? 0.2893 0.2694 0.2482 0.0542  -0.0595 -0.0233 63   PHE H C   
2292 O O   . PHE B 64  ? 0.2790 0.2531 0.2324 0.0511  -0.0601 -0.0236 63   PHE H O   
2293 C CB  . PHE B 64  ? 0.2933 0.2621 0.2416 0.0521  -0.0564 -0.0216 63   PHE H CB  
2294 C CG  . PHE B 64  ? 0.3166 0.2738 0.2518 0.0550  -0.0537 -0.0206 63   PHE H CG  
2295 C CD1 . PHE B 64  ? 0.3170 0.2781 0.2549 0.0585  -0.0517 -0.0194 63   PHE H CD1 
2296 C CD2 . PHE B 64  ? 0.3305 0.2718 0.2489 0.0546  -0.0531 -0.0205 63   PHE H CD2 
2297 C CE1 . PHE B 64  ? 0.3334 0.2824 0.2574 0.0625  -0.0489 -0.0183 63   PHE H CE1 
2298 C CE2 . PHE B 64  ? 0.3551 0.2823 0.2579 0.0581  -0.0506 -0.0196 63   PHE H CE2 
2299 C CZ  . PHE B 64  ? 0.3490 0.2797 0.2543 0.0624  -0.0482 -0.0186 63   PHE H CZ  
2300 N N   . LYS B 65  ? 0.2920 0.2823 0.2611 0.0547  -0.0612 -0.0236 64   LYS H N   
2301 C CA  . LYS B 65  ? 0.2898 0.2823 0.2623 0.0531  -0.0635 -0.0249 64   LYS H CA  
2302 C C   . LYS B 65  ? 0.2872 0.2751 0.2529 0.0564  -0.0633 -0.0253 64   LYS H C   
2303 O O   . LYS B 65  ? 0.2857 0.2743 0.2490 0.0611  -0.0621 -0.0245 64   LYS H O   
2304 C CB  . LYS B 65  ? 0.2960 0.2973 0.2774 0.0524  -0.0658 -0.0250 64   LYS H CB  
2305 C CG  . LYS B 65  ? 0.3145 0.3187 0.3014 0.0486  -0.0665 -0.0248 64   LYS H CG  
2306 C CD  . LYS B 65  ? 0.3455 0.3545 0.3376 0.0468  -0.0695 -0.0251 64   LYS H CD  
2307 C CE  . LYS B 65  ? 0.3806 0.3909 0.3764 0.0431  -0.0703 -0.0248 64   LYS H CE  
2308 N NZ  . LYS B 65  ? 0.4018 0.4126 0.3986 0.0405  -0.0737 -0.0252 64   LYS H NZ  
2309 N N   . GLY B 66  ? 0.2807 0.2646 0.2430 0.0544  -0.0641 -0.0260 65   GLY H N   
2310 C CA  . GLY B 66  ? 0.2901 0.2684 0.2449 0.0568  -0.0639 -0.0263 65   GLY H CA  
2311 C C   . GLY B 66  ? 0.3120 0.2791 0.2545 0.0559  -0.0624 -0.0255 65   GLY H C   
2312 O O   . GLY B 66  ? 0.3276 0.2878 0.2616 0.0575  -0.0622 -0.0257 65   GLY H O   
2313 N N   . LYS B 67  ? 0.3162 0.2798 0.2560 0.0530  -0.0614 -0.0246 66   LYS H N   
2314 C CA  . LYS B 67  ? 0.3285 0.2787 0.2537 0.0509  -0.0603 -0.0236 66   LYS H CA  
2315 C C   . LYS B 67  ? 0.3224 0.2726 0.2474 0.0433  -0.0613 -0.0221 66   LYS H C   
2316 O O   . LYS B 67  ? 0.3251 0.2663 0.2387 0.0387  -0.0620 -0.0208 66   LYS H O   
2317 C CB  . LYS B 67  ? 0.3452 0.2898 0.2645 0.0559  -0.0578 -0.0233 66   LYS H CB  
2318 C CG  . LYS B 67  ? 0.3887 0.3160 0.2898 0.0539  -0.0566 -0.0223 66   LYS H CG  
2319 C CD  . LYS B 67  ? 0.3998 0.3135 0.2855 0.0539  -0.0570 -0.0224 66   LYS H CD  
2320 C CE  . LYS B 67  ? 0.4214 0.3344 0.3047 0.0631  -0.0553 -0.0230 66   LYS H CE  
2321 N NZ  . LYS B 67  ? 0.4304 0.3244 0.2929 0.0640  -0.0548 -0.0229 66   LYS H NZ  
2322 N N   . ALA B 68  ? 0.3205 0.2803 0.2567 0.0419  -0.0615 -0.0220 67   ALA H N   
2323 C CA  . ALA B 68  ? 0.3293 0.2909 0.2661 0.0354  -0.0622 -0.0201 67   ALA H CA  
2324 C C   . ALA B 68  ? 0.3139 0.2878 0.2622 0.0345  -0.0633 -0.0196 67   ALA H C   
2325 O O   . ALA B 68  ? 0.3140 0.2940 0.2711 0.0385  -0.0634 -0.0213 67   ALA H O   
2326 C CB  . ALA B 68  ? 0.3339 0.2938 0.2710 0.0351  -0.0609 -0.0199 67   ALA H CB  
2327 N N   . THR B 69  ? 0.3218 0.2987 0.2685 0.0295  -0.0641 -0.0168 68   THR H N   
2328 C CA  . THR B 69  ? 0.3083 0.2968 0.2642 0.0297  -0.0644 -0.0155 68   THR H CA  
2329 C C   . THR B 69  ? 0.2951 0.2883 0.2513 0.0244  -0.0644 -0.0120 68   THR H C   
2330 O O   . THR B 69  ? 0.3047 0.2958 0.2532 0.0186  -0.0652 -0.0089 68   THR H O   
2331 C CB  . THR B 69  ? 0.3124 0.3048 0.2677 0.0308  -0.0652 -0.0143 68   THR H CB  
2332 O OG1 . THR B 69  ? 0.3131 0.3014 0.2679 0.0355  -0.0654 -0.0174 68   THR H OG1 
2333 C CG2 . THR B 69  ? 0.3077 0.3102 0.2705 0.0334  -0.0649 -0.0130 68   THR H CG2 
2334 N N   . LEU B 70  ? 0.2911 0.2904 0.2552 0.0260  -0.0637 -0.0121 69   LEU H N   
2335 C CA  . LEU B 70  ? 0.2784 0.2833 0.2438 0.0216  -0.0634 -0.0087 69   LEU H CA  
2336 C C   . LEU B 70  ? 0.2715 0.2884 0.2417 0.0232  -0.0631 -0.0053 69   LEU H C   
2337 O O   . LEU B 70  ? 0.2642 0.2833 0.2391 0.0293  -0.0624 -0.0070 69   LEU H O   
2338 C CB  . LEU B 70  ? 0.2823 0.2858 0.2523 0.0228  -0.0625 -0.0107 69   LEU H CB  
2339 C CG  . LEU B 70  ? 0.2837 0.2772 0.2499 0.0234  -0.0622 -0.0137 69   LEU H CG  
2340 C CD1 . LEU B 70  ? 0.2947 0.2889 0.2659 0.0241  -0.0613 -0.0147 69   LEU H CD1 
2341 C CD2 . LEU B 70  ? 0.3042 0.2886 0.2584 0.0187  -0.0626 -0.0122 69   LEU H CD2 
2342 N N   . THR B 71  ? 0.2813 0.3055 0.2493 0.0179  -0.0635 0.0000  70   THR H N   
2343 C CA  . THR B 71  ? 0.2989 0.3374 0.2714 0.0201  -0.0626 0.0047  70   THR H CA  
2344 C C   . THR B 71  ? 0.2971 0.3434 0.2703 0.0144  -0.0626 0.0095  70   THR H C   
2345 O O   . THR B 71  ? 0.3051 0.3440 0.2738 0.0081  -0.0638 0.0088  70   THR H O   
2346 C CB  . THR B 71  ? 0.2974 0.3424 0.2674 0.0201  -0.0631 0.0081  70   THR H CB  
2347 O OG1 . THR B 71  ? 0.3161 0.3578 0.2786 0.0110  -0.0652 0.0105  70   THR H OG1 
2348 C CG2 . THR B 71  ? 0.3159 0.3544 0.2859 0.0266  -0.0629 0.0036  70   THR H CG2 
2349 N N   . ALA B 72  ? 0.3070 0.3676 0.2846 0.0171  -0.0613 0.0146  71   ALA H N   
2350 C CA  . ALA B 72  ? 0.3239 0.3958 0.3029 0.0120  -0.0613 0.0206  71   ALA H CA  
2351 C C   . ALA B 72  ? 0.3367 0.4279 0.3183 0.0145  -0.0602 0.0284  71   ALA H C   
2352 O O   . ALA B 72  ? 0.3401 0.4348 0.3238 0.0239  -0.0582 0.0282  71   ALA H O   
2353 C CB  . ALA B 72  ? 0.3119 0.3806 0.2951 0.0149  -0.0599 0.0179  71   ALA H CB  
2354 N N   . ASP B 73  ? 0.3360 0.4394 0.3162 0.0062  -0.0617 0.0357  72   ASP H N   
2355 C CA  . ASP B 73  ? 0.3542 0.4806 0.3376 0.0078  -0.0606 0.0452  72   ASP H CA  
2356 C C   . ASP B 73  ? 0.3544 0.4921 0.3422 0.0080  -0.0593 0.0497  72   ASP H C   
2357 O O   . ASP B 73  ? 0.3344 0.4737 0.3201 -0.0024 -0.0617 0.0525  72   ASP H O   
2358 C CB  . ASP B 73  ? 0.3736 0.5083 0.3520 -0.0028 -0.0639 0.0517  72   ASP H CB  
2359 C CG  . ASP B 73  ? 0.3979 0.5597 0.3803 -0.0016 -0.0629 0.0628  72   ASP H CG  
2360 O OD1 . ASP B 73  ? 0.4127 0.5871 0.4009 0.0058  -0.0598 0.0664  72   ASP H OD1 
2361 O OD2 . ASP B 73  ? 0.4431 0.6129 0.4223 -0.0070 -0.0649 0.0678  72   ASP H OD2 
2362 N N   . LYS B 74  ? 0.3809 0.5223 0.3729 0.0196  -0.0556 0.0493  73   LYS H N   
2363 C CA  . LYS B 74  ? 0.4242 0.5751 0.4200 0.0217  -0.0537 0.0530  73   LYS H CA  
2364 C C   . LYS B 74  ? 0.4389 0.6146 0.4364 0.0151  -0.0546 0.0647  73   LYS H C   
2365 O O   . LYS B 74  ? 0.4293 0.6104 0.4284 0.0092  -0.0554 0.0677  73   LYS H O   
2366 C CB  . LYS B 74  ? 0.4595 0.6076 0.4562 0.0364  -0.0496 0.0507  73   LYS H CB  
2367 C CG  . LYS B 74  ? 0.5002 0.6258 0.4958 0.0390  -0.0495 0.0405  73   LYS H CG  
2368 C CD  . LYS B 74  ? 0.5333 0.6439 0.5255 0.0464  -0.0490 0.0338  73   LYS H CD  
2369 C CE  . LYS B 74  ? 0.5635 0.6693 0.5528 0.0585  -0.0457 0.0327  73   LYS H CE  
2370 N NZ  . LYS B 74  ? 0.5512 0.6383 0.5358 0.0634  -0.0461 0.0250  73   LYS H NZ  
2371 N N   . SER B 75  ? 0.4514 0.6423 0.4486 0.0151  -0.0548 0.0715  74   SER H N   
2372 C CA  . SER B 75  ? 0.4636 0.6827 0.4632 0.0091  -0.0557 0.0845  74   SER H CA  
2373 C C   . SER B 75  ? 0.4536 0.6713 0.4495 -0.0086 -0.0608 0.0867  74   SER H C   
2374 O O   . SER B 75  ? 0.4624 0.7006 0.4605 -0.0149 -0.0618 0.0964  74   SER H O   
2375 C CB  . SER B 75  ? 0.5004 0.7342 0.4996 0.0111  -0.0555 0.0909  74   SER H CB  
2376 O OG  . SER B 75  ? 0.5759 0.8055 0.5755 0.0271  -0.0511 0.0874  74   SER H OG  
2377 N N   . SER B 76  ? 0.3980 0.5924 0.3870 -0.0164 -0.0640 0.0788  75   SER H N   
2378 C CA  . SER B 76  ? 0.3894 0.5771 0.3702 -0.0334 -0.0692 0.0804  75   SER H CA  
2379 C C   . SER B 76  ? 0.3669 0.5318 0.3444 -0.0357 -0.0697 0.0717  75   SER H C   
2380 O O   . SER B 76  ? 0.3606 0.5142 0.3286 -0.0484 -0.0736 0.0716  75   SER H O   
2381 C CB  . SER B 76  ? 0.3986 0.5767 0.3711 -0.0400 -0.0723 0.0792  75   SER H CB  
2382 O OG  . SER B 76  ? 0.3879 0.5414 0.3578 -0.0332 -0.0711 0.0677  75   SER H OG  
2383 N N   . SER B 77  ? 0.3510 0.5084 0.3346 -0.0236 -0.0659 0.0649  76   SER H N   
2384 C CA  . SER B 77  ? 0.3331 0.4697 0.3148 -0.0238 -0.0657 0.0564  76   SER H CA  
2385 C C   . SER B 77  ? 0.3172 0.4312 0.2885 -0.0307 -0.0686 0.0502  76   SER H C   
2386 O O   . SER B 77  ? 0.3109 0.4123 0.2751 -0.0388 -0.0707 0.0484  76   SER H O   
2387 C CB  . SER B 77  ? 0.3375 0.4814 0.3199 -0.0306 -0.0666 0.0609  76   SER H CB  
2388 O OG  . SER B 77  ? 0.3448 0.5091 0.3359 -0.0228 -0.0635 0.0667  76   SER H OG  
2389 N N   . THR B 78  ? 0.3057 0.4143 0.2751 -0.0273 -0.0686 0.0474  77   THR H N   
2390 C CA  . THR B 78  ? 0.3173 0.4047 0.2758 -0.0324 -0.0710 0.0420  77   THR H CA  
2391 C C   . THR B 78  ? 0.3045 0.3785 0.2661 -0.0214 -0.0685 0.0330  77   THR H C   
2392 O O   . THR B 78  ? 0.2901 0.3721 0.2584 -0.0128 -0.0665 0.0328  77   THR H O   
2393 C CB  . THR B 78  ? 0.3352 0.4273 0.2859 -0.0409 -0.0741 0.0477  77   THR H CB  
2394 O OG1 . THR B 78  ? 0.3581 0.4644 0.3063 -0.0521 -0.0768 0.0569  77   THR H OG1 
2395 C CG2 . THR B 78  ? 0.3594 0.4275 0.2960 -0.0464 -0.0765 0.0426  77   THR H CG2 
2396 N N   . ALA B 79  ? 0.3043 0.3585 0.2601 -0.0221 -0.0688 0.0264  78   ALA H N   
2397 C CA  . ALA B 79  ? 0.3021 0.3428 0.2588 -0.0140 -0.0673 0.0185  78   ALA H CA  
2398 C C   . ALA B 79  ? 0.3026 0.3308 0.2479 -0.0180 -0.0692 0.0172  78   ALA H C   
2399 O O   . ALA B 79  ? 0.3303 0.3506 0.2634 -0.0278 -0.0718 0.0199  78   ALA H O   
2400 C CB  . ALA B 79  ? 0.3020 0.3318 0.2597 -0.0116 -0.0660 0.0134  78   ALA H CB  
2401 N N   . TYR B 80  ? 0.3221 0.3471 0.2696 -0.0109 -0.0683 0.0134  79   TYR H N   
2402 C CA  . TYR B 80  ? 0.3121 0.3249 0.2492 -0.0128 -0.0697 0.0116  79   TYR H CA  
2403 C C   . TYR B 80  ? 0.3141 0.3144 0.2519 -0.0048 -0.0680 0.0044  79   TYR H C   
2404 O O   . TYR B 80  ? 0.3012 0.3065 0.2494 0.0029  -0.0662 0.0014  79   TYR H O   
2405 C CB  . TYR B 80  ? 0.3181 0.3424 0.2574 -0.0124 -0.0703 0.0153  79   TYR H CB  
2406 C CG  . TYR B 80  ? 0.3235 0.3639 0.2627 -0.0202 -0.0720 0.0238  79   TYR H CG  
2407 C CD1 . TYR B 80  ? 0.3303 0.3904 0.2810 -0.0158 -0.0703 0.0280  79   TYR H CD1 
2408 C CD2 . TYR B 80  ? 0.3399 0.3760 0.2665 -0.0317 -0.0754 0.0283  79   TYR H CD2 
2409 C CE1 . TYR B 80  ? 0.3259 0.4045 0.2775 -0.0221 -0.0715 0.0371  79   TYR H CE1 
2410 C CE2 . TYR B 80  ? 0.3472 0.4013 0.2743 -0.0397 -0.0773 0.0373  79   TYR H CE2 
2411 C CZ  . TYR B 80  ? 0.3433 0.4203 0.2840 -0.0344 -0.0752 0.0420  79   TYR H CZ  
2412 O OH  . TYR B 80  ? 0.3632 0.4611 0.3053 -0.0415 -0.0769 0.0520  79   TYR H OH  
2413 N N   . MET B 81  ? 0.3301 0.3139 0.2551 -0.0070 -0.0689 0.0023  80   MET H N   
2414 C CA  . MET B 81  ? 0.3242 0.2974 0.2480 0.0005  -0.0674 -0.0032 80   MET H CA  
2415 C C   . MET B 81  ? 0.3351 0.3001 0.2484 -0.0006 -0.0686 -0.0031 80   MET H C   
2416 O O   . MET B 81  ? 0.3390 0.2912 0.2364 -0.0076 -0.0703 -0.0013 80   MET H O   
2417 C CB  . MET B 81  ? 0.3302 0.2893 0.2465 0.0014  -0.0663 -0.0058 80   MET H CB  
2418 C CG  . MET B 81  ? 0.3499 0.3022 0.2663 0.0100  -0.0646 -0.0103 80   MET H CG  
2419 S SD  . MET B 81  ? 0.3806 0.3211 0.2915 0.0144  -0.0623 -0.0130 80   MET H SD  
2420 C CE  . MET B 81  ? 0.3956 0.3154 0.2823 0.0070  -0.0635 -0.0108 80   MET H CE  
2421 N N   . GLN B 82  ? 0.3294 0.2998 0.2499 0.0056  -0.0680 -0.0051 81   GLN H N   
2422 C CA  . GLN B 82  ? 0.3633 0.3255 0.2750 0.0064  -0.0687 -0.0060 81   GLN H CA  
2423 C C   . GLN B 82  ? 0.3503 0.3005 0.2585 0.0137  -0.0670 -0.0109 81   GLN H C   
2424 O O   . GLN B 82  ? 0.3692 0.3259 0.2889 0.0203  -0.0655 -0.0136 81   GLN H O   
2425 C CB  . GLN B 82  ? 0.3815 0.3570 0.3024 0.0091  -0.0690 -0.0048 81   GLN H CB  
2426 C CG  . GLN B 82  ? 0.4445 0.4125 0.3562 0.0088  -0.0700 -0.0051 81   GLN H CG  
2427 C CD  . GLN B 82  ? 0.5168 0.4979 0.4332 0.0076  -0.0710 -0.0015 81   GLN H CD  
2428 O OE1 . GLN B 82  ? 0.6177 0.6117 0.5382 0.0032  -0.0716 0.0034  81   GLN H OE1 
2429 N NE2 . GLN B 82  ? 0.5619 0.5402 0.4768 0.0117  -0.0710 -0.0034 81   GLN H NE2 
2430 N N   . LEU B 83  ? 0.3629 0.2965 0.2547 0.0124  -0.0673 -0.0113 82   LEU H N   
2431 C CA  . LEU B 83  ? 0.3671 0.2900 0.2536 0.0206  -0.0653 -0.0150 82   LEU H CA  
2432 C C   . LEU B 83  ? 0.3729 0.2921 0.2540 0.0222  -0.0661 -0.0154 82   LEU H C   
2433 O O   . LEU B 83  ? 0.3950 0.3064 0.2636 0.0154  -0.0680 -0.0130 82   LEU H O   
2434 C CB  . LEU B 83  ? 0.3825 0.2866 0.2516 0.0198  -0.0644 -0.0150 82   LEU H CB  
2435 C CG  . LEU B 83  ? 0.3921 0.2992 0.2659 0.0185  -0.0635 -0.0147 82   LEU H CG  
2436 C CD1 . LEU B 83  ? 0.4204 0.3064 0.2731 0.0160  -0.0630 -0.0140 82   LEU H CD1 
2437 C CD2 . LEU B 83  ? 0.3878 0.3055 0.2769 0.0273  -0.0612 -0.0172 82   LEU H CD2 
2438 N N   . ASN B 84  A 0.3670 0.2908 0.2559 0.0304  -0.0648 -0.0181 82   ASN H N   
2439 C CA  . ASN B 84  A 0.3550 0.2780 0.2415 0.0325  -0.0655 -0.0187 82   ASN H CA  
2440 C C   . ASN B 84  A 0.3653 0.2753 0.2409 0.0396  -0.0637 -0.0207 82   ASN H C   
2441 O O   . ASN B 84  A 0.3599 0.2672 0.2352 0.0450  -0.0616 -0.0218 82   ASN H O   
2442 C CB  . ASN B 84  A 0.3435 0.2832 0.2472 0.0359  -0.0659 -0.0196 82   ASN H CB  
2443 C CG  . ASN B 84  A 0.3354 0.2819 0.2504 0.0429  -0.0646 -0.0222 82   ASN H CG  
2444 O OD1 . ASN B 84  A 0.3239 0.2695 0.2392 0.0490  -0.0639 -0.0239 82   ASN H OD1 
2445 N ND2 . ASN B 84  A 0.3172 0.2721 0.2420 0.0416  -0.0645 -0.0219 82   ASN H ND2 
2446 N N   . SER B 85  B 0.3664 0.2696 0.2334 0.0405  -0.0643 -0.0209 82   SER H N   
2447 C CA  . SER B 85  B 0.3855 0.2798 0.2447 0.0493  -0.0623 -0.0227 82   SER H CA  
2448 C C   . SER B 85  B 0.4070 0.2834 0.2487 0.0519  -0.0602 -0.0225 82   SER H C   
2449 O O   . SER B 85  B 0.4127 0.2892 0.2551 0.0610  -0.0574 -0.0234 82   SER H O   
2450 C CB  . SER B 85  B 0.3688 0.2789 0.2456 0.0569  -0.0613 -0.0245 82   SER H CB  
2451 O OG  . SER B 85  B 0.3599 0.2843 0.2510 0.0545  -0.0633 -0.0247 82   SER H OG  
2452 N N   . LEU B 86  C 0.4337 0.2942 0.2580 0.0442  -0.0614 -0.0209 82   LEU H N   
2453 C CA  . LEU B 86  C 0.4695 0.3123 0.2768 0.0451  -0.0597 -0.0204 82   LEU H CA  
2454 C C   . LEU B 86  C 0.5018 0.3252 0.2890 0.0546  -0.0567 -0.0212 82   LEU H C   
2455 O O   . LEU B 86  C 0.5188 0.3332 0.2956 0.0554  -0.0573 -0.0215 82   LEU H O   
2456 C CB  . LEU B 86  C 0.4826 0.3141 0.2763 0.0323  -0.0627 -0.0180 82   LEU H CB  
2457 C CG  . LEU B 86  C 0.4602 0.3106 0.2718 0.0241  -0.0648 -0.0163 82   LEU H CG  
2458 C CD1 . LEU B 86  C 0.4740 0.3149 0.2712 0.0107  -0.0684 -0.0128 82   LEU H CD1 
2459 C CD2 . LEU B 86  C 0.4558 0.3134 0.2780 0.0286  -0.0625 -0.0173 82   LEU H CD2 
2460 N N   . THR B 87  ? 0.5133 0.3306 0.2948 0.0626  -0.0533 -0.0213 83   THR H N   
2461 C CA  . THR B 87  ? 0.5363 0.3323 0.2945 0.0731  -0.0496 -0.0212 83   THR H CA  
2462 C C   . THR B 87  ? 0.5758 0.3509 0.3134 0.0717  -0.0484 -0.0203 83   THR H C   
2463 O O   . THR B 87  ? 0.5461 0.3279 0.2921 0.0633  -0.0502 -0.0198 83   THR H O   
2464 C CB  . THR B 87  ? 0.5323 0.3444 0.3044 0.0868  -0.0458 -0.0213 83   THR H CB  
2465 O OG1 . THR B 87  ? 0.5351 0.3587 0.3190 0.0886  -0.0443 -0.0206 83   THR H OG1 
2466 C CG2 . THR B 87  ? 0.5067 0.3423 0.3024 0.0866  -0.0477 -0.0222 83   THR H CG2 
2467 N N   . SER B 88  ? 0.5983 0.3489 0.3092 0.0806  -0.0450 -0.0199 84   SER H N   
2468 C CA  . SER B 88  ? 0.6431 0.3712 0.3312 0.0824  -0.0429 -0.0190 84   SER H CA  
2469 C C   . SER B 88  ? 0.6179 0.3665 0.3270 0.0861  -0.0408 -0.0185 84   SER H C   
2470 O O   . SER B 88  ? 0.6177 0.3537 0.3153 0.0821  -0.0408 -0.0179 84   SER H O   
2471 C CB  . SER B 88  ? 0.6752 0.3772 0.3338 0.0957  -0.0384 -0.0184 84   SER H CB  
2472 O OG  . SER B 88  ? 0.6669 0.3882 0.3409 0.1101  -0.0344 -0.0180 84   SER H OG  
2473 N N   . GLU B 89  ? 0.6003 0.3772 0.3363 0.0933  -0.0392 -0.0185 85   GLU H N   
