data_8Z8T
# 
_entry.id   8Z8T 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Z8T         pdb_00008z8t 10.2210/pdb8z8t/pdb 
WWPDB D_1300047218 ?            ?                   
# 
_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       2025-04-23 
_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                        8Z8T 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              hmorita@inm.u-toyama.ac.jp 
_pdbx_contact_author.name_first         Hiroyuki 
_pdbx_contact_author.name_last          Morita 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7788-8333 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Saw, Y.Y.H.'   1 ? 
'Nakashima, Y.' 2 ? 
'Morita, H.'    3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structural guided studies for Amaryllidaceae O-methyltransferases' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Saw, Y.Y.H.'   1 ? 
primary 'Nakashima, Y.' 2 ? 
primary 'Morita, H.'    3 ? 
# 
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 
;Norbelladine 4'-O-methyltransferase
;
27395.109 2   2.1.1.336 'S52T, Y186F' ? ? 
2 non-polymer syn GLYCEROL                              92.094    2   ?         ?             ? ? 
3 non-polymer syn 'MAGNESIUM ION'                       24.305    2   ?         ?             ? ? 
4 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE             384.411   2   ?         ?             ? ? 
5 non-polymer syn Norbelladine                          259.300   1   ?         ?             ? ? 
6 water       nat water                                 18.015    134 ?         ?             ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        NpN4OMT 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPGMGASIDDYSLVHKNILHSEDLLKYILETSAYPREHEQLKGLREVTEKHEWSTALVPADEGLFLSMLLKLMNAKRTIE
IGVYTGYSLLTTALALPEDGKITAIDVNKSYYEIGLPFIQKAGVEHKINFIESEALPVLDQMLEEMKEEDLYDYAFVDAD
KSNYANYHERLVKLVRIGGAILYDNTLWFGSVAYPEYPGLHPEEEVARLSFRNLNTFLAADPRVEISQVSIGDGVTICRR
LY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPGMGASIDDYSLVHKNILHSEDLLKYILETSAYPREHEQLKGLREVTEKHEWSTALVPADEGLFLSMLLKLMNAKRTIE
IGVYTGYSLLTTALALPEDGKITAIDVNKSYYEIGLPFIQKAGVEHKINFIESEALPVLDQMLEEMKEEDLYDYAFVDAD
KSNYANYHERLVKLVRIGGAILYDNTLWFGSVAYPEYPGLHPEEEVARLSFRNLNTFLAADPRVEISQVSIGDGVTICRR
LY
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL                  GOL   
3 'MAGNESIUM ION'           MG    
4 S-ADENOSYL-L-HOMOCYSTEINE SAH   
5 Norbelladine              A1LU2 
6 water                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   MET n 
1 5   GLY n 
1 6   ALA n 
1 7   SER n 
1 8   ILE n 
1 9   ASP n 
1 10  ASP n 
1 11  TYR n 
1 12  SER n 
1 13  LEU n 
1 14  VAL n 
1 15  HIS n 
1 16  LYS n 
1 17  ASN n 
1 18  ILE n 
1 19  LEU n 
1 20  HIS n 
1 21  SER n 
1 22  GLU n 
1 23  ASP n 
1 24  LEU n 
1 25  LEU n 
1 26  LYS n 
1 27  TYR n 
1 28  ILE n 
1 29  LEU n 
1 30  GLU n 
1 31  THR n 
1 32  SER n 
1 33  ALA n 
1 34  TYR n 
1 35  PRO n 
1 36  ARG n 
1 37  GLU n 
1 38  HIS n 
1 39  GLU n 
1 40  GLN n 
1 41  LEU n 
1 42  LYS n 
1 43  GLY n 
1 44  LEU n 
1 45  ARG n 
1 46  GLU n 
1 47  VAL n 
1 48  THR n 
1 49  GLU n 
1 50  LYS n 
1 51  HIS n 
1 52  GLU n 
1 53  TRP n 
1 54  SER n 
1 55  THR n 
1 56  ALA n 
1 57  LEU n 
1 58  VAL n 
1 59  PRO n 
1 60  ALA n 
1 61  ASP n 
1 62  GLU n 
1 63  GLY n 
1 64  LEU n 
1 65  PHE n 
1 66  LEU n 
1 67  SER n 
1 68  MET n 
1 69  LEU n 
1 70  LEU n 
1 71  LYS n 
1 72  LEU n 
1 73  MET n 
1 74  ASN n 
1 75  ALA n 
1 76  LYS n 
1 77  ARG n 
1 78  THR n 
1 79  ILE n 
1 80  GLU n 
1 81  ILE n 
1 82  GLY n 
1 83  VAL n 
1 84  TYR n 
1 85  THR n 
1 86  GLY n 
1 87  TYR n 
1 88  SER n 
1 89  LEU n 
1 90  LEU n 
1 91  THR n 
1 92  THR n 
1 93  ALA n 
1 94  LEU n 
1 95  ALA n 
1 96  LEU n 
1 97  PRO n 
1 98  GLU n 
1 99  ASP n 
1 100 GLY n 
1 101 LYS n 
1 102 ILE n 
1 103 THR n 
1 104 ALA n 
1 105 ILE n 
1 106 ASP n 
1 107 VAL n 
1 108 ASN n 
1 109 LYS n 
1 110 SER n 
1 111 TYR n 
1 112 TYR n 
1 113 GLU n 
1 114 ILE n 
1 115 GLY n 
1 116 LEU n 
1 117 PRO n 
1 118 PHE n 
1 119 ILE n 
1 120 GLN n 
1 121 LYS n 
1 122 ALA n 
1 123 GLY n 
1 124 VAL n 
1 125 GLU n 
1 126 HIS n 
1 127 LYS n 
1 128 ILE n 
1 129 ASN n 
1 130 PHE n 
1 131 ILE n 
1 132 GLU n 
1 133 SER n 
1 134 GLU n 
1 135 ALA n 
1 136 LEU n 
1 137 PRO n 
1 138 VAL n 
1 139 LEU n 
1 140 ASP n 
1 141 GLN n 
1 142 MET n 
1 143 LEU n 
1 144 GLU n 
1 145 GLU n 
1 146 MET n 
1 147 LYS n 
1 148 GLU n 
1 149 GLU n 
1 150 ASP n 
1 151 LEU n 
1 152 TYR n 
1 153 ASP n 
1 154 TYR n 
1 155 ALA n 
1 156 PHE n 
1 157 VAL n 
1 158 ASP n 
1 159 ALA n 
1 160 ASP n 
1 161 LYS n 
1 162 SER n 
1 163 ASN n 
1 164 TYR n 
1 165 ALA n 
1 166 ASN n 
1 167 TYR n 
1 168 HIS n 
1 169 GLU n 
1 170 ARG n 
1 171 LEU n 
1 172 VAL n 
1 173 LYS n 
1 174 LEU n 
1 175 VAL n 
1 176 ARG n 
1 177 ILE n 
1 178 GLY n 
1 179 GLY n 
1 180 ALA n 
1 181 ILE n 
1 182 LEU n 
1 183 TYR n 
1 184 ASP n 
1 185 ASN n 
1 186 THR n 
1 187 LEU n 
1 188 TRP n 
1 189 PHE n 
1 190 GLY n 
1 191 SER n 
1 192 VAL n 
1 193 ALA n 
1 194 TYR n 
1 195 PRO n 
1 196 GLU n 
1 197 TYR n 
1 198 PRO n 
1 199 GLY n 
1 200 LEU n 
1 201 HIS n 
1 202 PRO n 
1 203 GLU n 
1 204 GLU n 
1 205 GLU n 
1 206 VAL n 
1 207 ALA n 
1 208 ARG n 
1 209 LEU n 
1 210 SER n 
1 211 PHE n 
1 212 ARG n 
1 213 ASN n 
1 214 LEU n 
1 215 ASN n 
1 216 THR n 
1 217 PHE n 
1 218 LEU n 
1 219 ALA n 
1 220 ALA n 
1 221 ASP n 
1 222 PRO n 
1 223 ARG n 
1 224 VAL n 
1 225 GLU n 
1 226 ILE n 
1 227 SER n 
1 228 GLN n 
1 229 VAL n 
1 230 SER n 
1 231 ILE n 
1 232 GLY n 
1 233 ASP n 
1 234 GLY n 
1 235 VAL n 
1 236 THR n 
1 237 ILE n 
1 238 CYS n 
1 239 ARG n 
1 240 ARG n 
1 241 LEU n 
1 242 TYR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   242 
_entity_src_gen.gene_src_common_name               daffodil 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 N4OMT 
_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      'Narcissus pseudonarcissus MK-2014' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1540222 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli M15' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     1007065 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1LU2 non-polymer         . Norbelladine              ?                               'C15 H17 N O3'    259.300 
ALA   'L-peptide linking' y ALANINE                   ?                               'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                  ?                               'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                ?                               'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'           ?                               'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                  ?                               'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE                 ?                               'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'           ?                               'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                   ?                               'C2 H5 N O2'      75.067  
GOL   non-polymer         . GLYCEROL                  'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'        92.094  
HIS   'L-peptide linking' y HISTIDINE                 ?                               'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                     ?                               'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                ?                               'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                   ?                               'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                    ?                               'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                ?                               'C5 H11 N O2 S'   149.211 
MG    non-polymer         . 'MAGNESIUM ION'           ?                               'Mg 2'            24.305  
PHE   'L-peptide linking' y PHENYLALANINE             ?                               'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                   ?                               'C5 H9 N O2'      115.130 
SAH   non-polymer         . S-ADENOSYL-L-HOMOCYSTEINE ?                               'C14 H20 N6 O5 S' 384.411 
SER   'L-peptide linking' y SERINE                    ?                               'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                 ?                               'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                ?                               'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                  ?                               'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                    ?                               'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   PRO 2   -1  ?   ?   ?   A . n 
A 1 3   GLY 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   ?   ?   ?   A . n 
A 1 5   GLY 5   2   ?   ?   ?   A . n 
A 1 6   ALA 6   3   ?   ?   ?   A . n 
A 1 7   SER 7   4   ?   ?   ?   A . n 
A 1 8   ILE 8   5   ?   ?   ?   A . n 
A 1 9   ASP 9   6   6   ASP ASP A . n 
A 1 10  ASP 10  7   7   ASP ASP A . n 
A 1 11  TYR 11  8   8   TYR TYR A . n 
A 1 12  SER 12  9   9   SER SER A . n 
A 1 13  LEU 13  10  10  LEU LEU A . n 
A 1 14  VAL 14  11  11  VAL VAL A . n 
A 1 15  HIS 15  12  12  HIS HIS A . n 
A 1 16  LYS 16  13  13  LYS LYS A . n 
A 1 17  ASN 17  14  14  ASN ASN A . n 
A 1 18  ILE 18  15  15  ILE ILE A . n 
A 1 19  LEU 19  16  16  LEU LEU A . n 
A 1 20  HIS 20  17  17  HIS HIS A . n 
A 1 21  SER 21  18  18  SER SER A . n 
A 1 22  GLU 22  19  19  GLU GLU A . n 
A 1 23  ASP 23  20  20  ASP ASP A . n 
A 1 24  LEU 24  21  21  LEU LEU A . n 
A 1 25  LEU 25  22  22  LEU LEU A . n 
A 1 26  LYS 26  23  23  LYS LYS A . n 
A 1 27  TYR 27  24  24  TYR TYR A . n 
A 1 28  ILE 28  25  25  ILE ILE A . n 
A 1 29  LEU 29  26  26  LEU LEU A . n 
A 1 30  GLU 30  27  27  GLU GLU A . n 
A 1 31  THR 31  28  28  THR THR A . n 
A 1 32  SER 32  29  29  SER SER A . n 
A 1 33  ALA 33  30  30  ALA ALA A . n 
A 1 34  TYR 34  31  31  TYR TYR A . n 
A 1 35  PRO 35  32  32  PRO PRO A . n 
A 1 36  ARG 36  33  33  ARG ARG A . n 
A 1 37  GLU 37  34  34  GLU GLU A . n 
A 1 38  HIS 38  35  35  HIS HIS A . n 
A 1 39  GLU 39  36  36  GLU GLU A . n 
A 1 40  GLN 40  37  37  GLN GLN A . n 
A 1 41  LEU 41  38  38  LEU LEU A . n 
A 1 42  LYS 42  39  39  LYS LYS A . n 
A 1 43  GLY 43  40  40  GLY GLY A . n 
A 1 44  LEU 44  41  41  LEU LEU A . n 
A 1 45  ARG 45  42  42  ARG ARG A . n 
A 1 46  GLU 46  43  43  GLU GLU A . n 
A 1 47  VAL 47  44  44  VAL VAL A . n 
A 1 48  THR 48  45  45  THR THR A . n 
A 1 49  GLU 49  46  46  GLU GLU A . n 
A 1 50  LYS 50  47  47  LYS LYS A . n 
A 1 51  HIS 51  48  48  HIS HIS A . n 
A 1 52  GLU 52  49  49  GLU GLU A . n 
A 1 53  TRP 53  50  50  TRP TRP A . n 
A 1 54  SER 54  51  51  SER SER A . n 
A 1 55  THR 55  52  52  THR THR A . n 
A 1 56  ALA 56  53  53  ALA ALA A . n 
A 1 57  LEU 57  54  54  LEU LEU A . n 
A 1 58  VAL 58  55  55  VAL VAL A . n 
A 1 59  PRO 59  56  56  PRO PRO A . n 
A 1 60  ALA 60  57  57  ALA ALA A . n 
A 1 61  ASP 61  58  58  ASP ASP A . n 
A 1 62  GLU 62  59  59  GLU GLU A . n 
A 1 63  GLY 63  60  60  GLY GLY A . n 
A 1 64  LEU 64  61  61  LEU LEU A . n 
A 1 65  PHE 65  62  62  PHE PHE A . n 
A 1 66  LEU 66  63  63  LEU LEU A . n 
A 1 67  SER 67  64  64  SER SER A . n 
A 1 68  MET 68  65  65  MET MET A . n 
A 1 69  LEU 69  66  66  LEU LEU A . n 
A 1 70  LEU 70  67  67  LEU LEU A . n 
A 1 71  LYS 71  68  68  LYS LYS A . n 
A 1 72  LEU 72  69  69  LEU LEU A . n 
A 1 73  MET 73  70  70  MET MET A . n 
A 1 74  ASN 74  71  71  ASN ASN A . n 
A 1 75  ALA 75  72  72  ALA ALA A . n 
A 1 76  LYS 76  73  73  LYS LYS A . n 
A 1 77  ARG 77  74  74  ARG ARG A . n 
A 1 78  THR 78  75  75  THR THR A . n 
A 1 79  ILE 79  76  76  ILE ILE A . n 
A 1 80  GLU 80  77  77  GLU GLU A . n 
A 1 81  ILE 81  78  78  ILE ILE A . n 
A 1 82  GLY 82  79  79  GLY GLY A . n 
A 1 83  VAL 83  80  80  VAL VAL A . n 
A 1 84  TYR 84  81  81  TYR TYR A . n 
A 1 85  THR 85  82  82  THR THR A . n 
A 1 86  GLY 86  83  83  GLY GLY A . n 
A 1 87  TYR 87  84  84  TYR TYR A . n 
A 1 88  SER 88  85  85  SER SER A . n 
A 1 89  LEU 89  86  86  LEU LEU A . n 
A 1 90  LEU 90  87  87  LEU LEU A . n 
A 1 91  THR 91  88  88  THR THR A . n 
A 1 92  THR 92  89  89  THR THR A . n 
A 1 93  ALA 93  90  90  ALA ALA A . n 
A 1 94  LEU 94  91  91  LEU LEU A . n 
A 1 95  ALA 95  92  92  ALA ALA A . n 
A 1 96  LEU 96  93  93  LEU LEU A . n 
A 1 97  PRO 97  94  94  PRO PRO A . n 
A 1 98  GLU 98  95  95  GLU GLU A . n 
A 1 99  ASP 99  96  96  ASP ASP A . n 
A 1 100 GLY 100 97  97  GLY GLY A . n 
A 1 101 LYS 101 98  98  LYS LYS A . n 
A 1 102 ILE 102 99  99  ILE ILE A . n 
A 1 103 THR 103 100 100 THR THR A . n 
A 1 104 ALA 104 101 101 ALA ALA A . n 
A 1 105 ILE 105 102 102 ILE ILE A . n 
A 1 106 ASP 106 103 103 ASP ASP A . n 
A 1 107 VAL 107 104 104 VAL VAL A . n 
A 1 108 ASN 108 105 105 ASN ASN A . n 
A 1 109 LYS 109 106 106 LYS LYS A . n 
A 1 110 SER 110 107 107 SER SER A . n 
A 1 111 TYR 111 108 108 TYR TYR A . n 
A 1 112 TYR 112 109 109 TYR TYR A . n 
A 1 113 GLU 113 110 110 GLU GLU A . n 
A 1 114 ILE 114 111 111 ILE ILE A . n 
A 1 115 GLY 115 112 112 GLY GLY A . n 
A 1 116 LEU 116 113 113 LEU LEU A . n 
A 1 117 PRO 117 114 114 PRO PRO A . n 
A 1 118 PHE 118 115 115 PHE PHE A . n 
A 1 119 ILE 119 116 116 ILE ILE A . n 
A 1 120 GLN 120 117 117 GLN GLN A . n 
A 1 121 LYS 121 118 118 LYS LYS A . n 
A 1 122 ALA 122 119 119 ALA ALA A . n 
A 1 123 GLY 123 120 120 GLY GLY A . n 
A 1 124 VAL 124 121 121 VAL VAL A . n 
A 1 125 GLU 125 122 122 GLU GLU A . n 
A 1 126 HIS 126 123 123 HIS HIS A . n 
A 1 127 LYS 127 124 124 LYS LYS A . n 
A 1 128 ILE 128 125 125 ILE ILE A . n 
A 1 129 ASN 129 126 126 ASN ASN A . n 
A 1 130 PHE 130 127 127 PHE PHE A . n 
A 1 131 ILE 131 128 128 ILE ILE A . n 
A 1 132 GLU 132 129 129 GLU GLU A . n 
A 1 133 SER 133 130 130 SER SER A . n 
A 1 134 GLU 134 131 131 GLU GLU A . n 
A 1 135 ALA 135 132 132 ALA ALA A . n 
A 1 136 LEU 136 133 133 LEU LEU A . n 
A 1 137 PRO 137 134 134 PRO PRO A . n 
A 1 138 VAL 138 135 135 VAL VAL A . n 
A 1 139 LEU 139 136 136 LEU LEU A . n 
A 1 140 ASP 140 137 137 ASP ASP A . n 
A 1 141 GLN 141 138 138 GLN GLN A . n 
A 1 142 MET 142 139 139 MET MET A . n 
A 1 143 LEU 143 140 140 LEU LEU A . n 
A 1 144 GLU 144 141 141 GLU GLU A . n 
A 1 145 GLU 145 142 142 GLU GLU A . n 
A 1 146 MET 146 143 143 MET MET A . n 
A 1 147 LYS 147 144 144 LYS LYS A . n 
A 1 148 GLU 148 145 145 GLU GLU A . n 
A 1 149 GLU 149 146 146 GLU GLU A . n 
A 1 150 ASP 150 147 147 ASP ASP A . n 
A 1 151 LEU 151 148 148 LEU LEU A . n 
A 1 152 TYR 152 149 149 TYR TYR A . n 
A 1 153 ASP 153 150 150 ASP ASP A . n 
A 1 154 TYR 154 151 151 TYR TYR A . n 
A 1 155 ALA 155 152 152 ALA ALA A . n 
A 1 156 PHE 156 153 153 PHE PHE A . n 
A 1 157 VAL 157 154 154 VAL VAL A . n 
A 1 158 ASP 158 155 155 ASP ASP A . n 
A 1 159 ALA 159 156 156 ALA ALA A . n 
A 1 160 ASP 160 157 157 ASP ASP A . n 
A 1 161 LYS 161 158 158 LYS LYS A . n 
A 1 162 SER 162 159 159 SER SER A . n 
A 1 163 ASN 163 160 160 ASN ASN A . n 
A 1 164 TYR 164 161 161 TYR TYR A . n 
A 1 165 ALA 165 162 162 ALA ALA A . n 
A 1 166 ASN 166 163 163 ASN ASN A . n 
A 1 167 TYR 167 164 164 TYR TYR A . n 
A 1 168 HIS 168 165 165 HIS HIS A . n 
A 1 169 GLU 169 166 166 GLU GLU A . n 
A 1 170 ARG 170 167 167 ARG ARG A . n 
A 1 171 LEU 171 168 168 LEU LEU A . n 
A 1 172 VAL 172 169 169 VAL VAL A . n 
A 1 173 LYS 173 170 170 LYS LYS A . n 
A 1 174 LEU 174 171 171 LEU LEU A . n 
A 1 175 VAL 175 172 172 VAL VAL A . n 
A 1 176 ARG 176 173 173 ARG ARG A . n 
A 1 177 ILE 177 174 174 ILE ILE A . n 
A 1 178 GLY 178 175 175 GLY GLY A . n 
A 1 179 GLY 179 176 176 GLY GLY A . n 
A 1 180 ALA 180 177 177 ALA ALA A . n 
A 1 181 ILE 181 178 178 ILE ILE A . n 
A 1 182 LEU 182 179 179 LEU LEU A . n 
A 1 183 TYR 183 180 180 TYR TYR A . n 
A 1 184 ASP 184 181 181 ASP ASP A . n 
A 1 185 ASN 185 182 182 ASN ASN A . n 
A 1 186 THR 186 183 183 THR THR A . n 
A 1 187 LEU 187 184 184 LEU LEU A . n 
A 1 188 TRP 188 185 185 TRP TRP A . n 
A 1 189 PHE 189 186 186 PHE PHE A . n 
A 1 190 GLY 190 187 187 GLY GLY A . n 
A 1 191 SER 191 188 188 SER SER A . n 
A 1 192 VAL 192 189 189 VAL VAL A . n 
A 1 193 ALA 193 190 190 ALA ALA A . n 
A 1 194 TYR 194 191 191 TYR TYR A . n 
A 1 195 PRO 195 192 192 PRO PRO A . n 
A 1 196 GLU 196 193 193 GLU GLU A . n 
A 1 197 TYR 197 194 194 TYR TYR A . n 
A 1 198 PRO 198 195 195 PRO PRO A . n 
A 1 199 GLY 199 196 196 GLY GLY A . n 
A 1 200 LEU 200 197 197 LEU LEU A . n 
A 1 201 HIS 201 198 198 HIS HIS A . n 
A 1 202 PRO 202 199 199 PRO PRO A . n 
A 1 203 GLU 203 200 200 GLU GLU A . n 
A 1 204 GLU 204 201 201 GLU GLU A . n 
A 1 205 GLU 205 202 202 GLU GLU A . n 
A 1 206 VAL 206 203 203 VAL VAL A . n 
A 1 207 ALA 207 204 204 ALA ALA A . n 
A 1 208 ARG 208 205 205 ARG ARG A . n 
A 1 209 LEU 209 206 206 LEU LEU A . n 
A 1 210 SER 210 207 207 SER SER A . n 
A 1 211 PHE 211 208 208 PHE PHE A . n 
A 1 212 ARG 212 209 209 ARG ARG A . n 
A 1 213 ASN 213 210 210 ASN ASN A . n 
A 1 214 LEU 214 211 211 LEU LEU A . n 
A 1 215 ASN 215 212 212 ASN ASN A . n 
A 1 216 THR 216 213 213 THR THR A . n 
A 1 217 PHE 217 214 214 PHE PHE A . n 
A 1 218 LEU 218 215 215 LEU LEU A . n 
A 1 219 ALA 219 216 216 ALA ALA A . n 
A 1 220 ALA 220 217 217 ALA ALA A . n 
A 1 221 ASP 221 218 218 ASP ASP A . n 
A 1 222 PRO 222 219 219 PRO PRO A . n 
A 1 223 ARG 223 220 220 ARG ARG A . n 
A 1 224 VAL 224 221 221 VAL VAL A . n 
A 1 225 GLU 225 222 222 GLU GLU A . n 
A 1 226 ILE 226 223 223 ILE ILE A . n 
A 1 227 SER 227 224 224 SER SER A . n 
A 1 228 GLN 228 225 225 GLN GLN A . n 
A 1 229 VAL 229 226 226 VAL VAL A . n 
A 1 230 SER 230 227 227 SER SER A . n 
A 1 231 ILE 231 228 228 ILE ILE A . n 
A 1 232 GLY 232 229 229 GLY GLY A . n 
A 1 233 ASP 233 230 230 ASP ASP A . n 
A 1 234 GLY 234 231 231 GLY GLY A . n 
A 1 235 VAL 235 232 232 VAL VAL A . n 
A 1 236 THR 236 233 233 THR THR A . n 
A 1 237 ILE 237 234 234 ILE ILE A . n 
A 1 238 CYS 238 235 235 CYS CYS A . n 
A 1 239 ARG 239 236 236 ARG ARG A . n 
A 1 240 ARG 240 237 237 ARG ARG A . n 
A 1 241 LEU 241 238 238 LEU LEU A . n 
A 1 242 TYR 242 239 239 TYR TYR A . n 
B 1 1   GLY 1   -2  ?   ?   ?   B . n 
B 1 2   PRO 2   -1  ?   ?   ?   B . n 
B 1 3   GLY 3   0   ?   ?   ?   B . n 
B 1 4   MET 4   1   ?   ?   ?   B . n 
B 1 5   GLY 5   2   ?   ?   ?   B . n 
B 1 6   ALA 6   3   ?   ?   ?   B . n 
B 1 7   SER 7   4   ?   ?   ?   B . n 
B 1 8   ILE 8   5   ?   ?   ?   B . n 
B 1 9   ASP 9   6   6   ASP ASP B . n 
B 1 10  ASP 10  7   7   ASP ASP B . n 
B 1 11  TYR 11  8   8   TYR TYR B . n 
B 1 12  SER 12  9   9   SER SER B . n 
B 1 13  LEU 13  10  10  LEU LEU B . n 
B 1 14  VAL 14  11  11  VAL VAL B . n 
B 1 15  HIS 15  12  12  HIS HIS B . n 
B 1 16  LYS 16  13  13  LYS LYS B . n 
B 1 17  ASN 17  14  14  ASN ASN B . n 
B 1 18  ILE 18  15  15  ILE ILE B . n 
B 1 19  LEU 19  16  16  LEU LEU B . n 
B 1 20  HIS 20  17  17  HIS HIS B . n 
B 1 21  SER 21  18  18  SER SER B . n 
B 1 22  GLU 22  19  19  GLU GLU B . n 
B 1 23  ASP 23  20  20  ASP ASP B . n 
B 1 24  LEU 24  21  21  LEU LEU B . n 
B 1 25  LEU 25  22  22  LEU LEU B . n 
B 1 26  LYS 26  23  23  LYS LYS B . n 
B 1 27  TYR 27  24  24  TYR TYR B . n 
B 1 28  ILE 28  25  25  ILE ILE B . n 
B 1 29  LEU 29  26  26  LEU LEU B . n 
B 1 30  GLU 30  27  27  GLU GLU B . n 
B 1 31  THR 31  28  28  THR THR B . n 
B 1 32  SER 32  29  29  SER SER B . n 
B 1 33  ALA 33  30  30  ALA ALA B . n 
B 1 34  TYR 34  31  31  TYR TYR B . n 
B 1 35  PRO 35  32  32  PRO PRO B . n 
B 1 36  ARG 36  33  33  ARG ARG B . n 
B 1 37  GLU 37  34  34  GLU GLU B . n 
B 1 38  HIS 38  35  35  HIS HIS B . n 
B 1 39  GLU 39  36  36  GLU GLU B . n 
B 1 40  GLN 40  37  37  GLN GLN B . n 
B 1 41  LEU 41  38  38  LEU LEU B . n 
B 1 42  LYS 42  39  39  LYS LYS B . n 
B 1 43  GLY 43  40  40  GLY GLY B . n 
B 1 44  LEU 44  41  41  LEU LEU B . n 
B 1 45  ARG 45  42  42  ARG ARG B . n 
B 1 46  GLU 46  43  43  GLU GLU B . n 
B 1 47  VAL 47  44  44  VAL VAL B . n 
B 1 48  THR 48  45  45  THR THR B . n 
B 1 49  GLU 49  46  46  GLU GLU B . n 
B 1 50  LYS 50  47  47  LYS LYS B . n 
B 1 51  HIS 51  48  48  HIS HIS B . n 
B 1 52  GLU 52  49  49  GLU GLU B . n 
B 1 53  TRP 53  50  50  TRP TRP B . n 
B 1 54  SER 54  51  51  SER SER B . n 
B 1 55  THR 55  52  52  THR THR B . n 
B 1 56  ALA 56  53  53  ALA ALA B . n 
B 1 57  LEU 57  54  54  LEU LEU B . n 
B 1 58  VAL 58  55  55  VAL VAL B . n 
B 1 59  PRO 59  56  56  PRO PRO B . n 
B 1 60  ALA 60  57  57  ALA ALA B . n 
B 1 61  ASP 61  58  58  ASP ASP B . n 
B 1 62  GLU 62  59  59  GLU GLU B . n 
B 1 63  GLY 63  60  60  GLY GLY B . n 
B 1 64  LEU 64  61  61  LEU LEU B . n 
B 1 65  PHE 65  62  62  PHE PHE B . n 
B 1 66  LEU 66  63  63  LEU LEU B . n 
B 1 67  SER 67  64  64  SER SER B . n 
B 1 68  MET 68  65  65  MET MET B . n 
B 1 69  LEU 69  66  66  LEU LEU B . n 
B 1 70  LEU 70  67  67  LEU LEU B . n 
B 1 71  LYS 71  68  68  LYS LYS B . n 
B 1 72  LEU 72  69  69  LEU LEU B . n 
B 1 73  MET 73  70  70  MET MET B . n 
B 1 74  ASN 74  71  71  ASN ASN B . n 
B 1 75  ALA 75  72  72  ALA ALA B . n 
B 1 76  LYS 76  73  73  LYS LYS B . n 
B 1 77  ARG 77  74  74  ARG ARG B . n 
B 1 78  THR 78  75  75  THR THR B . n 
B 1 79  ILE 79  76  76  ILE ILE B . n 
B 1 80  GLU 80  77  77  GLU GLU B . n 
B 1 81  ILE 81  78  78  ILE ILE B . n 
B 1 82  GLY 82  79  79  GLY GLY B . n 
B 1 83  VAL 83  80  80  VAL VAL B . n 
B 1 84  TYR 84  81  81  TYR TYR B . n 
B 1 85  THR 85  82  82  THR THR B . n 
B 1 86  GLY 86  83  83  GLY GLY B . n 
B 1 87  TYR 87  84  84  TYR TYR B . n 
B 1 88  SER 88  85  85  SER SER B . n 
B 1 89  LEU 89  86  86  LEU LEU B . n 
B 1 90  LEU 90  87  87  LEU LEU B . n 
B 1 91  THR 91  88  88  THR THR B . n 
B 1 92  THR 92  89  89  THR THR B . n 
B 1 93  ALA 93  90  90  ALA ALA B . n 
B 1 94  LEU 94  91  91  LEU LEU B . n 
B 1 95  ALA 95  92  92  ALA ALA B . n 
B 1 96  LEU 96  93  93  LEU LEU B . n 
B 1 97  PRO 97  94  94  PRO PRO B . n 
B 1 98  GLU 98  95  95  GLU GLU B . n 
B 1 99  ASP 99  96  96  ASP ASP B . n 
B 1 100 GLY 100 97  97  GLY GLY B . n 
B 1 101 LYS 101 98  98  LYS LYS B . n 
B 1 102 ILE 102 99  99  ILE ILE B . n 
B 1 103 THR 103 100 100 THR THR B . n 
B 1 104 ALA 104 101 101 ALA ALA B . n 
B 1 105 ILE 105 102 102 ILE ILE B . n 
B 1 106 ASP 106 103 103 ASP ASP B . n 
B 1 107 VAL 107 104 104 VAL VAL B . n 
B 1 108 ASN 108 105 105 ASN ASN B . n 
B 1 109 LYS 109 106 106 LYS LYS B . n 
B 1 110 SER 110 107 107 SER SER B . n 
B 1 111 TYR 111 108 108 TYR TYR B . n 
B 1 112 TYR 112 109 109 TYR TYR B . n 
B 1 113 GLU 113 110 110 GLU GLU B . n 
B 1 114 ILE 114 111 111 ILE ILE B . n 
B 1 115 GLY 115 112 112 GLY GLY B . n 
B 1 116 LEU 116 113 113 LEU LEU B . n 
B 1 117 PRO 117 114 114 PRO PRO B . n 
B 1 118 PHE 118 115 115 PHE PHE B . n 
B 1 119 ILE 119 116 116 ILE ILE B . n 
B 1 120 GLN 120 117 117 GLN GLN B . n 
B 1 121 LYS 121 118 118 LYS LYS B . n 
B 1 122 ALA 122 119 119 ALA ALA B . n 
B 1 123 GLY 123 120 120 GLY GLY B . n 
B 1 124 VAL 124 121 121 VAL VAL B . n 
B 1 125 GLU 125 122 122 GLU GLU B . n 
B 1 126 HIS 126 123 123 HIS HIS B . n 
B 1 127 LYS 127 124 124 LYS LYS B . n 
B 1 128 ILE 128 125 125 ILE ILE B . n 
B 1 129 ASN 129 126 126 ASN ASN B . n 
B 1 130 PHE 130 127 127 PHE PHE B . n 
B 1 131 ILE 131 128 128 ILE ILE B . n 
B 1 132 GLU 132 129 129 GLU GLU B . n 
B 1 133 SER 133 130 130 SER SER B . n 
B 1 134 GLU 134 131 131 GLU GLU B . n 
B 1 135 ALA 135 132 132 ALA ALA B . n 
B 1 136 LEU 136 133 133 LEU LEU B . n 
B 1 137 PRO 137 134 134 PRO PRO B . n 
B 1 138 VAL 138 135 135 VAL VAL B . n 
B 1 139 LEU 139 136 136 LEU LEU B . n 
B 1 140 ASP 140 137 137 ASP ASP B . n 
B 1 141 GLN 141 138 138 GLN GLN B . n 
B 1 142 MET 142 139 139 MET MET B . n 
B 1 143 LEU 143 140 140 LEU LEU B . n 
B 1 144 GLU 144 141 141 GLU GLU B . n 
B 1 145 GLU 145 142 142 GLU GLU B . n 
B 1 146 MET 146 143 143 MET MET B . n 
B 1 147 LYS 147 144 144 LYS LYS B . n 
B 1 148 GLU 148 145 145 GLU GLU B . n 
B 1 149 GLU 149 146 146 GLU GLU B . n 
B 1 150 ASP 150 147 147 ASP ASP B . n 
B 1 151 LEU 151 148 148 LEU LEU B . n 
B 1 152 TYR 152 149 149 TYR TYR B . n 
B 1 153 ASP 153 150 150 ASP ASP B . n 
B 1 154 TYR 154 151 151 TYR TYR B . n 
B 1 155 ALA 155 152 152 ALA ALA B . n 
B 1 156 PHE 156 153 153 PHE PHE B . n 
B 1 157 VAL 157 154 154 VAL VAL B . n 
B 1 158 ASP 158 155 155 ASP ASP B . n 
B 1 159 ALA 159 156 156 ALA ALA B . n 
B 1 160 ASP 160 157 157 ASP ASP B . n 
B 1 161 LYS 161 158 158 LYS LYS B . n 
B 1 162 SER 162 159 159 SER SER B . n 
B 1 163 ASN 163 160 160 ASN ASN B . n 
B 1 164 TYR 164 161 161 TYR TYR B . n 
B 1 165 ALA 165 162 162 ALA ALA B . n 
B 1 166 ASN 166 163 163 ASN ASN B . n 
B 1 167 TYR 167 164 164 TYR TYR B . n 
B 1 168 HIS 168 165 165 HIS HIS B . n 
B 1 169 GLU 169 166 166 GLU GLU B . n 
B 1 170 ARG 170 167 167 ARG ARG B . n 
B 1 171 LEU 171 168 168 LEU LEU B . n 
B 1 172 VAL 172 169 169 VAL VAL B . n 
B 1 173 LYS 173 170 170 LYS LYS B . n 
B 1 174 LEU 174 171 171 LEU LEU B . n 
B 1 175 VAL 175 172 172 VAL VAL B . n 
B 1 176 ARG 176 173 173 ARG ARG B . n 
B 1 177 ILE 177 174 174 ILE ILE B . n 
B 1 178 GLY 178 175 175 GLY GLY B . n 
B 1 179 GLY 179 176 176 GLY GLY B . n 
B 1 180 ALA 180 177 177 ALA ALA B . n 
B 1 181 ILE 181 178 178 ILE ILE B . n 
B 1 182 LEU 182 179 179 LEU LEU B . n 
B 1 183 TYR 183 180 180 TYR TYR B . n 
B 1 184 ASP 184 181 181 ASP ASP B . n 
B 1 185 ASN 185 182 182 ASN ASN B . n 
B 1 186 THR 186 183 183 THR THR B . n 
B 1 187 LEU 187 184 184 LEU LEU B . n 
B 1 188 TRP 188 185 185 TRP TRP B . n 
B 1 189 PHE 189 186 186 PHE PHE B . n 
B 1 190 GLY 190 187 187 GLY GLY B . n 
B 1 191 SER 191 188 188 SER SER B . n 
B 1 192 VAL 192 189 189 VAL VAL B . n 
B 1 193 ALA 193 190 190 ALA ALA B . n 
B 1 194 TYR 194 191 191 TYR TYR B . n 
B 1 195 PRO 195 192 192 PRO PRO B . n 
B 1 196 GLU 196 193 193 GLU GLU B . n 
B 1 197 TYR 197 194 194 TYR TYR B . n 
B 1 198 PRO 198 195 195 PRO PRO B . n 
B 1 199 GLY 199 196 196 GLY GLY B . n 
B 1 200 LEU 200 197 197 LEU LEU B . n 
B 1 201 HIS 201 198 198 HIS HIS B . n 
B 1 202 PRO 202 199 199 PRO PRO B . n 
B 1 203 GLU 203 200 200 GLU GLU B . n 
B 1 204 GLU 204 201 201 GLU GLU B . n 
B 1 205 GLU 205 202 202 GLU GLU B . n 
B 1 206 VAL 206 203 203 VAL VAL B . n 
B 1 207 ALA 207 204 204 ALA ALA B . n 
B 1 208 ARG 208 205 205 ARG ARG B . n 
B 1 209 LEU 209 206 206 LEU LEU B . n 
B 1 210 SER 210 207 207 SER SER B . n 
B 1 211 PHE 211 208 208 PHE PHE B . n 
B 1 212 ARG 212 209 209 ARG ARG B . n 
B 1 213 ASN 213 210 210 ASN ASN B . n 
B 1 214 LEU 214 211 211 LEU LEU B . n 
B 1 215 ASN 215 212 212 ASN ASN B . n 
B 1 216 THR 216 213 213 THR THR B . n 
B 1 217 PHE 217 214 214 PHE PHE B . n 
B 1 218 LEU 218 215 215 LEU LEU B . n 
B 1 219 ALA 219 216 216 ALA ALA B . n 
B 1 220 ALA 220 217 217 ALA ALA B . n 
B 1 221 ASP 221 218 218 ASP ASP B . n 
B 1 222 PRO 222 219 219 PRO PRO B . n 
B 1 223 ARG 223 220 220 ARG ARG B . n 
B 1 224 VAL 224 221 221 VAL VAL B . n 
B 1 225 GLU 225 222 222 GLU GLU B . n 
B 1 226 ILE 226 223 223 ILE ILE B . n 
B 1 227 SER 227 224 224 SER SER B . n 
B 1 228 GLN 228 225 225 GLN GLN B . n 
B 1 229 VAL 229 226 226 VAL VAL B . n 
B 1 230 SER 230 227 227 SER SER B . n 
B 1 231 ILE 231 228 228 ILE ILE B . n 
B 1 232 GLY 232 229 229 GLY GLY B . n 
B 1 233 ASP 233 230 230 ASP ASP B . n 
B 1 234 GLY 234 231 231 GLY GLY B . n 
B 1 235 VAL 235 232 232 VAL VAL B . n 
B 1 236 THR 236 233 233 THR THR B . n 
B 1 237 ILE 237 234 234 ILE ILE B . n 
B 1 238 CYS 238 235 235 CYS CYS B . n 
B 1 239 ARG 239 236 236 ARG ARG B . n 
B 1 240 ARG 240 237 237 ARG ARG B . n 
B 1 241 LEU 241 238 238 LEU LEU B . n 
B 1 242 TYR 242 239 239 TYR TYR B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 GOL   ? ? GOL   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 A1LU2 ? ? A1LU2 ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG    ? ? MG    ? ? 'SUBJECT OF INVESTIGATION' ? 
4 SAH   ? ? SAH   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 GOL   1  501 501 GOL   GOL A . 
D 3 MG    1  502 301 MG    MG  A . 
E 4 SAH   1  503 401 SAH   SAH A . 
F 2 GOL   1  504 601 GOL   GOL A . 
G 5 A1LU2 1  701 701 A1LU2 LIG B . 
H 3 MG    1  702 301 MG    MG  B . 
I 4 SAH   1  703 401 SAH   SAH B . 
J 6 HOH   1  601 91  HOH   HOH A . 
J 6 HOH   2  602 47  HOH   HOH A . 
J 6 HOH   3  603 4   HOH   HOH A . 
J 6 HOH   4  604 50  HOH   HOH A . 
J 6 HOH   5  605 90  HOH   HOH A . 
J 6 HOH   6  606 53  HOH   HOH A . 
J 6 HOH   7  607 109 HOH   HOH A . 
J 6 HOH   8  608 46  HOH   HOH A . 
J 6 HOH   9  609 117 HOH   HOH A . 
J 6 HOH   10 610 3   HOH   HOH A . 
J 6 HOH   11 611 108 HOH   HOH A . 
J 6 HOH   12 612 10  HOH   HOH A . 
J 6 HOH   13 613 16  HOH   HOH A . 
J 6 HOH   14 614 84  HOH   HOH A . 
J 6 HOH   15 615 104 HOH   HOH A . 
J 6 HOH   16 616 20  HOH   HOH A . 
J 6 HOH   17 617 49  HOH   HOH A . 
J 6 HOH   18 618 39  HOH   HOH A . 
J 6 HOH   19 619 78  HOH   HOH A . 
J 6 HOH   20 620 56  HOH   HOH A . 
J 6 HOH   21 621 35  HOH   HOH A . 
J 6 HOH   22 622 116 HOH   HOH A . 
J 6 HOH   23 623 60  HOH   HOH A . 
J 6 HOH   24 624 1   HOH   HOH A . 
J 6 HOH   25 625 9   HOH   HOH A . 
J 6 HOH   26 626 44  HOH   HOH A . 
J 6 HOH   27 627 17  HOH   HOH A . 
J 6 HOH   28 628 18  HOH   HOH A . 
J 6 HOH   29 629 8   HOH   HOH A . 
J 6 HOH   30 630 26  HOH   HOH A . 
J 6 HOH   31 631 37  HOH   HOH A . 
J 6 HOH   32 632 29  HOH   HOH A . 
J 6 HOH   33 633 63  HOH   HOH A . 
J 6 HOH   34 634 28  HOH   HOH A . 
J 6 HOH   35 635 34  HOH   HOH A . 
J 6 HOH   36 636 2   HOH   HOH A . 
J 6 HOH   37 637 72  HOH   HOH A . 
J 6 HOH   38 638 80  HOH   HOH A . 
J 6 HOH   39 639 100 HOH   HOH A . 
J 6 HOH   40 640 42  HOH   HOH A . 
J 6 HOH   41 641 74  HOH   HOH A . 
J 6 HOH   42 642 83  HOH   HOH A . 
J 6 HOH   43 643 59  HOH   HOH A . 
J 6 HOH   44 644 86  HOH   HOH A . 
J 6 HOH   45 645 41  HOH   HOH A . 
J 6 HOH   46 646 85  HOH   HOH A . 
J 6 HOH   47 647 101 HOH   HOH A . 
J 6 HOH   48 648 15  HOH   HOH A . 
J 6 HOH   49 649 52  HOH   HOH A . 
J 6 HOH   50 650 76  HOH   HOH A . 
J 6 HOH   51 651 120 HOH   HOH A . 
J 6 HOH   52 652 51  HOH   HOH A . 
J 6 HOH   53 653 122 HOH   HOH A . 
J 6 HOH   54 654 127 HOH   HOH A . 
J 6 HOH   55 655 87  HOH   HOH A . 
J 6 HOH   56 656 113 HOH   HOH A . 
J 6 HOH   57 657 111 HOH   HOH A . 
J 6 HOH   58 658 58  HOH   HOH A . 
J 6 HOH   59 659 115 HOH   HOH A . 
J 6 HOH   60 660 102 HOH   HOH A . 
J 6 HOH   61 661 68  HOH   HOH A . 
J 6 HOH   62 662 118 HOH   HOH A . 
J 6 HOH   63 663 123 HOH   HOH A . 
J 6 HOH   64 664 119 HOH   HOH A . 
J 6 HOH   65 665 107 HOH   HOH A . 
J 6 HOH   66 666 110 HOH   HOH A . 
K 6 HOH   1  801 55  HOH   HOH B . 
K 6 HOH   2  802 132 HOH   HOH B . 
K 6 HOH   3  803 112 HOH   HOH B . 
K 6 HOH   4  804 22  HOH   HOH B . 
K 6 HOH   5  805 32  HOH   HOH B . 
K 6 HOH   6  806 40  HOH   HOH B . 
K 6 HOH   7  807 5   HOH   HOH B . 
K 6 HOH   8  808 11  HOH   HOH B . 
K 6 HOH   9  809 38  HOH   HOH B . 
K 6 HOH   10 810 12  HOH   HOH B . 
K 6 HOH   11 811 54  HOH   HOH B . 
K 6 HOH   12 812 81  HOH   HOH B . 
K 6 HOH   13 813 65  HOH   HOH B . 
K 6 HOH   14 814 64  HOH   HOH B . 
K 6 HOH   15 815 27  HOH   HOH B . 
K 6 HOH   16 816 24  HOH   HOH B . 
K 6 HOH   17 817 30  HOH   HOH B . 
K 6 HOH   18 818 7   HOH   HOH B . 
K 6 HOH   19 819 19  HOH   HOH B . 
K 6 HOH   20 820 13  HOH   HOH B . 
K 6 HOH   21 821 71  HOH   HOH B . 
K 6 HOH   22 822 95  HOH   HOH B . 
K 6 HOH   23 823 96  HOH   HOH B . 
K 6 HOH   24 824 61  HOH   HOH B . 
K 6 HOH   25 825 126 HOH   HOH B . 
K 6 HOH   26 826 99  HOH   HOH B . 
K 6 HOH   27 827 66  HOH   HOH B . 
K 6 HOH   28 828 69  HOH   HOH B . 
K 6 HOH   29 829 88  HOH   HOH B . 
K 6 HOH   30 830 106 HOH   HOH B . 
K 6 HOH   31 831 89  HOH   HOH B . 
K 6 HOH   32 832 6   HOH   HOH B . 
K 6 HOH   33 833 21  HOH   HOH B . 
K 6 HOH   34 834 25  HOH   HOH B . 
K 6 HOH   35 835 31  HOH   HOH B . 
K 6 HOH   36 836 75  HOH   HOH B . 
K 6 HOH   37 837 33  HOH   HOH B . 
K 6 HOH   38 838 93  HOH   HOH B . 
K 6 HOH   39 839 45  HOH   HOH B . 
K 6 HOH   40 840 57  HOH   HOH B . 
K 6 HOH   41 841 23  HOH   HOH B . 
K 6 HOH   42 842 43  HOH   HOH B . 
K 6 HOH   43 843 98  HOH   HOH B . 
K 6 HOH   44 844 36  HOH   HOH B . 
K 6 HOH   45 845 82  HOH   HOH B . 
K 6 HOH   46 846 131 HOH   HOH B . 
K 6 HOH   47 847 73  HOH   HOH B . 
K 6 HOH   48 848 134 HOH   HOH B . 
K 6 HOH   49 849 70  HOH   HOH B . 
K 6 HOH   50 850 105 HOH   HOH B . 
K 6 HOH   51 851 133 HOH   HOH B . 
K 6 HOH   52 852 67  HOH   HOH B . 
K 6 HOH   53 853 14  HOH   HOH B . 
K 6 HOH   54 854 77  HOH   HOH B . 
K 6 HOH   55 855 79  HOH   HOH B . 
K 6 HOH   56 856 94  HOH   HOH B . 
K 6 HOH   57 857 130 HOH   HOH B . 
K 6 HOH   58 858 125 HOH   HOH B . 
K 6 HOH   59 859 129 HOH   HOH B . 
K 6 HOH   60 860 124 HOH   HOH B . 
K 6 HOH   61 861 128 HOH   HOH B . 
K 6 HOH   62 862 103 HOH   HOH B . 
K 6 HOH   63 863 114 HOH   HOH B . 
K 6 HOH   64 864 92  HOH   HOH B . 
K 6 HOH   65 865 121 HOH   HOH B . 
K 6 HOH   66 866 48  HOH   HOH B . 
K 6 HOH   67 867 97  HOH   HOH B . 
K 6 HOH   68 868 62  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASP 6   ? CG  ? A ASP 9   CG  
2  1 Y 1 A ASP 6   ? OD1 ? A ASP 9   OD1 
3  1 Y 1 A ASP 6   ? OD2 ? A ASP 9   OD2 
4  1 Y 1 A LYS 73  ? CD  ? A LYS 76  CD  
5  1 Y 1 A LYS 73  ? CE  ? A LYS 76  CE  
6  1 Y 1 A LYS 73  ? NZ  ? A LYS 76  NZ  
7  1 Y 1 A LYS 144 ? CD  ? A LYS 147 CD  
8  1 Y 1 A LYS 144 ? CE  ? A LYS 147 CE  
9  1 Y 1 A LYS 144 ? NZ  ? A LYS 147 NZ  
10 1 Y 1 A GLU 146 ? CG  ? A GLU 149 CG  
11 1 Y 1 A GLU 146 ? CD  ? A GLU 149 CD  
12 1 Y 1 A GLU 146 ? OE1 ? A GLU 149 OE1 
13 1 Y 1 A GLU 146 ? OE2 ? A GLU 149 OE2 
14 1 Y 1 A LYS 170 ? CE  ? A LYS 173 CE  
15 1 Y 1 A LYS 170 ? NZ  ? A LYS 173 NZ  
16 1 Y 1 B ASP 6   ? CG  ? B ASP 9   CG  
17 1 Y 1 B ASP 6   ? OD1 ? B ASP 9   OD1 
18 1 Y 1 B ASP 6   ? OD2 ? B ASP 9   OD2 
19 1 Y 1 B LYS 23  ? CE  ? B LYS 26  CE  
20 1 Y 1 B LYS 23  ? NZ  ? B LYS 26  NZ  
21 1 Y 1 B GLU 36  ? CD  ? B GLU 39  CD  
22 1 Y 1 B GLU 36  ? OE1 ? B GLU 39  OE1 
23 1 Y 1 B GLU 36  ? OE2 ? B GLU 39  OE2 
24 1 Y 1 B LYS 47  ? CE  ? B LYS 50  CE  
25 1 Y 1 B LYS 47  ? NZ  ? B LYS 50  NZ  
26 1 Y 1 B GLU 95  ? CD  ? B GLU 98  CD  
27 1 Y 1 B GLU 95  ? OE1 ? B GLU 98  OE1 
28 1 Y 1 B GLU 95  ? OE2 ? B GLU 98  OE2 
29 1 Y 1 B LYS 98  ? CE  ? B LYS 101 CE  
30 1 Y 1 B LYS 98  ? NZ  ? B LYS 101 NZ  
31 1 Y 1 B LYS 106 ? CE  ? B LYS 109 CE  
32 1 Y 1 B LYS 106 ? NZ  ? B LYS 109 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.17.1_3660 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z8T 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     80.501 
_cell.length_a_esd                 ? 
_cell.length_b                     116.587 
_cell.length_b_esd                 ? 
_cell.length_c                     50.297 
_cell.length_c_esd                 ? 
_cell.volume                       472055.959 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Z8T 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z8T 
_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             2.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.89 
_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              9.0 
_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    '12% (w/v) PEG 8000, 0.2M MgCl2, 0.1M Tris-HCl (pH 9.0)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.03500 
_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                        'PHOTON FACTORY BEAMLINE BL-1A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03500 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL-1A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.B_iso_Wilson_estimate                          38.73 
_reflns.entry_id                                       8Z8T 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.18 
_reflns.d_resolution_low                               47.21 
_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                                     47597 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.0 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.088 
_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                                    2.18 
_reflns_shell.d_res_low                                     2.25 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2153 
_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                               8.6 
_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                                  0.758 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.943 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.39 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Z8T 
_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                            2.18 
_refine.ls_d_res_low                             47.21 
_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                     47597 
_refine.ls_number_reflns_R_free                  3735 
_refine.ls_number_reflns_R_work                  43862 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.79 
_refine.ls_percent_reflns_R_free                 7.85 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1808 
_refine.ls_R_factor_R_free                       0.2099 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1782 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 22.5284 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2430 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.18 
_refine_hist.d_res_low                        47.21 
_refine_hist.number_atoms_solvent             134 
_refine_hist.number_atoms_total               3957 
_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        3792 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_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' ? 0.0027  ? 3964 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5758  ? 5396 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0442  ? 603  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0035  ? 687  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 23.6751 ? 1463 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.18 2.21  . . 136 1599 100.00 . . . . 0.3069 . . . . . . . . . . . 0.3593 
'X-RAY DIFFRACTION' 2.21 2.24  . . 137 1628 99.94  . . . . 0.2888 . . . . . . . . . . . 0.3014 
'X-RAY DIFFRACTION' 2.24 2.27  . . 137 1612 100.00 . . . . 0.2863 . . . . . . . . . . . 0.3570 
'X-RAY DIFFRACTION' 2.27 2.30  . . 142 1676 100.00 . . . . 0.2535 . . . . . . . . . . . 0.2823 
'X-RAY DIFFRACTION' 2.30 2.33  . . 138 1572 99.82  . . . . 0.2411 . . . . . . . . . . . 0.2776 
'X-RAY DIFFRACTION' 2.33 2.37  . . 142 1672 99.89  . . . . 0.2414 . . . . . . . . . . . 0.2848 
'X-RAY DIFFRACTION' 2.37 2.41  . . 139 1610 100.00 . . . . 0.2362 . . . . . . . . . . . 0.2390 
'X-RAY DIFFRACTION' 2.41 2.45  . . 139 1609 99.94  . . . . 0.2273 . . . . . . . . . . . 0.2652 
'X-RAY DIFFRACTION' 2.45 2.50  . . 145 1654 99.89  . . . . 0.2185 . . . . . . . . . . . 0.2709 
'X-RAY DIFFRACTION' 2.50 2.54  . . 138 1625 100.00 . . . . 0.2214 . . . . . . . . . . . 0.2747 
'X-RAY DIFFRACTION' 2.54 2.60  . . 134 1629 99.94  . . . . 0.2078 . . . . . . . . . . . 0.2509 
'X-RAY DIFFRACTION' 2.60 2.65  . . 136 1649 99.94  . . . . 0.2102 . . . . . . . . . . . 0.2600 
'X-RAY DIFFRACTION' 2.65 2.71  . . 135 1591 99.83  . . . . 0.1902 . . . . . . . . . . . 0.2273 
'X-RAY DIFFRACTION' 2.71 2.78  . . 143 1644 99.50  . . . . 0.2014 . . . . . . . . . . . 0.2298 
'X-RAY DIFFRACTION' 2.78 2.86  . . 135 1600 99.43  . . . . 0.2052 . . . . . . . . . . . 0.2341 
'X-RAY DIFFRACTION' 2.86 2.94  . . 139 1622 99.38  . . . . 0.2025 . . . . . . . . . . . 0.2274 
'X-RAY DIFFRACTION' 2.94 3.04  . . 136 1596 98.63  . . . . 0.1887 . . . . . . . . . . . 0.2375 
'X-RAY DIFFRACTION' 3.04 3.14  . . 143 1652 98.95  . . . . 0.2001 . . . . . . . . . . . 0.2370 
'X-RAY DIFFRACTION' 3.14 3.27  . . 139 1591 99.71  . . . . 0.1834 . . . . . . . . . . . 0.1955 
'X-RAY DIFFRACTION' 3.27 3.42  . . 135 1642 100.00 . . . . 0.1637 . . . . . . . . . . . 0.1880 
'X-RAY DIFFRACTION' 3.42 3.60  . . 135 1619 100.00 . . . . 0.1688 . . . . . . . . . . . 0.1948 
'X-RAY DIFFRACTION' 3.60 3.82  . . 144 1619 100.00 . . . . 0.1540 . . . . . . . . . . . 0.2205 
'X-RAY DIFFRACTION' 3.82 4.12  . . 130 1641 100.00 . . . . 0.1448 . . . . . . . . . . . 0.1864 
'X-RAY DIFFRACTION' 4.12 4.53  . . 142 1636 100.00 . . . . 0.1273 . . . . . . . . . . . 0.1665 
'X-RAY DIFFRACTION' 4.53 5.19  . . 140 1602 100.00 . . . . 0.1449 . . . . . . . . . . . 0.1617 
'X-RAY DIFFRACTION' 5.19 6.53  . . 138 1638 100.00 . . . . 0.1705 . . . . . . . . . . . 0.2143 
'X-RAY DIFFRACTION' 6.54 47.21 . . 138 1634 99.66  . . . . 0.1492 . . . . . . . . . . . 0.1434 
# 
_struct.entry_id                     8Z8T 
_struct.title                        
;norbelladine 4'-O-methyltransferase S52T Y186F complexed with Mg and SAH
;
_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        8Z8T 
_struct_keywords.text            'O-methyltransferase family protein, NpN4OMT, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 5 ? 
H N N 3 ? 
I N N 4 ? 
J N N 6 ? 
K N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NOMT_NARAP 
_struct_ref.pdbx_db_accession          A0A077EWA5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MGASIDDYSLVHKNILHSEDLLKYILETSAYPREHEQLKGLREVTEKHEWSSALVPADEGLFLSMLLKLMNAKRTIEIGV
YTGYSLLTTALALPEDGKITAIDVNKSYYEIGLPFIQKAGVEHKINFIESEALPVLDQMLEEMKEEDLYDYAFVDADKSN
YANYHERLVKLVRIGGAILYDNTLWYGSVAYPEYPGLHPEEEVARLSFRNLNTFLAADPRVEISQVSIGDGVTICRRLY
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8Z8T A 4 ? 242 ? A0A077EWA5 1 ? 239 ? 1 239 
2 1 8Z8T B 4 ? 242 ? A0A077EWA5 1 ? 239 ? 1 239 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8Z8T GLY A 1   ? UNP A0A077EWA5 ?   ?   'expression tag'      -2  1  
1 8Z8T PRO A 2   ? UNP A0A077EWA5 ?   ?   'expression tag'      -1  2  
1 8Z8T GLY A 3   ? UNP A0A077EWA5 ?   ?   'expression tag'      0   3  
1 8Z8T THR A 55  ? UNP A0A077EWA5 SER 52  'engineered mutation' 52  4  
1 8Z8T PHE A 189 ? UNP A0A077EWA5 TYR 186 'engineered mutation' 186 5  
2 8Z8T GLY B 1   ? UNP A0A077EWA5 ?   ?   'expression tag'      -2  6  
2 8Z8T PRO B 2   ? UNP A0A077EWA5 ?   ?   'expression tag'      -1  7  
2 8Z8T GLY B 3   ? UNP A0A077EWA5 ?   ?   'expression tag'      0   8  
2 8Z8T THR B 55  ? UNP A0A077EWA5 SER 52  'engineered mutation' 52  9  
2 8Z8T PHE B 189 ? UNP A0A077EWA5 TYR 186 'engineered mutation' 186 10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4660  ? 
1 MORE         -33   ? 
1 'SSA (A^2)'  18240 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 21  ? ALA A 33  ? SER A 18  ALA A 30  1 ? 13 
HELX_P HELX_P2  AA2 TYR A 34  ? GLU A 37  ? TYR A 31  GLU A 34  5 ? 4  
HELX_P HELX_P3  AA3 HIS A 38  ? LYS A 50  ? HIS A 35  LYS A 47  1 ? 13 
HELX_P HELX_P4  AA4 TRP A 53  ? LEU A 57  ? TRP A 50  LEU A 54  5 ? 5  
HELX_P HELX_P5  AA5 PRO A 59  ? MET A 73  ? PRO A 56  MET A 70  1 ? 15 
HELX_P HELX_P6  AA6 GLY A 86  ? LEU A 96  ? GLY A 83  LEU A 93  1 ? 11 
HELX_P HELX_P7  AA7 ASN A 108 ? ALA A 122 ? ASN A 105 ALA A 119 1 ? 15 
HELX_P HELX_P8  AA8 VAL A 124 ? HIS A 126 ? VAL A 121 HIS A 123 5 ? 3  
HELX_P HELX_P9  AA9 GLU A 134 ? MET A 146 ? GLU A 131 MET A 143 1 ? 13 
HELX_P HELX_P10 AB1 LYS A 147 ? LEU A 151 ? LYS A 144 LEU A 148 5 ? 5  
HELX_P HELX_P11 AB2 ASP A 160 ? SER A 162 ? ASP A 157 SER A 159 5 ? 3  
HELX_P HELX_P12 AB3 ASN A 163 ? LEU A 174 ? ASN A 160 LEU A 171 1 ? 12 
HELX_P HELX_P13 AB4 LEU A 187 ? TYR A 194 ? LEU A 184 TYR A 191 5 ? 8  
HELX_P HELX_P14 AB5 HIS A 201 ? ASP A 221 ? HIS A 198 ASP A 218 1 ? 21 
HELX_P HELX_P15 AB6 SER B 21  ? SER B 32  ? SER B 18  SER B 29  1 ? 12 
HELX_P HELX_P16 AB7 ALA B 33  ? GLU B 37  ? ALA B 30  GLU B 34  5 ? 5  
HELX_P HELX_P17 AB8 HIS B 38  ? GLU B 49  ? HIS B 35  GLU B 46  1 ? 12 
HELX_P HELX_P18 AB9 TRP B 53  ? LEU B 57  ? TRP B 50  LEU B 54  5 ? 5  
HELX_P HELX_P19 AC1 PRO B 59  ? MET B 73  ? PRO B 56  MET B 70  1 ? 15 
HELX_P HELX_P20 AC2 GLY B 86  ? LEU B 96  ? GLY B 83  LEU B 93  1 ? 11 
HELX_P HELX_P21 AC3 ASN B 108 ? ALA B 122 ? ASN B 105 ALA B 119 1 ? 15 
HELX_P HELX_P22 AC4 VAL B 124 ? HIS B 126 ? VAL B 121 HIS B 123 5 ? 3  
HELX_P HELX_P23 AC5 GLU B 134 ? MET B 146 ? GLU B 131 MET B 143 1 ? 13 
HELX_P HELX_P24 AC6 LYS B 147 ? LEU B 151 ? LYS B 144 LEU B 148 5 ? 5  
HELX_P HELX_P25 AC7 ASP B 160 ? SER B 162 ? ASP B 157 SER B 159 5 ? 3  
HELX_P HELX_P26 AC8 ASN B 163 ? LEU B 174 ? ASN B 160 LEU B 171 1 ? 12 
HELX_P HELX_P27 AC9 LEU B 187 ? TYR B 194 ? LEU B 184 TYR B 191 5 ? 8  
HELX_P HELX_P28 AD1 HIS B 201 ? ASP B 221 ? HIS B 198 ASP B 218 1 ? 21 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP   158 OD1 ? ? ? 1_555 D MG  . MG ? ? A ASP   155 A MG  502 1_555 ? ? ? ? ? ? ? 2.148 ? ? 
metalc2  metalc ? ? A ASP   158 OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP   155 A MG  502 1_555 ? ? ? ? ? ? ? 2.895 ? ? 
metalc3  metalc ? ? A ASP   184 OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP   181 A MG  502 1_555 ? ? ? ? ? ? ? 1.941 ? ? 
metalc4  metalc ? ? A ASN   185 OD1 ? ? ? 1_555 D MG  . MG ? ? A ASN   182 A MG  502 1_555 ? ? ? ? ? ? ? 2.145 ? ? 
metalc5  metalc ? ? D MG    .   MG  ? ? ? 1_555 J HOH . O  ? ? A MG    502 A HOH 603 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc6  metalc ? ? D MG    .   MG  ? ? ? 1_555 J HOH . O  ? ? A MG    502 A HOH 609 1_555 ? ? ? ? ? ? ? 2.162 ? ? 
metalc7  metalc ? ? D MG    .   MG  ? ? ? 1_555 J HOH . O  ? ? A MG    502 A HOH 622 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc8  metalc ? ? B ASP   158 OD1 ? ? ? 1_555 H MG  . MG ? ? B ASP   155 B MG  702 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc9  metalc ? ? B ASP   158 OD2 ? ? ? 1_555 H MG  . MG ? ? B ASP   155 B MG  702 1_555 ? ? ? ? ? ? ? 2.859 ? ? 
metalc10 metalc ? ? B ASP   184 OD2 ? ? ? 1_555 H MG  . MG ? ? B ASP   181 B MG  702 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc11 metalc ? ? B ASN   185 OD1 ? ? ? 1_555 H MG  . MG ? ? B ASN   182 B MG  702 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
metalc12 metalc ? ? G A1LU2 .   O15 ? ? ? 1_555 H MG  . MG ? ? B A1LU2 701 B MG  702 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc13 metalc ? ? G A1LU2 .   O17 ? ? ? 1_555 H MG  . MG ? ? B A1LU2 701 B MG  702 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc14 metalc ? ? H MG    .   MG  ? ? ? 1_555 K HOH . O  ? ? B MG    702 B HOH 803 1_555 ? ? ? ? ? ? ? 2.220 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 OD2 ? A ASP   158 ? A ASP   155 ? 1_555 48.9  ? 
2  OD1 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 OD2 ? A ASP   184 ? A ASP   181 ? 1_555 90.5  ? 
3  OD2 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 OD2 ? A ASP   184 ? A ASP   181 ? 1_555 80.1  ? 
4  OD1 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 OD1 ? A ASN   185 ? A ASN   182 ? 1_555 89.2  ? 
5  OD2 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 OD1 ? A ASN   185 ? A ASN   182 ? 1_555 135.3 ? 
6  OD2 ? A ASP   184 ? A ASP   181 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 OD1 ? A ASN   185 ? A ASN   182 ? 1_555 86.4  ? 
7  OD1 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   603 ? 1_555 107.2 ? 
8  OD2 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   603 ? 1_555 60.5  ? 
9  OD2 ? A ASP   184 ? A ASP   181 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   603 ? 1_555 93.2  ? 
10 OD1 ? A ASN   185 ? A ASN   182 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   603 ? 1_555 163.6 ? 
11 OD1 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   609 ? 1_555 149.3 ? 
12 OD2 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   609 ? 1_555 135.3 ? 
13 OD2 ? A ASP   184 ? A ASP   181 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   609 ? 1_555 119.8 ? 
14 OD1 ? A ASN   185 ? A ASN   182 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   609 ? 1_555 88.2  ? 
15 O   ? J HOH   .   ? A HOH   603 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   609 ? 1_555 77.8  ? 
16 OD1 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   622 ? 1_555 80.9  ? 
17 OD2 ? A ASP   158 ? A ASP   155 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   622 ? 1_555 97.9  ? 
18 OD2 ? A ASP   184 ? A ASP   181 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   622 ? 1_555 169.8 ? 
19 OD1 ? A ASN   185 ? A ASN   182 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   622 ? 1_555 88.1  ? 
20 O   ? J HOH   .   ? A HOH   603 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   622 ? 1_555 94.5  ? 
21 O   ? J HOH   .   ? A HOH   609 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O   ? J HOH   .   ? A HOH   622 ? 1_555 68.5  ? 
22 OD1 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 OD2 ? B ASP   158 ? B ASP   155 ? 1_555 49.5  ? 
23 OD1 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 OD2 ? B ASP   184 ? B ASP   181 ? 1_555 90.6  ? 
24 OD2 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 OD2 ? B ASP   184 ? B ASP   181 ? 1_555 82.9  ? 
25 OD1 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 OD1 ? B ASN   185 ? B ASN   182 ? 1_555 87.6  ? 
26 OD2 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 OD1 ? B ASN   185 ? B ASN   182 ? 1_555 136.1 ? 
27 OD2 ? B ASP   184 ? B ASP   181 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 OD1 ? B ASN   185 ? B ASN   182 ? 1_555 90.1  ? 
28 OD1 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O15 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 81.0  ? 
29 OD2 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O15 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 93.1  ? 
30 OD2 ? B ASP   184 ? B ASP   181 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O15 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 171.4 ? 
31 OD1 ? B ASN   185 ? B ASN   182 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O15 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 87.7  ? 
32 OD1 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O17 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 158.7 ? 
33 OD2 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O17 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 135.8 ? 
34 OD2 ? B ASP   184 ? B ASP   181 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O17 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 110.1 ? 
35 OD1 ? B ASN   185 ? B ASN   182 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O17 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 87.2  ? 
36 O15 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O17 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 78.1  ? 
37 OD1 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O   ? K HOH   .   ? B HOH   803 ? 1_555 105.7 ? 
38 OD2 ? B ASP   158 ? B ASP   155 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O   ? K HOH   .   ? B HOH   803 ? 1_555 59.0  ? 
39 OD2 ? B ASP   184 ? B ASP   181 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O   ? K HOH   .   ? B HOH   803 ? 1_555 98.9  ? 
40 OD1 ? B ASN   185 ? B ASN   182 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O   ? K HOH   .   ? B HOH   803 ? 1_555 163.8 ? 
41 O15 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O   ? K HOH   .   ? B HOH   803 ? 1_555 85.3  ? 
42 O17 ? G A1LU2 .   ? B A1LU2 701 ? 1_555 MG ? H MG . ? B MG 702 ? 1_555 O   ? K HOH   .   ? B HOH   803 ? 1_555 77.0  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA2 6 7 ? 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 ILE A 128 ? GLU A 132 ? ILE A 125 GLU A 129 
AA1 2 LYS A 101 ? ASP A 106 ? LYS A 98  ASP A 103 
AA1 3 ARG A 77  ? ILE A 81  ? ARG A 74  ILE A 78  
AA1 4 TYR A 152 ? VAL A 157 ? TYR A 149 VAL A 154 
AA1 5 VAL A 175 ? ASP A 184 ? VAL A 172 ASP A 181 
AA1 6 VAL A 235 ? ARG A 240 ? VAL A 232 ARG A 237 
AA1 7 VAL A 224 ? VAL A 229 ? VAL A 221 VAL A 226 
AA2 1 ILE B 128 ? GLU B 132 ? ILE B 125 GLU B 129 
AA2 2 LYS B 101 ? ASP B 106 ? LYS B 98  ASP B 103 
AA2 3 ARG B 77  ? ILE B 81  ? ARG B 74  ILE B 78  
AA2 4 TYR B 152 ? VAL B 157 ? TYR B 149 VAL B 154 
AA2 5 VAL B 175 ? ASP B 184 ? VAL B 172 ASP B 181 
AA2 6 VAL B 235 ? ARG B 240 ? VAL B 232 ARG B 237 
AA2 7 VAL B 224 ? VAL B 229 ? VAL B 221 VAL B 226 
# 
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 O ILE A 131 ? O ILE A 128 N ALA A 104 ? N ALA A 101 
AA1 2 3 O THR A 103 ? O THR A 100 N GLU A 80  ? N GLU A 77  
AA1 3 4 N ARG A 77  ? N ARG A 74  O ASP A 153 ? O ASP A 150 
AA1 4 5 N ALA A 155 ? N ALA A 152 O LEU A 182 ? O LEU A 179 
AA1 5 6 N ILE A 181 ? N ILE A 178 O CYS A 238 ? O CYS A 235 
AA1 6 7 O VAL A 235 ? O VAL A 232 N VAL A 229 ? N VAL A 226 
AA2 1 2 O ILE B 131 ? O ILE B 128 N ALA B 104 ? N ALA B 101 
AA2 2 3 O THR B 103 ? O THR B 100 N GLU B 80  ? N GLU B 77  
AA2 3 4 N ILE B 81  ? N ILE B 78  O PHE B 156 ? O PHE B 153 
AA2 4 5 N VAL B 157 ? N VAL B 154 O LEU B 182 ? O LEU B 179 
AA2 5 6 N ILE B 181 ? N ILE B 178 O CYS B 238 ? O CYS B 235 
AA2 6 7 O VAL B 235 ? O VAL B 232 N VAL B 229 ? N VAL B 226 
# 
_pdbx_entry_details.entry_id                   8Z8T 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 30  ? ? -100.21 -64.23  
2  1 TYR A 81  ? ? 60.18   -128.98 
3  1 ASP A 155 ? ? -150.55 43.57   
4  1 ALA A 156 ? ? -112.70 -128.69 
5  1 PHE A 186 ? ? 59.40   18.99   
6  1 ALA B 30  ? ? -91.15  -62.85  
7  1 TRP B 50  ? ? -98.20  33.62   
8  1 TYR B 81  ? ? 60.74   -131.80 
9  1 ASP B 155 ? ? -153.34 42.60   
10 1 ALA B 156 ? ? -108.59 -133.43 
11 1 ALA B 156 ? ? -108.59 -134.13 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,z         
# 
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 38.6625403614 26.1809251059 28.1730802137 0.394971687999 ? -0.00162794618117 ? -0.0213569134682 ? 
0.414255639798 ? 0.0446286345332   ? 0.372028588867 ? 0.357248849399  ? 0.149711077144   ? 0.0526453763317   ? 0.342880590778  ? 
0.324136794952   ? 0.338818852428  ? 0.0503253599612  ? -0.028474935757  ? -0.105422836689  ? 0.30241896264    ? -0.213929844509  
? -0.232068636088  ? 0.141260498129   ? -0.00388986893769 ? -0.000108791261708 ? 
2  'X-RAY DIFFRACTION' ? refined 23.9769718993 23.0845399305 34.7673996287 0.347108284165 ? -0.104982755941   ? -0.0274575310391 ? 
0.348799264538 ? -0.00967516146054 ? 0.260585673857 ? 0.136581062031  ? 0.290526043954   ? -0.00343274154405 ? 0.643389501171  ? 
0.0970520582353  ? 0.250232608523  ? 0.275835896112   ? -0.413902963427  ? 0.278987302854   ? 0.602615641253   ? -0.052743551646  
? 0.444442046995   ? -0.17834116481   ? -0.318345075405   ? 0.00866083640766   ? 
3  'X-RAY DIFFRACTION' ? refined 26.4178546408 20.2733022525 24.9510276996 0.326685555654 ? -0.0208987822361  ? -0.0327553542632 ? 
0.351422637822 ? -0.0175876719106  ? 0.37084990288  ? 0.315416087138  ? 0.226350361457   ? -0.20951634154    ? 0.270647516332  ? 
0.0162331337569  ? 0.278420980668  ? 0.190167376748   ? -0.0203851247257 ? -0.402380701411  ? 0.00295355665834 ? -0.0563771308825 
? -0.0602281240853 ? 0.0895424555015  ? 0.159423493497    ? -8.64556408442e-05 ? 
4  'X-RAY DIFFRACTION' ? refined 19.6764220789 12.7595393009 21.1285046838 0.360177284178 ? -0.00803993459057 ? 0.0213942979153  ? 
0.423758787952 ? -0.0699954658374  ? 0.519256840474 ? 0.154942369887  ? 0.095505700052   ? -0.115721164285   ? 0.0500765730984 ? 
0.0469546454414  ? 0.152896143841  ? 0.0512467793137  ? -0.161131361994  ? -0.27988146109   ? -0.017766636759  ? -0.0322023618072 
? 0.0904360169044  ? 0.0860227993956  ? -0.561968785269   ? 0.00029318942961   ? 
5  'X-RAY DIFFRACTION' ? refined 16.8265632923 13.9208188594 24.1629085232 0.298413719081 ? -0.0422636492273  ? -0.0200975737553 ? 
0.281627165466 ? -0.0196895019313  ? 0.424226502006 ? 0.0499991618865 ? -0.114875892314  ? -0.104744598886   ? 0.122773380496  ? 
0.139585881393   ? 0.0605181693014 ? 0.14352692977    ? -0.254332144283  ? -0.0204546610687 ? 0.133208896552   ? -0.0731094489305 
? 0.131553784196   ? 0.191010121253   ? -0.213128847871   ? 3.28929402158e-05  ? 
6  'X-RAY DIFFRACTION' ? refined 19.442629465  10.2456668111 34.7743397619 0.570839241539 ? -0.100553162617   ? 0.0944291208006  ? 
0.480052230445 ? 0.0769789689438   ? 0.437138419562 ? 0.033795470353  ? 0.00917369726275 ? 0.03514692552     ? 0.0123969836803 ? 
-0.0035515834634 ? 0.0402414426873 ? 0.189189694314   ? -0.234673425092  ? -0.101457709268  ? 0.915456770127   ? -0.202955478135  
? -0.220008619165  ? 0.175874563663   ? -0.0251680897539  ? 0.000217704041392  ? 
7  'X-RAY DIFFRACTION' ? refined 17.5551255982 3.74158846014 20.1998681684 0.323467908541 ? -0.0950661106413  ? -0.0337385075787 ? 
0.335417343295 ? -0.0653122826203  ? 0.605512927591 ? 0.106471169314  ? 0.0612080329024  ? -0.0323849389523  ? 0.395552682931  ? 
-0.362499696769  ? 0.341709317897  ? -0.144410470821  ? 0.00135180494493 ? -0.654865276219  ? 0.0631037083353  ? 0.0204733506428  
? 0.717002309081   ? 0.216818577033   ? -0.263032534809   ? -0.0109488293255   ? 
8  'X-RAY DIFFRACTION' ? refined 18.8835225412 10.2390701612 13.2343590413 0.515293725212 ? -0.0389668280215  ? -0.0452558431663 ? 
0.430518612917 ? -0.0595739296214  ? 0.547503901221 ? 0.135883899881  ? 0.159469566343   ? -0.14850810608    ? 0.120108773486  ? 
-0.136642219502  ? 0.161664208019  ? 0.357555670343   ? -0.253890866673  ? -0.69326974669   ? -0.309881900355  ? -0.0823183694148 
? 0.259455599342   ? 0.590888093912   ? -0.347926270611   ? -7.98711300466e-05 ? 
9  'X-RAY DIFFRACTION' ? refined 34.101168023  13.8003819499 11.8995985224 0.369419235311 ? 0.0374490704597   ? 0.00791972606666 ? 
0.344033780307 ? -0.0828499991004  ? 0.371194338467 ? 0.724003735079  ? 0.712141679021   ? -0.188486409042   ? 1.47747530676   ? 
0.125227356549   ? 0.546697757858  ? -0.0706489342861 ? 0.0421440876892  ? -0.219296059076  ? -0.176741538778  ? 0.0154527778437  
? -0.280318489203  ? 0.137870148198   ? 0.0660967395422   ? -3.79461332538e-05 ? 
10 'X-RAY DIFFRACTION' ? refined 28.4009186977 38.5838843907 3.68795888715 0.40437847709  ? -0.00029042493944 ? -0.0120914056326 ? 
0.380947035408 ? 0.00187705830858  ? 0.278854007759 ? 0.350734006429  ? -0.0776269683334 ? -0.351935277533   ? 2.1657835109    ? 
-0.245335426404  ? 1.34174667882   ? -0.02036816668   ? 0.228872387005   ? 0.0712122879604  ? -0.456474470085  ? -0.0534938999412 
? -0.0217291864316 ? -0.0800704540115 ? 0.0710982705103   ? 4.19564248684e-05  ? 
11 'X-RAY DIFFRACTION' ? refined 26.0501834968 41.9787123942 20.0838775024 0.279840620661 ? 0.00200268361056  ? 0.0207002536219  ? 
0.300059988632 ? -0.0361921022077  ? 0.321146532922 ? 0.520257302677  ? -0.410629909412  ? 0.486416918734    ? 1.1533365628    ? 
-0.566898011013  ? 0.385011359234  ? 0.0121719766896  ? 0.0134221761967  ? 0.129336253106   ? -0.0183335460441 ? -0.0282475421557 
? -0.0301941490628 ? -0.0443379011814 ? 0.019520558505    ? -2.49278360068e-05 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 6 through 29 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 30 through 46 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 47 through 70 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 71 through 83 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 84 through 105 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 106 through 118 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 119 through 142 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 143 through 157 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 158 through 239 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 6 through 157 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 158 through 239 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -2 ? A GLY 1 
2  1 Y 1 A PRO -1 ? A PRO 2 
3  1 Y 1 A GLY 0  ? A GLY 3 
4  1 Y 1 A MET 1  ? A MET 4 
5  1 Y 1 A GLY 2  ? A GLY 5 
6  1 Y 1 A ALA 3  ? A ALA 6 
7  1 Y 1 A SER 4  ? A SER 7 
8  1 Y 1 A ILE 5  ? A ILE 8 
9  1 Y 1 B GLY -2 ? B GLY 1 
10 1 Y 1 B PRO -1 ? B PRO 2 
11 1 Y 1 B GLY 0  ? B GLY 3 
12 1 Y 1 B MET 1  ? B MET 4 
13 1 Y 1 B GLY 2  ? B GLY 5 
14 1 Y 1 B ALA 3  ? B ALA 6 
15 1 Y 1 B SER 4  ? B SER 7 
16 1 Y 1 B ILE 5  ? B ILE 8 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1LU2 C13    C  Y N 1   
A1LU2 C02    C  Y N 2   
A1LU2 C03    C  Y N 3   
A1LU2 C04    C  Y N 4   
A1LU2 C05    C  Y N 5   
A1LU2 C06    C  Y N 6   
A1LU2 C07    C  Y N 7   
A1LU2 C08    C  N N 8   
A1LU2 C09    C  N N 9   
A1LU2 C11    C  N N 10  
A1LU2 C12    C  Y N 11  
A1LU2 C14    C  Y N 12  
A1LU2 C16    C  Y N 13  
A1LU2 C18    C  Y N 14  
A1LU2 C19    C  Y N 15  
A1LU2 N10    N  N N 16  
A1LU2 O01    O  N N 17  
A1LU2 O15    O  N N 18  
A1LU2 O17    O  N N 19  
A1LU2 H131   H  N N 20  
A1LU2 H031   H  N N 21  
A1LU2 H041   H  N N 22  
A1LU2 H051   H  N N 23  
A1LU2 H061   H  N N 24  
A1LU2 H082   H  N N 25  
A1LU2 H081   H  N N 26  
A1LU2 H091   H  N N 27  
A1LU2 H092   H  N N 28  
A1LU2 H112   H  N N 29  
A1LU2 H111   H  N N 30  
A1LU2 H181   H  N N 31  
A1LU2 H191   H  N N 32  
A1LU2 H1     H  N N 33  
A1LU2 H011   H  N N 34  
A1LU2 H151   H  N N 35  
A1LU2 H171   H  N N 36  
ALA   N      N  N N 37  
ALA   CA     C  N S 38  
ALA   C      C  N N 39  
ALA   O      O  N N 40  
ALA   CB     C  N N 41  
ALA   OXT    O  N N 42  
ALA   H      H  N N 43  
ALA   H2     H  N N 44  
ALA   HA     H  N N 45  
ALA   HB1    H  N N 46  
ALA   HB2    H  N N 47  
ALA   HB3    H  N N 48  
ALA   HXT    H  N N 49  
ARG   N      N  N N 50  
ARG   CA     C  N S 51  
ARG   C      C  N N 52  
ARG   O      O  N N 53  
ARG   CB     C  N N 54  
ARG   CG     C  N N 55  
ARG   CD     C  N N 56  
ARG   NE     N  N N 57  
ARG   CZ     C  N N 58  
ARG   NH1    N  N N 59  
ARG   NH2    N  N N 60  
ARG   OXT    O  N N 61  
ARG   H      H  N N 62  
ARG   H2     H  N N 63  
ARG   HA     H  N N 64  
ARG   HB2    H  N N 65  
ARG   HB3    H  N N 66  
ARG   HG2    H  N N 67  
ARG   HG3    H  N N 68  
ARG   HD2    H  N N 69  
ARG   HD3    H  N N 70  
ARG   HE     H  N N 71  
ARG   HH11   H  N N 72  
ARG   HH12   H  N N 73  
ARG   HH21   H  N N 74  
ARG   HH22   H  N N 75  
ARG   HXT    H  N N 76  
ASN   N      N  N N 77  
ASN   CA     C  N S 78  
ASN   C      C  N N 79  
ASN   O      O  N N 80  
ASN   CB     C  N N 81  
ASN   CG     C  N N 82  
ASN   OD1    O  N N 83  
ASN   ND2    N  N N 84  
ASN   OXT    O  N N 85  
ASN   H      H  N N 86  
ASN   H2     H  N N 87  
ASN   HA     H  N N 88  
ASN   HB2    H  N N 89  
ASN   HB3    H  N N 90  
ASN   HD21   H  N N 91  
ASN   HD22   H  N N 92  
ASN   HXT    H  N N 93  
ASP   N      N  N N 94  
ASP   CA     C  N S 95  
ASP   C      C  N N 96  
ASP   O      O  N N 97  
ASP   CB     C  N N 98  
ASP   CG     C  N N 99  
ASP   OD1    O  N N 100 
ASP   OD2    O  N N 101 
ASP   OXT    O  N N 102 
ASP   H      H  N N 103 
ASP   H2     H  N N 104 
ASP   HA     H  N N 105 
ASP   HB2    H  N N 106 
ASP   HB3    H  N N 107 
ASP   HD2    H  N N 108 
ASP   HXT    H  N N 109 
CYS   N      N  N N 110 
CYS   CA     C  N R 111 
CYS   C      C  N N 112 
CYS   O      O  N N 113 
CYS   CB     C  N N 114 
CYS   SG     S  N N 115 
CYS   OXT    O  N N 116 
CYS   H      H  N N 117 
CYS   H2     H  N N 118 
CYS   HA     H  N N 119 
CYS   HB2    H  N N 120 
CYS   HB3    H  N N 121 
CYS   HG     H  N N 122 
CYS   HXT    H  N N 123 
GLN   N      N  N N 124 
GLN   CA     C  N S 125 
GLN   C      C  N N 126 
GLN   O      O  N N 127 
GLN   CB     C  N N 128 
GLN   CG     C  N N 129 
GLN   CD     C  N N 130 
GLN   OE1    O  N N 131 
GLN   NE2    N  N N 132 
GLN   OXT    O  N N 133 
GLN   H      H  N N 134 
GLN   H2     H  N N 135 
GLN   HA     H  N N 136 
GLN   HB2    H  N N 137 
GLN   HB3    H  N N 138 
GLN   HG2    H  N N 139 
GLN   HG3    H  N N 140 
GLN   HE21   H  N N 141 
GLN   HE22   H  N N 142 
GLN   HXT    H  N N 143 
GLU   N      N  N N 144 
GLU   CA     C  N S 145 
GLU   C      C  N N 146 
GLU   O      O  N N 147 
GLU   CB     C  N N 148 
GLU   CG     C  N N 149 
GLU   CD     C  N N 150 
GLU   OE1    O  N N 151 
GLU   OE2    O  N N 152 
GLU   OXT    O  N N 153 
GLU   H      H  N N 154 
GLU   H2     H  N N 155 
GLU   HA     H  N N 156 
GLU   HB2    H  N N 157 
GLU   HB3    H  N N 158 
GLU   HG2    H  N N 159 
GLU   HG3    H  N N 160 
GLU   HE2    H  N N 161 
GLU   HXT    H  N N 162 
GLY   N      N  N N 163 
GLY   CA     C  N N 164 
GLY   C      C  N N 165 
GLY   O      O  N N 166 
GLY   OXT    O  N N 167 
GLY   H      H  N N 168 
GLY   H2     H  N N 169 
GLY   HA2    H  N N 170 
GLY   HA3    H  N N 171 
GLY   HXT    H  N N 172 
GOL   C1     C  N N 173 
GOL   O1     O  N N 174 
GOL   C2     C  N N 175 
GOL   O2     O  N N 176 
GOL   C3     C  N N 177 
GOL   O3     O  N N 178 
GOL   H11    H  N N 179 
GOL   H12    H  N N 180 
GOL   HO1    H  N N 181 
GOL   H2     H  N N 182 
GOL   HO2    H  N N 183 
GOL   H31    H  N N 184 
GOL   H32    H  N N 185 
GOL   HO3    H  N N 186 
HIS   N      N  N N 187 
HIS   CA     C  N S 188 
HIS   C      C  N N 189 
HIS   O      O  N N 190 
HIS   CB     C  N N 191 
HIS   CG     C  Y N 192 
HIS   ND1    N  Y N 193 
HIS   CD2    C  Y N 194 
HIS   CE1    C  Y N 195 
HIS   NE2    N  Y N 196 
HIS   OXT    O  N N 197 
HIS   H      H  N N 198 
HIS   H2     H  N N 199 
HIS   HA     H  N N 200 
HIS   HB2    H  N N 201 
HIS   HB3    H  N N 202 
HIS   HD1    H  N N 203 
HIS   HD2    H  N N 204 
HIS   HE1    H  N N 205 
HIS   HE2    H  N N 206 
HIS   HXT    H  N N 207 
HOH   O      O  N N 208 
HOH   H1     H  N N 209 
HOH   H2     H  N N 210 
ILE   N      N  N N 211 
ILE   CA     C  N S 212 
ILE   C      C  N N 213 
ILE   O      O  N N 214 
ILE   CB     C  N S 215 
ILE   CG1    C  N N 216 
ILE   CG2    C  N N 217 
ILE   CD1    C  N N 218 
ILE   OXT    O  N N 219 
ILE   H      H  N N 220 
ILE   H2     H  N N 221 
ILE   HA     H  N N 222 
ILE   HB     H  N N 223 
ILE   HG12   H  N N 224 
ILE   HG13   H  N N 225 
ILE   HG21   H  N N 226 
ILE   HG22   H  N N 227 
ILE   HG23   H  N N 228 
ILE   HD11   H  N N 229 
ILE   HD12   H  N N 230 
ILE   HD13   H  N N 231 
ILE   HXT    H  N N 232 
LEU   N      N  N N 233 
LEU   CA     C  N S 234 
LEU   C      C  N N 235 
LEU   O      O  N N 236 
LEU   CB     C  N N 237 
LEU   CG     C  N N 238 
LEU   CD1    C  N N 239 
LEU   CD2    C  N N 240 
LEU   OXT    O  N N 241 
LEU   H      H  N N 242 
LEU   H2     H  N N 243 
LEU   HA     H  N N 244 
LEU   HB2    H  N N 245 
LEU   HB3    H  N N 246 
LEU   HG     H  N N 247 
LEU   HD11   H  N N 248 
LEU   HD12   H  N N 249 
LEU   HD13   H  N N 250 
LEU   HD21   H  N N 251 
LEU   HD22   H  N N 252 
LEU   HD23   H  N N 253 
LEU   HXT    H  N N 254 
LYS   N      N  N N 255 
LYS   CA     C  N S 256 
LYS   C      C  N N 257 
LYS   O      O  N N 258 
LYS   CB     C  N N 259 
LYS   CG     C  N N 260 
LYS   CD     C  N N 261 
LYS   CE     C  N N 262 
LYS   NZ     N  N N 263 
LYS   OXT    O  N N 264 
LYS   H      H  N N 265 
LYS   H2     H  N N 266 
LYS   HA     H  N N 267 
LYS   HB2    H  N N 268 
LYS   HB3    H  N N 269 
LYS   HG2    H  N N 270 
LYS   HG3    H  N N 271 
LYS   HD2    H  N N 272 
LYS   HD3    H  N N 273 
LYS   HE2    H  N N 274 
LYS   HE3    H  N N 275 
LYS   HZ1    H  N N 276 
LYS   HZ2    H  N N 277 
LYS   HZ3    H  N N 278 
LYS   HXT    H  N N 279 
MET   N      N  N N 280 
MET   CA     C  N S 281 
MET   C      C  N N 282 
MET   O      O  N N 283 
MET   CB     C  N N 284 
MET   CG     C  N N 285 
MET   SD     S  N N 286 
MET   CE     C  N N 287 
MET   OXT    O  N N 288 
MET   H      H  N N 289 
MET   H2     H  N N 290 
MET   HA     H  N N 291 
MET   HB2    H  N N 292 
MET   HB3    H  N N 293 
MET   HG2    H  N N 294 
MET   HG3    H  N N 295 
MET   HE1    H  N N 296 
MET   HE2    H  N N 297 
MET   HE3    H  N N 298 
MET   HXT    H  N N 299 
MG    MG     MG N N 300 
PHE   N      N  N N 301 
PHE   CA     C  N S 302 
PHE   C      C  N N 303 
PHE   O      O  N N 304 
PHE   CB     C  N N 305 
PHE   CG     C  Y N 306 
PHE   CD1    C  Y N 307 
PHE   CD2    C  Y N 308 
PHE   CE1    C  Y N 309 
PHE   CE2    C  Y N 310 
PHE   CZ     C  Y N 311 
PHE   OXT    O  N N 312 
PHE   H      H  N N 313 
PHE   H2     H  N N 314 
PHE   HA     H  N N 315 
PHE   HB2    H  N N 316 
PHE   HB3    H  N N 317 
PHE   HD1    H  N N 318 
PHE   HD2    H  N N 319 
PHE   HE1    H  N N 320 
PHE   HE2    H  N N 321 
PHE   HZ     H  N N 322 
PHE   HXT    H  N N 323 
PRO   N      N  N N 324 
PRO   CA     C  N S 325 
PRO   C      C  N N 326 
PRO   O      O  N N 327 
PRO   CB     C  N N 328 
PRO   CG     C  N N 329 
PRO   CD     C  N N 330 
PRO   OXT    O  N N 331 
PRO   H      H  N N 332 
PRO   HA     H  N N 333 
PRO   HB2    H  N N 334 
PRO   HB3    H  N N 335 
PRO   HG2    H  N N 336 
PRO   HG3    H  N N 337 
PRO   HD2    H  N N 338 
PRO   HD3    H  N N 339 
PRO   HXT    H  N N 340 
SAH   N      N  N N 341 
SAH   CA     C  N S 342 
SAH   CB     C  N N 343 
SAH   CG     C  N N 344 
SAH   SD     S  N N 345 
SAH   C      C  N N 346 
SAH   O      O  N N 347 
SAH   OXT    O  N N 348 
SAH   "C5'"  C  N N 349 
SAH   "C4'"  C  N S 350 
SAH   "O4'"  O  N N 351 
SAH   "C3'"  C  N S 352 
SAH   "O3'"  O  N N 353 
SAH   "C2'"  C  N R 354 
SAH   "O2'"  O  N N 355 
SAH   "C1'"  C  N R 356 
SAH   N9     N  Y N 357 
SAH   C8     C  Y N 358 
SAH   N7     N  Y N 359 
SAH   C5     C  Y N 360 
SAH   C6     C  Y N 361 
SAH   N6     N  N N 362 
SAH   N1     N  Y N 363 
SAH   C2     C  Y N 364 
SAH   N3     N  Y N 365 
SAH   C4     C  Y N 366 
SAH   HN1    H  N N 367 
SAH   HN2    H  N N 368 
SAH   HA     H  N N 369 
SAH   HB1    H  N N 370 
SAH   HB2    H  N N 371 
SAH   HG1    H  N N 372 
SAH   HG2    H  N N 373 
SAH   HXT    H  N N 374 
SAH   "H5'1" H  N N 375 
SAH   "H5'2" H  N N 376 
SAH   "H4'"  H  N N 377 
SAH   "H3'"  H  N N 378 
SAH   "HO3'" H  N N 379 
SAH   "H2'"  H  N N 380 
SAH   "HO2'" H  N N 381 
SAH   "H1'"  H  N N 382 
SAH   H8     H  N N 383 
SAH   HN61   H  N N 384 
SAH   HN62   H  N N 385 
SAH   H2     H  N N 386 
SER   N      N  N N 387 
SER   CA     C  N S 388 
SER   C      C  N N 389 
SER   O      O  N N 390 
SER   CB     C  N N 391 
SER   OG     O  N N 392 
SER   OXT    O  N N 393 
SER   H      H  N N 394 
SER   H2     H  N N 395 
SER   HA     H  N N 396 
SER   HB2    H  N N 397 
SER   HB3    H  N N 398 
SER   HG     H  N N 399 
SER   HXT    H  N N 400 
THR   N      N  N N 401 
THR   CA     C  N S 402 
THR   C      C  N N 403 
THR   O      O  N N 404 
THR   CB     C  N R 405 
THR   OG1    O  N N 406 
THR   CG2    C  N N 407 
THR   OXT    O  N N 408 
THR   H      H  N N 409 
THR   H2     H  N N 410 
THR   HA     H  N N 411 
THR   HB     H  N N 412 
THR   HG1    H  N N 413 
THR   HG21   H  N N 414 
THR   HG22   H  N N 415 
THR   HG23   H  N N 416 
THR   HXT    H  N N 417 
TRP   N      N  N N 418 
TRP   CA     C  N S 419 
TRP   C      C  N N 420 
TRP   O      O  N N 421 
TRP   CB     C  N N 422 
TRP   CG     C  Y N 423 
TRP   CD1    C  Y N 424 
TRP   CD2    C  Y N 425 
TRP   NE1    N  Y N 426 
TRP   CE2    C  Y N 427 
TRP   CE3    C  Y N 428 
TRP   CZ2    C  Y N 429 
TRP   CZ3    C  Y N 430 
TRP   CH2    C  Y N 431 
TRP   OXT    O  N N 432 
TRP   H      H  N N 433 
TRP   H2     H  N N 434 
TRP   HA     H  N N 435 
TRP   HB2    H  N N 436 
TRP   HB3    H  N N 437 
TRP   HD1    H  N N 438 
TRP   HE1    H  N N 439 
TRP   HE3    H  N N 440 
TRP   HZ2    H  N N 441 
TRP   HZ3    H  N N 442 
TRP   HH2    H  N N 443 
TRP   HXT    H  N N 444 
TYR   N      N  N N 445 
TYR   CA     C  N S 446 
TYR   C      C  N N 447 
TYR   O      O  N N 448 
TYR   CB     C  N N 449 
TYR   CG     C  Y N 450 
TYR   CD1    C  Y N 451 
TYR   CD2    C  Y N 452 
TYR   CE1    C  Y N 453 
TYR   CE2    C  Y N 454 
TYR   CZ     C  Y N 455 
TYR   OH     O  N N 456 
TYR   OXT    O  N N 457 
TYR   H      H  N N 458 
TYR   H2     H  N N 459 
TYR   HA     H  N N 460 
TYR   HB2    H  N N 461 
TYR   HB3    H  N N 462 
TYR   HD1    H  N N 463 
TYR   HD2    H  N N 464 
TYR   HE1    H  N N 465 
TYR   HE2    H  N N 466 
TYR   HH     H  N N 467 
TYR   HXT    H  N N 468 
VAL   N      N  N N 469 
VAL   CA     C  N S 470 
VAL   C      C  N N 471 
VAL   O      O  N N 472 
VAL   CB     C  N N 473 
VAL   CG1    C  N N 474 
VAL   CG2    C  N N 475 
VAL   OXT    O  N N 476 
VAL   H      H  N N 477 
VAL   H2     H  N N 478 
VAL   HA     H  N N 479 
VAL   HB     H  N N 480 
VAL   HG11   H  N N 481 
VAL   HG12   H  N N 482 
VAL   HG13   H  N N 483 
VAL   HG21   H  N N 484 
VAL   HG22   H  N N 485 
VAL   HG23   H  N N 486 
VAL   HXT    H  N N 487 
# 
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 
A1LU2 C02   O01    sing N N 1   
A1LU2 C04   C03    doub Y N 2   
A1LU2 C03   C02    sing Y N 3   
A1LU2 C05   C02    doub Y N 4   
A1LU2 C06   C05    sing Y N 5   
A1LU2 C07   C06    doub Y N 6   
A1LU2 C08   C07    sing N N 7   
A1LU2 C09   C08    sing N N 8   
A1LU2 N10   C09    sing N N 9   
A1LU2 C11   N10    sing N N 10  
A1LU2 C12   C11    sing N N 11  
A1LU2 C13   C12    doub Y N 12  
A1LU2 C14   C13    sing Y N 13  
A1LU2 O15   C14    sing N N 14  
A1LU2 C16   C14    doub Y N 15  
A1LU2 O17   C16    sing N N 16  
A1LU2 C18   C16    sing Y N 17  
A1LU2 C19   C18    doub Y N 18  
A1LU2 C04   C07    sing Y N 19  
A1LU2 C12   C19    sing Y N 20  
A1LU2 C13   H131   sing N N 21  
A1LU2 C03   H031   sing N N 22  
A1LU2 C04   H041   sing N N 23  
A1LU2 C05   H051   sing N N 24  
A1LU2 C06   H061   sing N N 25  
A1LU2 C08   H082   sing N N 26  
A1LU2 C08   H081   sing N N 27  
A1LU2 C09   H091   sing N N 28  
A1LU2 C09   H092   sing N N 29  
A1LU2 C11   H112   sing N N 30  
A1LU2 C11   H111   sing N N 31  
A1LU2 C18   H181   sing N N 32  
A1LU2 C19   H191   sing N N 33  
A1LU2 N10   H1     sing N N 34  
A1LU2 O01   H011   sing N N 35  
A1LU2 O15   H151   sing N N 36  
A1LU2 O17   H171   sing N N 37  
ALA   N     CA     sing N N 38  
ALA   N     H      sing N N 39  
ALA   N     H2     sing N N 40  
ALA   CA    C      sing N N 41  
ALA   CA    CB     sing N N 42  
ALA   CA    HA     sing N N 43  
ALA   C     O      doub N N 44  
ALA   C     OXT    sing N N 45  
ALA   CB    HB1    sing N N 46  
ALA   CB    HB2    sing N N 47  
ALA   CB    HB3    sing N N 48  
ALA   OXT   HXT    sing N N 49  
ARG   N     CA     sing N N 50  
ARG   N     H      sing N N 51  
ARG   N     H2     sing N N 52  
ARG   CA    C      sing N N 53  
ARG   CA    CB     sing N N 54  
ARG   CA    HA     sing N N 55  
ARG   C     O      doub N N 56  
ARG   C     OXT    sing N N 57  
ARG   CB    CG     sing N N 58  
ARG   CB    HB2    sing N N 59  
ARG   CB    HB3    sing N N 60  
ARG   CG    CD     sing N N 61  
ARG   CG    HG2    sing N N 62  
ARG   CG    HG3    sing N N 63  
ARG   CD    NE     sing N N 64  
ARG   CD    HD2    sing N N 65  
ARG   CD    HD3    sing N N 66  
ARG   NE    CZ     sing N N 67  
ARG   NE    HE     sing N N 68  
ARG   CZ    NH1    sing N N 69  
ARG   CZ    NH2    doub N N 70  
ARG   NH1   HH11   sing N N 71  
ARG   NH1   HH12   sing N N 72  
ARG   NH2   HH21   sing N N 73  
ARG   NH2   HH22   sing N N 74  
ARG   OXT   HXT    sing N N 75  
ASN   N     CA     sing N N 76  
ASN   N     H      sing N N 77  
ASN   N     H2     sing N N 78  
ASN   CA    C      sing N N 79  
ASN   CA    CB     sing N N 80  
ASN   CA    HA     sing N N 81  
ASN   C     O      doub N N 82  
ASN   C     OXT    sing N N 83  
ASN   CB    CG     sing N N 84  
ASN   CB    HB2    sing N N 85  
ASN   CB    HB3    sing N N 86  
ASN   CG    OD1    doub N N 87  
ASN   CG    ND2    sing N N 88  
ASN   ND2   HD21   sing N N 89  
ASN   ND2   HD22   sing N N 90  
ASN   OXT   HXT    sing N N 91  
ASP   N     CA     sing N N 92  
ASP   N     H      sing N N 93  
ASP   N     H2     sing N N 94  
ASP   CA    C      sing N N 95  
ASP   CA    CB     sing N N 96  
ASP   CA    HA     sing N N 97  
ASP   C     O      doub N N 98  
ASP   C     OXT    sing N N 99  
ASP   CB    CG     sing N N 100 
ASP   CB    HB2    sing N N 101 
ASP   CB    HB3    sing N N 102 
ASP   CG    OD1    doub N N 103 
ASP   CG    OD2    sing N N 104 
ASP   OD2   HD2    sing N N 105 
ASP   OXT   HXT    sing N N 106 
CYS   N     CA     sing N N 107 
CYS   N     H      sing N N 108 
CYS   N     H2     sing N N 109 
CYS   CA    C      sing N N 110 
CYS   CA    CB     sing N N 111 
CYS   CA    HA     sing N N 112 
CYS   C     O      doub N N 113 
CYS   C     OXT    sing N N 114 
CYS   CB    SG     sing N N 115 
CYS   CB    HB2    sing N N 116 
CYS   CB    HB3    sing N N 117 
CYS   SG    HG     sing N N 118 
CYS   OXT   HXT    sing N N 119 
GLN   N     CA     sing N N 120 
GLN   N     H      sing N N 121 
GLN   N     H2     sing N N 122 
GLN   CA    C      sing N N 123 
GLN   CA    CB     sing N N 124 
GLN   CA    HA     sing N N 125 
GLN   C     O      doub N N 126 
GLN   C     OXT    sing N N 127 
GLN   CB    CG     sing N N 128 
GLN   CB    HB2    sing N N 129 
GLN   CB    HB3    sing N N 130 
GLN   CG    CD     sing N N 131 
GLN   CG    HG2    sing N N 132 
GLN   CG    HG3    sing N N 133 
GLN   CD    OE1    doub N N 134 
GLN   CD    NE2    sing N N 135 
GLN   NE2   HE21   sing N N 136 
GLN   NE2   HE22   sing N N 137 
GLN   OXT   HXT    sing N N 138 
GLU   N     CA     sing N N 139 
GLU   N     H      sing N N 140 
GLU   N     H2     sing N N 141 
GLU   CA    C      sing N N 142 
GLU   CA    CB     sing N N 143 
GLU   CA    HA     sing N N 144 
GLU   C     O      doub N N 145 
GLU   C     OXT    sing N N 146 
GLU   CB    CG     sing N N 147 
GLU   CB    HB2    sing N N 148 
GLU   CB    HB3    sing N N 149 
GLU   CG    CD     sing N N 150 
GLU   CG    HG2    sing N N 151 
GLU   CG    HG3    sing N N 152 
GLU   CD    OE1    doub N N 153 
GLU   CD    OE2    sing N N 154 
GLU   OE2   HE2    sing N N 155 
GLU   OXT   HXT    sing N N 156 
GLY   N     CA     sing N N 157 
GLY   N     H      sing N N 158 
GLY   N     H2     sing N N 159 
GLY   CA    C      sing N N 160 
GLY   CA    HA2    sing N N 161 
GLY   CA    HA3    sing N N 162 
GLY   C     O      doub N N 163 
GLY   C     OXT    sing N N 164 
GLY   OXT   HXT    sing N N 165 
GOL   C1    O1     sing N N 166 
GOL   C1    C2     sing N N 167 
GOL   C1    H11    sing N N 168 
GOL   C1    H12    sing N N 169 
GOL   O1    HO1    sing N N 170 
GOL   C2    O2     sing N N 171 
GOL   C2    C3     sing N N 172 
GOL   C2    H2     sing N N 173 
GOL   O2    HO2    sing N N 174 
GOL   C3    O3     sing N N 175 
GOL   C3    H31    sing N N 176 
GOL   C3    H32    sing N N 177 
GOL   O3    HO3    sing N N 178 
HIS   N     CA     sing N N 179 
HIS   N     H      sing N N 180 
HIS   N     H2     sing N N 181 
HIS   CA    C      sing N N 182 
HIS   CA    CB     sing N N 183 
HIS   CA    HA     sing N N 184 
HIS   C     O      doub N N 185 
HIS   C     OXT    sing N N 186 
HIS   CB    CG     sing N N 187 
HIS   CB    HB2    sing N N 188 
HIS   CB    HB3    sing N N 189 
HIS   CG    ND1    sing Y N 190 
HIS   CG    CD2    doub Y N 191 
HIS   ND1   CE1    doub Y N 192 
HIS   ND1   HD1    sing N N 193 
HIS   CD2   NE2    sing Y N 194 
HIS   CD2   HD2    sing N N 195 
HIS   CE1   NE2    sing Y N 196 
HIS   CE1   HE1    sing N N 197 
HIS   NE2   HE2    sing N N 198 
HIS   OXT   HXT    sing N N 199 
HOH   O     H1     sing N N 200 
HOH   O     H2     sing N N 201 
ILE   N     CA     sing N N 202 
ILE   N     H      sing N N 203 
ILE   N     H2     sing N N 204 
ILE   CA    C      sing N N 205 
ILE   CA    CB     sing N N 206 
ILE   CA    HA     sing N N 207 
ILE   C     O      doub N N 208 
ILE   C     OXT    sing N N 209 
ILE   CB    CG1    sing N N 210 
ILE   CB    CG2    sing N N 211 
ILE   CB    HB     sing N N 212 
ILE   CG1   CD1    sing N N 213 
ILE   CG1   HG12   sing N N 214 
ILE   CG1   HG13   sing N N 215 
ILE   CG2   HG21   sing N N 216 
ILE   CG2   HG22   sing N N 217 
ILE   CG2   HG23   sing N N 218 
ILE   CD1   HD11   sing N N 219 
ILE   CD1   HD12   sing N N 220 
ILE   CD1   HD13   sing N N 221 
ILE   OXT   HXT    sing N N 222 
LEU   N     CA     sing N N 223 
LEU   N     H      sing N N 224 
LEU   N     H2     sing N N 225 
LEU   CA    C      sing N N 226 
LEU   CA    CB     sing N N 227 
LEU   CA    HA     sing N N 228 
LEU   C     O      doub N N 229 
LEU   C     OXT    sing N N 230 
LEU   CB    CG     sing N N 231 
LEU   CB    HB2    sing N N 232 
LEU   CB    HB3    sing N N 233 
LEU   CG    CD1    sing N N 234 
LEU   CG    CD2    sing N N 235 
LEU   CG    HG     sing N N 236 
LEU   CD1   HD11   sing N N 237 
LEU   CD1   HD12   sing N N 238 
LEU   CD1   HD13   sing N N 239 
LEU   CD2   HD21   sing N N 240 
LEU   CD2   HD22   sing N N 241 
LEU   CD2   HD23   sing N N 242 
LEU   OXT   HXT    sing N N 243 
LYS   N     CA     sing N N 244 
LYS   N     H      sing N N 245 
LYS   N     H2     sing N N 246 
LYS   CA    C      sing N N 247 
LYS   CA    CB     sing N N 248 
LYS   CA    HA     sing N N 249 
LYS   C     O      doub N N 250 
LYS   C     OXT    sing N N 251 
LYS   CB    CG     sing N N 252 
LYS   CB    HB2    sing N N 253 
LYS   CB    HB3    sing N N 254 
LYS   CG    CD     sing N N 255 
LYS   CG    HG2    sing N N 256 
LYS   CG    HG3    sing N N 257 
LYS   CD    CE     sing N N 258 
LYS   CD    HD2    sing N N 259 
LYS   CD    HD3    sing N N 260 
LYS   CE    NZ     sing N N 261 
LYS   CE    HE2    sing N N 262 
LYS   CE    HE3    sing N N 263 
LYS   NZ    HZ1    sing N N 264 
LYS   NZ    HZ2    sing N N 265 
LYS   NZ    HZ3    sing N N 266 
LYS   OXT   HXT    sing N N 267 
MET   N     CA     sing N N 268 
MET   N     H      sing N N 269 
MET   N     H2     sing N N 270 
MET   CA    C      sing N N 271 
MET   CA    CB     sing N N 272 
MET   CA    HA     sing N N 273 
MET   C     O      doub N N 274 
MET   C     OXT    sing N N 275 
MET   CB    CG     sing N N 276 
MET   CB    HB2    sing N N 277 
MET   CB    HB3    sing N N 278 
MET   CG    SD     sing N N 279 
MET   CG    HG2    sing N N 280 
MET   CG    HG3    sing N N 281 
MET   SD    CE     sing N N 282 
MET   CE    HE1    sing N N 283 
MET   CE    HE2    sing N N 284 
MET   CE    HE3    sing N N 285 
MET   OXT   HXT    sing N N 286 
PHE   N     CA     sing N N 287 
PHE   N     H      sing N N 288 
PHE   N     H2     sing N N 289 
PHE   CA    C      sing N N 290 
PHE   CA    CB     sing N N 291 
PHE   CA    HA     sing N N 292 
PHE   C     O      doub N N 293 
PHE   C     OXT    sing N N 294 
PHE   CB    CG     sing N N 295 
PHE   CB    HB2    sing N N 296 
PHE   CB    HB3    sing N N 297 
PHE   CG    CD1    doub Y N 298 
PHE   CG    CD2    sing Y N 299 
PHE   CD1   CE1    sing Y N 300 
PHE   CD1   HD1    sing N N 301 
PHE   CD2   CE2    doub Y N 302 
PHE   CD2   HD2    sing N N 303 
PHE   CE1   CZ     doub Y N 304 
PHE   CE1   HE1    sing N N 305 
PHE   CE2   CZ     sing Y N 306 
PHE   CE2   HE2    sing N N 307 
PHE   CZ    HZ     sing N N 308 
PHE   OXT   HXT    sing N N 309 
PRO   N     CA     sing N N 310 
PRO   N     CD     sing N N 311 
PRO   N     H      sing N N 312 
PRO   CA    C      sing N N 313 
PRO   CA    CB     sing N N 314 
PRO   CA    HA     sing N N 315 
PRO   C     O      doub N N 316 
PRO   C     OXT    sing N N 317 
PRO   CB    CG     sing N N 318 
PRO   CB    HB2    sing N N 319 
PRO   CB    HB3    sing N N 320 
PRO   CG    CD     sing N N 321 
PRO   CG    HG2    sing N N 322 
PRO   CG    HG3    sing N N 323 
PRO   CD    HD2    sing N N 324 
PRO   CD    HD3    sing N N 325 
PRO   OXT   HXT    sing N N 326 
SAH   N     CA     sing N N 327 
SAH   N     HN1    sing N N 328 
SAH   N     HN2    sing N N 329 
SAH   CA    CB     sing N N 330 
SAH   CA    C      sing N N 331 
SAH   CA    HA     sing N N 332 
SAH   CB    CG     sing N N 333 
SAH   CB    HB1    sing N N 334 
SAH   CB    HB2    sing N N 335 
SAH   CG    SD     sing N N 336 
SAH   CG    HG1    sing N N 337 
SAH   CG    HG2    sing N N 338 
SAH   SD    "C5'"  sing N N 339 
SAH   C     O      doub N N 340 
SAH   C     OXT    sing N N 341 
SAH   OXT   HXT    sing N N 342 
SAH   "C5'" "C4'"  sing N N 343 
SAH   "C5'" "H5'1" sing N N 344 
SAH   "C5'" "H5'2" sing N N 345 
SAH   "C4'" "O4'"  sing N N 346 
SAH   "C4'" "C3'"  sing N N 347 
SAH   "C4'" "H4'"  sing N N 348 
SAH   "O4'" "C1'"  sing N N 349 
SAH   "C3'" "O3'"  sing N N 350 
SAH   "C3'" "C2'"  sing N N 351 
SAH   "C3'" "H3'"  sing N N 352 
SAH   "O3'" "HO3'" sing N N 353 
SAH   "C2'" "O2'"  sing N N 354 
SAH   "C2'" "C1'"  sing N N 355 
SAH   "C2'" "H2'"  sing N N 356 
SAH   "O2'" "HO2'" sing N N 357 
SAH   "C1'" N9     sing N N 358 
SAH   "C1'" "H1'"  sing N N 359 
SAH   N9    C8     sing Y N 360 
SAH   N9    C4     sing Y N 361 
SAH   C8    N7     doub Y N 362 
SAH   C8    H8     sing N N 363 
SAH   N7    C5     sing Y N 364 
SAH   C5    C6     sing Y N 365 
SAH   C5    C4     doub Y N 366 
SAH   C6    N6     sing N N 367 
SAH   C6    N1     doub Y N 368 
SAH   N6    HN61   sing N N 369 
SAH   N6    HN62   sing N N 370 
SAH   N1    C2     sing Y N 371 
SAH   C2    N3     doub Y N 372 
SAH   C2    H2     sing N N 373 
SAH   N3    C4     sing Y N 374 
SER   N     CA     sing N N 375 
SER   N     H      sing N N 376 
SER   N     H2     sing N N 377 
SER   CA    C      sing N N 378 
SER   CA    CB     sing N N 379 
SER   CA    HA     sing N N 380 
SER   C     O      doub N N 381 
SER   C     OXT    sing N N 382 
SER   CB    OG     sing N N 383 
SER   CB    HB2    sing N N 384 
SER   CB    HB3    sing N N 385 
SER   OG    HG     sing N N 386 
SER   OXT   HXT    sing N N 387 
THR   N     CA     sing N N 388 
THR   N     H      sing N N 389 
THR   N     H2     sing N N 390 
THR   CA    C      sing N N 391 
THR   CA    CB     sing N N 392 
THR   CA    HA     sing N N 393 
THR   C     O      doub N N 394 
THR   C     OXT    sing N N 395 
THR   CB    OG1    sing N N 396 
THR   CB    CG2    sing N N 397 
THR   CB    HB     sing N N 398 
THR   OG1   HG1    sing N N 399 
THR   CG2   HG21   sing N N 400 
THR   CG2   HG22   sing N N 401 
THR   CG2   HG23   sing N N 402 
THR   OXT   HXT    sing N N 403 
TRP   N     CA     sing N N 404 
TRP   N     H      sing N N 405 
TRP   N     H2     sing N N 406 
TRP   CA    C      sing N N 407 
TRP   CA    CB     sing N N 408 
TRP   CA    HA     sing N N 409 
TRP   C     O      doub N N 410 
TRP   C     OXT    sing N N 411 
TRP   CB    CG     sing N N 412 
TRP   CB    HB2    sing N N 413 
TRP   CB    HB3    sing N N 414 
TRP   CG    CD1    doub Y N 415 
TRP   CG    CD2    sing Y N 416 
TRP   CD1   NE1    sing Y N 417 
TRP   CD1   HD1    sing N N 418 
TRP   CD2   CE2    doub Y N 419 
TRP   CD2   CE3    sing Y N 420 
TRP   NE1   CE2    sing Y N 421 
TRP   NE1   HE1    sing N N 422 
TRP   CE2   CZ2    sing Y N 423 
TRP   CE3   CZ3    doub Y N 424 
TRP   CE3   HE3    sing N N 425 
TRP   CZ2   CH2    doub Y N 426 
TRP   CZ2   HZ2    sing N N 427 
TRP   CZ3   CH2    sing Y N 428 
TRP   CZ3   HZ3    sing N N 429 
TRP   CH2   HH2    sing N N 430 
TRP   OXT   HXT    sing N N 431 
TYR   N     CA     sing N N 432 
TYR   N     H      sing N N 433 
TYR   N     H2     sing N N 434 
TYR   CA    C      sing N N 435 
TYR   CA    CB     sing N N 436 
TYR   CA    HA     sing N N 437 
TYR   C     O      doub N N 438 
TYR   C     OXT    sing N N 439 
TYR   CB    CG     sing N N 440 
TYR   CB    HB2    sing N N 441 
TYR   CB    HB3    sing N N 442 
TYR   CG    CD1    doub Y N 443 
TYR   CG    CD2    sing Y N 444 
TYR   CD1   CE1    sing Y N 445 
TYR   CD1   HD1    sing N N 446 
TYR   CD2   CE2    doub Y N 447 
TYR   CD2   HD2    sing N N 448 
TYR   CE1   CZ     doub Y N 449 
TYR   CE1   HE1    sing N N 450 
TYR   CE2   CZ     sing Y N 451 
TYR   CE2   HE2    sing N N 452 
TYR   CZ    OH     sing N N 453 
TYR   OH    HH     sing N N 454 
TYR   OXT   HXT    sing N N 455 
VAL   N     CA     sing N N 456 
VAL   N     H      sing N N 457 
VAL   N     H2     sing N N 458 
VAL   CA    C      sing N N 459 
VAL   CA    CB     sing N N 460 
VAL   CA    HA     sing N N 461 
VAL   C     O      doub N N 462 
VAL   C     OXT    sing N N 463 
VAL   CB    CG1    sing N N 464 
VAL   CB    CG2    sing N N 465 
VAL   CB    HB     sing N N 466 
VAL   CG1   HG11   sing N N 467 
VAL   CG1   HG12   sing N N 468 
VAL   CG1   HG13   sing N N 469 
VAL   CG2   HG21   sing N N 470 
VAL   CG2   HG22   sing N N 471 
VAL   CG2   HG23   sing N N 472 
VAL   OXT   HXT    sing N N 473 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Society for the Promotion of Science (JSPS)' Japan JP22H02777 1 
'Japan Society for the Promotion of Science (JSPS)' Japan JP22K15303 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8XDO 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 2' 
_space_group.name_Hall        'P 2 2ab' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Z8T 
_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]   0.012422 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008577 
_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]   0.019882 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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     . ASP   A 1 9   ? 44.15010 10.44647 36.33678  1.000 99.67974  ? 6   ASP   A N     1 
ATOM   2    C  CA    . ASP   A 1 9   ? 43.84076 10.58482 34.91790  1.000 97.21922  ? 6   ASP   A CA    1 
ATOM   3    C  C     . ASP   A 1 9   ? 44.92289 9.95513  34.04479  1.000 96.29727  ? 6   ASP   A C     1 
ATOM   4    O  O     . ASP   A 1 9   ? 46.11688 10.10225 34.31168  1.000 97.03528  ? 6   ASP   A O     1 
ATOM   5    C  CB    . ASP   A 1 9   ? 43.66821 12.05883 34.55061  1.000 95.14245  ? 6   ASP   A CB    1 
ATOM   6    N  N     . ASP   A 1 10  ? 44.49432 9.25050  32.99897  1.000 93.90676  ? 7   ASP   A N     1 
ATOM   7    C  CA    . ASP   A 1 10  ? 45.40929 8.64661  32.03916  1.000 90.65820  ? 7   ASP   A CA    1 
ATOM   8    C  C     . ASP   A 1 10  ? 45.53697 9.44354  30.75111  1.000 82.84281  ? 7   ASP   A C     1 
ATOM   9    O  O     . ASP   A 1 10  ? 46.60877 9.43609  30.13766  1.000 81.98240  ? 7   ASP   A O     1 
ATOM   10   C  CB    . ASP   A 1 10  ? 44.95936 7.22067  31.70180  1.000 92.52404  ? 7   ASP   A CB    1 
ATOM   11   C  CG    . ASP   A 1 10  ? 45.67664 6.17133  32.52736  1.000 96.13938  ? 7   ASP   A CG    1 
ATOM   12   O  OD1   . ASP   A 1 10  ? 46.92318 6.11062  32.46277  1.000 97.55846  ? 7   ASP   A OD1   1 
ATOM   13   O  OD2   . ASP   A 1 10  ? 44.99449 5.41116  33.24580  1.000 98.16273  ? 7   ASP   A OD2   1 
ATOM   14   N  N     . TYR   A 1 11  ? 44.47640 10.12795 30.32966  1.000 75.49271  ? 8   TYR   A N     1 
ATOM   15   C  CA    . TYR   A 1 11  ? 44.52575 10.90579 29.10263  1.000 70.07105  ? 8   TYR   A CA    1 
ATOM   16   C  C     . TYR   A 1 11  ? 45.38170 12.15543 29.28710  1.000 62.89792  ? 8   TYR   A C     1 
ATOM   17   O  O     . TYR   A 1 11  ? 45.63765 12.61376 30.40416  1.000 62.95654  ? 8   TYR   A O     1 
ATOM   18   C  CB    . TYR   A 1 11  ? 43.11997 11.30061 28.65060  1.000 70.89535  ? 8   TYR   A CB    1 
ATOM   19   C  CG    . TYR   A 1 11  ? 42.41506 10.24203 27.83514  1.000 73.46396  ? 8   TYR   A CG    1 
ATOM   20   C  CD1   . TYR   A 1 11  ? 42.86564 8.92778  27.82435  1.000 75.74827  ? 8   TYR   A CD1   1 
ATOM   21   C  CD2   . TYR   A 1 11  ? 41.30763 10.56172 27.05982  1.000 73.94905  ? 8   TYR   A CD2   1 
ATOM   22   C  CE1   . TYR   A 1 11  ? 42.22284 7.95813  27.07456  1.000 77.76722  ? 8   TYR   A CE1   1 
ATOM   23   C  CE2   . TYR   A 1 11  ? 40.66026 9.60135  26.30718  1.000 75.43496  ? 8   TYR   A CE2   1 
ATOM   24   C  CZ    . TYR   A 1 11  ? 41.12106 8.30231  26.31770  1.000 77.74812  ? 8   TYR   A CZ    1 
ATOM   25   O  OH    . TYR   A 1 11  ? 40.47607 7.34732  25.56764  1.000 79.19067  ? 8   TYR   A OH    1 
ATOM   26   N  N     . SER   A 1 12  ? 45.81623 12.71405 28.15977  1.000 56.42988  ? 9   SER   A N     1 
ATOM   27   C  CA    . SER   A 1 12  ? 46.74615 13.83461 28.15852  1.000 54.94727  ? 9   SER   A CA    1 
ATOM   28   C  C     . SER   A 1 12  ? 46.11004 15.15966 27.76046  1.000 52.70101  ? 9   SER   A C     1 
ATOM   29   O  O     . SER   A 1 12  ? 46.59755 16.21421 28.17950  1.000 50.48725  ? 9   SER   A O     1 
ATOM   30   C  CB    . SER   A 1 12  ? 47.91546 13.53955 27.21293  1.000 54.31977  ? 9   SER   A CB    1 
ATOM   31   O  OG    . SER   A 1 12  ? 48.87703 14.57417 27.25039  1.000 57.48574  ? 9   SER   A OG    1 
ATOM   32   N  N     . LEU   A 1 13  ? 45.02916 15.13703 26.97957  1.000 50.95092  ? 10  LEU   A N     1 
ATOM   33   C  CA    . LEU   A 1 13  ? 44.49185 16.34227 26.36094  1.000 50.35836  ? 10  LEU   A CA    1 
ATOM   34   C  C     . LEU   A 1 13  ? 43.33775 16.97807 27.12573  1.000 51.58640  ? 10  LEU   A C     1 
ATOM   35   O  O     . LEU   A 1 13  ? 42.87328 18.04730 26.71672  1.000 53.00180  ? 10  LEU   A O     1 
ATOM   36   C  CB    . LEU   A 1 13  ? 44.02153 16.03113 24.93550  1.000 46.55097  ? 10  LEU   A CB    1 
ATOM   37   C  CG    . LEU   A 1 13  ? 45.11010 15.70554 23.91763  1.000 50.10103  ? 10  LEU   A CG    1 
ATOM   38   C  CD1   . LEU   A 1 13  ? 44.50182 15.23037 22.60547  1.000 51.86396  ? 10  LEU   A CD1   1 
ATOM   39   C  CD2   . LEU   A 1 13  ? 46.00499 16.91862 23.69336  1.000 48.54765  ? 10  LEU   A CD2   1 
ATOM   40   N  N     . VAL   A 1 14  ? 42.88833 16.37416 28.23050  1.000 51.26587  ? 11  VAL   A N     1 
ATOM   41   C  CA    . VAL   A 1 14  ? 41.58926 16.71611 28.81443  1.000 55.40291  ? 11  VAL   A CA    1 
ATOM   42   C  C     . VAL   A 1 14  ? 41.46752 18.19614 29.16382  1.000 58.08542  ? 11  VAL   A C     1 
ATOM   43   O  O     . VAL   A 1 14  ? 40.36689 18.75991 29.11997  1.000 61.06372  ? 11  VAL   A O     1 
ATOM   44   C  CB    . VAL   A 1 14  ? 41.31521 15.82763 30.04710  1.000 54.53769  ? 11  VAL   A CB    1 
ATOM   45   C  CG1   . VAL   A 1 14  ? 41.33616 14.35906 29.65483  1.000 53.91491  ? 11  VAL   A CG1   1 
ATOM   46   C  CG2   . VAL   A 1 14  ? 42.32502 16.10240 31.14725  1.000 56.10993  ? 11  VAL   A CG2   1 
ATOM   47   N  N     . HIS   A 1 15  ? 42.57491 18.85366 29.50335  1.000 58.07330  ? 12  HIS   A N     1 
ATOM   48   C  CA    . HIS   A 1 15  ? 42.52865 20.23242 29.97564  1.000 59.20868  ? 12  HIS   A CA    1 
ATOM   49   C  C     . HIS   A 1 15  ? 42.84774 21.25886 28.89798  1.000 54.99387  ? 12  HIS   A C     1 
ATOM   50   O  O     . HIS   A 1 15  ? 42.79852 22.46040 29.17859  1.000 55.36718  ? 12  HIS   A O     1 
ATOM   51   C  CB    . HIS   A 1 15  ? 43.48818 20.42370 31.15439  1.000 65.52262  ? 12  HIS   A CB    1 
ATOM   52   C  CG    . HIS   A 1 15  ? 43.04440 19.74435 32.41158  1.000 71.57784  ? 12  HIS   A CG    1 
ATOM   53   N  ND1   . HIS   A 1 15  ? 41.79388 19.93549 32.95893  1.000 73.08973  ? 12  HIS   A ND1   1 
ATOM   54   C  CD2   . HIS   A 1 15  ? 43.68773 18.88211 33.23367  1.000 73.69862  ? 12  HIS   A CD2   1 
ATOM   55   C  CE1   . HIS   A 1 15  ? 41.68421 19.21593 34.06153  1.000 74.34662  ? 12  HIS   A CE1   1 
ATOM   56   N  NE2   . HIS   A 1 15  ? 42.81973 18.56811 34.25099  1.000 74.07762  ? 12  HIS   A NE2   1 
ATOM   57   N  N     . LYS   A 1 16  ? 43.16340 20.82709 27.68078  1.000 52.56306  ? 13  LYS   A N     1 
ATOM   58   C  CA    . LYS   A 1 16  ? 43.56199 21.75539 26.63201  1.000 52.57324  ? 13  LYS   A CA    1 
ATOM   59   C  C     . LYS   A 1 16  ? 42.34064 22.43408 26.01752  1.000 54.73638  ? 13  LYS   A C     1 
ATOM   60   O  O     . LYS   A 1 16  ? 41.34603 21.77437 25.69870  1.000 55.82456  ? 13  LYS   A O     1 
ATOM   61   C  CB    . LYS   A 1 16  ? 44.36028 21.02213 25.55571  1.000 52.49612  ? 13  LYS   A CB    1 
ATOM   62   C  CG    . LYS   A 1 16  ? 45.10521 21.94014 24.60227  1.000 51.72825  ? 13  LYS   A CG    1 
ATOM   63   C  CD    . LYS   A 1 16  ? 45.83465 21.14292 23.53730  1.000 52.31977  ? 13  LYS   A CD    1 
ATOM   64   C  CE    . LYS   A 1 16  ? 46.45712 22.05360 22.49156  1.000 54.32136  ? 13  LYS   A CE    1 
ATOM   65   N  NZ    . LYS   A 1 16  ? 46.90734 21.28699 21.29359  1.000 55.18516  ? 13  LYS   A NZ    1 
ATOM   66   N  N     . ASN   A 1 17  ? 42.42320 23.75329 25.85048  1.000 53.74271  ? 14  ASN   A N     1 
ATOM   67   C  CA    . ASN   A 1 17  ? 41.38044 24.55063 25.22023  1.000 52.38190  ? 14  ASN   A CA    1 
ATOM   68   C  C     . ASN   A 1 17  ? 41.72795 24.81609 23.76080  1.000 51.82667  ? 14  ASN   A C     1 
ATOM   69   O  O     . ASN   A 1 17  ? 42.90160 24.82724 23.37685  1.000 54.01667  ? 14  ASN   A O     1 
ATOM   70   C  CB    . ASN   A 1 17  ? 41.19725 25.88535 25.94812  1.000 51.47430  ? 14  ASN   A CB    1 
ATOM   71   C  CG    . ASN   A 1 17  ? 40.55908 25.72754 27.31126  1.000 53.00427  ? 14  ASN   A CG    1 
ATOM   72   O  OD1   . ASN   A 1 17  ? 39.54603 25.04350 27.45959  1.000 54.91105  ? 14  ASN   A OD1   1 
ATOM   73   N  ND2   . ASN   A 1 17  ? 41.15185 26.36182 28.31904  1.000 51.62158  ? 14  ASN   A ND2   1 
ATOM   74   N  N     . ILE   A 1 18  ? 40.69262 25.03254 22.94281  1.000 45.01968  ? 15  ILE   A N     1 
ATOM   75   C  CA    . ILE   A 1 18  ? 40.91004 25.47903 21.56993  1.000 43.30815  ? 15  ILE   A CA    1 
ATOM   76   C  C     . ILE   A 1 18  ? 40.75269 26.98671 21.41867  1.000 41.84469  ? 15  ILE   A C     1 
ATOM   77   O  O     . ILE   A 1 18  ? 41.06352 27.52324 20.34258  1.000 43.92744  ? 15  ILE   A O     1 
ATOM   78   C  CB    . ILE   A 1 18  ? 39.98718 24.75023 20.56840  1.000 42.39563  ? 15  ILE   A CB    1 
ATOM   79   C  CG1   . ILE   A 1 18  ? 38.52201 25.11172 20.81104  1.000 40.40987  ? 15  ILE   A CG1   1 
ATOM   80   C  CG2   . ILE   A 1 18  ? 40.19753 23.24058 20.64256  1.000 43.96525  ? 15  ILE   A CG2   1 