2474 C CA  . GLU B 89  ? 0.6215 0.4184 0.3771 0.0967  -0.0374 -0.0177 85   GLU H CA  
2475 C C   . GLU B 89  ? 0.5730 0.3806 0.3441 0.0828  -0.0416 -0.0184 85   GLU H C   
2476 O O   . GLU B 89  ? 0.6009 0.4177 0.3815 0.0838  -0.0403 -0.0178 85   GLU H O   
2477 C CB  . GLU B 89  ? 0.6543 0.4789 0.4340 0.1056  -0.0358 -0.0170 85   GLU H CB  
2478 C CG  . GLU B 89  ? 0.7238 0.5425 0.4903 0.1216  -0.0306 -0.0148 85   GLU H CG  
2479 C CD  . GLU B 89  ? 0.7779 0.6199 0.5627 0.1287  -0.0300 -0.0138 85   GLU H CD  
2480 O OE1 . GLU B 89  ? 0.8571 0.7029 0.6373 0.1426  -0.0254 -0.0107 85   GLU H OE1 
2481 O OE2 . GLU B 89  ? 0.8344 0.6907 0.6368 0.1209  -0.0341 -0.0156 85   GLU H OE2 
2482 N N   . ASP B 90  ? 0.5374 0.3431 0.3089 0.0708  -0.0460 -0.0192 86   ASP H N   
2483 C CA  . ASP B 90  ? 0.5291 0.3451 0.3134 0.0578  -0.0498 -0.0190 86   ASP H CA  
2484 C C   . ASP B 90  ? 0.5433 0.3360 0.3044 0.0491  -0.0513 -0.0178 86   ASP H C   
2485 O O   . ASP B 90  ? 0.5018 0.3032 0.2723 0.0394  -0.0538 -0.0169 86   ASP H O   
2486 C CB  . ASP B 90  ? 0.5234 0.3522 0.3206 0.0504  -0.0534 -0.0193 86   ASP H CB  
2487 C CG  . ASP B 90  ? 0.5157 0.3674 0.3361 0.0576  -0.0525 -0.0205 86   ASP H CG  
2488 O OD1 . ASP B 90  ? 0.4871 0.3549 0.3247 0.0606  -0.0514 -0.0206 86   ASP H OD1 
2489 O OD2 . ASP B 90  ? 0.4768 0.3294 0.2971 0.0598  -0.0531 -0.0211 86   ASP H OD2 
2490 N N   . SER B 91  ? 0.5493 0.3130 0.2799 0.0518  -0.0501 -0.0175 87   SER H N   
2491 C CA  . SER B 91  ? 0.5853 0.3225 0.2891 0.0442  -0.0514 -0.0163 87   SER H CA  
2492 C C   . SER B 91  ? 0.5633 0.3063 0.2743 0.0469  -0.0492 -0.0160 87   SER H C   
2493 O O   . SER B 91  ? 0.5625 0.3070 0.2745 0.0600  -0.0445 -0.0163 87   SER H O   
2494 C CB  . SER B 91  ? 0.6189 0.3218 0.2869 0.0500  -0.0495 -0.0163 87   SER H CB  
2495 O OG  . SER B 91  ? 0.6352 0.3329 0.2968 0.0454  -0.0522 -0.0163 87   SER H OG  
2496 N N   . ALA B 92  ? 0.5705 0.3168 0.2853 0.0345  -0.0526 -0.0148 88   ALA H N   
2497 C CA  . ALA B 92  ? 0.5454 0.2979 0.2678 0.0352  -0.0511 -0.0145 88   ALA H CA  
2498 C C   . ALA B 92  ? 0.5529 0.3052 0.2743 0.0191  -0.0558 -0.0126 88   ALA H C   
2499 O O   . ALA B 92  ? 0.5335 0.2855 0.2519 0.0078  -0.0602 -0.0111 88   ALA H O   
2500 C CB  . ALA B 92  ? 0.5165 0.3006 0.2721 0.0426  -0.0489 -0.0155 88   ALA H CB  
2501 N N   . VAL B 93  ? 0.5344 0.2916 0.2620 0.0181  -0.0550 -0.0121 89   VAL H N   
2502 C CA  . VAL B 93  ? 0.5388 0.3056 0.2744 0.0042  -0.0591 -0.0100 89   VAL H CA  
2503 C C   . VAL B 93  ? 0.4965 0.2972 0.2678 0.0070  -0.0583 -0.0107 89   VAL H C   
2504 O O   . VAL B 93  ? 0.4905 0.2999 0.2733 0.0183  -0.0544 -0.0125 89   VAL H O   
2505 C CB  . VAL B 93  ? 0.5563 0.3040 0.2729 0.0007  -0.0589 -0.0090 89   VAL H CB  
2506 C CG1 . VAL B 93  ? 0.5477 0.3084 0.2746 -0.0132 -0.0630 -0.0063 89   VAL H CG1 
2507 C CG2 . VAL B 93  ? 0.6000 0.3099 0.2773 -0.0017 -0.0597 -0.0084 89   VAL H CG2 
2508 N N   . TYR B 94  ? 0.4696 0.2880 0.2558 -0.0022 -0.0619 -0.0090 90   TYR H N   
2509 C CA  . TYR B 94  ? 0.4301 0.2784 0.2472 -0.0004 -0.0616 -0.0093 90   TYR H CA  
2510 C C   . TYR B 94  ? 0.4148 0.2718 0.2381 -0.0099 -0.0637 -0.0067 90   TYR H C   
2511 O O   . TYR B 94  ? 0.4233 0.2762 0.2366 -0.0218 -0.0674 -0.0031 90   TYR H O   
2512 C CB  . TYR B 94  ? 0.4165 0.2792 0.2459 -0.0012 -0.0632 -0.0091 90   TYR H CB  
2513 C CG  . TYR B 94  ? 0.4098 0.2678 0.2371 0.0089  -0.0609 -0.0119 90   TYR H CG  
2514 C CD1 . TYR B 94  ? 0.3942 0.2667 0.2395 0.0190  -0.0582 -0.0142 90   TYR H CD1 
2515 C CD2 . TYR B 94  ? 0.4411 0.2783 0.2460 0.0082  -0.0615 -0.0118 90   TYR H CD2 
2516 C CE1 . TYR B 94  ? 0.3984 0.2678 0.2415 0.0282  -0.0562 -0.0160 90   TYR H CE1 
2517 C CE2 . TYR B 94  ? 0.4399 0.2729 0.2421 0.0182  -0.0592 -0.0139 90   TYR H CE2 
2518 C CZ  . TYR B 94  ? 0.4241 0.2738 0.2457 0.0285  -0.0564 -0.0159 90   TYR H CZ  
2519 O OH  . TYR B 94  ? 0.4223 0.2698 0.2418 0.0383  -0.0542 -0.0174 90   TYR H OH  
2520 N N   . PHE B 95  ? 0.3942 0.2648 0.2345 -0.0050 -0.0615 -0.0078 91   PHE H N   
2521 C CA  . PHE B 95  ? 0.3808 0.2620 0.2296 -0.0123 -0.0630 -0.0054 91   PHE H CA  
2522 C C   . PHE B 95  ? 0.3547 0.2621 0.2294 -0.0107 -0.0630 -0.0052 91   PHE H C   
2523 O O   . PHE B 95  ? 0.3551 0.2713 0.2431 -0.0017 -0.0608 -0.0081 91   PHE H O   
2524 C CB  . PHE B 95  ? 0.3766 0.2500 0.2218 -0.0079 -0.0603 -0.0067 91   PHE H CB  
2525 C CG  . PHE B 95  ? 0.3929 0.2384 0.2098 -0.0096 -0.0602 -0.0064 91   PHE H CG  
2526 C CD1 . PHE B 95  ? 0.4098 0.2448 0.2119 -0.0217 -0.0635 -0.0033 91   PHE H CD1 
2527 C CD2 . PHE B 95  ? 0.4007 0.2297 0.2039 0.0006  -0.0569 -0.0087 91   PHE H CD2 
2528 C CE1 . PHE B 95  ? 0.4335 0.2390 0.2059 -0.0240 -0.0637 -0.0030 91   PHE H CE1 
2529 C CE2 . PHE B 95  ? 0.4384 0.2384 0.2120 -0.0001 -0.0565 -0.0083 91   PHE H CE2 
2530 C CZ  . PHE B 95  ? 0.4408 0.2280 0.1986 -0.0125 -0.0599 -0.0058 91   PHE H CZ  
2531 N N   . CYS B 96  ? 0.3549 0.2741 0.2355 -0.0192 -0.0654 -0.0016 92   CYS H N   
2532 C CA  . CYS B 96  ? 0.3435 0.2847 0.2460 -0.0168 -0.0647 -0.0011 92   CYS H CA  
2533 C C   . CYS B 96  ? 0.3414 0.2835 0.2464 -0.0183 -0.0638 -0.0006 92   CYS H C   
2534 O O   . CYS B 96  ? 0.3468 0.2753 0.2367 -0.0243 -0.0649 0.0007  92   CYS H O   
2535 C CB  . CYS B 96  ? 0.3682 0.3251 0.2775 -0.0225 -0.0670 0.0031  92   CYS H CB  
2536 S SG  . CYS B 96  ? 0.3991 0.3552 0.2967 -0.0367 -0.0705 0.0096  92   CYS H SG  
2537 N N   . LYS B 97  ? 0.3192 0.2753 0.2415 -0.0129 -0.0621 -0.0020 93   LYS H N   
2538 C CA  . LYS B 97  ? 0.3304 0.2883 0.2565 -0.0137 -0.0611 -0.0017 93   LYS H CA  
2539 C C   . LYS B 97  ? 0.2952 0.2711 0.2398 -0.0104 -0.0603 -0.0016 93   LYS H C   
2540 O O   . LYS B 97  ? 0.2725 0.2555 0.2263 -0.0047 -0.0597 -0.0034 93   LYS H O   
2541 C CB  . LYS B 97  ? 0.3645 0.3080 0.2829 -0.0076 -0.0588 -0.0052 93   LYS H CB  
2542 C CG  . LYS B 97  ? 0.4158 0.3636 0.3431 -0.0032 -0.0567 -0.0066 93   LYS H CG  
2543 C CD  . LYS B 97  ? 0.3692 0.3305 0.3141 0.0034  -0.0553 -0.0087 93   LYS H CD  
2544 C CE  . LYS B 97  ? 0.3546 0.3123 0.2987 0.0047  -0.0535 -0.0091 93   LYS H CE  
2545 N NZ  . LYS B 97  ? 0.3646 0.3351 0.3231 0.0047  -0.0533 -0.0089 93   LYS H NZ  
2546 N N   . ARG B 98  ? 0.2870 0.2678 0.2353 -0.0133 -0.0601 0.0001  94   ARG H N   
2547 C CA  . ARG B 98  ? 0.2670 0.2635 0.2301 -0.0108 -0.0594 0.0010  94   ARG H CA  
2548 C C   . ARG B 98  ? 0.2535 0.2495 0.2244 -0.0047 -0.0573 -0.0025 94   ARG H C   
2549 O O   . ARG B 98  ? 0.2350 0.2226 0.2009 -0.0051 -0.0565 -0.0036 94   ARG H O   
2550 C CB  . ARG B 98  ? 0.2636 0.2677 0.2262 -0.0178 -0.0605 0.0059  94   ARG H CB  
2551 C CG  . ARG B 98  ? 0.2675 0.2877 0.2429 -0.0145 -0.0595 0.0079  94   ARG H CG  
2552 C CD  . ARG B 98  ? 0.2717 0.3009 0.2462 -0.0213 -0.0606 0.0136  94   ARG H CD  
2553 N NE  . ARG B 98  ? 0.2688 0.2916 0.2395 -0.0253 -0.0606 0.0135  94   ARG H NE  
2554 C CZ  . ARG B 98  ? 0.2799 0.3122 0.2531 -0.0294 -0.0609 0.0179  94   ARG H CZ  
2555 N NH1 . ARG B 98  ? 0.2686 0.3181 0.2479 -0.0297 -0.0611 0.0232  94   ARG H NH1 
2556 N NH2 . ARG B 98  ? 0.2822 0.3074 0.2517 -0.0326 -0.0608 0.0172  94   ARG H NH2 
2557 N N   . SER B 99  ? 0.2294 0.2332 0.2107 0.0006  -0.0566 -0.0041 95   SER H N   
2558 C CA  . SER B 99  ? 0.2236 0.2297 0.2132 0.0048  -0.0554 -0.0064 95   SER H CA  
2559 C C   . SER B 99  ? 0.2169 0.2158 0.2050 0.0082  -0.0545 -0.0094 95   SER H C   
2560 O O   . SER B 99  ? 0.2194 0.2112 0.2003 0.0091  -0.0545 -0.0102 95   SER H O   
2561 C CB  . SER B 99  ? 0.2229 0.2325 0.2148 0.0019  -0.0549 -0.0045 95   SER H CB  
2562 O OG  . SER B 99  ? 0.2149 0.2288 0.2153 0.0055  -0.0541 -0.0059 95   SER H OG  
2563 N N   . LEU B 100 ? 0.2221 0.2240 0.2170 0.0103  -0.0537 -0.0106 96   LEU H N   
2564 C CA  . LEU B 100 ? 0.2252 0.2241 0.2204 0.0135  -0.0526 -0.0121 96   LEU H CA  
2565 C C   . LEU B 100 ? 0.2380 0.2309 0.2268 0.0114  -0.0513 -0.0110 96   LEU H C   
2566 O O   . LEU B 100 ? 0.2280 0.2204 0.2143 0.0069  -0.0518 -0.0093 96   LEU H O   
2567 C CB  . LEU B 100 ? 0.2236 0.2294 0.2286 0.0154  -0.0529 -0.0130 96   LEU H CB  
2568 C CG  . LEU B 100 ? 0.2242 0.2332 0.2330 0.0175  -0.0544 -0.0142 96   LEU H CG  
2569 C CD1 . LEU B 100 ? 0.2209 0.2342 0.2364 0.0174  -0.0554 -0.0147 96   LEU H CD1 
2570 C CD2 . LEU B 100 ? 0.2299 0.2372 0.2360 0.0206  -0.0544 -0.0150 96   LEU H CD2 
2571 N N   . PRO B 101 ? 0.2434 0.2320 0.2289 0.0150  -0.0497 -0.0115 97   PRO H N   
2572 C CA  . PRO B 101 ? 0.2491 0.2312 0.2280 0.0141  -0.0482 -0.0105 97   PRO H CA  
2573 C C   . PRO B 101 ? 0.2466 0.2356 0.2340 0.0111  -0.0483 -0.0099 97   PRO H C   
2574 O O   . PRO B 101 ? 0.2356 0.2335 0.2337 0.0123  -0.0487 -0.0104 97   PRO H O   
2575 C CB  . PRO B 101 ? 0.2579 0.2388 0.2353 0.0208  -0.0459 -0.0107 97   PRO H CB  
2576 C CG  . PRO B 101 ? 0.2551 0.2377 0.2331 0.0240  -0.0466 -0.0116 97   PRO H CG  
2577 C CD  . PRO B 101 ? 0.2369 0.2285 0.2256 0.0205  -0.0490 -0.0124 97   PRO H CD  
2578 N N   . GLY B 102 ? 0.2381 0.2224 0.2195 0.0066  -0.0484 -0.0085 98   GLY H N   
2579 C CA  . GLY B 102 ? 0.2394 0.2303 0.2281 0.0036  -0.0486 -0.0075 98   GLY H CA  
2580 C C   . GLY B 102 ? 0.2425 0.2315 0.2252 -0.0026 -0.0499 -0.0052 98   GLY H C   
2581 O O   . GLY B 102 ? 0.2468 0.2267 0.2176 -0.0054 -0.0506 -0.0044 98   GLY H O   
2582 N N   . THR B 103 ? 0.2506 0.2478 0.2402 -0.0050 -0.0503 -0.0037 99   THR H N   
2583 C CA  . THR B 103 ? 0.2677 0.2651 0.2519 -0.0116 -0.0514 -0.0004 99   THR H CA  
2584 C C   . THR B 103 ? 0.2513 0.2506 0.2307 -0.0154 -0.0533 0.0019  99   THR H C   
2585 O O   . THR B 103 ? 0.2428 0.2389 0.2133 -0.0222 -0.0549 0.0049  99   THR H O   
2586 C CB  . THR B 103 ? 0.3203 0.3271 0.3131 -0.0123 -0.0509 0.0010  99   THR H CB  
2587 O OG1 . THR B 103 ? 0.3853 0.3876 0.3694 -0.0187 -0.0517 0.0037  99   THR H OG1 
2588 C CG2 . THR B 103 ? 0.3262 0.3447 0.3257 -0.0119 -0.0515 0.0033  99   THR H CG2 
2589 N N   . PHE B 104 ? 0.2374 0.2408 0.2212 -0.0117 -0.0536 0.0007  100  PHE H N   
2590 C CA  . PHE B 104 ? 0.2323 0.2397 0.2126 -0.0151 -0.0553 0.0036  100  PHE H CA  
2591 C C   . PHE B 104 ? 0.2538 0.2489 0.2224 -0.0163 -0.0562 0.0023  100  PHE H C   
2592 O O   . PHE B 104 ? 0.2621 0.2593 0.2269 -0.0193 -0.0578 0.0044  100  PHE H O   
2593 C CB  . PHE B 104 ? 0.2180 0.2366 0.2081 -0.0103 -0.0550 0.0037  100  PHE H CB  
2594 C CG  . PHE B 104 ? 0.2067 0.2356 0.2049 -0.0087 -0.0540 0.0056  100  PHE H CG  
2595 C CD1 . PHE B 104 ? 0.2076 0.2465 0.2057 -0.0128 -0.0546 0.0109  100  PHE H CD1 
2596 C CD2 . PHE B 104 ? 0.2049 0.2337 0.2100 -0.0033 -0.0526 0.0026  100  PHE H CD2 
2597 C CE1 . PHE B 104 ? 0.2029 0.2512 0.2077 -0.0102 -0.0532 0.0130  100  PHE H CE1 
2598 C CE2 . PHE B 104 ? 0.2025 0.2382 0.2127 -0.0016 -0.0516 0.0043  100  PHE H CE2 
2599 C CZ  . PHE B 104 ? 0.1961 0.2415 0.2062 -0.0042 -0.0516 0.0094  100  PHE H CZ  
2600 N N   . ASP B 105 ? 0.2565 0.2398 0.2197 -0.0131 -0.0549 -0.0007 101  ASP H N   
2601 C CA  . ASP B 105 ? 0.2773 0.2469 0.2275 -0.0125 -0.0551 -0.0020 101  ASP H CA  
2602 C C   . ASP B 105 ? 0.2850 0.2466 0.2203 -0.0215 -0.0577 0.0012  101  ASP H C   
2603 O O   . ASP B 105 ? 0.2817 0.2398 0.2107 -0.0276 -0.0585 0.0036  101  ASP H O   
2604 C CB  . ASP B 105 ? 0.2808 0.2392 0.2250 -0.0073 -0.0528 -0.0045 101  ASP H CB  
2605 C CG  . ASP B 105 ? 0.2885 0.2340 0.2207 -0.0033 -0.0520 -0.0061 101  ASP H CG  
2606 O OD1 . ASP B 105 ? 0.2988 0.2493 0.2387 0.0034  -0.0507 -0.0081 101  ASP H OD1 
2607 O OD2 . ASP B 105 ? 0.3044 0.2341 0.2188 -0.0069 -0.0527 -0.0052 101  ASP H OD2 
2608 N N   . TYR B 106 ? 0.2937 0.2526 0.2230 -0.0233 -0.0592 0.0019  102  TYR H N   
2609 C CA  . TYR B 106 ? 0.3198 0.2722 0.2347 -0.0333 -0.0624 0.0058  102  TYR H CA  
2610 C C   . TYR B 106 ? 0.3203 0.2654 0.2276 -0.0319 -0.0631 0.0047  102  TYR H C   
2611 O O   . TYR B 106 ? 0.3149 0.2697 0.2342 -0.0254 -0.0620 0.0028  102  TYR H O   
2612 C CB  . TYR B 106 ? 0.3422 0.3131 0.2659 -0.0398 -0.0645 0.0110  102  TYR H CB  
2613 C CG  . TYR B 106 ? 0.4057 0.3713 0.3147 -0.0521 -0.0680 0.0161  102  TYR H CG  
2614 C CD1 . TYR B 106 ? 0.4632 0.4284 0.3693 -0.0577 -0.0688 0.0185  102  TYR H CD1 
2615 C CD2 . TYR B 106 ? 0.4716 0.4316 0.3684 -0.0589 -0.0710 0.0187  102  TYR H CD2 
2616 C CE1 . TYR B 106 ? 0.5228 0.4830 0.4143 -0.0704 -0.0727 0.0237  102  TYR H CE1 
2617 C CE2 . TYR B 106 ? 0.5228 0.4770 0.4042 -0.0720 -0.0750 0.0240  102  TYR H CE2 
2618 C CZ  . TYR B 106 ? 0.5560 0.5099 0.4344 -0.0779 -0.0760 0.0265  102  TYR H CZ  
2619 O OH  . TYR B 106 ? 0.6815 0.6297 0.5440 -0.0919 -0.0804 0.0321  102  TYR H OH  
2620 N N   . TRP B 107 ? 0.3368 0.2634 0.2234 -0.0374 -0.0649 0.0055  103  TRP H N   
2621 C CA  . TRP B 107 ? 0.3502 0.2651 0.2259 -0.0354 -0.0652 0.0040  103  TRP H CA  
2622 C C   . TRP B 107 ? 0.3730 0.2844 0.2358 -0.0469 -0.0694 0.0085  103  TRP H C   
2623 O O   . TRP B 107 ? 0.3866 0.2932 0.2384 -0.0575 -0.0723 0.0124  103  TRP H O   
2624 C CB  . TRP B 107 ? 0.3615 0.2531 0.2199 -0.0298 -0.0630 0.0007  103  TRP H CB  
2625 C CG  . TRP B 107 ? 0.3485 0.2456 0.2197 -0.0182 -0.0590 -0.0028 103  TRP H CG  
2626 C CD1 . TRP B 107 ? 0.3355 0.2403 0.2170 -0.0160 -0.0573 -0.0032 103  TRP H CD1 
2627 C CD2 . TRP B 107 ? 0.3427 0.2371 0.2153 -0.0077 -0.0562 -0.0060 103  TRP H CD2 
2628 N NE1 . TRP B 107 ? 0.3293 0.2386 0.2205 -0.0055 -0.0540 -0.0061 103  TRP H NE1 
2629 C CE2 . TRP B 107 ? 0.3425 0.2457 0.2281 -0.0002 -0.0533 -0.0076 103  TRP H CE2 
2630 C CE3 . TRP B 107 ? 0.3563 0.2427 0.2208 -0.0041 -0.0561 -0.0071 103  TRP H CE3 
2631 C CZ2 . TRP B 107 ? 0.3419 0.2480 0.2332 0.0102  -0.0505 -0.0098 103  TRP H CZ2 
2632 C CZ3 . TRP B 107 ? 0.3549 0.2437 0.2251 0.0069  -0.0530 -0.0096 103  TRP H CZ3 
2633 C CH2 . TRP B 107 ? 0.3576 0.2570 0.2413 0.0137  -0.0503 -0.0107 103  TRP H CH2 
2634 N N   . GLY B 108 ? 0.3658 0.2795 0.2291 -0.0457 -0.0702 0.0083  104  GLY H N   
2635 C CA  . GLY B 108 ? 0.3855 0.2907 0.2322 -0.0561 -0.0741 0.0121  104  GLY H CA  
2636 C C   . GLY B 108 ? 0.4214 0.2955 0.2398 -0.0588 -0.0748 0.0107  104  GLY H C   
2637 O O   . GLY B 108 ? 0.4139 0.2749 0.2279 -0.0493 -0.0713 0.0063  104  GLY H O   
2638 N N   . GLN B 109 ? 0.4431 0.3049 0.2417 -0.0704 -0.0791 0.0145  105  GLN H N   
2639 C CA  . GLN B 109 ? 0.4814 0.3087 0.2473 -0.0744 -0.0804 0.0136  105  GLN H CA  
2640 C C   . GLN B 109 ? 0.4913 0.3029 0.2479 -0.0642 -0.0778 0.0092  105  GLN H C   
2641 O O   . GLN B 109 ? 0.5017 0.2836 0.2317 -0.0627 -0.0772 0.0074  105  GLN H O   
2642 C CB  . GLN B 109 ? 0.5208 0.3409 0.2679 -0.0926 -0.0867 0.0200  105  GLN H CB  
2643 C CG  . GLN B 109 ? 0.5333 0.3524 0.2730 -0.0984 -0.0898 0.0224  105  GLN H CG  
2644 C CD  . GLN B 109 ? 0.5365 0.3907 0.3030 -0.1001 -0.0907 0.0264  105  GLN H CD  
2645 O OE1 . GLN B 109 ? 0.5191 0.3978 0.3118 -0.0926 -0.0878 0.0256  105  GLN H OE1 
2646 N NE2 . GLN B 109 ? 0.5506 0.4072 0.3095 -0.1100 -0.0948 0.0310  105  GLN H NE2 
2647 N N   . GLY B 110 ? 0.4729 0.3031 0.2498 -0.0565 -0.0759 0.0074  106  GLY H N   
2648 C CA  . GLY B 110 ? 0.4781 0.2973 0.2489 -0.0466 -0.0735 0.0037  106  GLY H CA  
2649 C C   . GLY B 110 ? 0.4868 0.2990 0.2444 -0.0549 -0.0773 0.0062  106  GLY H C   
2650 O O   . GLY B 110 ? 0.4992 0.3052 0.2424 -0.0694 -0.0821 0.0110  106  GLY H O   
2651 N N   . THR B 111 ? 0.4874 0.3014 0.2500 -0.0461 -0.0753 0.0034  107  THR H N   
2652 C CA  . THR B 111 ? 0.5047 0.3122 0.2563 -0.0509 -0.0780 0.0048  107  THR H CA  
2653 C C   . THR B 111 ? 0.5142 0.2987 0.2495 -0.0395 -0.0747 0.0004  107  THR H C   
2654 O O   . THR B 111 ? 0.4992 0.2943 0.2509 -0.0261 -0.0705 -0.0032 107  THR H O   
2655 C CB  . THR B 111 ? 0.4799 0.3174 0.2576 -0.0506 -0.0786 0.0063  107  THR H CB  
2656 O OG1 . THR B 111 ? 0.4722 0.3304 0.2625 -0.0602 -0.0813 0.0114  107  THR H OG1 