ATOM   81   C  CD1   . ILE   A 1 18  ? 37.60594 24.60756 19.72232  1.000 40.00002  ? 15  ILE   A CD1   1 
ATOM   82   N  N     . LEU   A 1 19  ? 40.28672 27.68485 22.45025  1.000 36.79891  ? 16  LEU   A N     1 
ATOM   83   C  CA    . LEU   A 1 19  ? 40.33536 29.13945 22.48008  1.000 38.33597  ? 16  LEU   A CA    1 
ATOM   84   C  C     . LEU   A 1 19  ? 41.66370 29.59221 23.08596  1.000 41.04823  ? 16  LEU   A C     1 
ATOM   85   O  O     . LEU   A 1 19  ? 42.36459 28.81886 23.74302  1.000 42.44442  ? 16  LEU   A O     1 
ATOM   86   C  CB    . LEU   A 1 19  ? 39.15319 29.70319 23.26867  1.000 38.34572  ? 16  LEU   A CB    1 
ATOM   87   C  CG    . LEU   A 1 19  ? 37.78062 29.23957 22.76154  1.000 37.93854  ? 16  LEU   A CG    1 
ATOM   88   C  CD1   . LEU   A 1 19  ? 36.65607 29.95241 23.49523  1.000 37.13657  ? 16  LEU   A CD1   1 
ATOM   89   C  CD2   . LEU   A 1 19  ? 37.65561 29.43638 21.25222  1.000 37.83723  ? 16  LEU   A CD2   1 
ATOM   90   N  N     . HIS   A 1 20  ? 42.01349 30.86291 22.85574  1.000 41.78097  ? 17  HIS   A N     1 
ATOM   91   C  CA    . HIS   A 1 20  ? 43.37592 31.28694 23.16982  1.000 42.96332  ? 17  HIS   A CA    1 
ATOM   92   C  C     . HIS   A 1 20  ? 43.62070 31.47130 24.66457  1.000 42.66934  ? 17  HIS   A C     1 
ATOM   93   O  O     . HIS   A 1 20  ? 44.78110 31.58162 25.07111  1.000 47.52322  ? 17  HIS   A O     1 
ATOM   94   C  CB    . HIS   A 1 20  ? 43.75444 32.56555 22.39727  1.000 45.52331  ? 17  HIS   A CB    1 
ATOM   95   C  CG    . HIS   A 1 20  ? 42.94901 33.78446 22.74524  1.000 52.97398  ? 17  HIS   A CG    1 
ATOM   96   N  ND1   . HIS   A 1 20  ? 42.47202 34.04250 24.01289  1.000 55.93452  ? 17  HIS   A ND1   1 
ATOM   97   C  CD2   . HIS   A 1 20  ? 42.57197 34.84026 21.98412  1.000 53.73158  ? 17  HIS   A CD2   1 
ATOM   98   C  CE1   . HIS   A 1 20  ? 41.81882 35.19105 24.01358  1.000 55.13264  ? 17  HIS   A CE1   1 
ATOM   99   N  NE2   . HIS   A 1 20  ? 41.86595 35.69638 22.79465  1.000 54.22126  ? 17  HIS   A NE2   1 
ATOM   100  N  N     . SER   A 1 21  ? 42.57554 31.50502 25.49014  1.000 40.75969  ? 18  SER   A N     1 
ATOM   101  C  CA    . SER   A 1 21  ? 42.76737 31.62091 26.92925  1.000 39.94378  ? 18  SER   A CA    1 
ATOM   102  C  C     . SER   A 1 21  ? 41.54894 31.07282 27.65460  1.000 39.06290  ? 18  SER   A C     1 
ATOM   103  O  O     . SER   A 1 21  ? 40.43617 31.06446 27.11812  1.000 36.54834  ? 18  SER   A O     1 
ATOM   104  C  CB    . SER   A 1 21  ? 43.01214 33.07229 27.36122  1.000 39.96643  ? 18  SER   A CB    1 
ATOM   105  O  OG    . SER   A 1 21  ? 41.83058 33.84589 27.23546  1.000 40.25895  ? 18  SER   A OG    1 
ATOM   106  N  N     . GLU   A 1 22  ? 41.77882 30.61920 28.88950  1.000 38.65281  ? 19  GLU   A N     1 
ATOM   107  C  CA    . GLU   A 1 22  ? 40.67589 30.22972 29.75877  1.000 45.55408  ? 19  GLU   A CA    1 
ATOM   108  C  C     . GLU   A 1 22  ? 39.76341 31.41327 30.05310  1.000 43.80467  ? 19  GLU   A C     1 
ATOM   109  O  O     . GLU   A 1 22  ? 38.54874 31.23839 30.21145  1.000 39.69500  ? 19  GLU   A O     1 
ATOM   110  C  CB    . GLU   A 1 22  ? 41.22732 29.64515 31.06081  1.000 51.19039  ? 19  GLU   A CB    1 
ATOM   111  C  CG    . GLU   A 1 22  ? 40.25331 28.77576 31.84644  1.000 58.26929  ? 19  GLU   A CG    1 
ATOM   112  C  CD    . GLU   A 1 22  ? 40.22874 27.33981 31.35425  1.000 68.32854  ? 19  GLU   A CD    1 
ATOM   113  O  OE1   . GLU   A 1 22  ? 39.18839 26.66733 31.51793  1.000 72.04558  ? 19  GLU   A OE1   1 
ATOM   114  O  OE2   . GLU   A 1 22  ? 41.25142 26.88199 30.80045  1.000 72.68394  ? 19  GLU   A OE2   1 
ATOM   115  N  N     . ASP   A 1 23  ? 40.33256 32.62187 30.12503  1.000 41.12306  ? 20  ASP   A N     1 
ATOM   116  C  CA    . ASP   A 1 23  ? 39.54012 33.81561 30.40845  1.000 41.25211  ? 20  ASP   A CA    1 
ATOM   117  C  C     . ASP   A 1 23  ? 38.48139 34.05620 29.33904  1.000 36.49223  ? 20  ASP   A C     1 
ATOM   118  O  O     . ASP   A 1 23  ? 37.36194 34.47979 29.64985  1.000 34.52127  ? 20  ASP   A O     1 
ATOM   119  C  CB    . ASP   A 1 23  ? 40.45625 35.03386 30.53405  1.000 44.79143  ? 20  ASP   A CB    1 
ATOM   120  C  CG    . ASP   A 1 23  ? 41.19563 35.07318 31.85774  1.000 49.04294  ? 20  ASP   A CG    1 
ATOM   121  O  OD1   . ASP   A 1 23  ? 40.98866 34.15870 32.68242  1.000 52.96157  ? 20  ASP   A OD1   1 
ATOM   122  O  OD2   . ASP   A 1 23  ? 41.97443 36.02317 32.07778  1.000 52.34379  ? 20  ASP   A OD2   1 
ATOM   123  N  N     . LEU   A 1 24  ? 38.81579 33.80447 28.07162  1.000 34.47137  ? 21  LEU   A N     1 
ATOM   124  C  CA    . LEU   A 1 24  ? 37.82758 33.98603 27.01385  1.000 33.89902  ? 21  LEU   A CA    1 
ATOM   125  C  C     . LEU   A 1 24  ? 36.71511 32.95120 27.12149  1.000 33.91670  ? 21  LEU   A C     1 
ATOM   126  O  O     . LEU   A 1 24  ? 35.53098 33.28497 26.98177  1.000 30.92230  ? 21  LEU   A O     1 
ATOM   127  C  CB    . LEU   A 1 24  ? 38.50028 33.91772 25.64157  1.000 33.97152  ? 21  LEU   A CB    1 
ATOM   128  C  CG    . LEU   A 1 24  ? 37.58472 34.20714 24.44826  1.000 33.06086  ? 21  LEU   A CG    1 
ATOM   129  C  CD1   . LEU   A 1 24  ? 36.77834 35.47978 24.69179  1.000 29.02074  ? 21  LEU   A CD1   1 
ATOM   130  C  CD2   . LEU   A 1 24  ? 38.39351 34.31579 23.15430  1.000 31.14524  ? 21  LEU   A CD2   1 
ATOM   131  N  N     . LEU   A 1 25  ? 37.07368 31.69132 27.37841  1.000 35.42535  ? 22  LEU   A N     1 
ATOM   132  C  CA    . LEU   A 1 25  ? 36.05538 30.66003 27.54390  1.000 38.10379  ? 22  LEU   A CA    1 
ATOM   133  C  C     . LEU   A 1 25  ? 35.15364 30.97107 28.73223  1.000 37.39873  ? 22  LEU   A C     1 
ATOM   134  O  O     . LEU   A 1 25  ? 33.92532 30.85616 28.64265  1.000 36.68989  ? 22  LEU   A O     1 
ATOM   135  C  CB    . LEU   A 1 25  ? 36.71438 29.29127 27.70859  1.000 38.01268  ? 22  LEU   A CB    1 
ATOM   136  C  CG    . LEU   A 1 25  ? 35.73565 28.12413 27.82438  1.000 36.95990  ? 22  LEU   A CG    1 
ATOM   137  C  CD1   . LEU   A 1 25  ? 34.69805 28.19353 26.71064  1.000 33.74242  ? 22  LEU   A CD1   1 
ATOM   138  C  CD2   . LEU   A 1 25  ? 36.48186 26.79671 27.78875  1.000 38.15019  ? 22  LEU   A CD2   1 
ATOM   139  N  N     . LYS   A 1 26  ? 35.74949 31.37612 29.85720  1.000 36.82712  ? 23  LYS   A N     1 
ATOM   140  C  CA    . LYS   A 1 26  ? 34.95060 31.69259 31.03557  1.000 40.81846  ? 23  LYS   A CA    1 
ATOM   141  C  C     . LYS   A 1 26  ? 34.06377 32.90616 30.80213  1.000 36.73664  ? 23  LYS   A C     1 
ATOM   142  O  O     . LYS   A 1 26  ? 32.94799 32.96083 31.33000  1.000 36.10290  ? 23  LYS   A O     1 
ATOM   143  C  CB    . LYS   A 1 26  ? 35.85493 31.91542 32.24737  1.000 47.94826  ? 23  LYS   A CB    1 
ATOM   144  C  CG    . LYS   A 1 26  ? 36.32136 30.63059 32.90934  1.000 53.72928  ? 23  LYS   A CG    1 
ATOM   145  C  CD    . LYS   A 1 26  ? 37.24535 30.91480 34.07975  1.000 61.09676  ? 23  LYS   A CD    1 
ATOM   146  C  CE    . LYS   A 1 26  ? 37.60622 29.63513 34.81637  1.000 65.25810  ? 23  LYS   A CE    1 
ATOM   147  N  NZ    . LYS   A 1 26  ? 37.16072 29.67347 36.23729  1.000 67.66793  ? 23  LYS   A NZ    1 
ATOM   148  N  N     . TYR   A 1 27  ? 34.53177 33.88004 30.01627  1.000 35.46857  ? 24  TYR   A N     1 
ATOM   149  C  CA    . TYR   A 1 27  ? 33.67643 35.00797 29.65875  1.000 33.90010  ? 24  TYR   A CA    1 
ATOM   150  C  C     . TYR   A 1 27  ? 32.42590 34.53091 28.92633  1.000 31.62462  ? 24  TYR   A C     1 
ATOM   151  O  O     . TYR   A 1 27  ? 31.30719 34.93573 29.25919  1.000 29.44365  ? 24  TYR   A O     1 
ATOM   152  C  CB    . TYR   A 1 27  ? 34.44265 36.02194 28.80083  1.000 31.14921  ? 24  TYR   A CB    1 
ATOM   153  C  CG    . TYR   A 1 27  ? 33.54452 37.12696 28.27902  1.000 32.51204  ? 24  TYR   A CG    1 
ATOM   154  C  CD1   . TYR   A 1 27  ? 33.26748 38.24979 29.05497  1.000 28.57275  ? 24  TYR   A CD1   1 
ATOM   155  C  CD2   . TYR   A 1 27  ? 32.94290 37.03176 27.02634  1.000 30.84639  ? 24  TYR   A CD2   1 
ATOM   156  C  CE1   . TYR   A 1 27  ? 32.43069 39.25232 28.59059  1.000 29.48574  ? 24  TYR   A CE1   1 
ATOM   157  C  CE2   . TYR   A 1 27  ? 32.10237 38.02754 26.55566  1.000 31.99439  ? 24  TYR   A CE2   1 
ATOM   158  C  CZ    . TYR   A 1 27  ? 31.84962 39.13520 27.34041  1.000 31.33622  ? 24  TYR   A CZ    1 
ATOM   159  O  OH    . TYR   A 1 27  ? 31.01486 40.12660 26.87308  1.000 29.44129  ? 24  TYR   A OH    1 
ATOM   160  N  N     . ILE   A 1 28  ? 32.60205 33.66877 27.92001  1.000 28.67662  ? 25  ILE   A N     1 
ATOM   161  C  CA    . ILE   A 1 28  ? 31.46956 33.17603 27.13585  1.000 31.15159  ? 25  ILE   A CA    1 
ATOM   162  C  C     . ILE   A 1 28  ? 30.47179 32.45835 28.03428  1.000 32.50114  ? 25  ILE   A C     1 
ATOM   163  O  O     . ILE   A 1 28  ? 29.26513 32.72798 27.99573  1.000 31.31403  ? 25  ILE   A O     1 
ATOM   164  C  CB    . ILE   A 1 28  ? 31.96055 32.25559 26.00294  1.000 33.11195  ? 25  ILE   A CB    1 
ATOM   165  C  CG1   . ILE   A 1 28  ? 32.86742 33.02066 25.03589  1.000 36.41586  ? 25  ILE   A CG1   1 
ATOM   166  C  CG2   . ILE   A 1 28  ? 30.78269 31.64468 25.25422  1.000 31.62973  ? 25  ILE   A CG2   1 
ATOM   167  C  CD1   . ILE   A 1 28  ? 33.42329 32.15323 23.91468  1.000 34.96454  ? 25  ILE   A CD1   1 
ATOM   168  N  N     . LEU   A 1 29  ? 30.96434 31.53711 28.86382  1.000 32.33872  ? 26  LEU   A N     1 
ATOM   169  C  CA    . LEU   A 1 29  ? 30.07840 30.74534 29.71051  1.000 34.30906  ? 26  LEU   A CA    1 
ATOM   170  C  C     . LEU   A 1 29  ? 29.37038 31.61859 30.74025  1.000 34.82301  ? 26  LEU   A C     1 
ATOM   171  O  O     . LEU   A 1 29  ? 28.16184 31.47909 30.96430  1.000 34.64914  ? 26  LEU   A O     1 
ATOM   172  C  CB    . LEU   A 1 29  ? 30.87506 29.63443 30.39663  1.000 35.37344  ? 26  LEU   A CB    1 
ATOM   173  C  CG    . LEU   A 1 29  ? 31.54797 28.62002 29.46934  1.000 34.56856  ? 26  LEU   A CG    1 
ATOM   174  C  CD1   . LEU   A 1 29  ? 32.54153 27.76842 30.23907  1.000 31.56591  ? 26  LEU   A CD1   1 
ATOM   175  C  CD2   . LEU   A 1 29  ? 30.50557 27.74411 28.77990  1.000 34.53577  ? 26  LEU   A CD2   1 
ATOM   176  N  N     . GLU   A 1 30  ? 30.10875 32.53444 31.37363  1.000 34.83135  ? 27  GLU   A N     1 
ATOM   177  C  CA    . GLU   A 1 30  ? 29.51718 33.35973 32.42209  1.000 33.31988  ? 27  GLU   A CA    1 
ATOM   178  C  C     . GLU   A 1 30  ? 28.58349 34.42071 31.85332  1.000 31.83037  ? 27  GLU   A C     1 
ATOM   179  O  O     . GLU   A 1 30  ? 27.60298 34.79398 32.50714  1.000 31.15789  ? 27  GLU   A O     1 
ATOM   180  C  CB    . GLU   A 1 30  ? 30.61796 34.01287 33.25599  1.000 33.92501  ? 27  GLU   A CB    1 
ATOM   181  C  CG    . GLU   A 1 30  ? 31.43032 33.02991 34.08299  1.000 38.61512  ? 27  GLU   A CG    1 
ATOM   182  C  CD    . GLU   A 1 30  ? 32.73201 33.62991 34.58174  1.000 41.95374  ? 27  GLU   A CD    1 
ATOM   183  O  OE1   . GLU   A 1 30  ? 33.06956 34.75766 34.15748  1.000 42.40732  ? 27  GLU   A OE1   1 
ATOM   184  O  OE2   . GLU   A 1 30  ? 33.41771 32.97443 35.39702  1.000 43.49031  ? 27  GLU   A OE2   1 
ATOM   185  N  N     . THR   A 1 31  ? 28.85943 34.91106 30.64653  1.000 29.26933  ? 28  THR   A N     1 
ATOM   186  C  CA    . THR   A 1 31  ? 28.05734 35.98272 30.07101  1.000 30.85872  ? 28  THR   A CA    1 
ATOM   187  C  C     . THR   A 1 31  ? 26.87270 35.46100 29.26649  1.000 35.56062  ? 28  THR   A C     1 
ATOM   188  O  O     . THR   A 1 31  ? 25.76364 35.99580 29.38317  1.000 34.82584  ? 28  THR   A O     1 
ATOM   189  C  CB    . THR   A 1 31  ? 28.92853 36.87203 29.17685  1.000 31.55659  ? 28  THR   A CB    1 
ATOM   190  O  OG1   . THR   A 1 31  ? 30.05617 37.35291 29.92344  1.000 30.86346  ? 28  THR   A OG1   1 
ATOM   191  C  CG2   . THR   A 1 31  ? 28.13015 38.05297 28.65105  1.000 31.42522  ? 28  THR   A CG2   1 
ATOM   192  N  N     . SER   A 1 32  ? 27.08197 34.41539 28.46195  1.000 33.72221  ? 29  SER   A N     1 
ATOM   193  C  CA    . SER   A 1 32  ? 26.11567 34.00728 27.45419  1.000 33.76741  ? 29  SER   A CA    1 
ATOM   194  C  C     . SER   A 1 32  ? 25.52366 32.61947 27.65464  1.000 41.04553  ? 29  SER   A C     1 
ATOM   195  O  O     . SER   A 1 32  ? 24.44667 32.35304 27.10850  1.000 44.64927  ? 29  SER   A O     1 
ATOM   196  C  CB    . SER   A 1 32  ? 26.75480 34.06219 26.05562  1.000 34.05998  ? 29  SER   A CB    1 
ATOM   197  O  OG    . SER   A 1 32  ? 27.20445 35.37111 25.74563  1.000 35.21772  ? 29  SER   A OG    1 
ATOM   198  N  N     . ALA   A 1 33  ? 26.18475 31.72872 28.39761  1.000 36.69228  ? 30  ALA   A N     1 
ATOM   199  C  CA    . ALA   A 1 33  ? 25.71680 30.35230 28.53848  1.000 33.29460  ? 30  ALA   A CA    1 
ATOM   200  C  C     . ALA   A 1 33  ? 24.97641 30.12282 29.85013  1.000 35.30982  ? 30  ALA   A C     1 
ATOM   201  O  O     . ALA   A 1 33  ? 23.77769 29.81221 29.84487  1.000 34.59620  ? 30  ALA   A O     1 
ATOM   202  C  CB    . ALA   A 1 33  ? 26.89476 29.37847 28.41451  1.000 28.65512  ? 30  ALA   A CB    1 
ATOM   203  N  N     . TYR   A 1 34  ? 25.67945 30.26107 30.97623  1.000 35.13507  ? 31  TYR   A N     1 
ATOM   204  C  CA    . TYR   A 1 34  ? 25.07971 30.01057 32.29128  1.000 37.42542  ? 31  TYR   A CA    1 
ATOM   205  C  C     . TYR   A 1 34  ? 23.79605 30.78625 32.52951  1.000 35.14580  ? 31  TYR   A C     1 
ATOM   206  O  O     . TYR   A 1 34  ? 22.82342 30.17854 33.04036  1.000 34.88955  ? 31  TYR   A O     1 
ATOM   207  C  CB    . TYR   A 1 34  ? 26.11822 30.31116 33.38400  1.000 40.16708  ? 31  TYR   A CB    1 
ATOM   208  C  CG    . TYR   A 1 34  ? 27.31405 29.37880 33.37497  1.000 45.33812  ? 31  TYR   A CG    1 
ATOM   209  C  CD1   . TYR   A 1 34  ? 27.19738 28.07025 32.91997  1.000 46.69056  ? 31  TYR   A CD1   1 
ATOM   210  C  CD2   . TYR   A 1 34  ? 28.56232 29.80952 33.81726  1.000 47.08882  ? 31  TYR   A CD2   1 
ATOM   211  C  CE1   . TYR   A 1 34  ? 28.28797 27.21345 32.91156  1.000 47.23929  ? 31  TYR   A CE1   1 
ATOM   212  C  CE2   . TYR   A 1 34  ? 29.65998 28.95874 33.81191  1.000 47.19426  ? 31  TYR   A CE2   1 
ATOM   213  C  CZ    . TYR   A 1 34  ? 29.51440 27.66324 33.35831  1.000 49.81176  ? 31  TYR   A CZ    1 
ATOM   214  O  OH    . TYR   A 1 34  ? 30.59827 26.81444 33.34831  1.000 53.80125  ? 31  TYR   A OH    1 
ATOM   215  N  N     . PRO   A 1 35  ? 23.67228 32.07542 32.20810  1.000 33.24351  ? 32  PRO   A N     1 
ATOM   216  C  CA    . PRO   A 1 35  ? 22.38983 32.76600 32.41009  1.000 31.97081  ? 32  PRO   A CA    1 
ATOM   217  C  C     . PRO   A 1 35  ? 21.25130 32.20808 31.56600  1.000 34.77989  ? 32  PRO   A C     1 
ATOM   218  O  O     . PRO   A 1 35  ? 20.08310 32.44971 31.89543  1.000 35.42154  ? 32  PRO   A O     1 
ATOM   219  C  CB    . PRO   A 1 35  ? 22.69775 34.21963 32.03456  1.000 29.25176  ? 32  PRO   A CB    1 
ATOM   220  C  CG    . PRO   A 1 35  ? 24.17328 34.34872 32.20902  1.000 29.22599  ? 32  PRO   A CG    1 
ATOM   221  C  CD    . PRO   A 1 35  ? 24.73224 33.02864 31.79696  1.000 26.42545  ? 32  PRO   A CD    1 
ATOM   222  N  N     . ARG   A 1 36  ? 21.54904 31.47687 30.49142  1.000 30.39339  ? 33  ARG   A N     1 
ATOM   223  C  CA    . ARG   A 1 36  ? 20.52715 30.90448 29.62525  1.000 32.89655  ? 33  ARG   A CA    1 
ATOM   224  C  C     . ARG   A 1 36  ? 20.34910 29.40797 29.83222  1.000 33.81846  ? 33  ARG   A C     1 
ATOM   225  O  O     . ARG   A 1 36  ? 19.55385 28.78325 29.12303  1.000 36.28634  ? 33  ARG   A O     1 
ATOM   226  C  CB    . ARG   A 1 36  ? 20.86872 31.18637 28.15901  1.000 31.88569  ? 33  ARG   A CB    1 
ATOM   227  C  CG    . ARG   A 1 36  ? 20.73320 32.64494 27.76301  1.000 31.87031  ? 33  ARG   A CG    1 
ATOM   228  C  CD    . ARG   A 1 36  ? 19.26795 33.02789 27.61205  1.000 32.62951  ? 33  ARG   A CD    1 
ATOM   229  N  NE    . ARG   A 1 36  ? 19.11034 34.39707 27.13105  1.000 31.27472  ? 33  ARG   A NE    1 
ATOM   230  C  CZ    . ARG   A 1 36  ? 18.02664 34.84671 26.50990  1.000 31.49980  ? 33  ARG   A CZ    1 
ATOM   231  N  NH1   . ARG   A 1 36  ? 17.00181 34.03257 26.29199  1.000 34.54244  ? 33  ARG   A NH1   1 
ATOM   232  N  NH2   . ARG   A 1 36  ? 17.96950 36.10689 26.10275  1.000 28.56028  ? 33  ARG   A NH2   1 
ATOM   233  N  N     . GLU   A 1 37  ? 21.06598 28.82185 30.78248  1.000 32.66225  ? 34  GLU   A N     1 
ATOM   234  C  CA    . GLU   A 1 37  ? 21.04678 27.38332 30.98300  1.000 33.51658  ? 34  GLU   A CA    1 
ATOM   235  C  C     . GLU   A 1 37  ? 19.86142 27.00363 31.85875  1.000 33.54800  ? 34  GLU   A C     1 
ATOM   236  O  O     . GLU   A 1 37  ? 19.67108 27.57340 32.93787  1.000 35.07748  ? 34  GLU   A O     1 
ATOM   237  C  CB    . GLU   A 1 37  ? 22.36044 26.93283 31.62353  1.000 34.94654  ? 34  GLU   A CB    1 
ATOM   238  C  CG    . GLU   A 1 37  ? 22.54956 25.43654 31.72440  1.000 35.39818  ? 34  GLU   A CG    1 
ATOM   239  C  CD    . GLU   A 1 37  ? 23.82853 25.07240 32.45068  1.000 38.49176  ? 34  GLU   A CD    1 
ATOM   240  O  OE1   . GLU   A 1 37  ? 24.16549 25.75399 33.44317  1.000 39.88403  ? 34  GLU   A OE1   1 
ATOM   241  O  OE2   . GLU   A 1 37  ? 24.49926 24.11083 32.02637  1.000 38.15214  ? 34  GLU   A OE2   1 
ATOM   242  N  N     . HIS   A 1 38  ? 19.05745 26.05371 31.38140  1.000 29.68713  ? 35  HIS   A N     1 
ATOM   243  C  CA    . HIS   A 1 38  ? 17.93556 25.55067 32.16110  1.000 32.39567  ? 35  HIS   A CA    1 
ATOM   244  C  C     . HIS   A 1 38  ? 18.41739 25.07883 33.52780  1.000 33.46111  ? 35  HIS   A C     1 
ATOM   245  O  O     . HIS   A 1 38  ? 19.53413 24.57234 33.67371  1.000 32.06337  ? 35  HIS   A O     1 
ATOM   246  C  CB    . HIS   A 1 38  ? 17.25354 24.40575 31.40658  1.000 34.51074  ? 35  HIS   A CB    1 
ATOM   247  C  CG    . HIS   A 1 38  ? 15.90335 24.03401 31.93962  1.000 35.76873  ? 35  HIS   A CG    1 
ATOM   248  N  ND1   . HIS   A 1 38  ? 15.73051 23.35420 33.12636  1.000 36.82350  ? 35  HIS   A ND1   1 
ATOM   249  C  CD2   . HIS   A 1 38  ? 14.66163 24.22541 31.43261  1.000 36.24279  ? 35  HIS   A CD2   1 
ATOM   250  C  CE1   . HIS   A 1 38  ? 14.44136 23.15108 33.33232  1.000 37.42203  ? 35  HIS   A CE1   1 
ATOM   251  N  NE2   . HIS   A 1 38  ? 13.77103 23.66819 32.31822  1.000 37.39788  ? 35  HIS   A NE2   1 
ATOM   252  N  N     . GLU   A 1 39  ? 17.56634 25.26570 34.53971  1.000 37.52026  ? 36  GLU   A N     1 
ATOM   253  C  CA    . GLU   A 1 39  ? 17.93196 24.88937 35.90353  1.000 44.11292  ? 36  GLU   A CA    1 
ATOM   254  C  C     . GLU   A 1 39  ? 18.31892 23.41590 35.99780  1.000 41.31357  ? 36  GLU   A C     1 
ATOM   255  O  O     . GLU   A 1 39  ? 19.27765 23.06214 36.69482  1.000 40.24911  ? 36  GLU   A O     1 
ATOM   256  C  CB    . GLU   A 1 39  ? 16.77827 25.20132 36.85617  1.000 54.09808  ? 36  GLU   A CB    1 
ATOM   257  C  CG    . GLU   A 1 39  ? 17.05577 24.84766 38.30471  1.000 66.87778  ? 36  GLU   A CG    1 
ATOM   258  C  CD    . GLU   A 1 39  ? 15.87383 25.14080 39.20797  1.000 80.77080  ? 36  GLU   A CD    1 
ATOM   259  O  OE1   . GLU   A 1 39  ? 14.79495 25.48823 38.68148  1.000 85.00240  ? 36  GLU   A OE1   1 
ATOM   260  O  OE2   . GLU   A 1 39  ? 16.02343 25.02545 40.44343  1.000 86.13916  ? 36  GLU   A OE2   1 
ATOM   261  N  N     . GLN   A 1 40  ? 17.59057 22.54090 35.29908  1.000 39.77837  ? 37  GLN   A N     1 
ATOM   262  C  CA    . GLN   A 1 40  ? 17.90602 21.11659 35.35054  1.000 41.48315  ? 37  GLN   A CA    1 
ATOM   263  C  C     . GLN   A 1 40  ? 19.17912 20.79189 34.57946  1.000 39.38971  ? 37  GLN   A C     1 
ATOM   264  O  O     . GLN   A 1 40  ? 19.85637 19.80738 34.89604  1.000 37.50763  ? 37  GLN   A O     1 
ATOM   265  C  CB    . GLN   A 1 40  ? 16.73024 20.29380 34.81938  1.000 44.45005  ? 37  GLN   A CB    1 
ATOM   266  C  CG    . GLN   A 1 40  ? 15.46229 20.45474 35.63848  1.000 45.50159  ? 37  GLN   A CG    1 
ATOM   267  C  CD    . GLN   A 1 40  ? 15.71268 20.25861 37.11930  1.000 48.60310  ? 37  GLN   A CD    1 
ATOM   268  O  OE1   . GLN   A 1 40  ? 16.35507 19.29024 37.52949  1.000 48.24497  ? 37  GLN   A OE1   1 
ATOM   269  N  NE2   . GLN   A 1 40  ? 15.22112 21.18871 37.93117  1.000 51.51622  ? 37  GLN   A NE2   1 
ATOM   270  N  N     . LEU   A 1 41  ? 19.52084 21.59499 33.56877  1.000 38.38056  ? 38  LEU   A N     1 
ATOM   271  C  CA    . LEU   A 1 41  ? 20.81427 21.42670 32.91313  1.000 36.56133  ? 38  LEU   A CA    1 
ATOM   272  C  C     . LEU   A 1 41  ? 21.95213 21.83601 33.83901  1.000 38.28765  ? 38  LEU   A C     1 
ATOM   273  O  O     . LEU   A 1 41  ? 23.01558 21.20530 33.84396  1.000 35.69898  ? 38  LEU   A O     1 
ATOM   274  C  CB    . LEU   A 1 41  ? 20.86097 22.23294 31.61560  1.000 34.14185  ? 38  LEU   A CB    1 
ATOM   275  C  CG    . LEU   A 1 41  ? 20.15723 21.61493 30.40818  1.000 36.32113  ? 38  LEU   A CG    1 
ATOM   276  C  CD1   . LEU   A 1 41  ? 20.03369 22.63895 29.27803  1.000 33.93255  ? 38  LEU   A CD1   1 
ATOM   277  C  CD2   . LEU   A 1 41  ? 20.91134 20.37374 29.94476  1.000 34.99228  ? 38  LEU   A CD2   1 
ATOM   278  N  N     . LYS   A 1 42  ? 21.74666 22.89274 34.62677  1.000 39.85389  ? 39  LYS   A N     1 
ATOM   279  C  CA    . LYS   A 1 42  ? 22.75750 23.31170 35.59085  1.000 38.42042  ? 39  LYS   A CA    1 
ATOM   280  C  C     . LYS   A 1 42  ? 23.00155 22.22451 36.63069  1.000 39.56341  ? 39  LYS   A C     1 
ATOM   281  O  O     . LYS   A 1 42  ? 24.15155 21.88916 36.93729  1.000 37.82290  ? 39  LYS   A O     1 
ATOM   282  C  CB    . LYS   A 1 42  ? 22.32542 24.61922 36.25536  1.000 42.71846  ? 39  LYS   A CB    1 
ATOM   283  C  CG    . LYS   A 1 42  ? 23.28354 25.15179 37.30790  1.000 46.48568  ? 39  LYS   A CG    1 
ATOM   284  C  CD    . LYS   A 1 42  ? 22.76984 26.47346 37.87128  1.000 51.88505  ? 39  LYS   A CD    1 
ATOM   285  C  CE    . LYS   A 1 42  ? 22.55657 26.40179 39.37338  1.000 56.24505  ? 39  LYS   A CE    1 
ATOM   286  N  NZ    . LYS   A 1 42  ? 23.84205 26.42592 40.12095  1.000 56.44934  ? 39  LYS   A NZ    1 
ATOM   287  N  N     . GLY   A 1 43  ? 21.92584 21.64912 37.17447  1.000 42.91696  ? 40  GLY   A N     1 
ATOM   288  C  CA    . GLY   A 1 43  ? 22.08648 20.58602 38.15421  1.000 44.32689  ? 40  GLY   A CA    1 
ATOM   289  C  C     . GLY   A 1 43  ? 22.76277 19.35529 37.57891  1.000 45.82831  ? 40  GLY   A C     1 
ATOM   290  O  O     . GLY   A 1 43  ? 23.61487 18.74217 38.22835  1.000 49.35522  ? 40  GLY   A O     1 
ATOM   291  N  N     . LEU   A 1 44  ? 22.39237 18.97581 36.35242  1.000 41.83026  ? 41  LEU   A N     1 
ATOM   292  C  CA    . LEU   A 1 44  ? 23.02926 17.82738 35.71645  1.000 41.68482  ? 41  LEU   A CA    1 
ATOM   293  C  C     . LEU   A 1 44  ? 24.51107 18.08694 35.47389  1.000 41.59228  ? 41  LEU   A C     1 
ATOM   294  O  O     . LEU   A 1 44  ? 25.34274 17.19243 35.66275  1.000 42.37826  ? 41  LEU   A O     1 
ATOM   295  C  CB    . LEU   A 1 44  ? 22.31559 17.48714 34.40618  1.000 41.01793  ? 41  LEU   A CB    1 
ATOM   296  C  CG    . LEU   A 1 44  ? 22.63763 16.15528 33.71786  1.000 41.71532  ? 41  LEU   A CG    1 
ATOM   297  C  CD1   . LEU   A 1 44  ? 21.44451 15.71186 32.88624  1.000 43.56341  ? 41  LEU   A CD1   1 
ATOM   298  C  CD2   . LEU   A 1 44  ? 23.88293 16.24356 32.83753  1.000 41.79360  ? 41  LEU   A CD2   1 
ATOM   299  N  N     . ARG   A 1 45  ? 24.86262 19.30469 35.05411  1.000 40.13420  ? 42  ARG   A N     1 
ATOM   300  C  CA    . ARG   A 1 45  ? 26.26731 19.61438 34.80751  1.000 39.56088  ? 42  ARG   A CA    1 
ATOM   301  C  C     . ARG   A 1 45  ? 27.07857 19.57211 36.09634  1.000 44.32901  ? 42  ARG   A C     1 
ATOM   302  O  O     . ARG   A 1 45  ? 28.20595 19.06658 36.10908  1.000 46.39176  ? 42  ARG   A O     1 
ATOM   303  C  CB    . ARG   A 1 45  ? 26.40037 20.98219 34.13913  1.000 37.63402  ? 42  ARG   A CB    1 
ATOM   304  C  CG    . ARG   A 1 45  ? 27.83850 21.48635 34.05737  1.000 36.51467  ? 42  ARG   A CG    1 
ATOM   305  C  CD    . ARG   A 1 45  ? 27.94555 22.77595 33.24532  1.000 35.28762  ? 42  ARG   A CD    1 
ATOM   306  N  NE    . ARG   A 1 45  ? 27.04878 23.81817 33.73968  1.000 35.20004  ? 42  ARG   A NE    1 
ATOM   307  C  CZ    . ARG   A 1 45  ? 27.30965 24.58568 34.79394  1.000 37.83499  ? 42  ARG   A CZ    1 
ATOM   308  N  NH1   . ARG   A 1 45  ? 28.44276 24.42482 35.46437  1.000 38.88051  ? 42  ARG   A NH1   1 
ATOM   309  N  NH2   . ARG   A 1 45  ? 26.44114 25.51196 35.17974  1.000 35.72497  ? 42  ARG   A NH2   1 
ATOM   310  N  N     . GLU   A 1 46  ? 26.51440 20.07774 37.19451  1.000 47.11161  ? 43  GLU   A N     1 
ATOM   311  C  CA    . GLU   A 1 46  ? 27.26983 20.16489 38.44030  1.000 52.83786  ? 43  GLU   A CA    1 
ATOM   312  C  C     . GLU   A 1 46  ? 27.57686 18.78545 39.01048  1.000 53.88367  ? 43  GLU   A C     1 
ATOM   313  O  O     . GLU   A 1 46  ? 28.68349 18.54787 39.50867  1.000 51.64898  ? 43  GLU   A O     1 
ATOM   314  C  CB    . GLU   A 1 46  ? 26.50896 21.02077 39.45191  1.000 57.72976  ? 43  GLU   A CB    1 
ATOM   315  C  CG    . GLU   A 1 46  ? 26.51663 22.50279 39.11244  1.000 60.38380  ? 43  GLU   A CG    1 
ATOM   316  C  CD    . GLU   A 1 46  ? 25.71558 23.33417 40.09219  1.000 66.69611  ? 43  GLU   A CD    1 
ATOM   317  O  OE1   . GLU   A 1 46  ? 24.93070 22.75019 40.86944  1.000 69.74499  ? 43  GLU   A OE1   1 
ATOM   318  O  OE2   . GLU   A 1 46  ? 25.87121 24.57361 40.08447  1.000 67.62000  ? 43  GLU   A OE2   1 
ATOM   319  N  N     A VAL   A 1 47  ? 26.62313 17.85177 38.93078  0.150 54.15779  ? 44  VAL   A N     1 
ATOM   320  N  N     B VAL   A 1 47  ? 26.60373 17.87116 38.96942  0.850 53.86854  ? 44  VAL   A N     1 
ATOM   321  C  CA    A VAL   A 1 47  ? 26.89144 16.50390 39.42392  0.150 54.55264  ? 44  VAL   A CA    1 
ATOM   322  C  CA    B VAL   A 1 47  ? 26.85996 16.49944 39.39577  0.850 54.41269  ? 44  VAL   A CA    1 
ATOM   323  C  C     A VAL   A 1 47  ? 27.82445 15.75640 38.47771  0.150 52.62373  ? 44  VAL   A C     1 
ATOM   324  C  C     B VAL   A 1 47  ? 27.90058 15.85255 38.49186  0.850 52.88491  ? 44  VAL   A C     1 
ATOM   325  O  O     A VAL   A 1 47  ? 28.59508 14.89130 38.91193  0.150 53.14964  ? 44  VAL   A O     1 
ATOM   326  O  O     B VAL   A 1 47  ? 28.81985 15.17081 38.96228  0.850 53.53329  ? 44  VAL   A O     1 
ATOM   327  C  CB    A VAL   A 1 47  ? 25.57709 15.73023 39.65089  0.150 55.88262  ? 44  VAL   A CB    1 
ATOM   328  C  CB    B VAL   A 1 47  ? 25.54767 15.69231 39.41538  0.850 55.71927  ? 44  VAL   A CB    1 
ATOM   329  C  CG1   A VAL   A 1 47  ? 24.72835 16.41877 40.71068  0.150 58.30480  ? 44  VAL   A CG1   1 
ATOM   330  C  CG1   B VAL   A 1 47  ? 25.81783 14.24276 39.77868  0.850 56.00529  ? 44  VAL   A CG1   1 
ATOM   331  C  CG2   A VAL   A 1 47  ? 24.80121 15.58213 38.35182  0.150 55.05868  ? 44  VAL   A CG2   1 
ATOM   332  C  CG2   B VAL   A 1 47  ? 24.55852 16.31195 40.38869  0.850 58.25939  ? 44  VAL   A CG2   1 
ATOM   333  N  N     . THR   A 1 48  ? 27.78473 16.07561 37.18092  1.000 49.27551  ? 45  THR   A N     1 
ATOM   334  C  CA    . THR   A 1 48  ? 28.66263 15.40106 36.23000  1.000 49.44146  ? 45  THR   A CA    1 
ATOM   335  C  C     . THR   A 1 48  ? 30.09988 15.89875 36.34298  1.000 51.98422  ? 45  THR   A C     1 
ATOM   336  O  O     . THR   A 1 48  ? 31.04633 15.11963 36.17101  1.000 50.90529  ? 45  THR   A O     1 
ATOM   337  C  CB    . THR   A 1 48  ? 28.13465 15.59047 34.80848  1.000 45.23204  ? 45  THR   A CB    1 
ATOM   338  O  OG1   . THR   A 1 48  ? 26.80863 15.05849 34.71890  1.000 45.25782  ? 45  THR   A OG1   1 
ATOM   339  C  CG2   . THR   A 1 48  ? 29.01954 14.87177 33.80909  1.000 43.74471  ? 45  THR   A CG2   1 
ATOM   340  N  N     A GLU   A 1 49  ? 30.27697 17.19418 36.62797  0.500 53.56506  ? 46  GLU   A N     1 
ATOM   341  N  N     B GLU   A 1 49  ? 30.29416 17.18745 36.63276  0.500 53.55361  ? 46  GLU   A N     1 
ATOM   342  C  CA    A GLU   A 1 49  ? 31.60704 17.76040 36.82795  0.500 53.22158  ? 46  GLU   A CA    1 
ATOM   343  C  CA    B GLU   A 1 49  ? 31.65512 17.69283 36.78031  0.500 53.13054  ? 46  GLU   A CA    1 
ATOM   344  C  C     A GLU   A 1 49  ? 32.37102 17.06000 37.94403  0.500 55.21070  ? 46  GLU   A C     1 
ATOM   345  C  C     B GLU   A 1 49  ? 32.39218 17.02901 37.93640  0.500 55.18230  ? 46  GLU   A C     1 
ATOM   346  O  O     A GLU   A 1 49  ? 33.60615 17.10443 37.95857  0.500 55.20023  ? 46  GLU   A O     1 
ATOM   347  O  O     B GLU   A 1 49  ? 33.62733 17.06290 37.96975  0.500 55.19954  ? 46  GLU   A O     1 
ATOM   348  C  CB    A GLU   A 1 49  ? 31.49994 19.25843 37.13011  0.500 52.44823  ? 46  GLU   A CB    1 
ATOM   349  C  CB    B GLU   A 1 49  ? 31.64811 19.21245 36.95917  0.500 52.21395  ? 46  GLU   A CB    1 
ATOM   350  C  CG    A GLU   A 1 49  ? 31.16252 20.12278 35.91839  0.500 50.54835  ? 46  GLU   A CG    1 
ATOM   351  C  CG    B GLU   A 1 49  ? 31.23856 19.98746 35.70742  0.500 50.39118  ? 46  GLU   A CG    1 
ATOM   352  C  CD    A GLU   A 1 49  ? 30.79128 21.54975 36.29282  0.500 49.43165  ? 46  GLU   A CD    1 
ATOM   353  C  CD    B GLU   A 1 49  ? 32.34773 20.09662 34.66421  0.500 48.49762  ? 46  GLU   A CD    1 
ATOM   354  O  OE1   A GLU   A 1 49  ? 30.44606 21.78846 37.46986  0.500 49.20060  ? 46  GLU   A OE1   1 
ATOM   355  O  OE1   B GLU   A 1 49  ? 32.27873 21.02168 33.82657  0.500 46.82276  ? 46  GLU   A OE1   1 
ATOM   356  O  OE2   A GLU   A 1 49  ? 30.84240 22.43289 35.40842  0.500 44.83790  ? 46  GLU   A OE2   1 
ATOM   357  O  OE2   B GLU   A 1 49  ? 33.28360 19.26884 34.67557  0.500 47.71512  ? 46  GLU   A OE2   1 
ATOM   358  N  N     . LYS   A 1 50  ? 31.66776 16.41891 38.87601  1.000 67.18851  ? 47  LYS   A N     1 
ATOM   359  C  CA    . LYS   A 1 50  ? 32.29711 15.63836 39.93157  1.000 69.22295  ? 47  LYS   A CA    1 
ATOM   360  C  C     . LYS   A 1 50  ? 32.61838 14.21394 39.49850  1.000 66.04161  ? 47  LYS   A C     1 
ATOM   361  O  O     . LYS   A 1 50  ? 33.34196 13.51547 40.21502  1.000 67.55934  ? 47  LYS   A O     1 
ATOM   362  C  CB    . LYS   A 1 50  ? 31.39800 15.58831 41.17120  1.000 73.12598  ? 47  LYS   A CB    1 
ATOM   363  C  CG    . LYS   A 1 50  ? 30.98621 16.94299 41.72691  1.000 76.57204  ? 47  LYS   A CG    1 
ATOM   364  C  CD    . LYS   A 1 50  ? 30.19479 16.76098 43.01707  1.000 80.25156  ? 47  LYS   A CD    1 
ATOM   365  C  CE    . LYS   A 1 50  ? 29.49344 18.04151 43.44050  1.000 80.72138  ? 47  LYS   A CE    1 
ATOM   366  N  NZ    . LYS   A 1 50  ? 30.44612 19.16125 43.67741  1.000 81.05359  ? 47  LYS   A NZ    1 
ATOM   367  N  N     . HIS   A 1 51  ? 32.09716 13.76672 38.35912  1.000 62.56630  ? 48  HIS   A N     1 
ATOM   368  C  CA    . HIS   A 1 51  ? 32.32325 12.40790 37.89482  1.000 57.90601  ? 48  HIS   A CA    1 
ATOM   369  C  C     . HIS   A 1 51  ? 33.72391 12.27218 37.30290  1.000 57.30473  ? 48  HIS   A C     1 
ATOM   370  O  O     . HIS   A 1 51  ? 34.33975 13.24674 36.86261  1.000 56.45944  ? 48  HIS   A O     1 
ATOM   371  C  CB    . HIS   A 1 51  ? 31.26693 12.01470 36.85991  1.000 57.00325  ? 48  HIS   A CB    1 
ATOM   372  C  CG    . HIS   A 1 51  ? 31.19178 10.54351 36.59714  1.000 58.93392  ? 48  HIS   A CG    1 
ATOM   373  N  ND1   . HIS   A 1 51  ? 31.93929 9.92217  35.61983  1.000 60.27883  ? 48  HIS   A ND1   1 
ATOM   374  C  CD2   . HIS   A 1 51  ? 30.45215 9.57069  37.18045  1.000 59.69690  ? 48  HIS   A CD2   1 
ATOM   375  C  CE1   . HIS   A 1 51  ? 31.66636 8.62938  35.61500  1.000 60.57775  ? 48  HIS   A CE1   1 
ATOM   376  N  NE2   . HIS   A 1 51  ? 30.76731 8.39000  36.55254  1.000 60.18046  ? 48  HIS   A NE2   1 
ATOM   377  N  N     . GLU   A 1 52  ? 34.22459 11.03359 37.29705  1.000 58.38156  ? 49  GLU   A N     1 
ATOM   378  C  CA    . GLU   A 1 52  ? 35.58059 10.77694 36.82010  1.000 58.76005  ? 49  GLU   A CA    1 
ATOM   379  C  C     . GLU   A 1 52  ? 35.73242 11.07577 35.33374  1.000 56.70323  ? 49  GLU   A C     1 
ATOM   380  O  O     . GLU   A 1 52  ? 36.81078 11.49464 34.89613  1.000 56.92643  ? 49  GLU   A O     1 
ATOM   381  C  CB    . GLU   A 1 52  ? 35.96877 9.32717  37.10959  1.000 65.88410  ? 49  GLU   A CB    1 
ATOM   382  C  CG    . GLU   A 1 52  ? 34.84892 8.33334  36.84546  1.000 73.17741  ? 49  GLU   A CG    1 
ATOM   383  C  CD    . GLU   A 1 52  ? 35.29912 6.89254  36.98161  1.000 78.22432  ? 49  GLU   A CD    1 
ATOM   384  O  OE1   . GLU   A 1 52  ? 36.43039 6.58091  36.55288  1.000 79.25063  ? 49  GLU   A OE1   1 
ATOM   385  O  OE2   . GLU   A 1 52  ? 34.52373 6.07372  37.52146  1.000 79.04877  ? 49  GLU   A OE2   1 
ATOM   386  N  N     . TRP   A 1 53  ? 34.67638 10.87103 34.54580  1.000 53.49958  ? 50  TRP   A N     1 
ATOM   387  C  CA    . TRP   A 1 53  ? 34.71498 11.09377 33.10702  1.000 53.08448  ? 50  TRP   A CA    1 
ATOM   388  C  C     . TRP   A 1 53  ? 34.13858 12.44483 32.70391  1.000 49.71393  ? 50  TRP   A C     1 
ATOM   389  O  O     . TRP   A 1 53  ? 33.67177 12.59640 31.57022  1.000 49.30641  ? 50  TRP   A O     1 
ATOM   390  C  CB    . TRP   A 1 53  ? 33.97991 9.96843  32.37849  1.000 57.64144  ? 50  TRP   A CB    1 
ATOM   391  C  CG    . TRP   A 1 53  ? 34.84053 8.77333  32.15839  1.000 65.73498  ? 50  TRP   A CG    1 
ATOM   392  C  CD1   . TRP   A 1 53  ? 34.75067 7.56804  32.78886  1.000 69.34002  ? 50  TRP   A CD1   1 
ATOM   393  C  CD2   . TRP   A 1 53  ? 35.94390 8.67324  31.25201  1.000 70.65064  ? 50  TRP   A CD2   1 
ATOM   394  N  NE1   . TRP   A 1 53  ? 35.72557 6.71864  32.32438  1.000 72.64064  ? 50  TRP   A NE1   1 
ATOM   395  C  CE2   . TRP   A 1 53  ? 36.47221 7.37382  31.38036  1.000 73.27704  ? 50  TRP   A CE2   1 
ATOM   396  C  CE3   . TRP   A 1 53  ? 36.53429 9.55607  30.34106  1.000 73.16768  ? 50  TRP   A CE3   1 
ATOM   397  C  CZ2   . TRP   A 1 53  ? 37.56350 6.93397  30.63242  1.000 75.24806  ? 50  TRP   A CZ2   1 
ATOM   398  C  CZ3   . TRP   A 1 53  ? 37.61751 9.11794  29.59924  1.000 74.90620  ? 50  TRP   A CZ3   1 
ATOM   399  C  CH2   . TRP   A 1 53  ? 38.12084 7.81850  29.75017  1.000 75.52825  ? 50  TRP   A CH2   1 
ATOM   400  N  N     . SER   A 1 54  ? 34.17536 13.43189 33.60306  1.000 48.27669  ? 51  SER   A N     1 
ATOM   401  C  CA    . SER   A 1 54  ? 33.61697 14.74797 33.31113  1.000 49.61994  ? 51  SER   A CA    1 
ATOM   402  C  C     . SER   A 1 54  ? 34.26164 15.40927 32.09771  1.000 54.25748  ? 51  SER   A C     1 
ATOM   403  O  O     . SER   A 1 54  ? 33.71918 16.39580 31.58552  1.000 56.15836  ? 51  SER   A O     1 
ATOM   404  C  CB    . SER   A 1 54  ? 33.76684 15.65416 34.53322  1.000 48.16160  ? 51  SER   A CB    1 
ATOM   405  O  OG    . SER   A 1 54  ? 35.13281 15.80453 34.88233  1.000 49.45749  ? 51  SER   A OG    1 
ATOM   406  N  N     . THR   A 1 55  ? 35.40266 14.89383 31.63006  1.000 54.81023  ? 52  THR   A N     1 
ATOM   407  C  CA    . THR   A 1 55  ? 36.06999 15.48558 30.47452  1.000 51.71068  ? 52  THR   A CA    1 
ATOM   408  C  C     . THR   A 1 55  ? 35.20326 15.39709 29.22131  1.000 47.81397  ? 52  THR   A C     1 
ATOM   409  O  O     . THR   A 1 55  ? 35.21887 16.30619 28.38222  1.000 45.80137  ? 52  THR   A O     1 
ATOM   410  C  CB    . THR   A 1 55  ? 37.42160 14.80465 30.24586  1.000 53.42406  ? 52  THR   A CB    1 
ATOM   411  O  OG1   . THR   A 1 55  ? 38.04004 15.33649 29.06725  1.000 58.78579  ? 52  THR   A OG1   1 
ATOM   412  C  CG2   . THR   A 1 55  ? 37.24860 13.30105 30.08470  1.000 53.36159  ? 52  THR   A CG2   1 
ATOM   413  N  N     . ALA   A 1 56  ? 34.42563 14.32024 29.08460  1.000 46.16660  ? 53  ALA   A N     1 
ATOM   414  C  CA    . ALA   A 1 56  ? 33.61775 14.10944 27.89060  1.000 42.34274  ? 53  ALA   A CA    1 
ATOM   415  C  C     . ALA   A 1 56  ? 32.32697 14.91740 27.89489  1.000 40.46188  ? 53  ALA   A C     1 
ATOM   416  O  O     . ALA   A 1 56  ? 31.59835 14.89288 26.89719  1.000 37.69069  ? 53  ALA   A O     1 
ATOM   417  C  CB    . ALA   A 1 56  ? 33.29851 12.62025 27.73434  1.000 41.31262  ? 53  ALA   A CB    1 
ATOM   418  N  N     . LEU   A 1 57  ? 32.03855 15.63080 28.98180  1.000 41.86582  ? 54  LEU   A N     1 
ATOM   419  C  CA    . LEU   A 1 57  ? 30.79197 16.37612 29.10901  1.000 38.93790  ? 54  LEU   A CA    1 
ATOM   420  C  C     . LEU   A 1 57  ? 30.70264 17.47688 28.05670  1.000 35.73038  ? 54  LEU   A C     1 
ATOM   421  O  O     . LEU   A 1 57  ? 31.64704 18.24730 27.86498  1.000 34.99080  ? 54  LEU   A O     1 
ATOM   422  C  CB    . LEU   A 1 57  ? 30.70249 16.97009 30.51607  1.000 39.98919  ? 54  LEU   A CB    1 
ATOM   423  C  CG    . LEU   A 1 57  ? 29.51890 17.84356 30.92862  1.000 40.72859  ? 54  LEU   A CG    1 
ATOM   424  C  CD1   . LEU   A 1 57  ? 28.21305 17.06491 30.86596  1.000 39.40528  ? 54  LEU   A CD1   1 
ATOM   425  C  CD2   . LEU   A 1 57  ? 29.75563 18.39871 32.32992  1.000 39.91145  ? 54  LEU   A CD2   1 
ATOM   426  N  N     . VAL   A 1 58  ? 29.56785 17.54373 27.37025  1.000 35.43911  ? 55  VAL   A N     1 
ATOM   427  C  CA    . VAL   A 1 58  ? 29.34494 18.62241 26.39866  1.000 35.43765  ? 55  VAL   A CA    1 
ATOM   428  C  C     . VAL   A 1 58  ? 29.27623 19.95317 27.13871  1.000 36.36246  ? 55  VAL   A C     1 
ATOM   429  O  O     . VAL   A 1 58  ? 28.48900 20.08767 28.09281  1.000 36.99114  ? 55  VAL   A O     1 
ATOM   430  C  CB    . VAL   A 1 58  ? 28.06498 18.36413 25.59922  1.000 32.80625  ? 55  VAL   A CB    1 
ATOM   431  C  CG1   . VAL   A 1 58  ? 27.55442 19.65780 24.96438  1.000 30.50890  ? 55  VAL   A CG1   1 
ATOM   432  C  CG2   . VAL   A 1 58  ? 28.32173 17.31774 24.52745  1.000 32.39273  ? 55  VAL   A CG2   1 
ATOM   433  N  N     . PRO   A 1 59  ? 30.07280 20.94998 26.76204  1.000 34.77409  ? 56  PRO   A N     1 
ATOM   434  C  CA    . PRO   A 1 59  ? 30.08596 22.21772 27.50008  1.000 34.16574  ? 56  PRO   A CA    1 
ATOM   435  C  C     . PRO   A 1 59  ? 28.83095 23.04951 27.25592  1.000 34.76659  ? 56  PRO   A C     1 
ATOM   436  O  O     . PRO   A 1 59  ? 28.10055 22.86260 26.28209  1.000 37.21890  ? 56  PRO   A O     1 
ATOM   437  C  CB    . PRO   A 1 59  ? 31.33540 22.92987 26.96609  1.000 31.22839  ? 56  PRO   A CB    1 
ATOM   438  C  CG    . PRO   A 1 59  ? 31.57109 22.32425 25.61970  1.000 33.94354  ? 56  PRO   A CG    1 
ATOM   439  C  CD    . PRO   A 1 59  ? 31.11158 20.89447 25.71839  1.000 31.28729  ? 56  PRO   A CD    1 
ATOM   440  N  N     . ALA   A 1 60  ? 28.60996 24.00374 28.16724  1.000 32.55684  ? 57  ALA   A N     1 
ATOM   441  C  CA    . ALA   A 1 60  ? 27.34201 24.72960 28.21603  1.000 35.69766  ? 57  ALA   A CA    1 
ATOM   442  C  C     . ALA   A 1 60  ? 27.14163 25.61476 26.99256  1.000 37.26916  ? 57  ALA   A C     1 
ATOM   443  O  O     . ALA   A 1 60  ? 26.01319 25.76427 26.50933  1.000 37.52066  ? 57  ALA   A O     1 
ATOM   444  C  CB    . ALA   A 1 60  ? 27.26627 25.57020 29.49105  1.000 33.27482  ? 57  ALA   A CB    1 
ATOM   445  N  N     . ASP   A 1 61  ? 28.21342 26.23457 26.48959  1.000 33.93760  ? 58  ASP   A N     1 
ATOM   446  C  CA    . ASP   A 1 61  ? 28.05560 27.09758 25.32138  1.000 31.97735  ? 58  ASP   A CA    1 
ATOM   447  C  C     . ASP   A 1 61  ? 27.73070 26.27920 24.07933  1.000 31.42359  ? 58  ASP   A C     1 
ATOM   448  O  O     . ASP   A 1 61  ? 26.88402 26.68067 23.26891  1.000 28.30022  ? 58  ASP   A O     1 
ATOM   449  C  CB    . ASP   A 1 61  ? 29.30745 27.94963 25.10215  1.000 34.23374  ? 58  ASP   A CB    1 
ATOM   450  C  CG    . ASP   A 1 61  ? 30.53668 27.12121 24.76010  1.000 42.26913  ? 58  ASP   A CG    1 
ATOM   451  O  OD1   . ASP   A 1 61  ? 30.68120 26.00392 25.30415  1.000 42.69381  ? 58  ASP   A OD1   1 
ATOM   452  O  OD2   . ASP   A 1 61  ? 31.36135 27.59542 23.94677  1.000 39.61525  ? 58  ASP   A OD2   1 
ATOM   453  N  N     . GLU   A 1 62  ? 28.36845 25.11242 23.92876  1.000 28.03021  ? 59  GLU   A N     1 
ATOM   454  C  CA    . GLU   A 1 62  ? 28.01230 24.22603 22.82665  1.000 29.52896  ? 59  GLU   A CA    1 
ATOM   455  C  C     . GLU   A 1 62  ? 26.57777 23.72833 22.96613  1.000 31.14088  ? 59  GLU   A C     1 
ATOM   456  O  O     . GLU   A 1 62  ? 25.87664 23.54455 21.96258  1.000 29.68641  ? 59  GLU   A O     1 
ATOM   457  C  CB    . GLU   A 1 62  ? 28.98307 23.04811 22.74777  1.000 28.31384  ? 59  GLU   A CB    1 
ATOM   458  C  CG    . GLU   A 1 62  ? 28.64586 22.07980 21.62225  1.000 31.51145  ? 59  GLU   A CG    1 
ATOM   459  C  CD    . GLU   A 1 62  ? 29.56317 20.87191 21.57710  1.000 38.26561  ? 59  GLU   A CD    1 
ATOM   460  O  OE1   . GLU   A 1 62  ? 30.71081 20.96739 22.06167  1.000 38.62719  ? 59  GLU   A OE1   1 
ATOM   461  O  OE2   . GLU   A 1 62  ? 29.13026 19.82442 21.05209  1.000 40.64338  ? 59  GLU   A OE2   1 
ATOM   462  N  N     . GLY   A 1 63  ? 26.11912 23.51724 24.20262  1.000 29.99289  ? 60  GLY   A N     1 
ATOM   463  C  CA    . GLY   A 1 63  ? 24.75426 23.05307 24.40608  1.000 30.98980  ? 60  GLY   A CA    1 
ATOM   464  C  C     . GLY   A 1 63  ? 23.72049 24.02019 23.85778  1.000 32.98292  ? 60  GLY   A C     1 
ATOM   465  O  O     . GLY   A 1 63  ? 22.77860 23.61776 23.17161  1.000 34.43905  ? 60  GLY   A O     1 
ATOM   466  N  N     . LEU   A 1 64  ? 23.89156 25.31408 24.14931  1.000 33.22341  ? 61  LEU   A N     1 
ATOM   467  C  CA    . LEU   A 1 64  ? 22.98678 26.32115 23.60374  1.000 30.74511  ? 61  LEU   A CA    1 
ATOM   468  C  C     . LEU   A 1 64  ? 23.06240 26.38083 22.08440  1.000 31.23495  ? 61  LEU   A C     1 
ATOM   469  O  O     . LEU   A 1 64  ? 22.06366 26.69062 21.42517  1.000 34.69367  ? 61  LEU   A O     1 
ATOM   470  C  CB    . LEU   A 1 64  ? 23.30167 27.68957 24.20289  1.000 29.03060  ? 61  LEU   A CB    1 
ATOM   471  C  CG    . LEU   A 1 64  ? 22.86286 27.88769 25.65304  1.000 33.33306  ? 61  LEU   A CG    1 
ATOM   472  C  CD1   . LEU   A 1 64  ? 23.36104 29.22831 26.16004  1.000 35.75001  ? 61  LEU   A CD1   1 
ATOM   473  C  CD2   . LEU   A 1 64  ? 21.34415 27.78691 25.77619  1.000 27.91355  ? 61  LEU   A CD2   1 
ATOM   474  N  N     . PHE   A 1 65  ? 24.23420 26.10108 21.51337  1.000 29.22864  ? 62  PHE   A N     1 
ATOM   475  C  CA    . PHE   A 1 65  ? 24.36461 26.05016 20.06017  1.000 28.69999  ? 62  PHE   A CA    1 
ATOM   476  C  C     . PHE   A 1 65  ? 23.56161 24.89245 19.47703  1.000 30.57954  ? 62  PHE   A C     1 
ATOM   477  O  O     . PHE   A 1 65  ? 22.85211 25.05741 18.47685  1.000 30.60111  ? 62  PHE   A O     1 
ATOM   478  C  CB    . PHE   A 1 65  ? 25.83975 25.93356 19.67918  1.000 32.31068  ? 62  PHE   A CB    1 
ATOM   479  C  CG    . PHE   A 1 65  ? 26.07712 25.73900 18.21293  1.000 36.74915  ? 62  PHE   A CG    1 
ATOM   480  C  CD1   . PHE   A 1 65  ? 25.60175 26.65653 17.29443  1.000 42.39259  ? 62  PHE   A CD1   1 
ATOM   481  C  CD2   . PHE   A 1 65  ? 26.78966 24.64402 17.75454  1.000 42.59252  ? 62  PHE   A CD2   1 
ATOM   482  C  CE1   . PHE   A 1 65  ? 25.82108 26.47921 15.94260  1.000 48.51493  ? 62  PHE   A CE1   1 
ATOM   483  C  CE2   . PHE   A 1 65  ? 27.01715 24.46251 16.40407  1.000 45.67831  ? 62  PHE   A CE2   1 
ATOM   484  C  CZ    . PHE   A 1 65  ? 26.53428 25.38187 15.49828  1.000 48.82409  ? 62  PHE   A CZ    1 
ATOM   485  N  N     . LEU   A 1 66  ? 23.66891 23.70728 20.08757  1.000 29.03085  ? 63  LEU   A N     1 
ATOM   486  C  CA    . LEU   A 1 66  ? 22.87439 22.56763 19.63830  1.000 33.23108  ? 63  LEU   A CA    1 
ATOM   487  C  C     . LEU   A 1 66  ? 21.38399 22.86045 19.74768  1.000 30.76694  ? 63  LEU   A C     1 
ATOM   488  O  O     . LEU   A 1 66  ? 20.61063 22.53154 18.84029  1.000 29.28323  ? 63  LEU   A O     1 
ATOM   489  C  CB    . LEU   A 1 66  ? 23.22778 21.32163 20.45118  1.000 36.49397  ? 63  LEU   A CB    1 
ATOM   490  C  CG    . LEU   A 1 66  ? 24.68956 20.87638 20.46204  1.000 37.98558  ? 63  LEU   A CG    1 
ATOM   491  C  CD1   . LEU   A 1 66  ? 24.85827 19.61813 21.30529  1.000 37.52778  ? 63  LEU   A CD1   1 
ATOM   492  C  CD2   . LEU   A 1 66  ? 25.18725 20.65452 19.04734  1.000 27.25817  ? 63  LEU   A CD2   1 
ATOM   493  N  N     . SER   A 1 67  ? 20.96532 23.47974 20.85511  1.000 32.12204  ? 64  SER   A N     1 
ATOM   494  C  CA    . SER   A 1 67  ? 19.55663 23.81820 21.04404  1.000 34.07647  ? 64  SER   A CA    1 
ATOM   495  C  C     . SER   A 1 67  ? 19.08293 24.83083 20.00819  1.000 35.46681  ? 64  SER   A C     1 
ATOM   496  O  O     . SER   A 1 67  ? 17.95202 24.74071 19.51324  1.000 34.22365  ? 64  SER   A O     1 
ATOM   497  C  CB    . SER   A 1 67  ? 19.33677 24.35757 22.45891  1.000 33.19778  ? 64  SER   A CB    1 
ATOM   498  O  OG    . SER   A 1 67  ? 18.00380 24.80255 22.63853  1.000 34.91295  ? 64  SER   A OG    1 
ATOM   499  N  N     . MET   A 1 68  ? 19.93240 25.80809 19.67445  1.000 32.53422  ? 65  MET   A N     1 
ATOM   500  C  CA    . MET   A 1 68  ? 19.56568 26.80024 18.66859  1.000 29.62353  ? 65  MET   A CA    1 
ATOM   501  C  C     . MET   A 1 68  ? 19.39636 26.16217 17.29365  1.000 32.84691  ? 65  MET   A C     1 
ATOM   502  O  O     . MET   A 1 68  ? 18.47216 26.51250 16.54992  1.000 37.29509  ? 65  MET   A O     1 
ATOM   503  C  CB    . MET   A 1 68  ? 20.61631 27.90804 18.62070  1.000 31.54041  ? 65  MET   A CB    1 
ATOM   504  C  CG    . MET   A 1 68  ? 20.36741 28.95849 17.54487  1.000 33.17938  ? 65  MET   A CG    1 
ATOM   505  S  SD    . MET   A 1 68  ? 18.93498 30.00931 17.88484  1.000 37.46833  ? 65  MET   A SD    1 
ATOM   506  C  CE    . MET   A 1 68  ? 19.51227 30.93596 19.31123  1.000 23.25989  ? 65  MET   A CE    1 
ATOM   507  N  N     . LEU   A 1 69  ? 20.28228 25.22703 16.93645  1.000 31.07405  ? 66  LEU   A N     1 
ATOM   508  C  CA    . LEU   A 1 69  ? 20.16657 24.53788 15.65348  1.000 34.17786  ? 66  LEU   A CA    1 
ATOM   509  C  C     . LEU   A 1 69  ? 18.85759 23.76370 15.56086  1.000 34.08130  ? 66  LEU   A C     1 
ATOM   510  O  O     . LEU   A 1 69  ? 18.16785 23.80597 14.53548  1.000 29.83438  ? 66  LEU   A O     1 
ATOM   511  C  CB    . LEU   A 1 69  ? 21.35422 23.59512 15.44994  1.000 35.82740  ? 66  LEU   A CB    1 
ATOM   512  C  CG    . LEU   A 1 69  ? 22.70096 24.22662 15.09672  1.000 42.60168  ? 66  LEU   A CG    1 
ATOM   513  C  CD1   . LEU   A 1 69  ? 23.79927 23.17869 15.07118  1.000 43.63259  ? 66  LEU   A CD1   1 
ATOM   514  C  CD2   . LEU   A 1 69  ? 22.61302 24.91676 13.75781  1.000 44.76533  ? 66  LEU   A CD2   1 
ATOM   515  N  N     . LEU   A 1 70  ? 18.51153 23.03394 16.62402  1.000 34.53742  ? 67  LEU   A N     1 
ATOM   516  C  CA    . LEU   A 1 70  ? 17.27765 22.25675 16.63963  1.000 32.37093  ? 67  LEU   A CA    1 
ATOM   517  C  C     . LEU   A 1 70  ? 16.06299 23.14019 16.38842  1.000 33.99783  ? 67  LEU   A C     1 
ATOM   518  O  O     . LEU   A 1 70  ? 15.19734 22.80999 15.56990  1.000 37.42443  ? 67  LEU   A O     1 
ATOM   519  C  CB    . LEU   A 1 70  ? 17.14171 21.53078 17.97828  1.000 33.41720  ? 67  LEU   A CB    1 
ATOM   520  C  CG    . LEU   A 1 70  ? 18.10292 20.36786 18.21779  1.000 36.83872  ? 67  LEU   A CG    1 
ATOM   521  C  CD1   . LEU   A 1 70  ? 18.19911 20.05540 19.70129  1.000 39.94684  ? 67  LEU   A CD1   1 
ATOM   522  C  CD2   . LEU   A 1 70  ? 17.64264 19.14680 17.44131  1.000 34.44499  ? 67  LEU   A CD2   1 
ATOM   523  N  N     . LYS   A 1 71  ? 15.98726 24.27845 17.08119  1.000 28.66569  ? 68  LYS   A N     1 
ATOM   524  C  CA    . LYS   A 1 71  ? 14.79991 25.11996 16.97276  1.000 34.59753  ? 68  LYS   A CA    1 
ATOM   525  C  C     . LYS   A 1 71  ? 14.72270 25.80513 15.61411  1.000 36.61444  ? 68  LYS   A C     1 
ATOM   526  O  O     . LYS   A 1 71  ? 13.64323 25.88387 15.01595  1.000 39.72713  ? 68  LYS   A O     1 
ATOM   527  C  CB    . LYS   A 1 71  ? 14.78042 26.14534 18.10510  1.000 35.21559  ? 68  LYS   A CB    1 
ATOM   528  C  CG    . LYS   A 1 71  ? 14.68019 25.50449 19.48071  1.000 41.64793  ? 68  LYS   A CG    1 
ATOM   529  C  CD    . LYS   A 1 71  ? 14.21812 26.48699 20.53641  1.000 44.13340  ? 68  LYS   A CD    1 
ATOM   530  C  CE    . LYS   A 1 71  ? 13.79664 25.75721 21.80283  1.000 52.27368  ? 68  LYS   A CE    1 
ATOM   531  N  NZ    . LYS   A 1 71  ? 13.15223 26.66098 22.79838  1.000 56.02082  ? 68  LYS   A NZ    1 
ATOM   532  N  N     . LEU   A 1 72  ? 15.85591 26.29515 15.10489  1.000 35.13197  ? 69  LEU   A N     1 
ATOM   533  C  CA    . LEU   A 1 72  ? 15.84483 26.99587 13.82500  1.000 37.50307  ? 69  LEU   A CA    1 
ATOM   534  C  C     . LEU   A 1 72  ? 15.44982 26.07364 12.67824  1.000 39.20943  ? 69  LEU   A C     1 
ATOM   535  O  O     . LEU   A 1 72  ? 14.87010 26.53149 11.68712  1.000 41.12990  ? 69  LEU   A O     1 
ATOM   536  C  CB    . LEU   A 1 72  ? 17.21357 27.62373 13.55697  1.000 35.79343  ? 69  LEU   A CB    1 
ATOM   537  C  CG    . LEU   A 1 72  ? 17.58221 28.84885 14.39644  1.000 35.58090  ? 69  LEU   A CG    1 
ATOM   538  C  CD1   . LEU   A 1 72  ? 19.01884 29.27591 14.12046  1.000 36.75007  ? 69  LEU   A CD1   1 
ATOM   539  C  CD2   . LEU   A 1 72  ? 16.61595 29.99343 14.12321  1.000 32.81176  ? 69  LEU   A CD2   1 
ATOM   540  N  N     . MET   A 1 73  ? 15.75648 24.78323 12.78334  1.000 38.42707  ? 70  MET   A N     1 
ATOM   541  C  CA    . MET   A 1 73  ? 15.36138 23.81951 11.76702  1.000 42.29799  ? 70  MET   A CA    1 
ATOM   542  C  C     . MET   A 1 73  ? 14.06550 23.10182 12.11483  1.000 39.41170  ? 70  MET   A C     1 
ATOM   543  O  O     . MET   A 1 73  ? 13.63011 22.23816 11.34774  1.000 42.26103  ? 70  MET   A O     1 
ATOM   544  C  CB    . MET   A 1 73  ? 16.47897 22.79570 11.53496  1.000 43.78832  ? 70  MET   A CB    1 
ATOM   545  C  CG    . MET   A 1 73  ? 16.61057 21.73885 12.62228  1.000 45.16767  ? 70  MET   A CG    1 
ATOM   546  S  SD    . MET   A 1 73  ? 17.91585 20.55136 12.24253  1.000 42.65254  ? 70  MET   A SD    1 
ATOM   547  C  CE    . MET   A 1 73  ? 17.31208 19.86856 10.69903  1.000 41.15737  ? 70  MET   A CE    1 
ATOM   548  N  N     . ASN   A 1 74  ? 13.44608 23.44181 13.24683  1.000 46.15451  ? 71  ASN   A N     1 
ATOM   549  C  CA    . ASN   A 1 74  ? 12.16385 22.87559 13.66415  1.000 48.09961  ? 71  ASN   A CA    1 
ATOM   550  C  C     . ASN   A 1 74  ? 12.20898 21.34808 13.66779  1.000 46.76398  ? 71  ASN   A C     1 
ATOM   551  O  O     . ASN   A 1 74  ? 11.31897 20.66967 13.14763  1.000 46.83744  ? 71  ASN   A O     1 
ATOM   552  C  CB    . ASN   A 1 74  ? 11.02591 23.38831 12.78033  1.000 52.13222  ? 71  ASN   A CB    1 
ATOM   553  C  CG    . ASN   A 1 74  ? 9.66544  23.20390 13.42080  1.000 59.36787  ? 71  ASN   A CG    1 
ATOM   554  O  OD1   . ASN   A 1 74  ? 9.50274  23.39631 14.62900  1.000 62.99238  ? 71  ASN   A OD1   1 
ATOM   555  N  ND2   . ASN   A 1 74  ? 8.67842  22.82340 12.61506  1.000 62.21724  ? 71  ASN   A ND2   1 
ATOM   556  N  N     . ALA   A 1 75  ? 13.27303 20.80659 14.25787  1.000 40.39082  ? 72  ALA   A N     1 
ATOM   557  C  CA    . ALA   A 1 75  ? 13.40265 19.36200 14.37753  1.000 40.16040  ? 72  ALA   A CA    1 
ATOM   558  C  C     . ALA   A 1 75  ? 12.31513 18.80457 15.28873  1.000 41.96733  ? 72  ALA   A C     1 
ATOM   559  O  O     . ALA   A 1 75  ? 11.92107 19.43373 16.27536  1.000 40.14996  ? 72  ALA   A O     1 
ATOM   560  C  CB    . ALA   A 1 75  ? 14.78641 18.99360 14.91655  1.000 39.10445  ? 72  ALA   A CB    1 
ATOM   561  N  N     . LYS   A 1 76  ? 11.81586 17.62194 14.93952  1.000 42.55104  ? 73  LYS   A N     1 
ATOM   562  C  CA    . LYS   A 1 76  ? 10.81533 16.93110 15.73943  1.000 42.86833  ? 73  LYS   A CA    1 
ATOM   563  C  C     . LYS   A 1 76  ? 11.23791 15.53459 16.16592  1.000 40.38995  ? 73  LYS   A C     1 
ATOM   564  O  O     . LYS   A 1 76  ? 10.86786 15.09910 17.25901  1.000 41.16807  ? 73  LYS   A O     1 
ATOM   565  C  CB    . LYS   A 1 76  ? 9.48641  16.83133 14.97227  1.000 42.79981  ? 73  LYS   A CB    1 
ATOM   566  C  CG    . LYS   A 1 76  ? 8.84491  18.17325 14.64566  1.000 45.69779  ? 73  LYS   A CG    1 
ATOM   567  N  N     . ARG   A 1 77  ? 12.00415 14.82478 15.34425  1.000 37.71807  ? 74  ARG   A N     1 
ATOM   568  C  CA    . ARG   A 1 77  ? 12.47914 13.49188 15.68242  1.000 48.56618  ? 74  ARG   A CA    1 
ATOM   569  C  C     . ARG   A 1 77  ? 13.99129 13.46571 15.53163  1.000 44.15833  ? 74  ARG   A C     1 
ATOM   570  O  O     . ARG   A 1 77  ? 14.51794 13.81690 14.47034  1.000 39.54595  ? 74  ARG   A O     1 
ATOM   571  C  CB    . ARG   A 1 77  ? 11.83096 12.42082 14.79811  1.000 51.55875  ? 74  ARG   A CB    1 
ATOM   572  C  CG    . ARG   A 1 77  ? 11.92900 11.03332 15.39302  1.000 59.25219  ? 74  ARG   A CG    1 
ATOM   573  C  CD    . ARG   A 1 77  ? 11.57272 9.95105  14.39569  1.000 69.04520  ? 74  ARG   A CD    1 
ATOM   574  N  NE    . ARG   A 1 77  ? 11.56277 8.63707  15.03326  1.000 76.93506  ? 74  ARG   A NE    1 
ATOM   575  C  CZ    . ARG   A 1 77  ? 11.53187 7.48477  14.37286  1.000 83.69540  ? 74  ARG   A CZ    1 
ATOM   576  N  NH1   . ARG   A 1 77  ? 11.52413 6.33517  15.03531  1.000 86.59279  ? 74  ARG   A NH1   1 
ATOM   577  N  NH2   . ARG   A 1 77  ? 11.51643 7.48179  13.04854  1.000 85.57144  ? 74  ARG   A NH2   1 
ATOM   578  N  N     . THR   A 1 78  ? 14.68435 13.06709 16.59638  1.000 36.71044  ? 75  THR   A N     1 
ATOM   579  C  CA    . THR   A 1 78  ? 16.13677 13.08802 16.62591  1.000 43.52285  ? 75  THR   A CA    1 
ATOM   580  C  C     . THR   A 1 78  ? 16.66433 11.75073 17.12259  1.000 43.30289  ? 75  THR   A C     1 
ATOM   581  O  O     . THR   A 1 78  ? 15.93250 10.93504 17.69154  1.000 40.99765  ? 75  THR   A O     1 
ATOM   582  C  CB    . THR   A 1 78  ? 16.68151 14.20878 17.52591  1.000 39.87816  ? 75  THR   A CB    1 
ATOM   583  O  OG1   . THR   A 1 78  ? 16.46534 13.86268 18.89715  1.000 43.62599  ? 75  THR   A OG1   1 
ATOM   584  C  CG2   . THR   A 1 78  ? 15.98934 15.53629 17.22925  1.000 37.81827  ? 75  THR   A CG2   1 
ATOM   585  N  N     . ILE   A 1 79  ? 17.95676 11.54100 16.89754  1.000 40.08118  ? 76  ILE   A N     1 
ATOM   586  C  CA    . ILE   A 1 79  ? 18.68017 10.39885 17.43619  1.000 44.06395  ? 76  ILE   A CA    1 
ATOM   587  C  C     . ILE   A 1 79  ? 19.96142 10.91385 18.08019  1.000 40.12339  ? 76  ILE   A C     1 
ATOM   588  O  O     . ILE   A 1 79  ? 20.60244 11.83520 17.56258  1.000 34.77301  ? 76  ILE   A O     1 
ATOM   589  C  CB    . ILE   A 1 79  ? 18.97106 9.34283  16.34652  1.000 47.51483  ? 76  ILE   A CB    1 
ATOM   590  C  CG1   . ILE   A 1 79  ? 19.93286 8.27617  16.86230  1.000 49.24935  ? 76  ILE   A CG1   1 
ATOM   591  C  CG2   . ILE   A 1 79  ? 19.50229 10.00122 15.08100  1.000 46.02383  ? 76  ILE   A CG2   1 
ATOM   592  C  CD1   . ILE   A 1 79  ? 19.92202 7.01720  16.03763  1.000 54.00973  ? 76  ILE   A CD1   1 
ATOM   593  N  N     . GLU   A 1 80  ? 20.31016 10.33968 19.23093  1.000 43.24554  ? 77  GLU   A N     1 
ATOM   594  C  CA    . GLU   A 1 80  ? 21.45360 10.77335 20.02421  1.000 45.41817  ? 77  GLU   A CA    1 
ATOM   595  C  C     . GLU   A 1 80  ? 22.32687 9.56239  20.31598  1.000 45.61792  ? 77  GLU   A C     1 
ATOM   596  O  O     . GLU   A 1 80  ? 21.88038 8.61919  20.97647  1.000 43.71218  ? 77  GLU   A O     1 
ATOM   597  C  CB    . GLU   A 1 80  ? 20.99277 11.43385 21.32712  1.000 50.85194  ? 77  GLU   A CB    1 
ATOM   598  C  CG    . GLU   A 1 80  ? 22.07794 12.20079 22.06855  1.000 58.51411  ? 77  GLU   A CG    1 
ATOM   599  C  CD    . GLU   A 1 80  ? 21.88739 13.70628 21.98539  1.000 65.15289  ? 77  GLU   A CD    1 
ATOM   600  O  OE1   . GLU   A 1 80  ? 22.73434 14.44158 22.53130  1.000 64.50685  ? 77  GLU   A OE1   1 
ATOM   601  O  OE2   . GLU   A 1 80  ? 20.88906 14.15460 21.37851  1.000 68.63934  ? 77  GLU   A OE2   1 
ATOM   602  N  N     . ILE   A 1 81  ? 23.56570 9.59069  19.83296  1.000 43.30433  ? 78  ILE   A N     1 
ATOM   603  C  CA    . ILE   A 1 81  ? 24.50269 8.48020  19.97691  1.000 43.54881  ? 78  ILE   A CA    1 
ATOM   604  C  C     . ILE   A 1 81  ? 25.61359 8.92896  20.91766  1.000 39.87642  ? 78  ILE   A C     1 
ATOM   605  O  O     . ILE   A 1 81  ? 26.42178 9.79939  20.57035  1.000 37.23728  ? 78  ILE   A O     1 
ATOM   606  C  CB    . ILE   A 1 81  ? 25.06389 8.03333  18.62052  1.000 46.34508  ? 78  ILE   A CB    1 
ATOM   607  C  CG1   . ILE   A 1 81  ? 23.92070 7.58241  17.70364  1.000 49.76564  ? 78  ILE   A CG1   1 
ATOM   608  C  CG2   . ILE   A 1 81  ? 26.09369 6.93241  18.80470  1.000 43.88524  ? 78  ILE   A CG2   1 
ATOM   609  C  CD1   . ILE   A 1 81  ? 24.34520 7.31050  16.27478  1.000 50.77985  ? 78  ILE   A CD1   1 
ATOM   610  N  N     . GLY   A 1 82  ? 25.65953 8.33448  22.10767  1.000 39.13440  ? 79  GLY   A N     1 
ATOM   611  C  CA    . GLY   A 1 82  ? 26.58018 8.77727  23.13660  1.000 36.53154  ? 79  GLY   A CA    1 
ATOM   612  C  C     . GLY   A 1 82  ? 25.89555 9.71418  24.10924  1.000 37.55510  ? 79  GLY   A C     1 
ATOM   613  O  O     . GLY   A 1 82  ? 25.85321 10.92776 23.88876  1.000 38.88750  ? 79  GLY   A O     1 
ATOM   614  N  N     . VAL   A 1 83  ? 25.35064 9.16093  25.18641  1.000 38.12404  ? 80  VAL   A N     1 
ATOM   615  C  CA    . VAL   A 1 83  ? 24.50799 9.90643  26.11331  1.000 37.21772  ? 80  VAL   A CA    1 
ATOM   616  C  C     . VAL   A 1 83  ? 25.29038 10.38149 27.32796  1.000 39.96220  ? 80  VAL   A C     1 
ATOM   617  O  O     . VAL   A 1 83  ? 25.18685 11.54384 27.72367  1.000 39.38319  ? 80  VAL   A O     1 
ATOM   618  C  CB    . VAL   A 1 83  ? 23.29388 9.04742  26.53215  1.000 37.38084  ? 80  VAL   A CB    1 
ATOM   619  C  CG1   . VAL   A 1 83  ? 22.46312 9.77449  27.58064  1.000 34.64540  ? 80  VAL   A CG1   1 
ATOM   620  C  CG2   . VAL   A 1 83  ? 22.44864 8.70166  25.31487  1.000 38.08476  ? 80  VAL   A CG2   1 
ATOM   621  N  N     . TYR   A 1 84  ? 26.06904 9.48806  27.93484  1.000 39.47474  ? 81  TYR   A N     1 
ATOM   622  C  CA    . TYR   A 1 84  ? 26.82173 9.76998  29.16473  1.000 40.47138  ? 81  TYR   A CA    1 
ATOM   623  C  C     . TYR   A 1 84  ? 25.77983 10.14377 30.23283  1.000 41.58264  ? 81  TYR   A C     1 
ATOM   624  O  O     . TYR   A 1 84  ? 24.81444 9.39864  30.41263  1.000 46.10160  ? 81  TYR   A O     1 
ATOM   625  C  CB    . TYR   A 1 84  ? 27.90551 10.80709 28.89219  1.000 37.90873  ? 81  TYR   A CB    1 
ATOM   626  C  CG    . TYR   A 1 84  ? 28.82118 11.07280 30.06613  1.000 39.51586  ? 81  TYR   A CG    1 
ATOM   627  C  CD1   . TYR   A 1 84  ? 29.22938 10.03882 30.90153  1.000 41.50617  ? 81  TYR   A CD1   1 
ATOM   628  C  CD2   . TYR   A 1 84  ? 29.28472 12.35502 30.33425  1.000 39.91216  ? 81  TYR   A CD2   1 
ATOM   629  C  CE1   . TYR   A 1 84  ? 30.07015 10.27619 31.97827  1.000 43.25276  ? 81  TYR   A CE1   1 
ATOM   630  C  CE2   . TYR   A 1 84  ? 30.12483 12.60297 31.40508  1.000 43.31441  ? 81  TYR   A CE2   1 
ATOM   631  C  CZ    . TYR   A 1 84  ? 30.51413 11.56000 32.22531  1.000 46.06584  ? 81  TYR   A CZ    1 
ATOM   632  O  OH    . TYR   A 1 84  ? 31.34944 11.80640 33.29321  1.000 45.89718  ? 81  TYR   A OH    1 
ATOM   633  N  N     . THR   A 1 85  ? 25.94090 11.26649 30.93504  1.000 40.02119  ? 82  THR   A N     1 
ATOM   634  C  CA    . THR   A 1 85  ? 24.96404 11.63899 31.95257  1.000 40.99977  ? 82  THR   A CA    1 
ATOM   635  C  C     . THR   A 1 85  ? 23.74498 12.34182 31.37256  1.000 40.61710  ? 82  THR   A C     1 
ATOM   636  O  O     . THR   A 1 85  ? 22.76646 12.54228 32.09921  1.000 39.67325  ? 82  THR   A O     1 
ATOM   637  C  CB    . THR   A 1 85  ? 25.61374 12.52700 33.01925  1.000 40.87327  ? 82  THR   A CB    1 
ATOM   638  O  OG1   . THR   A 1 85  ? 26.18507 13.69208 32.40540  1.000 38.97013  ? 82  THR   A OG1   1 
ATOM   639  C  CG2   . THR   A 1 85  ? 26.69883 11.75439 33.75944  1.000 35.35194  ? 82  THR   A CG2   1 
ATOM   640  N  N     . GLY   A 1 86  ? 23.77888 12.72177 30.10001  1.000 41.59693  ? 83  GLY   A N     1 
ATOM   641  C  CA    . GLY   A 1 86  ? 22.60442 13.22071 29.41594  1.000 39.46252  ? 83  GLY   A CA    1 
ATOM   642  C  C     . GLY   A 1 86  ? 22.50512 14.72069 29.23640  1.000 37.11471  ? 83  GLY   A C     1 
ATOM   643  O  O     . GLY   A 1 86  ? 21.38841 15.22634 29.06968  1.000 34.24104  ? 83  GLY   A O     1 
ATOM   644  N  N     . TYR   A 1 87  ? 23.62378 15.44841 29.25407  1.000 29.48936  ? 84  TYR   A N     1 
ATOM   645  C  CA    . TYR   A 1 87  ? 23.54725 16.90194 29.12841  1.000 31.77387  ? 84  TYR   A CA    1 
ATOM   646  C  C     . TYR   A 1 87  ? 23.02539 17.31073 27.75443  1.000 32.62807  ? 84  TYR   A C     1 
ATOM   647  O  O     . TYR   A 1 87  ? 22.08711 18.10954 27.64776  1.000 35.38901  ? 84  TYR   A O     1 
ATOM   648  C  CB    . TYR   A 1 87  ? 24.91236 17.53649 29.39750  1.000 28.19096  ? 84  TYR   A CB    1 
ATOM   649  C  CG    . TYR   A 1 87  ? 24.83346 19.03923 29.53196  1.000 27.83644  ? 84  TYR   A CG    1 
ATOM   650  C  CD1   . TYR   A 1 87  ? 24.95479 19.86347 28.41908  1.000 25.55392  ? 84  TYR   A CD1   1 
ATOM   651  C  CD2   . TYR   A 1 87  ? 24.61929 19.63560 30.76980  1.000 29.22952  ? 84  TYR   A CD2   1 
ATOM   652  C  CE1   . TYR   A 1 87  ? 24.87575 21.23838 28.53571  1.000 26.23265  ? 84  TYR   A CE1   1 
ATOM   653  C  CE2   . TYR   A 1 87  ? 24.53569 21.01343 30.89590  1.000 28.91340  ? 84  TYR   A CE2   1 
ATOM   654  C  CZ    . TYR   A 1 87  ? 24.66497 21.80768 29.77546  1.000 27.50009  ? 84  TYR   A CZ    1 
ATOM   655  O  OH    . TYR   A 1 87  ? 24.57479 23.17599 29.89454  1.000 27.15487  ? 84  TYR   A OH    1 
ATOM   656  N  N     . SER   A 1 88  ? 23.62537 16.77669 26.68532  1.000 31.03727  ? 85  SER   A N     1 
ATOM   657  C  CA    . SER   A 1 88  ? 23.13220 17.09088 25.34786  1.000 32.24847  ? 85  SER   A CA    1 
ATOM   658  C  C     . SER   A 1 88  ? 21.76575 16.46804 25.10037  1.000 31.76528  ? 85  SER   A C     1 
ATOM   659  O  O     . SER   A 1 88  ? 20.95783 17.02849 24.35049  1.000 33.77972  ? 85  SER   A O     1 
ATOM   660  C  CB    . SER   A 1 88  ? 24.12911 16.62747 24.28304  1.000 34.02257  ? 85  SER   A CB    1 
ATOM   661  O  OG    . SER   A 1 88  ? 24.21545 15.21183 24.23809  1.000 33.32325  ? 85  SER   A OG    1 
ATOM   662  N  N     . LEU   A 1 89  ? 21.49005 15.31835 25.72072  1.000 30.69196  ? 86  LEU   A N     1 
ATOM   663  C  CA    . LEU   A 1 89  ? 20.18219 14.69079 25.57753  1.000 29.54976  ? 86  LEU   A CA    1 
ATOM   664  C  C     . LEU   A 1 89  ? 19.09279 15.55482 26.20351  1.000 32.23800  ? 86  LEU   A C     1 
ATOM   665  O  O     . LEU   A 1 89  ? 18.03958 15.78400 25.59740  1.000 34.60212  ? 86  LEU   A O     1 
ATOM   666  C  CB    . LEU   A 1 89  ? 20.20400 13.29821 26.20781  1.000 31.85276  ? 86  LEU   A CB    1 
ATOM   667  C  CG    . LEU   A 1 89  ? 18.89329 12.51245 26.18929  1.000 33.43542  ? 86  LEU   A CG    1 
ATOM   668  C  CD1   . LEU   A 1 89  ? 18.36531 12.38225 24.76903  1.000 33.70176  ? 86  LEU   A CD1   1 
ATOM   669  C  CD2   . LEU   A 1 89  ? 19.09166 11.13708 26.82935  1.000 33.64050  ? 86  LEU   A CD2   1 
ATOM   670  N  N     . LEU   A 1 90  ? 19.33356 16.04830 27.42092  1.000 31.92183  ? 87  LEU   A N     1 
ATOM   671  C  CA    . LEU   A 1 90  ? 18.39349 16.97292 28.04732  1.000 31.32938  ? 87  LEU   A CA    1 
ATOM   672  C  C     . LEU   A 1 90  ? 18.26603 18.26113 27.24146  1.000 32.40681  ? 87  LEU   A C     1 
ATOM   673  O  O     . LEU   A 1 90  ? 17.16115 18.79565 27.08604  1.000 33.82293  ? 87  LEU   A O     1 
ATOM   674  C  CB    . LEU   A 1 90  ? 18.83019 17.27279 29.48223  1.000 28.94530  ? 87  LEU   A CB    1 
ATOM   675  C  CG    . LEU   A 1 90  ? 17.89855 18.18154 30.29003  1.000 32.03615  ? 87  LEU   A CG    1 
ATOM   676  C  CD1   . LEU   A 1 90  ? 16.43760 17.74893 30.14780  1.000 27.94653  ? 87  LEU   A CD1   1 
ATOM   677  C  CD2   . LEU   A 1 90  ? 18.31583 18.19090 31.75155  1.000 30.37316  ? 87  LEU   A CD2   1 
ATOM   678  N  N     . THR   A 1 91  ? 19.38888 18.77607 26.72843  1.000 30.83346  ? 88  THR   A N     1 
ATOM   679  C  CA    . THR   A 1 91  ? 19.35228 19.93983 25.84517  1.000 30.95350  ? 88  THR   A CA    1 
ATOM   680  C  C     . THR   A 1 91  ? 18.43247 19.69704 24.65357  1.000 32.90806  ? 88  THR   A C     1 
ATOM   681  O  O     . THR   A 1 91  ? 17.59925 20.54493 24.31539  1.000 35.48913  ? 88  THR   A O     1 
ATOM   682  C  CB    . THR   A 1 91  ? 20.76866 20.27867 25.36520  1.000 31.65597  ? 88  THR   A CB    1 
ATOM   683  O  OG1   . THR   A 1 91  ? 21.58467 20.65098 26.48307  1.000 33.75130  ? 88  THR   A OG1   1 
ATOM   684  C  CG2   . THR   A 1 91  ? 20.74594 21.42306 24.35612  1.000 27.53597  ? 88  THR   A CG2   1 
ATOM   685  N  N     . THR   A 1 92  ? 18.56866 18.53513 24.00617  1.000 35.04334  ? 89  THR   A N     1 
ATOM   686  C  CA    . THR   A 1 92  ? 17.72944 18.21825 22.85368  1.000 36.40309  ? 89  THR   A CA    1 
ATOM   687  C  C     . THR   A 1 92  ? 16.26332 18.08411 23.25273  1.000 38.51183  ? 89  THR   A C     1 
ATOM   688  O  O     . THR   A 1 92  ? 15.37547 18.57511 22.54640  1.000 37.79884  ? 89  THR   A O     1 
ATOM   689  C  CB    . THR   A 1 92  ? 18.21783 16.93122 22.18231  1.000 33.42171  ? 89  THR   A CB    1 
ATOM   690  O  OG1   . THR   A 1 92  ? 19.54721 17.12064 21.68481  1.000 32.23301  ? 89  THR   A OG1   1 
ATOM   691  C  CG2   . THR   A 1 92  ? 17.30028 16.54248 21.02551  1.000 30.70186  ? 89  THR   A CG2   1 
ATOM   692  N  N     . ALA   A 1 93  ? 15.99087 17.42873 24.38433  1.000 37.07575  ? 90  ALA   A N     1 
ATOM   693  C  CA    . ALA   A 1 93  ? 14.61003 17.23056 24.81221  1.000 38.01352  ? 90  ALA   A CA    1 
ATOM   694  C  C     . ALA   A 1 93  ? 13.94233 18.55177 25.17487  1.000 41.98326  ? 90  ALA   A C     1 
ATOM   695  O  O     . ALA   A 1 93  ? 12.74572 18.73937 24.92347  1.000 42.96575  ? 90  ALA   A O     1 
ATOM   696  C  CB    . ALA   A 1 93  ? 14.56343 16.25797 25.99016  1.000 38.85859  ? 90  ALA   A CB    1 
ATOM   697  N  N     . LEU   A 1 94  ? 14.69879 19.48497 25.76065  1.000 43.90166  ? 91  LEU   A N     1 
ATOM   698  C  CA    . LEU   A 1 94  ? 14.12343 20.77922 26.11721  1.000 41.46066  ? 91  LEU   A CA    1 
ATOM   699  C  C     . LEU   A 1 94  ? 13.84470 21.63298 24.88508  1.000 41.07263  ? 91  LEU   A C     1 
ATOM   700  O  O     . LEU   A 1 94  ? 12.92826 22.46166 24.90167  1.000 39.13850  ? 91  LEU   A O     1 
ATOM   701  C  CB    . LEU   A 1 94  ? 15.05157 21.52147 27.07952  1.000 39.13112  ? 91  LEU   A CB    1 
ATOM   702  C  CG    . LEU   A 1 94  ? 15.09553 20.99639 28.51542  1.000 35.90095  ? 91  LEU   A CG    1 
ATOM   703  C  CD1   . LEU   A 1 94  ? 16.26061 21.61986 29.28885  1.000 31.97716  ? 91  LEU   A CD1   1 
ATOM   704  C  CD2   . LEU   A 1 94  ? 13.78220 21.28749 29.20658  1.000 36.09578  ? 91  LEU   A CD2   1 
ATOM   705  N  N     . ALA   A 1 95  ? 14.61524 21.44564 23.81124  1.000 40.10253  ? 92  ALA   A N     1 
ATOM   706  C  CA    . ALA   A 1 95  ? 14.41977 22.23670 22.60066  1.000 35.13557  ? 92  ALA   A CA    1 
ATOM   707  C  C     . ALA   A 1 95  ? 13.23860 21.74940 21.76979  1.000 33.53585  ? 92  ALA   A C     1 
ATOM   708  O  O     . ALA   A 1 95  ? 12.57011 22.55919 21.12060  1.000 34.73002  ? 92  ALA   A O     1 
ATOM   709  C  CB    . ALA   A 1 95  ? 15.69068 22.21605 21.74912  1.000 28.22603  ? 92  ALA   A CB    1 
ATOM   710  N  N     . LEU   A 1 96  ? 12.97695 20.44535 21.76623  1.000 32.23879  ? 93  LEU   A N     1 
ATOM   711  C  CA    . LEU   A 1 96  ? 11.93974 19.88242 20.92296  1.000 37.11559  ? 93  LEU   A CA    1 
ATOM   712  C  C     . LEU   A 1 96  ? 10.55277 20.31661 21.39659  1.000 38.43932  ? 93  LEU   A C     1 
ATOM   713  O  O     . LEU   A 1 96  ? 10.37086 20.70617 22.55279  1.000 35.87275  ? 93  LEU   A O     1 
ATOM   714  C  CB    . LEU   A 1 96  ? 12.03477 18.35784 20.91767  1.000 37.21474  ? 93  LEU   A CB    1 
ATOM   715  C  CG    . LEU   A 1 96  ? 13.27893 17.76342 20.25439  1.000 38.36595  ? 93  LEU   A CG    1 
ATOM   716  C  CD1   . LEU   A 1 96  ? 13.13842 16.25642 20.13007  1.000 37.71171  ? 93  LEU   A CD1   1 
ATOM   717  C  CD2   . LEU   A 1 96  ? 13.53080 18.39999 18.89386  1.000 35.40582  ? 93  LEU   A CD2   1 
ATOM   718  N  N     . PRO   A 1 97  ? 9.55496  20.26199 20.51570  1.000 35.87344  ? 94  PRO   A N     1 
ATOM   719  C  CA    . PRO   A 1 97  ? 8.17562  20.51968 20.94712  1.000 38.86980  ? 94  PRO   A CA    1 
ATOM   720  C  C     . PRO   A 1 97  ? 7.69457  19.45404 21.92222  1.000 39.76875  ? 94  PRO   A C     1 
ATOM   721  O  O     . PRO   A 1 97  ? 8.37717  18.46800 22.20741  1.000 41.44077  ? 94  PRO   A O     1 
ATOM   722  C  CB    . PRO   A 1 97  ? 7.37587  20.49208 19.63908  1.000 37.52713  ? 94  PRO   A CB    1 
ATOM   723  C  CG    . PRO   A 1 97  ? 8.21481  19.68511 18.69900  1.000 38.26494  ? 94  PRO   A CG    1 
ATOM   724  C  CD    . PRO   A 1 97  ? 9.64115  20.00723 19.06745  1.000 34.01963  ? 94  PRO   A CD    1 
ATOM   725  N  N     . GLU   A 1 98  ? 6.48475  19.67076 22.44521  1.000 40.92074  ? 95  GLU   A N     1 
ATOM   726  C  CA    . GLU   A 1 98  ? 5.92744  18.75513 23.43758  1.000 45.12374  ? 95  GLU   A CA    1 
ATOM   727  C  C     . GLU   A 1 98  ? 5.80097  17.33486 22.89883  1.000 43.68322  ? 95  GLU   A C     1 
ATOM   728  O  O     . GLU   A 1 98  ? 5.93690  16.36934 23.65960  1.000 44.53252  ? 95  GLU   A O     1 
ATOM   729  C  CB    . GLU   A 1 98  ? 4.56471  19.26321 23.90944  1.000 48.89084  ? 95  GLU   A CB    1 
ATOM   730  C  CG    . GLU   A 1 98  ? 4.63522  20.44648 24.86015  1.000 57.54396  ? 95  GLU   A CG    1 
ATOM   731  C  CD    . GLU   A 1 98  ? 5.10578  20.04965 26.24615  1.000 67.62317  ? 95  GLU   A CD    1 
ATOM   732  O  OE1   . GLU   A 1 98  ? 5.64045  20.91933 26.96660  1.000 71.39563  ? 95  GLU   A OE1   1 
ATOM   733  O  OE2   . GLU   A 1 98  ? 4.93858  18.86736 26.61622  1.000 71.13704  ? 95  GLU   A OE2   1 
ATOM   734  N  N     . ASP   A 1 99  ? 5.54685  17.18269 21.59832  1.000 39.26277  ? 96  ASP   A N     1 
ATOM   735  C  CA    . ASP   A 1 99  ? 5.36146  15.87091 20.99214  1.000 42.21399  ? 96  ASP   A CA    1 
ATOM   736  C  C     . ASP   A 1 99  ? 6.58761  15.41351 20.21063  1.000 43.64915  ? 96  ASP   A C     1 
ATOM   737  O  O     . ASP   A 1 99  ? 6.47536  14.52968 19.35412  1.000 42.15357  ? 96  ASP   A O     1 
ATOM   738  C  CB    . ASP   A 1 99  ? 4.12317  15.86917 20.09229  1.000 41.41985  ? 96  ASP   A CB    1 
ATOM   739  C  CG    . ASP   A 1 99  ? 4.24809  16.82696 18.92348  1.000 41.85161  ? 96  ASP   A CG    1 
ATOM   740  O  OD1   . ASP   A 1 99  ? 5.01017  17.81168 19.03442  1.000 45.56037  ? 96  ASP   A OD1   1 
ATOM   741  O  OD2   . ASP   A 1 99  ? 3.58577  16.59823 17.89121  1.000 41.34374  ? 96  ASP   A OD2   1 
ATOM   742  N  N     . GLY   A 1 100 ? 7.75512  15.99882 20.48361  1.000 42.39919  ? 97  GLY   A N     1 
ATOM   743  C  CA    . GLY   A 1 100 ? 8.97578  15.51095 19.87996  1.000 39.95960  ? 97  GLY   A CA    1 
ATOM   744  C  C     . GLY   A 1 100 ? 9.39576  14.16909 20.44966  1.000 40.16532  ? 97  GLY   A C     1 
ATOM   745  O  O     . GLY   A 1 100 ? 8.95761  13.74883 21.52259  1.000 39.19108  ? 97  GLY   A O     1 
ATOM   746  N  N     . LYS   A 1 101 ? 10.27192 13.48482 19.71281  1.000 37.31447  ? 98  LYS   A N     1 
ATOM   747  C  CA    . LYS   A 1 101 ? 10.72432 12.15246 20.08733  1.000 41.67394  ? 98  LYS   A CA    1 
ATOM   748  C  C     . LYS   A 1 101 ? 12.21944 12.03287 19.83832  1.000 40.87562  ? 98  LYS   A C     1 
ATOM   749  O  O     . LYS   A 1 101 ? 12.73536 12.55699 18.84689  1.000 38.61854  ? 98  LYS   A O     1 
ATOM   750  C  CB    . LYS   A 1 101 ? 9.97316  11.06457 19.30856  1.000 47.06817  ? 98  LYS   A CB    1 
ATOM   751  C  CG    . LYS   A 1 101 ? 9.09803  10.16975 20.17645  1.000 56.86575  ? 98  LYS   A CG    1 
ATOM   752  C  CD    . LYS   A 1 101 ? 9.92813  9.41291  21.20562  1.000 61.17909  ? 98  LYS   A CD    1 
ATOM   753  C  CE    . LYS   A 1 101 ? 9.04796  8.55571  22.10100  1.000 63.75178  ? 98  LYS   A CE    1 
ATOM   754  N  NZ    . LYS   A 1 101 ? 9.75125  8.12632  23.34228  1.000 65.20813  ? 98  LYS   A NZ    1 
ATOM   755  N  N     . ILE   A 1 102 ? 12.90675 11.34129 20.74709  1.000 39.29875  ? 99  ILE   A N     1 
ATOM   756  C  CA    . ILE   A 1 102 ? 14.34988 11.14344 20.68159  1.000 38.21308  ? 99  ILE   A CA    1 
ATOM   757  C  C     . ILE   A 1 102 ? 14.65259 9.66872  20.88997  1.000 38.45644  ? 99  ILE   A C     1 
ATOM   758  O  O     . ILE   A 1 102 ? 14.08892 9.03119  21.78600  1.000 34.72163  ? 99  ILE   A O     1 
ATOM   759  C  CB    . ILE   A 1 102 ? 15.10013 11.97548 21.74317  1.000 38.53274  ? 99  ILE   A CB    1 
ATOM   760  C  CG1   . ILE   A 1 102 ? 14.69303 13.44539 21.68299  1.000 36.21202  ? 99  ILE   A CG1   1 
ATOM   761  C  CG2   . ILE   A 1 102 ? 16.60720 11.82118 21.57497  1.000 38.53546  ? 99  ILE   A CG2   1 
ATOM   762  C  CD1   . ILE   A 1 102 ? 15.14949 14.23616 22.88355  1.000 37.10521  ? 99  ILE   A CD1   1 
ATOM   763  N  N     . THR   A 1 103 ? 15.55211 9.13043  20.07275  1.000 37.04962  ? 100 THR   A N     1 
ATOM   764  C  CA    . THR   A 1 103 ? 16.13700 7.81934  20.32004  1.000 38.28454  ? 100 THR   A CA    1 
ATOM   765  C  C     . THR   A 1 103 ? 17.55930 8.03193  20.82763  1.000 39.14119  ? 100 THR   A C     1 
ATOM   766  O  O     . THR   A 1 103 ? 18.41679 8.53780  20.09512  1.000 39.57426  ? 100 THR   A O     1 
ATOM   767  C  CB    . THR   A 1 103 ? 16.13382 6.94939  19.06654  1.000 38.41867  ? 100 THR   A CB    1 
ATOM   768  O  OG1   . THR   A 1 103 ? 14.79629 6.80465  18.57186  1.000 37.98779  ? 100 THR   A OG1   1 
ATOM   769  C  CG2   . THR   A 1 103 ? 16.67915 5.58342  19.41257  1.000 37.91000  ? 100 THR   A CG2   1 
ATOM   770  N  N     . ALA   A 1 104 ? 17.80282 7.65343  22.08041  1.000 37.87728  ? 101 ALA   A N     1 
ATOM   771  C  CA    . ALA   A 1 104 ? 19.09951 7.81286  22.72460  1.000 37.06075  ? 101 ALA   A CA    1 
ATOM   772  C  C     . ALA   A 1 104 ? 19.75456 6.44879  22.87682  1.000 39.33949  ? 101 ALA   A C     1 
ATOM   773  O  O     . ALA   A 1 104 ? 19.11943 5.50389  23.35540  1.000 39.60450  ? 101 ALA   A O     1 
ATOM   774  C  CB    . ALA   A 1 104 ? 18.95364 8.48841  24.08953  1.000 34.79629  ? 101 ALA   A CB    1 
ATOM   775  N  N     . ILE   A 1 105 ? 21.02018 6.34933  22.47287  1.000 38.81696  ? 102 ILE   A N     1 
ATOM   776  C  CA    . ILE   A 1 105 ? 21.74474 5.08401  22.44995  1.000 42.05264  ? 102 ILE   A CA    1 
ATOM   777  C  C     . ILE   A 1 105 ? 23.05927 5.26278  23.19540  1.000 40.60055  ? 102 ILE   A C     1 
ATOM   778  O  O     . ILE   A 1 105 ? 23.82686 6.18638  22.90245  1.000 42.60627  ? 102 ILE   A O     1 
ATOM   779  C  CB    . ILE   A 1 105 ? 22.00682 4.59689  21.01092  1.000 42.91568  ? 102 ILE   A CB    1 
ATOM   780  C  CG1   . ILE   A 1 105 ? 20.74658 4.73246  20.15915  1.000 41.59817  ? 102 ILE   A CG1   1 
ATOM   781  C  CG2   . ILE   A 1 105 ? 22.48578 3.15154  21.01376  1.000 43.80378  ? 102 ILE   A CG2   1 
ATOM   782  C  CD1   . ILE   A 1 105 ? 20.98851 4.52691  18.68451  1.000 42.36700  ? 102 ILE   A CD1   1 
ATOM   783  N  N     . ASP   A 1 106 ? 23.31742 4.37851  24.15342  1.000 38.53476  ? 103 ASP   A N     1 
ATOM   784  C  CA    . ASP   A 1 106 ? 24.57224 4.38090  24.88727  1.000 40.47826  ? 103 ASP   A CA    1 
ATOM   785  C  C     . ASP   A 1 106 ? 24.79977 2.98096  25.43587  1.000 44.13840  ? 103 ASP   A C     1 
ATOM   786  O  O     . ASP   A 1 106 ? 23.84634 2.24947  25.71824  1.000 41.19676  ? 103 ASP   A O     1 
ATOM   787  C  CB    . ASP   A 1 106 ? 24.56814 5.42184  26.01635  1.000 39.67277  ? 103 ASP   A CB    1 
ATOM   788  C  CG    . ASP   A 1 106 ? 25.96727 5.74050  26.52716  1.000 43.79904  ? 103 ASP   A CG    1 
ATOM   789  O  OD1   . ASP   A 1 106 ? 26.58741 4.86527  27.17069  1.000 44.93608  ? 103 ASP   A OD1   1 
ATOM   790  O  OD2   . ASP   A 1 106 ? 26.45211 6.86629  26.27308  1.000 40.49815  ? 103 ASP   A OD2   1 
ATOM   791  N  N     . VAL   A 1 107 ? 26.07460 2.60965  25.57222  1.000 42.13417  ? 104 VAL   A N     1 
ATOM   792  C  CA    . VAL   A 1 107 ? 26.40709 1.28570  26.08565  1.000 44.32877  ? 104 VAL   A CA    1 
ATOM   793  C  C     . VAL   A 1 107 ? 26.27204 1.19867  27.59844  1.000 46.47948  ? 104 VAL   A C     1 
ATOM   794  O  O     . VAL   A 1 107 ? 26.16710 0.09128  28.13794  1.000 50.82025  ? 104 VAL   A O     1 
ATOM   795  C  CB    . VAL   A 1 107 ? 27.83600 0.88043  25.68544  1.000 43.23788  ? 104 VAL   A CB    1 
ATOM   796  C  CG1   . VAL   A 1 107 ? 27.93216 0.67476  24.18466  1.000 43.17837  ? 104 VAL   A CG1   1 
ATOM   797  C  CG2   . VAL   A 1 107 ? 28.84347 1.93662  26.15152  1.000 38.20227  ? 104 VAL   A CG2   1 
ATOM   798  N  N     . ASN   A 1 108 ? 26.26657 2.32973  28.29762  1.000 46.79308  ? 105 ASN   A N     1 
ATOM   799  C  CA    . ASN   A 1 108 ? 26.34509 2.37078  29.75621  1.000 50.16672  ? 105 ASN   A CA    1 
ATOM   800  C  C     . ASN   A 1 108 ? 25.13585 3.13743  30.28759  1.000 49.67086  ? 105 ASN   A C     1 
ATOM   801  O  O     . ASN   A 1 108 ? 25.14925 4.36901  30.36171  1.000 51.04471  ? 105 ASN   A O     1 
ATOM   802  C  CB    . ASN   A 1 108 ? 27.66810 3.01226  30.19178  1.000 52.68813  ? 105 ASN   A CB    1 
ATOM   803  C  CG    . ASN   A 1 108 ? 27.94483 2.84847  31.67339  1.000 58.40115  ? 105 ASN   A CG    1 
ATOM   804  O  OD1   . ASN   A 1 108 ? 27.04588 2.96880  32.50588  1.000 60.49164  ? 105 ASN   A OD1   1 
ATOM   805  N  ND2   . ASN   A 1 108 ? 29.20186 2.57532  32.01046  1.000 59.63558  ? 105 ASN   A ND2   1 
ATOM   806  N  N     . LYS   A 1 109 ? 24.08992 2.40134  30.66931  1.000 56.74204  ? 106 LYS   A N     1 
ATOM   807  C  CA    . LYS   A 1 109 ? 22.89775 3.04140  31.21070  1.000 56.76419  ? 106 LYS   A CA    1 
ATOM   808  C  C     . LYS   A 1 109 ? 23.14440 3.65525  32.58095  1.000 53.00369  ? 106 LYS   A C     1 
ATOM   809  O  O     . LYS   A 1 109 ? 22.41717 4.57402  32.96878  1.000 52.12850  ? 106 LYS   A O     1 
ATOM   810  C  CB    . LYS   A 1 109 ? 21.74413 2.03786  31.28713  1.000 61.09648  ? 106 LYS   A CB    1 
ATOM   811  C  CG    . LYS   A 1 109 ? 20.37307 2.66585  31.51942  1.000 66.37678  ? 106 LYS   A CG    1 
ATOM   812  C  CD    . LYS   A 1 109 ? 19.26170 1.72468  31.07475  1.000 69.01913  ? 106 LYS   A CD    1 
ATOM   813  C  CE    . LYS   A 1 109 ? 17.90848 2.42817  30.98431  1.000 70.04002  ? 106 LYS   A CE    1 
ATOM   814  N  NZ    . LYS   A 1 109 ? 17.28708 2.67718  32.31584  1.000 70.90157  ? 106 LYS   A NZ    1 
ATOM   815  N  N     . SER   A 1 110 ? 24.15719 3.18288  33.31353  1.000 52.71746  ? 107 SER   A N     1 
ATOM   816  C  CA    . SER   A 1 110 ? 24.40689 3.71119  34.65200  1.000 54.16264  ? 107 SER   A CA    1 
ATOM   817  C  C     . SER   A 1 110 ? 24.81140 5.18176  34.60304  1.000 51.13276  ? 107 SER   A C     1 
ATOM   818  O  O     . SER   A 1 110 ? 24.47946 5.95402  35.51093  1.000 49.96460  ? 107 SER   A O     1 
ATOM   819  C  CB    . SER   A 1 110 ? 25.47710 2.87855  35.35620  1.000 56.48655  ? 107 SER   A CB    1 
ATOM   820  O  OG    . SER   A 1 110 ? 26.72955 3.00584  34.70824  1.000 62.60782  ? 107 SER   A OG    1 
ATOM   821  N  N     . TYR   A 1 111 ? 25.53581 5.58719  33.55616  1.000 48.31773  ? 108 TYR   A N     1 
ATOM   822  C  CA    . TYR   A 1 111 ? 25.79111 7.00972  33.34292  1.000 47.17158  ? 108 TYR   A CA    1 
ATOM   823  C  C     . TYR   A 1 111 ? 24.48277 7.76983  33.18094  1.000 44.78680  ? 108 TYR   A C     1 
ATOM   824  O  O     . TYR   A 1 111 ? 24.28161 8.82999  33.78567  1.000 41.17101  ? 108 TYR   A O     1 
ATOM   825  C  CB    . TYR   A 1 111 ? 26.66780 7.21758  32.10633  1.000 44.29605  ? 108 TYR   A CB    1 
ATOM   826  C  CG    . TYR   A 1 111 ? 28.06303 6.64780  32.19636  1.000 44.67348  ? 108 TYR   A CG    1 
ATOM   827  C  CD1   . TYR   A 1 111 ? 28.66735 6.41407  33.42510  1.000 48.38030  ? 108 TYR   A CD1   1 
ATOM   828  C  CD2   . TYR   A 1 111 ? 28.78294 6.35410  31.04514  1.000 45.56871  ? 108 TYR   A CD2   1 
ATOM   829  C  CE1   . TYR   A 1 111 ? 29.95019 5.89630  33.50351  1.000 49.96590  ? 108 TYR   A CE1   1 
ATOM   830  C  CE2   . TYR   A 1 111 ? 30.06436 5.83578  31.11357  1.000 49.29162  ? 108 TYR   A CE2   1 
ATOM   831  C  CZ    . TYR   A 1 111 ? 30.64210 5.61012  32.34456  1.000 50.36066  ? 108 TYR   A CZ    1 
ATOM   832  O  OH    . TYR   A 1 111 ? 31.91391 5.09401  32.41247  1.000 53.67694  ? 108 TYR   A OH    1 
ATOM   833  N  N     . TYR   A 1 112 ? 23.58027 7.23235  32.35658  1.000 45.67374  ? 109 TYR   A N     1 
ATOM   834  C  CA    . TYR   A 1 112 ? 22.30161 7.88254  32.09507  1.000 46.36406  ? 109 TYR   A CA    1 
ATOM   835  C  C     . TYR   A 1 112 ? 21.47076 8.01950  33.36288  1.000 45.44624  ? 109 TYR   A C     1 
ATOM   836  O  O     . TYR   A 1 112 ? 20.74304 9.00657  33.52295  1.000 45.86431  ? 109 TYR   A O     1 
ATOM   837  C  CB    . TYR   A 1 112 ? 21.54653 7.09201  31.02533  1.000 46.17854  ? 109 TYR   A CB    1 
ATOM   838  C  CG    . TYR   A 1 112 ? 20.13768 7.56135  30.75229  1.000 47.99808  ? 109 TYR   A CG    1 
ATOM   839  C  CD1   . TYR   A 1 112 ? 19.89543 8.78903  30.14879  1.000 46.32595  ? 109 TYR   A CD1   1 
ATOM   840  C  CD2   . TYR   A 1 112 ? 19.04828 6.76142  31.07281  1.000 45.62374  ? 109 TYR   A CD2   1 
ATOM   841  C  CE1   . TYR   A 1 112 ? 18.60569 9.21306  29.88793  1.000 42.36206  ? 109 TYR   A CE1   1 
ATOM   842  C  CE2   . TYR   A 1 112 ? 17.75749 7.17612  30.81444  1.000 44.48865  ? 109 TYR   A CE2   1 
ATOM   843  C  CZ    . TYR   A 1 112 ? 17.54194 8.40158  30.22298  1.000 44.35224  ? 109 TYR   A CZ    1 
ATOM   844  O  OH    . TYR   A 1 112 ? 16.25502 8.81559  29.96927  1.000 44.95609  ? 109 TYR   A OH    1 
ATOM   845  N  N     . GLU   A 1 113 ? 21.57841 7.05296  34.27913  1.000 44.97971  ? 110 GLU   A N     1 
ATOM   846  C  CA    . GLU   A 1 113 ? 20.85396 7.12801  35.54358  1.000 49.69618  ? 110 GLU   A CA    1 
ATOM   847  C  C     . GLU   A 1 113 ? 21.30935 8.29743  36.40800  1.000 48.02579  ? 110 GLU   A C     1 
ATOM   848  O  O     . GLU   A 1 113 ? 20.55185 8.74019  37.27758  1.000 49.41277  ? 110 GLU   A O     1 
ATOM   849  C  CB    . GLU   A 1 113 ? 21.01957 5.82204  36.32340  1.000 58.34120  ? 110 GLU   A CB    1 
ATOM   850  C  CG    . GLU   A 1 113 ? 20.70726 4.56671  35.52216  1.000 67.98134  ? 110 GLU   A CG    1 
ATOM   851  C  CD    . GLU   A 1 113 ? 19.26900 4.11233  35.65921  1.000 76.39509  ? 110 GLU   A CD    1 
ATOM   852  O  OE1   . GLU   A 1 113 ? 19.03682 3.06860  36.30816  1.000 80.29410  ? 110 GLU   A OE1   1 
ATOM   853  O  OE2   . GLU   A 1 113 ? 18.37176 4.79637  35.12242  1.000 78.56811  ? 110 GLU   A OE2   1 
ATOM   854  N  N     . ILE   A 1 114 ? 22.52775 8.80148  36.19869  1.000 46.41406  ? 111 ILE   A N     1 
ATOM   855  C  CA    . ILE   A 1 114 ? 23.00925 9.92812  36.99301  1.000 47.38941  ? 111 ILE   A CA    1 
ATOM   856  C  C     . ILE   A 1 114 ? 22.22948 11.19413 36.65605  1.000 46.03491  ? 111 ILE   A C     1 
ATOM   857  O  O     . ILE   A 1 114 ? 21.86181 11.96989 37.54727  1.000 49.20995  ? 111 ILE   A O     1 
ATOM   858  C  CB    . ILE   A 1 114 ? 24.52287 10.11882 36.78105  1.000 46.78731  ? 111 ILE   A CB    1 
ATOM   859  C  CG1   . ILE   A 1 114 ? 25.28753 8.86962  37.22717  1.000 46.40259  ? 111 ILE   A CG1   1 
ATOM   860  C  CG2   . ILE   A 1 114 ? 25.02362 11.35936 37.51469  1.000 45.45615  ? 111 ILE   A CG2   1 
ATOM   861  C  CD1   . ILE   A 1 114 ? 26.78003 8.93390  36.95637  1.000 45.76289  ? 111 ILE   A CD1   1 
ATOM   862  N  N     . GLY   A 1 115 ? 21.95895 11.42097 35.37264  1.000 42.31239  ? 112 GLY   A N     1 
ATOM   863  C  CA    . GLY   A 1 115 ? 21.26956 12.62244 34.94641  1.000 40.62877  ? 112 GLY   A CA    1 
ATOM   864  C  C     . GLY   A 1 115 ? 19.77062 12.45950 34.79379  1.000 43.25481  ? 112 GLY   A C     1 
ATOM   865  O  O     . GLY   A 1 115 ? 19.04565 13.45127 34.67049  1.000 42.42349  ? 112 GLY   A O     1 
ATOM   866  N  N     . LEU   A 1 116 ? 19.29651 11.21547 34.79805  1.000 44.56846  ? 113 LEU   A N     1 
ATOM   867  C  CA    . LEU   A 1 116 ? 17.86666 10.95664 34.64130  1.000 46.66419  ? 113 LEU   A CA    1 
ATOM   868  C  C     . LEU   A 1 116 ? 16.98173 11.71186 35.63145  1.000 47.58815  ? 113 LEU   A C     1 
ATOM   869  O  O     . LEU   A 1 116 ? 15.92489 12.21026 35.20539  1.000 47.47731  ? 113 LEU   A O     1 
ATOM   870  C  CB    . LEU   A 1 116 ? 17.60662 9.44492  34.72977  1.000 47.47094  ? 113 LEU   A CB    1 
ATOM   871  C  CG    . LEU   A 1 116 ? 16.14012 9.01027  34.65238  1.000 48.94941  ? 113 LEU   A CG    1 
ATOM   872  C  CD1   . LEU   A 1 116 ? 15.48145 9.51833  33.36381  1.000 48.31533  ? 113 LEU   A CD1   1 
ATOM   873  C  CD2   . LEU   A 1 116 ? 16.00742 7.49454  34.77873  1.000 45.16327  ? 113 LEU   A CD2   1 
ATOM   874  N  N     . PRO   A 1 117 ? 17.32012 11.83861 36.92360  1.000 47.70115  ? 114 PRO   A N     1 
ATOM   875  C  CA    . PRO   A 1 117 ? 16.45696 12.63960 37.81110  1.000 49.29701  ? 114 PRO   A CA    1 
ATOM   876  C  C     . PRO   A 1 117 ? 16.24487 14.06310 37.32450  1.000 45.71066  ? 114 PRO   A C     1 
ATOM   877  O  O     . PRO   A 1 117 ? 15.12155 14.57879 37.40221  1.000 44.07727  ? 114 PRO   A O     1 
ATOM   878  C  CB    . PRO   A 1 117 ? 17.20652 12.60291 39.15000  1.000 52.72322  ? 114 PRO   A CB    1 
ATOM   879  C  CG    . PRO   A 1 117 ? 17.98207 11.34114 39.10688  1.000 53.22654  ? 114 PRO   A CG    1 
ATOM   880  C  CD    . PRO   A 1 117 ? 18.40933 11.18624 37.67606  1.000 49.03678  ? 114 PRO   A CD    1 
ATOM   881  N  N     . PHE   A 1 118 ? 17.29708 14.71426 36.82022  1.000 42.70188  ? 115 PHE   A N     1 
ATOM   882  C  CA    . PHE   A 1 118 ? 17.14320 16.06467 36.28742  1.000 44.95514  ? 115 PHE   A CA    1 
ATOM   883  C  C     . PHE   A 1 118 ? 16.26353 16.06548 35.04374  1.000 44.35762  ? 115 PHE   A C     1 
ATOM   884  O  O     . PHE   A 1 118 ? 15.44199 16.97071 34.85446  1.000 45.16163  ? 115 PHE   A O     1 
ATOM   885  C  CB    . PHE   A 1 118 ? 18.51516 16.66658 35.97994  1.000 47.10371  ? 115 PHE   A CB    1 
ATOM   886  C  CG    . PHE   A 1 118 ? 19.47274 16.60281 37.13483  1.000 48.06364  ? 115 PHE   A CG    1 
ATOM   887  C  CD1   . PHE   A 1 118 ? 20.30915 15.51031 37.29716  1.000 47.23221  ? 115 PHE   A CD1   1 
ATOM   888  C  CD2   . PHE   A 1 118 ? 19.52882 17.62741 38.06557  1.000 49.47201  ? 115 PHE   A CD2   1 
ATOM   889  C  CE1   . PHE   A 1 118 ? 21.18551 15.44160 38.36117  1.000 49.56371  ? 115 PHE   A CE1   1 
ATOM   890  C  CE2   . PHE   A 1 118 ? 20.40625 17.56458 39.13421  1.000 50.82936  ? 115 PHE   A CE2   1 
ATOM   891  C  CZ    . PHE   A 1 118 ? 21.23552 16.47029 39.28049  1.000 50.66804  ? 115 PHE   A CZ    1 
ATOM   892  N  N     . ILE   A 1 119 ? 16.42000 15.05309 34.18717  1.000 44.22528  ? 116 ILE   A N     1 
ATOM   893  C  CA    . ILE   A 1 119 ? 15.57781 14.93391 33.00047  1.000 45.64760  ? 116 ILE   A CA    1 
ATOM   894  C  C     . ILE   A 1 119 ? 14.11273 14.78894 33.39700  1.000 48.58080  ? 116 ILE   A C     1 
ATOM   895  O  O     . ILE   A 1 119 ? 13.22297 15.38958 32.78130  1.000 47.88672  ? 116 ILE   A O     1 
ATOM   896  C  CB    . ILE   A 1 119 ? 16.05117 13.75147 32.13524  1.000 44.34214  ? 116 ILE   A CB    1 
ATOM   897  C  CG1   . ILE   A 1 119 ? 17.46839 14.00113 31.61711  1.000 43.14531  ? 116 ILE   A CG1   1 
ATOM   898  C  CG2   . ILE   A 1 119 ? 15.08465 13.49921 30.98861  1.000 43.42122  ? 116 ILE   A CG2   1 
ATOM   899  C  CD1   . ILE   A 1 119 ? 18.01888 12.85186 30.80169  1.000 43.79920  ? 116 ILE   A CD1   1 
ATOM   900  N  N     . GLN   A 1 120 ? 13.83961 13.99819 34.43637  1.000 48.06460  ? 117 GLN   A N     1 
ATOM   901  C  CA    . GLN   A 1 120 ? 12.46017 13.79542 34.86518  1.000 48.71815  ? 117 GLN   A CA    1 
ATOM   902  C  C     . GLN   A 1 120 ? 11.86094 15.07390 35.43379  1.000 51.06581  ? 117 GLN   A C     1 
ATOM   903  O  O     . GLN   A 1 120 ? 10.72427 15.43032 35.10388  1.000 48.37168  ? 117 GLN   A O     1 
ATOM   904  C  CB    . GLN   A 1 120 ? 12.39411 12.66740 35.89112  1.000 50.74582  ? 117 GLN   A CB    1 
ATOM   905  C  CG    . GLN   A 1 120 ? 12.52272 11.28152 35.28149  1.000 56.97748  ? 117 GLN   A CG    1 
ATOM   906  C  CD    . GLN   A 1 120 ? 12.81064 10.21205 36.31229  1.000 62.90444  ? 117 GLN   A CD    1 
ATOM   907  O  OE1   . GLN   A 1 120 ? 13.33116 10.49823 37.39148  1.000 65.10375  ? 117 GLN   A OE1   1 
ATOM   908  N  NE2   . GLN   A 1 120 ? 12.47297 8.96871  35.98566  1.000 64.72735  ? 117 GLN   A NE2   1 
ATOM   909  N  N     . LYS   A 1 121 ? 12.60985 15.78097 36.28444  1.000 54.40069  ? 118 LYS   A N     1 
ATOM   910  C  CA    . LYS   A 1 121 ? 12.09921 17.01365 36.87073  1.000 55.20459  ? 118 LYS   A CA    1 
ATOM   911  C  C     . LYS   A 1 121 ? 11.93082 18.11538 35.83291  1.000 48.83220  ? 118 LYS   A C     1 
ATOM   912  O  O     . LYS   A 1 121 ? 11.12888 19.03102 36.04410  1.000 47.44732  ? 118 LYS   A O     1 
ATOM   913  C  CB    . LYS   A 1 121 ? 13.01986 17.47503 37.99985  1.000 62.51412  ? 118 LYS   A CB    1 
ATOM   914  C  CG    . LYS   A 1 121 ? 12.39880 18.50496 38.92730  1.000 69.98407  ? 118 LYS   A CG    1 
ATOM   915  C  CD    . LYS   A 1 121 ? 13.31867 18.79261 40.10006  1.000 76.84638  ? 118 LYS   A CD    1 
ATOM   916  C  CE    . LYS   A 1 121 ? 12.96750 20.10800 40.77680  1.000 79.90091  ? 118 LYS   A CE    1 
ATOM   917  N  NZ    . LYS   A 1 121 ? 14.08331 20.58351 41.64513  1.000 81.56182  ? 118 LYS   A NZ    1 
ATOM   918  N  N     . ALA   A 1 122 ? 12.66499 18.05059 34.72016  1.000 40.05766  ? 119 ALA   A N     1 
ATOM   919  C  CA    . ALA   A 1 122 ? 12.38673 18.93971 33.60018  1.000 41.23711  ? 119 ALA   A CA    1 
ATOM   920  C  C     . ALA   A 1 122 ? 11.11630 18.54560 32.85850  1.000 43.64018  ? 119 ALA   A C     1 
ATOM   921  O  O     . ALA   A 1 122 ? 10.64089 19.31988 32.02008  1.000 43.66048  ? 119 ALA   A O     1 
ATOM   922  C  CB    . ALA   A 1 122 ? 13.57246 18.96479 32.63123  1.000 40.84771  ? 119 ALA   A CB    1 
ATOM   923  N  N     . GLY   A 1 123 ? 10.56568 17.36654 33.14189  1.000 45.57722  ? 120 GLY   A N     1 
ATOM   924  C  CA    . GLY   A 1 123 ? 9.29454  16.95999 32.57048  1.000 49.08832  ? 120 GLY   A CA    1 
ATOM   925  C  C     . GLY   A 1 123 ? 9.33961  16.57017 31.11105  1.000 49.21989  ? 120 GLY   A C     1 
ATOM   926  O  O     . GLY   A 1 123 ? 8.32699  16.69825 30.41532  1.000 51.15611  ? 120 GLY   A O     1 
ATOM   927  N  N     . VAL   A 1 124 ? 10.48417 16.08569 30.62499  1.000 45.63641  ? 121 VAL   A N     1 
ATOM   928  C  CA    . VAL   A 1 124 ? 10.65860 15.76830 29.21542  1.000 44.47698  ? 121 VAL   A CA    1 
ATOM   929  C  C     . VAL   A 1 124 ? 11.11433 14.33130 28.99703  1.000 45.31559  ? 121 VAL   A C     1 
ATOM   930  O  O     . VAL   A 1 124 ? 11.51698 13.97851 27.88837  1.000 47.21266  ? 121 VAL   A O     1 
ATOM   931  C  CB    . VAL   A 1 124 ? 11.63075 16.75490 28.53795  1.000 43.47843  ? 121 VAL   A CB    1 
ATOM   932  C  CG1   . VAL   A 1 124 ? 11.02877 18.14666 28.50258  1.000 45.37134  ? 121 VAL   A CG1   1 
ATOM   933  C  CG2   . VAL   A 1 124 ? 12.97669 16.76698 29.26044  1.000 40.17836  ? 121 VAL   A CG2   1 
ATOM   934  N  N     . GLU   A 1 125 ? 11.04927 13.48588 30.03041  1.000 45.39604  ? 122 GLU   A N     1 
ATOM   935  C  CA    . GLU   A 1 125 ? 11.49129 12.10289 29.87166  1.000 48.85383  ? 122 GLU   A CA    1 
ATOM   936  C  C     . GLU   A 1 125 ? 10.60410 11.33306 28.89953  1.000 47.48921  ? 122 GLU   A C     1 
ATOM   937  O  O     . GLU   A 1 125 ? 11.07788 10.40458 28.23359  1.000 41.79253  ? 122 GLU   A O     1 
ATOM   938  C  CB    . GLU   A 1 125 ? 11.52149 11.39066 31.22397  1.000 52.38043  ? 122 GLU   A CB    1 
ATOM   939  C  CG    . GLU   A 1 125 ? 12.09116 9.97956  31.15250  1.000 53.18579  ? 122 GLU   A CG    1 
ATOM   940  C  CD    . GLU   A 1 125 ? 11.72429 9.13022  32.35226  1.000 57.12585  ? 122 GLU   A CD    1 
ATOM   941  O  OE1   . GLU   A 1 125 ? 10.82467 9.53474  33.11844  1.000 59.37297  ? 122 GLU   A OE1   1 
ATOM   942  O  OE2   . GLU   A 1 125 ? 12.33664 8.05477  32.52714  1.000 58.28193  ? 122 GLU   A OE2   1 
ATOM   943  N  N     . HIS   A 1 126 ? 9.32611  11.70899 28.79455  1.000 43.07221  ? 123 HIS   A N     1 
ATOM   944  C  CA    . HIS   A 1 126 ? 8.41250  11.02350 27.88750  1.000 44.18270  ? 123 HIS   A CA    1 
ATOM   945  C  C     . HIS   A 1 126 ? 8.86008  11.11117 26.43362  1.000 45.13734  ? 123 HIS   A C     1 
ATOM   946  O  O     . HIS   A 1 126 ? 8.43204  10.28991 25.61711  1.000 48.41446  ? 123 HIS   A O     1 
ATOM   947  C  CB    . HIS   A 1 126 ? 7.00448  11.60402 28.02787  1.000 43.22682  ? 123 HIS   A CB    1 
ATOM   948  C  CG    . HIS   A 1 126 ? 6.85870  12.96925 27.43297  1.000 42.03701  ? 123 HIS   A CG    1 
ATOM   949  N  ND1   . HIS   A 1 126 ? 7.29307  14.11085 28.07223  1.000 42.46706  ? 123 HIS   A ND1   1 
ATOM   950  C  CD2   . HIS   A 1 126 ? 6.34051  13.37381 26.24932  1.000 40.38579  ? 123 HIS   A CD2   1 
ATOM   951  C  CE1   . HIS   A 1 126 ? 7.04775  15.16061 27.30776  1.000 39.24585  ? 123 HIS   A CE1   1 
ATOM   952  N  NE2   . HIS   A 1 126 ? 6.46712  14.74109 26.19823  1.000 42.32246  ? 123 HIS   A NE2   1 
ATOM   953  N  N     . LYS   A 1 127 ? 9.70328  12.08619 26.08892  1.000 44.11762  ? 124 LYS   A N     1 
ATOM   954  C  CA    . LYS   A 1 127 ? 10.18688 12.22918 24.72160  1.000 43.61469  ? 124 LYS   A CA    1 
ATOM   955  C  C     . LYS   A 1 127 ? 11.33812 11.28938 24.39074  1.000 42.46217  ? 124 LYS   A C     1 
ATOM   956  O  O     . LYS   A 1 127 ? 11.72218 11.20229 23.21903  1.000 38.81716  ? 124 LYS   A O     1 
ATOM   957  C  CB    . LYS   A 1 127 ? 10.64835 13.66650 24.46138  1.000 41.88684  ? 124 LYS   A CB    1 