2657 C CG2 . THR B 111 ? 0.5068 0.3379 0.2736 -0.0548 -0.0811 0.0078  107  THR H CG2 
2658 N N   . THR B 112 ? 0.5752 0.3295 0.2786 -0.0449 -0.0766 0.0013  108  THR H N   
2659 C CA  . THR B 112 ? 0.6141 0.3447 0.2982 -0.0342 -0.0736 -0.0020 108  THR H CA  
2660 C C   . THR B 112 ? 0.6201 0.3609 0.3127 -0.0331 -0.0745 -0.0022 108  THR H C   
2661 O O   . THR B 112 ? 0.6623 0.4053 0.3502 -0.0461 -0.0793 0.0014  108  THR H O   
2662 C CB  . THR B 112 ? 0.6733 0.3640 0.3162 -0.0402 -0.0754 -0.0010 108  THR H CB  
2663 O OG1 . THR B 112 ? 0.6776 0.3624 0.3160 -0.0413 -0.0746 -0.0007 108  THR H OG1 
2664 C CG2 . THR B 112 ? 0.7052 0.3711 0.3272 -0.0270 -0.0715 -0.0043 108  THR H CG2 
2665 N N   . LEU B 113 ? 0.6062 0.3545 0.3111 -0.0185 -0.0702 -0.0059 109  LEU H N   
2666 C CA  . LEU B 113 ? 0.6122 0.3647 0.3205 -0.0156 -0.0705 -0.0066 109  LEU H CA  
2667 C C   . LEU B 113 ? 0.6236 0.3464 0.3047 -0.0062 -0.0676 -0.0089 109  LEU H C   
2668 O O   . LEU B 113 ? 0.5947 0.3134 0.2757 0.0069  -0.0629 -0.0113 109  LEU H O   
2669 C CB  . LEU B 113 ? 0.5854 0.3693 0.3278 -0.0063 -0.0680 -0.0087 109  LEU H CB  
2670 C CG  . LEU B 113 ? 0.5908 0.3791 0.3376 -0.0007 -0.0675 -0.0101 109  LEU H CG  
2671 C CD1 . LEU B 113 ? 0.5887 0.3787 0.3308 -0.0135 -0.0723 -0.0067 109  LEU H CD1 
2672 C CD2 . LEU B 113 ? 0.5637 0.3793 0.3410 0.0087  -0.0650 -0.0123 109  LEU H CD2 
2673 N N   . THR B 114 ? 0.6651 0.3685 0.3237 -0.0127 -0.0705 -0.0076 110  THR H N   
2674 C CA  . THR B 114 ? 0.6878 0.3635 0.3204 -0.0028 -0.0677 -0.0097 110  THR H CA  
2675 C C   . THR B 114 ? 0.6931 0.3813 0.3375 0.0002  -0.0680 -0.0105 110  THR H C   
2676 O O   . THR B 114 ? 0.6935 0.3873 0.3389 -0.0125 -0.0728 -0.0079 110  THR H O   
2677 C CB  . THR B 114 ? 0.7447 0.3818 0.3359 -0.0132 -0.0711 -0.0076 110  THR H CB  
2678 O OG1 . THR B 114 ? 0.7479 0.3766 0.3312 -0.0171 -0.0712 -0.0067 110  THR H OG1 
2679 C CG2 . THR B 114 ? 0.7692 0.3740 0.3297 -0.0023 -0.0679 -0.0096 110  THR H CG2 
2680 N N   . VAL B 115 ? 0.6832 0.3771 0.3364 0.0163  -0.0631 -0.0133 111  VAL H N   
2681 C CA  . VAL B 115 ? 0.7162 0.4172 0.3760 0.0215  -0.0627 -0.0145 111  VAL H CA  
2682 C C   . VAL B 115 ? 0.7825 0.4480 0.4062 0.0271  -0.0611 -0.0150 111  VAL H C   
2683 O O   . VAL B 115 ? 0.8205 0.4721 0.4316 0.0403  -0.0563 -0.0162 111  VAL H O   
2684 C CB  . VAL B 115 ? 0.6717 0.4016 0.3629 0.0345  -0.0590 -0.0166 111  VAL H CB  
2685 C CG1 . VAL B 115 ? 0.6644 0.4031 0.3636 0.0386  -0.0591 -0.0176 111  VAL H CG1 
2686 C CG2 . VAL B 115 ? 0.6381 0.3975 0.3597 0.0294  -0.0603 -0.0162 111  VAL H CG2 
2687 N N   . SER B 116 ? 0.8580 0.5084 0.4638 0.0171  -0.0651 -0.0136 112  SER H N   
2688 C CA  . SER B 116 ? 0.9157 0.5316 0.4862 0.0215  -0.0642 -0.0141 112  SER H CA  
2689 C C   . SER B 116 ? 0.9209 0.5407 0.4971 0.0422  -0.0577 -0.0166 112  SER H C   
2690 O O   . SER B 116 ? 0.9812 0.5758 0.5323 0.0530  -0.0537 -0.0171 112  SER H O   
2691 C CB  . SER B 116 ? 0.9435 0.5574 0.5086 0.0099  -0.0691 -0.0125 112  SER H CB  
2692 O OG  . SER B 116 ? 0.9729 0.5930 0.5401 -0.0095 -0.0752 -0.0089 112  SER H OG  
2693 N N   . GLY B 126 ? 0.6339 0.4583 0.3540 0.1397  -0.0235 0.0119  122  GLY H N   
2694 C CA  . GLY B 126 ? 0.5965 0.4460 0.3374 0.1370  -0.0277 0.0072  122  GLY H CA  
2695 C C   . GLY B 126 ? 0.5827 0.4380 0.3311 0.1300  -0.0249 0.0088  122  GLY H C   
2696 O O   . GLY B 126 ? 0.6415 0.5131 0.3993 0.1325  -0.0286 0.0052  122  GLY H O   
2697 N N   . GLY B 127 ? 0.5653 0.4079 0.3090 0.1218  -0.0187 0.0136  123  GLY H N   
2698 C CA  . GLY B 127 ? 0.5303 0.3802 0.2820 0.1147  -0.0159 0.0148  123  GLY H CA  
2699 C C   . GLY B 127 ? 0.5100 0.3748 0.2827 0.1039  -0.0166 0.0126  123  GLY H C   
2700 O O   . GLY B 127 ? 0.4967 0.3717 0.2787 0.0994  -0.0160 0.0121  123  GLY H O   
2701 N N   . GLY B 128 ? 0.5097 0.3755 0.2890 0.1003  -0.0180 0.0112  124  GLY H N   
2702 C CA  . GLY B 128 ? 0.5001 0.3794 0.2982 0.0908  -0.0189 0.0090  124  GLY H CA  
2703 C C   . GLY B 128 ? 0.4845 0.3828 0.2962 0.0931  -0.0246 0.0043  124  GLY H C   
2704 O O   . GLY B 128 ? 0.4951 0.3976 0.3028 0.1022  -0.0284 0.0019  124  GLY H O   
2705 N N   . GLY B 129 ? 0.5054 0.4148 0.3324 0.0850  -0.0251 0.0028  125  GLY H N   
2706 C CA  . GLY B 129 ? 0.4829 0.4089 0.3231 0.0853  -0.0301 -0.0015 125  GLY H CA  
2707 C C   . GLY B 129 ? 0.4911 0.4221 0.3354 0.0872  -0.0336 -0.0043 125  GLY H C   
2708 O O   . GLY B 129 ? 0.4997 0.4221 0.3400 0.0856  -0.0317 -0.0026 125  GLY H O   
2709 N N   . SER B 130 ? 0.4782 0.4228 0.3305 0.0897  -0.0383 -0.0087 126  SER H N   
2710 C CA  . SER B 130 ? 0.4885 0.4419 0.3476 0.0901  -0.0417 -0.0121 126  SER H CA  
2711 C C   . SER B 130 ? 0.4755 0.4410 0.3499 0.0824  -0.0434 -0.0144 126  SER H C   
2712 O O   . SER B 130 ? 0.4466 0.4149 0.3251 0.0795  -0.0433 -0.0144 126  SER H O   
2713 C CB  . SER B 130 ? 0.4911 0.4506 0.3455 0.0997  -0.0456 -0.0157 126  SER H CB  
2714 O OG  . SER B 130 ? 0.5690 0.5151 0.4074 0.1073  -0.0439 -0.0132 126  SER H OG  
2715 N N   . SER B 131 ? 0.4987 0.4702 0.3804 0.0792  -0.0448 -0.0161 127  SER H N   
2716 C CA  . SER B 131 ? 0.4942 0.4770 0.3891 0.0725  -0.0468 -0.0186 127  SER H CA  
2717 C C   . SER B 131 ? 0.5213 0.5154 0.4197 0.0756  -0.0506 -0.0231 127  SER H C   
2718 O O   . SER B 131 ? 0.6031 0.5992 0.4950 0.0836  -0.0524 -0.0250 127  SER H O   
2719 C CB  . SER B 131 ? 0.4945 0.4808 0.3945 0.0693  -0.0471 -0.0193 127  SER H CB  
2720 O OG  . SER B 131 ? 0.4830 0.4586 0.3791 0.0670  -0.0438 -0.0158 127  SER H OG  
2721 N N   . GLY B 132 ? 0.5011 0.5021 0.4087 0.0699  -0.0520 -0.0249 128  GLY H N   
2722 C CA  . GLY B 132 ? 0.5076 0.5204 0.4207 0.0703  -0.0558 -0.0298 128  GLY H CA  
2723 C C   . GLY B 132 ? 0.5095 0.5328 0.4280 0.0694  -0.0577 -0.0332 128  GLY H C   
2724 O O   . GLY B 132 ? 0.4594 0.4815 0.3810 0.0651  -0.0563 -0.0316 128  GLY H O   
2725 N N   . SER B 133 ? 0.5139 0.5485 0.4339 0.0730  -0.0610 -0.0382 129  SER H N   
2726 C CA  . SER B 133 ? 0.5368 0.5848 0.4632 0.0715  -0.0630 -0.0425 129  SER H CA  
2727 C C   . SER B 133 ? 0.5016 0.5531 0.4380 0.0608  -0.0626 -0.0429 129  SER H C   
2728 O O   . SER B 133 ? 0.4946 0.5541 0.4362 0.0572  -0.0628 -0.0445 129  SER H O   
2729 C CB  . SER B 133 ? 0.5432 0.6037 0.4693 0.0775  -0.0666 -0.0483 129  SER H CB  
2730 O OG  . SER B 133 ? 0.5595 0.6229 0.4895 0.0743  -0.0681 -0.0507 129  SER H OG  
2731 N N   . SER B 134 ? 0.4896 0.5342 0.4273 0.0562  -0.0620 -0.0410 130  SER H N   
2732 C CA  . SER B 134 ? 0.4699 0.5146 0.4148 0.0467  -0.0617 -0.0410 130  SER H CA  
2733 C C   . SER B 134 ? 0.4382 0.4738 0.3834 0.0425  -0.0586 -0.0361 130  SER H C   
2734 O O   . SER B 134 ? 0.4214 0.4566 0.3716 0.0350  -0.0582 -0.0357 130  SER H O   
2735 C CB  . SER B 134 ? 0.5395 0.5805 0.4841 0.0456  -0.0629 -0.0418 130  SER H CB  
2736 O OG  . SER B 134 ? 0.5804 0.6187 0.5296 0.0373  -0.0626 -0.0414 130  SER H OG  
2737 N N   . ASP B 135 ? 0.3989 0.4267 0.3384 0.0466  -0.0565 -0.0325 1001 ASP H N   
2738 C CA  . ASP B 135 ? 0.3639 0.3839 0.3038 0.0427  -0.0537 -0.0283 1001 ASP H CA  
2739 C C   . ASP B 135 ? 0.3500 0.3755 0.2946 0.0390  -0.0535 -0.0289 1001 ASP H C   
2740 O O   . ASP B 135 ? 0.3337 0.3674 0.2785 0.0421  -0.0547 -0.0314 1001 ASP H O   
2741 C CB  . ASP B 135 ? 0.3817 0.3925 0.3143 0.0473  -0.0514 -0.0249 1001 ASP H CB  
2742 C CG  . ASP B 135 ? 0.3905 0.3954 0.3181 0.0504  -0.0508 -0.0237 1001 ASP H CG  
2743 O OD1 . ASP B 135 ? 0.4202 0.4175 0.3407 0.0541  -0.0486 -0.0211 1001 ASP H OD1 
2744 O OD2 . ASP B 135 ? 0.3507 0.3584 0.2808 0.0492  -0.0525 -0.0255 1001 ASP H OD2 
2745 N N   . VAL B 136 ? 0.3214 0.3431 0.2692 0.0331  -0.0520 -0.0266 1002 VAL H N   
2746 C CA  . VAL B 136 ? 0.3071 0.3334 0.2585 0.0301  -0.0513 -0.0266 1002 VAL H CA  
2747 C C   . VAL B 136 ? 0.3049 0.3276 0.2517 0.0348  -0.0500 -0.0249 1002 VAL H C   
2748 O O   . VAL B 136 ? 0.3131 0.3262 0.2558 0.0362  -0.0482 -0.0220 1002 VAL H O   
2749 C CB  . VAL B 136 ? 0.3019 0.3247 0.2569 0.0233  -0.0502 -0.0247 1002 VAL H CB  
2750 C CG1 . VAL B 136 ? 0.3005 0.3287 0.2586 0.0206  -0.0495 -0.0247 1002 VAL H CG1 
2751 C CG2 . VAL B 136 ? 0.2997 0.3228 0.2571 0.0188  -0.0514 -0.0261 1002 VAL H CG2 
2752 N N   . VAL B 137 ? 0.3098 0.3401 0.2572 0.0371  -0.0507 -0.0268 1003 VAL H N   
2753 C CA  . VAL B 137 ? 0.3042 0.3308 0.2470 0.0415  -0.0497 -0.0255 1003 VAL H CA  
2754 C C   . VAL B 137 ? 0.3051 0.3337 0.2523 0.0368  -0.0487 -0.0247 1003 VAL H C   
2755 O O   . VAL B 137 ? 0.3046 0.3435 0.2574 0.0332  -0.0495 -0.0268 1003 VAL H O   
2756 C CB  . VAL B 137 ? 0.3154 0.3487 0.2543 0.0490  -0.0517 -0.0286 1003 VAL H CB  
2757 C CG1 . VAL B 137 ? 0.3282 0.3572 0.2616 0.0538  -0.0511 -0.0277 1003 VAL H CG1 
2758 C CG2 . VAL B 137 ? 0.3266 0.3567 0.2600 0.0543  -0.0527 -0.0292 1003 VAL H CG2 
2759 N N   . MET B 138 ? 0.2993 0.3186 0.2437 0.0365  -0.0468 -0.0218 1004 MET H N   
2760 C CA  . MET B 138 ? 0.3054 0.3257 0.2528 0.0332  -0.0458 -0.0209 1004 MET H CA  
2761 C C   . MET B 138 ? 0.3223 0.3413 0.2648 0.0387  -0.0459 -0.0214 1004 MET H C   
2762 O O   . MET B 138 ? 0.3530 0.3619 0.2885 0.0426  -0.0450 -0.0200 1004 MET H O   
2763 C CB  . MET B 138 ? 0.3032 0.3149 0.2513 0.0290  -0.0438 -0.0180 1004 MET H CB  
2764 C CG  . MET B 138 ? 0.3008 0.3122 0.2522 0.0247  -0.0440 -0.0176 1004 MET H CG  
2765 S SD  . MET B 138 ? 0.3008 0.3212 0.2585 0.0191  -0.0450 -0.0190 1004 MET H SD  
2766 C CE  . MET B 138 ? 0.3399 0.3587 0.2994 0.0161  -0.0435 -0.0172 1004 MET H CE  
2767 N N   . THR B 139 ? 0.3288 0.3580 0.2741 0.0394  -0.0469 -0.0236 1005 THR H N   
2768 C CA  . THR B 139 ? 0.3337 0.3633 0.2739 0.0459  -0.0477 -0.0249 1005 THR H CA  
2769 C C   . THR B 139 ? 0.3233 0.3524 0.2655 0.0434  -0.0467 -0.0240 1005 THR H C   
2770 O O   . THR B 139 ? 0.3067 0.3458 0.2554 0.0393  -0.0467 -0.0248 1005 THR H O   
2771 C CB  . THR B 139 ? 0.3460 0.3898 0.2873 0.0502  -0.0501 -0.0290 1005 THR H CB  
2772 O OG1 . THR B 139 ? 0.3557 0.3993 0.2948 0.0528  -0.0511 -0.0299 1005 THR H OG1 
2773 C CG2 . THR B 139 ? 0.3446 0.3889 0.2799 0.0579  -0.0512 -0.0306 1005 THR H CG2 
2774 N N   . GLN B 140 ? 0.3283 0.3460 0.2645 0.0458  -0.0457 -0.0224 1006 GLN H N   
2775 C CA  . GLN B 140 ? 0.3321 0.3496 0.2688 0.0454  -0.0453 -0.0224 1006 GLN H CA  
2776 C C   . GLN B 140 ? 0.3724 0.3918 0.3027 0.0536  -0.0471 -0.0248 1006 GLN H C   
2777 O O   . GLN B 140 ? 0.4158 0.4236 0.3370 0.0588  -0.0472 -0.0243 1006 GLN H O   
2778 C CB  . GLN B 140 ? 0.3054 0.3095 0.2396 0.0425  -0.0432 -0.0198 1006 GLN H CB  
2779 C CG  . GLN B 140 ? 0.2963 0.3008 0.2369 0.0354  -0.0419 -0.0181 1006 GLN H CG  
2780 C CD  . GLN B 140 ? 0.2939 0.2874 0.2325 0.0326  -0.0399 -0.0163 1006 GLN H CD  
2781 O OE1 . GLN B 140 ? 0.2656 0.2537 0.2035 0.0307  -0.0387 -0.0150 1006 GLN H OE1 
2782 N NE2 . GLN B 140 ? 0.3092 0.3003 0.2473 0.0323  -0.0394 -0.0166 1006 GLN H NE2 
2783 N N   . SER B 141 ? 0.4086 0.4421 0.3430 0.0549  -0.0485 -0.0275 1007 SER H N   
2784 C CA  . SER B 141 ? 0.4749 0.5140 0.4039 0.0636  -0.0508 -0.0307 1007 SER H CA  
2785 C C   . SER B 141 ? 0.4926 0.5205 0.4138 0.0681  -0.0509 -0.0303 1007 SER H C   
2786 O O   . SER B 141 ? 0.5199 0.5438 0.4319 0.0769  -0.0526 -0.0320 1007 SER H O   
2787 C CB  . SER B 141 ? 0.4951 0.5543 0.4315 0.0628  -0.0520 -0.0339 1007 SER H CB  
2788 O OG  . SER B 141 ? 0.5106 0.5777 0.4524 0.0590  -0.0521 -0.0346 1007 SER H OG  
2789 N N   . HIS B 142 ? 0.4800 0.5006 0.4031 0.0629  -0.0491 -0.0281 1008 HIS H N   
2790 C CA  . HIS B 142 ? 0.4820 0.4902 0.3973 0.0665  -0.0491 -0.0280 1008 HIS H CA  
2791 C C   . HIS B 142 ? 0.4460 0.4358 0.3561 0.0635  -0.0469 -0.0251 1008 HIS H C   
2792 O O   . HIS B 142 ? 0.4261 0.4144 0.3421 0.0561  -0.0450 -0.0232 1008 HIS H O   
2793 C CB  . HIS B 142 ? 0.5372 0.5529 0.4579 0.0641  -0.0491 -0.0288 1008 HIS H CB  
2794 C CG  . HIS B 142 ? 0.6034 0.6379 0.5288 0.0668  -0.0508 -0.0318 1008 HIS H CG  
2795 N ND1 . HIS B 142 ? 0.6555 0.6968 0.5764 0.0748  -0.0531 -0.0347 1008 HIS H ND1 
2796 C CD2 . HIS B 142 ? 0.6311 0.6798 0.5649 0.0626  -0.0504 -0.0323 1008 HIS H CD2 
2797 C CE1 . HIS B 142 ? 0.6675 0.7277 0.5948 0.0749  -0.0540 -0.0373 1008 HIS H CE1 
2798 N NE2 . HIS B 142 ? 0.6804 0.7449 0.6154 0.0671  -0.0521 -0.0357 1008 HIS H NE2 
2799 N N   . LYS B 143 ? 0.4247 0.4005 0.3230 0.0693  -0.0472 -0.0249 1009 LYS H N   
2800 C CA  . LYS B 143 ? 0.4368 0.3942 0.3288 0.0661  -0.0446 -0.0223 1009 LYS H CA  
2801 C C   . LYS B 143 ? 0.4025 0.3516 0.2930 0.0634  -0.0437 -0.0224 1009 LYS H C   
2802 O O   . LYS B 143 ? 0.3928 0.3315 0.2828 0.0574  -0.0411 -0.0207 1009 LYS H O   
2803 C CB  . LYS B 143 ? 0.4815 0.4253 0.3596 0.0734  -0.0449 -0.0219 1009 LYS H CB  
2804 C CG  . LYS B 143 ? 0.5359 0.4882 0.4148 0.0770  -0.0462 -0.0223 1009 LYS H CG  
2805 C CD  . LYS B 143 ? 0.5867 0.5259 0.4586 0.0764  -0.0441 -0.0196 1009 LYS H CD  
2806 C CE  . LYS B 143 ? 0.5893 0.5396 0.4666 0.0766  -0.0449 -0.0198 1009 LYS H CE  
2807 N NZ  . LYS B 143 ? 0.5874 0.5354 0.4706 0.0682  -0.0421 -0.0171 1009 LYS H NZ  
2808 N N   . PHE B 144 ? 0.4103 0.3649 0.3000 0.0680  -0.0458 -0.0249 1010 PHE H N   
2809 C CA  . PHE B 144 ? 0.4147 0.3629 0.3029 0.0665  -0.0456 -0.0258 1010 PHE H CA  
2810 C C   . PHE B 144 ? 0.4119 0.3771 0.3093 0.0663  -0.0471 -0.0277 1010 PHE H C   
2811 O O   . PHE B 144 ? 0.4067 0.3847 0.3053 0.0717  -0.0493 -0.0296 1010 PHE H O   
2812 C CB  . PHE B 144 ? 0.4492 0.3827 0.3231 0.0744  -0.0470 -0.0272 1010 PHE H CB  
2813 C CG  . PHE B 144 ? 0.4974 0.4118 0.3601 0.0747  -0.0451 -0.0250 1010 PHE H CG  
2814 C CD1 . PHE B 144 ? 0.5201 0.4198 0.3803 0.0675  -0.0420 -0.0234 1010 PHE H CD1 
2815 C CD2 . PHE B 144 ? 0.5348 0.4470 0.3897 0.0819  -0.0462 -0.0247 1010 PHE H CD2 
2816 C CE1 . PHE B 144 ? 0.5649 0.4472 0.4146 0.0669  -0.0397 -0.0211 1010 PHE H CE1 
2817 C CE2 . PHE B 144 ? 0.5563 0.4500 0.3997 0.0823  -0.0442 -0.0223 1010 PHE H CE2 
2818 C CZ  . PHE B 144 ? 0.5602 0.4389 0.4011 0.0744  -0.0407 -0.0203 1010 PHE H CZ  
2819 N N   . MET B 145 ? 0.3842 0.3495 0.2871 0.0605  -0.0460 -0.0276 1011 MET H N   
2820 C CA  . MET B 145 ? 0.3962 0.3752 0.3060 0.0605  -0.0472 -0.0293 1011 MET H CA  
2821 C C   . MET B 145 ? 0.3771 0.3471 0.2840 0.0595  -0.0470 -0.0305 1011 MET H C   
2822 O O   . MET B 145 ? 0.3655 0.3242 0.2713 0.0543  -0.0451 -0.0295 1011 MET H O   
2823 C CB  . MET B 145 ? 0.3898 0.3819 0.3114 0.0537  -0.0460 -0.0278 1011 MET H CB  
2824 C CG  . MET B 145 ? 0.4146 0.4172 0.3395 0.0545  -0.0464 -0.0273 1011 MET H CG  
2825 S SD  . MET B 145 ? 0.4389 0.4564 0.3759 0.0470  -0.0452 -0.0258 1011 MET H SD  
2826 C CE  . MET B 145 ? 0.4635 0.4934 0.4034 0.0490  -0.0463 -0.0278 1011 MET H CE  
2827 N N   . SER B 146 ? 0.3923 0.3687 0.2985 0.0642  -0.0490 -0.0330 1012 SER H N   
2828 C CA  . SER B 146 ? 0.3963 0.3663 0.3002 0.0641  -0.0495 -0.0349 1012 SER H CA  
2829 C C   . SER B 146 ? 0.3780 0.3628 0.2922 0.0605  -0.0494 -0.0352 1012 SER H C   
2830 O O   . SER B 146 ? 0.3528 0.3528 0.2718 0.0623  -0.0501 -0.0353 1012 SER H O   
2831 C CB  . SER B 146 ? 0.4319 0.3967 0.3256 0.0732  -0.0521 -0.0377 1012 SER H CB  
2832 O OG  . SER B 146 ? 0.5083 0.4529 0.3902 0.0751  -0.0517 -0.0373 1012 SER H OG  
2833 N N   . THR B 147 ? 0.3809 0.3614 0.2974 0.0560  -0.0486 -0.0359 1013 THR H N   
2834 C CA  . THR B 147 ? 0.3810 0.3743 0.3051 0.0543  -0.0488 -0.0366 1013 THR H CA  
2835 C C   . THR B 147 ? 0.3841 0.3708 0.3055 0.0548  -0.0497 -0.0395 1013 THR H C   
2836 O O   . THR B 147 ? 0.4129 0.3842 0.3272 0.0546  -0.0496 -0.0408 1013 THR H O   
2837 C CB  . THR B 147 ? 0.4101 0.4079 0.3427 0.0468  -0.0469 -0.0348 1013 THR H CB  
2838 O OG1 . THR B 147 ? 0.4168 0.4055 0.3495 0.0418  -0.0450 -0.0332 1013 THR H OG1 
2839 C CG2 . THR B 147 ? 0.3771 0.3907 0.3166 0.0461  -0.0468 -0.0334 1013 THR H CG2 