ATOM   958  C  CG    . LYS   A 1 127 ? 9.64698  14.75095 24.82584  1.000 42.55913  ? 124 LYS   A CG    1 
ATOM   959  C  CD    . LYS   A 1 127 ? 10.16940 16.11347 24.38421  1.000 37.87277  ? 124 LYS   A CD    1 
ATOM   960  C  CE    . LYS   A 1 127 ? 9.37905  17.24918 24.99554  1.000 34.61713  ? 124 LYS   A CE    1 
ATOM   961  N  NZ    . LYS   A 1 127 ? 9.86268  18.57408 24.50468  1.000 32.66097  ? 124 LYS   A NZ    1 
ATOM   962  N  N     . ILE   A 1 128 ? 11.89104 10.58887 25.37760  1.000 41.59714  ? 125 ILE   A N     1 
ATOM   963  C  CA    . ILE   A 1 128 ? 13.15528 9.87600  25.23417  1.000 43.71655  ? 125 ILE   A CA    1 
ATOM   964  C  C     . ILE   A 1 128 ? 12.89161 8.37782  25.20895  1.000 45.72981  ? 125 ILE   A C     1 
ATOM   965  O  O     . ILE   A 1 128 ? 12.18486 7.84692  26.07499  1.000 44.82206  ? 125 ILE   A O     1 
ATOM   966  C  CB    . ILE   A 1 128 ? 14.12908 10.23737 26.36829  1.000 40.73114  ? 125 ILE   A CB    1 
ATOM   967  C  CG1   . ILE   A 1 128 ? 14.46183 11.72772 26.32086  1.000 41.65995  ? 125 ILE   A CG1   1 
ATOM   968  C  CG2   . ILE   A 1 128 ? 15.39066 9.38912  26.27861  1.000 40.58051  ? 125 ILE   A CG2   1 
ATOM   969  C  CD1   . ILE   A 1 128 ? 15.14749 12.23492 27.55991  1.000 43.58824  ? 125 ILE   A CD1   1 
ATOM   970  N  N     . ASN   A 1 129 ? 13.46550 7.70078  24.22114  1.000 44.98150  ? 126 ASN   A N     1 
ATOM   971  C  CA    . ASN   A 1 129 ? 13.51937 6.24328  24.16797  1.000 49.51737  ? 126 ASN   A CA    1 
ATOM   972  C  C     . ASN   A 1 129 ? 14.98912 5.86299  24.31802  1.000 47.79056  ? 126 ASN   A C     1 
ATOM   973  O  O     . ASN   A 1 129 ? 15.76946 5.98687  23.37006  1.000 44.82180  ? 126 ASN   A O     1 
ATOM   974  C  CB    . ASN   A 1 129 ? 12.92653 5.71125  22.86559  1.000 50.19496  ? 126 ASN   A CB    1 
ATOM   975  C  CG    . ASN   A 1 129 ? 13.05219 4.20384  22.74058  1.000 52.11686  ? 126 ASN   A CG    1 
ATOM   976  O  OD1   . ASN   A 1 129 ? 13.09305 3.48655  23.74102  1.000 53.57782  ? 126 ASN   A OD1   1 
ATOM   977  N  ND2   . ASN   A 1 129 ? 13.11938 3.71642  21.50740  1.000 52.10288  ? 126 ASN   A ND2   1 
ATOM   978  N  N     . PHE   A 1 130 ? 15.36988 5.42084  25.51378  1.000 46.63241  ? 127 PHE   A N     1 
ATOM   979  C  CA    . PHE   A 1 130 ? 16.75721 5.08327  25.79503  1.000 47.28983  ? 127 PHE   A CA    1 
ATOM   980  C  C     . PHE   A 1 130 ? 17.01494 3.61663  25.47506  1.000 47.55711  ? 127 PHE   A C     1 
ATOM   981  O  O     . PHE   A 1 130 ? 16.28086 2.73491  25.93071  1.000 51.34885  ? 127 PHE   A O     1 
ATOM   982  C  CB    . PHE   A 1 130 ? 17.11161 5.37299  27.25324  1.000 45.83882  ? 127 PHE   A CB    1 
ATOM   983  C  CG    . PHE   A 1 130 ? 18.57130 5.19548  27.55702  1.000 45.70880  ? 127 PHE   A CG    1 
ATOM   984  C  CD1   . PHE   A 1 130 ? 19.06316 3.96615  27.96351  1.000 46.49398  ? 127 PHE   A CD1   1 
ATOM   985  C  CD2   . PHE   A 1 130 ? 19.45488 6.25233  27.41699  1.000 43.77352  ? 127 PHE   A CD2   1 
ATOM   986  C  CE1   . PHE   A 1 130 ? 20.40616 3.79347  28.22917  1.000 45.04737  ? 127 PHE   A CE1   1 
ATOM   987  C  CE2   . PHE   A 1 130 ? 20.80117 6.08678  27.68611  1.000 44.52802  ? 127 PHE   A CE2   1 
ATOM   988  C  CZ    . PHE   A 1 130 ? 21.27535 4.85512  28.09412  1.000 42.20566  ? 127 PHE   A CZ    1 
ATOM   989  N  N     . ILE   A 1 131 ? 18.06657 3.36199  24.70239  1.000 46.12086  ? 128 ILE   A N     1 
ATOM   990  C  CA    . ILE   A 1 131 ? 18.44582 2.01534  24.29036  1.000 45.99426  ? 128 ILE   A CA    1 
ATOM   991  C  C     . ILE   A 1 131 ? 19.85372 1.76250  24.81014  1.000 45.15716  ? 128 ILE   A C     1 
ATOM   992  O  O     . ILE   A 1 131 ? 20.81030 2.41410  24.36954  1.000 40.03802  ? 128 ILE   A O     1 
ATOM   993  C  CB    . ILE   A 1 131 ? 18.37603 1.83942  22.76670  1.000 44.59034  ? 128 ILE   A CB    1 
ATOM   994  C  CG1   . ILE   A 1 131 ? 16.95430 2.11379  22.26240  1.000 48.25066  ? 128 ILE   A CG1   1 
ATOM   995  C  CG2   . ILE   A 1 131 ? 18.84300 0.44329  22.36351  1.000 41.10743  ? 128 ILE   A CG2   1 
ATOM   996  C  CD1   . ILE   A 1 131 ? 16.81866 2.06944  20.75459  1.000 47.88857  ? 128 ILE   A CD1   1 
ATOM   997  N  N     . GLU   A 1 132 ? 19.98491 0.82825  25.75241  1.000 47.06592  ? 129 GLU   A N     1 
ATOM   998  C  CA    . GLU   A 1 132 ? 21.28786 0.47547  26.31506  1.000 50.79803  ? 129 GLU   A CA    1 
ATOM   999  C  C     . GLU   A 1 132 ? 21.92351 -0.58236 25.42406  1.000 50.48837  ? 129 GLU   A C     1 
ATOM   1000 O  O     . GLU   A 1 132 ? 21.61633 -1.77043 25.53931  1.000 53.55106  ? 129 GLU   A O     1 
ATOM   1001 C  CB    . GLU   A 1 132 ? 21.15435 -0.02237 27.74901  1.000 53.92376  ? 129 GLU   A CB    1 
ATOM   1002 C  CG    . GLU   A 1 132 ? 22.49453 -0.33881 28.39152  1.000 59.86500  ? 129 GLU   A CG    1 
ATOM   1003 C  CD    . GLU   A 1 132 ? 22.36138 -0.96027 29.76838  1.000 67.21540  ? 129 GLU   A CD    1 
ATOM   1004 O  OE1   . GLU   A 1 132 ? 21.33196 -1.61894 30.03286  1.000 67.79954  ? 129 GLU   A OE1   1 
ATOM   1005 O  OE2   . GLU   A 1 132 ? 23.29090 -0.78304 30.58663  1.000 69.44029  ? 129 GLU   A OE2   1 
ATOM   1006 N  N     . SER   A 1 133 ? 22.81643 -0.15219 24.53667  1.000 48.87975  ? 130 SER   A N     1 
ATOM   1007 C  CA    . SER   A 1 133 ? 23.47186 -1.05589 23.59875  1.000 52.82270  ? 130 SER   A CA    1 
ATOM   1008 C  C     . SER   A 1 133 ? 24.57234 -0.30165 22.86760  1.000 53.55098  ? 130 SER   A C     1 
ATOM   1009 O  O     . SER   A 1 133 ? 24.69272 0.92154  22.97111  1.000 52.67258  ? 130 SER   A O     1 
ATOM   1010 C  CB    . SER   A 1 133 ? 22.48293 -1.64161 22.58875  1.000 55.23096  ? 130 SER   A CB    1 
ATOM   1011 O  OG    . SER   A 1 133 ? 23.17172 -2.14755 21.45690  1.000 56.07161  ? 130 SER   A OG    1 
ATOM   1012 N  N     . GLU   A 1 134 ? 25.37398 -1.05496 22.12018  1.000 57.07588  ? 131 GLU   A N     1 
ATOM   1013 C  CA    . GLU   A 1 134 ? 26.28544 -0.44990 21.16265  1.000 55.21458  ? 131 GLU   A CA    1 
ATOM   1014 C  C     . GLU   A 1 134 ? 25.48884 0.14598  20.00754  1.000 51.57025  ? 131 GLU   A C     1 
ATOM   1015 O  O     . GLU   A 1 134 ? 24.44335 -0.37430 19.61259  1.000 50.10907  ? 131 GLU   A O     1 
ATOM   1016 C  CB    . GLU   A 1 134 ? 27.28662 -1.48195 20.63939  1.000 54.44196  ? 131 GLU   A CB    1 
ATOM   1017 C  CG    . GLU   A 1 134 ? 27.99436 -2.27332 21.72499  1.000 58.17228  ? 131 GLU   A CG    1 
ATOM   1018 C  CD    . GLU   A 1 134 ? 29.09841 -3.15053 21.17363  1.000 65.45375  ? 131 GLU   A CD    1 
ATOM   1019 O  OE1   . GLU   A 1 134 ? 29.80627 -2.70189 20.24740  1.000 68.23628  ? 131 GLU   A OE1   1 
ATOM   1020 O  OE2   . GLU   A 1 134 ? 29.25577 -4.28965 21.66042  1.000 70.12035  ? 131 GLU   A OE2   1 
ATOM   1021 N  N     . ALA   A 1 135 ? 25.99974 1.24719  19.45761  1.000 50.51648  ? 132 ALA   A N     1 
ATOM   1022 C  CA    . ALA   A 1 135 ? 25.21847 2.01973  18.49563  1.000 53.02170  ? 132 ALA   A CA    1 
ATOM   1023 C  C     . ALA   A 1 135 ? 25.09389 1.30496  17.15497  1.000 52.55108  ? 132 ALA   A C     1 
ATOM   1024 O  O     . ALA   A 1 135 ? 24.01339 1.29707  16.55506  1.000 52.53709  ? 132 ALA   A O     1 
ATOM   1025 C  CB    . ALA   A 1 135 ? 25.83784 3.40504  18.31049  1.000 51.59761  ? 132 ALA   A CB    1 
ATOM   1026 N  N     . LEU   A 1 136 ? 26.18268 0.70907  16.66076  1.000 53.16319  ? 133 LEU   A N     1 
ATOM   1027 C  CA    . LEU   A 1 136 ? 26.15661 0.09782  15.33526  1.000 56.40175  ? 133 LEU   A CA    1 
ATOM   1028 C  C     . LEU   A 1 136 ? 25.09248 -0.98828 15.18701  1.000 54.43111  ? 133 LEU   A C     1 
ATOM   1029 O  O     . LEU   A 1 136 ? 24.37985 -0.97833 14.17543  1.000 55.59631  ? 133 LEU   A O     1 
ATOM   1030 C  CB    . LEU   A 1 136 ? 27.54543 -0.44062 14.97333  1.000 60.11137  ? 133 LEU   A CB    1 
ATOM   1031 C  CG    . LEU   A 1 136 ? 28.51529 0.53683  14.30512  1.000 63.79712  ? 133 LEU   A CG    1 
ATOM   1032 C  CD1   . LEU   A 1 136 ? 29.81940 -0.16534 13.96262  1.000 64.85076  ? 133 LEU   A CD1   1 
ATOM   1033 C  CD2   . LEU   A 1 136 ? 27.89097 1.14433  13.05781  1.000 65.53800  ? 133 LEU   A CD2   1 
ATOM   1034 N  N     . PRO   A 1 137 ? 24.94039 -1.93824 16.12341  1.000 53.56654  ? 134 PRO   A N     1 
ATOM   1035 C  CA    . PRO   A 1 137 ? 23.83901 -2.90661 15.96251  1.000 53.68045  ? 134 PRO   A CA    1 
ATOM   1036 C  C     . PRO   A 1 137 ? 22.46850 -2.25645 15.94093  1.000 55.38570  ? 134 PRO   A C     1 
ATOM   1037 O  O     . PRO   A 1 137 ? 21.60053 -2.67750 15.16443  1.000 55.59855  ? 134 PRO   A O     1 
ATOM   1038 C  CB    . PRO   A 1 137 ? 24.01199 -3.83105 17.17657  1.000 53.83754  ? 134 PRO   A CB    1 
ATOM   1039 C  CG    . PRO   A 1 137 ? 25.44213 -3.71836 17.53168  1.000 53.23037  ? 134 PRO   A CG    1 
ATOM   1040 C  CD    . PRO   A 1 137 ? 25.79770 -2.28877 17.26730  1.000 52.16976  ? 134 PRO   A CD    1 
ATOM   1041 N  N     . VAL   A 1 138 ? 22.24816 -1.23640 16.77419  1.000 53.89466  ? 135 VAL   A N     1 
ATOM   1042 C  CA    . VAL   A 1 138 ? 20.95103 -0.56822 16.80128  1.000 54.62339  ? 135 VAL   A CA    1 
ATOM   1043 C  C     . VAL   A 1 138 ? 20.71029 0.18431  15.49756  1.000 53.40427  ? 135 VAL   A C     1 
ATOM   1044 O  O     . VAL   A 1 138 ? 19.61086 0.13312  14.93119  1.000 53.48215  ? 135 VAL   A O     1 
ATOM   1045 C  CB    . VAL   A 1 138 ? 20.85419 0.36372  18.02388  1.000 54.24568  ? 135 VAL   A CB    1 
ATOM   1046 C  CG1   . VAL   A 1 138 ? 19.47405 0.99677  18.10233  1.000 53.49265  ? 135 VAL   A CG1   1 
ATOM   1047 C  CG2   . VAL   A 1 138 ? 21.16502 -0.39888 19.30415  1.000 55.20577  ? 135 VAL   A CG2   1 
ATOM   1048 N  N     . LEU   A 1 139 ? 21.73455 0.88321  14.99500  1.000 49.77937  ? 136 LEU   A N     1 
ATOM   1049 C  CA    . LEU   A 1 139 ? 21.58949 1.62115  13.74269  1.000 51.66115  ? 136 LEU   A CA    1 
ATOM   1050 C  C     . LEU   A 1 139 ? 21.28385 0.68825  12.57700  1.000 57.47591  ? 136 LEU   A C     1 
ATOM   1051 O  O     . LEU   A 1 139 ? 20.48554 1.02753  11.69540  1.000 58.01627  ? 136 LEU   A O     1 
ATOM   1052 C  CB    . LEU   A 1 139 ? 22.85494 2.42925  13.45522  1.000 46.25100  ? 136 LEU   A CB    1 
ATOM   1053 C  CG    . LEU   A 1 139 ? 23.16952 3.58444  14.40445  1.000 44.74505  ? 136 LEU   A CG    1 
ATOM   1054 C  CD1   . LEU   A 1 139 ? 24.42440 4.31503  13.95025  1.000 43.00716  ? 136 LEU   A CD1   1 
ATOM   1055 C  CD2   . LEU   A 1 139 ? 21.99007 4.53960  14.49431  1.000 42.45652  ? 136 LEU   A CD2   1 
ATOM   1056 N  N     . ASP   A 1 140 ? 21.91639 -0.48865 12.54906  1.000 60.79305  ? 137 ASP   A N     1 
ATOM   1057 C  CA    . ASP   A 1 140 ? 21.67030 -1.43266 11.46282  1.000 62.21993  ? 137 ASP   A CA    1 
ATOM   1058 C  C     . ASP   A 1 140 ? 20.24687 -1.97243 11.51021  1.000 67.94367  ? 137 ASP   A C     1 
ATOM   1059 O  O     . ASP   A 1 140 ? 19.60710 -2.14377 10.46583  1.000 72.13140  ? 137 ASP   A O     1 
ATOM   1060 C  CB    . ASP   A 1 140 ? 22.68121 -2.57830 11.51690  1.000 61.35252  ? 137 ASP   A CB    1 
ATOM   1061 C  CG    . ASP   A 1 140 ? 24.05563 -2.16998 11.01619  1.000 61.66477  ? 137 ASP   A CG    1 
ATOM   1062 O  OD1   . ASP   A 1 140 ? 24.13200 -1.28679 10.13553  1.000 61.22719  ? 137 ASP   A OD1   1 
ATOM   1063 O  OD2   . ASP   A 1 140 ? 25.06088 -2.73501 11.49950  1.000 62.50632  ? 137 ASP   A OD2   1 
ATOM   1064 N  N     . GLN   A 1 141 ? 19.73420 -2.25333 12.70967  1.000 68.68514  ? 138 GLN   A N     1 
ATOM   1065 C  CA    . GLN   A 1 141 ? 18.34869 -2.69337 12.82228  1.000 71.76771  ? 138 GLN   A CA    1 
ATOM   1066 C  C     . GLN   A 1 141 ? 17.38222 -1.56741 12.48045  1.000 71.76786  ? 138 GLN   A C     1 
ATOM   1067 O  O     . GLN   A 1 141 ? 16.28328 -1.82684 11.97789  1.000 73.21982  ? 138 GLN   A O     1 
ATOM   1068 C  CB    . GLN   A 1 141 ? 18.07856 -3.23013 14.22930  1.000 75.06398  ? 138 GLN   A CB    1 
ATOM   1069 C  CG    . GLN   A 1 141 ? 16.69406 -3.83551 14.42270  1.000 78.85281  ? 138 GLN   A CG    1 
ATOM   1070 C  CD    . GLN   A 1 141 ? 16.49150 -5.12681 13.64457  1.000 82.85149  ? 138 GLN   A CD    1 
ATOM   1071 O  OE1   . GLN   A 1 141 ? 17.43989 -5.70303 13.10856  1.000 84.35305  ? 138 GLN   A OE1   1 
ATOM   1072 N  NE2   . GLN   A 1 141 ? 15.24660 -5.58901 13.58376  1.000 83.60132  ? 138 GLN   A NE2   1 
ATOM   1073 N  N     . MET   A 1 142 ? 17.77640 -0.31627 12.73278  1.000 69.15322  ? 139 MET   A N     1 
ATOM   1074 C  CA    . MET   A 1 142 ? 16.94204 0.81581  12.34439  1.000 69.50048  ? 139 MET   A CA    1 
ATOM   1075 C  C     . MET   A 1 142 ? 16.83003 0.93037  10.83129  1.000 70.23910  ? 139 MET   A C     1 
ATOM   1076 O  O     . MET   A 1 142 ? 15.75178 1.22643  10.30668  1.000 71.49785  ? 139 MET   A O     1 
ATOM   1077 C  CB    . MET   A 1 142 ? 17.50234 2.11015  12.92456  1.000 68.24481  ? 139 MET   A CB    1 
ATOM   1078 C  CG    . MET   A 1 142 ? 17.26670 2.28368  14.40076  1.000 68.75293  ? 139 MET   A CG    1 
ATOM   1079 S  SD    . MET   A 1 142 ? 18.04103 3.79435  14.98508  1.000 68.61443  ? 139 MET   A SD    1 
ATOM   1080 C  CE    . MET   A 1 142 ? 17.64263 3.69295  16.71795  1.000 71.29093  ? 139 MET   A CE    1 
ATOM   1081 N  N     . LEU   A 1 143 ? 17.93446 0.71343  10.11319  1.000 71.98653  ? 140 LEU   A N     1 
ATOM   1082 C  CA    . LEU   A 1 143 ? 17.88938 0.79938  8.65785   1.000 76.47638  ? 140 LEU   A CA    1 
ATOM   1083 C  C     . LEU   A 1 143 ? 17.04514 -0.31451 8.05248   1.000 84.50669  ? 140 LEU   A C     1 
ATOM   1084 O  O     . LEU   A 1 143 ? 16.41506 -0.11231 7.00802   1.000 85.64643  ? 140 LEU   A O     1 
ATOM   1085 C  CB    . LEU   A 1 143 ? 19.30318 0.76728  8.07938   1.000 76.04429  ? 140 LEU   A CB    1 
ATOM   1086 C  CG    . LEU   A 1 143 ? 19.78933 2.09422  7.49506   1.000 77.33338  ? 140 LEU   A CG    1 
ATOM   1087 C  CD1   . LEU   A 1 143 ? 21.12077 1.91040  6.78669   1.000 77.79065  ? 140 LEU   A CD1   1 
ATOM   1088 C  CD2   . LEU   A 1 143 ? 18.74781 2.67468  6.54897   1.000 78.86143  ? 140 LEU   A CD2   1 
ATOM   1089 N  N     . GLU   A 1 144 ? 17.01803 -1.49005 8.68605   1.000 89.80364  ? 141 GLU   A N     1 
ATOM   1090 C  CA    . GLU   A 1 144 ? 16.16854 -2.57402 8.20713   1.000 93.07646  ? 141 GLU   A CA    1 
ATOM   1091 C  C     . GLU   A 1 144 ? 14.69219 -2.31822 8.47892   1.000 92.84814  ? 141 GLU   A C     1 
ATOM   1092 O  O     . GLU   A 1 144 ? 13.84159 -2.92537 7.82025   1.000 96.88443  ? 141 GLU   A O     1 
ATOM   1093 C  CB    . GLU   A 1 144 ? 16.59168 -3.89806 8.84699   1.000 97.62169  ? 141 GLU   A CB    1 
ATOM   1094 C  CG    . GLU   A 1 144 ? 17.65787 -4.65300 8.06962   1.000 102.39937 ? 141 GLU   A CG    1 
ATOM   1095 C  CD    . GLU   A 1 144 ? 18.31558 -5.74577 8.89065   1.000 106.46626 ? 141 GLU   A CD    1 
ATOM   1096 O  OE1   . GLU   A 1 144 ? 19.22253 -6.42519 8.36317   1.000 107.37115 ? 141 GLU   A OE1   1 
ATOM   1097 O  OE2   . GLU   A 1 144 ? 17.93147 -5.92129 10.06646  1.000 107.87930 ? 141 GLU   A OE2   1 
ATOM   1098 N  N     . GLU   A 1 145 ? 14.36900 -1.42957 9.42189   1.000 87.42751  ? 142 GLU   A N     1 
ATOM   1099 C  CA    . GLU   A 1 145 ? 12.99051 -1.18794 9.82456   1.000 87.76178  ? 142 GLU   A CA    1 
ATOM   1100 C  C     . GLU   A 1 145 ? 12.43392 0.15785  9.38775   1.000 85.63975  ? 142 GLU   A C     1 
ATOM   1101 O  O     . GLU   A 1 145 ? 11.21128 0.32597  9.38513   1.000 86.54395  ? 142 GLU   A O     1 
ATOM   1102 C  CB    . GLU   A 1 145 ? 12.85790 -1.28397 11.35171  1.000 89.19925  ? 142 GLU   A CB    1 
ATOM   1103 C  CG    . GLU   A 1 145 ? 12.69657 -2.69362 11.88452  1.000 92.82732  ? 142 GLU   A CG    1 
ATOM   1104 C  CD    . GLU   A 1 145 ? 12.89787 -2.77066 13.38628  1.000 94.47923  ? 142 GLU   A CD    1 
ATOM   1105 O  OE1   . GLU   A 1 145 ? 13.50673 -3.75735 13.85291  1.000 95.42206  ? 142 GLU   A OE1   1 
ATOM   1106 O  OE2   . GLU   A 1 145 ? 12.45813 -1.84152 14.09891  1.000 93.64393  ? 142 GLU   A OE2   1 
ATOM   1107 N  N     . MET   A 1 146 ? 13.28313 1.11079  9.02200   1.000 98.86078  ? 143 MET   A N     1 
ATOM   1108 C  CA    . MET   A 1 146 ? 12.84157 2.48807  8.85743   1.000 99.13070  ? 143 MET   A CA    1 
ATOM   1109 C  C     . MET   A 1 146 ? 12.09576 2.67298  7.54271   1.000 98.46382  ? 143 MET   A C     1 
ATOM   1110 O  O     . MET   A 1 146 ? 12.56795 2.25265  6.48106   1.000 96.31898  ? 143 MET   A O     1 
ATOM   1111 C  CB    . MET   A 1 146 ? 14.03458 3.44100  8.92307   1.000 99.64736  ? 143 MET   A CB    1 
ATOM   1112 C  CG    . MET   A 1 146 ? 13.65153 4.89123  9.14997   1.000 102.06157 ? 143 MET   A CG    1 
ATOM   1113 S  SD    . MET   A 1 146 ? 14.58280 5.63004  10.50508  1.000 104.87342 ? 143 MET   A SD    1 
ATOM   1114 C  CE    . MET   A 1 146 ? 14.24772 4.47002  11.82966  1.000 106.86668 ? 143 MET   A CE    1 
ATOM   1115 N  N     . LYS   A 1 147 ? 10.92761 3.30067  7.62237   1.000 99.25165  ? 144 LYS   A N     1 
ATOM   1116 C  CA    . LYS   A 1 147 ? 10.20270 3.75261  6.44753   1.000 100.68124 ? 144 LYS   A CA    1 
ATOM   1117 C  C     . LYS   A 1 147 ? 10.58967 5.19164  6.12348   1.000 106.02728 ? 144 LYS   A C     1 
ATOM   1118 O  O     . LYS   A 1 147 ? 11.11000 5.92588  6.96813   1.000 105.73335 ? 144 LYS   A O     1 
ATOM   1119 C  CB    . LYS   A 1 147 ? 8.69208  3.64775  6.66559   1.000 98.67063  ? 144 LYS   A CB    1 
ATOM   1120 C  CG    . LYS   A 1 147 ? 8.19623  2.23569  6.93161   1.000 96.45211  ? 144 LYS   A CG    1 
ATOM   1121 N  N     . GLU   A 1 148 ? 10.32816 5.58766  4.87412   1.000 111.47603 ? 145 GLU   A N     1 
ATOM   1122 C  CA    . GLU   A 1 148 ? 10.65658 6.94106  4.43848   1.000 115.09868 ? 145 GLU   A CA    1 
ATOM   1123 C  C     . GLU   A 1 148 ? 9.95134  7.98968  5.29061   1.000 116.15828 ? 145 GLU   A C     1 
ATOM   1124 O  O     . GLU   A 1 148 ? 10.48005 9.08917  5.49059   1.000 117.89711 ? 145 GLU   A O     1 
ATOM   1125 C  CB    . GLU   A 1 148 ? 10.28854 7.11258  2.96257   1.000 119.78305 ? 145 GLU   A CB    1 
ATOM   1126 C  CG    . GLU   A 1 148 ? 11.28376 7.92472  2.14058   1.000 124.21697 ? 145 GLU   A CG    1 
ATOM   1127 C  CD    . GLU   A 1 148 ? 11.08108 9.42189  2.27137   1.000 126.76269 ? 145 GLU   A CD    1 
ATOM   1128 O  OE1   . GLU   A 1 148 ? 11.97280 10.18130 1.83603   1.000 126.47905 ? 145 GLU   A OE1   1 
ATOM   1129 O  OE2   . GLU   A 1 148 ? 10.03126 9.84028  2.80406   1.000 127.75400 ? 145 GLU   A OE2   1 
ATOM   1130 N  N     . GLU   A 1 149 ? 8.76559  7.66625  5.81198   1.000 109.39743 ? 146 GLU   A N     1 
ATOM   1131 C  CA    . GLU   A 1 149 ? 8.02295  8.59819  6.65180   1.000 101.45683 ? 146 GLU   A CA    1 
ATOM   1132 C  C     . GLU   A 1 149 ? 8.56634  8.68296  8.07259   1.000 94.25735  ? 146 GLU   A C     1 
ATOM   1133 O  O     . GLU   A 1 149 ? 8.04891  9.47703  8.86450   1.000 93.29324  ? 146 GLU   A O     1 
ATOM   1134 C  CB    . GLU   A 1 149 ? 6.54485  8.20063  6.69037   1.000 102.84890 ? 146 GLU   A CB    1 
ATOM   1135 N  N     . ASP   A 1 150 ? 9.58833  7.89882  8.41353   1.000 88.55612  ? 147 ASP   A N     1 
ATOM   1136 C  CA    . ASP   A 1 150 ? 10.10891 7.84083  9.77238   1.000 82.82433  ? 147 ASP   A CA    1 
ATOM   1137 C  C     . ASP   A 1 150 ? 11.50112 8.43784  9.91793   1.000 74.27808  ? 147 ASP   A C     1 
ATOM   1138 O  O     . ASP   A 1 150 ? 12.04630 8.42589  11.02598  1.000 72.93857  ? 147 ASP   A O     1 
ATOM   1139 C  CB    . ASP   A 1 150 ? 10.12896 6.38948  10.26720  1.000 88.11442  ? 147 ASP   A CB    1 
ATOM   1140 C  CG    . ASP   A 1 150 ? 8.73996  5.84132  10.52917  1.000 90.51094  ? 147 ASP   A CG    1 
ATOM   1141 O  OD1   . ASP   A 1 150 ? 7.84749  6.63174  10.90342  1.000 89.00788  ? 147 ASP   A OD1   1 
ATOM   1142 O  OD2   . ASP   A 1 150 ? 8.54228  4.61797  10.36315  1.000 91.49733  ? 147 ASP   A OD2   1 
ATOM   1143 N  N     . LEU   A 1 151 ? 12.08649 8.96042  8.84279   1.000 68.66614  ? 148 LEU   A N     1 
ATOM   1144 C  CA    . LEU   A 1 151 ? 13.46342 9.43592  8.89104   1.000 64.15010  ? 148 LEU   A CA    1 
ATOM   1145 C  C     . LEU   A 1 151 ? 13.62218 10.56071 9.91096   1.000 59.00186  ? 148 LEU   A C     1 
ATOM   1146 O  O     . LEU   A 1 151 ? 12.71817 11.37432 10.12349  1.000 57.42974  ? 148 LEU   A O     1 
ATOM   1147 C  CB    . LEU   A 1 151 ? 13.90590 9.91112  7.50635   1.000 63.96548  ? 148 LEU   A CB    1 
ATOM   1148 C  CG    . LEU   A 1 151 ? 13.99714 8.82844  6.42859   1.000 65.61269  ? 148 LEU   A CG    1 
ATOM   1149 C  CD1   . LEU   A 1 151 ? 14.10582 9.45580  5.04907   1.000 64.60242  ? 148 LEU   A CD1   1 
ATOM   1150 C  CD2   . LEU   A 1 151 ? 15.17742 7.90545  6.69362   1.000 65.28083  ? 148 LEU   A CD2   1 
ATOM   1151 N  N     . TYR   A 1 152 ? 14.79058 10.59560 10.54786  1.000 54.44031  ? 149 TYR   A N     1 
ATOM   1152 C  CA    . TYR   A 1 152 ? 15.06812 11.57729 11.58600  1.000 49.74976  ? 149 TYR   A CA    1 
ATOM   1153 C  C     . TYR   A 1 152 ? 15.43930 12.92704 10.98187  1.000 42.51359  ? 149 TYR   A C     1 
ATOM   1154 O  O     . TYR   A 1 152 ? 15.98782 13.01286 9.87894   1.000 41.19678  ? 149 TYR   A O     1 
ATOM   1155 C  CB    . TYR   A 1 152 ? 16.20176 11.09561 12.49384  1.000 52.78695  ? 149 TYR   A CB    1 
ATOM   1156 C  CG    . TYR   A 1 152 ? 15.86719 9.87661  13.32775  1.000 60.31580  ? 149 TYR   A CG    1 
ATOM   1157 C  CD1   . TYR   A 1 152 ? 15.22919 10.00516 14.55536  1.000 60.57080  ? 149 TYR   A CD1   1 
ATOM   1158 C  CD2   . TYR   A 1 152 ? 16.19969 8.59812  12.89311  1.000 63.77470  ? 149 TYR   A CD2   1 
ATOM   1159 C  CE1   . TYR   A 1 152 ? 14.92600 8.89777  15.32338  1.000 61.65651  ? 149 TYR   A CE1   1 
ATOM   1160 C  CE2   . TYR   A 1 152 ? 15.89882 7.48221  13.65504  1.000 63.26297  ? 149 TYR   A CE2   1 
ATOM   1161 C  CZ    . TYR   A 1 152 ? 15.26148 7.63873  14.86930  1.000 63.74163  ? 149 TYR   A CZ    1 
ATOM   1162 O  OH    . TYR   A 1 152 ? 14.95995 6.53582  15.63664  1.000 66.07928  ? 149 TYR   A OH    1 
ATOM   1163 N  N     . ASP   A 1 153 ? 15.13418 13.99180 11.72679  1.000 37.83805  ? 150 ASP   A N     1 
ATOM   1164 C  CA    . ASP   A 1 153 ? 15.54014 15.33149 11.31923  1.000 39.41318  ? 150 ASP   A CA    1 
ATOM   1165 C  C     . ASP   A 1 153 ? 16.98386 15.62981 11.69170  1.000 40.18637  ? 150 ASP   A C     1 
ATOM   1166 O  O     . ASP   A 1 153 ? 17.66615 16.36748 10.97304  1.000 37.77761  ? 150 ASP   A O     1 
ATOM   1167 C  CB    . ASP   A 1 153 ? 14.64730 16.38839 11.97105  1.000 37.97455  ? 150 ASP   A CB    1 
ATOM   1168 C  CG    . ASP   A 1 153 ? 13.19340 16.25319 11.58315  1.000 38.44471  ? 150 ASP   A CG    1 
ATOM   1169 O  OD1   . ASP   A 1 153 ? 12.90107 16.12583 10.37513  1.000 39.45109  ? 150 ASP   A OD1   1 
ATOM   1170 O  OD2   . ASP   A 1 153 ? 12.34263 16.27617 12.49532  1.000 36.15554  ? 150 ASP   A OD2   1 
ATOM   1171 N  N     . TYR   A 1 154 ? 17.45922 15.07243 12.80172  1.000 42.98819  ? 151 TYR   A N     1 
ATOM   1172 C  CA    . TYR   A 1 154 ? 18.67564 15.54653 13.44135  1.000 40.51809  ? 151 TYR   A CA    1 
ATOM   1173 C  C     . TYR   A 1 154 ? 19.35557 14.37696 14.13393  1.000 37.12987  ? 151 TYR   A C     1 
ATOM   1174 O  O     . TYR   A 1 154 ? 18.68670 13.51657 14.71083  1.000 38.18325  ? 151 TYR   A O     1 
ATOM   1175 C  CB    . TYR   A 1 154 ? 18.33275 16.66678 14.43235  1.000 42.10517  ? 151 TYR   A CB    1 
ATOM   1176 C  CG    . TYR   A 1 154 ? 19.43450 17.11757 15.36876  1.000 43.38717  ? 151 TYR   A CG    1 
ATOM   1177 C  CD1   . TYR   A 1 154 ? 19.67559 16.44980 16.56511  1.000 45.62466  ? 151 TYR   A CD1   1 
ATOM   1178 C  CD2   . TYR   A 1 154 ? 20.19146 18.24837 15.08665  1.000 43.83768  ? 151 TYR   A CD2   1 
ATOM   1179 C  CE1   . TYR   A 1 154 ? 20.66474 16.87249 17.43396  1.000 48.21983  ? 151 TYR   A CE1   1 
ATOM   1180 C  CE2   . TYR   A 1 154 ? 21.18334 18.68037 15.95079  1.000 46.20630  ? 151 TYR   A CE2   1 
ATOM   1181 C  CZ    . TYR   A 1 154 ? 21.41295 17.98831 17.12387  1.000 49.20598  ? 151 TYR   A CZ    1 
ATOM   1182 O  OH    . TYR   A 1 154 ? 22.39399 18.40809 17.99180  1.000 51.18541  ? 151 TYR   A OH    1 
ATOM   1183 N  N     . ALA   A 1 155 ? 20.68382 14.35105 14.06881  1.000 35.85380  ? 152 ALA   A N     1 
ATOM   1184 C  CA    . ALA   A 1 155 ? 21.47481 13.29877 14.69065  1.000 35.64723  ? 152 ALA   A CA    1 
ATOM   1185 C  C     . ALA   A 1 155 ? 22.70777 13.91413 15.33087  1.000 36.84792  ? 152 ALA   A C     1 
ATOM   1186 O  O     . ALA   A 1 155 ? 23.43522 14.66585 14.67616  1.000 39.93549  ? 152 ALA   A O     1 
ATOM   1187 C  CB    . ALA   A 1 155 ? 21.88912 12.23899 13.66493  1.000 36.72386  ? 152 ALA   A CB    1 
ATOM   1188 N  N     . PHE   A 1 156 ? 22.94182 13.59495 16.60140  1.000 37.32390  ? 153 PHE   A N     1 
ATOM   1189 C  CA    . PHE   A 1 156 ? 24.11912 14.05728 17.32696  1.000 36.05090  ? 153 PHE   A CA    1 
ATOM   1190 C  C     . PHE   A 1 156 ? 24.99009 12.85083 17.65303  1.000 36.90138  ? 153 PHE   A C     1 
ATOM   1191 O  O     . PHE   A 1 156 ? 24.53884 11.92129 18.33222  1.000 35.36837  ? 153 PHE   A O     1 
ATOM   1192 C  CB    . PHE   A 1 156 ? 23.72467 14.81368 18.59735  1.000 31.14923  ? 153 PHE   A CB    1 
ATOM   1193 C  CG    . PHE   A 1 156 ? 24.88657 15.45445 19.30657  1.000 32.56189  ? 153 PHE   A CG    1 
ATOM   1194 C  CD1   . PHE   A 1 156 ? 25.63998 16.43771 18.68179  1.000 34.55804  ? 153 PHE   A CD1   1 
ATOM   1195 C  CD2   . PHE   A 1 156 ? 25.22056 15.08102 20.59868  1.000 33.63622  ? 153 PHE   A CD2   1 
ATOM   1196 C  CE1   . PHE   A 1 156 ? 26.71185 17.02890 19.32682  1.000 36.27021  ? 153 PHE   A CE1   1 
ATOM   1197 C  CE2   . PHE   A 1 156 ? 26.29102 15.67193 21.25380  1.000 38.20078  ? 153 PHE   A CE2   1 
ATOM   1198 C  CZ    . PHE   A 1 156 ? 27.03779 16.64650 20.61423  1.000 38.62676  ? 153 PHE   A CZ    1 
ATOM   1199 N  N     . VAL   A 1 157 ? 26.22870 12.86470 17.16356  1.000 35.88267  ? 154 VAL   A N     1 
ATOM   1200 C  CA    . VAL   A 1 157 ? 27.14630 11.73611 17.27906  1.000 38.45611  ? 154 VAL   A CA    1 
ATOM   1201 C  C     . VAL   A 1 157 ? 28.26339 12.11497 18.24226  1.000 41.18853  ? 154 VAL   A C     1 
ATOM   1202 O  O     . VAL   A 1 157 ? 29.06968 13.01095 17.95233  1.000 36.04481  ? 154 VAL   A O     1 
ATOM   1203 C  CB    . VAL   A 1 157 ? 27.71404 11.33154 15.91194  1.000 40.65505  ? 154 VAL   A CB    1 
ATOM   1204 C  CG1   . VAL   A 1 157 ? 28.59755 10.09867 16.05351  1.000 41.84343  ? 154 VAL   A CG1   1 
ATOM   1205 C  CG2   . VAL   A 1 157 ? 26.58912 11.08576 14.92419  1.000 42.76710  ? 154 VAL   A CG2   1 
ATOM   1206 N  N     . ASP   A 1 158 ? 28.32082 11.41851 19.37861  1.000 43.60630  ? 155 ASP   A N     1 
ATOM   1207 C  CA    . ASP   A 1 158 ? 29.26316 11.76509 20.43247  1.000 42.10764  ? 155 ASP   A CA    1 
ATOM   1208 C  C     . ASP   A 1 158 ? 29.65562 10.52028 21.22178  1.000 40.26280  ? 155 ASP   A C     1 
ATOM   1209 O  O     . ASP   A 1 158 ? 29.71759 10.56171 22.45015  1.000 36.66114  ? 155 ASP   A O     1 
ATOM   1210 C  CB    . ASP   A 1 158 ? 28.64443 12.82281 21.35493  1.000 42.03169  ? 155 ASP   A CB    1 
ATOM   1211 C  CG    . ASP   A 1 158 ? 29.67203 13.53416 22.22237  1.000 43.83588  ? 155 ASP   A CG    1 
ATOM   1212 O  OD1   . ASP   A 1 158 ? 30.87737 13.44334 21.92320  1.000 48.16941  ? 155 ASP   A OD1   1 
ATOM   1213 O  OD2   . ASP   A 1 158 ? 29.26627 14.18245 23.21516  1.000 43.00182  ? 155 ASP   A OD2   1 
ATOM   1214 N  N     . ALA   A 1 159 ? 29.92695 9.40658  20.54145  1.000 41.91185  ? 156 ALA   A N     1 
ATOM   1215 C  CA    . ALA   A 1 159 ? 30.22277 8.15881  21.24053  1.000 42.49826  ? 156 ALA   A CA    1 
ATOM   1216 C  C     . ALA   A 1 159 ? 31.66463 7.71190  21.05041  1.000 43.67021  ? 156 ALA   A C     1 
ATOM   1217 O  O     . ALA   A 1 159 ? 32.60213 8.47452  21.30057  1.000 44.44739  ? 156 ALA   A O     1 
ATOM   1218 C  CB    . ALA   A 1 159 ? 29.27469 7.04824  20.77317  1.000 42.38944  ? 156 ALA   A CB    1 
ATOM   1219 N  N     . ASP   A 1 160 ? 31.83667 6.45739  20.64589  1.000 47.19772  ? 157 ASP   A N     1 
ATOM   1220 C  CA    . ASP   A 1 160 ? 33.15134 5.89168  20.37195  1.000 51.02386  ? 157 ASP   A CA    1 
ATOM   1221 C  C     . ASP   A 1 160 ? 33.78605 6.63871  19.20855  1.000 46.04300  ? 157 ASP   A C     1 
ATOM   1222 O  O     . ASP   A 1 160 ? 33.32074 6.53986  18.06844  1.000 45.34675  ? 157 ASP   A O     1 
ATOM   1223 C  CB    . ASP   A 1 160 ? 33.03315 4.40475  20.05744  1.000 61.89560  ? 157 ASP   A CB    1 
ATOM   1224 C  CG    . ASP   A 1 160 ? 34.38199 3.74807  19.88420  1.000 72.34846  ? 157 ASP   A CG    1 
ATOM   1225 O  OD1   . ASP   A 1 160 ? 35.37222 4.33428  20.36169  1.000 74.70367  ? 157 ASP   A OD1   1 
ATOM   1226 O  OD2   . ASP   A 1 160 ? 34.45109 2.67074  19.26051  1.000 77.19093  ? 157 ASP   A OD2   1 
ATOM   1227 N  N     . LYS   A 1 161 ? 34.86888 7.36277  19.49465  1.000 40.99371  ? 158 LYS   A N     1 
ATOM   1228 C  CA    . LYS   A 1 161 ? 35.43645 8.28104  18.51322  1.000 43.43353  ? 158 LYS   A CA    1 
ATOM   1229 C  C     . LYS   A 1 161 ? 35.90598 7.55386  17.25820  1.000 49.48279  ? 158 LYS   A C     1 
ATOM   1230 O  O     . LYS   A 1 161 ? 35.65049 8.01028  16.13765  1.000 54.24812  ? 158 LYS   A O     1 
ATOM   1231 C  CB    . LYS   A 1 161 ? 36.58233 9.06538  19.14807  1.000 42.35688  ? 158 LYS   A CB    1 
ATOM   1232 C  CG    . LYS   A 1 161 ? 36.17914 9.77942  20.42707  1.000 41.27514  ? 158 LYS   A CG    1 
ATOM   1233 C  CD    . LYS   A 1 161 ? 34.91583 10.61082 20.22035  1.000 38.35500  ? 158 LYS   A CD    1 
ATOM   1234 C  CE    . LYS   A 1 161 ? 34.43473 11.19910 21.53763  1.000 35.54697  ? 158 LYS   A CE    1 
ATOM   1235 N  NZ    . LYS   A 1 161 ? 33.04020 11.70224 21.44991  1.000 31.74579  ? 158 LYS   A NZ    1 
ATOM   1236 N  N     . SER   A 1 162 ? 36.57937 6.41635  17.41824  1.000 50.24449  ? 159 SER   A N     1 
ATOM   1237 C  CA    . SER   A 1 162 ? 37.12178 5.70788  16.26363  1.000 52.02883  ? 159 SER   A CA    1 
ATOM   1238 C  C     . SER   A 1 162 ? 36.04478 5.08153  15.38737  1.000 53.25751  ? 159 SER   A C     1 
ATOM   1239 O  O     . SER   A 1 162 ? 36.37941 4.48003  14.36172  1.000 55.31518  ? 159 SER   A O     1 
ATOM   1240 C  CB    . SER   A 1 162 ? 38.10821 4.63297  16.72943  1.000 52.94898  ? 159 SER   A CB    1 
ATOM   1241 O  OG    . SER   A 1 162 ? 37.45375 3.62445  17.47858  1.000 55.00823  ? 159 SER   A OG    1 
ATOM   1242 N  N     . ASN   A 1 163 ? 34.77138 5.21328  15.75116  1.000 53.12159  ? 160 ASN   A N     1 
ATOM   1243 C  CA    . ASN   A 1 163 ? 33.67856 4.59868  15.01176  1.000 50.76743  ? 160 ASN   A CA    1 
ATOM   1244 C  C     . ASN   A 1 163 ? 32.80572 5.61558  14.28140  1.000 46.79448  ? 160 ASN   A C     1 
ATOM   1245 O  O     . ASN   A 1 163 ? 31.76425 5.23406  13.73280  1.000 47.85734  ? 160 ASN   A O     1 
ATOM   1246 C  CB    . ASN   A 1 163 ? 32.81865 3.75477  15.95726  1.000 53.58491  ? 160 ASN   A CB    1 
ATOM   1247 C  CG    . ASN   A 1 163 ? 32.78552 2.28834  15.56699  1.000 58.48710  ? 160 ASN   A CG    1 
ATOM   1248 O  OD1   . ASN   A 1 163 ? 33.18013 1.91855  14.46110  1.000 60.56200  ? 160 ASN   A OD1   1 
ATOM   1249 N  ND2   . ASN   A 1 163 ? 32.30354 1.44574  16.47380  1.000 58.32609  ? 160 ASN   A ND2   1 
ATOM   1250 N  N     . TYR   A 1 164 ? 33.19848 6.89666  14.25968  1.000 41.40433  ? 161 TYR   A N     1 
ATOM   1251 C  CA    . TYR   A 1 164 ? 32.36091 7.91510  13.62693  1.000 38.76964  ? 161 TYR   A CA    1 
ATOM   1252 C  C     . TYR   A 1 164 ? 32.10982 7.59996  12.15838  1.000 39.59807  ? 161 TYR   A C     1 
ATOM   1253 O  O     . TYR   A 1 164 ? 30.97407 7.70084  11.68251  1.000 41.70866  ? 161 TYR   A O     1 
ATOM   1254 C  CB    . TYR   A 1 164 ? 32.99787 9.29679  13.75399  1.000 37.31197  ? 161 TYR   A CB    1 
ATOM   1255 C  CG    . TYR   A 1 164 ? 32.73566 10.01566 15.06019  1.000 37.35726  ? 161 TYR   A CG    1 
ATOM   1256 C  CD1   . TYR   A 1 164 ? 32.53780 9.31450  16.24526  1.000 39.71964  ? 161 TYR   A CD1   1 
ATOM   1257 C  CD2   . TYR   A 1 164 ? 32.68075 11.40330 15.10366  1.000 33.89822  ? 161 TYR   A CD2   1 
ATOM   1258 C  CE1   . TYR   A 1 164 ? 32.30250 9.98122  17.44078  1.000 35.37892  ? 161 TYR   A CE1   1 
ATOM   1259 C  CE2   . TYR   A 1 164 ? 32.44470 12.07456 16.28670  1.000 31.34282  ? 161 TYR   A CE2   1 
ATOM   1260 C  CZ    . TYR   A 1 164 ? 32.26090 11.36401 17.45050  1.000 32.98387  ? 161 TYR   A CZ    1 
ATOM   1261 O  OH    . TYR   A 1 164 ? 32.03843 12.05041 18.62326  1.000 32.98497  ? 161 TYR   A OH    1 
ATOM   1262 N  N     . ALA   A 1 165 ? 33.15924 7.22248  11.42250  1.000 40.87100  ? 162 ALA   A N     1 
ATOM   1263 C  CA    . ALA   A 1 165 ? 32.99903 6.92523  10.00210  1.000 42.10949  ? 162 ALA   A CA    1 
ATOM   1264 C  C     . ALA   A 1 165 ? 32.01166 5.78659  9.77061   1.000 44.35293  ? 162 ALA   A C     1 
ATOM   1265 O  O     . ALA   A 1 165 ? 31.30455 5.77663  8.75733   1.000 43.51970  ? 162 ALA   A O     1 
ATOM   1266 C  CB    . ALA   A 1 165 ? 34.35502 6.59242  9.37935   1.000 38.80878  ? 162 ALA   A CB    1 
ATOM   1267 N  N     . ASN   A 1 166 ? 31.94197 4.82717  10.69676  1.000 45.48005  ? 163 ASN   A N     1 
ATOM   1268 C  CA    . ASN   A 1 166 ? 30.96948 3.74558  10.57578  1.000 43.01483  ? 163 ASN   A CA    1 
ATOM   1269 C  C     . ASN   A 1 166 ? 29.55733 4.24695  10.85516  1.000 44.09661  ? 163 ASN   A C     1 
ATOM   1270 O  O     . ASN   A 1 166 ? 28.61312 3.90443  10.13318  1.000 45.62015  ? 163 ASN   A O     1 
ATOM   1271 C  CB    . ASN   A 1 166 ? 31.34274 2.59816  11.51765  1.000 44.88149  ? 163 ASN   A CB    1 
ATOM   1272 C  CG    . ASN   A 1 166 ? 32.47817 1.74526  10.97517  1.000 50.66573  ? 163 ASN   A CG    1 
ATOM   1273 O  OD1   . ASN   A 1 166 ? 32.46121 1.34003  9.81281   1.000 52.28218  ? 163 ASN   A OD1   1 
ATOM   1274 N  ND2   . ASN   A 1 166 ? 33.47388 1.47539  11.81350  1.000 52.26214  ? 163 ASN   A ND2   1 
ATOM   1275 N  N     . TYR   A 1 167 ? 29.39368 5.05725  11.90532  1.000 42.73513  ? 164 TYR   A N     1 
ATOM   1276 C  CA    . TYR   A 1 167 ? 28.10086 5.68380  12.16558  1.000 44.94709  ? 164 TYR   A CA    1 
ATOM   1277 C  C     . TYR   A 1 167 ? 27.63913 6.50745  10.97011  1.000 44.11198  ? 164 TYR   A C     1 
ATOM   1278 O  O     . TYR   A 1 167 ? 26.45450 6.49097  10.61420  1.000 42.07484  ? 164 TYR   A O     1 
ATOM   1279 C  CB    . TYR   A 1 167 ? 28.18474 6.56995  13.40888  1.000 45.31806  ? 164 TYR   A CB    1 
ATOM   1280 C  CG    . TYR   A 1 167 ? 28.61990 5.85681  14.66917  1.000 48.83263  ? 164 TYR   A CG    1 
ATOM   1281 C  CD1   . TYR   A 1 167 ? 28.16180 4.57947  14.96687  1.000 49.18992  ? 164 TYR   A CD1   1 
ATOM   1282 C  CD2   . TYR   A 1 167 ? 29.49035 6.46545  15.56462  1.000 48.17496  ? 164 TYR   A CD2   1 
ATOM   1283 C  CE1   . TYR   A 1 167 ? 28.55891 3.93055  16.12175  1.000 48.37264  ? 164 TYR   A CE1   1 
ATOM   1284 C  CE2   . TYR   A 1 167 ? 29.88996 5.82532  16.72057  1.000 47.38321  ? 164 TYR   A CE2   1 
ATOM   1285 C  CZ    . TYR   A 1 167 ? 29.42231 4.55911  16.99451  1.000 49.95708  ? 164 TYR   A CZ    1 
ATOM   1286 O  OH    . TYR   A 1 167 ? 29.82417 3.91893  18.14502  1.000 56.03456  ? 164 TYR   A OH    1 
ATOM   1287 N  N     . HIS   A 1 168 ? 28.56878 7.22881  10.33654  1.000 42.19939  ? 165 HIS   A N     1 
ATOM   1288 C  CA    . HIS   A 1 168 ? 28.22137 8.11275  9.22803   1.000 43.54914  ? 165 HIS   A CA    1 
ATOM   1289 C  C     . HIS   A 1 168 ? 27.51859 7.36194  8.10339   1.000 44.90011  ? 165 HIS   A C     1 
ATOM   1290 O  O     . HIS   A 1 168 ? 26.51774 7.84271  7.55865   1.000 46.03529  ? 165 HIS   A O     1 
ATOM   1291 C  CB    . HIS   A 1 168 ? 29.48135 8.80149  8.70132   1.000 42.06997  ? 165 HIS   A CB    1 
ATOM   1292 C  CG    . HIS   A 1 168 ? 29.21460 9.79565  7.61409   1.000 42.05082  ? 165 HIS   A CG    1 
ATOM   1293 N  ND1   . HIS   A 1 168 ? 28.48927 10.94952 7.82226   1.000 40.18165  ? 165 HIS   A ND1   1 
ATOM   1294 C  CD2   . HIS   A 1 168 ? 29.57058 9.80590  6.30741   1.000 41.76965  ? 165 HIS   A CD2   1 
ATOM   1295 C  CE1   . HIS   A 1 168 ? 28.41402 11.63005 6.69213   1.000 40.78380  ? 165 HIS   A CE1   1 
ATOM   1296 N  NE2   . HIS   A 1 168 ? 29.06088 10.95734 5.75707   1.000 41.93621  ? 165 HIS   A NE2   1 
ATOM   1297 N  N     . GLU   A 1 169 ? 28.02909 6.18294  7.73782   1.000 47.48409  ? 166 GLU   A N     1 
ATOM   1298 C  CA    . GLU   A 1 169 ? 27.44391 5.44184  6.62407   1.000 49.70746  ? 166 GLU   A CA    1 
ATOM   1299 C  C     . GLU   A 1 169 ? 26.01757 4.99553  6.92449   1.000 49.49990  ? 166 GLU   A C     1 
ATOM   1300 O  O     . GLU   A 1 169 ? 25.19948 4.88551  6.00411   1.000 50.74411  ? 166 GLU   A O     1 
ATOM   1301 C  CB    . GLU   A 1 169 ? 28.32323 4.24158  6.27107   1.000 51.02348  ? 166 GLU   A CB    1 
ATOM   1302 C  CG    . GLU   A 1 169 ? 29.70131 4.62743  5.75530   1.000 52.76229  ? 166 GLU   A CG    1 
ATOM   1303 C  CD    . GLU   A 1 169 ? 29.63364 5.51450  4.52463   1.000 57.36885  ? 166 GLU   A CD    1 
ATOM   1304 O  OE1   . GLU   A 1 169 ? 28.75459 5.28282  3.66614   1.000 60.61811  ? 166 GLU   A OE1   1 
ATOM   1305 O  OE2   . GLU   A 1 169 ? 30.45201 6.45227  4.41924   1.000 58.74129  ? 166 GLU   A OE2   1 
ATOM   1306 N  N     . ARG   A 1 170 ? 25.69650 4.74367  8.19479   1.000 47.08535  ? 167 ARG   A N     1 
ATOM   1307 C  CA    . ARG   A 1 170 ? 24.32004 4.42194  8.55412   1.000 48.15891  ? 167 ARG   A CA    1 
ATOM   1308 C  C     . ARG   A 1 170 ? 23.45354 5.67470  8.62393   1.000 47.20813  ? 167 ARG   A C     1 
ATOM   1309 O  O     . ARG   A 1 170 ? 22.30733 5.66655  8.16108   1.000 48.49738  ? 167 ARG   A O     1 
ATOM   1310 C  CB    . ARG   A 1 170 ? 24.27543 3.67991  9.89313   1.000 52.30996  ? 167 ARG   A CB    1 
ATOM   1311 C  CG    . ARG   A 1 170 ? 24.63321 2.19934  9.82666   1.000 55.87027  ? 167 ARG   A CG    1 
ATOM   1312 C  CD    . ARG   A 1 170 ? 26.12814 1.98258  9.68470   1.000 57.77749  ? 167 ARG   A CD    1 
ATOM   1313 N  NE    . ARG   A 1 170 ? 26.49449 0.57194  9.77580   1.000 59.63542  ? 167 ARG   A NE    1 
ATOM   1314 C  CZ    . ARG   A 1 170 ? 27.73649 0.11681  9.64954   1.000 60.93647  ? 167 ARG   A CZ    1 
ATOM   1315 N  NH1   . ARG   A 1 170 ? 28.73415 0.96219  9.42620   1.000 60.05324  ? 167 ARG   A NH1   1 
ATOM   1316 N  NH2   . ARG   A 1 170 ? 27.98220 -1.18242 9.74607   1.000 62.89741  ? 167 ARG   A NH2   1 
ATOM   1317 N  N     . LEU   A 1 171 ? 23.99055 6.76389  9.18233   1.000 43.95531  ? 168 LEU   A N     1 
ATOM   1318 C  CA    . LEU   A 1 171 ? 23.16785 7.93317  9.47715   1.000 41.87133  ? 168 LEU   A CA    1 
ATOM   1319 C  C     . LEU   A 1 171 ? 22.80871 8.72425  8.22523   1.000 41.72558  ? 168 LEU   A C     1 
ATOM   1320 O  O     . LEU   A 1 171 ? 21.75256 9.36761  8.18940   1.000 41.07044  ? 168 LEU   A O     1 
ATOM   1321 C  CB    . LEU   A 1 171 ? 23.87879 8.82387  10.49235  1.000 40.30558  ? 168 LEU   A CB    1 
ATOM   1322 C  CG    . LEU   A 1 171 ? 23.85350 8.24346  11.90480  1.000 43.50103  ? 168 LEU   A CG    1 
ATOM   1323 C  CD1   . LEU   A 1 171 ? 24.86562 8.93127  12.78975  1.000 42.53791  ? 168 LEU   A CD1   1 
ATOM   1324 C  CD2   . LEU   A 1 171 ? 22.44678 8.35361  12.49453  1.000 41.17950  ? 168 LEU   A CD2   1 
ATOM   1325 N  N     . VAL   A 1 172 ? 23.65501 8.69400  7.19255   1.000 39.06912  ? 169 VAL   A N     1 
ATOM   1326 C  CA    . VAL   A 1 172 ? 23.30366 9.33463  5.93290   1.000 42.38350  ? 169 VAL   A CA    1 
ATOM   1327 C  C     . VAL   A 1 172 ? 22.10815 8.67235  5.26792   1.000 46.15815  ? 169 VAL   A C     1 
ATOM   1328 O  O     . VAL   A 1 172 ? 21.57177 9.20910  4.29369   1.000 48.76098  ? 169 VAL   A O     1 
ATOM   1329 C  CB    . VAL   A 1 172 ? 24.50315 9.35023  4.96141   1.000 44.71376  ? 169 VAL   A CB    1 
ATOM   1330 C  CG1   . VAL   A 1 172 ? 25.59705 10.24106 5.49686   1.000 44.90508  ? 169 VAL   A CG1   1 
ATOM   1331 C  CG2   . VAL   A 1 172 ? 25.01891 7.93355  4.71129   1.000 47.23171  ? 169 VAL   A CG2   1 
ATOM   1332 N  N     . LYS   A 1 173 ? 21.68048 7.51365  5.76920   1.000 48.10188  ? 170 LYS   A N     1 
ATOM   1333 C  CA    . LYS   A 1 173 ? 20.48240 6.84520  5.28940   1.000 48.25362  ? 170 LYS   A CA    1 
ATOM   1334 C  C     . LYS   A 1 173 ? 19.32880 6.91409  6.27848   1.000 46.65199  ? 170 LYS   A C     1 
ATOM   1335 O  O     . LYS   A 1 173 ? 18.20341 6.55594  5.91678   1.000 49.55171  ? 170 LYS   A O     1 
ATOM   1336 C  CB    . LYS   A 1 173 ? 20.79151 5.37477  4.96734   1.000 47.34193  ? 170 LYS   A CB    1 
ATOM   1337 C  CG    . LYS   A 1 173 ? 21.99200 5.18855  4.05129   1.000 48.06663  ? 170 LYS   A CG    1 
ATOM   1338 C  CD    . LYS   A 1 173 ? 22.31862 3.71750  3.85737   1.000 51.29153  ? 170 LYS   A CD    1 
ATOM   1339 N  N     . LEU   A 1 174 ? 19.57553 7.36777  7.50868   1.000 46.49408  ? 171 LEU   A N     1 
ATOM   1340 C  CA    . LEU   A 1 174 ? 18.55745 7.41357  8.54725   1.000 45.40574  ? 171 LEU   A CA    1 
ATOM   1341 C  C     . LEU   A 1 174 ? 18.06310 8.81922  8.85874   1.000 45.15351  ? 171 LEU   A C     1 
ATOM   1342 O  O     . LEU   A 1 174 ? 17.04771 8.95938  9.55086   1.000 46.19476  ? 171 LEU   A O     1 
ATOM   1343 C  CB    . LEU   A 1 174 ? 19.08850 6.76275  9.83331   1.000 45.23297  ? 171 LEU   A CB    1 
ATOM   1344 C  CG    . LEU   A 1 174 ? 19.28646 5.24764  9.74388   1.000 51.01372  ? 171 LEU   A CG    1 
ATOM   1345 C  CD1   . LEU   A 1 174 ? 20.34120 4.77511  10.73587  1.000 53.24656  ? 171 LEU   A CD1   1 
ATOM   1346 C  CD2   . LEU   A 1 174 ? 17.96431 4.52074  9.97121   1.000 49.25644  ? 171 LEU   A CD2   1 
ATOM   1347 N  N     . VAL   A 1 175 ? 18.74639 9.85606  8.38349   1.000 44.91304  ? 172 VAL   A N     1 
ATOM   1348 C  CA    . VAL   A 1 175 ? 18.26927 11.22752 8.50471   1.000 43.41456  ? 172 VAL   A CA    1 
ATOM   1349 C  C     . VAL   A 1 175 ? 17.64752 11.63254 7.17847   1.000 44.65127  ? 172 VAL   A C     1 
ATOM   1350 O  O     . VAL   A 1 175 ? 18.11427 11.22285 6.10562   1.000 45.89427  ? 172 VAL   A O     1 
ATOM   1351 C  CB    . VAL   A 1 175 ? 19.39844 12.19519 8.91180   1.000 44.46897  ? 172 VAL   A CB    1 
ATOM   1352 C  CG1   . VAL   A 1 175 ? 20.03072 11.75320 10.22350  1.000 42.75807  ? 172 VAL   A CG1   1 
ATOM   1353 C  CG2   . VAL   A 1 175 ? 20.44389 12.30360 7.81071   1.000 49.56930  ? 172 VAL   A CG2   1 
ATOM   1354 N  N     . ARG   A 1 176 ? 16.58183 12.42428 7.24987   1.000 43.21480  ? 173 ARG   A N     1 
ATOM   1355 C  CA    . ARG   A 1 176 ? 15.89526 12.85750 6.04548   1.000 44.85382  ? 173 ARG   A CA    1 
ATOM   1356 C  C     . ARG   A 1 176 ? 16.81481 13.70667 5.17257   1.000 48.00197  ? 173 ARG   A C     1 
ATOM   1357 O  O     . ARG   A 1 176 ? 17.83559 14.23776 5.62177   1.000 48.54613  ? 173 ARG   A O     1 
ATOM   1358 C  CB    . ARG   A 1 176 ? 14.64642 13.66001 6.40145   1.000 41.43301  ? 173 ARG   A CB    1 
ATOM   1359 C  CG    . ARG   A 1 176 ? 14.94623 14.97524 7.10660   1.000 39.87047  ? 173 ARG   A CG    1 
ATOM   1360 C  CD    . ARG   A 1 176 ? 13.69510 15.81632 7.26450   1.000 41.31934  ? 173 ARG   A CD    1 
ATOM   1361 N  NE    . ARG   A 1 176 ? 13.94174 17.05172 8.00441   1.000 43.17678  ? 173 ARG   A NE    1 
ATOM   1362 C  CZ    . ARG   A 1 176 ? 14.38862 18.18032 7.45933   1.000 44.50198  ? 173 ARG   A CZ    1 
ATOM   1363 N  NH1   . ARG   A 1 176 ? 14.57712 19.25361 8.21840   1.000 42.33139  ? 173 ARG   A NH1   1 
ATOM   1364 N  NH2   . ARG   A 1 176 ? 14.65039 18.23794 6.15910   1.000 43.34769  ? 173 ARG   A NH2   1 
ATOM   1365 N  N     . ILE   A 1 177 ? 16.43969 13.82552 3.89785   1.000 47.35004  ? 174 ILE   A N     1 
ATOM   1366 C  CA    . ILE   A 1 177 ? 17.09940 14.78697 3.02826   1.000 46.90667  ? 174 ILE   A CA    1 
ATOM   1367 C  C     . ILE   A 1 177 ? 16.84656 16.17924 3.57997   1.000 46.88938  ? 174 ILE   A C     1 
ATOM   1368 O  O     . ILE   A 1 177 ? 15.71408 16.52946 3.93720   1.000 48.83880  ? 174 ILE   A O     1 
ATOM   1369 C  CB    . ILE   A 1 177 ? 16.60190 14.63791 1.58300   1.000 47.18899  ? 174 ILE   A CB    1 
ATOM   1370 C  CG1   . ILE   A 1 177 ? 16.79926 13.19587 1.10850   1.000 48.95160  ? 174 ILE   A CG1   1 
ATOM   1371 C  CG2   . ILE   A 1 177 ? 17.32947 15.60856 0.66593   1.000 43.71742  ? 174 ILE   A CG2   1 
ATOM   1372 C  CD1   . ILE   A 1 177 ? 16.49488 12.96730 -0.35982  1.000 48.48798  ? 174 ILE   A CD1   1 
ATOM   1373 N  N     . GLY   A 1 178 ? 17.90701 16.97692 3.67603   1.000 44.41550  ? 175 GLY   A N     1 
ATOM   1374 C  CA    . GLY   A 1 178 ? 17.84147 18.22806 4.39244   1.000 42.57394  ? 175 GLY   A CA    1 
ATOM   1375 C  C     . GLY   A 1 178 ? 18.01893 18.10695 5.88880   1.000 43.36275  ? 175 GLY   A C     1 
ATOM   1376 O  O     . GLY   A 1 178 ? 18.12269 19.13809 6.56885   1.000 41.77380  ? 175 GLY   A O     1 
ATOM   1377 N  N     . GLY   A 1 179 ? 18.04993 16.88780 6.42623   1.000 42.15745  ? 176 GLY   A N     1 
ATOM   1378 C  CA    . GLY   A 1 179 ? 18.32587 16.69349 7.83291   1.000 42.76228  ? 176 GLY   A CA    1 
ATOM   1379 C  C     . GLY   A 1 179 ? 19.79173 16.90382 8.16007   1.000 41.57515  ? 176 GLY   A C     1 
ATOM   1380 O  O     . GLY   A 1 179 ? 20.66074 16.96482 7.28881   1.000 39.59009  ? 176 GLY   A O     1 
ATOM   1381 N  N     . ALA   A 1 180 ? 20.07026 17.00604 9.45730   1.000 40.13064  ? 177 ALA   A N     1 
ATOM   1382 C  CA    . ALA   A 1 180 ? 21.38947 17.38238 9.94321   1.000 40.67785  ? 177 ALA   A CA    1 
ATOM   1383 C  C     . ALA   A 1 180 ? 22.02021 16.25468 10.74946  1.000 40.58552  ? 177 ALA   A C     1 
ATOM   1384 O  O     . ALA   A 1 180 ? 21.35731 15.61969 11.57451  1.000 42.12353  ? 177 ALA   A O     1 
ATOM   1385 C  CB    . ALA   A 1 180 ? 21.31406 18.65172 10.79983  1.000 37.61239  ? 177 ALA   A CB    1 
ATOM   1386 N  N     . ILE   A 1 181 ? 23.30683 16.01562 10.50625  1.000 38.80805  ? 178 ILE   A N     1 
ATOM   1387 C  CA    . ILE   A 1 181 ? 24.11775 15.09759 11.29892  1.000 36.51651  ? 178 ILE   A CA    1 
ATOM   1388 C  C     . ILE   A 1 181 ? 25.28262 15.89590 11.86196  1.000 37.51227  ? 178 ILE   A C     1 
ATOM   1389 O  O     . ILE   A 1 181 ? 26.04347 16.50926 11.10234  1.000 38.14513  ? 178 ILE   A O     1 
ATOM   1390 C  CB    . ILE   A 1 181 ? 24.62798 13.90810 10.47152  1.000 40.42903  ? 178 ILE   A CB    1 
ATOM   1391 C  CG1   . ILE   A 1 181 ? 23.47760 13.20694 9.75282   1.000 42.35359  ? 178 ILE   A CG1   1 
ATOM   1392 C  CG2   . ILE   A 1 181 ? 25.37187 12.91756 11.36466  1.000 40.95940  ? 178 ILE   A CG2   1 
ATOM   1393 C  CD1   . ILE   A 1 181 ? 23.94062 12.08222 8.85350   1.000 42.73709  ? 178 ILE   A CD1   1 
ATOM   1394 N  N     . LEU   A 1 182 ? 25.41910 15.89631 13.18451  1.000 35.11581  ? 179 LEU   A N     1 
ATOM   1395 C  CA    . LEU   A 1 182 ? 26.46486 16.64416 13.86847  1.000 34.92530  ? 179 LEU   A CA    1 
ATOM   1396 C  C     . LEU   A 1 182 ? 27.42599 15.67914 14.54812  1.000 37.07624  ? 179 LEU   A C     1 
ATOM   1397 O  O     . LEU   A 1 182 ? 26.99481 14.77674 15.27264  1.000 40.00423  ? 179 LEU   A O     1 
ATOM   1398 C  CB    . LEU   A 1 182 ? 25.86845 17.60381 14.89895  1.000 36.74657  ? 179 LEU   A CB    1 
ATOM   1399 C  CG    . LEU   A 1 182 ? 25.30312 18.93219 14.39157  1.000 38.05639  ? 179 LEU   A CG    1 
ATOM   1400 C  CD1   . LEU   A 1 182 ? 24.02780 18.74409 13.58274  1.000 36.22973  ? 179 LEU   A CD1   1 
ATOM   1401 C  CD2   . LEU   A 1 182 ? 25.06019 19.85829 15.56712  1.000 37.20515  ? 179 LEU   A CD2   1 
ATOM   1402 N  N     . TYR   A 1 183 ? 28.72228 15.87296 14.31747  1.000 34.40765  ? 180 TYR   A N     1 
ATOM   1403 C  CA    . TYR   A 1 183 ? 29.76534 15.07135 14.94430  1.000 31.39445  ? 180 TYR   A CA    1 
ATOM   1404 C  C     . TYR   A 1 183 ? 30.51637 15.91878 15.96040  1.000 33.32017  ? 180 TYR   A C     1 
ATOM   1405 O  O     . TYR   A 1 183 ? 30.99151 17.01153 15.63765  1.000 35.22258  ? 180 TYR   A O     1 
ATOM   1406 C  CB    . TYR   A 1 183 ? 30.72928 14.50827 13.89832  1.000 31.00599  ? 180 TYR   A CB    1 
ATOM   1407 C  CG    . TYR   A 1 183 ? 30.03688 13.60788 12.90763  1.000 36.69212  ? 180 TYR   A CG    1 
ATOM   1408 C  CD1   . TYR   A 1 183 ? 29.83519 12.26288 13.18809  1.000 41.89706  ? 180 TYR   A CD1   1 
ATOM   1409 C  CD2   . TYR   A 1 183 ? 29.55543 14.10772 11.70530  1.000 37.90103  ? 180 TYR   A CD2   1 
ATOM   1410 C  CE1   . TYR   A 1 183 ? 29.18704 11.43566 12.28985  1.000 42.48131  ? 180 TYR   A CE1   1 
ATOM   1411 C  CE2   . TYR   A 1 183 ? 28.90642 13.28992 10.80092  1.000 36.95752  ? 180 TYR   A CE2   1 
ATOM   1412 C  CZ    . TYR   A 1 183 ? 28.72703 11.95596 11.09801  1.000 40.26568  ? 180 TYR   A CZ    1 
ATOM   1413 O  OH    . TYR   A 1 183 ? 28.07682 11.14168 10.20103  1.000 40.62466  ? 180 TYR   A OH    1 
ATOM   1414 N  N     . ASP   A 1 184 ? 30.62360 15.41004 17.17923  1.000 34.72904  ? 181 ASP   A N     1 
ATOM   1415 C  CA    . ASP   A 1 184 ? 31.29020 16.11388 18.26055  1.000 32.12199  ? 181 ASP   A CA    1 
ATOM   1416 C  C     . ASP   A 1 184 ? 32.78019 15.78351 18.27756  1.000 29.24308  ? 181 ASP   A C     1 
ATOM   1417 O  O     . ASP   A 1 184 ? 33.19833 14.71188 17.83337  1.000 31.39696  ? 181 ASP   A O     1 
ATOM   1418 C  CB    . ASP   A 1 184 ? 30.64831 15.73793 19.59513  1.000 31.19032  ? 181 ASP   A CB    1 
ATOM   1419 C  CG    . ASP   A 1 184 ? 30.92959 16.74717 20.67555  1.000 35.02076  ? 181 ASP   A CG    1 
ATOM   1420 O  OD1   . ASP   A 1 184 ? 30.88220 17.95525 20.37467  1.000 37.08233  ? 181 ASP   A OD1   1 
ATOM   1421 O  OD2   . ASP   A 1 184 ? 31.17813 16.33427 21.82421  1.000 40.78472  ? 181 ASP   A OD2   1 
ATOM   1422 N  N     . ASN   A 1 185 ? 33.57973 16.73267 18.77850  1.000 30.14051  ? 182 ASN   A N     1 
ATOM   1423 C  CA    . ASN   A 1 185 ? 35.01873 16.57748 19.02053  1.000 34.66207  ? 182 ASN   A CA    1 
ATOM   1424 C  C     . ASN   A 1 185 ? 35.85148 16.48949 17.74380  1.000 31.85413  ? 182 ASN   A C     1 
ATOM   1425 O  O     . ASN   A 1 185 ? 36.95246 15.93160 17.77038  1.000 33.58050  ? 182 ASN   A O     1 
ATOM   1426 C  CB    . ASN   A 1 185 ? 35.32140 15.35202 19.89436  1.000 37.66026  ? 182 ASN   A CB    1 
ATOM   1427 C  CG    . ASN   A 1 185 ? 34.58428 15.37793 21.20820  1.000 46.40555  ? 182 ASN   A CG    1 
ATOM   1428 O  OD1   . ASN   A 1 185 ? 33.48836 14.82907 21.32940  1.000 50.83386  ? 182 ASN   A OD1   1 
ATOM   1429 N  ND2   . ASN   A 1 185 ? 35.18503 16.01086 22.20856  1.000 47.77936  ? 182 ASN   A ND2   1 
ATOM   1430 N  N     . THR   A 1 186 ? 35.38166 17.05049 16.62527  1.000 30.03515  ? 183 THR   A N     1 
ATOM   1431 C  CA    . THR   A 1 186 ? 36.08820 16.87275 15.35696  1.000 34.55054  ? 183 THR   A CA    1 
ATOM   1432 C  C     . THR   A 1 186 ? 37.41783 17.61806 15.29137  1.000 36.16877  ? 183 THR   A C     1 
ATOM   1433 O  O     . THR   A 1 186 ? 38.20771 17.35122 14.37728  1.000 38.23088  ? 183 THR   A O     1 
ATOM   1434 C  CB    . THR   A 1 186 ? 35.20153 17.29617 14.18187  1.000 33.48053  ? 183 THR   A CB    1 
ATOM   1435 O  OG1   . THR   A 1 186 ? 34.68879 18.61331 14.40947  1.000 33.53141  ? 183 THR   A OG1   1 
ATOM   1436 C  CG2   . THR   A 1 186 ? 34.04619 16.32445 14.02586  1.000 33.07864  ? 183 THR   A CG2   1 
ATOM   1437 N  N     . LEU   A 1 187 ? 37.68994 18.53021 16.22515  1.000 33.87946  ? 184 LEU   A N     1 
ATOM   1438 C  CA    . LEU   A 1 187 ? 39.00056 19.15736 16.32828  1.000 36.02680  ? 184 LEU   A CA    1 
ATOM   1439 C  C     . LEU   A 1 187 ? 39.90304 18.48399 17.35482  1.000 36.57328  ? 184 LEU   A C     1 
ATOM   1440 O  O     . LEU   A 1 187 ? 41.10148 18.77674 17.37913  1.000 41.48924  ? 184 LEU   A O     1 
ATOM   1441 C  CB    . LEU   A 1 187 ? 38.85663 20.64672 16.67181  1.000 34.38794  ? 184 LEU   A CB    1 
ATOM   1442 C  CG    . LEU   A 1 187 ? 38.19648 21.51193 15.59341  1.000 33.84564  ? 184 LEU   A CG    1 
ATOM   1443 C  CD1   . LEU   A 1 187 ? 38.12658 22.96739 16.03577  1.000 34.49920  ? 184 LEU   A CD1   1 
ATOM   1444 C  CD2   . LEU   A 1 187 ? 38.92277 21.37945 14.25864  1.000 30.19501  ? 184 LEU   A CD2   1 
ATOM   1445 N  N     . TRP   A 1 188 ? 39.35342 17.60229 18.19567  1.000 36.08906  ? 185 TRP   A N     1 
ATOM   1446 C  CA    . TRP   A 1 188 ? 40.09105 16.81967 19.18661  1.000 35.30902  ? 185 TRP   A CA    1 
ATOM   1447 C  C     . TRP   A 1 188 ? 41.14701 17.63409 19.92841  1.000 36.94138  ? 185 TRP   A C     1 
ATOM   1448 O  O     . TRP   A 1 188 ? 42.34815 17.36762 19.80288  1.000 36.46011  ? 185 TRP   A O     1 
ATOM   1449 C  CB    . TRP   A 1 188 ? 40.73833 15.60183 18.52244  1.000 38.14599  ? 185 TRP   A CB    1 
ATOM   1450 C  CG    . TRP   A 1 188 ? 41.05291 14.49066 19.48968  1.000 42.79787  ? 185 TRP   A CG    1 
ATOM   1451 C  CD1   . TRP   A 1 188 ? 42.27537 13.92728 19.72299  1.000 42.51261  ? 185 TRP   A CD1   1 
ATOM   1452 C  CD2   . TRP   A 1 188 ? 40.12897 13.81855 20.36265  1.000 42.37089  ? 185 TRP   A CD2   1 
ATOM   1453 N  NE1   . TRP   A 1 188 ? 42.17033 12.94468 20.68042  1.000 42.48107  ? 185 TRP   A NE1   1 
ATOM   1454 C  CE2   . TRP   A 1 188 ? 40.86474 12.85729 21.08846  1.000 41.62238  ? 185 TRP   A CE2   1 
ATOM   1455 C  CE3   . TRP   A 1 188 ? 38.75288 13.93404 20.59754  1.000 42.90203  ? 185 TRP   A CE3   1 
ATOM   1456 C  CZ2   . TRP   A 1 188 ? 40.27317 12.01810 22.03212  1.000 39.19423  ? 185 TRP   A CZ2   1 
ATOM   1457 C  CZ3   . TRP   A 1 188 ? 38.16574 13.09761 21.53657  1.000 43.10701  ? 185 TRP   A CZ3   1 
ATOM   1458 C  CH2   . TRP   A 1 188 ? 38.92713 12.15154 22.24130  1.000 41.02762  ? 185 TRP   A CH2   1 
ATOM   1459 N  N     . PHE   A 1 189 ? 40.70674 18.63439 20.69312  1.000 36.38526  ? 186 PHE   A N     1 
ATOM   1460 C  CA    . PHE   A 1 189 ? 41.57831 19.46597 21.52202  1.000 37.62296  ? 186 PHE   A CA    1 
ATOM   1461 C  C     . PHE   A 1 189 ? 42.63853 20.19235 20.70216  1.000 42.00358  ? 186 PHE   A C     1 
ATOM   1462 O  O     . PHE   A 1 189 ? 43.64719 20.64831 21.24970  1.000 45.20054  ? 186 PHE   A O     1 
ATOM   1463 C  CB    . PHE   A 1 189 ? 42.23738 18.63835 22.63428  1.000 39.92008  ? 186 PHE   A CB    1 
ATOM   1464 C  CG    . PHE   A 1 189 ? 41.25406 17.87954 23.48553  1.000 44.86195  ? 186 PHE   A CG    1 
ATOM   1465 C  CD1   . PHE   A 1 189 ? 40.69244 18.46672 24.60946  1.000 45.99838  ? 186 PHE   A CD1   1 
ATOM   1466 C  CD2   . PHE   A 1 189 ? 40.88294 16.58328 23.15572  1.000 44.59671  ? 186 PHE   A CD2   1 
ATOM   1467 C  CE1   . PHE   A 1 189 ? 39.78523 17.77390 25.39456  1.000 45.33690  ? 186 PHE   A CE1   1 
ATOM   1468 C  CE2   . PHE   A 1 189 ? 39.97256 15.88522 23.93442  1.000 45.25177  ? 186 PHE   A CE2   1 
ATOM   1469 C  CZ    . PHE   A 1 189 ? 39.42233 16.48289 25.05534  1.000 43.81062  ? 186 PHE   A CZ    1 
ATOM   1470 N  N     . GLY   A 1 190 ? 42.42571 20.31433 19.39198  1.000 40.01679  ? 187 GLY   A N     1 
ATOM   1471 C  CA    . GLY   A 1 190 ? 43.36421 20.97349 18.51398  1.000 38.33384  ? 187 GLY   A CA    1 
ATOM   1472 C  C     . GLY   A 1 190 ? 44.45867 20.08838 17.95843  1.000 40.80726  ? 187 GLY   A C     1 
ATOM   1473 O  O     . GLY   A 1 190 ? 45.18227 20.52442 17.05372  1.000 38.61990  ? 187 GLY   A O     1 
ATOM   1474 N  N     . SER   A 1 191 ? 44.59267 18.85388 18.45263  1.000 42.47123  ? 188 SER   A N     1 
ATOM   1475 C  CA    . SER   A 1 191 ? 45.71108 18.00343 18.05795  1.000 43.76733  ? 188 SER   A CA    1 
ATOM   1476 C  C     . SER   A 1 191 ? 45.59454 17.49524 16.62514  1.000 45.07902  ? 188 SER   A C     1 
ATOM   1477 O  O     . SER   A 1 191 ? 46.57799 16.96757 16.08987  1.000 40.44125  ? 188 SER   A O     1 
ATOM   1478 C  CB    . SER   A 1 191 ? 45.83191 16.81947 19.01890  1.000 40.75489  ? 188 SER   A CB    1 
ATOM   1479 O  OG    . SER   A 1 191 ? 44.66490 16.01322 18.98166  1.000 37.64867  ? 188 SER   A OG    1 
ATOM   1480 N  N     . VAL   A 1 192 ? 44.42235 17.63412 15.99715  1.000 41.52078  ? 189 VAL   A N     1 
ATOM   1481 C  CA    . VAL   A 1 192 ? 44.25675 17.19042 14.61740  1.000 40.04796  ? 189 VAL   A CA    1 
ATOM   1482 C  C     . VAL   A 1 192 ? 45.02097 18.07416 13.63914  1.000 41.27564  ? 189 VAL   A C     1 
ATOM   1483 O  O     . VAL   A 1 192 ? 45.25490 17.66800 12.49328  1.000 38.79189  ? 189 VAL   A O     1 
ATOM   1484 C  CB    . VAL   A 1 192 ? 42.76462 17.15500 14.23694  1.000 37.30496  ? 189 VAL   A CB    1 
ATOM   1485 C  CG1   . VAL   A 1 192 ? 41.99908 16.17528 15.12646  1.000 37.08422  ? 189 VAL   A CG1   1 
ATOM   1486 C  CG2   . VAL   A 1 192 ? 42.16998 18.54799 14.32855  1.000 35.72195  ? 189 VAL   A CG2   1 
ATOM   1487 N  N     . ALA   A 1 193 ? 45.42479 19.27408 14.06403  1.000 40.66223  ? 190 ALA   A N     1 
ATOM   1488 C  CA    . ALA   A 1 193 ? 46.00700 20.25262 13.15468  1.000 42.56353  ? 190 ALA   A CA    1 
ATOM   1489 C  C     . ALA   A 1 193 ? 47.40204 19.87519 12.66941  1.000 45.18782  ? 190 ALA   A C     1 
ATOM   1490 O  O     . ALA   A 1 193 ? 47.90589 20.51819 11.74253  1.000 45.64141  ? 190 ALA   A O     1 
ATOM   1491 C  CB    . ALA   A 1 193 ? 46.05047 21.62329 13.83064  1.000 41.74161  ? 190 ALA   A CB    1 
ATOM   1492 N  N     . TYR   A 1 194 ? 48.03431 18.86324 13.25937  1.000 46.11529  ? 191 TYR   A N     1 
ATOM   1493 C  CA    . TYR   A 1 194 ? 49.38819 18.49652 12.88006  1.000 50.89325  ? 191 TYR   A CA    1 
ATOM   1494 C  C     . TYR   A 1 194 ? 49.44823 17.02995 12.47191  1.000 53.51454  ? 191 TYR   A C     1 
ATOM   1495 O  O     . TYR   A 1 194 ? 48.64813 16.21664 12.94474  1.000 57.26588  ? 191 TYR   A O     1 
ATOM   1496 C  CB    . TYR   A 1 194 ? 50.37242 18.74419 14.03128  1.000 52.85207  ? 191 TYR   A CB    1 
ATOM   1497 C  CG    . TYR   A 1 194 ? 50.25121 20.11773 14.65172  1.000 52.82310  ? 191 TYR   A CG    1 
ATOM   1498 C  CD1   . TYR   A 1 194 ? 49.42552 20.33367 15.74759  1.000 53.19459  ? 191 TYR   A CD1   1 
ATOM   1499 C  CD2   . TYR   A 1 194 ? 50.95855 21.19899 14.14112  1.000 51.47550  ? 191 TYR   A CD2   1 
ATOM   1500 C  CE1   . TYR   A 1 194 ? 49.30772 21.58687 16.31820  1.000 54.60265  ? 191 TYR   A CE1   1 
ATOM   1501 C  CE2   . TYR   A 1 194 ? 50.84686 22.45649 14.70661  1.000 51.38673  ? 191 TYR   A CE2   1 
ATOM   1502 C  CZ    . TYR   A 1 194 ? 50.02294 22.64305 15.79508  1.000 56.85974  ? 191 TYR   A CZ    1 
ATOM   1503 O  OH    . TYR   A 1 194 ? 49.90601 23.89294 16.35996  1.000 64.79806  ? 191 TYR   A OH    1 
ATOM   1504 N  N     . PRO   A 1 195 ? 50.37708 16.66471 11.58436  1.000 55.20000  ? 192 PRO   A N     1 
ATOM   1505 C  CA    . PRO   A 1 195 ? 50.50887 15.24289 11.21707  1.000 54.00450  ? 192 PRO   A CA    1 
ATOM   1506 C  C     . PRO   A 1 195 ? 50.81862 14.34225 12.40102  1.000 49.63127  ? 192 PRO   A C     1 
ATOM   1507 O  O     . PRO   A 1 195 ? 50.32275 13.20935 12.46084  1.000 47.02434  ? 192 PRO   A O     1 
ATOM   1508 C  CB    . PRO   A 1 195 ? 51.65305 15.25616 10.19342  1.000 56.56142  ? 192 PRO   A CB    1 
ATOM   1509 C  CG    . PRO   A 1 195 ? 51.63652 16.64267 9.62890   1.000 57.55719  ? 192 PRO   A CG    1 
ATOM   1510 C  CD    . PRO   A 1 195 ? 51.24604 17.53382 10.77301  1.000 55.50606  ? 192 PRO   A CD    1 
ATOM   1511 N  N     . GLU   A 1 196 ? 51.62213 14.81836 13.35041  1.000 47.68692  ? 193 GLU   A N     1 
ATOM   1512 C  CA    . GLU   A 1 196 ? 51.98828 14.05297 14.53212  1.000 51.46454  ? 193 GLU   A CA    1 
ATOM   1513 C  C     . GLU   A 1 196 ? 51.80353 14.91042 15.77481  1.000 48.04757  ? 193 GLU   A C     1 
ATOM   1514 O  O     . GLU   A 1 196 ? 51.86769 16.14093 15.71535  1.000 46.09107  ? 193 GLU   A O     1 
ATOM   1515 C  CB    . GLU   A 1 196 ? 53.44206 13.54756 14.45543  1.000 59.16247  ? 193 GLU   A CB    1 
ATOM   1516 C  CG    . GLU   A 1 196 ? 53.59522 12.16882 13.82334  1.000 67.72141  ? 193 GLU   A CG    1 
ATOM   1517 C  CD    . GLU   A 1 196 ? 52.96051 11.06747 14.65866  1.000 76.72069  ? 193 GLU   A CD    1 
ATOM   1518 O  OE1   . GLU   A 1 196 ? 52.65575 9.99396  14.09675  1.000 79.73423  ? 193 GLU   A OE1   1 
ATOM   1519 O  OE2   . GLU   A 1 196 ? 52.76240 11.27381 15.87677  1.000 80.05872  ? 193 GLU   A OE2   1 
ATOM   1520 N  N     . TYR   A 1 197 ? 51.57395 14.24726 16.90513  1.000 49.19991  ? 194 TYR   A N     1 
ATOM   1521 C  CA    . TYR   A 1 197 ? 51.34425 14.96184 18.15442  1.000 46.95250  ? 194 TYR   A CA    1 
ATOM   1522 C  C     . TYR   A 1 197 ? 51.87474 14.15035 19.33258  1.000 46.60320  ? 194 TYR   A C     1 
ATOM   1523 O  O     . TYR   A 1 197 ? 51.26186 13.14931 19.72566  1.000 44.75500  ? 194 TYR   A O     1 
ATOM   1524 C  CB    . TYR   A 1 197 ? 49.85306 15.26642 18.33286  1.000 41.96030  ? 194 TYR   A CB    1 
ATOM   1525 C  CG    . TYR   A 1 197 ? 49.58252 16.37260 19.32689  1.000 40.24328  ? 194 TYR   A CG    1 
ATOM   1526 C  CD1   . TYR   A 1 197 ? 49.48588 16.10344 20.68577  1.000 39.87027  ? 194 TYR   A CD1   1 
ATOM   1527 C  CD2   . TYR   A 1 197 ? 49.44098 17.68985 18.90793  1.000 38.90043  ? 194 TYR   A CD2   1 
ATOM   1528 C  CE1   . TYR   A 1 197 ? 49.24908 17.11262 21.60017  1.000 39.97263  ? 194 TYR   A CE1   1 
ATOM   1529 C  CE2   . TYR   A 1 197 ? 49.20745 18.70640 19.81548  1.000 40.25120  ? 194 TYR   A CE2   1 
ATOM   1530 C  CZ    . TYR   A 1 197 ? 49.11339 18.41126 21.16212  1.000 41.18613  ? 194 TYR   A CZ    1 
ATOM   1531 O  OH    . TYR   A 1 197 ? 48.87830 19.41667 22.07356  1.000 40.94174  ? 194 TYR   A OH    1 
ATOM   1532 N  N     . PRO   A 1 198 ? 52.99912 14.54996 19.92311  1.000 45.86993  ? 195 PRO   A N     1 
ATOM   1533 C  CA    . PRO   A 1 198 ? 53.59459 13.75383 21.00294  1.000 44.78643  ? 195 PRO   A CA    1 
ATOM   1534 C  C     . PRO   A 1 198 ? 52.81431 13.86030 22.30739  1.000 44.48982  ? 195 PRO   A C     1 
ATOM   1535 O  O     . PRO   A 1 198 ? 52.01089 14.77202 22.52324  1.000 46.55640  ? 195 PRO   A O     1 
ATOM   1536 C  CB    . PRO   A 1 198 ? 54.99977 14.35269 21.15640  1.000 47.39020  ? 195 PRO   A CB    1 
ATOM   1537 C  CG    . PRO   A 1 198 ? 55.21666 15.19331 19.91835  1.000 46.60647  ? 195 PRO   A CG    1 
ATOM   1538 C  CD    . PRO   A 1 198 ? 53.86280 15.67149 19.52178  1.000 40.09226  ? 195 PRO   A CD    1 
ATOM   1539 N  N     . GLY   A 1 199 ? 53.06568 12.88613 23.18152  1.000 44.77868  ? 196 GLY   A N     1 
ATOM   1540 C  CA    . GLY   A 1 199 ? 52.57791 12.89723 24.54555  1.000 47.67314  ? 196 GLY   A CA    1 
ATOM   1541 C  C     . GLY   A 1 199 ? 51.17489 12.37484 24.75978  1.000 54.19080  ? 196 GLY   A C     1 
ATOM   1542 O  O     . GLY   A 1 199 ? 50.58631 12.66000 25.80909  1.000 56.62316  ? 196 GLY   A O     1 
ATOM   1543 N  N     . LEU   A 1 200 ? 50.62432 11.60920 23.82018  1.000 54.33218  ? 197 LEU   A N     1 
ATOM   1544 C  CA    . LEU   A 1 200 ? 49.23389 11.17861 23.88514  1.000 50.39436  ? 197 LEU   A CA    1 
ATOM   1545 C  C     . LEU   A 1 200 ? 49.11940 9.73705  24.36029  1.000 53.80168  ? 197 LEU   A C     1 
ATOM   1546 O  O     . LEU   A 1 200 ? 49.97150 8.89586  24.05900  1.000 57.43413  ? 197 LEU   A O     1 
ATOM   1547 C  CB    . LEU   A 1 200 ? 48.55116 11.31481 22.52195  1.000 42.54566  ? 197 LEU   A CB    1 
ATOM   1548 C  CG    . LEU   A 1 200 ? 48.43375 12.73527 21.97233  1.000 43.36591  ? 197 LEU   A CG    1 
ATOM   1549 C  CD1   . LEU   A 1 200 ? 47.55644 12.76880 20.73066  1.000 42.26121  ? 197 LEU   A CD1   1 
ATOM   1550 C  CD2   . LEU   A 1 200 ? 47.89338 13.66623 23.04099  1.000 41.43956  ? 197 LEU   A CD2   1 
ATOM   1551 N  N     . HIS   A 1 201 ? 48.05481 9.46539  25.10651  1.000 53.33894  ? 198 HIS   A N     1 
ATOM   1552 C  CA    . HIS   A 1 201 ? 47.65522 8.09730  25.38034  1.000 55.83177  ? 198 HIS   A CA    1 
ATOM   1553 C  C     . HIS   A 1 201 ? 47.40846 7.36644  24.05822  1.000 57.26110  ? 198 HIS   A C     1 
ATOM   1554 O  O     . HIS   A 1 201 ? 46.99618 7.98233  23.07028  1.000 58.23613  ? 198 HIS   A O     1 
ATOM   1555 C  CB    . HIS   A 1 201 ? 46.39453 8.09081  26.24733  1.000 55.03221  ? 198 HIS   A CB    1 
ATOM   1556 C  CG    . HIS   A 1 201 ? 46.00938 6.73977  26.76300  1.000 59.95290  ? 198 HIS   A CG    1 
ATOM   1557 N  ND1   . HIS   A 1 201 ? 45.42072 5.77972  25.96908  1.000 61.10574  ? 198 HIS   A ND1   1 
ATOM   1558 C  CD2   . HIS   A 1 201 ? 46.10855 6.19660  27.99936  1.000 62.78991  ? 198 HIS   A CD2   1 
ATOM   1559 C  CE1   . HIS   A 1 201 ? 45.18594 4.69823  26.69058  1.000 62.94716  ? 198 HIS   A CE1   1 
ATOM   1560 N  NE2   . HIS   A 1 201 ? 45.59237 4.92564  27.92632  1.000 63.15055  ? 198 HIS   A NE2   1 
ATOM   1561 N  N     . PRO   A 1 202 ? 47.68728 6.05909  24.00115  1.000 56.64953  ? 199 PRO   A N     1 
ATOM   1562 C  CA    . PRO   A 1 202 ? 47.46070 5.31542  22.74590  1.000 54.06386  ? 199 PRO   A CA    1 
ATOM   1563 C  C     . PRO   A 1 202 ? 46.09408 5.53197  22.10722  1.000 52.86590  ? 199 PRO   A C     1 
ATOM   1564 O  O     . PRO   A 1 202 ? 46.02365 5.85691  20.91528  1.000 53.55325  ? 199 PRO   A O     1 
ATOM   1565 C  CB    . PRO   A 1 202 ? 47.67137 3.86383  23.18540  1.000 52.10161  ? 199 PRO   A CB    1 
ATOM   1566 C  CG    . PRO   A 1 202 ? 48.72126 3.97125  24.24650  1.000 53.60690  ? 199 PRO   A CG    1 
ATOM   1567 C  CD    . PRO   A 1 202 ? 48.43342 5.25556  24.98773  1.000 54.82396  ? 199 PRO   A CD    1 
ATOM   1568 N  N     . GLU   A 1 203 ? 45.00312 5.36821  22.85912  1.000 52.13740  ? 200 GLU   A N     1 
ATOM   1569 C  CA    . GLU   A 1 203 ? 43.68110 5.55276  22.26976  1.000 52.09209  ? 200 GLU   A CA    1 
ATOM   1570 C  C     . GLU   A 1 203 ? 43.31537 7.02261  22.09205  1.000 48.43159  ? 200 GLU   A C     1 
ATOM   1571 O  O     . GLU   A 1 203 ? 42.36571 7.32537  21.36119  1.000 45.21314  ? 200 GLU   A O     1 
ATOM   1572 C  CB    . GLU   A 1 203 ? 42.61834 4.83193  23.10365  1.000 59.70723  ? 200 GLU   A CB    1 
ATOM   1573 C  CG    . GLU   A 1 203 ? 42.60026 5.19518  24.57210  1.000 68.29882  ? 200 GLU   A CG    1 
ATOM   1574 C  CD    . GLU   A 1 203 ? 41.87935 4.15730  25.41353  1.000 75.48975  ? 200 GLU   A CD    1 
ATOM   1575 O  OE1   . GLU   A 1 203 ? 41.34840 3.18785  24.83154  1.000 77.87600  ? 200 GLU   A OE1   1 
ATOM   1576 O  OE2   . GLU   A 1 203 ? 41.84720 4.30594  26.65414  1.000 77.77538  ? 200 GLU   A OE2   1 
ATOM   1577 N  N     . GLU   A 1 204 ? 44.04268 7.93983  22.73662  1.000 48.56283  ? 201 GLU   A N     1 
ATOM   1578 C  CA    . GLU   A 1 204 ? 43.95728 9.34425  22.34920  1.000 45.92331  ? 201 GLU   A CA    1 
ATOM   1579 C  C     . GLU   A 1 204 ? 44.51280 9.54772  20.94764  1.000 45.72046  ? 201 GLU   A C     1 
ATOM   1580 O  O     . GLU   A 1 204 ? 43.97411 10.33944 20.16392  1.000 40.84348  ? 201 GLU   A O     1 
ATOM   1581 C  CB    . GLU   A 1 204 ? 44.71366 10.22146 23.34636  1.000 47.54991  ? 201 GLU   A CB    1 
ATOM   1582 C  CG    . GLU   A 1 204 ? 43.85603 10.86043 24.41778  1.000 46.54695  ? 201 GLU   A CG    1 
ATOM   1583 C  CD    . GLU   A 1 204 ? 44.66295 11.76566 25.33178  1.000 47.02493  ? 201 GLU   A CD    1 
ATOM   1584 O  OE1   . GLU   A 1 204 ? 45.85058 11.46034 25.57443  1.000 44.38154  ? 201 GLU   A OE1   1 
ATOM   1585 O  OE2   . GLU   A 1 204 ? 44.11490 12.78788 25.79695  1.000 46.10376  ? 201 GLU   A OE2   1 
ATOM   1586 N  N     . GLU   A 1 205 ? 45.59422 8.83364  20.61619  1.000 47.04495  ? 202 GLU   A N     1 
ATOM   1587 C  CA    . GLU   A 1 205 ? 46.19256 8.94110  19.28984  1.000 48.72801  ? 202 GLU   A CA    1 
ATOM   1588 C  C     . GLU   A 1 205 ? 45.32832 8.27769  18.22409  1.000 48.44103  ? 202 GLU   A C     1 
ATOM   1589 O  O     . GLU   A 1 205 ? 45.30426 8.73578  17.07527  1.000 47.04516  ? 202 GLU   A O     1 
ATOM   1590 C  CB    . GLU   A 1 205 ? 47.59693 8.33104  19.30322  1.000 50.26573  ? 202 GLU   A CB    1 
ATOM   1591 C  CG    . GLU   A 1 205 ? 48.32361 8.36541  17.96112  1.000 53.91812  ? 202 GLU   A CG    1 
ATOM   1592 C  CD    . GLU   A 1 205 ? 48.69605 9.77130  17.50971  1.000 56.31110  ? 202 GLU   A CD    1 
ATOM   1593 O  OE1   . GLU   A 1 205 ? 48.54937 10.72625 18.30138  1.000 57.67987  ? 202 GLU   A OE1   1 
ATOM   1594 O  OE2   . GLU   A 1 205 ? 49.14147 9.92012  16.35367  1.000 57.18728  ? 202 GLU   A OE2   1 
ATOM   1595 N  N     . VAL   A 1 206 ? 44.61719 7.20456  18.57865  1.000 50.36496  ? 203 VAL   A N     1 
ATOM   1596 C  CA    . VAL   A 1 206 ? 43.70637 6.56711  17.63092  1.000 47.92244  ? 203 VAL   A CA    1 
ATOM   1597 C  C     . VAL   A 1 206 ? 42.57528 7.52254  17.26127  1.000 44.15498  ? 203 VAL   A C     1 
ATOM   1598 O  O     . VAL   A 1 206 ? 42.21954 7.66676  16.08702  1.000 43.01738  ? 203 VAL   A O     1 
ATOM   1599 C  CB    . VAL   A 1 206 ? 43.16312 5.24777  18.20898  1.000 47.73625  ? 203 VAL   A CB    1 
ATOM   1600 C  CG1   . VAL   A 1 206 ? 42.02767 4.70427  17.34054  1.000 45.75250  ? 203 VAL   A CG1   1 
ATOM   1601 C  CG2   . VAL   A 1 206 ? 44.28285 4.22493  18.34445  1.000 47.26436  ? 203 VAL   A CG2   1 
ATOM   1602 N  N     . ALA   A 1 207 ? 41.99698 8.18677  18.26528  1.000 44.18355  ? 204 ALA   A N     1 
ATOM   1603 C  CA    . ALA   A 1 207 ? 40.91987 9.13852  18.00089  1.000 44.20892  ? 204 ALA   A CA    1 
ATOM   1604 C  C     . ALA   A 1 207 ? 41.41680 10.30042 17.15377  1.000 41.91891  ? 204 ALA   A C     1 
ATOM   1605 O  O     . ALA   A 1 207 ? 40.73069 10.74704 16.22736  1.000 42.37831  ? 204 ALA   A O     1 
ATOM   1606 C  CB    . ALA   A 1 207 ? 40.33271 9.64907  19.31707  1.000 41.55942  ? 204 ALA   A CB    1 
ATOM   1607 N  N     . ARG   A 1 208 ? 42.61373 10.80241 17.46293  1.000 43.63221  ? 205 ARG   A N     1 
ATOM   1608 C  CA    . ARG   A 1 208 ? 43.18520 11.91107 16.70535  1.000 41.93773  ? 205 ARG   A CA    1 
ATOM   1609 C  C     . ARG   A 1 208 ? 43.30127 11.56144 15.22782  1.000 40.85174  ? 205 ARG   A C     1 
ATOM   1610 O  O     . ARG   A 1 208 ? 42.87509 12.33121 14.35900  1.000 37.85742  ? 205 ARG   A O     1 
ATOM   1611 C  CB    . ARG   A 1 208 ? 44.55360 12.28084 17.28132  1.000 39.40698  ? 205 ARG   A CB    1 
ATOM   1612 C  CG    . ARG   A 1 208 ? 45.10434 13.59558 16.76332  1.000 38.88507  ? 205 ARG   A CG    1 
ATOM   1613 C  CD    . ARG   A 1 208 ? 46.52528 13.82792 17.24972  1.000 41.61957  ? 205 ARG   A CD    1 
ATOM   1614 N  NE    . ARG   A 1 208 ? 47.47807 12.95070 16.58143  1.000 44.69571  ? 205 ARG   A NE    1 
ATOM   1615 C  CZ    . ARG   A 1 208 ? 48.03715 13.22056 15.40710  1.000 47.13162  ? 205 ARG   A CZ    1 
ATOM   1616 N  NH1   . ARG   A 1 208 ? 47.73601 14.34754 14.77296  1.000 44.82657  ? 205 ARG   A NH1   1 
ATOM   1617 N  NH2   . ARG   A 1 208 ? 48.89702 12.36510 14.86715  1.000 48.54590  ? 205 ARG   A NH2   1 
ATOM   1618 N  N     . LEU   A 1 209 ? 43.87678 10.39565 14.92462  1.000 43.96638  ? 206 LEU   A N     1 
ATOM   1619 C  CA    . LEU   A 1 209 ? 44.00590 9.97236  13.53506  1.000 45.26868  ? 206 LEU   A CA    1 
ATOM   1620 C  C     . LEU   A 1 209 ? 42.64341 9.69427  12.91368  1.000 44.27985  ? 206 LEU   A C     1 
ATOM   1621 O  O     . LEU   A 1 209 ? 42.42551 9.97794  11.72966  1.000 45.78742  ? 206 LEU   A O     1 
ATOM   1622 C  CB    . LEU   A 1 209 ? 44.90218 8.73794  13.44896  1.000 44.75523  ? 206 LEU   A CB    1 
ATOM   1623 C  CG    . LEU   A 1 209 ? 46.36115 8.95766  13.85522  1.000 47.29423  ? 206 LEU   A CG    1 
ATOM   1624 C  CD1   . LEU   A 1 209 ? 47.07934 7.62737  14.02620  1.000 47.17692  ? 206 LEU   A CD1   1 
ATOM   1625 C  CD2   . LEU   A 1 209 ? 47.07931 9.82730  12.82939  1.000 46.96984  ? 206 LEU   A CD2   1 
ATOM   1626 N  N     . SER   A 1 210 ? 41.71517 9.13671  13.69434  1.000 42.55939  ? 207 SER   A N     1 
ATOM   1627 C  CA    . SER   A 1 210 ? 40.37931 8.86899  13.17204  1.000 41.30780  ? 207 SER   A CA    1 
ATOM   1628 C  C     . SER   A 1 210 ? 39.66402 10.16180 12.79972  1.000 42.38532  ? 207 SER   A C     1 
ATOM   1629 O  O     . SER   A 1 210 ? 38.92480 10.20560 11.80866  1.000 45.36580  ? 207 SER   A O     1 
ATOM   1630 C  CB    . SER   A 1 210 ? 39.56601 8.07697  14.19459  1.000 44.04475  ? 207 SER   A CB    1 
ATOM   1631 O  OG    . SER   A 1 210 ? 38.24894 7.84406  13.72794  1.000 49.81177  ? 207 SER   A OG    1 
ATOM   1632 N  N     . PHE   A 1 211 ? 39.87497 11.22729 13.57608  1.000 39.74030  ? 208 PHE   A N     1 
ATOM   1633 C  CA    . PHE   A 1 211 ? 39.24505 12.50049 13.24734  1.000 39.24629  ? 208 PHE   A CA    1 
ATOM   1634 C  C     . PHE   A 1 211 ? 39.92731 13.16383 12.05836  1.000 41.53752  ? 208 PHE   A C     1 
ATOM   1635 O  O     . PHE   A 1 211 ? 39.26046 13.79083 11.22701  1.000 41.30268  ? 208 PHE   A O     1 
ATOM   1636 C  CB    . PHE   A 1 211 ? 39.24688 13.42175 14.46597  1.000 39.23463  ? 208 PHE   A CB    1 
ATOM   1637 C  CG    . PHE   A 1 211 ? 38.09357 13.18270 15.40148  1.000 39.44805  ? 208 PHE   A CG    1 
ATOM   1638 C  CD1   . PHE   A 1 211 ? 36.79234 13.39869 14.98052  1.000 34.77169  ? 208 PHE   A CD1   1 
ATOM   1639 C  CD2   . PHE   A 1 211 ? 38.30814 12.74040 16.69572  1.000 41.60372  ? 208 PHE   A CD2   1 
ATOM   1640 C  CE1   . PHE   A 1 211 ? 35.72355 13.17652 15.82996  1.000 35.18224  ? 208 PHE   A CE1   1 
ATOM   1641 C  CE2   . PHE   A 1 211 ? 37.24245 12.51738 17.55348  1.000 39.04125  ? 208 PHE   A CE2   1 
ATOM   1642 C  CZ    . PHE   A 1 211 ? 35.94981 12.73867 17.11822  1.000 36.48188  ? 208 PHE   A CZ    1 
ATOM   1643 N  N     . ARG   A 1 212 ? 41.25369 13.03658 11.95647  1.000 41.00876  ? 209 ARG   A N     1 
ATOM   1644 C  CA    . ARG   A 1 212 ? 41.94952 13.55621 10.78354  1.000 41.65859  ? 209 ARG   A CA    1 
ATOM   1645 C  C     . ARG   A 1 212 ? 41.43676 12.90024 9.50800   1.000 41.58461  ? 209 ARG   A C     1 
ATOM   1646 O  O     . ARG   A 1 212 ? 41.19803 13.58182 8.50390   1.000 41.47102  ? 209 ARG   A O     1 
ATOM   1647 C  CB    . ARG   A 1 212 ? 43.45959 13.35501 10.92928  1.000 43.96526  ? 209 ARG   A CB    1 
ATOM   1648 C  CG    . ARG   A 1 212 ? 44.14321 14.44317 11.74474  1.000 45.49689  ? 209 ARG   A CG    1 
ATOM   1649 C  CD    . ARG   A 1 212 ? 45.62728 14.15994 11.95670  1.000 46.91740  ? 209 ARG   A CD    1 
ATOM   1650 N  NE    . ARG   A 1 212 ? 46.38659 14.13368 10.70843  1.000 48.43818  ? 209 ARG   A NE    1 
ATOM   1651 C  CZ    . ARG   A 1 212 ? 46.86671 15.21471 10.09949  1.000 48.05106  ? 209 ARG   A CZ    1 
ATOM   1652 N  NH1   . ARG   A 1 212 ? 46.66100 16.41897 10.61679  1.000 42.31006  ? 209 ARG   A NH1   1 
ATOM   1653 N  NH2   . ARG   A 1 212 ? 47.55298 15.09257 8.97014   1.000 50.54521  ? 209 ARG   A NH2   1 
ATOM   1654 N  N     . ASN   A 1 213 ? 41.24800 11.57817 9.53219   1.000 42.48634  ? 210 ASN   A N     1 
ATOM   1655 C  CA    . ASN   A 1 213 ? 40.66889 10.89302 8.38008   1.000 43.90874  ? 210 ASN   A CA    1 
ATOM   1656 C  C     . ASN   A 1 213 ? 39.21150 11.28794 8.17759   1.000 44.83859  ? 210 ASN   A C     1 
ATOM   1657 O  O     . ASN   A 1 213 ? 38.77316 11.50112 7.04087   1.000 45.16636  ? 210 ASN   A O     1 
ATOM   1658 C  CB    . ASN   A 1 213 ? 40.79492 9.37723  8.54847   1.000 45.63079  ? 210 ASN   A CB    1 
ATOM   1659 C  CG    . ASN   A 1 213 ? 42.23004 8.89274  8.42145   1.000 49.73347  ? 210 ASN   A CG    1 
ATOM   1660 O  OD1   . ASN   A 1 213 ? 43.03039 9.47517  7.68688   1.000 50.32259  ? 210 ASN   A OD1   1 
ATOM   1661 N  ND2   . ASN   A 1 213 ? 42.56126 7.82171  9.13679   1.000 47.55414  ? 210 ASN   A ND2   1 
ATOM   1662 N  N     . LEU   A 1 214 ? 38.44729 11.39642 9.26854   1.000 45.17501  ? 211 LEU   A N     1 
ATOM   1663 C  CA    . LEU   A 1 214 ? 37.03359 11.74029 9.15087   1.000 42.93864  ? 211 LEU   A CA    1 
ATOM   1664 C  C     . LEU   A 1 214 ? 36.84412 13.12276 8.53864   1.000 42.55994  ? 211 LEU   A C     1 
ATOM   1665 O  O     . LEU   A 1 214 ? 35.97840 13.31328 7.67562   1.000 45.11923  ? 211 LEU   A O     1 
ATOM   1666 C  CB    . LEU   A 1 214 ? 36.35916 11.67054 10.52054  1.000 41.72045  ? 211 LEU   A CB    1 
ATOM   1667 C  CG    . LEU   A 1 214 ? 34.87836 12.05307 10.53868  1.000 41.01231  ? 211 LEU   A CG    1 
ATOM   1668 C  CD1   . LEU   A 1 214 ? 34.03015 10.92940 9.95790   1.000 38.77208  ? 211 LEU   A CD1   1 
ATOM   1669 C  CD2   . LEU   A 1 214 ? 34.41618 12.42124 11.94715  1.000 42.87670  ? 211 LEU   A CD2   1 
ATOM   1670 N  N     . ASN   A 1 215 ? 37.64214 14.10164 8.97370   1.000 39.65982  ? 212 ASN   A N     1 
ATOM   1671 C  CA    . ASN   A 1 215 ? 37.47242 15.46463 8.47995   1.000 38.91535  ? 212 ASN   A CA    1 
ATOM   1672 C  C     . ASN   A 1 215 ? 37.78240 15.55715 6.99151   1.000 38.23244  ? 212 ASN   A C     1 
ATOM   1673 O  O     . ASN   A 1 215 ? 37.10185 16.27745 6.25190   1.000 42.78149  ? 212 ASN   A O     1 
ATOM   1674 C  CB    . ASN   A 1 215 ? 38.35316 16.42510 9.27894   1.000 38.46830  ? 212 ASN   A CB    1 
ATOM   1675 C  CG    . ASN   A 1 215 ? 37.98143 16.46577 10.74888  1.000 38.38126  ? 212 ASN   A CG    1 
ATOM   1676 O  OD1   . ASN   A 1 215 ? 36.86969 16.08966 11.12882  1.000 37.01921  ? 212 ASN   A OD1   1 
ATOM   1677 N  ND2   . ASN   A 1 215 ? 38.91168 16.92105 11.58621  1.000 35.22940  ? 212 ASN   A ND2   1 
ATOM   1678 N  N     . THR   A 1 216 ? 38.80555 14.83554 6.53327   1.000 39.54726  ? 213 THR   A N     1 
ATOM   1679 C  CA    . THR   A 1 216 ? 39.11117 14.81142 5.10642   1.000 41.14829  ? 213 THR   A CA    1 
ATOM   1680 C  C     . THR   A 1 216 ? 38.00752 14.11285 4.32228   1.000 43.55970  ? 213 THR   A C     1 
ATOM   1681 O  O     . THR   A 1 216 ? 37.62726 14.56653 3.23641   1.000 47.73048  ? 213 THR   A O     1 
ATOM   1682 C  CB    . THR   A 1 216 ? 40.46068 14.12561 4.86907   1.000 42.53757  ? 213 THR   A CB    1 
ATOM   1683 O  OG1   . THR   A 1 216 ? 41.49973 14.87337 5.51597   1.000 43.72401  ? 213 THR   A OG1   1 
ATOM   1684 C  CG2   . THR   A 1 216 ? 40.76740 14.03064 3.37835   1.000 40.44571  ? 213 THR   A CG2   1 
ATOM   1685 N  N     . PHE   A 1 217 ? 37.47319 13.01501 4.86315   1.000 42.04309  ? 214 PHE   A N     1 
ATOM   1686 C  CA    . PHE   A 1 217 ? 36.41851 12.27976 4.17077   1.000 43.97329  ? 214 PHE   A CA    1 
ATOM   1687 C  C     . PHE   A 1 217 ? 35.14491 13.11109 4.06303   1.000 46.09217  ? 214 PHE   A C     1 
ATOM   1688 O  O     . PHE   A 1 217 ? 34.50963 13.15933 3.00241   1.000 46.40442  ? 214 PHE   A O     1 
ATOM   1689 C  CB    . PHE   A 1 217 ? 36.14163 10.95913 4.89194   1.000 45.72275  ? 214 PHE   A CB    1 
ATOM   1690 C  CG    . PHE   A 1 217 ? 35.05257 10.13634 4.25689   1.000 51.40267  ? 214 PHE   A CG    1 
ATOM   1691 C  CD1   . PHE   A 1 217 ? 33.72703 10.30005 4.63612   1.000 50.73003  ? 214 PHE   A CD1   1 
ATOM   1692 C  CD2   . PHE   A 1 217 ? 35.35427 9.19693  3.28221   1.000 51.81001  ? 214 PHE   A CD2   1 
ATOM   1693 C  CE1   . PHE   A 1 217 ? 32.72434 9.54881  4.05041   1.000 52.08400  ? 214 PHE   A CE1   1 
ATOM   1694 C  CE2   . PHE   A 1 217 ? 34.35546 8.44115  2.69538   1.000 51.99655  ? 214 PHE   A CE2   1 
ATOM   1695 C  CZ    . PHE   A 1 217 ? 33.03834 8.61703  3.07968   1.000 51.79846  ? 214 PHE   A CZ    1 
ATOM   1696 N  N     . LEU   A 1 218 ? 34.75220 13.77037 5.15794   1.000 44.01218  ? 215 LEU   A N     1 
ATOM   1697 C  CA    . LEU   A 1 218 ? 33.50780 14.53431 5.15261   1.000 42.08518  ? 215 LEU   A CA    1 
ATOM   1698 C  C     . LEU   A 1 218 ? 33.57772 15.71028 4.18517   1.000 42.83705  ? 215 LEU   A C     1 
ATOM   1699 O  O     . LEU   A 1 218 ? 32.58202 16.04094 3.53028   1.000 40.01624  ? 215 LEU   A O     1 
ATOM   1700 C  CB    . LEU   A 1 218 ? 33.18093 15.01572 6.56446   1.000 36.03207  ? 215 LEU   A CB    1 
ATOM   1701 C  CG    . LEU   A 1 218 ? 32.70825 13.93809 7.54367   1.000 36.86173  ? 215 LEU   A CG    1 
ATOM   1702 C  CD1   . LEU   A 1 218 ? 32.47690 14.53896 8.93085   1.000 35.39765  ? 215 LEU   A CD1   1 
ATOM   1703 C  CD2   . LEU   A 1 218 ? 31.43821 13.25840 7.03200   1.000 33.50327  ? 215 LEU   A CD2   1 
ATOM   1704 N  N     . ALA   A 1 219 ? 34.74518 16.34898 4.07562   1.000 43.43745  ? 216 ALA   A N     1 
ATOM   1705 C  CA    . ALA   A 1 219 ? 34.88885 17.47707 3.16146   1.000 42.55994  ? 216 ALA   A CA    1 
ATOM   1706 C  C     . ALA   A 1 219 ? 34.74837 17.04761 1.70728   1.000 47.02843  ? 216 ALA   A C     1 
ATOM   1707 O  O     . ALA   A 1 219 ? 34.34522 17.85265 0.86100   1.000 50.18095  ? 216 ALA   A O     1 
ATOM   1708 C  CB    . ALA   A 1 219 ? 36.23578 18.16449 3.38436   1.000 39.95947  ? 216 ALA   A CB    1 
ATOM   1709 N  N     . ALA   A 1 220 ? 35.06985 15.79274 1.39599   1.000 46.32760  ? 217 ALA   A N     1 
ATOM   1710 C  CA    . ALA   A 1 220 ? 34.96441 15.28971 0.03374   1.000 47.50227  ? 217 ALA   A CA    1 
ATOM   1711 C  C     . ALA   A 1 220 ? 33.67241 14.52614 -0.22914  1.000 46.26240  ? 217 ALA   A C     1 
ATOM   1712 O  O     . ALA   A 1 220 ? 33.38201 14.21864 -1.39000  1.000 47.39518  ? 217 ALA   A O     1 
ATOM   1713 C  CB    . ALA   A 1 220 ? 36.16226 14.38866 -0.28848  1.000 47.43154  ? 217 ALA   A CB    1 
ATOM   1714 N  N     . ASP   A 1 221 ? 32.89966 14.22230 0.80352   1.000 43.86719  ? 218 ASP   A N     1 
ATOM   1715 C  CA    . ASP   A 1 221 ? 31.68810 13.41825 0.67796   1.000 43.99642  ? 218 ASP   A CA    1 
ATOM   1716 C  C     . ASP   A 1 221 ? 30.60794 14.18001 -0.08411  1.000 44.30905  ? 218 ASP   A C     1 
ATOM   1717 O  O     . ASP   A 1 221 ? 30.07296 15.16369 0.44432   1.000 42.74283  ? 218 ASP   A O     1 
ATOM   1718 C  CB    . ASP   A 1 221 ? 31.19139 13.02574 2.06874   1.000 46.41458  ? 218 ASP   A CB    1 
ATOM   1719 C  CG    . ASP   A 1 221 ? 30.10321 11.96539 2.03366   1.000 47.39442  ? 218 ASP   A CG    1 
ATOM   1720 O  OD1   . ASP   A 1 221 ? 29.54467 11.69329 0.95047   1.000 49.03919  ? 218 ASP   A OD1   1 
ATOM   1721 O  OD2   . ASP   A 1 221 ? 29.81272 11.39387 3.10409   1.000 47.63249  ? 218 ASP   A OD2   1 
ATOM   1722 N  N     . PRO   A 1 222 ? 30.24763 13.76390 -1.30093  1.000 45.51415  ? 219 PRO   A N     1 
ATOM   1723 C  CA    . PRO   A 1 222 ? 29.23901 14.51301 -2.06726  1.000 46.38110  ? 219 PRO   A CA    1 
ATOM   1724 C  C     . PRO   A 1 222 ? 27.81956 14.32653 -1.56103  1.000 48.23355  ? 219 PRO   A C     1 
ATOM   1725 O  O     . PRO   A 1 222 ? 26.92842 15.07198 -1.99007  1.000 49.05500  ? 219 PRO   A O     1 
ATOM   1726 C  CB    . PRO   A 1 222 ? 29.39668 13.95349 -3.48453  1.000 45.31080  ? 219 PRO   A CB    1 
ATOM   1727 C  CG    . PRO   A 1 222 ? 29.85321 12.54735 -3.26349  1.000 47.01973  ? 219 PRO   A CG    1 
ATOM   1728 C  CD    . PRO   A 1 222 ? 30.73368 12.58111 -2.03222  1.000 46.71457  ? 219 PRO   A CD    1 
ATOM   1729 N  N     . ARG   A 1 223 ? 27.57968 13.36828 -0.66512  1.000 47.04221  ? 220 ARG   A N     1 
ATOM   1730 C  CA    . ARG   A 1 223 ? 26.24133 13.14372 -0.13899  1.000 45.29460  ? 220 ARG   A CA    1 
ATOM   1731 C  C     . ARG   A 1 223 ? 25.78882 14.23101 0.82356   1.000 47.86183  ? 220 ARG   A C     1 
ATOM   1732 O  O     . ARG   A 1 223 ? 24.60634 14.25379 1.17877   1.000 49.64274  ? 220 ARG   A O     1 
ATOM   1733 C  CB    . ARG   A 1 223 ? 26.17574 11.78861 0.56635   1.000 44.19650  ? 220 ARG   A CB    1 
ATOM   1734 C  CG    . ARG   A 1 223 ? 26.31947 10.59330 -0.36025  1.000 46.11398  ? 220 ARG   A CG    1 
ATOM   1735 C  CD    . ARG   A 1 223 ? 26.59337 9.32606  0.43128   1.000 45.55537  ? 220 ARG   A CD    1 
ATOM   1736 N  NE    . ARG   A 1 223 ? 27.82770 9.43271  1.20144   1.000 46.09938  ? 220 ARG   A NE    1 
ATOM   1737 C  CZ    . ARG   A 1 223 ? 28.34517 8.45040  1.93209   1.000 48.55871  ? 220 ARG   A CZ    1 
ATOM   1738 N  NH1   . ARG   A 1 223 ? 27.73829 7.27291  1.99577   1.000 46.53966  ? 220 ARG   A NH1   1 
ATOM   1739 N  NH2   . ARG   A 1 223 ? 29.47653 8.64512  2.59712   1.000 48.82777  ? 220 ARG   A NH2   1 
ATOM   1740 N  N     . VAL   A 1 224 ? 26.68256 15.12150 1.25927   1.000 46.23329  ? 221 VAL   A N     1 
ATOM   1741 C  CA    . VAL   A 1 224 ? 26.35212 16.09485 2.29339   1.000 47.20859  ? 221 VAL   A CA    1 
ATOM   1742 C  C     . VAL   A 1 224 ? 27.10377 17.39616 2.04367   1.000 47.94640  ? 221 VAL   A C     1 
ATOM   1743 O  O     . VAL   A 1 224 ? 28.16501 17.41059 1.41565   1.000 47.64651  ? 221 VAL   A O     1 
ATOM   1744 C  CB    . VAL   A 1 224 ? 26.69899 15.58020 3.71349   1.000 47.26038  ? 221 VAL   A CB    1 
ATOM   1745 C  CG1   . VAL   A 1 224 ? 25.78423 14.43970 4.14178   1.000 48.30635  ? 221 VAL   A CG1   1 
ATOM   1746 C  CG2   . VAL   A 1 224 ? 28.16833 15.16571 3.78208   1.000 44.01583  ? 221 VAL   A CG2   1 
ATOM   1747 N  N     A GLU   A 1 225 ? 26.54063 18.48620 2.54683   0.460 47.77820  ? 222 GLU   A N     1 
ATOM   1748 N  N     B GLU   A 1 225 ? 26.52260 18.49004 2.52796   0.540 47.71943  ? 222 GLU   A N     1 
ATOM   1749 C  CA    A GLU   A 1 225 ? 27.26712 19.73574 2.71601   0.460 48.63038  ? 222 GLU   A CA    1 
ATOM   1750 C  CA    B GLU   A 1 225 ? 27.22531 19.74626 2.74340   0.540 48.61683  ? 222 GLU   A CA    1 
ATOM   1751 C  C     A GLU   A 1 225 ? 27.61638 19.88939 4.19000   0.460 46.89904  ? 222 GLU   A C     1 
ATOM   1752 C  C     B GLU   A 1 225 ? 27.64738 19.81156 4.20473   0.540 46.87979  ? 222 GLU   A C     1 
ATOM   1753 O  O     A GLU   A 1 225 ? 26.82888 19.51920 5.06556   0.460 46.71725  ? 222 GLU   A O     1 
ATOM   1754 O  O     B GLU   A 1 225 ? 26.94599 19.31225 5.08805   0.540 46.36583  ? 222 GLU   A O     1 
ATOM   1755 C  CB    A GLU   A 1 225 ? 26.44734 20.93061 2.22466   0.460 50.66316  ? 222 GLU   A CB    1 
ATOM   1756 C  CB    B GLU   A 1 225 ? 26.34116 20.94744 2.39775   0.540 50.46661  ? 222 GLU   A CB    1 
ATOM   1757 C  CG    A GLU   A 1 225 ? 25.01091 20.94289 2.70812   0.460 52.81824  ? 222 GLU   A CG    1 
ATOM   1758 C  CG    B GLU   A 1 225 ? 25.99570 21.07415 0.92263   0.540 53.90638  ? 222 GLU   A CG    1 
ATOM   1759 C  CD    A GLU   A 1 225 ? 24.12509 21.84001 1.86629   0.460 55.27420  ? 222 GLU   A CD    1 
ATOM   1760 C  CD    B GLU   A 1 225 ? 24.75937 21.92383 0.68156   0.540 56.47624  ? 222 GLU   A CD    1 
ATOM   1761 O  OE1   A GLU   A 1 225 ? 22.93423 21.98734 2.20488   0.460 55.48717  ? 222 GLU   A OE1   1 
ATOM   1762 O  OE1   B GLU   A 1 225 ? 24.02719 22.20308 1.65584   0.540 55.46850  ? 222 GLU   A OE1   1 
ATOM   1763 O  OE2   A GLU   A 1 225 ? 24.61860 22.39379 0.86151   0.460 56.32486  ? 222 GLU   A OE2   1 
ATOM   1764 O  OE2   B GLU   A 1 225 ? 24.51593 22.30777 -0.48370  0.540 58.00317  ? 222 GLU   A OE2   1 
ATOM   1765 N  N     . ILE   A 1 226 ? 28.80846 20.41576 4.46159   1.000 44.37323  ? 223 ILE   A N     1 
ATOM   1766 C  CA    . ILE   A 1 226 ? 29.36605 20.40705 5.80630   1.000 40.30967  ? 223 ILE   A CA    1 
ATOM   1767 C  C     . ILE   A 1 226 ? 29.69520 21.81428 6.28495   1.000 37.91107  ? 223 ILE   A C     1 
ATOM   1768 O  O     . ILE   A 1 226 ? 29.79582 22.76536 5.50699   1.000 38.12324  ? 223 ILE   A O     1 
ATOM   1769 C  CB    . ILE   A 1 226 ? 30.62238 19.51562 5.90884   1.000 41.47823  ? 223 ILE   A CB    1 
ATOM   1770 C  CG1   . ILE   A 1 226 ? 31.79614 20.15133 5.16180   1.000 41.74055  ? 223 ILE   A CG1   1 
ATOM   1771 C  CG2   . ILE   A 1 226 ? 30.32921 18.10938 5.38794   1.000 42.81572  ? 223 ILE   A CG2   1 
ATOM   1772 C  CD1   . ILE   A 1 226 ? 33.13731 19.55874 5.53388   1.000 42.42371  ? 223 ILE   A CD1   1 
ATOM   1773 N  N     . SER   A 1 227 ? 29.85823 21.92425 7.60181   1.000 36.89178  ? 224 SER   A N     1 
ATOM   1774 C  CA    . SER   A 1 227 ? 30.36834 23.13039 8.24196   1.000 38.27142  ? 224 SER   A CA    1 
ATOM   1775 C  C     . SER   A 1 227 ? 31.05172 22.72126 9.53739   1.000 38.52168  ? 224 SER   A C     1 
ATOM   1776 O  O     . SER   A 1 227 ? 30.39317 22.21360 10.45146  1.000 34.42885  ? 224 SER   A O     1 
ATOM   1777 C  CB    . SER   A 1 227 ? 29.24950 24.13325 8.51934   1.000 38.22907  ? 224 SER   A CB    1 
ATOM   1778 O  OG    . SER   A 1 227 ? 29.73223 25.21201 9.30314   1.000 38.39347  ? 224 SER   A OG    1 
ATOM   1779 N  N     . GLN   A 1 228 ? 32.36353 22.93334 9.61566   1.000 36.56797  ? 225 GLN   A N     1 
ATOM   1780 C  CA    . GLN   A 1 228 ? 33.11874 22.65348 10.83036  1.000 35.44461  ? 225 GLN   A CA    1 
ATOM   1781 C  C     . GLN   A 1 228 ? 33.15871 23.91404 11.68581  1.000 35.94770  ? 225 GLN   A C     1 
ATOM   1782 O  O     . GLN   A 1 228 ? 33.63614 24.96306 11.23433  1.000 35.53269  ? 225 GLN   A O     1 
ATOM   1783 C  CB    . GLN   A 1 228 ? 34.53170 22.17332 10.50085  1.000 35.89559  ? 225 GLN   A CB    1 
ATOM   1784 C  CG    . GLN   A 1 228 ? 35.28303 21.62810 11.70611  1.000 36.99557  ? 225 GLN   A CG    1 
ATOM   1785 C  CD    . GLN   A 1 228 ? 36.50835 20.81877 11.31904  1.000 39.96858  ? 225 GLN   A CD    1 
ATOM   1786 O  OE1   . GLN   A 1 228 ? 37.18273 21.12224 10.33515  1.000 45.87711  ? 225 GLN   A OE1   1 
ATOM   1787 N  NE2   . GLN   A 1 228 ? 36.79509 19.77476 12.08862  1.000 34.49767  ? 225 GLN   A NE2   1 
ATOM   1788 N  N     . VAL   A 1 229 ? 32.66060 23.81047 12.91632  1.000 33.58280  ? 226 VAL   A N     1 
ATOM   1789 C  CA    . VAL   A 1 229 ? 32.47974 24.95831 13.79769  1.000 31.59348  ? 226 VAL   A CA    1 
ATOM   1790 C  C     . VAL   A 1 229 ? 33.39957 24.79525 14.99874  1.000 30.86628  ? 226 VAL   A C     1 
ATOM   1791 O  O     . VAL   A 1 229 ? 33.32726 23.78572 15.71128  1.000 30.32925  ? 226 VAL   A O     1 
ATOM   1792 C  CB    . VAL   A 1 229 ? 31.01584 25.10225 14.24060  1.000 34.47294  ? 226 VAL   A CB    1 
ATOM   1793 C  CG1   . VAL   A 1 229 ? 30.82698 26.36851 15.07144  1.000 29.75367  ? 226 VAL   A CG1   1 
ATOM   1794 C  CG2   . VAL   A 1 229 ? 30.08968 25.08798 13.01848  1.000 34.03622  ? 226 VAL   A CG2   1 
ATOM   1795 N  N     . SER   A 1 230 ? 34.24504 25.80062 15.23530  1.000 30.13794  ? 227 SER   A N     1 
ATOM   1796 C  CA    . SER   A 1 230 ? 35.21230 25.78284 16.33250  1.000 31.01045  ? 227 SER   A CA    1 
ATOM   1797 C  C     . SER   A 1 230 ? 34.55172 26.17513 17.66017  1.000 33.51086  ? 227 SER   A C     1 
ATOM   1798 O  O     . SER   A 1 230 ? 34.97487 27.10049 18.35653  1.000 32.91786  ? 227 SER   A O     1 
ATOM   1799 C  CB    . SER   A 1 230 ? 36.38553 26.70057 16.00430  1.000 31.52983  ? 227 SER   A CB    1 
ATOM   1800 O  OG    . SER   A 1 230 ? 35.93926 28.01805 15.71473  1.000 33.03685  ? 227 SER   A OG    1 
ATOM   1801 N  N     . ILE   A 1 231 ? 33.49389 25.43670 18.01022  1.000 29.33103  ? 228 ILE   A N     1 
ATOM   1802 C  CA    . ILE   A 1 231 ? 32.80992 25.59297 19.28955  1.000 25.15806  ? 228 ILE   A CA    1 
ATOM   1803 C  C     . ILE   A 1 231 ? 33.00587 24.32006 20.10498  1.000 28.25064  ? 228 ILE   A C     1 
ATOM   1804 O  O     . ILE   A 1 231 ? 33.04870 23.20831 19.56056  1.000 31.78070  ? 228 ILE   A O     1 
ATOM   1805 C  CB    . ILE   A 1 231 ? 31.30942 25.91331 19.10294  1.000 30.23121  ? 228 ILE   A CB    1 
ATOM   1806 C  CG1   . ILE   A 1 231 ? 30.66866 26.27582 20.44209  1.000 27.74692  ? 228 ILE   A CG1   1 
ATOM   1807 C  CG2   . ILE   A 1 231 ? 30.57092 24.74238 18.44804  1.000 25.12953  ? 228 ILE   A CG2   1 
ATOM   1808 C  CD1   . ILE   A 1 231 ? 29.26654 26.79296 20.31136  1.000 30.65903  ? 228 ILE   A CD1   1 
ATOM   1809 N  N     . GLY   A 1 232 ? 33.13595 24.48774 21.42045  1.000 27.49203  ? 229 GLY   A N     1 
ATOM   1810 C  CA    . GLY   A 1 232 ? 33.39263 23.34089 22.27970  1.000 27.44703  ? 229 GLY   A CA    1 
ATOM   1811 C  C     . GLY   A 1 232 ? 34.74415 22.73399 21.93799  1.000 31.96446  ? 229 GLY   A C     1 
ATOM   1812 O  O     . GLY   A 1 232 ? 35.78782 23.39499 22.01478  1.000 28.90072  ? 229 GLY   A O     1 
ATOM   1813 N  N     . ASP   A 1 233 ? 34.73659 21.45142 21.57156  1.000 33.64485  ? 230 ASP   A N     1 
ATOM   1814 C  CA    . ASP   A 1 233 ? 35.90519 20.76491 21.03871  1.000 37.28956  ? 230 ASP   A CA    1 
ATOM   1815 C  C     . ASP   A 1 233 ? 35.83551 20.62449 19.51939  1.000 38.29323  ? 230 ASP   A C     1 
ATOM   1816 O  O     . ASP   A 1 233 ? 36.52719 19.77825 18.94133  1.000 36.30992  ? 230 ASP   A O     1 
ATOM   1817 C  CB    . ASP   A 1 233 ? 36.05921 19.38823 21.69374  1.000 41.15323  ? 230 ASP   A CB    1 
ATOM   1818 C  CG    . ASP   A 1 233 ? 37.42505 18.77163 21.44204  1.000 47.68371  ? 230 ASP   A CG    1 
ATOM   1819 O  OD1   . ASP   A 1 233 ? 38.37272 19.54279 21.20170  1.000 50.33696  ? 230 ASP   A OD1   1 
ATOM   1820 O  OD2   . ASP   A 1 233 ? 37.54609 17.52630 21.45790  1.000 47.88317  ? 230 ASP   A OD2   1 
ATOM   1821 N  N     . GLY   A 1 234 ? 35.01064 21.43609 18.86269  1.000 36.42757  ? 231 GLY   A N     1 
ATOM   1822 C  CA    . GLY   A 1 234 ? 34.81818 21.31805 17.43251  1.000 32.69771  ? 231 GLY   A CA    1 
ATOM   1823 C  C     . GLY   A 1 234 ? 33.60877 20.47068 17.10156  1.000 35.60345  ? 231 GLY   A C     1 
ATOM   1824 O  O     . GLY   A 1 234 ? 33.52252 19.31067 17.51618  1.000 35.02608  ? 231 GLY   A O     1 
ATOM   1825 N  N     . VAL   A 1 235 ? 32.65841 21.04544 16.36904  1.000 36.55781  ? 232 VAL   A N     1 
ATOM   1826 C  CA    . VAL   A 1 235 ? 31.47009 20.33820 15.91215  1.000 33.65843  ? 232 VAL   A CA    1 
ATOM   1827 C  C     . VAL   A 1 235 ? 31.39610 20.47539 14.40080  1.000 35.38821  ? 232 VAL   A C     1 
ATOM   1828 O  O     . VAL   A 1 235 ? 31.51916 21.58495 13.86900  1.000 35.61972  ? 232 VAL   A O     1 
ATOM   1829 C  CB    . VAL   A 1 235 ? 30.18831 20.88549 16.56804  1.000 34.33065  ? 232 VAL   A CB    1 
ATOM   1830 C  CG1   . VAL   A 1 235 ? 28.95821 20.19529 15.99470  1.000 35.24094  ? 232 VAL   A CG1   1 
ATOM   1831 C  CG2   . VAL   A 1 235 ? 30.25181 20.71271 18.07716  1.000 35.54208  ? 232 VAL   A CG2   1 
ATOM   1832 N  N     . THR   A 1 236 ? 31.21090 19.35568 13.70995  1.000 34.07275  ? 233 THR   A N     1 
ATOM   1833 C  CA    . THR   A 1 236 ? 31.03115 19.34814 12.26475  1.000 35.19232  ? 233 THR   A CA    1 
ATOM   1834 C  C     . THR   A 1 236 ? 29.56588 19.08060 11.95580  1.000 35.84657  ? 233 THR   A C     1 