2840 N N   . SER B 148 ? 0.3866 0.3845 0.3134 0.0546  -0.0503 -0.0405 1014 SER H N   
2841 C CA  . SER B 148 ? 0.3687 0.3633 0.2952 0.0542  -0.0511 -0.0435 1014 SER H CA  
2842 C C   . SER B 148 ? 0.3611 0.3624 0.2960 0.0480  -0.0496 -0.0426 1014 SER H C   
2843 O O   . SER B 148 ? 0.3099 0.3221 0.2504 0.0464  -0.0487 -0.0399 1014 SER H O   
2844 C CB  . SER B 148 ? 0.3940 0.3965 0.3184 0.0609  -0.0534 -0.0459 1014 SER H CB  
2845 O OG  . SER B 148 ? 0.4327 0.4282 0.3483 0.0675  -0.0550 -0.0470 1014 SER H OG  
2846 N N   . VAL B 149 ? 0.3284 0.3231 0.2636 0.0445  -0.0493 -0.0449 1015 VAL H N   
2847 C CA  . VAL B 149 ? 0.3210 0.3229 0.2637 0.0398  -0.0484 -0.0449 1015 VAL H CA  
2848 C C   . VAL B 149 ? 0.2981 0.3147 0.2448 0.0427  -0.0491 -0.0440 1015 VAL H C   
2849 O O   . VAL B 149 ? 0.3115 0.3321 0.2558 0.0477  -0.0509 -0.0459 1015 VAL H O   
2850 C CB  . VAL B 149 ? 0.3369 0.3321 0.2794 0.0366  -0.0485 -0.0489 1015 VAL H CB  
2851 C CG1 . VAL B 149 ? 0.3256 0.3308 0.2752 0.0339  -0.0483 -0.0500 1015 VAL H CG1 
2852 C CG2 . VAL B 149 ? 0.3543 0.3358 0.2937 0.0316  -0.0467 -0.0490 1015 VAL H CG2 
2853 N N   . GLY B 150 ? 0.2827 0.3066 0.2346 0.0397  -0.0478 -0.0412 1016 GLY H N   
2854 C CA  . GLY B 150 ? 0.2776 0.3137 0.2324 0.0413  -0.0479 -0.0397 1016 GLY H CA  
2855 C C   . GLY B 150 ? 0.2703 0.3130 0.2250 0.0425  -0.0472 -0.0365 1016 GLY H C   
2856 O O   . GLY B 150 ? 0.2539 0.3058 0.2107 0.0422  -0.0465 -0.0344 1016 GLY H O   
2857 N N   . ASP B 151 ? 0.2921 0.3305 0.2440 0.0436  -0.0473 -0.0360 1017 ASP H N   
2858 C CA  . ASP B 151 ? 0.3058 0.3518 0.2583 0.0444  -0.0467 -0.0337 1017 ASP H CA  
2859 C C   . ASP B 151 ? 0.3016 0.3478 0.2576 0.0392  -0.0449 -0.0303 1017 ASP H C   
2860 O O   . ASP B 151 ? 0.2784 0.3176 0.2356 0.0357  -0.0442 -0.0299 1017 ASP H O   
2861 C CB  . ASP B 151 ? 0.3408 0.3824 0.2886 0.0484  -0.0478 -0.0350 1017 ASP H CB  
2862 C CG  . ASP B 151 ? 0.3537 0.3977 0.2974 0.0549  -0.0499 -0.0382 1017 ASP H CG  
2863 O OD1 . ASP B 151 ? 0.3836 0.4345 0.3288 0.0561  -0.0503 -0.0392 1017 ASP H OD1 
2864 O OD2 . ASP B 151 ? 0.4026 0.4411 0.3408 0.0592  -0.0512 -0.0397 1017 ASP H OD2 
2865 N N   . ARG B 152 ? 0.3054 0.3596 0.2626 0.0386  -0.0441 -0.0283 1018 ARG H N   
2866 C CA  . ARG B 152 ? 0.3207 0.3743 0.2803 0.0340  -0.0426 -0.0254 1018 ARG H CA  
2867 C C   . ARG B 152 ? 0.3214 0.3708 0.2792 0.0350  -0.0430 -0.0257 1018 ARG H C   
2868 O O   . ARG B 152 ? 0.3158 0.3692 0.2713 0.0394  -0.0441 -0.0274 1018 ARG H O   
2869 C CB  . ARG B 152 ? 0.3570 0.4206 0.3185 0.0317  -0.0413 -0.0232 1018 ARG H CB  
2870 C CG  . ARG B 152 ? 0.3859 0.4482 0.3491 0.0269  -0.0400 -0.0206 1018 ARG H CG  
2871 C CD  . ARG B 152 ? 0.4348 0.5029 0.3986 0.0231  -0.0382 -0.0180 1018 ARG H CD  
2872 N NE  . ARG B 152 ? 0.4849 0.5499 0.4476 0.0227  -0.0379 -0.0170 1018 ARG H NE  
2873 C CZ  . ARG B 152 ? 0.5525 0.6230 0.5139 0.0241  -0.0375 -0.0169 1018 ARG H CZ  
2874 N NH1 . ARG B 152 ? 0.5617 0.6286 0.5214 0.0244  -0.0374 -0.0161 1018 ARG H NH1 
2875 N NH2 . ARG B 152 ? 0.5756 0.6560 0.5370 0.0256  -0.0371 -0.0176 1018 ARG H NH2 
2876 N N   . VAL B 153 ? 0.2954 0.3371 0.2537 0.0319  -0.0423 -0.0244 1019 VAL H N   
2877 C CA  . VAL B 153 ? 0.3139 0.3503 0.2700 0.0329  -0.0426 -0.0244 1019 VAL H CA  
2878 C C   . VAL B 153 ? 0.2892 0.3298 0.2482 0.0293  -0.0416 -0.0222 1019 VAL H C   
2879 O O   . VAL B 153 ? 0.2511 0.2905 0.2125 0.0253  -0.0406 -0.0205 1019 VAL H O   
2880 C CB  . VAL B 153 ? 0.3287 0.3523 0.2824 0.0318  -0.0422 -0.0248 1019 VAL H CB  
2881 C CG1 . VAL B 153 ? 0.3608 0.3783 0.3124 0.0315  -0.0418 -0.0238 1019 VAL H CG1 
2882 C CG2 . VAL B 153 ? 0.3577 0.3758 0.3073 0.0351  -0.0432 -0.0274 1019 VAL H CG2 
2883 N N   . SER B 154 ? 0.2795 0.3250 0.2380 0.0309  -0.0420 -0.0226 1020 SER H N   
2884 C CA  . SER B 154 ? 0.2894 0.3380 0.2505 0.0273  -0.0413 -0.0211 1020 SER H CA  
2885 C C   . SER B 154 ? 0.2941 0.3373 0.2524 0.0297  -0.0420 -0.0217 1020 SER H C   
2886 O O   . SER B 154 ? 0.3020 0.3492 0.2578 0.0346  -0.0433 -0.0236 1020 SER H O   
2887 C CB  . SER B 154 ? 0.3127 0.3748 0.2765 0.0261  -0.0410 -0.0214 1020 SER H CB  
2888 O OG  . SER B 154 ? 0.3184 0.3844 0.2835 0.0243  -0.0401 -0.0205 1020 SER H OG  
2889 N N   . ILE B 155 ? 0.2792 0.3149 0.2377 0.0268  -0.0413 -0.0201 1021 ILE H N   
2890 C CA  . ILE B 155 ? 0.2879 0.3174 0.2432 0.0289  -0.0417 -0.0202 1021 ILE H CA  
2891 C C   . ILE B 155 ? 0.2852 0.3199 0.2436 0.0259  -0.0416 -0.0195 1021 ILE H C   
2892 O O   . ILE B 155 ? 0.2708 0.3055 0.2322 0.0213  -0.0407 -0.0180 1021 ILE H O   
2893 C CB  . ILE B 155 ? 0.2906 0.3076 0.2434 0.0277  -0.0408 -0.0193 1021 ILE H CB  
2894 C CG1 . ILE B 155 ? 0.2975 0.3086 0.2468 0.0301  -0.0409 -0.0205 1021 ILE H CG1 
2895 C CG2 . ILE B 155 ? 0.2841 0.2949 0.2335 0.0291  -0.0407 -0.0188 1021 ILE H CG2 
2896 C CD1 . ILE B 155 ? 0.3143 0.3143 0.2619 0.0275  -0.0395 -0.0200 1021 ILE H CD1 
2897 N N   . THR B 156 ? 0.2949 0.3350 0.2522 0.0290  -0.0426 -0.0211 1022 THR H N   
2898 C CA  . THR B 156 ? 0.3167 0.3643 0.2774 0.0261  -0.0428 -0.0214 1022 THR H CA  
2899 C C   . THR B 156 ? 0.3113 0.3524 0.2695 0.0275  -0.0432 -0.0212 1022 THR H C   
2900 O O   . THR B 156 ? 0.3166 0.3506 0.2693 0.0326  -0.0437 -0.0216 1022 THR H O   
2901 C CB  . THR B 156 ? 0.3338 0.3958 0.2965 0.0279  -0.0437 -0.0240 1022 THR H CB  
2902 O OG1 . THR B 156 ? 0.3702 0.4322 0.3282 0.0352  -0.0453 -0.0263 1022 THR H OG1 
2903 C CG2 . THR B 156 ? 0.3467 0.4149 0.3112 0.0267  -0.0430 -0.0241 1022 THR H CG2 
2904 N N   . CYS B 157 ? 0.3215 0.3649 0.2828 0.0234  -0.0430 -0.0207 1023 CYS H N   
2905 C CA  . CYS B 157 ? 0.3359 0.3746 0.2954 0.0242  -0.0435 -0.0207 1023 CYS H CA  
2906 C C   . CYS B 157 ? 0.3271 0.3757 0.2905 0.0213  -0.0442 -0.0224 1023 CYS H C   
2907 O O   . CYS B 157 ? 0.3111 0.3636 0.2783 0.0157  -0.0434 -0.0218 1023 CYS H O   
2908 C CB  . CYS B 157 ? 0.3854 0.4135 0.3444 0.0213  -0.0424 -0.0181 1023 CYS H CB  
2909 S SG  . CYS B 157 ? 0.4828 0.5052 0.4389 0.0232  -0.0428 -0.0180 1023 CYS H SG  
2910 N N   . LYS B 158 ? 0.3088 0.3619 0.2710 0.0251  -0.0457 -0.0247 1024 LYS H N   
2911 C CA  . LYS B 158 ? 0.3273 0.3899 0.2933 0.0221  -0.0465 -0.0269 1024 LYS H CA  
2912 C C   . LYS B 158 ? 0.3128 0.3684 0.2769 0.0226  -0.0471 -0.0265 1024 LYS H C   
2913 O O   . LYS B 158 ? 0.3411 0.3910 0.3002 0.0285  -0.0477 -0.0264 1024 LYS H O   
2914 C CB  . LYS B 158 ? 0.3660 0.4425 0.3326 0.0266  -0.0481 -0.0310 1024 LYS H CB  
2915 C CG  . LYS B 158 ? 0.4123 0.5013 0.3839 0.0225  -0.0488 -0.0342 1024 LYS H CG  
2916 C CD  . LYS B 158 ? 0.4772 0.5839 0.4527 0.0222  -0.0490 -0.0379 1024 LYS H CD  
2917 C CE  . LYS B 158 ? 0.5061 0.6249 0.4871 0.0161  -0.0492 -0.0412 1024 LYS H CE  
2918 N NZ  . LYS B 158 ? 0.5126 0.6294 0.4970 0.0059  -0.0469 -0.0390 1024 LYS H NZ  
2919 N N   . ALA B 159 ? 0.3118 0.3679 0.2789 0.0169  -0.0470 -0.0265 1025 ALA H N   
2920 C CA  . ALA B 159 ? 0.2895 0.3409 0.2554 0.0171  -0.0479 -0.0268 1025 ALA H CA  
2921 C C   . ALA B 159 ? 0.3064 0.3696 0.2744 0.0181  -0.0497 -0.0310 1025 ALA H C   
2922 O O   . ALA B 159 ? 0.2917 0.3665 0.2642 0.0141  -0.0497 -0.0334 1025 ALA H O   
2923 C CB  . ALA B 159 ? 0.2934 0.3381 0.2607 0.0108  -0.0471 -0.0248 1025 ALA H CB  
2924 N N   . SER B 160 ? 0.3099 0.3709 0.2749 0.0228  -0.0511 -0.0321 1026 SER H N   
2925 C CA  . SER B 160 ? 0.3228 0.3952 0.2893 0.0250  -0.0533 -0.0368 1026 SER H CA  
2926 C C   . SER B 160 ? 0.3361 0.4118 0.3073 0.0172  -0.0536 -0.0385 1026 SER H C   
2927 O O   . SER B 160 ? 0.3333 0.4213 0.3077 0.0166  -0.0552 -0.0431 1026 SER H O   
2928 C CB  . SER B 160 ? 0.3163 0.3841 0.2770 0.0330  -0.0546 -0.0372 1026 SER H CB  
2929 O OG  . SER B 160 ? 0.2929 0.3491 0.2514 0.0316  -0.0540 -0.0346 1026 SER H OG  
2930 N N   . GLN B 161 ? 0.3400 0.4049 0.3110 0.0119  -0.0523 -0.0353 1027 GLN H N   
2931 C CA  . GLN B 161 ? 0.3471 0.4122 0.3209 0.0040  -0.0525 -0.0365 1027 GLN H CA  
2932 C C   . GLN B 161 ? 0.3402 0.3960 0.3135 -0.0016 -0.0505 -0.0327 1027 GLN H C   
2933 O O   . GLN B 161 ? 0.3312 0.3806 0.3024 0.0010  -0.0493 -0.0294 1027 GLN H O   
2934 C CB  . GLN B 161 ? 0.3821 0.4419 0.3541 0.0051  -0.0542 -0.0377 1027 GLN H CB  
2935 C CG  . GLN B 161 ? 0.4107 0.4600 0.3776 0.0115  -0.0542 -0.0348 1027 GLN H CG  
2936 C CD  . GLN B 161 ? 0.4134 0.4613 0.3786 0.0142  -0.0562 -0.0369 1027 GLN H CD  
2937 O OE1 . GLN B 161 ? 0.4461 0.4897 0.4115 0.0100  -0.0569 -0.0375 1027 GLN H OE1 
2938 N NE2 . GLN B 161 ? 0.4124 0.4621 0.3743 0.0219  -0.0571 -0.0377 1027 GLN H NE2 
2939 N N   . ASP B 162 ? 0.3353 0.3906 0.3101 -0.0093 -0.0502 -0.0335 1028 ASP H N   
2940 C CA  . ASP B 162 ? 0.3214 0.3671 0.2943 -0.0149 -0.0484 -0.0302 1028 ASP H CA  
2941 C C   . ASP B 162 ? 0.3114 0.3432 0.2799 -0.0113 -0.0486 -0.0268 1028 ASP H C   
2942 O O   . ASP B 162 ? 0.2905 0.3167 0.2570 -0.0108 -0.0501 -0.0276 1028 ASP H O   
2943 C CB  . ASP B 162 ? 0.3445 0.3901 0.3179 -0.0236 -0.0482 -0.0320 1028 ASP H CB  
2944 C CG  . ASP B 162 ? 0.3658 0.4011 0.3358 -0.0295 -0.0462 -0.0285 1028 ASP H CG  
2945 O OD1 . ASP B 162 ? 0.3337 0.3617 0.3011 -0.0264 -0.0453 -0.0248 1028 ASP H OD1 
2946 O OD2 . ASP B 162 ? 0.3892 0.4228 0.3584 -0.0373 -0.0456 -0.0297 1028 ASP H OD2 
2947 N N   . VAL B 163 ? 0.2870 0.3140 0.2540 -0.0092 -0.0473 -0.0235 1029 VAL H N   
2948 C CA  . VAL B 163 ? 0.2724 0.2880 0.2357 -0.0063 -0.0474 -0.0209 1029 VAL H CA  
2949 C C   . VAL B 163 ? 0.2700 0.2776 0.2307 -0.0102 -0.0463 -0.0184 1029 VAL H C   
2950 O O   . VAL B 163 ? 0.2730 0.2731 0.2310 -0.0075 -0.0461 -0.0162 1029 VAL H O   
2951 C CB  . VAL B 163 ? 0.2775 0.2935 0.2406 -0.0003 -0.0468 -0.0196 1029 VAL H CB  
2952 C CG1 . VAL B 163 ? 0.2826 0.3027 0.2457 0.0044  -0.0479 -0.0216 1029 VAL H CG1 
2953 C CG2 . VAL B 163 ? 0.2667 0.2876 0.2316 -0.0004 -0.0454 -0.0188 1029 VAL H CG2 
2954 N N   . GLY B 164 ? 0.2581 0.2673 0.2190 -0.0163 -0.0455 -0.0187 1030 GLY H N   
2955 C CA  . GLY B 164 ? 0.2595 0.2595 0.2161 -0.0200 -0.0444 -0.0161 1030 GLY H CA  
2956 C C   . GLY B 164 ? 0.2528 0.2535 0.2096 -0.0171 -0.0431 -0.0138 1030 GLY H C   
2957 O O   . GLY B 164 ? 0.2497 0.2602 0.2104 -0.0168 -0.0422 -0.0143 1030 GLY H O   
2958 N N   . THR B 165 ? 0.2448 0.2362 0.1975 -0.0148 -0.0432 -0.0116 1031 THR H N   
2959 C CA  . THR B 165 ? 0.2465 0.2385 0.1995 -0.0115 -0.0424 -0.0100 1031 THR H CA  
2960 C C   . THR B 165 ? 0.2496 0.2390 0.2026 -0.0060 -0.0432 -0.0100 1031 THR H C   
2961 O O   . THR B 165 ? 0.2528 0.2418 0.2056 -0.0036 -0.0427 -0.0091 1031 THR H O   
2962 C CB  . THR B 165 ? 0.2510 0.2363 0.1990 -0.0138 -0.0414 -0.0078 1031 THR H CB  
2963 O OG1 . THR B 165 ? 0.2517 0.2258 0.1938 -0.0136 -0.0427 -0.0072 1031 THR H OG1 
2964 C CG2 . THR B 165 ? 0.2531 0.2425 0.2014 -0.0198 -0.0398 -0.0075 1031 THR H CG2 
2965 N N   . ALA B 166 ? 0.2526 0.2424 0.2065 -0.0041 -0.0443 -0.0114 1032 ALA H N   
2966 C CA  . ALA B 166 ? 0.2490 0.2370 0.2027 0.0004  -0.0446 -0.0115 1032 ALA H CA  
2967 C C   . ALA B 166 ? 0.2456 0.2397 0.2026 0.0028  -0.0436 -0.0118 1032 ALA H C   
2968 O O   . ALA B 166 ? 0.2465 0.2421 0.2040 0.0050  -0.0439 -0.0127 1032 ALA H O   
2969 C CB  . ALA B 166 ? 0.2520 0.2364 0.2039 0.0014  -0.0462 -0.0127 1032 ALA H CB  
2970 N N   . VAL B 167 ? 0.2348 0.2311 0.1930 0.0027  -0.0425 -0.0111 1033 VAL H N   
2971 C CA  . VAL B 167 ? 0.2301 0.2304 0.1902 0.0049  -0.0416 -0.0114 1033 VAL H CA  
2972 C C   . VAL B 167 ? 0.2267 0.2251 0.1866 0.0060  -0.0407 -0.0108 1033 VAL H C   
2973 O O   . VAL B 167 ? 0.2267 0.2241 0.1860 0.0048  -0.0408 -0.0101 1033 VAL H O   
2974 C CB  . VAL B 167 ? 0.2293 0.2363 0.1913 0.0038  -0.0414 -0.0120 1033 VAL H CB  
2975 C CG1 . VAL B 167 ? 0.2354 0.2448 0.1979 0.0066  -0.0407 -0.0122 1033 VAL H CG1 
2976 C CG2 . VAL B 167 ? 0.2360 0.2468 0.1986 0.0033  -0.0424 -0.0135 1033 VAL H CG2 
2977 N N   . ALA B 168 ? 0.2169 0.2149 0.1771 0.0080  -0.0399 -0.0112 1034 ALA H N   
2978 C CA  . ALA B 168 ? 0.2170 0.2143 0.1777 0.0086  -0.0389 -0.0113 1034 ALA H CA  
2979 C C   . ALA B 168 ? 0.2201 0.2186 0.1810 0.0095  -0.0380 -0.0117 1034 ALA H C   
2980 O O   . ALA B 168 ? 0.2239 0.2226 0.1836 0.0109  -0.0381 -0.0119 1034 ALA H O   
2981 C CB  . ALA B 168 ? 0.2218 0.2167 0.1818 0.0093  -0.0384 -0.0117 1034 ALA H CB  
2982 N N   . TRP B 169 ? 0.2151 0.2141 0.1769 0.0093  -0.0373 -0.0122 1035 TRP H N   
2983 C CA  . TRP B 169 ? 0.2328 0.2311 0.1939 0.0102  -0.0365 -0.0129 1035 TRP H CA  
2984 C C   . TRP B 169 ? 0.2322 0.2279 0.1934 0.0093  -0.0351 -0.0138 1035 TRP H C   
2985 O O   . TRP B 169 ? 0.2335 0.2314 0.1967 0.0084  -0.0352 -0.0145 1035 TRP H O   
2986 C CB  . TRP B 169 ? 0.2296 0.2318 0.1918 0.0105  -0.0370 -0.0132 1035 TRP H CB  
2987 C CG  . TRP B 169 ? 0.2336 0.2398 0.1959 0.0109  -0.0379 -0.0128 1035 TRP H CG  
2988 C CD1 . TRP B 169 ? 0.2469 0.2564 0.2103 0.0091  -0.0385 -0.0120 1035 TRP H CD1 
2989 C CD2 . TRP B 169 ? 0.2380 0.2462 0.1990 0.0133  -0.0383 -0.0134 1035 TRP H CD2 
2990 N NE1 . TRP B 169 ? 0.2377 0.2523 0.2015 0.0093  -0.0389 -0.0124 1035 TRP H NE1 
2991 C CE2 . TRP B 169 ? 0.2373 0.2519 0.1998 0.0124  -0.0390 -0.0134 1035 TRP H CE2 
2992 C CE3 . TRP B 169 ? 0.2461 0.2506 0.2039 0.0162  -0.0380 -0.0142 1035 TRP H CE3 
2993 C CZ2 . TRP B 169 ? 0.2373 0.2571 0.1993 0.0146  -0.0397 -0.0146 1035 TRP H CZ2 
2994 C CZ3 . TRP B 169 ? 0.2546 0.2625 0.2107 0.0193  -0.0390 -0.0151 1035 TRP H CZ3 
2995 C CH2 . TRP B 169 ? 0.2491 0.2657 0.2079 0.0187  -0.0399 -0.0155 1035 TRP H CH2 
2996 N N   . TYR B 170 ? 0.2472 0.2383 0.2057 0.0097  -0.0338 -0.0140 1036 TYR H N   
2997 C CA  . TYR B 170 ? 0.2562 0.2440 0.2140 0.0077  -0.0318 -0.0151 1036 TYR H CA  
2998 C C   . TYR B 170 ? 0.2657 0.2497 0.2211 0.0081  -0.0313 -0.0160 1036 TYR H C   
2999 O O   . TYR B 170 ? 0.2593 0.2409 0.2115 0.0108  -0.0321 -0.0154 1036 TYR H O   
3000 C CB  . TYR B 170 ? 0.2599 0.2433 0.2148 0.0073  -0.0303 -0.0143 1036 TYR H CB  
3001 C CG  . TYR B 170 ? 0.2541 0.2411 0.2112 0.0070  -0.0307 -0.0140 1036 TYR H CG  
3002 C CD1 . TYR B 170 ? 0.2495 0.2398 0.2092 0.0049  -0.0298 -0.0154 1036 TYR H CD1 
3003 C CD2 . TYR B 170 ? 0.2637 0.2512 0.2200 0.0089  -0.0322 -0.0129 1036 TYR H CD2 
3004 C CE1 . TYR B 170 ? 0.2511 0.2444 0.2118 0.0055  -0.0304 -0.0154 1036 TYR H CE1 
3005 C CE2 . TYR B 170 ? 0.2636 0.2532 0.2211 0.0090  -0.0329 -0.0128 1036 TYR H CE2 
3006 C CZ  . TYR B 170 ? 0.2653 0.2575 0.2246 0.0077  -0.0320 -0.0140 1036 TYR H CZ  
3007 O OH  . TYR B 170 ? 0.2855 0.2800 0.2453 0.0086  -0.0329 -0.0144 1036 TYR H OH  
3008 N N   . GLN B 171 ? 0.2606 0.2444 0.2174 0.0055  -0.0301 -0.0178 1037 GLN H N   
3009 C CA  . GLN B 171 ? 0.2777 0.2554 0.2312 0.0048  -0.0291 -0.0191 1037 GLN H CA  
3010 C C   . GLN B 171 ? 0.2922 0.2625 0.2420 0.0017  -0.0263 -0.0191 1037 GLN H C   
3011 O O   . GLN B 171 ? 0.2836 0.2581 0.2367 -0.0013 -0.0249 -0.0197 1037 GLN H O   
3012 C CB  . GLN B 171 ? 0.2870 0.2698 0.2446 0.0031  -0.0296 -0.0216 1037 GLN H CB  
3013 C CG  . GLN B 171 ? 0.3067 0.2838 0.2613 0.0026  -0.0291 -0.0235 1037 GLN H CG  
3014 C CD  . GLN B 171 ? 0.3157 0.2993 0.2750 0.0011  -0.0298 -0.0265 1037 GLN H CD  
3015 O OE1 . GLN B 171 ? 0.3240 0.3105 0.2840 0.0036  -0.0315 -0.0273 1037 GLN H OE1 
3016 N NE2 . GLN B 171 ? 0.3052 0.2928 0.2681 -0.0025 -0.0285 -0.0284 1037 GLN H NE2 
3017 N N   . GLN B 172 ? 0.3133 0.2735 0.2562 0.0023  -0.0252 -0.0187 1038 GLN H N   
3018 C CA  . GLN B 172 ? 0.3472 0.2985 0.2854 -0.0017 -0.0218 -0.0188 1038 GLN H CA  
3019 C C   . GLN B 172 ? 0.3582 0.2995 0.2906 -0.0029 -0.0209 -0.0202 1038 GLN H C   
3020 O O   . GLN B 172 ? 0.3533 0.2890 0.2805 0.0016  -0.0225 -0.0196 1038 GLN H O   
3021 C CB  . GLN B 172 ? 0.3731 0.3177 0.3051 -0.0001 -0.0205 -0.0161 1038 GLN H CB  
3022 C CG  . GLN B 172 ? 0.3946 0.3348 0.3246 -0.0058 -0.0166 -0.0162 1038 GLN H CG  