ATOM   1835 O  O     . THR   A 1 236 ? 29.04736 18.00300 12.27079  1.000 37.31765  ? 233 THR   A O     1 
ATOM   1836 C  CB    . THR   A 1 236 ? 31.91914 18.30119 11.59490  1.000 33.18544  ? 233 THR   A CB    1 
ATOM   1837 O  OG1   . THR   A 1 236 ? 33.29386 18.60342 11.85816  1.000 34.79699  ? 233 THR   A OG1   1 
ATOM   1838 C  CG2   . THR   A 1 236 ? 31.69045 18.30728 10.09563  1.000 30.55345  ? 233 THR   A CG2   1 
ATOM   1839 N  N     . ILE   A 1 237 ? 28.90763 20.05941 11.34639  1.000 33.96220  ? 234 ILE   A N     1 
ATOM   1840 C  CA    . ILE   A 1 237 ? 27.51477 19.93388 10.94002  1.000 31.12562  ? 234 ILE   A CA    1 
ATOM   1841 C  C     . ILE   A 1 237 ? 27.47220 19.40675 9.51389   1.000 35.92461  ? 234 ILE   A C     1 
ATOM   1842 O  O     . ILE   A 1 237 ? 28.11513 19.96496 8.61768   1.000 36.38724  ? 234 ILE   A O     1 
ATOM   1843 C  CB    . ILE   A 1 237 ? 26.78815 21.28444 11.04776  1.000 35.59481  ? 234 ILE   A CB    1 
ATOM   1844 C  CG1   . ILE   A 1 237 ? 27.12211 21.96865 12.37656  1.000 34.12064  ? 234 ILE   A CG1   1 
ATOM   1845 C  CG2   . ILE   A 1 237 ? 25.27842 21.09665 10.90648  1.000 35.96647  ? 234 ILE   A CG2   1 
ATOM   1846 C  CD1   . ILE   A 1 237 ? 26.51215 23.34475 12.52829  1.000 31.15274  ? 234 ILE   A CD1   1 
ATOM   1847 N  N     . CYS   A 1 238 ? 26.72671 18.32600 9.30390   1.000 36.36268  ? 235 CYS   A N     1 
ATOM   1848 C  CA    . CYS   A 1 238 ? 26.48088 17.77867 7.97838   1.000 39.55618  ? 235 CYS   A CA    1 
ATOM   1849 C  C     . CYS   A 1 238 ? 25.00267 17.91884 7.64474   1.000 41.75334  ? 235 CYS   A C     1 
ATOM   1850 O  O     . CYS   A 1 238 ? 24.14393 17.77114 8.51889   1.000 44.48528  ? 235 CYS   A O     1 
ATOM   1851 C  CB    . CYS   A 1 238 ? 26.89310 16.30537 7.89583   1.000 42.33842  ? 235 CYS   A CB    1 
ATOM   1852 S  SG    . CYS   A 1 238 ? 28.59442 15.97695 8.39578   1.000 42.95236  ? 235 CYS   A SG    1 
ATOM   1853 N  N     . ARG   A 1 239 ? 24.70938 18.21337 6.38245   1.000 37.78642  ? 236 ARG   A N     1 
ATOM   1854 C  CA    . ARG   A 1 239 ? 23.33968 18.30379 5.89400   1.000 39.35969  ? 236 ARG   A CA    1 
ATOM   1855 C  C     . ARG   A 1 239 ? 23.20488 17.37315 4.69934   1.000 38.04024  ? 236 ARG   A C     1 
ATOM   1856 O  O     . ARG   A 1 239 ? 23.93274 17.52137 3.71341   1.000 41.09870  ? 236 ARG   A O     1 
ATOM   1857 C  CB    . ARG   A 1 239 ? 22.98080 19.74246 5.51573   1.000 39.51654  ? 236 ARG   A CB    1 
ATOM   1858 C  CG    . ARG   A 1 239 ? 21.56746 19.90899 4.97906   1.000 43.94597  ? 236 ARG   A CG    1 
ATOM   1859 C  CD    . ARG   A 1 239 ? 21.22773 21.37264 4.76381   1.000 49.48424  ? 236 ARG   A CD    1 
ATOM   1860 N  NE    . ARG   A 1 239 ? 19.91926 21.54581 4.13912   1.000 57.75490  ? 236 ARG   A NE    1 
ATOM   1861 C  CZ    . ARG   A 1 239 ? 19.72079 21.61138 2.82584   1.000 61.97473  ? 236 ARG   A CZ    1 
ATOM   1862 N  NH1   . ARG   A 1 239 ? 20.74876 21.51978 1.99256   1.000 60.17813  ? 236 ARG   A NH1   1 
ATOM   1863 N  NH2   . ARG   A 1 239 ? 18.49413 21.76990 2.34530   1.000 65.58156  ? 236 ARG   A NH2   1 
ATOM   1864 N  N     . ARG   A 1 240 ? 22.28524 16.41472 4.79094   1.000 38.36773  ? 237 ARG   A N     1 
ATOM   1865 C  CA    . ARG   A 1 240 ? 22.15833 15.39977 3.75244   1.000 41.04097  ? 237 ARG   A CA    1 
ATOM   1866 C  C     . ARG   A 1 240 ? 21.58948 15.99879 2.47171   1.000 42.07436  ? 237 ARG   A C     1 
ATOM   1867 O  O     . ARG   A 1 240 ? 20.53955 16.64845 2.48748   1.000 41.77588  ? 237 ARG   A O     1 
ATOM   1868 C  CB    . ARG   A 1 240 ? 21.27016 14.25428 4.22981   1.000 41.49530  ? 237 ARG   A CB    1 
ATOM   1869 C  CG    . ARG   A 1 240 ? 21.07468 13.18239 3.17296   1.000 40.81263  ? 237 ARG   A CG    1 
ATOM   1870 C  CD    . ARG   A 1 240 ? 20.10978 12.10333 3.62042   1.000 39.62836  ? 237 ARG   A CD    1 
ATOM   1871 N  NE    . ARG   A 1 240 ? 19.88704 11.13521 2.54965   1.000 40.84856  ? 237 ARG   A NE    1 
ATOM   1872 C  CZ    . ARG   A 1 240 ? 18.99997 10.14677 2.59822   1.000 40.56762  ? 237 ARG   A CZ    1 
ATOM   1873 N  NH1   . ARG   A 1 240 ? 18.23531 9.98507  3.66990   1.000 38.34070  ? 237 ARG   A NH1   1 
ATOM   1874 N  NH2   . ARG   A 1 240 ? 18.87557 9.32255  1.56737   1.000 40.70325  ? 237 ARG   A NH2   1 
ATOM   1875 N  N     . LEU   A 1 241 ? 22.27763 15.75952 1.35566   1.000 44.17634  ? 238 LEU   A N     1 
ATOM   1876 C  CA    . LEU   A 1 241 ? 21.85595 16.28559 0.06298   1.000 47.15863  ? 238 LEU   A CA    1 
ATOM   1877 C  C     . LEU   A 1 241 ? 20.97689 15.30827 -0.70853  1.000 50.77925  ? 238 LEU   A C     1 
ATOM   1878 O  O     . LEU   A 1 241 ? 20.00992 15.72675 -1.35366  1.000 52.42972  ? 238 LEU   A O     1 
ATOM   1879 C  CB    . LEU   A 1 241 ? 23.08127 16.65658 -0.77241  1.000 43.54360  ? 238 LEU   A CB    1 
ATOM   1880 C  CG    . LEU   A 1 241 ? 23.89949 17.80962 -0.19360  1.000 45.47084  ? 238 LEU   A CG    1 
ATOM   1881 C  CD1   . LEU   A 1 241 ? 25.14965 18.08162 -1.03192  1.000 44.01592  ? 238 LEU   A CD1   1 
ATOM   1882 C  CD2   . LEU   A 1 241 ? 23.02797 19.05137 -0.08686  1.000 42.88653  ? 238 LEU   A CD2   1 
ATOM   1883 N  N     . TYR   A 1 242 ? 21.29460 14.01850 -0.66258  1.000 52.01168  ? 239 TYR   A N     1 
ATOM   1884 C  CA    . TYR   A 1 242 ? 20.48016 13.00684 -1.32714  1.000 56.47171  ? 239 TYR   A CA    1 
ATOM   1885 C  C     . TYR   A 1 242 ? 20.67384 11.63534 -0.68429  1.000 58.27904  ? 239 TYR   A C     1 
ATOM   1886 O  O     . TYR   A 1 242 ? 19.89863 10.70867 -0.92376  1.000 60.58131  ? 239 TYR   A O     1 
ATOM   1887 C  CB    . TYR   A 1 242 ? 20.80963 12.94401 -2.82284  1.000 57.20286  ? 239 TYR   A CB    1 
ATOM   1888 C  CG    . TYR   A 1 242 ? 22.25812 12.63252 -3.12755  1.000 58.72074  ? 239 TYR   A CG    1 
ATOM   1889 C  CD1   . TYR   A 1 242 ? 22.71114 11.31996 -3.17138  1.000 60.66755  ? 239 TYR   A CD1   1 
ATOM   1890 C  CD2   . TYR   A 1 242 ? 23.17108 13.64976 -3.37996  1.000 57.66408  ? 239 TYR   A CD2   1 
ATOM   1891 C  CE1   . TYR   A 1 242 ? 24.03127 11.02801 -3.44749  1.000 61.80950  ? 239 TYR   A CE1   1 
ATOM   1892 C  CE2   . TYR   A 1 242 ? 24.49594 13.36672 -3.66170  1.000 58.33098  ? 239 TYR   A CE2   1 
ATOM   1893 C  CZ    . TYR   A 1 242 ? 24.91883 12.05274 -3.69341  1.000 60.53896  ? 239 TYR   A CZ    1 
ATOM   1894 O  OH    . TYR   A 1 242 ? 26.23292 11.75489 -3.96946  1.000 61.31765  ? 239 TYR   A OH    1 
ATOM   1895 O  OXT   . TYR   A 1 242 ? 21.60973 11.41831 0.08577   1.000 57.59582  ? 239 TYR   A OXT   1 
ATOM   1896 N  N     . ASP   B 1 9   ? 49.00650 48.78248 11.94424  1.000 99.03562  ? 6   ASP   B N     1 
ATOM   1897 C  CA    . ASP   B 1 9   ? 49.93328 49.87557 12.21117  1.000 100.57364 ? 6   ASP   B CA    1 
ATOM   1898 C  C     . ASP   B 1 9   ? 49.19726 51.06663 12.81926  1.000 98.19943  ? 6   ASP   B C     1 
ATOM   1899 O  O     . ASP   B 1 9   ? 49.81237 51.95940 13.40648  1.000 98.77951  ? 6   ASP   B O     1 
ATOM   1900 C  CB    . ASP   B 1 9   ? 50.65906 50.29109 10.92982  1.000 102.29783 ? 6   ASP   B CB    1 
ATOM   1901 N  N     . ASP   B 1 10  ? 47.87475 51.07537 12.66798  1.000 93.33292  ? 7   ASP   B N     1 
ATOM   1902 C  CA    . ASP   B 1 10  ? 47.01441 52.06039 13.31132  1.000 89.63353  ? 7   ASP   B CA    1 
ATOM   1903 C  C     . ASP   B 1 10  ? 45.99639 51.44725 14.25958  1.000 82.38565  ? 7   ASP   B C     1 
ATOM   1904 O  O     . ASP   B 1 10  ? 45.64434 52.08192 15.25602  1.000 79.09684  ? 7   ASP   B O     1 
ATOM   1905 C  CB    . ASP   B 1 10  ? 46.26806 52.90271 12.26197  1.000 91.10213  ? 7   ASP   B CB    1 
ATOM   1906 C  CG    . ASP   B 1 10  ? 46.87302 54.28481 12.08419  1.000 93.86480  ? 7   ASP   B CG    1 
ATOM   1907 O  OD1   . ASP   B 1 10  ? 47.94740 54.55233 12.66460  1.000 95.48479  ? 7   ASP   B OD1   1 
ATOM   1908 O  OD2   . ASP   B 1 10  ? 46.26982 55.10843 11.36680  1.000 94.36781  ? 7   ASP   B OD2   1 
ATOM   1909 N  N     . TYR   B 1 11  ? 45.51667 50.23912 13.97782  1.000 78.93410  ? 8   TYR   B N     1 
ATOM   1910 C  CA    . TYR   B 1 11  ? 44.60275 49.51656 14.84946  1.000 75.53640  ? 8   TYR   B CA    1 
ATOM   1911 C  C     . TYR   B 1 11  ? 45.30953 48.28704 15.40712  1.000 69.73590  ? 8   TYR   B C     1 
ATOM   1912 O  O     . TYR   B 1 11  ? 46.13597 47.67258 14.72600  1.000 68.77671  ? 8   TYR   B O     1 
ATOM   1913 C  CB    . TYR   B 1 11  ? 43.32947 49.12369 14.09526  1.000 76.43214  ? 8   TYR   B CB    1 
ATOM   1914 C  CG    . TYR   B 1 11  ? 42.50484 50.31502 13.64608  1.000 80.11648  ? 8   TYR   B CG    1 
ATOM   1915 C  CD1   . TYR   B 1 11  ? 42.69145 50.88391 12.39111  1.000 81.28187  ? 8   TYR   B CD1   1 
ATOM   1916 C  CD2   . TYR   B 1 11  ? 41.54709 50.87701 14.48272  1.000 81.16711  ? 8   TYR   B CD2   1 
ATOM   1917 C  CE1   . TYR   B 1 11  ? 41.94205 51.97453 11.98060  1.000 82.02481  ? 8   TYR   B CE1   1 
ATOM   1918 C  CE2   . TYR   B 1 11  ? 40.79554 51.96700 14.08142  1.000 81.41938  ? 8   TYR   B CE2   1 
ATOM   1919 C  CZ    . TYR   B 1 11  ? 40.99582 52.50997 12.83022  1.000 82.62473  ? 8   TYR   B CZ    1 
ATOM   1920 O  OH    . TYR   B 1 11  ? 40.24832 53.59364 12.42911  1.000 84.18015  ? 8   TYR   B OH    1 
ATOM   1921 N  N     . SER   B 1 12  ? 44.98005 47.93203 16.64919  1.000 66.88884  ? 9   SER   B N     1 
ATOM   1922 C  CA    . SER   B 1 12  ? 45.79496 47.01144 17.43251  1.000 68.48523  ? 9   SER   B CA    1 
ATOM   1923 C  C     . SER   B 1 12  ? 45.33502 45.55852 17.38245  1.000 67.51306  ? 9   SER   B C     1 
ATOM   1924 O  O     . SER   B 1 12  ? 46.15946 44.66258 17.59569  1.000 68.68769  ? 9   SER   B O     1 
ATOM   1925 C  CB    . SER   B 1 12  ? 45.82746 47.46600 18.89616  1.000 68.10804  ? 9   SER   B CB    1 
ATOM   1926 O  OG    . SER   B 1 12  ? 46.06204 48.85941 18.98676  1.000 70.17230  ? 9   SER   B OG    1 
ATOM   1927 N  N     . LEU   B 1 13  ? 44.05919 45.29834 17.10892  1.000 66.07407  ? 10  LEU   B N     1 
ATOM   1928 C  CA    . LEU   B 1 13  ? 43.50009 43.95441 17.20499  1.000 65.91397  ? 10  LEU   B CA    1 
ATOM   1929 C  C     . LEU   B 1 13  ? 43.62479 43.14529 15.91888  1.000 68.25987  ? 10  LEU   B C     1 
ATOM   1930 O  O     . LEU   B 1 13  ? 43.27450 41.96056 15.91888  1.000 70.21943  ? 10  LEU   B O     1 
ATOM   1931 C  CB    . LEU   B 1 13  ? 42.02154 44.03001 17.60112  1.000 63.81430  ? 10  LEU   B CB    1 
ATOM   1932 C  CG    . LEU   B 1 13  ? 41.63942 44.67331 18.93472  1.000 64.02365  ? 10  LEU   B CG    1 
ATOM   1933 C  CD1   . LEU   B 1 13  ? 40.13525 44.89379 18.99449  1.000 59.42538  ? 10  LEU   B CD1   1 
ATOM   1934 C  CD2   . LEU   B 1 13  ? 42.09917 43.80529 20.09227  1.000 65.57433  ? 10  LEU   B CD2   1 
ATOM   1935 N  N     . VAL   B 1 14  ? 44.12570 43.74446 14.83482  1.000 69.33343  ? 11  VAL   B N     1 
ATOM   1936 C  CA    . VAL   B 1 14  ? 44.00199 43.14550 13.50844  1.000 69.75780  ? 11  VAL   B CA    1 
ATOM   1937 C  C     . VAL   B 1 14  ? 44.75325 41.82542 13.36667  1.000 66.26749  ? 11  VAL   B C     1 
ATOM   1938 O  O     . VAL   B 1 14  ? 44.40684 41.01871 12.49647  1.000 63.93040  ? 11  VAL   B O     1 
ATOM   1939 C  CB    . VAL   B 1 14  ? 44.46944 44.14532 12.43270  1.000 74.71836  ? 11  VAL   B CB    1 
ATOM   1940 C  CG1   . VAL   B 1 14  ? 43.57567 45.37966 12.42873  1.000 77.57816  ? 11  VAL   B CG1   1 
ATOM   1941 C  CG2   . VAL   B 1 14  ? 45.91555 44.53475 12.65834  1.000 73.65894  ? 11  VAL   B CG2   1 
ATOM   1942 N  N     . HIS   B 1 15  ? 45.77391 41.57255 14.18576  1.000 65.93761  ? 12  HIS   B N     1 
ATOM   1943 C  CA    . HIS   B 1 15  ? 46.56407 40.35370 14.06738  1.000 66.70129  ? 12  HIS   B CA    1 
ATOM   1944 C  C     . HIS   B 1 15  ? 46.22385 39.32358 15.13983  1.000 67.21987  ? 12  HIS   B C     1 
ATOM   1945 O  O     . HIS   B 1 15  ? 47.02187 38.41285 15.39077  1.000 69.60604  ? 12  HIS   B O     1 
ATOM   1946 C  CB    . HIS   B 1 15  ? 48.05679 40.68285 14.10608  1.000 68.11660  ? 12  HIS   B CB    1 
ATOM   1947 C  CG    . HIS   B 1 15  ? 48.52542 41.49768 12.94093  1.000 69.24910  ? 12  HIS   B CG    1 
ATOM   1948 N  ND1   . HIS   B 1 15  ? 48.48233 41.03525 11.64309  1.000 68.58396  ? 12  HIS   B ND1   1 
ATOM   1949 C  CD2   . HIS   B 1 15  ? 49.05148 42.74370 12.87852  1.000 69.88846  ? 12  HIS   B CD2   1 
ATOM   1950 C  CE1   . HIS   B 1 15  ? 48.95867 41.96231 10.83121  1.000 69.24721  ? 12  HIS   B CE1   1 
ATOM   1951 N  NE2   . HIS   B 1 15  ? 49.31260 43.00823 11.55585  1.000 70.53770  ? 12  HIS   B NE2   1 
ATOM   1952 N  N     . LYS   B 1 16  ? 45.05655 39.44042 15.76547  1.000 63.34902  ? 13  LYS   B N     1 
ATOM   1953 C  CA    . LYS   B 1 16  ? 44.64078 38.53599 16.82571  1.000 59.51533  ? 13  LYS   B CA    1 
ATOM   1954 C  C     . LYS   B 1 16  ? 43.54281 37.59748 16.34389  1.000 57.75579  ? 13  LYS   B C     1 
ATOM   1955 O  O     . LYS   B 1 16  ? 42.72084 37.95118 15.49491  1.000 56.14300  ? 13  LYS   B O     1 
ATOM   1956 C  CB    . LYS   B 1 16  ? 44.15071 39.31850 18.04455  1.000 57.61347  ? 13  LYS   B CB    1 
ATOM   1957 C  CG    . LYS   B 1 16  ? 45.26098 39.76679 18.96938  1.000 59.02943  ? 13  LYS   B CG    1 
ATOM   1958 C  CD    . LYS   B 1 16  ? 45.04913 41.18630 19.44347  1.000 59.75207  ? 13  LYS   B CD    1 
ATOM   1959 C  CE    . LYS   B 1 16  ? 45.27606 41.28736 20.93467  1.000 62.34307  ? 13  LYS   B CE    1 
ATOM   1960 N  NZ    . LYS   B 1 16  ? 46.50893 40.56698 21.37201  1.000 65.22924  ? 13  LYS   B NZ    1 
ATOM   1961 N  N     . ASN   B 1 17  ? 43.54145 36.39126 16.90217  1.000 56.64307  ? 14  ASN   B N     1 
ATOM   1962 C  CA    . ASN   B 1 17  ? 42.52058 35.39514 16.63027  1.000 53.44055  ? 14  ASN   B CA    1 
ATOM   1963 C  C     . ASN   B 1 17  ? 42.07948 34.79567 17.95758  1.000 50.74802  ? 14  ASN   B C     1 
ATOM   1964 O  O     . ASN   B 1 17  ? 42.81230 34.83282 18.94838  1.000 52.19260  ? 14  ASN   B O     1 
ATOM   1965 C  CB    . ASN   B 1 17  ? 43.03905 34.30609 15.68053  1.000 59.08896  ? 14  ASN   B CB    1 
ATOM   1966 C  CG    . ASN   B 1 17  ? 41.92162 33.59140 14.94680  1.000 65.24556  ? 14  ASN   B CG    1 
ATOM   1967 O  OD1   . ASN   B 1 17  ? 41.56512 32.45812 15.28086  1.000 64.87916  ? 14  ASN   B OD1   1 
ATOM   1968 N  ND2   . ASN   B 1 17  ? 41.35494 34.25567 13.94345  1.000 65.69089  ? 14  ASN   B ND2   1 
ATOM   1969 N  N     . ILE   B 1 18  ? 40.86262 34.25063 17.98062  1.000 48.00375  ? 15  ILE   B N     1 
ATOM   1970 C  CA    . ILE   B 1 18  ? 40.31522 33.71886 19.22701  1.000 43.66878  ? 15  ILE   B CA    1 
ATOM   1971 C  C     . ILE   B 1 18  ? 40.66899 32.25207 19.46175  1.000 38.52373  ? 15  ILE   B C     1 
ATOM   1972 O  O     . ILE   B 1 18  ? 40.51140 31.76267 20.59147  1.000 38.36437  ? 15  ILE   B O     1 
ATOM   1973 C  CB    . ILE   B 1 18  ? 38.78636 33.89420 19.28395  1.000 40.39429  ? 15  ILE   B CB    1 
ATOM   1974 C  CG1   . ILE   B 1 18  ? 38.12100 33.14466 18.13115  1.000 39.73519  ? 15  ILE   B CG1   1 
ATOM   1975 C  CG2   . ILE   B 1 18  ? 38.41009 35.38269 19.25740  1.000 38.30183  ? 15  ILE   B CG2   1 
ATOM   1976 C  CD1   . ILE   B 1 18  ? 36.61851 33.06830 18.25431  1.000 35.70756  ? 15  ILE   B CD1   1 
ATOM   1977 N  N     . LEU   B 1 19  ? 41.13676 31.53839 18.43904  1.000 36.28830  ? 16  LEU   B N     1 
ATOM   1978 C  CA    . LEU   B 1 19  ? 41.59550 30.17295 18.63875  1.000 38.55142  ? 16  LEU   B CA    1 
ATOM   1979 C  C     . LEU   B 1 19  ? 43.01509 30.17026 19.20291  1.000 42.76347  ? 16  LEU   B C     1 
ATOM   1980 O  O     . LEU   B 1 19  ? 43.73608 31.16917 19.13827  1.000 39.33018  ? 16  LEU   B O     1 
ATOM   1981 C  CB    . LEU   B 1 19  ? 41.53672 29.38876 17.33169  1.000 37.14985  ? 16  LEU   B CB    1 
ATOM   1982 C  CG    . LEU   B 1 19  ? 40.16068 29.31712 16.65806  1.000 36.61566  ? 16  LEU   B CG    1 
ATOM   1983 C  CD1   . LEU   B 1 19  ? 40.17404 28.30263 15.52487  1.000 36.45188  ? 16  LEU   B CD1   1 
ATOM   1984 C  CD2   . LEU   B 1 19  ? 39.05520 28.99564 17.66507  1.000 35.10965  ? 16  LEU   B CD2   1 
ATOM   1985 N  N     . HIS   B 1 20  ? 43.41936 29.02363 19.75988  1.000 47.06888  ? 17  HIS   B N     1 
ATOM   1986 C  CA    . HIS   B 1 20  ? 44.66992 28.99131 20.51358  1.000 50.81350  ? 17  HIS   B CA    1 
ATOM   1987 C  C     . HIS   B 1 20  ? 45.90753 29.03244 19.62323  1.000 48.40429  ? 17  HIS   B C     1 
ATOM   1988 O  O     . HIS   B 1 20  ? 46.99998 29.31795 20.12549  1.000 46.44832  ? 17  HIS   B O     1 
ATOM   1989 C  CB    . HIS   B 1 20  ? 44.71512 27.76531 21.44350  1.000 58.21204  ? 17  HIS   B CB    1 
ATOM   1990 C  CG    . HIS   B 1 20  ? 44.74012 26.43867 20.74056  1.000 66.36418  ? 17  HIS   B CG    1 
ATOM   1991 N  ND1   . HIS   B 1 20  ? 44.28936 25.28046 21.33800  1.000 68.32224  ? 17  HIS   B ND1   1 
ATOM   1992 C  CD2   . HIS   B 1 20  ? 45.18332 26.07613 19.51269  1.000 69.34691  ? 17  HIS   B CD2   1 
ATOM   1993 C  CE1   . HIS   B 1 20  ? 44.43999 24.26676 20.50421  1.000 68.38897  ? 17  HIS   B CE1   1 
ATOM   1994 N  NE2   . HIS   B 1 20  ? 44.98189 24.72252 19.38944  1.000 68.75111  ? 17  HIS   B NE2   1 
ATOM   1995 N  N     . SER   B 1 21  ? 45.77193 28.76282 18.32619  1.000 46.08018  ? 18  SER   B N     1 
ATOM   1996 C  CA    . SER   B 1 21  ? 46.92613 28.76503 17.44052  1.000 47.62178  ? 18  SER   B CA    1 
ATOM   1997 C  C     . SER   B 1 21  ? 46.47353 29.05373 16.01910  1.000 46.30253  ? 18  SER   B C     1 
ATOM   1998 O  O     . SER   B 1 21  ? 45.36622 28.68454 15.61534  1.000 41.92437  ? 18  SER   B O     1 
ATOM   1999 C  CB    . SER   B 1 21  ? 47.68307 27.43085 17.48329  1.000 52.25989  ? 18  SER   B CB    1 
ATOM   2000 O  OG    . SER   B 1 21  ? 47.07990 26.46736 16.63489  1.000 53.04292  ? 18  SER   B OG    1 
ATOM   2001 N  N     . GLU   B 1 22  ? 47.34872 29.72724 15.26771  1.000 49.43992  ? 19  GLU   B N     1 
ATOM   2002 C  CA    . GLU   B 1 22  ? 47.10807 29.93405 13.84469  1.000 51.40315  ? 19  GLU   B CA    1 
ATOM   2003 C  C     . GLU   B 1 22  ? 47.07380 28.61051 13.09138  1.000 47.26959  ? 19  GLU   B C     1 
ATOM   2004 O  O     . GLU   B 1 22  ? 46.38681 28.49540 12.07027  1.000 46.78359  ? 19  GLU   B O     1 
ATOM   2005 C  CB    . GLU   B 1 22  ? 48.18872 30.85044 13.26670  1.000 60.26995  ? 19  GLU   B CB    1 
ATOM   2006 C  CG    . GLU   B 1 22  ? 48.02071 31.19834 11.79449  1.000 70.97136  ? 19  GLU   B CG    1 
ATOM   2007 C  CD    . GLU   B 1 22  ? 47.32402 32.53053 11.58290  1.000 81.09153  ? 19  GLU   B CD    1 
ATOM   2008 O  OE1   . GLU   B 1 22  ? 47.61535 33.48472 12.33739  1.000 84.56458  ? 19  GLU   B OE1   1 
ATOM   2009 O  OE2   . GLU   B 1 22  ? 46.48032 32.62227 10.66478  1.000 83.51681  ? 19  GLU   B OE2   1 
ATOM   2010 N  N     . ASP   B 1 23  ? 47.80346 27.60232 13.58025  1.000 43.22096  ? 20  ASP   B N     1 
ATOM   2011 C  CA    . ASP   B 1 23  ? 47.84250 26.31130 12.89967  1.000 41.86846  ? 20  ASP   B CA    1 
ATOM   2012 C  C     . ASP   B 1 23  ? 46.48010 25.62986 12.91818  1.000 41.28657  ? 20  ASP   B C     1 
ATOM   2013 O  O     . ASP   B 1 23  ? 46.08469 24.99761 11.93113  1.000 40.16749  ? 20  ASP   B O     1 
ATOM   2014 C  CB    . ASP   B 1 23  ? 48.89855 25.40865 13.53857  1.000 43.62284  ? 20  ASP   B CB    1 
ATOM   2015 C  CG    . ASP   B 1 23  ? 50.30716 25.95839 13.38983  1.000 51.21231  ? 20  ASP   B CG    1 
ATOM   2016 O  OD1   . ASP   B 1 23  ? 50.52715 26.80431 12.49557  1.000 51.93039  ? 20  ASP   B OD1   1 
ATOM   2017 O  OD2   . ASP   B 1 23  ? 51.19220 25.53968 14.16712  1.000 52.66903  ? 20  ASP   B OD2   1 
ATOM   2018 N  N     . LEU   B 1 24  ? 45.75100 25.74057 14.03152  1.000 41.21969  ? 21  LEU   B N     1 
ATOM   2019 C  CA    . LEU   B 1 24  ? 44.42261 25.13775 14.10679  1.000 39.36894  ? 21  LEU   B CA    1 
ATOM   2020 C  C     . LEU   B 1 24  ? 43.46024 25.81522 13.13856  1.000 41.20412  ? 21  LEU   B C     1 
ATOM   2021 O  O     . LEU   B 1 24  ? 42.69519 25.14549 12.43362  1.000 42.27226  ? 21  LEU   B O     1 
ATOM   2022 C  CB    . LEU   B 1 24  ? 43.89130 25.20851 15.53919  1.000 36.11943  ? 21  LEU   B CB    1 
ATOM   2023 C  CG    . LEU   B 1 24  ? 42.50432 24.60068 15.76768  1.000 38.25892  ? 21  LEU   B CG    1 
ATOM   2024 C  CD1   . LEU   B 1 24  ? 42.45645 23.16730 15.26509  1.000 36.72321  ? 21  LEU   B CD1   1 
ATOM   2025 C  CD2   . LEU   B 1 24  ? 42.12255 24.66596 17.23626  1.000 36.81485  ? 21  LEU   B CD2   1 
ATOM   2026 N  N     . LEU   B 1 25  ? 43.48434 27.15011 13.09234  1.000 38.12680  ? 22  LEU   B N     1 
ATOM   2027 C  CA    . LEU   B 1 25  ? 42.62539 27.86650 12.15395  1.000 36.32604  ? 22  LEU   B CA    1 
ATOM   2028 C  C     . LEU   B 1 25  ? 42.96823 27.51387 10.71193  1.000 37.62023  ? 22  LEU   B C     1 
ATOM   2029 O  O     . LEU   B 1 25  ? 42.07003 27.31203 9.88414   1.000 38.06233  ? 22  LEU   B O     1 
ATOM   2030 C  CB    . LEU   B 1 25  ? 42.74169 29.37432 12.37401  1.000 37.64523  ? 22  LEU   B CB    1 
ATOM   2031 C  CG    . LEU   B 1 25  ? 41.86941 30.23049 11.44802  1.000 41.53271  ? 22  LEU   B CG    1 
ATOM   2032 C  CD1   . LEU   B 1 25  ? 40.39729 29.85091 11.59657  1.000 39.75494  ? 22  LEU   B CD1   1 
ATOM   2033 C  CD2   . LEU   B 1 25  ? 42.06886 31.71005 11.73109  1.000 42.94829  ? 22  LEU   B CD2   1 
ATOM   2034 N  N     . LYS   B 1 26  ? 44.26465 27.43861 10.39130  1.000 35.85975  ? 23  LYS   B N     1 
ATOM   2035 C  CA    . LYS   B 1 26  ? 44.67469 27.03836 9.04880   1.000 39.73123  ? 23  LYS   B CA    1 
ATOM   2036 C  C     . LYS   B 1 26  ? 44.20629 25.62455 8.72537   1.000 40.18720  ? 23  LYS   B C     1 
ATOM   2037 O  O     . LYS   B 1 26  ? 43.77674 25.35014 7.59848   1.000 43.53486  ? 23  LYS   B O     1 
ATOM   2038 C  CB    . LYS   B 1 26  ? 46.19504 27.14277 8.90172   1.000 43.03533  ? 23  LYS   B CB    1 
ATOM   2039 C  CG    . LYS   B 1 26  ? 46.71297 28.56028 8.72819   1.000 46.77307  ? 23  LYS   B CG    1 
ATOM   2040 C  CD    . LYS   B 1 26  ? 48.22597 28.57725 8.53771   1.000 51.60686  ? 23  LYS   B CD    1 
ATOM   2041 N  N     . TYR   B 1 27  ? 44.28961 24.71169 9.69782   1.000 36.46887  ? 24  TYR   B N     1 
ATOM   2042 C  CA    . TYR   B 1 27  ? 43.77813 23.35983 9.48764   1.000 38.55584  ? 24  TYR   B CA    1 
ATOM   2043 C  C     . TYR   B 1 27  ? 42.29466 23.38136 9.13969   1.000 37.07615  ? 24  TYR   B C     1 
ATOM   2044 O  O     . TYR   B 1 27  ? 41.85755 22.70684 8.20028   1.000 38.40858  ? 24  TYR   B O     1 
ATOM   2045 C  CB    . TYR   B 1 27  ? 44.01894 22.49760 10.72786  1.000 39.40655  ? 24  TYR   B CB    1 
ATOM   2046 C  CG    . TYR   B 1 27  ? 43.36959 21.13393 10.63089  1.000 42.24466  ? 24  TYR   B CG    1 
ATOM   2047 C  CD1   . TYR   B 1 27  ? 44.02117 20.07694 10.00551  1.000 46.18849  ? 24  TYR   B CD1   1 
ATOM   2048 C  CD2   . TYR   B 1 27  ? 42.09983 20.90506 11.15291  1.000 41.51475  ? 24  TYR   B CD2   1 
ATOM   2049 C  CE1   . TYR   B 1 27  ? 43.43019 18.83025 9.90628   1.000 45.83549  ? 24  TYR   B CE1   1 
ATOM   2050 C  CE2   . TYR   B 1 27  ? 41.50056 19.66310 11.05545  1.000 43.41571  ? 24  TYR   B CE2   1 
ATOM   2051 C  CZ    . TYR   B 1 27  ? 42.16945 18.62968 10.43245  1.000 42.88828  ? 24  TYR   B CZ    1 
ATOM   2052 O  OH    . TYR   B 1 27  ? 41.57248 17.39416 10.34094  1.000 39.25365  ? 24  TYR   B OH    1 
ATOM   2053 N  N     . ILE   B 1 28  ? 41.50215 24.14619 9.89570   1.000 36.36681  ? 25  ILE   B N     1 
ATOM   2054 C  CA    . ILE   B 1 28  ? 40.06480 24.22895 9.63897   1.000 37.17539  ? 25  ILE   B CA    1 
ATOM   2055 C  C     . ILE   B 1 28  ? 39.80372 24.75538 8.23377   1.000 39.99452  ? 25  ILE   B C     1 
ATOM   2056 O  O     . ILE   B 1 28  ? 39.02663 24.17493 7.46722   1.000 44.11062  ? 25  ILE   B O     1 
ATOM   2057 C  CB    . ILE   B 1 28  ? 39.37795 25.11057 10.69695  1.000 34.23079  ? 25  ILE   B CB    1 
ATOM   2058 C  CG1   . ILE   B 1 28  ? 39.51587 24.49166 12.08628  1.000 34.73467  ? 25  ILE   B CG1   1 
ATOM   2059 C  CG2   . ILE   B 1 28  ? 37.90881 25.34102 10.33728  1.000 36.22646  ? 25  ILE   B CG2   1 
ATOM   2060 C  CD1   . ILE   B 1 28  ? 38.95833 25.36021 13.18905  1.000 34.20954  ? 25  ILE   B CD1   1 
ATOM   2061 N  N     . LEU   B 1 29  ? 40.44255 25.87392 7.88344   1.000 38.67159  ? 26  LEU   B N     1 
ATOM   2062 C  CA    . LEU   B 1 29  ? 40.21450 26.48173 6.57656   1.000 40.65656  ? 26  LEU   B CA    1 
ATOM   2063 C  C     . LEU   B 1 29  ? 40.62367 25.54290 5.44918   1.000 41.77779  ? 26  LEU   B C     1 
ATOM   2064 O  O     . LEU   B 1 29  ? 39.90433 25.40833 4.45070   1.000 38.07711  ? 26  LEU   B O     1 
ATOM   2065 C  CB    . LEU   B 1 29  ? 40.98123 27.80096 6.47320   1.000 39.82627  ? 26  LEU   B CB    1 
ATOM   2066 C  CG    . LEU   B 1 29  ? 40.59621 28.90788 7.45516   1.000 38.38173  ? 26  LEU   B CG    1 
ATOM   2067 C  CD1   . LEU   B 1 29  ? 41.60251 30.06210 7.40209   1.000 32.05836  ? 26  LEU   B CD1   1 
ATOM   2068 C  CD2   . LEU   B 1 29  ? 39.17823 29.40188 7.16971   1.000 37.80322  ? 26  LEU   B CD2   1 
ATOM   2069 N  N     . GLU   B 1 30  ? 41.77550 24.88136 5.59338   1.000 42.10201  ? 27  GLU   B N     1 
ATOM   2070 C  CA    . GLU   B 1 30  ? 42.30170 24.05791 4.51078   1.000 45.31479  ? 27  GLU   B CA    1 
ATOM   2071 C  C     . GLU   B 1 30  ? 41.57748 22.72154 4.40867   1.000 46.96666  ? 27  GLU   B C     1 
ATOM   2072 O  O     . GLU   B 1 30  ? 41.35209 22.22074 3.30082   1.000 46.12336  ? 27  GLU   B O     1 
ATOM   2073 C  CB    . GLU   B 1 30  ? 43.80215 23.83534 4.70109   1.000 44.98228  ? 27  GLU   B CB    1 
ATOM   2074 C  CG    . GLU   B 1 30  ? 44.65538 25.05107 4.38280   1.000 50.70459  ? 27  GLU   B CG    1 
ATOM   2075 C  CD    . GLU   B 1 30  ? 46.12106 24.83633 4.71220   1.000 59.33893  ? 27  GLU   B CD    1 
ATOM   2076 O  OE1   . GLU   B 1 30  ? 46.47818 23.72320 5.15295   1.000 62.02132  ? 27  GLU   B OE1   1 
ATOM   2077 O  OE2   . GLU   B 1 30  ? 46.91564 25.78381 4.53556   1.000 64.34152  ? 27  GLU   B OE2   1 
ATOM   2078 N  N     . THR   B 1 31  ? 41.20901 22.12733 5.54400   1.000 46.00294  ? 28  THR   B N     1 
ATOM   2079 C  CA    . THR   B 1 31  ? 40.57277 20.81547 5.50761   1.000 47.65498  ? 28  THR   B CA    1 
ATOM   2080 C  C     . THR   B 1 31  ? 39.09376 20.91942 5.15730   1.000 47.75732  ? 28  THR   B C     1 
ATOM   2081 O  O     . THR   B 1 31  ? 38.59529 20.16457 4.31432   1.000 46.65163  ? 28  THR   B O     1 
ATOM   2082 C  CB    . THR   B 1 31  ? 40.74481 20.10314 6.85038   1.000 49.44727  ? 28  THR   B CB    1 
ATOM   2083 O  OG1   . THR   B 1 31  ? 42.13949 19.94056 7.13358   1.000 50.77791  ? 28  THR   B OG1   1 
ATOM   2084 C  CG2   . THR   B 1 31  ? 40.07285 18.73824 6.81965   1.000 50.91707  ? 28  THR   B CG2   1 
ATOM   2085 N  N     . SER   B 1 32  ? 38.38048 21.85598 5.78587   1.000 44.79803  ? 29  SER   B N     1 
ATOM   2086 C  CA    . SER   B 1 32  ? 36.92423 21.87573 5.74314   1.000 46.14566  ? 29  SER   B CA    1 
ATOM   2087 C  C     . SER   B 1 32  ? 36.32812 23.04769 4.97891   1.000 47.50710  ? 29  SER   B C     1 
ATOM   2088 O  O     . SER   B 1 32  ? 35.25434 22.89573 4.39209   1.000 50.92561  ? 29  SER   B O     1 
ATOM   2089 C  CB    . SER   B 1 32  ? 36.35543 21.88475 7.16826   1.000 44.41456  ? 29  SER   B CB    1 
ATOM   2090 O  OG    . SER   B 1 32  ? 36.83295 20.78129 7.91749   1.000 46.58505  ? 29  SER   B OG    1 
ATOM   2091 N  N     . ALA   B 1 33  ? 36.98337 24.20763 4.97011   1.000 44.58738  ? 30  ALA   B N     1 
ATOM   2092 C  CA    . ALA   B 1 33  ? 36.37289 25.41175 4.41419   1.000 46.62088  ? 30  ALA   B CA    1 
ATOM   2093 C  C     . ALA   B 1 33  ? 36.69231 25.58963 2.93196   1.000 47.79346  ? 30  ALA   B C     1 
ATOM   2094 O  O     . ALA   B 1 33  ? 35.78496 25.58701 2.09360   1.000 46.35827  ? 30  ALA   B O     1 
ATOM   2095 C  CB    . ALA   B 1 33  ? 36.81122 26.64254 5.21700   1.000 48.51208  ? 30  ALA   B CB    1 
ATOM   2096 N  N     . TYR   B 1 34  ? 37.97182 25.75798 2.59816   1.000 50.55652  ? 31  TYR   B N     1 
ATOM   2097 C  CA    . TYR   B 1 34  ? 38.36689 25.96755 1.20926   1.000 50.48342  ? 31  TYR   B CA    1 
ATOM   2098 C  C     . TYR   B 1 34  ? 37.89019 24.88123 0.24360   1.000 48.41832  ? 31  TYR   B C     1 
ATOM   2099 O  O     . TYR   B 1 34  ? 37.49525 25.22388 -0.87453  1.000 47.94041  ? 31  TYR   B O     1 
ATOM   2100 C  CB    . TYR   B 1 34  ? 39.89306 26.12890 1.12334   1.000 52.98049  ? 31  TYR   B CB    1 
ATOM   2101 C  CG    . TYR   B 1 34  ? 40.42661 27.35747 1.83166   1.000 54.21202  ? 31  TYR   B CG    1 
ATOM   2102 C  CD1   . TYR   B 1 34  ? 39.62984 28.48221 2.01179   1.000 54.36588  ? 31  TYR   B CD1   1 
ATOM   2103 C  CD2   . TYR   B 1 34  ? 41.72709 27.39149 2.32171   1.000 54.34316  ? 31  TYR   B CD2   1 
ATOM   2104 C  CE1   . TYR   B 1 34  ? 40.11512 29.60745 2.65986   1.000 56.11224  ? 31  TYR   B CE1   1 
ATOM   2105 C  CE2   . TYR   B 1 34  ? 42.22041 28.51276 2.96979   1.000 54.20756  ? 31  TYR   B CE2   1 
ATOM   2106 C  CZ    . TYR   B 1 34  ? 41.41249 29.61528 3.13557   1.000 56.19361  ? 31  TYR   B CZ    1 
ATOM   2107 O  OH    . TYR   B 1 34  ? 41.90362 30.72845 3.78094   1.000 59.17866  ? 31  TYR   B OH    1 
ATOM   2108 N  N     . PRO   B 1 35  ? 37.90822 23.57968 0.59562   1.000 48.70975  ? 32  PRO   B N     1 
ATOM   2109 C  CA    . PRO   B 1 35  ? 37.36507 22.57543 -0.34145  1.000 49.81586  ? 32  PRO   B CA    1 
ATOM   2110 C  C     . PRO   B 1 35  ? 35.87018 22.70143 -0.59469  1.000 46.26471  ? 32  PRO   B C     1 
ATOM   2111 O  O     . PRO   B 1 35  ? 35.37564 22.10931 -1.56190  1.000 47.27897  ? 32  PRO   B O     1 
ATOM   2112 C  CB    . PRO   B 1 35  ? 37.69273 21.24241 0.34840   1.000 49.96127  ? 32  PRO   B CB    1 
ATOM   2113 C  CG    . PRO   B 1 35  ? 38.83391 21.55355 1.24983   1.000 52.57424  ? 32  PRO   B CG    1 
ATOM   2114 C  CD    . PRO   B 1 35  ? 38.59016 22.94564 1.73354   1.000 49.04667  ? 32  PRO   B CD    1 
ATOM   2115 N  N     . ARG   B 1 36  ? 35.13670 23.44303 0.23130   1.000 41.43272  ? 33  ARG   B N     1 
ATOM   2116 C  CA    . ARG   B 1 36  ? 33.70424 23.63656 0.04836   1.000 45.05684  ? 33  ARG   B CA    1 
ATOM   2117 C  C     . ARG   B 1 36  ? 33.35880 25.05857 -0.37332  1.000 47.18113  ? 33  ARG   B C     1 
ATOM   2118 O  O     . ARG   B 1 36  ? 32.17623 25.42085 -0.39788  1.000 46.66554  ? 33  ARG   B O     1 
ATOM   2119 C  CB    . ARG   B 1 36  ? 32.95808 23.27557 1.33341   1.000 42.38969  ? 33  ARG   B CB    1 
ATOM   2120 C  CG    . ARG   B 1 36  ? 33.04753 21.80890 1.70465   1.000 43.58033  ? 33  ARG   B CG    1 
ATOM   2121 C  CD    . ARG   B 1 36  ? 32.20581 20.95486 0.77521   1.000 43.35058  ? 33  ARG   B CD    1 
ATOM   2122 N  NE    . ARG   B 1 36  ? 32.21553 19.55096 1.17843   1.000 44.97476  ? 33  ARG   B NE    1 
ATOM   2123 C  CZ    . ARG   B 1 36  ? 31.19743 18.71605 0.99639   1.000 46.08991  ? 33  ARG   B CZ    1 
ATOM   2124 N  NH1   . ARG   B 1 36  ? 30.08148 19.14506 0.42063   1.000 45.35348  ? 33  ARG   B NH1   1 
ATOM   2125 N  NH2   . ARG   B 1 36  ? 31.28972 17.45529 1.39845   1.000 45.84112  ? 33  ARG   B NH2   1 
ATOM   2126 N  N     . GLU   B 1 37  ? 34.35932 25.86934 -0.70459  1.000 46.32745  ? 34  GLU   B N     1 
ATOM   2127 C  CA    . GLU   B 1 37  ? 34.14979 27.26894 -1.04331  1.000 43.64620  ? 34  GLU   B CA    1 
ATOM   2128 C  C     . GLU   B 1 37  ? 33.85965 27.38600 -2.53442  1.000 42.35081  ? 34  GLU   B C     1 
ATOM   2129 O  O     . GLU   B 1 37  ? 34.63018 26.88777 -3.36194  1.000 42.53140  ? 34  GLU   B O     1 
ATOM   2130 C  CB    . GLU   B 1 37  ? 35.37512 28.09699 -0.65954  1.000 47.20902  ? 34  GLU   B CB    1 
ATOM   2131 C  CG    . GLU   B 1 37  ? 35.16197 29.59870 -0.72525  1.000 50.58126  ? 34  GLU   B CG    1 
ATOM   2132 C  CD    . GLU   B 1 37  ? 36.42936 30.38534 -0.42474  1.000 54.12789  ? 34  GLU   B CD    1 
ATOM   2133 O  OE1   . GLU   B 1 37  ? 37.53169 29.90529 -0.77426  1.000 53.51742  ? 34  GLU   B OE1   1 
ATOM   2134 O  OE2   . GLU   B 1 37  ? 36.32054 31.48086 0.16876   1.000 52.44671  ? 34  GLU   B OE2   1 
ATOM   2135 N  N     . HIS   B 1 38  ? 32.74259 28.03038 -2.86936  1.000 41.39760  ? 35  HIS   B N     1 
ATOM   2136 C  CA    . HIS   B 1 38  ? 32.40597 28.30221 -4.26023  1.000 43.67415  ? 35  HIS   B CA    1 
ATOM   2137 C  C     . HIS   B 1 38  ? 33.54402 29.05574 -4.94100  1.000 47.47187  ? 35  HIS   B C     1 
ATOM   2138 O  O     . HIS   B 1 38  ? 34.27360 29.82533 -4.30731  1.000 49.69692  ? 35  HIS   B O     1 
ATOM   2139 C  CB    . HIS   B 1 38  ? 31.10852 29.11311 -4.32640  1.000 45.55959  ? 35  HIS   B CB    1 
ATOM   2140 C  CG    . HIS   B 1 38  ? 30.46460 29.13016 -5.67749  1.000 48.26831  ? 35  HIS   B CG    1 
ATOM   2141 N  ND1   . HIS   B 1 38  ? 30.84182 30.00707 -6.67202  1.000 50.71096  ? 35  HIS   B ND1   1 
ATOM   2142 C  CD2   . HIS   B 1 38  ? 29.45490 28.38862 -6.19183  1.000 47.81666  ? 35  HIS   B CD2   1 
ATOM   2143 C  CE1   . HIS   B 1 38  ? 30.09577 29.80141 -7.74304  1.000 51.62059  ? 35  HIS   B CE1   1 
ATOM   2144 N  NE2   . HIS   B 1 38  ? 29.24676 28.82438 -7.47786  1.000 50.99226  ? 35  HIS   B NE2   1 
ATOM   2145 N  N     B GLU   B 1 39  ? 33.69615 28.81577 -6.24650  0.310 46.84237  ? 36  GLU   B N     1 
ATOM   2146 N  N     C GLU   B 1 39  ? 33.69050 28.83903 -6.25216  0.690 46.66335  ? 36  GLU   B N     1 
ATOM   2147 C  CA    B GLU   B 1 39  ? 34.78710 29.43257 -6.99460  0.310 47.47848  ? 36  GLU   B CA    1 
ATOM   2148 C  CA    C GLU   B 1 39  ? 34.81176 29.43700 -6.97247  0.690 47.37184  ? 36  GLU   B CA    1 
ATOM   2149 C  C     B GLU   B 1 39  ? 34.71334 30.95277 -6.93176  0.310 48.19073  ? 36  GLU   B C     1 
ATOM   2150 C  C     C GLU   B 1 39  ? 34.72314 30.96027 -6.98259  0.690 48.31654  ? 36  GLU   B C     1 
ATOM   2151 O  O     B GLU   B 1 39  ? 35.73797 31.62662 -6.77238  0.310 49.29428  ? 36  GLU   B O     1 
ATOM   2152 O  O     C GLU   B 1 39  ? 35.74998 31.64624 -6.92557  0.690 49.90595  ? 36  GLU   B O     1 
ATOM   2153 C  CB    B GLU   B 1 39  ? 34.75999 28.95456 -8.44609  0.310 48.26418  ? 36  GLU   B CB    1 
ATOM   2154 C  CB    C GLU   B 1 39  ? 34.88297 28.88659 -8.39901  0.690 48.20233  ? 36  GLU   B CB    1 
ATOM   2155 C  CG    B GLU   B 1 39  ? 35.79921 29.61206 -9.33543  0.310 48.69289  ? 36  GLU   B CG    1 
ATOM   2156 C  CG    C GLU   B 1 39  ? 33.69251 29.23080 -9.27821  0.690 48.62180  ? 36  GLU   B CG    1 
ATOM   2157 N  N     . GLN   B 1 40  ? 33.50673 31.51056 -7.04348  1.000 46.86163  ? 37  GLN   B N     1 
ATOM   2158 C  CA    . GLN   B 1 40  ? 33.36185 32.96231 -7.00801  1.000 45.48211  ? 37  GLN   B CA    1 
ATOM   2159 C  C     . GLN   B 1 40  ? 33.57055 33.51428 -5.60249  1.000 43.70833  ? 37  GLN   B C     1 
ATOM   2160 O  O     . GLN   B 1 40  ? 34.00817 34.66026 -5.44738  1.000 43.58811  ? 37  GLN   B O     1 
ATOM   2161 C  CB    . GLN   B 1 40  ? 31.99265 33.36806 -7.55424  1.000 44.81442  ? 37  GLN   B CB    1 
ATOM   2162 C  CG    . GLN   B 1 40  ? 31.76503 32.95934 -9.00834  1.000 45.52278  ? 37  GLN   B CG    1 
ATOM   2163 C  CD    . GLN   B 1 40  ? 32.83590 33.49150 -9.94888  1.000 47.31799  ? 37  GLN   B CD    1 
ATOM   2164 O  OE1   . GLN   B 1 40  ? 33.34738 34.59786 -9.76901  1.000 49.71376  ? 37  GLN   B OE1   1 
ATOM   2165 N  NE2   . GLN   B 1 40  ? 33.18339 32.69916 -10.95630 1.000 45.69644  ? 37  GLN   B NE2   1 
ATOM   2166 N  N     . LEU   B 1 41  ? 33.26570 32.72359 -4.57075  1.000 44.26510  ? 38  LEU   B N     1 
ATOM   2167 C  CA    . LEU   B 1 41  ? 33.62878 33.11990 -3.21380  1.000 41.30212  ? 38  LEU   B CA    1 
ATOM   2168 C  C     . LEU   B 1 41  ? 35.14239 33.13176 -3.03880  1.000 43.25561  ? 38  LEU   B C     1 
ATOM   2169 O  O     . LEU   B 1 41  ? 35.69330 34.02337 -2.38242  1.000 43.29495  ? 38  LEU   B O     1 
ATOM   2170 C  CB    . LEU   B 1 41  ? 32.97826 32.18086 -2.19769  1.000 38.36689  ? 38  LEU   B CB    1 
ATOM   2171 C  CG    . LEU   B 1 41  ? 31.51053 32.40674 -1.83686  1.000 40.37830  ? 38  LEU   B CG    1 
ATOM   2172 C  CD1   . LEU   B 1 41  ? 31.01820 31.30084 -0.91763  1.000 38.02285  ? 38  LEU   B CD1   1 
ATOM   2173 C  CD2   . LEU   B 1 41  ? 31.34096 33.76332 -1.17368  1.000 41.33931  ? 38  LEU   B CD2   1 
ATOM   2174 N  N     . LYS   B 1 42  ? 35.82842 32.14790 -3.62347  1.000 48.30409  ? 39  LYS   B N     1 
ATOM   2175 C  CA    . LYS   B 1 42  ? 37.28624 32.11755 -3.57332  1.000 54.96193  ? 39  LYS   B CA    1 
ATOM   2176 C  C     . LYS   B 1 42  ? 37.88711 33.34301 -4.25297  1.000 54.54291  ? 39  LYS   B C     1 
ATOM   2177 O  O     . LYS   B 1 42  ? 38.85209 33.93232 -3.74959  1.000 55.68888  ? 39  LYS   B O     1 
ATOM   2178 C  CB    . LYS   B 1 42  ? 37.79211 30.82858 -4.22361  1.000 60.33181  ? 39  LYS   B CB    1 
ATOM   2179 C  CG    . LYS   B 1 42  ? 39.30181 30.70308 -4.33863  1.000 65.73011  ? 39  LYS   B CG    1 
ATOM   2180 C  CD    . LYS   B 1 42  ? 39.66362 29.57196 -5.29156  1.000 69.31270  ? 39  LYS   B CD    1 
ATOM   2181 C  CE    . LYS   B 1 42  ? 41.16945 29.42148 -5.45337  1.000 73.64113  ? 39  LYS   B CE    1 
ATOM   2182 N  NZ    . LYS   B 1 42  ? 41.79747 28.70830 -4.30588  1.000 75.47163  ? 39  LYS   B NZ    1 
ATOM   2183 N  N     . GLY   B 1 43  ? 37.32351 33.74884 -5.39247  1.000 50.79556  ? 40  GLY   B N     1 
ATOM   2184 C  CA    . GLY   B 1 43  ? 37.85331 34.90845 -6.09269  1.000 50.68160  ? 40  GLY   B CA    1 
ATOM   2185 C  C     . GLY   B 1 43  ? 37.62748 36.20206 -5.32969  1.000 50.44408  ? 40  GLY   B C     1 
ATOM   2186 O  O     . GLY   B 1 43  ? 38.54589 37.01209 -5.17245  1.000 48.44669  ? 40  GLY   B O     1 
ATOM   2187 N  N     . LEU   B 1 44  ? 36.39767 36.41167 -4.84891  1.000 49.98007  ? 41  LEU   B N     1 
ATOM   2188 C  CA    . LEU   B 1 44  ? 36.09541 37.61152 -4.07119  1.000 49.40629  ? 41  LEU   B CA    1 
ATOM   2189 C  C     . LEU   B 1 44  ? 36.99554 37.71188 -2.84728  1.000 46.44537  ? 41  LEU   B C     1 
ATOM   2190 O  O     . LEU   B 1 44  ? 37.48137 38.79709 -2.50929  1.000 44.95382  ? 41  LEU   B O     1 
ATOM   2191 C  CB    . LEU   B 1 44  ? 34.61996 37.60650 -3.65883  1.000 49.90719  ? 41  LEU   B CB    1 
ATOM   2192 C  CG    . LEU   B 1 44  ? 33.95510 38.85760 -3.06967  1.000 52.95242  ? 41  LEU   B CG    1 
ATOM   2193 C  CD1   . LEU   B 1 44  ? 32.44571 38.75910 -3.21653  1.000 50.29484  ? 41  LEU   B CD1   1 
ATOM   2194 C  CD2   . LEU   B 1 44  ? 34.30960 39.06882 -1.60199  1.000 54.99814  ? 41  LEU   B CD2   1 
ATOM   2195 N  N     . ARG   B 1 45  ? 37.22701 36.58833 -2.16888  1.000 46.87364  ? 42  ARG   B N     1 
ATOM   2196 C  CA    . ARG   B 1 45  ? 38.06580 36.60666 -0.97787  1.000 47.93042  ? 42  ARG   B CA    1 
ATOM   2197 C  C     . ARG   B 1 45  ? 39.49677 37.00124 -1.31711  1.000 51.73541  ? 42  ARG   B C     1 
ATOM   2198 O  O     . ARG   B 1 45  ? 40.11081 37.80354 -0.60512  1.000 49.81755  ? 42  ARG   B O     1 
ATOM   2199 C  CB    . ARG   B 1 45  ? 38.03016 35.23931 -0.29424  1.000 46.67475  ? 42  ARG   B CB    1 
ATOM   2200 C  CG    . ARG   B 1 45  ? 39.04075 35.08329 0.83296   1.000 47.94753  ? 42  ARG   B CG    1 
ATOM   2201 C  CD    . ARG   B 1 45  ? 38.88228 33.74934 1.54671   1.000 46.94378  ? 42  ARG   B CD    1 
ATOM   2202 N  NE    . ARG   B 1 45  ? 38.92916 32.62289 0.61794   1.000 47.74028  ? 42  ARG   B NE    1 
ATOM   2203 C  CZ    . ARG   B 1 45  ? 40.04899 32.03853 0.20475   1.000 48.30945  ? 42  ARG   B CZ    1 
ATOM   2204 N  NH1   . ARG   B 1 45  ? 41.22455 32.47530 0.63689   1.000 48.35537  ? 42  ARG   B NH1   1 
ATOM   2205 N  NH2   . ARG   B 1 45  ? 39.99263 31.01878 -0.64297  1.000 46.65315  ? 42  ARG   B NH2   1 
ATOM   2206 N  N     . GLU   B 1 46  ? 40.03659 36.46977 -2.41729  1.000 52.30881  ? 43  GLU   B N     1 
ATOM   2207 C  CA    . GLU   B 1 46  ? 41.45053 36.67794 -2.70835  1.000 54.26122  ? 43  GLU   B CA    1 
ATOM   2208 C  C     . GLU   B 1 46  ? 41.73549 38.09327 -3.19518  1.000 53.67703  ? 43  GLU   B C     1 
ATOM   2209 O  O     . GLU   B 1 46  ? 42.84385 38.59773 -2.98899  1.000 52.75113  ? 43  GLU   B O     1 
ATOM   2210 C  CB    . GLU   B 1 46  ? 41.93594 35.63994 -3.71929  1.000 55.80236  ? 43  GLU   B CB    1 
ATOM   2211 C  CG    . GLU   B 1 46  ? 42.29359 34.30789 -3.07249  1.000 57.97877  ? 43  GLU   B CG    1 
ATOM   2212 C  CD    . GLU   B 1 46  ? 42.54631 33.20160 -4.07970  1.000 61.49121  ? 43  GLU   B CD    1 
ATOM   2213 O  OE1   . GLU   B 1 46  ? 42.25494 33.40329 -5.27709  1.000 63.24896  ? 43  GLU   B OE1   1 
ATOM   2214 O  OE2   . GLU   B 1 46  ? 43.03431 32.12603 -3.66969  1.000 61.98752  ? 43  GLU   B OE2   1 
ATOM   2215 N  N     . VAL   B 1 47  ? 40.76557 38.75683 -3.82876  1.000 56.57977  ? 44  VAL   B N     1 
ATOM   2216 C  CA    . VAL   B 1 47  ? 40.96416 40.16807 -4.14852  1.000 59.27363  ? 44  VAL   B CA    1 
ATOM   2217 C  C     . VAL   B 1 47  ? 40.79704 41.01945 -2.89513  1.000 59.56067  ? 44  VAL   B C     1 
ATOM   2218 O  O     . VAL   B 1 47  ? 41.50338 42.01830 -2.70727  1.000 62.21316  ? 44  VAL   B O     1 
ATOM   2219 C  CB    . VAL   B 1 47  ? 40.02117 40.62200 -5.28281  1.000 58.86108  ? 44  VAL   B CB    1 
ATOM   2220 C  CG1   . VAL   B 1 47  ? 40.19759 39.73960 -6.50687  1.000 61.36204  ? 44  VAL   B CG1   1 
ATOM   2221 C  CG2   . VAL   B 1 47  ? 38.56689 40.63873 -4.83306  1.000 57.31070  ? 44  VAL   B CG2   1 
ATOM   2222 N  N     . THR   B 1 48  ? 39.88139 40.62396 -2.00506  1.000 52.26201  ? 45  THR   B N     1 
ATOM   2223 C  CA    . THR   B 1 48  ? 39.65300 41.39091 -0.78582  1.000 50.78222  ? 45  THR   B CA    1 
ATOM   2224 C  C     . THR   B 1 48  ? 40.86473 41.34886 0.13250   1.000 53.51362  ? 45  THR   B C     1 
ATOM   2225 O  O     . THR   B 1 48  ? 41.16023 42.33591 0.81545   1.000 54.98927  ? 45  THR   B O     1 
ATOM   2226 C  CB    . THR   B 1 48  ? 38.41735 40.86081 -0.05627  1.000 45.73905  ? 45  THR   B CB    1 
ATOM   2227 O  OG1   . THR   B 1 48  ? 37.28726 40.90932 -0.93507  1.000 46.76767  ? 45  THR   B OG1   1 
ATOM   2228 C  CG2   . THR   B 1 48  ? 38.12437 41.69169 1.18850   1.000 40.73469  ? 45  THR   B CG2   1 
ATOM   2229 N  N     . GLU   B 1 49  ? 41.58335 40.22326 0.15312   1.000 55.47477  ? 46  GLU   B N     1 
ATOM   2230 C  CA    . GLU   B 1 49  ? 42.74163 40.08804 1.02817   1.000 58.51534  ? 46  GLU   B CA    1 
ATOM   2231 C  C     . GLU   B 1 49  ? 43.82431 41.11190 0.71563   1.000 61.38183  ? 46  GLU   B C     1 
ATOM   2232 O  O     . GLU   B 1 49  ? 44.64955 41.40930 1.58632   1.000 63.05423  ? 46  GLU   B O     1 
ATOM   2233 C  CB    . GLU   B 1 49  ? 43.30469 38.66928 0.92957   1.000 60.93810  ? 46  GLU   B CB    1 
ATOM   2234 C  CG    . GLU   B 1 49  ? 42.37940 37.60792 1.50854   1.000 66.80846  ? 46  GLU   B CG    1 
ATOM   2235 C  CD    . GLU   B 1 49  ? 42.80091 36.19352 1.15095   1.000 74.79778  ? 46  GLU   B CD    1 
ATOM   2236 O  OE1   . GLU   B 1 49  ? 42.41298 35.25431 1.88137   1.000 75.37034  ? 46  GLU   B OE1   1 
ATOM   2237 O  OE2   . GLU   B 1 49  ? 43.51830 36.01798 0.14023   1.000 78.46493  ? 46  GLU   B OE2   1 
ATOM   2238 N  N     . LYS   B 1 50  ? 43.83258 41.66593 -0.49514  1.000 61.54243  ? 47  LYS   B N     1 
ATOM   2239 C  CA    . LYS   B 1 50  ? 44.77458 42.71145 -0.86812  1.000 60.59598  ? 47  LYS   B CA    1 
ATOM   2240 C  C     . LYS   B 1 50  ? 44.23856 44.11210 -0.60055  1.000 57.54127  ? 47  LYS   B C     1 
ATOM   2241 O  O     . LYS   B 1 50  ? 44.97086 45.08718 -0.79214  1.000 57.96651  ? 47  LYS   B O     1 
ATOM   2242 C  CB    . LYS   B 1 50  ? 45.15263 42.57632 -2.34616  1.000 64.42229  ? 47  LYS   B CB    1 
ATOM   2243 C  CG    . LYS   B 1 50  ? 45.63915 41.18870 -2.73457  1.000 65.81146  ? 47  LYS   B CG    1 
ATOM   2244 C  CD    . LYS   B 1 50  ? 46.78958 40.73635 -1.84830  1.000 68.49588  ? 47  LYS   B CD    1 
ATOM   2245 N  N     . HIS   B 1 51  ? 42.98812 44.23577 -0.16697  1.000 56.90212  ? 48  HIS   B N     1 
ATOM   2246 C  CA    . HIS   B 1 51  ? 42.41991 45.52962 0.17230   1.000 55.62666  ? 48  HIS   B CA    1 
ATOM   2247 C  C     . HIS   B 1 51  ? 42.89193 45.96572 1.55808   1.000 56.03416  ? 48  HIS   B C     1 
ATOM   2248 O  O     . HIS   B 1 51  ? 43.23738 45.14428 2.41191   1.000 54.22861  ? 48  HIS   B O     1 
ATOM   2249 C  CB    . HIS   B 1 51  ? 40.89267 45.46797 0.11799   1.000 54.46684  ? 48  HIS   B CB    1 
ATOM   2250 C  CG    . HIS   B 1 51  ? 40.22601 46.80595 0.19469   1.000 56.55230  ? 48  HIS   B CG    1 
ATOM   2251 N  ND1   . HIS   B 1 51  ? 39.77953 47.34936 1.38023   1.000 56.06621  ? 48  HIS   B ND1   1 
ATOM   2252 C  CD2   . HIS   B 1 51  ? 39.92032 47.70509 -0.77023  1.000 57.10618  ? 48  HIS   B CD2   1 
ATOM   2253 C  CE1   . HIS   B 1 51  ? 39.23130 48.52778 1.14279   1.000 56.65376  ? 48  HIS   B CE1   1 
ATOM   2254 N  NE2   . HIS   B 1 51  ? 39.30455 48.76730 -0.15414  1.000 57.65725  ? 48  HIS   B NE2   1 
ATOM   2255 N  N     . GLU   B 1 52  ? 42.90121 47.28445 1.77632   1.000 58.50956  ? 49  GLU   B N     1 
ATOM   2256 C  CA    . GLU   B 1 52  ? 43.45699 47.82207 3.01574   1.000 61.03959  ? 49  GLU   B CA    1 
ATOM   2257 C  C     . GLU   B 1 52  ? 42.65128 47.39979 4.24075   1.000 59.10026  ? 49  GLU   B C     1 
ATOM   2258 O  O     . GLU   B 1 52  ? 43.22246 47.23573 5.32438   1.000 55.82375  ? 49  GLU   B O     1 
ATOM   2259 C  CB    . GLU   B 1 52  ? 43.54244 49.34718 2.94041   1.000 66.15532  ? 49  GLU   B CB    1 
ATOM   2260 C  CG    . GLU   B 1 52  ? 42.19883 50.04164 2.82204   1.000 71.10059  ? 49  GLU   B CG    1 
ATOM   2261 C  CD    . GLU   B 1 52  ? 42.25462 51.49250 3.25687   1.000 76.68668  ? 49  GLU   B CD    1 
ATOM   2262 O  OE1   . GLU   B 1 52  ? 42.25224 52.38161 2.37845   1.000 78.05559  ? 49  GLU   B OE1   1 
ATOM   2263 O  OE2   . GLU   B 1 52  ? 42.30896 51.74105 4.48097   1.000 77.12366  ? 49  GLU   B OE2   1 
ATOM   2264 N  N     . TRP   B 1 53  ? 41.33600 47.21928 4.09665   1.000 60.05435  ? 50  TRP   B N     1 
ATOM   2265 C  CA    . TRP   B 1 53  ? 40.46612 46.82154 5.19828   1.000 59.20996  ? 50  TRP   B CA    1 
ATOM   2266 C  C     . TRP   B 1 53  ? 40.17952 45.32278 5.20089   1.000 54.17818  ? 50  TRP   B C     1 
ATOM   2267 O  O     . TRP   B 1 53  ? 39.08434 44.90271 5.59022   1.000 54.87964  ? 50  TRP   B O     1 
ATOM   2268 C  CB    . TRP   B 1 53  ? 39.15181 47.60389 5.15353   1.000 59.70770  ? 50  TRP   B CB    1 
ATOM   2269 C  CG    . TRP   B 1 53  ? 39.26936 49.03757 5.57382   1.000 65.12694  ? 50  TRP   B CG    1 
ATOM   2270 C  CD1   . TRP   B 1 53  ? 39.33600 50.12853 4.75653   1.000 67.40703  ? 50  TRP   B CD1   1 
ATOM   2271 C  CD2   . TRP   B 1 53  ? 39.32607 49.53831 6.91637   1.000 68.90332  ? 50  TRP   B CD2   1 
ATOM   2272 N  NE1   . TRP   B 1 53  ? 39.43369 51.27656 5.50532   1.000 68.70013  ? 50  TRP   B NE1   1 