3023 C CD  . GLN B 172 ? 0.4314 0.3640 0.3542 -0.0044 -0.0148 -0.0135 1038 GLN H CD  
3024 O OE1 . GLN B 172 ? 0.4926 0.4219 0.4131 -0.0088 -0.0114 -0.0131 1038 GLN H OE1 
3025 N NE2 . GLN B 172 ? 0.4329 0.3639 0.3524 0.0018  -0.0172 -0.0117 1038 GLN H NE2 
3026 N N   . LYS B 173 ? 0.3770 0.3175 0.3111 -0.0089 -0.0186 -0.0225 1039 LYS H N   
3027 C CA  . LYS B 173 ? 0.4050 0.3335 0.3325 -0.0120 -0.0168 -0.0241 1039 LYS H CA  
3028 C C   . LYS B 173 ? 0.4369 0.3529 0.3562 -0.0160 -0.0127 -0.0225 1039 LYS H C   
3029 O O   . LYS B 173 ? 0.4189 0.3389 0.3403 -0.0186 -0.0107 -0.0213 1039 LYS H O   
3030 C CB  . LYS B 173 ? 0.4015 0.3381 0.3364 -0.0165 -0.0169 -0.0282 1039 LYS H CB  
3031 C CG  . LYS B 173 ? 0.4019 0.3485 0.3426 -0.0118 -0.0207 -0.0294 1039 LYS H CG  
3032 C CD  . LYS B 173 ? 0.4007 0.3532 0.3465 -0.0150 -0.0211 -0.0336 1039 LYS H CD  
3033 C CE  . LYS B 173 ? 0.4066 0.3697 0.3579 -0.0101 -0.0247 -0.0343 1039 LYS H CE  
3034 N NZ  . LYS B 173 ? 0.4146 0.3838 0.3705 -0.0124 -0.0254 -0.0387 1039 LYS H NZ  
3035 N N   . PRO B 174 ? 0.4947 0.3945 0.4037 -0.0169 -0.0113 -0.0224 1040 PRO H N   
3036 C CA  . PRO B 174 ? 0.5254 0.4105 0.4242 -0.0207 -0.0071 -0.0205 1040 PRO H CA  
3037 C C   . PRO B 174 ? 0.5124 0.4036 0.4168 -0.0301 -0.0031 -0.0222 1040 PRO H C   
3038 O O   . PRO B 174 ? 0.4919 0.3924 0.4045 -0.0347 -0.0032 -0.0261 1040 PRO H O   
3039 C CB  . PRO B 174 ? 0.5743 0.4414 0.4617 -0.0200 -0.0069 -0.0212 1040 PRO H CB  
3040 C CG  . PRO B 174 ? 0.5674 0.4403 0.4575 -0.0119 -0.0120 -0.0220 1040 PRO H CG  
3041 C CD  . PRO B 174 ? 0.5467 0.4405 0.4520 -0.0137 -0.0137 -0.0242 1040 PRO H CD  
3042 N N   . GLY B 175 ? 0.5272 0.4156 0.4280 -0.0319 0.0000  -0.0196 1041 GLY H N   
3043 C CA  . GLY B 175 ? 0.5474 0.4428 0.4528 -0.0403 0.0042  -0.0209 1041 GLY H CA  
3044 C C   . GLY B 175 ? 0.5424 0.4601 0.4625 -0.0409 0.0023  -0.0237 1041 GLY H C   
3045 O O   . GLY B 175 ? 0.5576 0.4840 0.4831 -0.0480 0.0054  -0.0262 1041 GLY H O   
3046 N N   . GLN B 176 ? 0.4972 0.4242 0.4235 -0.0339 -0.0024 -0.0237 1042 GLN H N   
3047 C CA  . GLN B 176 ? 0.4808 0.4270 0.4191 -0.0333 -0.0045 -0.0260 1042 GLN H CA  
3048 C C   . GLN B 176 ? 0.4347 0.3856 0.3740 -0.0270 -0.0066 -0.0229 1042 GLN H C   
3049 O O   . GLN B 176 ? 0.4484 0.3899 0.3807 -0.0223 -0.0075 -0.0195 1042 GLN H O   
3050 C CB  . GLN B 176 ? 0.4942 0.4471 0.4384 -0.0310 -0.0081 -0.0288 1042 GLN H CB  
3051 C CG  . GLN B 176 ? 0.5357 0.4871 0.4808 -0.0374 -0.0065 -0.0330 1042 GLN H CG  
3052 C CD  . GLN B 176 ? 0.5590 0.5212 0.5117 -0.0348 -0.0101 -0.0363 1042 GLN H CD  
3053 O OE1 . GLN B 176 ? 0.6283 0.5907 0.5825 -0.0387 -0.0098 -0.0401 1042 GLN H OE1 
3054 N NE2 . GLN B 176 ? 0.5581 0.5286 0.5149 -0.0283 -0.0137 -0.0348 1042 GLN H NE2 
3055 N N   . SER B 177 ? 0.4062 0.3714 0.3536 -0.0267 -0.0077 -0.0243 1043 SER H N   
3056 C CA  . SER B 177 ? 0.3799 0.3497 0.3285 -0.0212 -0.0099 -0.0219 1043 SER H CA  
3057 C C   . SER B 177 ? 0.3548 0.3273 0.3060 -0.0154 -0.0144 -0.0214 1043 SER H C   
3058 O O   . SER B 177 ? 0.3549 0.3304 0.3094 -0.0156 -0.0159 -0.0235 1043 SER H O   
3059 C CB  . SER B 177 ? 0.4020 0.3845 0.3567 -0.0228 -0.0092 -0.0238 1043 SER H CB  
3060 O OG  . SER B 177 ? 0.4176 0.4116 0.3800 -0.0228 -0.0114 -0.0273 1043 SER H OG  
3061 N N   . PRO B 178 ? 0.3326 0.3034 0.2817 -0.0102 -0.0165 -0.0186 1044 PRO H N   
3062 C CA  . PRO B 178 ? 0.3252 0.3000 0.2771 -0.0057 -0.0203 -0.0182 1044 PRO H CA  
3063 C C   . PRO B 178 ? 0.3238 0.3099 0.2830 -0.0059 -0.0220 -0.0206 1044 PRO H C   
3064 O O   . PRO B 178 ? 0.3127 0.3051 0.2749 -0.0076 -0.0211 -0.0220 1044 PRO H O   
3065 C CB  . PRO B 178 ? 0.3134 0.2874 0.2632 -0.0017 -0.0216 -0.0157 1044 PRO H CB  
3066 C CG  . PRO B 178 ? 0.3345 0.2992 0.2771 -0.0027 -0.0187 -0.0140 1044 PRO H CG  
3067 C CD  . PRO B 178 ? 0.3340 0.2997 0.2779 -0.0086 -0.0153 -0.0159 1044 PRO H CD  
3068 N N   . LYS B 179 ? 0.2922 0.2808 0.2536 -0.0039 -0.0244 -0.0212 1045 LYS H N   
3069 C CA  . LYS B 179 ? 0.3140 0.3120 0.2807 -0.0030 -0.0264 -0.0231 1045 LYS H CA  
3070 C C   . LYS B 179 ? 0.2775 0.2764 0.2441 0.0009  -0.0292 -0.0210 1045 LYS H C   
3071 O O   . LYS B 179 ? 0.2595 0.2551 0.2242 0.0024  -0.0301 -0.0198 1045 LYS H O   
3072 C CB  . LYS B 179 ? 0.3609 0.3609 0.3297 -0.0048 -0.0263 -0.0259 1045 LYS H CB  
3073 C CG  . LYS B 179 ? 0.4548 0.4564 0.4250 -0.0099 -0.0234 -0.0288 1045 LYS H CG  
3074 C CD  . LYS B 179 ? 0.5237 0.5243 0.4945 -0.0135 -0.0223 -0.0319 1045 LYS H CD  
3075 C CE  . LYS B 179 ? 0.5907 0.5936 0.5629 -0.0196 -0.0189 -0.0347 1045 LYS H CE  
3076 N NZ  . LYS B 179 ? 0.6030 0.6011 0.5716 -0.0210 -0.0164 -0.0321 1045 LYS H NZ  
3077 N N   . LEU B 180 ? 0.2606 0.2643 0.2289 0.0025  -0.0305 -0.0210 1046 LEU H N   
3078 C CA  . LEU B 180 ? 0.2492 0.2526 0.2166 0.0053  -0.0329 -0.0190 1046 LEU H CA  
3079 C C   . LEU B 180 ? 0.2355 0.2413 0.2040 0.0062  -0.0341 -0.0196 1046 LEU H C   
3080 O O   . LEU B 180 ? 0.2283 0.2389 0.1990 0.0062  -0.0344 -0.0219 1046 LEU H O   
3081 C CB  . LEU B 180 ? 0.2509 0.2569 0.2184 0.0069  -0.0340 -0.0191 1046 LEU H CB  
3082 C CG  . LEU B 180 ? 0.2475 0.2514 0.2130 0.0089  -0.0362 -0.0172 1046 LEU H CG  
3083 C CD1 . LEU B 180 ? 0.2494 0.2492 0.2132 0.0087  -0.0362 -0.0151 1046 LEU H CD1 
3084 C CD2 . LEU B 180 ? 0.2496 0.2546 0.2140 0.0108  -0.0374 -0.0177 1046 LEU H CD2 
3085 N N   . LEU B 181 ? 0.2255 0.2293 0.1926 0.0072  -0.0350 -0.0178 1047 LEU H N   
3086 C CA  . LEU B 181 ? 0.2391 0.2458 0.2068 0.0082  -0.0361 -0.0180 1047 LEU H CA  
3087 C C   . LEU B 181 ? 0.2295 0.2365 0.1957 0.0094  -0.0375 -0.0162 1047 LEU H C   
3088 O O   . LEU B 181 ? 0.2461 0.2553 0.2119 0.0106  -0.0384 -0.0167 1047 LEU H O   
3089 C CB  . LEU B 181 ? 0.2434 0.2485 0.2101 0.0085  -0.0359 -0.0173 1047 LEU H CB  
3090 C CG  . LEU B 181 ? 0.2722 0.2758 0.2388 0.0081  -0.0351 -0.0191 1047 LEU H CG  
3091 C CD1 . LEU B 181 ? 0.2707 0.2754 0.2392 0.0062  -0.0341 -0.0218 1047 LEU H CD1 
3092 C CD2 . LEU B 181 ? 0.2730 0.2718 0.2365 0.0089  -0.0346 -0.0182 1047 LEU H CD2 
3093 N N   . ILE B 182 ? 0.2349 0.2394 0.1997 0.0090  -0.0378 -0.0144 1048 ILE H N   
3094 C CA  . ILE B 182 ? 0.2276 0.2310 0.1904 0.0088  -0.0387 -0.0126 1048 ILE H CA  
3095 C C   . ILE B 182 ? 0.2245 0.2246 0.1860 0.0085  -0.0391 -0.0119 1048 ILE H C   
3096 O O   . ILE B 182 ? 0.2141 0.2137 0.1763 0.0083  -0.0385 -0.0121 1048 ILE H O   
3097 C CB  . ILE B 182 ? 0.2365 0.2419 0.1995 0.0081  -0.0385 -0.0117 1048 ILE H CB  
3098 C CG1 . ILE B 182 ? 0.2367 0.2456 0.2007 0.0089  -0.0383 -0.0125 1048 ILE H CG1 
3099 C CG2 . ILE B 182 ? 0.2476 0.2521 0.2088 0.0065  -0.0390 -0.0101 1048 ILE H CG2 
3100 C CD1 . ILE B 182 ? 0.2463 0.2559 0.2087 0.0095  -0.0388 -0.0120 1048 ILE H CD1 
3101 N N   . TYR B 183 ? 0.2243 0.2217 0.1832 0.0087  -0.0401 -0.0111 1049 TYR H N   
3102 C CA  . TYR B 183 ? 0.2283 0.2221 0.1854 0.0082  -0.0409 -0.0106 1049 TYR H CA  
3103 C C   . TYR B 183 ? 0.2472 0.2371 0.2006 0.0067  -0.0416 -0.0091 1049 TYR H C   
3104 O O   . TYR B 183 ? 0.2496 0.2394 0.2014 0.0063  -0.0415 -0.0083 1049 TYR H O   
3105 C CB  . TYR B 183 ? 0.2357 0.2284 0.1921 0.0103  -0.0413 -0.0117 1049 TYR H CB  
3106 C CG  . TYR B 183 ? 0.2371 0.2291 0.1911 0.0125  -0.0422 -0.0124 1049 TYR H CG  
3107 C CD1 . TYR B 183 ? 0.2475 0.2340 0.1965 0.0139  -0.0438 -0.0119 1049 TYR H CD1 
3108 C CD2 . TYR B 183 ? 0.2431 0.2398 0.1992 0.0137  -0.0417 -0.0139 1049 TYR H CD2 
3109 C CE1 . TYR B 183 ? 0.2575 0.2428 0.2028 0.0172  -0.0450 -0.0126 1049 TYR H CE1 
3110 C CE2 . TYR B 183 ? 0.2464 0.2437 0.2001 0.0166  -0.0429 -0.0151 1049 TYR H CE2 
3111 C CZ  . TYR B 183 ? 0.2428 0.2342 0.1907 0.0188  -0.0446 -0.0143 1049 TYR H CZ  
3112 O OH  . TYR B 183 ? 0.2742 0.2657 0.2184 0.0229  -0.0460 -0.0156 1049 TYR H OH  
3113 N N   . TRP B 184 ? 0.2726 0.2593 0.2246 0.0055  -0.0423 -0.0089 1050 TRP H N   
3114 C CA  . TRP B 184 ? 0.2845 0.2674 0.2333 0.0024  -0.0426 -0.0077 1050 TRP H CA  
3115 C C   . TRP B 184 ? 0.2667 0.2544 0.2174 -0.0001 -0.0414 -0.0070 1050 TRP H C   
3116 O O   . TRP B 184 ? 0.2690 0.2539 0.2163 -0.0024 -0.0410 -0.0057 1050 TRP H O   
3117 C CB  . TRP B 184 ? 0.3238 0.2986 0.2661 0.0034  -0.0436 -0.0069 1050 TRP H CB  
3118 C CG  . TRP B 184 ? 0.3441 0.3142 0.2838 0.0060  -0.0452 -0.0078 1050 TRP H CG  
3119 C CD1 . TRP B 184 ? 0.3802 0.3490 0.3177 0.0104  -0.0462 -0.0088 1050 TRP H CD1 
3120 C CD2 . TRP B 184 ? 0.3369 0.3033 0.2753 0.0046  -0.0461 -0.0083 1050 TRP H CD2 
3121 N NE1 . TRP B 184 ? 0.3960 0.3613 0.3315 0.0120  -0.0475 -0.0097 1050 TRP H NE1 
3122 C CE2 . TRP B 184 ? 0.3406 0.3037 0.2763 0.0086  -0.0476 -0.0094 1050 TRP H CE2 
3123 C CE3 . TRP B 184 ? 0.3136 0.2806 0.2533 0.0005  -0.0459 -0.0084 1050 TRP H CE3 
3124 C CZ2 . TRP B 184 ? 0.3422 0.3012 0.2759 0.0087  -0.0490 -0.0103 1050 TRP H CZ2 
3125 C CZ3 . TRP B 184 ? 0.3386 0.3020 0.2767 0.0003  -0.0473 -0.0095 1050 TRP H CZ3 
3126 C CH2 . TRP B 184 ? 0.3281 0.2872 0.2631 0.0045  -0.0488 -0.0103 1050 TRP H CH2 
3127 N N   . ALA B 185 ? 0.2488 0.2434 0.2040 0.0004  -0.0408 -0.0079 1051 ALA H N   
3128 C CA  . ALA B 185 ? 0.2422 0.2435 0.1999 -0.0011 -0.0398 -0.0080 1051 ALA H CA  
3129 C C   . ALA B 185 ? 0.2436 0.2466 0.2010 -0.0001 -0.0391 -0.0073 1051 ALA H C   
3130 O O   . ALA B 185 ? 0.2454 0.2544 0.2054 0.0005  -0.0386 -0.0080 1051 ALA H O   
3131 C CB  . ALA B 185 ? 0.2481 0.2506 0.2051 -0.0053 -0.0396 -0.0077 1051 ALA H CB  
3132 N N   . SER B 186 ? 0.2613 0.2591 0.2148 0.0001  -0.0393 -0.0062 1052 SER H N   
3133 C CA  . SER B 186 ? 0.2566 0.2561 0.2088 0.0009  -0.0386 -0.0055 1052 SER H CA  
3134 C C   . SER B 186 ? 0.2650 0.2610 0.2147 0.0044  -0.0394 -0.0058 1052 SER H C   
3135 O O   . SER B 186 ? 0.2596 0.2574 0.2081 0.0058  -0.0391 -0.0055 1052 SER H O   
3136 C CB  . SER B 186 ? 0.2651 0.2629 0.2136 -0.0026 -0.0376 -0.0036 1052 SER H CB  
3137 O OG  . SER B 186 ? 0.2850 0.2734 0.2277 -0.0037 -0.0381 -0.0024 1052 SER H OG  
3138 N N   . THR B 187 ? 0.2615 0.2542 0.2109 0.0063  -0.0404 -0.0068 1053 THR H N   
3139 C CA  . THR B 187 ? 0.2750 0.2661 0.2221 0.0101  -0.0414 -0.0078 1053 THR H CA  
3140 C C   . THR B 187 ? 0.2651 0.2626 0.2175 0.0118  -0.0412 -0.0102 1053 THR H C   
3141 O O   . THR B 187 ? 0.2373 0.2362 0.1930 0.0111  -0.0408 -0.0112 1053 THR H O   
3142 C CB  . THR B 187 ? 0.2985 0.2831 0.2414 0.0115  -0.0427 -0.0078 1053 THR H CB  
3143 O OG1 . THR B 187 ? 0.3242 0.3014 0.2610 0.0095  -0.0427 -0.0055 1053 THR H OG1 
3144 C CG2 . THR B 187 ? 0.3113 0.2963 0.2521 0.0162  -0.0439 -0.0095 1053 THR H CG2 
3145 N N   . ARG B 188 ? 0.2481 0.2490 0.2008 0.0138  -0.0413 -0.0113 1054 ARG H N   
3146 C CA  A ARG B 188 ? 0.2400 0.2466 0.1974 0.0147  -0.0410 -0.0141 1054 ARG H CA  
3147 C CA  B ARG B 188 ? 0.2571 0.2637 0.2146 0.0146  -0.0410 -0.0141 1054 ARG H CA  
3148 C C   . ARG B 188 ? 0.2517 0.2593 0.2094 0.0166  -0.0417 -0.0163 1054 ARG H C   
3149 O O   . ARG B 188 ? 0.2318 0.2378 0.1855 0.0196  -0.0430 -0.0164 1054 ARG H O   
3150 C CB  A ARG B 188 ? 0.2286 0.2393 0.1863 0.0162  -0.0411 -0.0150 1054 ARG H CB  
3151 C CB  B ARG B 188 ? 0.2677 0.2784 0.2256 0.0160  -0.0410 -0.0150 1054 ARG H CB  
3152 C CG  A ARG B 188 ? 0.2139 0.2295 0.1765 0.0156  -0.0405 -0.0176 1054 ARG H CG  
3153 C CG  B ARG B 188 ? 0.2784 0.2944 0.2407 0.0164  -0.0408 -0.0184 1054 ARG H CG  
3154 C CD  A ARG B 188 ? 0.2082 0.2283 0.1712 0.0175  -0.0409 -0.0193 1054 ARG H CD  
3155 C CD  B ARG B 188 ? 0.2925 0.3124 0.2556 0.0174  -0.0409 -0.0194 1054 ARG H CD  
3156 N NE  A ARG B 188 ? 0.1982 0.2179 0.1568 0.0205  -0.0419 -0.0186 1054 ARG H NE  
3157 N NE  B ARG B 188 ? 0.3102 0.3287 0.2710 0.0168  -0.0405 -0.0166 1054 ARG H NE  
3158 C CZ  A ARG B 188 ? 0.1989 0.2212 0.1565 0.0237  -0.0431 -0.0209 1054 ARG H CZ  
3159 C CZ  B ARG B 188 ? 0.2872 0.3052 0.2439 0.0184  -0.0408 -0.0151 1054 ARG H CZ  
3160 N NH1 A ARG B 188 ? 0.1913 0.2178 0.1529 0.0236  -0.0433 -0.0243 1054 ARG H NH1 
3161 N NH1 B ARG B 188 ? 0.2645 0.2822 0.2194 0.0170  -0.0400 -0.0127 1054 ARG H NH1 
3162 N NH2 A ARG B 188 ? 0.2081 0.2286 0.1600 0.0272  -0.0441 -0.0199 1054 ARG H NH2 
3163 N NH2 B ARG B 188 ? 0.3139 0.3316 0.2677 0.0216  -0.0419 -0.0160 1054 ARG H NH2 
3164 N N   . HIS B 189 ? 0.2394 0.2496 0.2012 0.0152  -0.0408 -0.0179 1055 HIS H N   
3165 C CA  . HIS B 189 ? 0.2596 0.2732 0.2229 0.0164  -0.0409 -0.0206 1055 HIS H CA  
3166 C C   . HIS B 189 ? 0.2556 0.2761 0.2206 0.0184  -0.0415 -0.0239 1055 HIS H C   
3167 O O   . HIS B 189 ? 0.2445 0.2675 0.2113 0.0177  -0.0411 -0.0248 1055 HIS H O   
3168 C CB  . HIS B 189 ? 0.2741 0.2882 0.2407 0.0133  -0.0392 -0.0211 1055 HIS H CB  
3169 C CG  . HIS B 189 ? 0.2761 0.2937 0.2438 0.0139  -0.0389 -0.0233 1055 HIS H CG  
3170 N ND1 . HIS B 189 ? 0.3035 0.3252 0.2747 0.0114  -0.0371 -0.0256 1055 HIS H ND1 
3171 C CD2 . HIS B 189 ? 0.2907 0.3084 0.2559 0.0169  -0.0403 -0.0237 1055 HIS H CD2 
3172 C CE1 . HIS B 189 ? 0.2843 0.3099 0.2557 0.0126  -0.0371 -0.0273 1055 HIS H CE1 
3173 N NE2 . HIS B 189 ? 0.2952 0.3186 0.2631 0.0163  -0.0393 -0.0263 1055 HIS H NE2 
3174 N N   . THR B 190 ? 0.2801 0.3043 0.2444 0.0213  -0.0425 -0.0263 1056 THR H N   
3175 C CA  . THR B 190 ? 0.3014 0.3341 0.2675 0.0239  -0.0434 -0.0304 1056 THR H CA  
3176 C C   . THR B 190 ? 0.2822 0.3204 0.2542 0.0201  -0.0417 -0.0330 1056 THR H C   
3177 O O   . THR B 190 ? 0.2837 0.3219 0.2587 0.0162  -0.0398 -0.0334 1056 THR H O   
3178 C CB  . THR B 190 ? 0.3388 0.3776 0.3053 0.0265  -0.0442 -0.0336 1056 THR H CB  
3179 O OG1 . THR B 190 ? 0.3728 0.4047 0.3327 0.0304  -0.0459 -0.0313 1056 THR H OG1 
3180 C CG2 . THR B 190 ? 0.3452 0.3944 0.3137 0.0296  -0.0453 -0.0385 1056 THR H CG2 
3181 N N   . GLY B 191 ? 0.2961 0.3381 0.2690 0.0212  -0.0424 -0.0349 1057 GLY H N   
3182 C CA  . GLY B 191 ? 0.2935 0.3409 0.2717 0.0177  -0.0410 -0.0384 1057 GLY H CA  
3183 C C   . GLY B 191 ? 0.2860 0.3271 0.2644 0.0144  -0.0397 -0.0360 1057 GLY H C   
3184 O O   . GLY B 191 ? 0.3117 0.3553 0.2930 0.0121  -0.0390 -0.0387 1057 GLY H O   
3185 N N   . VAL B 192 ? 0.2477 0.2812 0.2228 0.0144  -0.0396 -0.0315 1058 VAL H N   
3186 C CA  . VAL B 192 ? 0.2437 0.2723 0.2184 0.0124  -0.0387 -0.0295 1058 VAL H CA  
3187 C C   . VAL B 192 ? 0.2418 0.2726 0.2156 0.0149  -0.0399 -0.0298 1058 VAL H C   
3188 O O   . VAL B 192 ? 0.2400 0.2720 0.2111 0.0181  -0.0413 -0.0289 1058 VAL H O   
3189 C CB  . VAL B 192 ? 0.2433 0.2654 0.2152 0.0121  -0.0385 -0.0253 1058 VAL H CB  
3190 C CG1 . VAL B 192 ? 0.2505 0.2695 0.2216 0.0113  -0.0380 -0.0235 1058 VAL H CG1 
3191 C CG2 . VAL B 192 ? 0.2350 0.2552 0.2076 0.0101  -0.0373 -0.0251 1058 VAL H CG2 
3192 N N   . PRO B 193 ? 0.2523 0.2832 0.2275 0.0137  -0.0395 -0.0312 1059 PRO H N   
3193 C CA  . PRO B 193 ? 0.2502 0.2836 0.2243 0.0163  -0.0406 -0.0316 1059 PRO H CA  
3194 C C   . PRO B 193 ? 0.2445 0.2756 0.2148 0.0182  -0.0410 -0.0274 1059 PRO H C   
3195 O O   . PRO B 193 ? 0.2144 0.2412 0.1835 0.0167  -0.0403 -0.0243 1059 PRO H O   
3196 C CB  . PRO B 193 ? 0.2572 0.2889 0.2325 0.0144  -0.0400 -0.0333 1059 PRO H CB  
3197 C CG  . PRO B 193 ? 0.2623 0.2924 0.2399 0.0106  -0.0385 -0.0356 1059 PRO H CG  
3198 C CD  . PRO B 193 ? 0.2578 0.2857 0.2346 0.0101  -0.0379 -0.0328 1059 PRO H CD  
3199 N N   . ASP B 194 ? 0.2467 0.2811 0.2150 0.0214  -0.0421 -0.0275 1060 ASP H N   
3200 C CA  . ASP B 194 ? 0.2547 0.2870 0.2184 0.0228  -0.0421 -0.0236 1060 ASP H CA  
3201 C C   . ASP B 194 ? 0.2481 0.2790 0.2119 0.0209  -0.0411 -0.0214 1060 ASP H C   
3202 O O   . ASP B 194 ? 0.2631 0.2916 0.2242 0.0200  -0.0405 -0.0180 1060 ASP H O   
3203 C CB  . ASP B 194 ? 0.2584 0.2946 0.2195 0.0267  -0.0431 -0.0245 1060 ASP H CB  
3204 C CG  . ASP B 194 ? 0.2769 0.3150 0.2364 0.0300  -0.0445 -0.0265 1060 ASP H CG  
3205 O OD1 . ASP B 194 ? 0.2465 0.2813 0.2049 0.0295  -0.0445 -0.0256 1060 ASP H OD1 
3206 O OD2 . ASP B 194 ? 0.2596 0.3026 0.2181 0.0337  -0.0456 -0.0290 1060 ASP H OD2 
3207 N N   . ARG B 195 ? 0.2500 0.2824 0.2164 0.0205  -0.0411 -0.0235 1061 ARG H N   
3208 C CA  . ARG B 195 ? 0.2417 0.2742 0.2077 0.0202  -0.0406 -0.0221 1061 ARG H CA  
3209 C C   . ARG B 195 ? 0.2449 0.2737 0.2109 0.0178  -0.0397 -0.0200 1061 ARG H C   
3210 O O   . ARG B 195 ? 0.2296 0.2598 0.1951 0.0180  -0.0395 -0.0190 1061 ARG H O   
3211 C CB  . ARG B 195 ? 0.2384 0.2719 0.2057 0.0213  -0.0411 -0.0254 1061 ARG H CB  
3212 C CG  . ARG B 195 ? 0.2383 0.2672 0.2072 0.0191  -0.0407 -0.0276 1061 ARG H CG  
3213 C CD  . ARG B 195 ? 0.2423 0.2706 0.2114 0.0199  -0.0413 -0.0311 1061 ARG H CD  
3214 N NE  . ARG B 195 ? 0.2447 0.2675 0.2145 0.0170  -0.0404 -0.0334 1061 ARG H NE  
3215 C CZ  . ARG B 195 ? 0.2451 0.2694 0.2174 0.0149  -0.0403 -0.0365 1061 ARG H CZ  
3216 N NH1 . ARG B 195 ? 0.2285 0.2598 0.2028 0.0163  -0.0412 -0.0378 1061 ARG H NH1 
3217 N NH2 . ARG B 195 ? 0.2465 0.2656 0.2190 0.0113  -0.0390 -0.0384 1061 ARG H NH2 
3218 N N   . PHE B 196 ? 0.2291 0.2541 0.1957 0.0161  -0.0395 -0.0197 1062 PHE H N   
3219 C CA  . PHE B 196 ? 0.2431 0.2647 0.2094 0.0143  -0.0388 -0.0178 1062 PHE H CA  
3220 C C   . PHE B 196 ? 0.2345 0.2557 0.1989 0.0134  -0.0387 -0.0150 1062 PHE H C   
3221 O O   . PHE B 196 ? 0.2377 0.2574 0.2005 0.0137  -0.0391 -0.0146 1062 PHE H O   
3222 C CB  . PHE B 196 ? 0.2290 0.2468 0.1964 0.0129  -0.0384 -0.0189 1062 PHE H CB  
3223 C CG  . PHE B 196 ? 0.2274 0.2434 0.1957 0.0126  -0.0380 -0.0213 1062 PHE H CG  
3224 C CD1 . PHE B 196 ? 0.2373 0.2551 0.2071 0.0126  -0.0381 -0.0243 1062 PHE H CD1 
3225 C CD2 . PHE B 196 ? 0.2296 0.2415 0.1963 0.0125  -0.0374 -0.0209 1062 PHE H CD2 
3226 C CE1 . PHE B 196 ? 0.2432 0.2577 0.2129 0.0115  -0.0375 -0.0267 1062 PHE H CE1 
3227 C CE2 . PHE B 196 ? 0.2443 0.2519 0.2099 0.0122  -0.0369 -0.0228 1062 PHE H CE2 
3228 C CZ  . PHE B 196 ? 0.2429 0.2513 0.2099 0.0112  -0.0368 -0.0257 1062 PHE H CZ  
3229 N N   . THR B 197 ? 0.2389 0.2616 0.2028 0.0123  -0.0383 -0.0134 1063 THR H N   
3230 C CA  . THR B 197 ? 0.2435 0.2650 0.2053 0.0101  -0.0379 -0.0109 1063 THR H CA  
3231 C C   . THR B 197 ? 0.2394 0.2607 0.2023 0.0084  -0.0378 -0.0106 1063 THR H C   
3232 O O   . THR B 197 ? 0.2539 0.2770 0.2184 0.0097  -0.0379 -0.0120 1063 THR H O   
3233 C CB  . THR B 197 ? 0.2405 0.2656 0.2002 0.0095  -0.0373 -0.0095 1063 THR H CB  
3234 O OG1 . THR B 197 ? 0.2333 0.2648 0.1950 0.0103  -0.0371 -0.0105 1063 THR H OG1 
3235 C CG2 . THR B 197 ? 0.2566 0.2808 0.2139 0.0118  -0.0376 -0.0096 1063 THR H CG2 
3236 N N   . GLY B 198 ? 0.2483 0.2666 0.2096 0.0060  -0.0376 -0.0090 1064 GLY H N   
3237 C CA  . GLY B 198 ? 0.2409 0.2604 0.2034 0.0042  -0.0376 -0.0090 1064 GLY H CA  
3238 C C   . GLY B 198 ? 0.2383 0.2594 0.1994 0.0006  -0.0369 -0.0077 1064 GLY H C   
3239 O O   . GLY B 198 ? 0.2336 0.2507 0.1913 -0.0009 -0.0364 -0.0060 1064 GLY H O   
3240 N N   . SER B 199 ? 0.2521 0.2784 0.2151 -0.0009 -0.0368 -0.0085 1065 SER H N   
3241 C CA  . SER B 199 ? 0.2687 0.2973 0.2310 -0.0056 -0.0359 -0.0077 1065 SER H CA  
3242 C C   . SER B 199 ? 0.2572 0.2889 0.2218 -0.0067 -0.0365 -0.0094 1065 SER H C   
3243 O O   . SER B 199 ? 0.2619 0.2949 0.2283 -0.0030 -0.0376 -0.0109 1065 SER H O   
3244 C CB  . SER B 199 ? 0.2628 0.3000 0.2258 -0.0069 -0.0346 -0.0077 1065 SER H CB  
3245 O OG  . SER B 199 ? 0.2777 0.3229 0.2440 -0.0033 -0.0353 -0.0100 1065 SER H OG  
3246 N N   . GLY B 200 ? 0.2674 0.2995 0.2313 -0.0118 -0.0359 -0.0091 1066 GLY H N   
3247 C CA  . GLY B 200 ? 0.2717 0.3090 0.2382 -0.0133 -0.0365 -0.0113 1066 GLY H CA  
3248 C C   . GLY B 200 ? 0.2826 0.3114 0.2467 -0.0165 -0.0371 -0.0109 1066 GLY H C   
3249 O O   . GLY B 200 ? 0.2760 0.2941 0.2362 -0.0161 -0.0374 -0.0090 1066 GLY H O   
3250 N N   . SER B 201 ? 0.2821 0.3166 0.2485 -0.0193 -0.0374 -0.0130 1067 SER H N   
3251 C CA  A SER B 201 ? 0.2855 0.3134 0.2502 -0.0221 -0.0383 -0.0136 1067 SER H CA  
3252 C CA  B SER B 201 ? 0.2887 0.3168 0.2532 -0.0228 -0.0382 -0.0135 1067 SER H CA  
3253 C C   . SER B 201 ? 0.2943 0.3328 0.2632 -0.0230 -0.0392 -0.0172 1067 SER H C   
3254 O O   . SER B 201 ? 0.3178 0.3691 0.2904 -0.0230 -0.0386 -0.0190 1067 SER H O   
3255 C CB  A SER B 201 ? 0.2960 0.3162 0.2562 -0.0286 -0.0370 -0.0118 1067 SER H CB  
3256 C CB  B SER B 201 ? 0.3006 0.3230 0.2612 -0.0297 -0.0365 -0.0119 1067 SER H CB  
3257 O OG  A SER B 201 ? 0.2870 0.3167 0.2492 -0.0344 -0.0351 -0.0128 1067 SER H OG  
3258 O OG  B SER B 201 ? 0.3006 0.3147 0.2582 -0.0331 -0.0374 -0.0124 1067 SER H OG  
3259 N N   . GLY B 202 ? 0.2755 0.3098 0.2438 -0.0232 -0.0407 -0.0185 1068 GLY H N   
3260 C CA  . GLY B 202 ? 0.2791 0.3235 0.2511 -0.0237 -0.0418 -0.0224 1068 GLY H CA  
3261 C C   . GLY B 202 ? 0.2644 0.3146 0.2382 -0.0158 -0.0432 -0.0237 1068 GLY H C   
3262 O O   . GLY B 202 ? 0.2580 0.3010 0.2298 -0.0114 -0.0444 -0.0231 1068 GLY H O   
3263 N N   . THR B 203 ? 0.2860 0.3483 0.2627 -0.0138 -0.0429 -0.0255 1069 THR H N   
3264 C CA  . THR B 203 ? 0.2894 0.3565 0.2663 -0.0057 -0.0444 -0.0271 1069 THR H CA  
3265 C C   . THR B 203 ? 0.3000 0.3683 0.2762 -0.0017 -0.0436 -0.0257 1069 THR H C   
3266 O O   . THR B 203 ? 0.3291 0.3981 0.3036 0.0051  -0.0447 -0.0266 1069 THR H O   
3267 C CB  . THR B 203 ? 0.2996 0.3811 0.2798 -0.0049 -0.0458 -0.0319 1069 THR H CB  
3268 O OG1 . THR B 203 ? 0.2925 0.3865 0.2763 -0.0090 -0.0445 -0.0335 1069 THR H OG1 
3269 C CG2 . THR B 203 ? 0.3191 0.3994 0.3000 -0.0086 -0.0468 -0.0339 1069 THR H CG2 
3270 N N   . ASP B 204 ? 0.2926 0.3602 0.2691 -0.0053 -0.0419 -0.0237 1070 ASP H N   
3271 C CA  . ASP B 204 ? 0.2959 0.3665 0.2720 -0.0013 -0.0414 -0.0231 1070 ASP H CA  
3272 C C   . ASP B 204 ? 0.2800 0.3389 0.2535 -0.0018 -0.0404 -0.0195 1070 ASP H C   
3273 O O   . ASP B 204 ? 0.2697 0.3248 0.2427 -0.0072 -0.0392 -0.0177 1070 ASP H O   
3274 C CB  . ASP B 204 ? 0.3224 0.4068 0.3015 -0.0039 -0.0404 -0.0249 1070 ASP H CB  
3275 C CG  . ASP B 204 ? 0.3779 0.4766 0.3600 -0.0027 -0.0417 -0.0293 1070 ASP H CG  
3276 O OD1 . ASP B 204 ? 0.4067 0.5071 0.3873 0.0047  -0.0435 -0.0312 1070 ASP H OD1 
3277 O OD2 . ASP B 204 ? 0.4421 0.5484 0.4273 -0.0094 -0.0408 -0.0309 1070 ASP H OD2 
3278 N N   . PHE B 205 ? 0.2519 0.3055 0.2234 0.0035  -0.0409 -0.0188 1071 PHE H N   
3279 C CA  . PHE B 205 ? 0.2475 0.2916 0.2171 0.0035  -0.0401 -0.0161 1071 PHE H CA  
3280 C C   . PHE B 205 ? 0.2521 0.2976 0.2209 0.0076  -0.0400 -0.0164 1071 PHE H C   
3281 O O   . PHE B 205 ? 0.2611 0.3101 0.2290 0.0124  -0.0409 -0.0183 1071 PHE H O   
3282 C CB  . PHE B 205 ? 0.2427 0.2766 0.2103 0.0046  -0.0405 -0.0151 1071 PHE H CB  
3283 C CG  . PHE B 205 ? 0.2459 0.2777 0.2136 0.0010  -0.0409 -0.0151 1071 PHE H CG  
3284 C CD1 . PHE B 205 ? 0.2496 0.2755 0.2160 -0.0028 -0.0404 -0.0133 1071 PHE H CD1 
3285 C CD2 . PHE B 205 ? 0.2547 0.2909 0.2233 0.0018  -0.0420 -0.0172 1071 PHE H CD2 
3286 C CE1 . PHE B 205 ? 0.2634 0.2867 0.2291 -0.0063 -0.0408 -0.0136 1071 PHE H CE1 
3287 C CE2 . PHE B 205 ? 0.2623 0.2971 0.2311 -0.0019 -0.0425 -0.0177 1071 PHE H CE2 
3288 C CZ  . PHE B 205 ? 0.2500 0.2777 0.2172 -0.0061 -0.0419 -0.0159 1071 PHE H CZ  
3289 N N   . THR B 206 ? 0.2392 0.2815 0.2075 0.0065  -0.0391 -0.0148 1072 THR H N   
3290 C CA  . THR B 206 ? 0.2433 0.2860 0.2108 0.0099  -0.0391 -0.0152 1072 THR H CA  
3291 C C   . THR B 206 ? 0.2437 0.2778 0.2100 0.0098  -0.0387 -0.0138 1072 THR H C   
3292 O O   . THR B 206 ? 0.2695 0.3014 0.2358 0.0067  -0.0381 -0.0122 1072 THR H O   
3293 C CB  . THR B 206 ? 0.2582 0.3104 0.2270 0.0091  -0.0385 -0.0156 1072 THR H CB  
3294 O OG1 . THR B 206 ? 0.2843 0.3466 0.2549 0.0089  -0.0388 -0.0175 1072 THR H OG1 
3295 C CG2 . THR B 206 ? 0.2590 0.3115 0.2267 0.0133  -0.0389 -0.0164 1072 THR H CG2 
3296 N N   . LEU B 207 ? 0.2406 0.2705 0.2056 0.0131  -0.0390 -0.0146 1073 LEU H N   
3297 C CA  . LEU B 207 ? 0.2472 0.2720 0.2118 0.0132  -0.0386 -0.0143 1073 LEU H CA  
3298 C C   . LEU B 207 ? 0.2462 0.2755 0.2107 0.0152  -0.0388 -0.0153 1073 LEU H C   
3299 O O   . LEU B 207 ? 0.2504 0.2814 0.2135 0.0185  -0.0394 -0.0168 1073 LEU H O   
3300 C CB  . LEU B 207 ? 0.2460 0.2633 0.2089 0.0146  -0.0385 -0.0149 1073 LEU H CB  
3301 C CG  . LEU B 207 ? 0.2533 0.2668 0.2163 0.0144  -0.0380 -0.0156 1073 LEU H CG  
3302 C CD1 . LEU B 207 ? 0.2421 0.2550 0.2066 0.0120  -0.0378 -0.0147 1073 LEU H CD1 
3303 C CD2 . LEU B 207 ? 0.2526 0.2590 0.2133 0.0151  -0.0375 -0.0165 1073 LEU H CD2 
3304 N N   . THR B 208 ? 0.2514 0.2823 0.2165 0.0140  -0.0384 -0.0147 1074 THR H N   
3305 C CA  . THR B 208 ? 0.2551 0.2904 0.2201 0.0161  -0.0386 -0.0158 1074 THR H CA  
3306 C C   . THR B 208 ? 0.2511 0.2815 0.2158 0.0170  -0.0389 -0.0168 1074 THR H C   
3307 O O   . THR B 208 ? 0.2496 0.2769 0.2148 0.0153  -0.0386 -0.0161 1074 THR H O   
3308 C CB  . THR B 208 ? 0.2519 0.2940 0.2172 0.0144  -0.0379 -0.0144 1074 THR H CB  
3309 O OG1 . THR B 208 ? 0.2600 0.3074 0.2261 0.0128  -0.0376 -0.0141 1074 THR H OG1 
3310 C CG2 . THR B 208 ? 0.2718 0.3193 0.2367 0.0171  -0.0381 -0.0156 1074 THR H CG2 
3311 N N   . ILE B 209 ? 0.2641 0.2942 0.2279 0.0199  -0.0395 -0.0189 1075 ILE H N   
3312 C CA  . ILE B 209 ? 0.2541 0.2812 0.2179 0.0204  -0.0397 -0.0208 1075 ILE H CA  
3313 C C   . ILE B 209 ? 0.2624 0.2958 0.2260 0.0229  -0.0404 -0.0218 1075 ILE H C   
3314 O O   . ILE B 209 ? 0.2808 0.3155 0.2428 0.0257  -0.0411 -0.0231 1075 ILE H O   
3315 C CB  . ILE B 209 ? 0.2646 0.2841 0.2267 0.0209  -0.0398 -0.0227 1075 ILE H CB  
3316 C CG1 . ILE B 209 ? 0.2684 0.2826 0.2299 0.0191  -0.0390 -0.0214 1075 ILE H CG1 
3317 C CG2 . ILE B 209 ? 0.2587 0.2763 0.2221 0.0197  -0.0397 -0.0248 1075 ILE H CG2 
3318 C CD1 . ILE B 209 ? 0.2862 0.2914 0.2441 0.0196  -0.0385 -0.0227 1075 ILE H CD1 
3319 N N   . SER B 210 ? 0.2460 0.2829 0.2103 0.0223  -0.0402 -0.0210 1076 SER H N   
3320 C CA  . SER B 210 ? 0.2452 0.2882 0.2089 0.0249  -0.0407 -0.0220 1076 SER H CA  
3321 C C   . SER B 210 ? 0.2418 0.2822 0.2056 0.0268  -0.0418 -0.0254 1076 SER H C   
3322 O O   . SER B 210 ? 0.2452 0.2807 0.2102 0.0249  -0.0417 -0.0266 1076 SER H O   
3323 C CB  . SER B 210 ? 0.2599 0.3061 0.2229 0.0239  -0.0400 -0.0198 1076 SER H CB  
3324 O OG  . SER B 210 ? 0.2808 0.3288 0.2433 0.0213  -0.0388 -0.0169 1076 SER H OG  
3325 N N   . ASN B 211 ? 0.2318 0.2759 0.1944 0.0301  -0.0427 -0.0273 1077 ASN H N   
3326 C CA  . ASN B 211 ? 0.2295 0.2715 0.1921 0.0317  -0.0439 -0.0311 1077 ASN H CA  
3327 C C   . ASN B 211 ? 0.2335 0.2665 0.1961 0.0294  -0.0438 -0.0329 1077 ASN H C   
3328 O O   . ASN B 211 ? 0.2277 0.2586 0.1920 0.0273  -0.0437 -0.0349 1077 ASN H O   
3329 C CB  . ASN B 211 ? 0.2248 0.2707 0.1886 0.0317  -0.0441 -0.0315 1077 ASN H CB  
3330 C CG  . ASN B 211 ? 0.2358 0.2831 0.1998 0.0341  -0.0456 -0.0358 1077 ASN H CG  
3331 O OD1 . ASN B 211 ? 0.2470 0.2979 0.2120 0.0348  -0.0461 -0.0370 1077 ASN H OD1 
3332 N ND2 . ASN B 211 ? 0.2115 0.2563 0.1740 0.0358  -0.0465 -0.0381 1077 ASN H ND2 
3333 N N   . VAL B 212 ? 0.2511 0.2791 0.2113 0.0297  -0.0435 -0.0322 1078 VAL H N   
3334 C CA  . VAL B 212 ? 0.2576 0.2755 0.2163 0.0272  -0.0428 -0.0329 1078 VAL H CA  
3335 C C   . VAL B 212 ? 0.2652 0.2778 0.2228 0.0267  -0.0433 -0.0368 1078 VAL H C   
3336 O O   . VAL B 212 ? 0.2601 0.2738 0.2157 0.0300  -0.0448 -0.0391 1078 VAL H O   
3337 C CB  . VAL B 212 ? 0.2750 0.2887 0.2300 0.0291  -0.0428 -0.0315 1078 VAL H CB  
3338 C CG1 . VAL B 212 ? 0.2869 0.2995 0.2373 0.0340  -0.0443 -0.0336 1078 VAL H CG1 
3339 C CG2 . VAL B 212 ? 0.2858 0.2894 0.2387 0.0263  -0.0415 -0.0311 1078 VAL H CG2 
3340 N N   . GLN B 213 ? 0.2557 0.2631 0.2146 0.0223  -0.0421 -0.0379 1079 GLN H N   
3341 C CA  . GLN B 213 ? 0.2627 0.2646 0.2209 0.0199  -0.0420 -0.0420 1079 GLN H CA  
3342 C C   . GLN B 213 ? 0.2907 0.2795 0.2438 0.0173  -0.0405 -0.0419 1079 GLN H C   
3343 O O   . GLN B 213 ? 0.2682 0.2537 0.2197 0.0170  -0.0395 -0.0387 1079 GLN H O   
3344 C CB  . GLN B 213 ? 0.2519 0.2600 0.2157 0.0164  -0.0415 -0.0439 1079 GLN H CB  
3345 C CG  . GLN B 213 ? 0.2556 0.2751 0.2226 0.0197  -0.0430 -0.0438 1079 GLN H CG  
3346 C CD  . GLN B 213 ? 0.2579 0.2797 0.2232 0.0236  -0.0448 -0.0463 1079 GLN H CD  
3347 O OE1 . GLN B 213 ? 0.2725 0.2912 0.2373 0.0225  -0.0454 -0.0506 1079 GLN H OE1 
3348 N NE2 . GLN B 213 ? 0.2529 0.2796 0.2168 0.0278  -0.0456 -0.0439 1079 GLN H NE2 
3349 N N   . SER B 214 ? 0.3163 0.2971 0.2662 0.0156  -0.0405 -0.0455 1080 SER H N   
3350 C CA  . SER B 214 ? 0.3465 0.3123 0.2897 0.0127  -0.0388 -0.0456 1080 SER H CA  
3351 C C   . SER B 214 ? 0.3516 0.3166 0.2976 0.0069  -0.0360 -0.0439 1080 SER H C   
3352 O O   . SER B 214 ? 0.3556 0.3103 0.2959 0.0061  -0.0344 -0.0417 1080 SER H O   
3353 C CB  . SER B 214 ? 0.3892 0.3466 0.3286 0.0108  -0.0390 -0.0501 1080 SER H CB  
3354 O OG  . SER B 214 ? 0.4224 0.3872 0.3687 0.0057  -0.0385 -0.0536 1080 SER H OG  
3355 N N   . GLU B 215 ? 0.3277 0.3035 0.2814 0.0039  -0.0355 -0.0449 1081 GLU H N   
3356 C CA  . GLU B 215 ? 0.3293 0.3054 0.2855 -0.0009 -0.0330 -0.0437 1081 GLU H CA  
3357 C C   . GLU B 215 ? 0.2985 0.2753 0.2538 0.0019  -0.0330 -0.0388 1081 GLU H C   
3358 O O   . GLU B 215 ? 0.3049 0.2801 0.2606 -0.0011 -0.0310 -0.0373 1081 GLU H O   
3359 C CB  . GLU B 215 ? 0.3275 0.3161 0.2917 -0.0036 -0.0331 -0.0464 1081 GLU H CB  
3360 C CG  . GLU B 215 ? 0.3399 0.3399 0.3083 0.0010  -0.0352 -0.0448 1081 GLU H CG  
3361 C CD  . GLU B 215 ? 0.3846 0.3959 0.3593 -0.0005 -0.0353 -0.0472 1081 GLU H CD  
3362 O OE1 . GLU B 215 ? 0.3762 0.3962 0.3535 0.0032  -0.0373 -0.0475 1081 GLU H OE1 
3363 O OE2 . GLU B 215 ? 0.3945 0.4060 0.3711 -0.0051 -0.0333 -0.0484 1081 GLU H OE2 
3364 N N   . ASP B 216 ? 0.2805 0.2603 0.2348 0.0074  -0.0350 -0.0367 1082 ASP H N   
3365 C CA  . ASP B 216 ? 0.2766 0.2584 0.2305 0.0100  -0.0352 -0.0327 1082 ASP H CA  
3366 C C   . ASP B 216 ? 0.3003 0.2713 0.2465 0.0122  -0.0348 -0.0310 1082 ASP H C   
3367 O O   . ASP B 216 ? 0.2950 0.2672 0.2404 0.0143  -0.0349 -0.0282 1082 ASP H O   
3368 C CB  . ASP B 216 ? 0.2611 0.2526 0.2177 0.0140  -0.0372 -0.0316 1082 ASP H CB  
3369 C CG  . ASP B 216 ? 0.2613 0.2625 0.2236 0.0132  -0.0378 -0.0328 1082 ASP H CG  
3370 O OD1 . ASP B 216 ? 0.2457 0.2485 0.2111 0.0098  -0.0368 -0.0338 1082 ASP H OD1 
3371 O OD2 . ASP B 216 ? 0.2510 0.2584 0.2140 0.0164  -0.0393 -0.0330 1082 ASP H OD2 
3372 N N   . LEU B 217 ? 0.3195 0.2797 0.2595 0.0121  -0.0344 -0.0328 1083 LEU H N   
3373 C CA  . LEU B 217 ? 0.3448 0.2926 0.2754 0.0150  -0.0341 -0.0313 1083 LEU H CA  
3374 C C   . LEU B 217 ? 0.3569 0.2986 0.2860 0.0108  -0.0313 -0.0294 1083 LEU H C   
3375 O O   . LEU B 217 ? 0.3887 0.3281 0.3196 0.0047  -0.0291 -0.0308 1083 LEU H O   
3376 C CB  . LEU B 217 ? 0.3809 0.3172 0.3041 0.0159  -0.0344 -0.0340 1083 LEU H CB  
3377 C CG  . LEU B 217 ? 0.3997 0.3426 0.3243 0.0205  -0.0373 -0.0363 1083 LEU H CG  
3378 C CD1 . LEU B 217 ? 0.4498 0.3798 0.3662 0.0215  -0.0378 -0.0393 1083 LEU H CD1 
3379 C CD2 . LEU B 217 ? 0.4039 0.3546 0.3283 0.0273  -0.0394 -0.0344 1083 LEU H CD2 
3380 N N   . ALA B 218 ? 0.3446 0.2861 0.2715 0.0137  -0.0314 -0.0265 1084 ALA H N   
3381 C CA  . ALA B 218 ? 0.3488 0.2883 0.2759 0.0104  -0.0291 -0.0243 1084 ALA H CA  
3382 C C   . ALA B 218 ? 0.3437 0.2841 0.2679 0.0156  -0.0302 -0.0217 1084 ALA H C   
3383 O O   . ALA B 218 ? 0.3304 0.2752 0.2541 0.0209  -0.0327 -0.0220 1084 ALA H O   
3384 C CB  . ALA B 218 ? 0.3418 0.2934 0.2788 0.0063  -0.0286 -0.0247 1084 ALA H CB  
3385 N N   . ASP B 219 ? 0.3477 0.2858 0.2709 0.0141  -0.0286 -0.0197 1085 ASP H N   
3386 C CA  . ASP B 219 ? 0.3461 0.2877 0.2684 0.0184  -0.0298 -0.0177 1085 ASP H CA  
3387 C C   . ASP B 219 ? 0.3183 0.2734 0.2503 0.0167  -0.0307 -0.0173 1085 ASP H C   
3388 O O   . ASP B 219 ? 0.3250 0.2835 0.2621 0.0121  -0.0295 -0.0177 1085 ASP H O   
3389 C CB  . ASP B 219 ? 0.3884 0.3201 0.3037 0.0184  -0.0277 -0.0157 1085 ASP H CB  
3390 C CG  . ASP B 219 ? 0.4405 0.3560 0.3433 0.0211  -0.0268 -0.0156 1085 ASP H CG  
3391 O OD1 . ASP B 219 ? 0.4798 0.3928 0.3787 0.0254  -0.0287 -0.0169 1085 ASP H OD1 
3392 O OD2 . ASP B 219 ? 0.5027 0.4077 0.3993 0.0186  -0.0240 -0.0142 1085 ASP H OD2 
3393 N N   . TYR B 220 ? 0.2959 0.2583 0.2297 0.0205  -0.0328 -0.0167 1086 TYR H N   
3394 C CA  . TYR B 220 ? 0.2859 0.2593 0.2273 0.0189  -0.0337 -0.0161 1086 TYR H CA  
3395 C C   . TYR B 220 ? 0.2819 0.2563 0.2217 0.0212  -0.0343 -0.0149 1086 TYR H C   
3396 O O   . TYR B 220 ? 0.2903 0.2634 0.2256 0.0257  -0.0354 -0.0151 1086 TYR H O   
3397 C CB  . TYR B 220 ? 0.2723 0.2546 0.2179 0.0200  -0.0355 -0.0171 1086 TYR H CB  
3398 C CG  . TYR B 220 ? 0.2740 0.2563 0.2217 0.0178  -0.0351 -0.0186 1086 TYR H CG  
3399 C CD1 . TYR B 220 ? 0.2745 0.2515 0.2181 0.0196  -0.0353 -0.0201 1086 TYR H CD1 
3400 C CD2 . TYR B 220 ? 0.2613 0.2484 0.2144 0.0143  -0.0347 -0.0187 1086 TYR H CD2 
3401 C CE1 . TYR B 220 ? 0.2859 0.2633 0.2316 0.0175  -0.0351 -0.0220 1086 TYR H CE1 
3402 C CE2 . TYR B 220 ? 0.2553 0.2435 0.2104 0.0128  -0.0345 -0.0206 1086 TYR H CE2 
3403 C CZ  . TYR B 220 ? 0.2628 0.2468 0.2148 0.0141  -0.0347 -0.0223 1086 TYR H CZ  
3404 O OH  . TYR B 220 ? 0.2598 0.2454 0.2142 0.0122  -0.0347 -0.0246 1086 TYR H OH  
3405 N N   . PHE B 221 ? 0.2815 0.2588 0.2250 0.0186  -0.0338 -0.0139 1087 PHE H N   
3406 C CA  . PHE B 221 ? 0.2974 0.2759 0.2399 0.0203  -0.0344 -0.0130 1087 PHE H CA  
3407 C C   . PHE B 221 ? 0.2811 0.2680 0.2298 0.0182  -0.0356 -0.0130 1087 PHE H C   
3408 O O   . PHE B 221 ? 0.2679 0.2561 0.2201 0.0151  -0.0351 -0.0129 1087 PHE H O   
3409 C CB  . PHE B 221 ? 0.3095 0.2810 0.2486 0.0191  -0.0324 -0.0120 1087 PHE H CB  
3410 C CG  . PHE B 221 ? 0.3593 0.3200 0.2903 0.0207  -0.0307 -0.0116 1087 PHE H CG  
3411 C CD1 . PHE B 221 ? 0.3653 0.3198 0.2948 0.0172  -0.0285 -0.0119 1087 PHE H CD1 
3412 C CD2 . PHE B 221 ? 0.3718 0.3280 0.2959 0.0257  -0.0314 -0.0111 1087 PHE H CD2 
3413 C CE1 . PHE B 221 ? 0.3807 0.3230 0.3013 0.0181  -0.0267 -0.0114 1087 PHE H CE1 
3414 C CE2 . PHE B 221 ? 0.3931 0.3370 0.3077 0.0277  -0.0298 -0.0105 1087 PHE H CE2 
3415 C CZ  . PHE B 221 ? 0.3956 0.3318 0.3081 0.0235  -0.0274 -0.0104 1087 PHE H CZ  
3416 N N   . CYS B 222 ? 0.2927 0.2849 0.2422 0.0199  -0.0372 -0.0132 1088 CYS H N   
3417 C CA  . CYS B 222 ? 0.2954 0.2930 0.2492 0.0174  -0.0381 -0.0130 1088 CYS H CA  
3418 C C   . CYS B 222 ? 0.2851 0.2793 0.2373 0.0177  -0.0379 -0.0124 1088 CYS H C   
3419 O O   . CYS B 222 ? 0.2850 0.2747 0.2327 0.0205  -0.0373 -0.0123 1088 CYS H O   
3420 C CB  . CYS B 222 ? 0.3344 0.3400 0.2904 0.0177  -0.0396 -0.0139 1088 CYS H CB  
3421 S SG  . CYS B 222 ? 0.4059 0.4130 0.3579 0.0229  -0.0407 -0.0153 1088 CYS H SG  
3422 N N   . GLN B 223 ? 0.2664 0.2622 0.2212 0.0153  -0.0384 -0.0122 1089 GLN H N   
3423 C CA  . GLN B 223 ? 0.2728 0.2665 0.2263 0.0158  -0.0387 -0.0120 1089 GLN H CA  
3424 C C   . GLN B 223 ? 0.2656 0.2630 0.2216 0.0139  -0.0404 -0.0125 1089 GLN H C   
3425 O O   . GLN B 223 ? 0.2602 0.2583 0.2181 0.0114  -0.0405 -0.0122 1089 GLN H O   
3426 C CB  . GLN B 223 ? 0.2839 0.2738 0.2371 0.0147  -0.0372 -0.0114 1089 GLN H CB  
3427 C CG  . GLN B 223 ? 0.3111 0.2993 0.2625 0.0158  -0.0374 -0.0113 1089 GLN H CG  
3428 C CD  . GLN B 223 ? 0.3342 0.3211 0.2858 0.0147  -0.0361 -0.0112 1089 GLN H CD  
3429 O OE1 . GLN B 223 ? 0.3175 0.3053 0.2711 0.0129  -0.0353 -0.0114 1089 GLN H OE1 
3430 N NE2 . GLN B 223 ? 0.4007 0.3864 0.3503 0.0161  -0.0360 -0.0111 1089 GLN H NE2 
3431 N N   . GLN B 224 ? 0.2584 0.2569 0.2136 0.0150  -0.0416 -0.0133 1090 GLN H N   
3432 C CA  . GLN B 224 ? 0.2519 0.2514 0.2086 0.0125  -0.0430 -0.0139 1090 GLN H CA  
3433 C C   . GLN B 224 ? 0.2478 0.2427 0.2027 0.0132  -0.0432 -0.0136 1090 GLN H C   
3434 O O   . GLN B 224 ? 0.2478 0.2409 0.2005 0.0160  -0.0425 -0.0134 1090 GLN H O   
3435 C CB  . GLN B 224 ? 0.2547 0.2597 0.2123 0.0125  -0.0445 -0.0158 1090 GLN H CB  
3436 C CG  . GLN B 224 ? 0.2620 0.2670 0.2171 0.0165  -0.0452 -0.0168 1090 GLN H CG  
3437 C CD  . GLN B 224 ? 0.2512 0.2531 0.2052 0.0164  -0.0462 -0.0173 1090 GLN H CD  
3438 O OE1 . GLN B 224 ? 0.2525 0.2526 0.2074 0.0132  -0.0470 -0.0175 1090 GLN H OE1 
3439 N NE2 . GLN B 224 ? 0.2689 0.2692 0.2198 0.0204  -0.0462 -0.0174 1090 GLN H NE2 
3440 N N   . TYR B 225 ? 0.2302 0.2228 0.1852 0.0112  -0.0440 -0.0135 1091 TYR H N   
3441 C CA  . TYR B 225 ? 0.2496 0.2385 0.2025 0.0124  -0.0447 -0.0137 1091 TYR H CA  
3442 C C   . TYR B 225 ? 0.2654 0.2521 0.2172 0.0106  -0.0468 -0.0147 1091 TYR H C   
3443 O O   . TYR B 225 ? 0.2713 0.2536 0.2207 0.0112  -0.0478 -0.0149 1091 TYR H O   
3444 C CB  . TYR B 225 ? 0.2444 0.2315 0.1971 0.0130  -0.0436 -0.0130 1091 TYR H CB  
3445 C CG  . TYR B 225 ? 0.2463 0.2326 0.1994 0.0111  -0.0438 -0.0124 1091 TYR H CG  
3446 C CD1 . TYR B 225 ? 0.2528 0.2351 0.2034 0.0111  -0.0451 -0.0126 1091 TYR H CD1 
3447 C CD2 . TYR B 225 ? 0.2483 0.2372 0.2035 0.0099  -0.0426 -0.0118 1091 TYR H CD2 
3448 C CE1 . TYR B 225 ? 0.2576 0.2384 0.2073 0.0101  -0.0452 -0.0119 1091 TYR H CE1 
3449 C CE2 . TYR B 225 ? 0.2557 0.2441 0.2108 0.0086  -0.0426 -0.0113 1091 TYR H CE2 
3450 C CZ  . TYR B 225 ? 0.2562 0.2404 0.2084 0.0088  -0.0438 -0.0112 1091 TYR H CZ  
3451 O OH  . TYR B 225 ? 0.2547 0.2377 0.2057 0.0081  -0.0439 -0.0106 1091 TYR H OH  
3452 N N   . SER B 226 ? 0.2837 0.2739 0.2371 0.0084  -0.0474 -0.0157 1092 SER H N   
3453 C CA  . SER B 226 ? 0.2911 0.2799 0.2436 0.0056  -0.0492 -0.0173 1092 SER H CA  
3454 C C   . SER B 226 ? 0.3060 0.2939 0.2570 0.0084  -0.0507 -0.0189 1092 SER H C   
3455 O O   . SER B 226 ? 0.3148 0.2978 0.2634 0.0072  -0.0523 -0.0199 1092 SER H O   
3456 C CB  . SER B 226 ? 0.3106 0.3061 0.2661 0.0024  -0.0490 -0.0184 1092 SER H CB  
3457 O OG  . SER B 226 ? 0.3263 0.3216 0.2815 -0.0010 -0.0505 -0.0205 1092 SER H OG  
3458 N N   . SER B 227 ? 0.2868 0.2785 0.2381 0.0122  -0.0503 -0.0193 1093 SER H N   
3459 C CA  . SER B 227 ? 0.3143 0.3061 0.2639 0.0154  -0.0518 -0.0210 1093 SER H CA  
3460 C C   . SER B 227 ? 0.2912 0.2833 0.2390 0.0201  -0.0502 -0.0197 1093 SER H C   
3461 O O   . SER B 227 ? 0.2866 0.2799 0.2350 0.0205  -0.0483 -0.0182 1093 SER H O   
3462 C CB  . SER B 227 ? 0.3236 0.3214 0.2749 0.0145  -0.0534 -0.0239 1093 SER H CB  
3463 O OG  . SER B 227 ? 0.3634 0.3674 0.3164 0.0159  -0.0523 -0.0237 1093 SER H OG  
3464 N N   . TYR B 228 ? 0.2658 0.2561 0.2110 0.0233  -0.0509 -0.0203 1094 TYR H N   
3465 C CA  . TYR B 228 ? 0.2732 0.2633 0.2155 0.0275  -0.0491 -0.0191 1094 TYR H CA  
3466 C C   . TYR B 228 ? 0.2826 0.2764 0.2236 0.0307  -0.0499 -0.0204 1094 TYR H C   
3467 O O   . TYR B 228 ? 0.2888 0.2859 0.2309 0.0306  -0.0523 -0.0231 1094 TYR H O   
3468 C CB  . TYR B 228 ? 0.2670 0.2545 0.2067 0.0298  -0.0493 -0.0191 1094 TYR H CB  
3469 C CG  . TYR B 228 ? 0.2754 0.2606 0.2158 0.0281  -0.0483 -0.0180 1094 TYR H CG  
3470 C CD1 . TYR B 228 ? 0.2769 0.2595 0.2173 0.0268  -0.0503 -0.0190 1094 TYR H CD1 
3471 C CD2 . TYR B 228 ? 0.2699 0.2553 0.2105 0.0277  -0.0453 -0.0161 1094 TYR H CD2 
3472 C CE1 . TYR B 228 ? 0.2726 0.2537 0.2129 0.0263  -0.0497 -0.0184 1094 TYR H CE1 
3473 C CE2 . TYR B 228 ? 0.2787 0.2638 0.2204 0.0264  -0.0445 -0.0157 1094 TYR H CE2 
3474 C CZ  . TYR B 228 ? 0.2788 0.2623 0.2204 0.0261  -0.0469 -0.0169 1094 TYR H CZ  
3475 O OH  . TYR B 228 ? 0.2979 0.2818 0.2401 0.0258  -0.0462 -0.0168 1094 TYR H OH  
3476 N N   . PRO B 229 ? 0.2865 0.2796 0.2245 0.0338  -0.0480 -0.0190 1095 PRO H N   
3477 C CA  . PRO B 229 ? 0.2911 0.2801 0.2277 0.0330  -0.0449 -0.0162 1095 PRO H CA  
3478 C C   . PRO B 229 ? 0.2729 0.2626 0.2130 0.0294  -0.0441 -0.0155 1095 PRO H C   
3479 O O   . PRO B 229 ? 0.2548 0.2482 0.1969 0.0288  -0.0453 -0.0167 1095 PRO H O   
3480 C CB  . PRO B 229 ? 0.2944 0.2810 0.2252 0.0375  -0.0433 -0.0152 1095 PRO H CB  
3481 C CG  . PRO B 229 ? 0.3034 0.2949 0.2341 0.0404  -0.0459 -0.0176 1095 PRO H CG  
3482 C CD  . PRO B 229 ? 0.2968 0.2928 0.2317 0.0384  -0.0488 -0.0203 1095 PRO H CD  
3483 N N   . LEU B 230 ? 0.2736 0.2607 0.2146 0.0270  -0.0422 -0.0139 1096 LEU H N   
3484 C CA  . LEU B 230 ? 0.2754 0.2629 0.2192 0.0240  -0.0413 -0.0133 1096 LEU H CA  
3485 C C   . LEU B 230 ? 0.2698 0.2561 0.2109 0.0261  -0.0401 -0.0126 1096 LEU H C   
3486 O O   . LEU B 230 ? 0.2664 0.2488 0.2025 0.0288  -0.0386 -0.0117 1096 LEU H O   
3487 C CB  . LEU B 230 ? 0.2835 0.2692 0.2284 0.0218  -0.0395 -0.0122 1096 LEU H CB  
3488 C CG  . LEU B 230 ? 0.2984 0.2845 0.2441 0.0215  -0.0406 -0.0130 1096 LEU H CG  
3489 C CD1 . LEU B 230 ? 0.2982 0.2846 0.2454 0.0198  -0.0391 -0.0127 1096 LEU H CD1 
3490 C CD2 . LEU B 230 ? 0.3010 0.2878 0.2485 0.0202  -0.0434 -0.0141 1096 LEU H CD2 
3491 N N   . THR B 231 ? 0.2635 0.2527 0.2066 0.0253  -0.0408 -0.0132 1097 THR H N   
3492 C CA  . THR B 231 ? 0.2658 0.2538 0.2053 0.0284  -0.0402 -0.0130 1097 THR H CA  
3493 C C   . THR B 231 ? 0.2636 0.2519 0.2054 0.0261  -0.0394 -0.0126 1097 THR H C   
3494 O O   . THR B 231 ? 0.2640 0.2562 0.2108 0.0226  -0.0401 -0.0130 1097 THR H O   
3495 C CB  . THR B 231 ? 0.2729 0.2663 0.2116 0.0319  -0.0425 -0.0151 1097 THR H CB  
3496 O OG1 . THR B 231 ? 0.2891 0.2897 0.2337 0.0286  -0.0443 -0.0168 1097 THR H OG1 
3497 C CG2 . THR B 231 ? 0.2799 0.2719 0.2149 0.0355  -0.0431 -0.0156 1097 THR H CG2 
3498 N N   . PHE B 232 ? 0.2761 0.2597 0.2134 0.0283  -0.0381 -0.0119 1098 PHE H N   
3499 C CA  . PHE B 232 ? 0.2878 0.2702 0.2258 0.0269  -0.0372 -0.0117 1098 PHE H CA  
3500 C C   . PHE B 232 ? 0.2917 0.2765 0.2273 0.0310  -0.0386 -0.0129 1098 PHE H C   
3501 O O   . PHE B 232 ? 0.3137 0.2971 0.2441 0.0357  -0.0393 -0.0134 1098 PHE H O   
3502 C CB  . PHE B 232 ? 0.2944 0.2682 0.2284 0.0258  -0.0344 -0.0102 1098 PHE H CB  
3503 C CG  . PHE B 232 ? 0.2921 0.2654 0.2289 0.0218  -0.0328 -0.0096 1098 PHE H CG  
3504 C CD1 . PHE B 232 ? 0.2980 0.2693 0.2325 0.0223  -0.0319 -0.0089 1098 PHE H CD1 
3505 C CD2 . PHE B 232 ? 0.2774 0.2531 0.2190 0.0180  -0.0323 -0.0100 1098 PHE H CD2 
3506 C CE1 . PHE B 232 ? 0.3042 0.2763 0.2412 0.0191  -0.0304 -0.0088 1098 PHE H CE1 
3507 C CE2 . PHE B 232 ? 0.2852 0.2615 0.2290 0.0151  -0.0310 -0.0100 1098 PHE H CE2 
3508 C CZ  . PHE B 232 ? 0.2929 0.2680 0.2347 0.0156  -0.0301 -0.0095 1098 PHE H CZ  
3509 N N   . GLY B 233 ? 0.3030 0.2910 0.2413 0.0298  -0.0389 -0.0135 1099 GLY H N   
3510 C CA  . GLY B 233 ? 0.3002 0.2894 0.2351 0.0342  -0.0399 -0.0147 1099 GLY H CA  
3511 C C   . GLY B 233 ? 0.3168 0.2943 0.2429 0.0374  -0.0384 -0.0137 1099 GLY H C   
3512 O O   . GLY B 233 ? 0.3133 0.2825 0.2375 0.0345  -0.0360 -0.0119 1099 GLY H O   
3513 N N   . GLY B 234 ? 0.3225 0.2989 0.2428 0.0432  -0.0396 -0.0149 1100 GLY H N   
3514 C CA  . GLY B 234 ? 0.3421 0.3048 0.2519 0.0469  -0.0383 -0.0138 1100 GLY H CA  
3515 C C   . GLY B 234 ? 0.3361 0.2925 0.2453 0.0438  -0.0368 -0.0135 1100 GLY H C   
3516 O O   . GLY B 234 ? 0.3504 0.2933 0.2503 0.0454  -0.0353 -0.0125 1100 GLY H O   
3517 N N   . GLY B 235 ? 0.3203 0.2846 0.2381 0.0395  -0.0371 -0.0141 1101 GLY H N   
3518 C CA  . GLY B 235 ? 0.3277 0.2866 0.2452 0.0366  -0.0359 -0.0142 1101 GLY H CA  
3519 C C   . GLY B 235 ? 0.3206 0.2821 0.2365 0.0406  -0.0377 -0.0160 1101 GLY H C   
3520 O O   . GLY B 235 ? 0.3266 0.2888 0.2371 0.0471  -0.0395 -0.0171 1101 GLY H O   
3521 N N   . THR B 236 ? 0.3218 0.2858 0.2422 0.0374  -0.0375 -0.0167 1102 THR H N   
3522 C CA  . THR B 236 ? 0.3462 0.3108 0.2644 0.0407  -0.0389 -0.0186 1102 THR H CA  
3523 C C   . THR B 236 ? 0.3606 0.3146 0.2762 0.0373  -0.0371 -0.0186 1102 THR H C   
3524 O O   . THR B 236 ? 0.3546 0.3115 0.2769 0.0313  -0.0358 -0.0183 1102 THR H O   
3525 C CB  . THR B 236 ? 0.3337 0.3134 0.2605 0.0399  -0.0404 -0.0197 1102 THR H CB  
3526 O OG1 . THR B 236 ? 0.3315 0.3211 0.2608 0.0419  -0.0417 -0.0200 1102 THR H OG1 
3527 C CG2 . THR B 236 ? 0.3417 0.3236 0.2667 0.0434  -0.0418 -0.0217 1102 THR H CG2 
3528 N N   . LYS B 237 ? 0.3794 0.3223 0.2856 0.0413  -0.0374 -0.0195 1103 LYS H N   
3529 C CA  . LYS B 237 ? 0.4086 0.3412 0.3116 0.0383  -0.0361 -0.0204 1103 LYS H CA  
3530 C C   . LYS B 237 ? 0.3753 0.3159 0.2819 0.0402  -0.0382 -0.0227 1103 LYS H C   
3531 O O   . LYS B 237 ? 0.3459 0.2883 0.2482 0.0470  -0.0405 -0.0240 1103 LYS H O   
3532 C CB  . LYS B 237 ? 0.4697 0.3837 0.3588 0.0415  -0.0352 -0.0202 1103 LYS H CB  
3533 C CG  . LYS B 237 ? 0.5107 0.4126 0.3961 0.0367  -0.0334 -0.0212 1103 LYS H CG  
3534 C CD  . LYS B 237 ? 0.5788 0.4598 0.4487 0.0397  -0.0323 -0.0206 1103 LYS H CD  
3535 C CE  . LYS B 237 ? 0.6405 0.5088 0.5049 0.0365  -0.0313 -0.0225 1103 LYS H CE  
3536 N NZ  . LYS B 237 ? 0.6587 0.5301 0.5318 0.0263  -0.0286 -0.0232 1103 LYS H NZ  
3537 N N   . LEU B 238 ? 0.3543 0.3009 0.2690 0.0348  -0.0375 -0.0234 1104 LEU H N   
3538 C CA  . LEU B 238 ? 0.3506 0.3044 0.2686 0.0364  -0.0393 -0.0256 1104 LEU H CA  
3539 C C   . LEU B 238 ? 0.3477 0.2889 0.2591 0.0360  -0.0389 -0.0276 1104 LEU H C   
3540 O O   . LEU B 238 ? 0.3689 0.3033 0.2809 0.0299  -0.0367 -0.0277 1104 LEU H O   
3541 C CB  . LEU B 238 ? 0.3434 0.3094 0.2721 0.0313  -0.0388 -0.0253 1104 LEU H CB  
3542 C CG  . LEU B 238 ? 0.3489 0.3235 0.2814 0.0327  -0.0404 -0.0272 1104 LEU H CG  
3543 C CD1 . LEU B 238 ? 0.3531 0.3363 0.2847 0.0387  -0.0425 -0.0276 1104 LEU H CD1 
3544 C CD2 . LEU B 238 ? 0.3352 0.3194 0.2766 0.0280  -0.0397 -0.0266 1104 LEU H CD2 
3545 N N   . GLU B 239 ? 0.3840 0.3226 0.2894 0.0422  -0.0411 -0.0295 1105 GLU H N   
3546 C CA  . GLU B 239 ? 0.4035 0.3282 0.3009 0.0427  -0.0412 -0.0318 1105 GLU H CA  
3547 C C   . GLU B 239 ? 0.3993 0.3322 0.2995 0.0458  -0.0436 -0.0346 1105 GLU H C   
3548 O O   . GLU B 239 ? 0.3480 0.2956 0.2537 0.0490  -0.0451 -0.0345 1105 GLU H O   
3549 C CB  . GLU B 239 ? 0.4353 0.3446 0.3186 0.0492  -0.0419 -0.0316 1105 GLU H CB  
3550 C CG  . GLU B 239 ? 0.4803 0.3827 0.3594 0.0484  -0.0400 -0.0287 1105 GLU H CG  
3551 C CD  . GLU B 239 ? 0.5155 0.4038 0.3796 0.0567  -0.0412 -0.0285 1105 GLU H CD  
3552 O OE1 . GLU B 239 ? 0.5300 0.4001 0.3842 0.0547  -0.0391 -0.0275 1105 GLU H OE1 
3553 O OE2 . GLU B 239 ? 0.5487 0.4446 0.4107 0.0653  -0.0442 -0.0296 1105 GLU H OE2 
3554 N N   . MET B 240 ? 0.4455 0.3685 0.3415 0.0445  -0.0437 -0.0372 1106 MET H N   
3555 C CA  . MET B 240 ? 0.4782 0.4058 0.3743 0.0484  -0.0462 -0.0404 1106 MET H CA  
3556 C C   . MET B 240 ? 0.4786 0.4027 0.3650 0.0583  -0.0489 -0.0415 1106 MET H C   
3557 O O   . MET B 240 ? 0.4739 0.3810 0.3485 0.0609  -0.0487 -0.0412 1106 MET H O   
3558 C CB  . MET B 240 ? 0.5310 0.4465 0.4239 0.0439  -0.0454 -0.0433 1106 MET H CB  
3559 C CG  . MET B 240 ? 0.6003 0.5253 0.4981 0.0452  -0.0475 -0.0466 1106 MET H CG  
3560 S SD  . MET B 240 ? 0.6751 0.6207 0.5887 0.0396  -0.0464 -0.0455 1106 MET H SD  
3561 C CE  . MET B 240 ? 0.6427 0.5803 0.5585 0.0303  -0.0442 -0.0481 1106 MET H CE  
3562 N N   . LYS B 241 ? 0.4955 0.4347 0.3857 0.0639  -0.0513 -0.0426 1107 LYS H N   
3563 C CA  . LYS B 241 ? 0.5782 0.5163 0.4594 0.0742  -0.0543 -0.0448 1107 LYS H CA  
3564 C C   . LYS B 241 ? 0.6289 0.5446 0.4966 0.0767  -0.0551 -0.0470 1107 LYS H C   
3565 O O   . LYS B 241 ? 0.6441 0.5545 0.5128 0.0724  -0.0548 -0.0491 1107 LYS H O   
3566 C CB  . LYS B 241 ? 0.6219 0.5766 0.5090 0.0778  -0.0564 -0.0472 1107 LYS H CB  
3567 C CG  . LYS B 241 ? 0.6674 0.6405 0.5581 0.0834  -0.0577 -0.0468 1107 LYS H CG  
3568 C CD  . LYS B 241 ? 0.7027 0.6916 0.6059 0.0768  -0.0556 -0.0440 1107 LYS H CD  
3569 C CE  . LYS B 241 ? 0.7430 0.7474 0.6489 0.0806  -0.0563 -0.0435 1107 LYS H CE  
3570 N NZ  . LYS B 241 ? 0.7648 0.7874 0.6821 0.0758  -0.0550 -0.0422 1107 LYS H NZ  
3571 N N   . ALA C 1   ? 0.2382 0.3024 0.2748 0.0005  0.0065  0.0096  1    ALA M N   
3572 C CA  . ALA C 1   ? 0.2230 0.2928 0.2646 0.0022  0.0063  0.0101  1    ALA M CA  
3573 C C   . ALA C 1   ? 0.2305 0.2997 0.2729 0.0053  0.0080  0.0097  1    ALA M C   
3574 O O   . ALA C 1   ? 0.2411 0.3063 0.2801 0.0059  0.0096  0.0087  1    ALA M O   
3575 C CB  . ALA C 1   ? 0.2241 0.2981 0.2680 0.0005  0.0065  0.0099  1    ALA M CB  
3576 N N   . PRO C 2   ? 0.2042 0.2767 0.2504 0.0078  0.0075  0.0103  2    PRO M N   
3577 C CA  . PRO C 2   ? 0.1908 0.2677 0.2405 0.0073  0.0052  0.0113  2    PRO M CA  
3578 C C   . PRO C 2   ? 0.1812 0.2549 0.2284 0.0074  0.0036  0.0121  2    PRO M C   
3579 O O   . PRO C 2   ? 0.1936 0.2699 0.2422 0.0067  0.0018  0.0127  2    PRO M O   
3580 C CB  . PRO C 2   ? 0.1983 0.2804 0.2531 0.0102  0.0055  0.0115  2    PRO M CB  
3581 C CG  . PRO C 2   ? 0.2028 0.2809 0.2551 0.0132  0.0072  0.0111  2    PRO M CG  
3582 C CD  . PRO C 2   ? 0.2094 0.2831 0.2574 0.0117  0.0090  0.0101  2    PRO M CD  
3583 N N   . GLY C 3   ? 0.1859 0.2535 0.2289 0.0082  0.0042  0.0121  3    GLY M N   
3584 C CA  . GLY C 3   ? 0.2011 0.2642 0.2405 0.0078  0.0030  0.0132  3    GLY M CA  
3585 C C   . GLY C 3   ? 0.2008 0.2629 0.2379 0.0041  0.0028  0.0132  3    GLY M C   
3586 O O   . GLY C 3   ? 0.2234 0.2865 0.2606 0.0023  0.0035  0.0123  3    GLY M O   
3587 N N   . SER C 4   ? 0.1971 0.2582 0.2326 0.0030  0.0017  0.0144  4    SER M N   
3588 C CA  . SER C 4   ? 0.1907 0.2525 0.2248 -0.0002 0.0014  0.0146  4    SER M CA  
3589 C C   . SER C 4   ? 0.2024 0.2591 0.2326 -0.0018 0.0014  0.0156  4    SER M C   
3590 O O   . SER C 4   ? 0.2349 0.2882 0.2634 -0.0004 0.0013  0.0167  4    SER M O   
3591 C CB  . SER C 4   ? 0.1897 0.2568 0.2261 -0.0001 0.0000  0.0153  4    SER M CB  
3592 O OG  . SER C 4   ? 0.1770 0.2461 0.2129 -0.0027 0.0000  0.0152  4    SER M OG  
3593 N N   . THR C 5   ? 0.1929 0.2493 0.2216 -0.0050 0.0015  0.0156  5    THR M N   
3594 C CA  . THR C 5   ? 0.1953 0.2467 0.2205 -0.0073 0.0016  0.0167  5    THR M CA  
3595 C C   . THR C 5   ? 0.1993 0.2537 0.2246 -0.0086 0.0011  0.0186  5    THR M C   
3596 O O   . THR C 5   ? 0.1849 0.2454 0.2127 -0.0084 0.0006  0.0187  5    THR M O   
3597 C CB  . THR C 5   ? 0.1912 0.2411 0.2148 -0.0106 0.0017  0.0156  5    THR M CB  
3598 O OG1 . THR C 5   ? 0.1851 0.2418 0.2116 -0.0115 0.0014  0.0151  5    THR M OG1 
3599 C CG2 . THR C 5   ? 0.1983 0.2427 0.2197 -0.0093 0.0025  0.0138  5    THR M CG2 
3600 N N   . ALA C 6   ? 0.2197 0.2694 0.2421 -0.0096 0.0012  0.0201  6    ALA M N   
3601 C CA  . ALA C 6   ? 0.2429 0.2952 0.2650 -0.0109 0.0011  0.0223  6    ALA M CA  
3602 C C   . ALA C 6   ? 0.2601 0.3158 0.2828 -0.0150 0.0012  0.0226  6    ALA M C   
3603 O O   . ALA C 6   ? 0.2609 0.3150 0.2832 -0.0173 0.0011  0.0214  6    ALA M O   
3604 C CB  . ALA C 6   ? 0.2702 0.3156 0.2883 -0.0111 0.0013  0.0241  6    ALA M CB  
3605 N N   . PRO C 7   ? 0.2491 0.3097 0.2725 -0.0159 0.0014  0.0245  7    PRO M N   
3606 C CA  . PRO C 7   ? 0.2676 0.3329 0.2923 -0.0195 0.0015  0.0251  7    PRO M CA  
3607 C C   . PRO C 7   ? 0.3019 0.3630 0.3246 -0.0237 0.0016  0.0259  7    PRO M C   
3608 O O   . PRO C 7   ? 0.3671 0.4324 0.3914 -0.0271 0.0015  0.0261  7    PRO M O   
3609 C CB  . PRO C 7   ? 0.2573 0.3289 0.2829 -0.0188 0.0020  0.0271  7    PRO M CB  
3610 C CG  . PRO C 7   ? 0.2538 0.3247 0.2787 -0.0146 0.0018  0.0270  7    PRO M CG  
3611 C CD  . PRO C 7   ? 0.2565 0.3197 0.2797 -0.0133 0.0014  0.0260  7    PRO M CD  
3612 N N   . NH2 C 8   ? 0.3131 0.3662 0.3324 -0.0241 0.0018  0.0267  8    NH2 M N   
3613 N N   . ALA D 1   ? 0.3197 0.3376 0.3422 0.0161  -0.0630 -0.0167 1    ALA N N   
3614 C CA  . ALA D 1   ? 0.2952 0.3190 0.3213 0.0166  -0.0613 -0.0151 1    ALA N CA  
3615 C C   . ALA D 1   ? 0.2941 0.3245 0.3248 0.0136  -0.0630 -0.0133 1    ALA N C   
3616 O O   . ALA D 1   ? 0.3169 0.3488 0.3478 0.0109  -0.0661 -0.0129 1    ALA N O   
3617 C CB  . ALA D 1   ? 0.2957 0.3211 0.3203 0.0204  -0.0600 -0.0150 1    ALA N CB  
3618 N N   . PRO D 2   ? 0.2890 0.3234 0.3227 0.0132  -0.0613 -0.0117 2    PRO N N   
3619 C CA  . PRO D 2   ? 0.2659 0.2974 0.2980 0.0153  -0.0581 -0.0119 2    PRO N CA  
3620 C C   . PRO D 2   ? 0.2491 0.2747 0.2793 0.0136  -0.0577 -0.0130 2    PRO N C   
3621 O O   . PRO D 2   ? 0.2587 0.2813 0.2861 0.0147  -0.0556 -0.0131 2    PRO N O   
3622 C CB  . PRO D 2   ? 0.2700 0.3091 0.3060 0.0158  -0.0567 -0.0092 2    PRO N CB  
3623 C CG  . PRO D 2   ? 0.2810 0.3266 0.3217 0.0114  -0.0599 -0.0077 2    PRO N CG  
3624 C CD  . PRO D 2   ? 0.2987 0.3418 0.3373 0.0102  -0.0629 -0.0090 2    PRO N CD  
3625 N N   . GLY D 3   ? 0.2373 0.2605 0.2675 0.0109  -0.0597 -0.0135 3    GLY N N   
3626 C CA  . GLY D 3   ? 0.2449 0.2628 0.2724 0.0105  -0.0591 -0.0141 3    GLY N CA  
3627 C C   . GLY D 3   ? 0.2402 0.2546 0.2635 0.0131  -0.0588 -0.0150 3    GLY N C   
3628 O O   . GLY D 3   ? 0.2470 0.2613 0.2693 0.0143  -0.0598 -0.0157 3    GLY N O   
3629 N N   . SER D 4   ? 0.2296 0.2423 0.2508 0.0139  -0.0574 -0.0144 4    SER N N   
3630 C CA  . SER D 4   ? 0.2304 0.2423 0.2481 0.0164  -0.0570 -0.0142 4    SER N CA  
3631 C C   . SER D 4   ? 0.2415 0.2501 0.2555 0.0185  -0.0569 -0.0136 4    SER N C   
3632 O O   . SER D 4   ? 0.3009 0.3085 0.3148 0.0180  -0.0563 -0.0130 4    SER N O   
3633 C CB  . SER D 4   ? 0.2255 0.2406 0.2432 0.0156  -0.0552 -0.0126 4    SER N CB  
3634 O OG  . SER D 4   ? 0.2106 0.2266 0.2253 0.0171  -0.0552 -0.0118 4    SER N OG  
3635 N N   . THR D 5   ? 0.2381 0.2455 0.2481 0.0219  -0.0567 -0.0133 5    THR N N   
3636 C CA  . THR D 5   ? 0.2420 0.2453 0.2462 0.0258  -0.0561 -0.0125 5    THR N CA  
3637 C C   . THR D 5   ? 0.2428 0.2532 0.2472 0.0282  -0.0535 -0.0089 5    THR N C   
3638 O O   . THR D 5   ? 0.2343 0.2523 0.2417 0.0267  -0.0529 -0.0071 5    THR N O   
3639 C CB  . THR D 5   ? 0.2527 0.2506 0.2513 0.0290  -0.0573 -0.0137 5    THR N CB  
3640 O OG1 . THR D 5   ? 0.2318 0.2366 0.2336 0.0291  -0.0568 -0.0130 5    THR N OG1 
3641 C CG2 . THR D 5   ? 0.2569 0.2477 0.2538 0.0259  -0.0605 -0.0164 5    THR N CG2 
3642 N N   . ALA D 6   ? 0.2572 0.2649 0.2577 0.0312  -0.0523 -0.0076 6    ALA N N   
3643 C CA  . ALA D 6   ? 0.2601 0.2763 0.2605 0.0344  -0.0497 -0.0032 6    ALA N CA  
3644 C C   . ALA D 6   ? 0.2768 0.2969 0.2732 0.0401  -0.0485 -0.0007 6    ALA N C   
3645 O O   . ALA D 6   ? 0.2933 0.3073 0.2854 0.0427  -0.0494 -0.0025 6    ALA N O   
3646 C CB  . ALA D 6   ? 0.2857 0.2959 0.2809 0.0379  -0.0484 -0.0026 6    ALA N CB  
3647 N N   . PRO D 7   ? 0.2816 0.3144 0.2802 0.0413  -0.0466 0.0043  7    PRO N N   
3648 C CA  . PRO D 7   ? 0.2982 0.3384 0.2940 0.0467  -0.0452 0.0081  7    PRO N CA  
3649 C C   . PRO D 7   ? 0.3324 0.3679 0.3197 0.0560  -0.0431 0.0095  7    PRO N C   
3650 O O   . PRO D 7   ? 0.3699 0.4129 0.3547 0.0615  -0.0415 0.0133  7    PRO N O   
3651 C CB  . PRO D 7   ? 0.2902 0.3470 0.2915 0.0431  -0.0444 0.0138  7    PRO N CB  
3652 C CG  . PRO D 7   ? 0.2838 0.3410 0.2877 0.0400  -0.0441 0.0141  7    PRO N CG  
3653 C CD  . PRO D 7   ? 0.2708 0.3125 0.2742 0.0377  -0.0458 0.0073  7    PRO N CD  
3654 N N   . NH2 D 8   ? 0.3244 0.3482 0.3056 0.0590  -0.0425 0.0076  8    NH2 N N   
3655 C C1  . EDO E .   ? 0.2784 0.3629 0.3248 -0.0049 -0.0046 0.0112  301  EDO A C1  
3656 O O1  . EDO E .   ? 0.2466 0.3305 0.2929 -0.0064 -0.0046 0.0110  301  EDO A O1  
3657 C C2  . EDO E .   ? 0.2522 0.3381 0.3008 -0.0039 -0.0065 0.0113  301  EDO A C2  
3658 O O2  . EDO E .   ? 0.2988 0.3855 0.3495 -0.0049 -0.0080 0.0112  301  EDO A O2  
3659 C C1  . EDO F .   ? 0.6761 0.7267 0.6975 -0.0225 -0.0065 0.0169  302  EDO A C1  
3660 O O1  . EDO F .   ? 0.6544 0.7063 0.6752 -0.0234 -0.0034 0.0180  302  EDO A O1  
3661 C C2  . EDO F .   ? 0.7004 0.7555 0.7285 -0.0244 -0.0068 0.0169  302  EDO A C2  
3662 O O2  . EDO F .   ? 0.6627 0.7212 0.6930 -0.0218 -0.0079 0.0154  302  EDO A O2  
3663 C C1  . EDO G .   ? 0.1938 0.2636 0.1977 -0.0122 -0.0046 0.0069  303  EDO A C1  
3664 O O1  . EDO G .   ? 0.1848 0.2535 0.1866 -0.0107 -0.0050 0.0079  303  EDO A O1  
3665 C C2  . EDO G .   ? 0.1988 0.2728 0.2044 -0.0127 -0.0068 0.0066  303  EDO A C2  
3666 O O2  . EDO G .   ? 0.2076 0.2819 0.2094 -0.0126 -0.0086 0.0062  303  EDO A O2  
3667 C C1  . EDO H .   ? 0.5678 0.6342 0.5796 -0.0176 -0.0019 0.0046  304  EDO A C1  
3668 O O1  . EDO H .   ? 0.5449 0.6148 0.5583 -0.0193 -0.0039 0.0049  304  EDO A O1  
3669 C C2  . EDO H .   ? 0.5964 0.6601 0.6036 -0.0173 -0.0016 0.0037  304  EDO A C2  
3670 O O2  . EDO H .   ? 0.6275 0.6865 0.6322 -0.0165 0.0004  0.0029  304  EDO A O2  
3671 C C1  . EDO I .   ? 0.5727 0.6263 0.5884 -0.0146 0.0034  0.0048  305  EDO A C1  
3672 O O1  . EDO I .   ? 0.5753 0.6292 0.5936 -0.0143 0.0032  0.0059  305  EDO A O1  
3673 C C2  . EDO I .   ? 0.5572 0.6158 0.5744 -0.0159 0.0020  0.0053  305  EDO A C2  
3674 O O2  . EDO I .   ? 0.5839 0.6423 0.5985 -0.0159 0.0021  0.0045  305  EDO A O2  
3675 C C1  . EDO J .   ? 0.5583 0.6126 0.5839 -0.0836 -0.0512 0.0345  306  EDO A C1  
3676 O O1  . EDO J .   ? 0.5759 0.6431 0.5999 -0.0888 -0.0535 0.0414  306  EDO A O1  
3677 C C2  . EDO J .   ? 0.5879 0.6430 0.6082 -0.0847 -0.0488 0.0333  306  EDO A C2  
3678 O O2  . EDO J .   ? 0.5865 0.6321 0.6073 -0.0795 -0.0448 0.0258  306  EDO A O2  
3679 C C1  . EDO K .   ? 0.3670 0.3976 0.3028 -0.0925 0.0092  -0.0221 307  EDO A C1  
3680 O O1  . EDO K .   ? 0.3402 0.3694 0.2733 -0.0933 0.0129  -0.0271 307  EDO A O1  
3681 C C2  . EDO K .   ? 0.3639 0.3892 0.2969 -0.0949 0.0065  -0.0219 307  EDO A C2  
3682 O O2  . EDO K .   ? 0.3158 0.3458 0.2563 -0.0911 0.0040  -0.0173 307  EDO A O2  
3683 C C1  . EDO L .   ? 0.3600 0.4131 0.3743 -0.0161 0.0032  0.0333  301  EDO H C1  
3684 O O1  . EDO L .   ? 0.3302 0.3907 0.3466 -0.0137 0.0031  0.0332  301  EDO H O1  
3685 C C2  . EDO L .   ? 0.3953 0.4451 0.4105 -0.0146 0.0023  0.0306  301  EDO H C2  
3686 O O2  . EDO L .   ? 0.4097 0.4501 0.4213 -0.0155 0.0023  0.0307  301  EDO H O2  
3687 C C1  . EDO M .   ? 0.6178 0.5083 0.4516 -0.0712 -0.0739 0.0164  302  EDO H C1  
3688 O O1  . EDO M .   ? 0.6770 0.5375 0.4846 -0.0711 -0.0740 0.0141  302  EDO H O1  
3689 C C2  . EDO M .   ? 0.5688 0.4703 0.4221 -0.0592 -0.0694 0.0123  302  EDO H C2  
3690 O O2  . EDO M .   ? 0.4807 0.3787 0.3381 -0.0477 -0.0661 0.0076  302  EDO H O2  
3691 C C1  . EDO N .   ? 0.4238 0.4018 0.3942 0.0211  -0.0517 -0.0138 303  EDO H C1  
3692 O O1  . EDO N .   ? 0.4500 0.4194 0.4103 0.0250  -0.0509 -0.0143 303  EDO H O1  
3693 C C2  . EDO N .   ? 0.4014 0.3728 0.3653 0.0195  -0.0503 -0.0128 303  EDO H C2  
3694 O O2  . EDO N .   ? 0.4570 0.4153 0.4067 0.0235  -0.0481 -0.0126 303  EDO H O2  
3695 C C1  . EDO O .   ? 0.4971 0.4504 0.3499 0.0910  -0.0371 -0.0084 304  EDO H C1  
3696 O O1  . EDO O .   ? 0.5049 0.4609 0.3638 0.0883  -0.0388 -0.0099 304  EDO H O1  
3697 C C2  . EDO O .   ? 0.5126 0.4529 0.3499 0.0961  -0.0334 -0.0045 304  EDO H C2  
3698 O O2  . EDO O .   ? 0.4727 0.4117 0.3030 0.1003  -0.0322 -0.0035 304  EDO H O2  
3703 O O5  . A2G Q .   ? 0.1700 0.2445 0.2069 -0.0012 -0.0020 0.0164  101  A2G M O5  
3704 C C1  . A2G Q .   ? 0.1684 0.2421 0.2060 -0.0023 -0.0011 0.0152  101  A2G M C1  
3705 C C2  . A2G Q .   ? 0.1597 0.2353 0.1966 -0.0047 -0.0010 0.0148  101  A2G M C2  
3706 N N2  . A2G Q .   ? 0.1433 0.2175 0.1801 -0.0057 -0.0002 0.0137  101  A2G M N2  
3707 C C3  . A2G Q .   ? 0.1598 0.2349 0.1945 -0.0064 -0.0008 0.0161  101  A2G M C3  
3708 O O3  . A2G Q .   ? 0.1488 0.2269 0.1836 -0.0080 -0.0010 0.0156  101  A2G M O3  
3709 C C4  . A2G Q .   ? 0.1632 0.2399 0.1976 -0.0048 -0.0015 0.0174  101  A2G M C4  
3710 O O4  . A2G Q .   ? 0.1616 0.2422 0.1972 -0.0035 -0.0026 0.0169  101  A2G M O4  
3711 C C5  . A2G Q .   ? 0.1697 0.2433 0.2041 -0.0026 -0.0017 0.0177  101  A2G M C5  
3712 C C6  . A2G Q .   ? 0.1806 0.2550 0.2138 -0.0011 -0.0023 0.0192  101  A2G M C6  
3713 O O6  . A2G Q .   ? 0.1761 0.2467 0.2081 0.0002  -0.0023 0.0200  101  A2G M O6  
3714 C C7  . A2G Q .   ? 0.1400 0.2165 0.1777 -0.0060 -0.0004 0.0128  101  A2G M C7  
3715 O O7  . A2G Q .   ? 0.1372 0.2166 0.1760 -0.0054 -0.0014 0.0129  101  A2G M O7  
3716 C C8  . A2G Q .   ? 0.1340 0.2086 0.1707 -0.0071 0.0005  0.0118  101  A2G M C8  
3717 O O5  . A2G R .   ? 0.2068 0.2624 0.2310 -0.0157 0.0011  0.0132  102  A2G M O5  
3718 C C1  . A2G R .   ? 0.1913 0.2494 0.2171 -0.0150 0.0009  0.0150  102  A2G M C1  
3719 C C2  . A2G R .   ? 0.1805 0.2461 0.2092 -0.0149 0.0004  0.0154  102  A2G M C2  
3720 N N2  . A2G R .   ? 0.1744 0.2422 0.2040 -0.0136 0.0003  0.0170  102  A2G M N2  
3721 C C3  . A2G R .   ? 0.1743 0.2420 0.2047 -0.0126 0.0005  0.0139  102  A2G M C3  
3722 O O3  . A2G R .   ? 0.1571 0.2306 0.1895 -0.0123 -0.0001 0.0143  102  A2G M O3  
3723 C C4  . A2G R .   ? 0.1866 0.2513 0.2153 -0.0135 0.0009  0.0123  102  A2G M C4  
3724 O O4  . A2G R .   ? 0.1863 0.2529 0.2142 -0.0163 0.0001  0.0122  102  A2G M O4  
3725 C C5  . A2G R .   ? 0.2009 0.2590 0.2269 -0.0133 0.0016  0.0120  102  A2G M C5  
3726 C C6  . A2G R .   ? 0.2198 0.2744 0.2430 -0.0144 0.0019  0.0103  102  A2G M C6  
3727 O O6  . A2G R .   ? 0.2292 0.2766 0.2491 -0.0135 0.0026  0.0097  102  A2G M O6  
3728 C C7  . A2G R .   ? 0.1831 0.2554 0.2134 -0.0151 0.0000  0.0183  102  A2G M C7  
3729 O O7  . A2G R .   ? 0.2006 0.2761 0.2315 -0.0172 -0.0002 0.0181  102  A2G M O7  
3730 C C8  . A2G R .   ? 0.1818 0.2562 0.2123 -0.0133 0.0001  0.0200  102  A2G M C8  
3731 O O5  . A2G S .   ? 0.2106 0.2306 0.2231 0.0122  -0.0536 -0.0080 101  A2G N O5  
3732 C C1  . A2G S .   ? 0.2098 0.2269 0.2226 0.0148  -0.0546 -0.0106 101  A2G N C1  
3733 C C2  . A2G S .   ? 0.2120 0.2299 0.2214 0.0158  -0.0551 -0.0099 101  A2G N C2  
3734 N N2  . A2G S .   ? 0.2116 0.2266 0.2213 0.0184  -0.0561 -0.0125 101  A2G N N2  
3735 C C3  . A2G S .   ? 0.2153 0.2384 0.2244 0.0176  -0.0545 -0.0072 101  A2G N C3  
3736 O O3  . A2G S .   ? 0.2069 0.2326 0.2134 0.0187  -0.0549 -0.0059 101  A2G N O3  
3737 C C4  . A2G S .   ? 0.2094 0.2376 0.2190 0.0146  -0.0536 -0.0039 101  A2G N C4  
3738 O O4  . A2G S .   ? 0.2201 0.2476 0.2261 0.0097  -0.0541 -0.0027 101  A2G N O4  
3739 C C5  . A2G S .   ? 0.2172 0.2425 0.2297 0.0138  -0.0531 -0.0055 101  A2G N C5  
3740 C C6  . A2G S .   ? 0.2283 0.2584 0.2410 0.0108  -0.0523 -0.0022 101  A2G N C6  
3741 O O6  . A2G S .   ? 0.2293 0.2582 0.2449 0.0117  -0.0516 -0.0030 101  A2G N O6  
3742 C C7  . A2G S .   ? 0.2138 0.2269 0.2207 0.0186  -0.0565 -0.0131 101  A2G N C7  
3743 O O7  . A2G S .   ? 0.2142 0.2254 0.2168 0.0162  -0.0561 -0.0120 101  A2G N O7  
3744 C C8  . A2G S .   ? 0.2203 0.2317 0.2280 0.0213  -0.0577 -0.0153 101  A2G N C8  
3745 O O5  . A2G T .   ? 0.2528 0.2506 0.2467 0.0341  -0.0584 -0.0147 102  A2G N O5  
3746 C C1  . A2G T .   ? 0.2452 0.2493 0.2417 0.0341  -0.0562 -0.0120 102  A2G N C1  
3747 C C2  . A2G T .   ? 0.2406 0.2543 0.2410 0.0328  -0.0552 -0.0097 102  A2G N C2  
3748 N N2  . A2G T .   ? 0.2392 0.2599 0.2421 0.0312  -0.0536 -0.0065 102  A2G N N2  
3749 C C3  . A2G T .   ? 0.2352 0.2488 0.2390 0.0286  -0.0567 -0.0118 102  A2G N C3  
3750 O O3  . A2G T .   ? 0.2233 0.2426 0.2276 0.0266  -0.0561 -0.0098 102  A2G N O3  
3751 C C4  . A2G T .   ? 0.2411 0.2484 0.2426 0.0301  -0.0587 -0.0148 102  A2G N C4  
3752 O O4  . A2G T .   ? 0.2300 0.2374 0.2275 0.0340  -0.0584 -0.0141 102  A2G N O4  
3753 C C5  . A2G T .   ? 0.2495 0.2499 0.2485 0.0302  -0.0599 -0.0164 102  A2G N C5  
3754 C C6  . A2G T .   ? 0.2732 0.2668 0.2679 0.0310  -0.0623 -0.0186 102  A2G N C6  
3755 O O6  . A2G T .   ? 0.2785 0.2646 0.2694 0.0291  -0.0642 -0.0196 102  A2G N O6  
3756 C C7  . A2G T .   ? 0.2552 0.2848 0.2577 0.0325  -0.0522 -0.0023 102  A2G N C7  
3757 O O7  . A2G T .   ? 0.2562 0.2886 0.2562 0.0357  -0.0520 -0.0009 102  A2G N O7  
3758 C C8  . A2G T .   ? 0.2439 0.2814 0.2491 0.0298  -0.0510 0.0012  102  A2G N C8  
# 