ATOM   2273 C  CE2   . TRP   B 1 53  ? 39.42970 50.94171 6.83403   1.000 70.56043  ? 50  TRP   B CE2   1 
ATOM   2274 C  CE3   . TRP   B 1 53  ? 39.30133 48.93611 8.17935   1.000 70.03147  ? 50  TRP   B CE3   1 
ATOM   2275 C  CZ2   . TRP   B 1 53  ? 39.50904 51.75208 7.96526   1.000 72.73486  ? 50  TRP   B CZ2   1 
ATOM   2276 C  CZ3   . TRP   B 1 53  ? 39.38050 49.74233 9.30155   1.000 71.21722  ? 50  TRP   B CZ3   1 
ATOM   2277 C  CH2   . TRP   B 1 53  ? 39.48278 51.13515 9.18670   1.000 73.15382  ? 50  TRP   B CH2   1 
ATOM   2278 N  N     . SER   B 1 54  ? 41.14573 44.50455 4.77713   1.000 51.50139  ? 51  SER   B N     1 
ATOM   2279 C  CA    . SER   B 1 54  ? 40.91565 43.06684 4.67422   1.000 50.23390  ? 51  SER   B CA    1 
ATOM   2280 C  C     . SER   B 1 54  ? 40.65906 42.41913 6.02867   1.000 50.13223  ? 51  SER   B C     1 
ATOM   2281 O  O     . SER   B 1 54  ? 40.12923 41.30323 6.07866   1.000 47.64999  ? 51  SER   B O     1 
ATOM   2282 C  CB    . SER   B 1 54  ? 42.10749 42.38911 3.99593   1.000 48.64298  ? 51  SER   B CB    1 
ATOM   2283 O  OG    . SER   B 1 54  ? 43.25939 42.45321 4.81694   1.000 50.54099  ? 51  SER   B OG    1 
ATOM   2284 N  N     . THR   B 1 55  ? 41.02280 43.08932 7.12501   1.000 50.15542  ? 52  THR   B N     1 
ATOM   2285 C  CA    . THR   B 1 55  ? 40.78133 42.52959 8.45044   1.000 50.16550  ? 52  THR   B CA    1 
ATOM   2286 C  C     . THR   B 1 55  ? 39.29230 42.37020 8.73528   1.000 45.10844  ? 52  THR   B C     1 
ATOM   2287 O  O     . THR   B 1 55  ? 38.90293 41.51377 9.53682   1.000 46.95885  ? 52  THR   B O     1 
ATOM   2288 C  CB    . THR   B 1 55  ? 41.42838 43.41252 9.51671   1.000 56.31107  ? 52  THR   B CB    1 
ATOM   2289 O  OG1   . THR   B 1 55  ? 40.72763 44.66021 9.59521   1.000 60.31541  ? 52  THR   B OG1   1 
ATOM   2290 C  CG2   . THR   B 1 55  ? 42.87891 43.68305 9.16321   1.000 61.27990  ? 52  THR   B CG2   1 
ATOM   2291 N  N     . ALA   B 1 56  ? 38.44861 43.17663 8.09193   1.000 38.86746  ? 53  ALA   B N     1 
ATOM   2292 C  CA    . ALA   B 1 56  ? 37.00767 43.11598 8.30568   1.000 39.76002  ? 53  ALA   B CA    1 
ATOM   2293 C  C     . ALA   B 1 56  ? 36.33677 41.96959 7.56018   1.000 39.71485  ? 53  ALA   B C     1 
ATOM   2294 O  O     . ALA   B 1 56  ? 35.13623 41.74528 7.75602   1.000 35.80505  ? 53  ALA   B O     1 
ATOM   2295 C  CB    . ALA   B 1 56  ? 36.36185 44.43933 7.88766   1.000 37.53149  ? 53  ALA   B CB    1 
ATOM   2296 N  N     . LEU   B 1 57  ? 37.07455 41.24537 6.72198   1.000 38.95023  ? 54  LEU   B N     1 
ATOM   2297 C  CA    . LEU   B 1 57  ? 36.48247 40.20597 5.89059   1.000 38.41222  ? 54  LEU   B CA    1 
ATOM   2298 C  C     . LEU   B 1 57  ? 35.97619 39.04332 6.73941   1.000 38.18881  ? 54  LEU   B C     1 
ATOM   2299 O  O     . LEU   B 1 57  ? 36.68398 38.55236 7.62594   1.000 37.34540  ? 54  LEU   B O     1 
ATOM   2300 C  CB    . LEU   B 1 57  ? 37.51264 39.71315 4.87690   1.000 43.34882  ? 54  LEU   B CB    1 
ATOM   2301 C  CG    . LEU   B 1 57  ? 37.14569 38.54007 3.96754   1.000 44.72941  ? 54  LEU   B CG    1 
ATOM   2302 C  CD1   . LEU   B 1 57  ? 35.95526 38.88948 3.08131   1.000 41.59633  ? 54  LEU   B CD1   1 
ATOM   2303 C  CD2   . LEU   B 1 57  ? 38.35413 38.12932 3.13157   1.000 45.64631  ? 54  LEU   B CD2   1 
ATOM   2304 N  N     . VAL   B 1 58  ? 34.75041 38.60425 6.46439   1.000 39.46120  ? 55  VAL   B N     1 
ATOM   2305 C  CA    . VAL   B 1 58  ? 34.18940 37.41712 7.10539   1.000 38.79349  ? 55  VAL   B CA    1 
ATOM   2306 C  C     . VAL   B 1 58  ? 34.99682 36.20110 6.65664   1.000 39.55177  ? 55  VAL   B C     1 
ATOM   2307 O  O     . VAL   B 1 58  ? 35.11839 35.95633 5.44894   1.000 40.54357  ? 55  VAL   B O     1 
ATOM   2308 C  CB    . VAL   B 1 58  ? 32.70019 37.24796 6.77184   1.000 33.83814  ? 55  VAL   B CB    1 
ATOM   2309 C  CG1   . VAL   B 1 58  ? 32.23619 35.82905 7.11062   1.000 28.09581  ? 55  VAL   B CG1   1 
ATOM   2310 C  CG2   . VAL   B 1 58  ? 31.87750 38.28156 7.51837   1.000 34.36851  ? 55  VAL   B CG2   1 
ATOM   2311 N  N     . PRO   B 1 59  ? 35.55663 35.42546 7.58251   1.000 37.11631  ? 56  PRO   B N     1 
ATOM   2312 C  CA    . PRO   B 1 59  ? 36.43065 34.31087 7.18651   1.000 38.77230  ? 56  PRO   B CA    1 
ATOM   2313 C  C     . PRO   B 1 59  ? 35.64829 33.17939 6.53469   1.000 41.52325  ? 56  PRO   B C     1 
ATOM   2314 O  O     . PRO   B 1 59  ? 34.41619 33.11390 6.57966   1.000 38.87235  ? 56  PRO   B O     1 
ATOM   2315 C  CB    . PRO   B 1 59  ? 37.06456 33.86791 8.50955   1.000 37.96197  ? 56  PRO   B CB    1 
ATOM   2316 C  CG    . PRO   B 1 59  ? 36.08543 34.28960 9.55437   1.000 36.27951  ? 56  PRO   B CG    1 
ATOM   2317 C  CD    . PRO   B 1 59  ? 35.44838 35.55775 9.04372   1.000 34.72513  ? 56  PRO   B CD    1 
ATOM   2318 N  N     . ALA   B 1 60  ? 36.40741 32.26026 5.92695   1.000 40.89666  ? 57  ALA   B N     1 
ATOM   2319 C  CA    . ALA   B 1 60  ? 35.80645 31.21879 5.09892   1.000 39.28672  ? 57  ALA   B CA    1 
ATOM   2320 C  C     . ALA   B 1 60  ? 35.07206 30.17855 5.93674   1.000 38.65672  ? 57  ALA   B C     1 
ATOM   2321 O  O     . ALA   B 1 60  ? 34.03824 29.65290 5.50805   1.000 36.97072  ? 57  ALA   B O     1 
ATOM   2322 C  CB    . ALA   B 1 60  ? 36.87708 30.54861 4.23970   1.000 40.35018  ? 57  ALA   B CB    1 
ATOM   2323 N  N     . ASP   B 1 61  ? 35.59315 29.85205 7.12298   1.000 36.46605  ? 58  ASP   B N     1 
ATOM   2324 C  CA    . ASP   B 1 61  ? 34.93118 28.84754 7.95150   1.000 38.64005  ? 58  ASP   B CA    1 
ATOM   2325 C  C     . ASP   B 1 61  ? 33.62742 29.38671 8.52363   1.000 40.56802  ? 58  ASP   B C     1 
ATOM   2326 O  O     . ASP   B 1 61  ? 32.63633 28.65242 8.62338   1.000 44.43810  ? 58  ASP   B O     1 
ATOM   2327 C  CB    . ASP   B 1 61  ? 35.86356 28.36871 9.06998   1.000 40.03937  ? 58  ASP   B CB    1 
ATOM   2328 C  CG    . ASP   B 1 61  ? 36.16877 29.45435 10.09576  1.000 43.85818  ? 58  ASP   B CG    1 
ATOM   2329 O  OD1   . ASP   B 1 61  ? 36.30180 30.63760 9.70396   1.000 44.12513  ? 58  ASP   B OD1   1 
ATOM   2330 O  OD2   . ASP   B 1 61  ? 36.27841 29.11983 11.29735  1.000 41.90288  ? 58  ASP   B OD2   1 
ATOM   2331 N  N     . GLU   B 1 62  ? 33.60425 30.67070 8.89288   1.000 38.24429  ? 59  GLU   B N     1 
ATOM   2332 C  CA    . GLU   B 1 62  ? 32.35637 31.28714 9.32891   1.000 38.56276  ? 59  GLU   B CA    1 
ATOM   2333 C  C     . GLU   B 1 62  ? 31.36464 31.39560 8.17643   1.000 37.62446  ? 59  GLU   B C     1 
ATOM   2334 O  O     . GLU   B 1 62  ? 30.16124 31.18732 8.36650   1.000 37.47878  ? 59  GLU   B O     1 
ATOM   2335 C  CB    . GLU   B 1 62  ? 32.62894 32.66485 9.92921   1.000 35.13564  ? 59  GLU   B CB    1 
ATOM   2336 C  CG    . GLU   B 1 62  ? 31.36131 33.40424 10.32880  1.000 36.90318  ? 59  GLU   B CG    1 
ATOM   2337 C  CD    . GLU   B 1 62  ? 31.62828 34.82734 10.77144  1.000 37.75070  ? 59  GLU   B CD    1 
ATOM   2338 O  OE1   . GLU   B 1 62  ? 32.72199 35.08815 11.31859  1.000 36.02976  ? 59  GLU   B OE1   1 
ATOM   2339 O  OE2   . GLU   B 1 62  ? 30.74431 35.68505 10.56343  1.000 36.98484  ? 59  GLU   B OE2   1 
ATOM   2340 N  N     . GLY   B 1 63  ? 31.85321 31.71415 6.97390   1.000 37.61067  ? 60  GLY   B N     1 
ATOM   2341 C  CA    . GLY   B 1 63  ? 30.96406 31.82898 5.82669   1.000 39.24878  ? 60  GLY   B CA    1 
ATOM   2342 C  C     . GLY   B 1 63  ? 30.19249 30.55094 5.55258   1.000 41.03887  ? 60  GLY   B C     1 
ATOM   2343 O  O     . GLY   B 1 63  ? 28.98181 30.58050 5.31829   1.000 39.72881  ? 60  GLY   B O     1 
ATOM   2344 N  N     . LEU   B 1 64  ? 30.88584 29.40703 5.57843   1.000 38.90758  ? 61  LEU   B N     1 
ATOM   2345 C  CA    . LEU   B 1 64  ? 30.20029 28.12777 5.41796   1.000 39.83036  ? 61  LEU   B CA    1 
ATOM   2346 C  C     . LEU   B 1 64  ? 29.21580 27.87130 6.55004   1.000 37.76181  ? 61  LEU   B C     1 
ATOM   2347 O  O     . LEU   B 1 64  ? 28.21713 27.16854 6.35640   1.000 34.46571  ? 61  LEU   B O     1 
ATOM   2348 C  CB    . LEU   B 1 64  ? 31.21494 26.98908 5.34038   1.000 37.77009  ? 61  LEU   B CB    1 
ATOM   2349 C  CG    . LEU   B 1 64  ? 31.85871 26.74435 3.97673   1.000 43.25434  ? 61  LEU   B CG    1 
ATOM   2350 C  CD1   . LEU   B 1 64  ? 32.90044 25.66064 4.09486   1.000 47.08043  ? 61  LEU   B CD1   1 
ATOM   2351 C  CD2   . LEU   B 1 64  ? 30.80585 26.34869 2.95719   1.000 44.40288  ? 61  LEU   B CD2   1 
ATOM   2352 N  N     . PHE   B 1 65  ? 29.48577 28.41835 7.73694   1.000 37.23684  ? 62  PHE   B N     1 
ATOM   2353 C  CA    . PHE   B 1 65  ? 28.56088 28.26112 8.85411   1.000 39.22203  ? 62  PHE   B CA    1 
ATOM   2354 C  C     . PHE   B 1 65  ? 27.28032 29.05695 8.62726   1.000 38.06830  ? 62  PHE   B C     1 
ATOM   2355 O  O     . PHE   B 1 65  ? 26.18257 28.57168 8.92041   1.000 38.45432  ? 62  PHE   B O     1 
ATOM   2356 C  CB    . PHE   B 1 65  ? 29.24698 28.68179 10.15249  1.000 40.63715  ? 62  PHE   B CB    1 
ATOM   2357 C  CG    . PHE   B 1 65  ? 28.33713 28.70718 11.34364  1.000 45.24381  ? 62  PHE   B CG    1 
ATOM   2358 C  CD1   . PHE   B 1 65  ? 27.72700 27.54916 11.78977  1.000 48.24175  ? 62  PHE   B CD1   1 
ATOM   2359 C  CD2   . PHE   B 1 65  ? 28.10772 29.88877 12.02921  1.000 50.13201  ? 62  PHE   B CD2   1 
ATOM   2360 C  CE1   . PHE   B 1 65  ? 26.89545 27.56864 12.88845  1.000 51.69914  ? 62  PHE   B CE1   1 
ATOM   2361 C  CE2   . PHE   B 1 65  ? 27.27914 29.91676 13.13364  1.000 51.15859  ? 62  PHE   B CE2   1 
ATOM   2362 C  CZ    . PHE   B 1 65  ? 26.67148 28.75460 13.56284  1.000 53.25863  ? 62  PHE   B CZ    1 
ATOM   2363 N  N     . LEU   B 1 66  ? 27.39997 30.28084 8.10885   1.000 37.69270  ? 63  LEU   B N     1 
ATOM   2364 C  CA    . LEU   B 1 66  ? 26.21642 31.04800 7.73513   1.000 37.96806  ? 63  LEU   B CA    1 
ATOM   2365 C  C     . LEU   B 1 66  ? 25.42113 30.32376 6.65706   1.000 40.82348  ? 63  LEU   B C     1 
ATOM   2366 O  O     . LEU   B 1 66  ? 24.18815 30.25439 6.71663   1.000 39.19159  ? 63  LEU   B O     1 
ATOM   2367 C  CB    . LEU   B 1 66  ? 26.62342 32.43985 7.25008   1.000 36.02243  ? 63  LEU   B CB    1 
ATOM   2368 C  CG    . LEU   B 1 66  ? 27.58601 33.23801 8.13028   1.000 33.73697  ? 63  LEU   B CG    1 
ATOM   2369 C  CD1   . LEU   B 1 66  ? 27.89540 34.58703 7.48647   1.000 32.83640  ? 63  LEU   B CD1   1 
ATOM   2370 C  CD2   . LEU   B 1 66  ? 27.02637 33.41834 9.53784   1.000 33.50010  ? 63  LEU   B CD2   1 
ATOM   2371 N  N     . SER   B 1 67  ? 26.12009 29.78224 5.65580   1.000 40.31973  ? 64  SER   B N     1 
ATOM   2372 C  CA    . SER   B 1 67  ? 25.45174 29.04183 4.58953   1.000 41.09286  ? 64  SER   B CA    1 
ATOM   2373 C  C     . SER   B 1 67  ? 24.67295 27.85590 5.14310   1.000 39.57650  ? 64  SER   B C     1 
ATOM   2374 O  O     . SER   B 1 67  ? 23.54472 27.58994 4.71211   1.000 36.16297  ? 64  SER   B O     1 
ATOM   2375 C  CB    . SER   B 1 67  ? 26.47958 28.57334 3.55817   1.000 43.59144  ? 64  SER   B CB    1 
ATOM   2376 O  OG    . SER   B 1 67  ? 25.86901 27.80079 2.53986   1.000 50.96470  ? 64  SER   B OG    1 
ATOM   2377 N  N     . MET   B 1 68  ? 25.25928 27.13179 6.10104   1.000 37.06906  ? 65  MET   B N     1 
ATOM   2378 C  CA    . MET   B 1 68  ? 24.57343 25.99359 6.70355   1.000 36.91554  ? 65  MET   B CA    1 
ATOM   2379 C  C     . MET   B 1 68  ? 23.32108 26.43704 7.45315   1.000 37.66605  ? 65  MET   B C     1 
ATOM   2380 O  O     . MET   B 1 68  ? 22.25972 25.81576 7.33187   1.000 36.54873  ? 65  MET   B O     1 
ATOM   2381 C  CB    . MET   B 1 68  ? 25.52393 25.24940 7.63986   1.000 36.72500  ? 65  MET   B CB    1 
ATOM   2382 C  CG    . MET   B 1 68  ? 24.89655 24.05756 8.33895   1.000 36.79814  ? 65  MET   B CG    1 
ATOM   2383 S  SD    . MET   B 1 68  ? 24.46867 22.72716 7.19811   1.000 39.74163  ? 65  MET   B SD    1 
ATOM   2384 C  CE    . MET   B 1 68  ? 26.09176 22.25596 6.60297   1.000 38.00217  ? 65  MET   B CE    1 
ATOM   2385 N  N     . LEU   B 1 69  ? 23.43290 27.50891 8.24511   1.000 38.58904  ? 66  LEU   B N     1 
ATOM   2386 C  CA    . LEU   B 1 69  ? 22.28189 28.00112 8.99804   1.000 40.66308  ? 66  LEU   B CA    1 
ATOM   2387 C  C     . LEU   B 1 69  ? 21.13954 28.39310 8.07056   1.000 39.89667  ? 66  LEU   B C     1 
ATOM   2388 O  O     . LEU   B 1 69  ? 19.97516 28.06306 8.33255   1.000 37.42475  ? 66  LEU   B O     1 
ATOM   2389 C  CB    . LEU   B 1 69  ? 22.68673 29.19446 9.86497   1.000 44.78821  ? 66  LEU   B CB    1 
ATOM   2390 C  CG    . LEU   B 1 69  ? 23.62202 28.93656 11.04306  1.000 53.69074  ? 66  LEU   B CG    1 
ATOM   2391 C  CD1   . LEU   B 1 69  ? 23.89749 30.22793 11.79496  1.000 56.35313  ? 66  LEU   B CD1   1 
ATOM   2392 C  CD2   . LEU   B 1 69  ? 23.01836 27.90439 11.96884  1.000 56.09030  ? 66  LEU   B CD2   1 
ATOM   2393 N  N     . LEU   B 1 70  ? 21.45409 29.10838 6.98681   1.000 36.11214  ? 67  LEU   B N     1 
ATOM   2394 C  CA    . LEU   B 1 70  ? 20.42121 29.54215 6.05348   1.000 38.23166  ? 67  LEU   B CA    1 
ATOM   2395 C  C     . LEU   B 1 70  ? 19.65510 28.35772 5.48337   1.000 40.42774  ? 67  LEU   B C     1 
ATOM   2396 O  O     . LEU   B 1 70  ? 18.42425 28.40213 5.37204   1.000 40.51055  ? 67  LEU   B O     1 
ATOM   2397 C  CB    . LEU   B 1 70  ? 21.04709 30.36182 4.92772   1.000 38.84673  ? 67  LEU   B CB    1 
ATOM   2398 C  CG    . LEU   B 1 70  ? 21.49677 31.77406 5.28780   1.000 37.79616  ? 67  LEU   B CG    1 
ATOM   2399 C  CD1   . LEU   B 1 70  ? 22.41964 32.31297 4.21503   1.000 39.50428  ? 67  LEU   B CD1   1 
ATOM   2400 C  CD2   . LEU   B 1 70  ? 20.28634 32.67370 5.45288   1.000 37.79341  ? 67  LEU   B CD2   1 
ATOM   2401 N  N     . LYS   B 1 71  ? 20.36452 27.28568 5.12275   1.000 41.12935  ? 68  LYS   B N     1 
ATOM   2402 C  CA    . LYS   B 1 71  ? 19.70295 26.14816 4.49441   1.000 43.16185  ? 68  LYS   B CA    1 
ATOM   2403 C  C     . LYS   B 1 71  ? 18.92684 25.31883 5.51046   1.000 44.22766  ? 68  LYS   B C     1 
ATOM   2404 O  O     . LYS   B 1 71  ? 17.81531 24.85894 5.22178   1.000 42.20701  ? 68  LYS   B O     1 
ATOM   2405 C  CB    . LYS   B 1 71  ? 20.73112 25.28911 3.76490   1.000 44.55633  ? 68  LYS   B CB    1 
ATOM   2406 C  CG    . LYS   B 1 71  ? 21.32267 25.96437 2.54424   1.000 45.98120  ? 68  LYS   B CG    1 
ATOM   2407 C  CD    . LYS   B 1 71  ? 22.30019 25.05578 1.83299   1.000 49.46242  ? 68  LYS   B CD    1 
ATOM   2408 C  CE    . LYS   B 1 71  ? 22.78891 25.68698 0.54607   1.000 53.61343  ? 68  LYS   B CE    1 
ATOM   2409 N  NZ    . LYS   B 1 71  ? 23.91315 24.92044 -0.06000  1.000 59.16312  ? 68  LYS   B NZ    1 
ATOM   2410 N  N     . LEU   B 1 72  ? 19.49087 25.11850 6.70500   1.000 42.09922  ? 69  LEU   B N     1 
ATOM   2411 C  CA    . LEU   B 1 72  ? 18.80859 24.31079 7.71259   1.000 41.17934  ? 69  LEU   B CA    1 
ATOM   2412 C  C     . LEU   B 1 72  ? 17.47693 24.92993 8.12026   1.000 40.58376  ? 69  LEU   B C     1 
ATOM   2413 O  O     . LEU   B 1 72  ? 16.50585 24.21005 8.38321   1.000 42.55168  ? 69  LEU   B O     1 
ATOM   2414 C  CB    . LEU   B 1 72  ? 19.70787 24.11677 8.93419   1.000 39.58975  ? 69  LEU   B CB    1 
ATOM   2415 C  CG    . LEU   B 1 72  ? 20.82531 23.07940 8.77996   1.000 37.49044  ? 69  LEU   B CG    1 
ATOM   2416 C  CD1   . LEU   B 1 72  ? 21.67206 23.01001 10.03962  1.000 36.62619  ? 69  LEU   B CD1   1 
ATOM   2417 C  CD2   . LEU   B 1 72  ? 20.24068 21.71352 8.44446   1.000 36.74755  ? 69  LEU   B CD2   1 
ATOM   2418 N  N     . MET   B 1 73  ? 17.40675 26.25837 8.17797   1.000 39.98391  ? 70  MET   B N     1 
ATOM   2419 C  CA    . MET   B 1 73  ? 16.17219 26.93847 8.54645   1.000 41.75718  ? 70  MET   B CA    1 
ATOM   2420 C  C     . MET   B 1 73  ? 15.31869 27.30360 7.34052   1.000 43.56852  ? 70  MET   B C     1 
ATOM   2421 O  O     . MET   B 1 73  ? 14.25166 27.90211 7.51663   1.000 44.35557  ? 70  MET   B O     1 
ATOM   2422 C  CB    . MET   B 1 73  ? 16.47299 28.20168 9.36254   1.000 39.60415  ? 70  MET   B CB    1 
ATOM   2423 C  CG    . MET   B 1 73  ? 16.99084 29.37265 8.54933   1.000 42.69633  ? 70  MET   B CG    1 
ATOM   2424 S  SD    . MET   B 1 73  ? 17.32522 30.81355 9.58207   1.000 42.92450  ? 70  MET   B SD    1 
ATOM   2425 C  CE    . MET   B 1 73  ? 15.67338 31.22702 10.14588  1.000 40.71208  ? 70  MET   B CE    1 
ATOM   2426 N  N     . ASN   B 1 74  ? 15.76519 26.96384 6.12913   1.000 42.65620  ? 71  ASN   B N     1 
ATOM   2427 C  CA    . ASN   B 1 74  ? 14.99928 27.19773 4.90423   1.000 47.38214  ? 71  ASN   B CA    1 
ATOM   2428 C  C     . ASN   B 1 74  ? 14.68648 28.68413 4.72310   1.000 45.90329  ? 71  ASN   B C     1 
ATOM   2429 O  O     . ASN   B 1 74  ? 13.54973 29.07619 4.45589   1.000 47.60968  ? 71  ASN   B O     1 
ATOM   2430 C  CB    . ASN   B 1 74  ? 13.71642 26.35938 4.89486   1.000 52.04093  ? 71  ASN   B CB    1 
ATOM   2431 C  CG    . ASN   B 1 74  ? 13.07283 26.28810 3.52247   1.000 61.00973  ? 71  ASN   B CG    1 
ATOM   2432 O  OD1   . ASN   B 1 74  ? 13.76042 26.18198 2.50651   1.000 64.95741  ? 71  ASN   B OD1   1 
ATOM   2433 N  ND2   . ASN   B 1 74  ? 11.74525 26.35418 3.48631   1.000 63.20066  ? 71  ASN   B ND2   1 
ATOM   2434 N  N     . ALA   B 1 75  ? 15.71217 29.51893 4.87731   1.000 41.51064  ? 72  ALA   B N     1 
ATOM   2435 C  CA    . ALA   B 1 75  ? 15.52608 30.95486 4.72144   1.000 41.77805  ? 72  ALA   B CA    1 
ATOM   2436 C  C     . ALA   B 1 75  ? 15.19229 31.29964 3.27503   1.000 46.08402  ? 72  ALA   B C     1 
ATOM   2437 O  O     . ALA   B 1 75  ? 15.71017 30.68981 2.33541   1.000 47.12107  ? 72  ALA   B O     1 
ATOM   2438 C  CB    . ALA   B 1 75  ? 16.78008 31.70846 5.16583   1.000 40.11902  ? 72  ALA   B CB    1 
ATOM   2439 N  N     . LYS   B 1 76  ? 14.31218 32.27974 3.10397   1.000 48.18412  ? 73  LYS   B N     1 
ATOM   2440 C  CA    . LYS   B 1 76  ? 13.89149 32.76676 1.79561   1.000 51.31538  ? 73  LYS   B CA    1 
ATOM   2441 C  C     . LYS   B 1 76  ? 14.13672 34.25361 1.61396   1.000 52.92801  ? 73  LYS   B C     1 
ATOM   2442 O  O     . LYS   B 1 76  ? 14.57226 34.67974 0.54029   1.000 55.37684  ? 73  LYS   B O     1 
ATOM   2443 C  CB    . LYS   B 1 76  ? 12.39785 32.47846 1.57444   1.000 50.68219  ? 73  LYS   B CB    1 
ATOM   2444 C  CG    . LYS   B 1 76  ? 12.02488 31.00725 1.52166   1.000 59.71697  ? 73  LYS   B CG    1 
ATOM   2445 C  CD    . LYS   B 1 76  ? 11.93519 30.51463 0.08375   1.000 66.20972  ? 73  LYS   B CD    1 
ATOM   2446 C  CE    . LYS   B 1 76  ? 10.86905 29.43975 -0.07251  1.000 69.99306  ? 73  LYS   B CE    1 
ATOM   2447 N  NZ    . LYS   B 1 76  ? 9.71094  29.92098 -0.88344  1.000 74.18515  ? 73  LYS   B NZ    1 
ATOM   2448 N  N     . ARG   B 1 77  ? 13.86199 35.05605 2.63761   1.000 51.35712  ? 74  ARG   B N     1 
ATOM   2449 C  CA    . ARG   B 1 77  ? 14.01735 36.50294 2.58020   1.000 51.17134  ? 74  ARG   B CA    1 
ATOM   2450 C  C     . ARG   B 1 77  ? 14.94629 36.92461 3.70897   1.000 47.01668  ? 74  ARG   B C     1 
ATOM   2451 O  O     . ARG   B 1 77  ? 14.66428 36.65677 4.88160   1.000 45.57775  ? 74  ARG   B O     1 
ATOM   2452 C  CB    . ARG   B 1 77  ? 12.65924 37.19989 2.68945   1.000 54.42233  ? 74  ARG   B CB    1 
ATOM   2453 C  CG    . ARG   B 1 77  ? 12.70988 38.69897 2.47548   1.000 61.11886  ? 74  ARG   B CG    1 
ATOM   2454 C  CD    . ARG   B 1 77  ? 11.31681 39.30200 2.47071   1.000 67.79531  ? 74  ARG   B CD    1 
ATOM   2455 N  NE    . ARG   B 1 77  ? 11.35882 40.75802 2.37109   1.000 72.84157  ? 74  ARG   B NE    1 
ATOM   2456 C  CZ    . ARG   B 1 77  ? 11.43369 41.42839 1.22556   1.000 74.96381  ? 74  ARG   B CZ    1 
ATOM   2457 N  NH1   . ARG   B 1 77  ? 11.46722 42.75508 1.23314   1.000 76.08466  ? 74  ARG   B NH1   1 
ATOM   2458 N  NH2   . ARG   B 1 77  ? 11.47512 40.77327 0.07244   1.000 73.83185  ? 74  ARG   B NH2   1 
ATOM   2459 N  N     . THR   B 1 78  ? 16.05937 37.56319 3.35680   1.000 44.81708  ? 75  THR   B N     1 
ATOM   2460 C  CA    . THR   B 1 78  ? 17.08195 37.92218 4.32737   1.000 44.29143  ? 75  THR   B CA    1 
ATOM   2461 C  C     . THR   B 1 78  ? 17.46068 39.38779 4.16919   1.000 42.60275  ? 75  THR   B C     1 
ATOM   2462 O  O     . THR   B 1 78  ? 17.16648 40.02647 3.15624   1.000 44.49053  ? 75  THR   B O     1 
ATOM   2463 C  CB    . THR   B 1 78  ? 18.34594 37.05580 4.18256   1.000 42.40320  ? 75  THR   B CB    1 
ATOM   2464 O  OG1   . THR   B 1 78  ? 19.05141 37.43050 2.99368   1.000 43.21994  ? 75  THR   B OG1   1 
ATOM   2465 C  CG2   . THR   B 1 78  ? 17.98990 35.57601 4.10549   1.000 41.24349  ? 75  THR   B CG2   1 
ATOM   2466 N  N     . ILE   B 1 79  ? 18.13025 39.91166 5.19050   1.000 39.94095  ? 76  ILE   B N     1 
ATOM   2467 C  CA    . ILE   B 1 79  ? 18.65547 41.26978 5.18037   1.000 41.52817  ? 76  ILE   B CA    1 
ATOM   2468 C  C     . ILE   B 1 79  ? 20.09552 41.22605 5.67769   1.000 42.08731  ? 76  ILE   B C     1 
ATOM   2469 O  O     . ILE   B 1 79  ? 20.41489 40.50618 6.62896   1.000 38.20640  ? 76  ILE   B O     1 
ATOM   2470 C  CB    . ILE   B 1 79  ? 17.79032 42.22403 6.03380   1.000 44.85713  ? 76  ILE   B CB    1 
ATOM   2471 C  CG1   . ILE   B 1 79  ? 18.44848 43.59788 6.15672   1.000 48.76339  ? 76  ILE   B CG1   1 
ATOM   2472 C  CG2   . ILE   B 1 79  ? 17.51381 41.62874 7.39862   1.000 44.31664  ? 76  ILE   B CG2   1 
ATOM   2473 C  CD1   . ILE   B 1 79  ? 17.54100 44.64991 6.74887   1.000 52.02965  ? 76  ILE   B CD1   1 
ATOM   2474 N  N     . GLU   B 1 80  ? 20.96647 41.98176 5.01126   1.000 44.47307  ? 77  GLU   B N     1 
ATOM   2475 C  CA    . GLU   B 1 80  ? 22.40166 41.95647 5.27172   1.000 43.79922  ? 77  GLU   B CA    1 
ATOM   2476 C  C     . GLU   B 1 80  ? 22.86210 43.37677 5.56289   1.000 42.77855  ? 77  GLU   B C     1 
ATOM   2477 O  O     . GLU   B 1 80  ? 22.79883 44.24362 4.68512   1.000 44.58857  ? 77  GLU   B O     1 
ATOM   2478 C  CB    . GLU   B 1 80  ? 23.16169 41.37535 4.07484   1.000 44.05499  ? 77  GLU   B CB    1 
ATOM   2479 C  CG    . GLU   B 1 80  ? 24.58881 40.94538 4.37058   1.000 51.45600  ? 77  GLU   B CG    1 
ATOM   2480 C  CD    . GLU   B 1 80  ? 24.75207 39.43447 4.35880   1.000 58.85036  ? 77  GLU   B CD    1 
ATOM   2481 O  OE1   . GLU   B 1 80  ? 25.81144 38.94701 4.80616   1.000 58.71883  ? 77  GLU   B OE1   1 
ATOM   2482 O  OE2   . GLU   B 1 80  ? 23.82006 38.73394 3.90368   1.000 60.82822  ? 77  GLU   B OE2   1 
ATOM   2483 N  N     . ILE   B 1 81  ? 23.32622 43.61280 6.78547   1.000 39.01014  ? 78  ILE   B N     1 
ATOM   2484 C  CA    . ILE   B 1 81  ? 23.73079 44.93966 7.24009   1.000 39.82719  ? 78  ILE   B CA    1 
ATOM   2485 C  C     . ILE   B 1 81  ? 25.24777 44.94400 7.37192   1.000 37.26774  ? 78  ILE   B C     1 
ATOM   2486 O  O     . ILE   B 1 81  ? 25.80575 44.29609 8.26685   1.000 35.98046  ? 78  ILE   B O     1 
ATOM   2487 C  CB    . ILE   B 1 81  ? 23.05406 45.31710 8.56356   1.000 43.25502  ? 78  ILE   B CB    1 
ATOM   2488 C  CG1   . ILE   B 1 81  ? 21.53366 45.25130 8.41095   1.000 47.33586  ? 78  ILE   B CG1   1 
ATOM   2489 C  CG2   . ILE   B 1 81  ? 23.48977 46.70164 9.00741   1.000 42.88932  ? 78  ILE   B CG2   1 
ATOM   2490 C  CD1   . ILE   B 1 81  ? 20.78130 45.57074 9.67916   1.000 50.42096  ? 78  ILE   B CD1   1 
ATOM   2491 N  N     . GLY   B 1 82  ? 25.91581 45.68331 6.48823   1.000 39.43402  ? 79  GLY   B N     1 
ATOM   2492 C  CA    . GLY   B 1 82  ? 27.36569 45.68133 6.43142   1.000 42.20263  ? 79  GLY   B CA    1 
ATOM   2493 C  C     . GLY   B 1 82  ? 27.87023 44.72018 5.37545   1.000 42.31815  ? 79  GLY   B C     1 
ATOM   2494 O  O     . GLY   B 1 82  ? 28.05869 43.53243 5.65009   1.000 41.05194  ? 79  GLY   B O     1 
ATOM   2495 N  N     . VAL   B 1 83  ? 28.09128 45.21910 4.16282   1.000 40.94928  ? 80  VAL   B N     1 
ATOM   2496 C  CA    . VAL   B 1 83  ? 28.37414 44.35359 3.01999   1.000 42.80394  ? 80  VAL   B CA    1 
ATOM   2497 C  C     . VAL   B 1 83  ? 29.86867 44.25541 2.74236   1.000 38.85339  ? 80  VAL   B C     1 
ATOM   2498 O  O     . VAL   B 1 83  ? 30.39430 43.15951 2.52938   1.000 37.10146  ? 80  VAL   B O     1 
ATOM   2499 C  CB    . VAL   B 1 83  ? 27.60131 44.85253 1.77968   1.000 45.02942  ? 80  VAL   B CB    1 
ATOM   2500 C  CG1   . VAL   B 1 83  ? 27.99775 44.05201 0.54389   1.000 44.96715  ? 80  VAL   B CG1   1 
ATOM   2501 C  CG2   . VAL   B 1 83  ? 26.10767 44.76297 2.02465   1.000 42.40436  ? 80  VAL   B CG2   1 
ATOM   2502 N  N     . TYR   B 1 84  ? 30.56446 45.39138 2.72404   1.000 38.82518  ? 81  TYR   B N     1 
ATOM   2503 C  CA    . TYR   B 1 84  ? 31.99507 45.46092 2.38599   1.000 39.58400  ? 81  TYR   B CA    1 
ATOM   2504 C  C     . TYR   B 1 84  ? 32.13831 44.93738 0.95984   1.000 42.57774  ? 81  TYR   B C     1 
ATOM   2505 O  O     . TYR   B 1 84  ? 31.37220 45.36529 0.07839   1.000 44.65388  ? 81  TYR   B O     1 
ATOM   2506 C  CB    . TYR   B 1 84  ? 32.81518 44.73408 3.44731   1.000 38.72673  ? 81  TYR   B CB    1 
ATOM   2507 C  CG    . TYR   B 1 84  ? 34.30822 44.87073 3.27338   1.000 42.68234  ? 81  TYR   B CG    1 
ATOM   2508 C  CD1   . TYR   B 1 84  ? 34.85824 45.97467 2.62847   1.000 41.22231  ? 81  TYR   B CD1   1 
ATOM   2509 C  CD2   . TYR   B 1 84  ? 35.16951 43.88450 3.73823   1.000 43.15860  ? 81  TYR   B CD2   1 
ATOM   2510 C  CE1   . TYR   B 1 84  ? 36.23065 46.09547 2.46392   1.000 39.24651  ? 81  TYR   B CE1   1 
ATOM   2511 C  CE2   . TYR   B 1 84  ? 36.53502 43.99500 3.57732   1.000 42.17267  ? 81  TYR   B CE2   1 
ATOM   2512 C  CZ    . TYR   B 1 84  ? 37.05941 45.10174 2.94106   1.000 40.91376  ? 81  TYR   B CZ    1 
ATOM   2513 O  OH    . TYR   B 1 84  ? 38.41987 45.20334 2.79009   1.000 42.70011  ? 81  TYR   B OH    1 
ATOM   2514 N  N     . THR   B 1 85  ? 33.07186 44.02854 0.67465   1.000 43.59924  ? 82  THR   B N     1 
ATOM   2515 C  CA    . THR   B 1 85  ? 33.20616 43.50535 -0.67820  1.000 44.52027  ? 82  THR   B CA    1 
ATOM   2516 C  C     . THR   B 1 85  ? 32.18006 42.42722 -1.00171  1.000 47.45214  ? 82  THR   B C     1 
ATOM   2517 O  O     . THR   B 1 85  ? 32.11809 41.98593 -2.15389  1.000 51.52395  ? 82  THR   B O     1 
ATOM   2518 C  CB    . THR   B 1 85  ? 34.61631 42.95836 -0.90629  1.000 41.64664  ? 82  THR   B CB    1 
ATOM   2519 O  OG1   . THR   B 1 85  ? 34.87491 41.88951 0.01100   1.000 39.56666  ? 82  THR   B OG1   1 
ATOM   2520 C  CG2   . THR   B 1 85  ? 35.65227 44.06268 -0.70937  1.000 41.67592  ? 82  THR   B CG2   1 
ATOM   2521 N  N     . GLY   B 1 86  ? 31.38973 41.99157 -0.02639  1.000 43.60518  ? 83  GLY   B N     1 
ATOM   2522 C  CA    . GLY   B 1 86  ? 30.25003 41.13841 -0.28449  1.000 43.16555  ? 83  GLY   B CA    1 
ATOM   2523 C  C     . GLY   B 1 86  ? 30.43874 39.65223 -0.06112  1.000 44.19482  ? 83  GLY   B C     1 
ATOM   2524 O  O     . GLY   B 1 86  ? 29.64480 38.86794 -0.59743  1.000 42.11538  ? 83  GLY   B O     1 
ATOM   2525 N  N     . TYR   B 1 87  ? 31.44377 39.23673 0.71818   1.000 41.19547  ? 84  TYR   B N     1 
ATOM   2526 C  CA    . TYR   B 1 87  ? 31.67667 37.80663 0.91120   1.000 38.56149  ? 84  TYR   B CA    1 
ATOM   2527 C  C     . TYR   B 1 87  ? 30.48437 37.13621 1.58650   1.000 38.40964  ? 84  TYR   B C     1 
ATOM   2528 O  O     . TYR   B 1 87  ? 29.95006 36.14120 1.08141   1.000 41.06160  ? 84  TYR   B O     1 
ATOM   2529 C  CB    . TYR   B 1 87  ? 32.95115 37.57253 1.72127   1.000 36.24695  ? 84  TYR   B CB    1 
ATOM   2530 C  CG    . TYR   B 1 87  ? 33.35816 36.11693 1.75737   1.000 36.02506  ? 84  TYR   B CG    1 
ATOM   2531 C  CD1   . TYR   B 1 87  ? 34.10380 35.56003 0.72452   1.000 36.46456  ? 84  TYR   B CD1   1 
ATOM   2532 C  CD2   . TYR   B 1 87  ? 32.98122 35.29308 2.81185   1.000 33.93557  ? 84  TYR   B CD2   1 
ATOM   2533 C  CE1   . TYR   B 1 87  ? 34.46970 34.22399 0.74432   1.000 34.23237  ? 84  TYR   B CE1   1 
ATOM   2534 C  CE2   . TYR   B 1 87  ? 33.34353 33.95482 2.84197   1.000 31.69148  ? 84  TYR   B CE2   1 
ATOM   2535 C  CZ    . TYR   B 1 87  ? 34.08765 33.42800 1.80578   1.000 33.04629  ? 84  TYR   B CZ    1 
ATOM   2536 O  OH    . TYR   B 1 87  ? 34.44740 32.10059 1.82829   1.000 35.26998  ? 84  TYR   B OH    1 
ATOM   2537 N  N     . SER   B 1 88  ? 30.05121 37.66732 2.73408   1.000 35.19998  ? 85  SER   B N     1 
ATOM   2538 C  CA    . SER   B 1 88  ? 28.88847 37.09710 3.40779   1.000 35.85250  ? 85  SER   B CA    1 
ATOM   2539 C  C     . SER   B 1 88  ? 27.61891 37.28298 2.58524   1.000 35.39078  ? 85  SER   B C     1 
ATOM   2540 O  O     . SER   B 1 88  ? 26.72318 36.43330 2.63420   1.000 34.79104  ? 85  SER   B O     1 
ATOM   2541 C  CB    . SER   B 1 88  ? 28.72361 37.71244 4.79997   1.000 36.35651  ? 85  SER   B CB    1 
ATOM   2542 O  OG    . SER   B 1 88  ? 28.41175 39.09305 4.72870   1.000 36.73380  ? 85  SER   B OG    1 
ATOM   2543 N  N     . LEU   B 1 89  ? 27.52879 38.37436 1.82048   1.000 35.75280  ? 86  LEU   B N     1 
ATOM   2544 C  CA    . LEU   B 1 89  ? 26.38316 38.57411 0.93614   1.000 37.37303  ? 86  LEU   B CA    1 
ATOM   2545 C  C     . LEU   B 1 89  ? 26.33878 37.50722 -0.15371  1.000 41.78040  ? 86  LEU   B C     1 
ATOM   2546 O  O     . LEU   B 1 89  ? 25.30889 36.85277 -0.35933  1.000 43.19438  ? 86  LEU   B O     1 
ATOM   2547 C  CB    . LEU   B 1 89  ? 26.43853 39.97270 0.32137   1.000 38.88166  ? 86  LEU   B CB    1 
ATOM   2548 C  CG    . LEU   B 1 89  ? 25.34011 40.32563 -0.68439  1.000 40.90899  ? 86  LEU   B CG    1 
ATOM   2549 C  CD1   . LEU   B 1 89  ? 23.96855 40.26708 -0.02654  1.000 31.13116  ? 86  LEU   B CD1   1 
ATOM   2550 C  CD2   . LEU   B 1 89  ? 25.59420 41.69800 -1.29459  1.000 36.88865  ? 86  LEU   B CD2   1 
ATOM   2551 N  N     . LEU   B 1 90  ? 27.45507 37.31920 -0.86412  1.000 40.78046  ? 87  LEU   B N     1 
ATOM   2552 C  CA    . LEU   B 1 90  ? 27.51805 36.28117 -1.88921  1.000 40.25526  ? 87  LEU   B CA    1 
ATOM   2553 C  C     . LEU   B 1 90  ? 27.30841 34.89641 -1.28713  1.000 41.04470  ? 87  LEU   B C     1 
ATOM   2554 O  O     . LEU   B 1 90  ? 26.66592 34.03577 -1.90251  1.000 43.06943  ? 87  LEU   B O     1 
ATOM   2555 C  CB    . LEU   B 1 90  ? 28.85600 36.35455 -2.62616  1.000 37.45532  ? 87  LEU   B CB    1 
ATOM   2556 C  CG    . LEU   B 1 90  ? 29.13337 35.27741 -3.67957  1.000 40.53613  ? 87  LEU   B CG    1 
ATOM   2557 C  CD1   . LEU   B 1 90  ? 28.02871 35.24228 -4.72748  1.000 41.38777  ? 87  LEU   B CD1   1 
ATOM   2558 C  CD2   . LEU   B 1 90  ? 30.49265 35.49830 -4.33579  1.000 37.93771  ? 87  LEU   B CD2   1 
ATOM   2559 N  N     . THR   B 1 91  ? 27.84766 34.66340 -0.08607  1.000 37.89981  ? 88  THR   B N     1 
ATOM   2560 C  CA    . THR   B 1 91  ? 27.58244 33.41937 0.63025   1.000 39.56095  ? 88  THR   B CA    1 
ATOM   2561 C  C     . THR   B 1 91  ? 26.08469 33.21211 0.82972   1.000 39.46651  ? 88  THR   B C     1 
ATOM   2562 O  O     . THR   B 1 91  ? 25.55867 32.11644 0.60269   1.000 38.07650  ? 88  THR   B O     1 
ATOM   2563 C  CB    . THR   B 1 91  ? 28.30323 33.42990 1.98175   1.000 39.55036  ? 88  THR   B CB    1 
ATOM   2564 O  OG1   . THR   B 1 91  ? 29.72139 33.44485 1.77807   1.000 38.74134  ? 88  THR   B OG1   1 
ATOM   2565 C  CG2   . THR   B 1 91  ? 27.92435 32.20623 2.80229   1.000 38.85664  ? 88  THR   B CG2   1 
ATOM   2566 N  N     . THR   B 1 92  ? 25.38228 34.26660 1.25209   1.000 40.13225  ? 89  THR   B N     1 
ATOM   2567 C  CA    . THR   B 1 92  ? 23.94009 34.17830 1.46378   1.000 41.27426  ? 89  THR   B CA    1 
ATOM   2568 C  C     . THR   B 1 92  ? 23.20133 33.93300 0.15213   1.000 44.06962  ? 89  THR   B C     1 
ATOM   2569 O  O     . THR   B 1 92  ? 22.30343 33.08438 0.08414   1.000 45.79127  ? 89  THR   B O     1 
ATOM   2570 C  CB    . THR   B 1 92  ? 23.43550 35.45893 2.13288   1.000 37.34164  ? 89  THR   B CB    1 
ATOM   2571 O  OG1   . THR   B 1 92  ? 24.11138 35.64582 3.38304   1.000 37.33180  ? 89  THR   B OG1   1 
ATOM   2572 C  CG2   . THR   B 1 92  ? 21.93268 35.39344 2.37255   1.000 32.10675  ? 89  THR   B CG2   1 
ATOM   2573 N  N     . ALA   B 1 93  ? 23.57013 34.66528 -0.90416  1.000 42.32136  ? 90  ALA   B N     1 
ATOM   2574 C  CA    . ALA   B 1 93  ? 22.86465 34.53561 -2.17606  1.000 45.79056  ? 90  ALA   B CA    1 
ATOM   2575 C  C     . ALA   B 1 93  ? 23.03390 33.14175 -2.76845  1.000 48.31126  ? 90  ALA   B C     1 
ATOM   2576 O  O     . ALA   B 1 93  ? 22.10920 32.60780 -3.39436  1.000 47.63641  ? 90  ALA   B O     1 
ATOM   2577 C  CB    . ALA   B 1 93  ? 23.35306 35.59976 -3.15604  1.000 45.50638  ? 90  ALA   B CB    1 
ATOM   2578 N  N     . LEU   B 1 94  ? 24.20936 32.53630 -2.58260  1.000 45.81764  ? 91  LEU   B N     1 
ATOM   2579 C  CA    . LEU   B 1 94  ? 24.43566 31.18088 -3.06957  1.000 44.22942  ? 91  LEU   B CA    1 
ATOM   2580 C  C     . LEU   B 1 94  ? 23.71346 30.13290 -2.23323  1.000 45.03649  ? 91  LEU   B C     1 
ATOM   2581 O  O     . LEU   B 1 94  ? 23.45922 29.03162 -2.73055  1.000 49.17287  ? 91  LEU   B O     1 
ATOM   2582 C  CB    . LEU   B 1 94  ? 25.93344 30.87144 -3.09752  1.000 43.75181  ? 91  LEU   B CB    1 
ATOM   2583 C  CG    . LEU   B 1 94  ? 26.75323 31.50204 -4.22315  1.000 47.56167  ? 91  LEU   B CG    1 
ATOM   2584 C  CD1   . LEU   B 1 94  ? 28.23624 31.39306 -3.91404  1.000 46.40063  ? 91  LEU   B CD1   1 
ATOM   2585 C  CD2   . LEU   B 1 94  ? 26.43723 30.83764 -5.55983  1.000 51.31167  ? 91  LEU   B CD2   1 
ATOM   2586 N  N     . ALA   B 1 95  ? 23.38269 30.44171 -0.98049  1.000 43.18759  ? 92  ALA   B N     1 
ATOM   2587 C  CA    . ALA   B 1 95  ? 22.71716 29.47741 -0.11277  1.000 44.73834  ? 92  ALA   B CA    1 
ATOM   2588 C  C     . ALA   B 1 95  ? 21.20314 29.48935 -0.25820  1.000 46.78996  ? 92  ALA   B C     1 
ATOM   2589 O  O     . ALA   B 1 95  ? 20.55777 28.46587 -0.00494  1.000 50.10440  ? 92  ALA   B O     1 
ATOM   2590 C  CB    . ALA   B 1 95  ? 23.08157 29.74230 1.34977   1.000 43.64396  ? 92  ALA   B CB    1 
ATOM   2591 N  N     . LEU   B 1 96  ? 20.62647 30.61717 -0.65476  1.000 46.13410  ? 93  LEU   B N     1 
ATOM   2592 C  CA    . LEU   B 1 96  ? 19.18520 30.75506 -0.77176  1.000 46.75245  ? 93  LEU   B CA    1 
ATOM   2593 C  C     . LEU   B 1 96  ? 18.66859 30.04943 -2.02128  1.000 45.59787  ? 93  LEU   B C     1 
ATOM   2594 O  O     . LEU   B 1 96  ? 19.41937 29.82328 -2.97396  1.000 47.61687  ? 93  LEU   B O     1 
ATOM   2595 C  CB    . LEU   B 1 96  ? 18.80798 32.23312 -0.81438  1.000 47.52653  ? 93  LEU   B CB    1 
ATOM   2596 C  CG    . LEU   B 1 96  ? 19.06244 33.01572 0.47148   1.000 46.06221  ? 93  LEU   B CG    1 
ATOM   2597 C  CD1   . LEU   B 1 96  ? 18.64639 34.46169 0.29931   1.000 45.96486  ? 93  LEU   B CD1   1 
ATOM   2598 C  CD2   . LEU   B 1 96  ? 18.31723 32.37552 1.62892   1.000 43.33576  ? 93  LEU   B CD2   1 
ATOM   2599 N  N     . PRO   B 1 97  ? 17.38488 29.68844 -2.04269  1.000 45.71661  ? 94  PRO   B N     1 
ATOM   2600 C  CA    . PRO   B 1 97  ? 16.78772 29.15079 -3.27298  1.000 47.54249  ? 94  PRO   B CA    1 
ATOM   2601 C  C     . PRO   B 1 97  ? 16.80300 30.18727 -4.38622  1.000 49.57145  ? 94  PRO   B C     1 
ATOM   2602 O  O     . PRO   B 1 97  ? 17.08658 31.36915 -4.17501  1.000 47.69459  ? 94  PRO   B O     1 
ATOM   2603 C  CB    . PRO   B 1 97  ? 15.35677 28.79185 -2.85545  1.000 47.12917  ? 94  PRO   B CB    1 
ATOM   2604 C  CG    . PRO   B 1 97  ? 15.09850 29.61314 -1.62815  1.000 47.56839  ? 94  PRO   B CG    1 
ATOM   2605 C  CD    . PRO   B 1 97  ? 16.42366 29.70831 -0.92672  1.000 43.21816  ? 94  PRO   B CD    1 
ATOM   2606 N  N     . GLU   B 1 98  ? 16.48312 29.72246 -5.59940  1.000 52.52475  ? 95  GLU   B N     1 
ATOM   2607 C  CA    . GLU   B 1 98  ? 16.54684 30.59341 -6.77119  1.000 58.09470  ? 95  GLU   B CA    1 
ATOM   2608 C  C     . GLU   B 1 98  ? 15.65722 31.82308 -6.62074  1.000 61.29903  ? 95  GLU   B C     1 
ATOM   2609 O  O     . GLU   B 1 98  ? 15.96486 32.88256 -7.18028  1.000 61.73910  ? 95  GLU   B O     1 
ATOM   2610 C  CB    . GLU   B 1 98  ? 16.16484 29.81079 -8.02865  1.000 61.16478  ? 95  GLU   B CB    1 
ATOM   2611 C  CG    . GLU   B 1 98  ? 17.13790 28.69747 -8.38389  1.000 62.83837  ? 95  GLU   B CG    1 
ATOM   2612 N  N     . ASP   B 1 99  ? 14.56618 31.71036 -5.86633  1.000 61.97356  ? 96  ASP   B N     1 
ATOM   2613 C  CA    . ASP   B 1 99  ? 13.63817 32.81238 -5.65369  1.000 62.00655  ? 96  ASP   B CA    1 
ATOM   2614 C  C     . ASP   B 1 99  ? 13.95122 33.62295 -4.39868  1.000 55.91395  ? 96  ASP   B C     1 
ATOM   2615 O  O     . ASP   B 1 99  ? 13.13053 34.45385 -3.99389  1.000 54.45577  ? 96  ASP   B O     1 
ATOM   2616 C  CB    . ASP   B 1 99  ? 12.20403 32.27981 -5.58242  1.000 65.45382  ? 96  ASP   B CB    1 
ATOM   2617 C  CG    . ASP   B 1 99  ? 12.04943 31.16773 -4.56728  1.000 70.50670  ? 96  ASP   B CG    1 
ATOM   2618 O  OD1   . ASP   B 1 99  ? 12.86984 30.22557 -4.58511  1.000 73.34844  ? 96  ASP   B OD1   1 
ATOM   2619 O  OD2   . ASP   B 1 99  ? 11.11526 31.23847 -3.74261  1.000 73.71136  ? 96  ASP   B OD2   1 
ATOM   2620 N  N     . GLY   B 1 100 ? 15.10959 33.40423 -3.77880  1.000 53.20267  ? 97  GLY   B N     1 
ATOM   2621 C  CA    . GLY   B 1 100 ? 15.44304 34.13053 -2.56759  1.000 51.52300  ? 97  GLY   B CA    1 
ATOM   2622 C  C     . GLY   B 1 100 ? 15.71312 35.60003 -2.83195  1.000 50.45980  ? 97  GLY   B C     1 
ATOM   2623 O  O     . GLY   B 1 100 ? 16.19087 35.99240 -3.89682  1.000 50.52844  ? 97  GLY   B O     1 
ATOM   2624 N  N     . LYS   B 1 101 ? 15.40335 36.42709 -1.83414  1.000 48.99859  ? 98  LYS   B N     1 
ATOM   2625 C  CA    . LYS   B 1 101 ? 15.56267 37.87245 -1.93321  1.000 49.88116  ? 98  LYS   B CA    1 
ATOM   2626 C  C     . LYS   B 1 101 ? 16.37153 38.37760 -0.74935  1.000 47.38321  ? 98  LYS   B C     1 
ATOM   2627 O  O     . LYS   B 1 101 ? 16.13096 37.96808 0.39078   1.000 47.07761  ? 98  LYS   B O     1 
ATOM   2628 C  CB    . LYS   B 1 101 ? 14.20254 38.57556 -1.98636  1.000 53.30920  ? 98  LYS   B CB    1 
ATOM   2629 C  CG    . LYS   B 1 101 ? 13.49910 38.44869 -3.32776  1.000 60.15286  ? 98  LYS   B CG    1 
ATOM   2630 C  CD    . LYS   B 1 101 ? 12.09519 37.89245 -3.16775  1.000 65.21740  ? 98  LYS   B CD    1 
ATOM   2631 N  N     . ILE   B 1 102 ? 17.32356 39.26790 -1.02175  1.000 44.76760  ? 99  ILE   B N     1 
ATOM   2632 C  CA    . ILE   B 1 102 ? 18.20133 39.82875 -0.00254  1.000 43.31779  ? 99  ILE   B CA    1 
ATOM   2633 C  C     . ILE   B 1 102 ? 18.13332 41.34527 -0.08120  1.000 44.55326  ? 99  ILE   B C     1 
ATOM   2634 O  O     . ILE   B 1 102 ? 18.21726 41.91799 -1.17395  1.000 47.19510  ? 99  ILE   B O     1 
ATOM   2635 C  CB    . ILE   B 1 102 ? 19.65964 39.36461 -0.17774  1.000 43.85173  ? 99  ILE   B CB    1 
ATOM   2636 C  CG1   . ILE   B 1 102 ? 19.74915 37.84085 -0.21950  1.000 39.03987  ? 99  ILE   B CG1   1 
ATOM   2637 C  CG2   . ILE   B 1 102 ? 20.53931 39.94373 0.93013   1.000 42.43181  ? 99  ILE   B CG2   1 
ATOM   2638 C  CD1   . ILE   B 1 102 ? 21.10558 37.34014 -0.64315  1.000 36.32704  ? 99  ILE   B CD1   1 
ATOM   2639 N  N     . THR   B 1 103 ? 17.99305 41.99316 1.07365   1.000 41.75124  ? 100 THR   B N     1 
ATOM   2640 C  CA    . THR   B 1 103 ? 18.16149 43.43634 1.18868   1.000 43.28324  ? 100 THR   B CA    1 
ATOM   2641 C  C     . THR   B 1 103 ? 19.54024 43.69205 1.78920   1.000 44.07355  ? 100 THR   B C     1 
ATOM   2642 O  O     . THR   B 1 103 ? 19.79255 43.34950 2.94901   1.000 42.77442  ? 100 THR   B O     1 
ATOM   2643 C  CB    . THR   B 1 103 ? 17.06228 44.06292 2.04333   1.000 46.91608  ? 100 THR   B CB    1 
ATOM   2644 O  OG1   . THR   B 1 103 ? 15.78262 43.58056 1.61393   1.000 49.61919  ? 100 THR   B OG1   1 
ATOM   2645 C  CG2   . THR   B 1 103 ? 17.09037 45.57600 1.89336   1.000 47.23742  ? 100 THR   B CG2   1 
ATOM   2646 N  N     . ALA   B 1 104 ? 20.43325 44.27588 0.99538   1.000 43.01705  ? 101 ALA   B N     1 
ATOM   2647 C  CA    . ALA   B 1 104 ? 21.80773 44.53406 1.40335   1.000 46.22976  ? 101 ALA   B CA    1 
ATOM   2648 C  C     . ALA   B 1 104 ? 21.99234 46.02655 1.63887   1.000 48.49046  ? 101 ALA   B C     1 
ATOM   2649 O  O     . ALA   B 1 104 ? 21.56513 46.84570 0.81771   1.000 49.02684  ? 101 ALA   B O     1 
ATOM   2650 C  CB    . ALA   B 1 104 ? 22.79607 44.03082 0.34835   1.000 46.29333  ? 101 ALA   B CB    1 
ATOM   2651 N  N     . ILE   B 1 105 ? 22.62676 46.37483 2.75846   1.000 47.12527  ? 102 ILE   B N     1 
ATOM   2652 C  CA    . ILE   B 1 105 ? 22.77873 47.75965 3.18847   1.000 46.14079  ? 102 ILE   B CA    1 
ATOM   2653 C  C     . ILE   B 1 105 ? 24.23649 48.00943 3.55189   1.000 46.67699  ? 102 ILE   B C     1 
ATOM   2654 O  O     . ILE   B 1 105 ? 24.85503 47.20721 4.26133   1.000 44.25280  ? 102 ILE   B O     1 
ATOM   2655 C  CB    . ILE   B 1 105 ? 21.85978 48.08478 4.38647   1.000 42.99360  ? 102 ILE   B CB    1 
ATOM   2656 C  CG1   . ILE   B 1 105 ? 20.40778 47.70488 4.07720   1.000 43.12800  ? 102 ILE   B CG1   1 
ATOM   2657 C  CG2   . ILE   B 1 105 ? 21.95849 49.55900 4.75120   1.000 37.78627  ? 102 ILE   B CG2   1 
ATOM   2658 C  CD1   . ILE   B 1 105 ? 19.46918 47.85513 5.25947   1.000 41.98757  ? 102 ILE   B CD1   1 
ATOM   2659 N  N     . ASP   B 1 106 ? 24.78062 49.12767 3.07153   1.000 45.61980  ? 103 ASP   B N     1 
ATOM   2660 C  CA    . ASP   B 1 106 ? 26.15552 49.51916 3.35089   1.000 44.88954  ? 103 ASP   B CA    1 
ATOM   2661 C  C     . ASP   B 1 106 ? 26.34727 50.96714 2.91853   1.000 44.47077  ? 103 ASP   B C     1 
ATOM   2662 O  O     . ASP   B 1 106 ? 25.87097 51.36664 1.85373   1.000 44.36231  ? 103 ASP   B O     1 
ATOM   2663 C  CB    . ASP   B 1 106 ? 27.15076 48.60061 2.62561   1.000 43.99731  ? 103 ASP   B CB    1 
ATOM   2664 C  CG    . ASP   B 1 106 ? 28.56079 48.70985 3.18049   1.000 45.12608  ? 103 ASP   B CG    1 
ATOM   2665 O  OD1   . ASP   B 1 106 ? 29.18166 49.78376 3.03302   1.000 46.34323  ? 103 ASP   B OD1   1 
ATOM   2666 O  OD2   . ASP   B 1 106 ? 29.04163 47.72312 3.77781   1.000 45.08805  ? 103 ASP   B OD2   1 
ATOM   2667 N  N     . VAL   B 1 107 ? 27.04623 51.74528 3.74957   1.000 44.92625  ? 104 VAL   B N     1 
ATOM   2668 C  CA    . VAL   B 1 107 ? 27.24959 53.16101 3.45700   1.000 45.68473  ? 104 VAL   B CA    1 
ATOM   2669 C  C     . VAL   B 1 107 ? 28.16457 53.38152 2.26207   1.000 46.40536  ? 104 VAL   B C     1 
ATOM   2670 O  O     . VAL   B 1 107 ? 28.16458 54.47288 1.68291   1.000 50.08594  ? 104 VAL   B O     1 
ATOM   2671 C  CB    . VAL   B 1 107 ? 27.82588 53.89282 4.68325   1.000 47.41197  ? 104 VAL   B CB    1 
ATOM   2672 C  CG1   . VAL   B 1 107 ? 26.76244 54.07651 5.74266   1.000 50.50092  ? 104 VAL   B CG1   1 
ATOM   2673 C  CG2   . VAL   B 1 107 ? 29.01393 53.12045 5.24723   1.000 45.52618  ? 104 VAL   B CG2   1 
ATOM   2674 N  N     . ASN   B 1 108 ? 28.94806 52.37885 1.87331   1.000 45.47868  ? 105 ASN   B N     1 
ATOM   2675 C  CA    . ASN   B 1 108 ? 30.00670 52.54772 0.88000   1.000 48.13161  ? 105 ASN   B CA    1 
ATOM   2676 C  C     . ASN   B 1 108 ? 29.84399 51.48180 -0.19967  1.000 47.65938  ? 105 ASN   B C     1 
ATOM   2677 O  O     . ASN   B 1 108 ? 30.26737 50.33714 -0.01709  1.000 48.10516  ? 105 ASN   B O     1 
ATOM   2678 C  CB    . ASN   B 1 108 ? 31.37750 52.46307 1.54575   1.000 49.09748  ? 105 ASN   B CB    1 
ATOM   2679 C  CG    . ASN   B 1 108 ? 32.48079 53.04645 0.69115   1.000 51.62363  ? 105 ASN   B CG    1 
ATOM   2680 O  OD1   . ASN   B 1 108 ? 32.36796 53.10999 -0.53280  1.000 53.92887  ? 105 ASN   B OD1   1 
ATOM   2681 N  ND2   . ASN   B 1 108 ? 33.56046 53.47747 1.33514   1.000 50.83617  ? 105 ASN   B ND2   1 
ATOM   2682 N  N     . LYS   B 1 109 ? 29.24133 51.85973 -1.32757  1.000 47.69831  ? 106 LYS   B N     1 
ATOM   2683 C  CA    . LYS   B 1 109 ? 29.05839 50.92697 -2.43190  1.000 52.46061  ? 106 LYS   B CA    1 
ATOM   2684 C  C     . LYS   B 1 109 ? 30.33865 50.69629 -3.22394  1.000 52.75112  ? 106 LYS   B C     1 
ATOM   2685 O  O     . LYS   B 1 109 ? 30.40201 49.73843 -4.00362  1.000 51.74224  ? 106 LYS   B O     1 
ATOM   2686 C  CB    . LYS   B 1 109 ? 27.94756 51.42416 -3.36562  1.000 57.32173  ? 106 LYS   B CB    1 
ATOM   2687 C  CG    . LYS   B 1 109 ? 27.41506 50.36996 -4.33115  1.000 59.79329  ? 106 LYS   B CG    1 
ATOM   2688 C  CD    . LYS   B 1 109 ? 26.17144 50.85222 -5.06209  1.000 61.51665  ? 106 LYS   B CD    1 
ATOM   2689 N  N     . SER   B 1 110 ? 31.35554 51.54354 -3.04281  1.000 52.84372  ? 107 SER   B N     1 
ATOM   2690 C  CA    . SER   B 1 110 ? 32.63673 51.31027 -3.70086  1.000 52.09646  ? 107 SER   B CA    1 
ATOM   2691 C  C     . SER   B 1 110 ? 33.20841 49.95334 -3.31225  1.000 50.71581  ? 107 SER   B C     1 
ATOM   2692 O  O     . SER   B 1 110 ? 33.75080 49.23346 -4.15941  1.000 53.64129  ? 107 SER   B O     1 
ATOM   2693 C  CB    . SER   B 1 110 ? 33.62135 52.42628 -3.35020  1.000 56.72128  ? 107 SER   B CB    1 
ATOM   2694 O  OG    . SER   B 1 110 ? 32.98011 53.68972 -3.34628  1.000 62.89703  ? 107 SER   B OG    1 
ATOM   2695 N  N     . TYR   B 1 111 ? 33.09346 49.58728 -2.03195  1.000 46.58841  ? 108 TYR   B N     1 
ATOM   2696 C  CA    . TYR   B 1 111 ? 33.49943 48.25354 -1.60132  1.000 45.53700  ? 108 TYR   B CA    1 
ATOM   2697 C  C     . TYR   B 1 111 ? 32.68313 47.17950 -2.30781  1.000 48.16727  ? 108 TYR   B C     1 
ATOM   2698 O  O     . TYR   B 1 111 ? 33.22557 46.15057 -2.72921  1.000 51.25134  ? 108 TYR   B O     1 
ATOM   2699 C  CB    . TYR   B 1 111 ? 33.34100 48.11484 -0.08695  1.000 43.44406  ? 108 TYR   B CB    1 
ATOM   2700 C  CG    . TYR   B 1 111 ? 34.15172 49.08418 0.74596   1.000 43.98964  ? 108 TYR   B CG    1 
ATOM   2701 C  CD1   . TYR   B 1 111 ? 35.36929 49.58349 0.29331   1.000 46.31578  ? 108 TYR   B CD1   1 
ATOM   2702 C  CD2   . TYR   B 1 111 ? 33.70011 49.49246 1.99675   1.000 40.96796  ? 108 TYR   B CD2   1 
ATOM   2703 C  CE1   . TYR   B 1 111 ? 36.11222 50.46672 1.06576   1.000 43.66862  ? 108 TYR   B CE1   1 
ATOM   2704 C  CE2   . TYR   B 1 111 ? 34.43167 50.37107 2.77218   1.000 41.35597  ? 108 TYR   B CE2   1 
ATOM   2705 C  CZ    . TYR   B 1 111 ? 35.63581 50.85638 2.30381   1.000 43.39753  ? 108 TYR   B CZ    1 
ATOM   2706 O  OH    . TYR   B 1 111 ? 36.35744 51.73028 3.08481   1.000 44.72629  ? 108 TYR   B OH    1 
ATOM   2707 N  N     . TYR   B 1 112 ? 31.37295 47.40514 -2.44343  1.000 47.13117  ? 109 TYR   B N     1 
ATOM   2708 C  CA    . TYR   B 1 112 ? 30.49186 46.40459 -3.03508  1.000 51.16950  ? 109 TYR   B CA    1 
ATOM   2709 C  C     . TYR   B 1 112 ? 30.84018 46.13808 -4.49302  1.000 56.58906  ? 109 TYR   B C     1 
ATOM   2710 O  O     . TYR   B 1 112 ? 30.72325 44.99949 -4.96254  1.000 54.93630  ? 109 TYR   B O     1 
ATOM   2711 C  CB    . TYR   B 1 112 ? 29.03920 46.86220 -2.90110  1.000 50.87861  ? 109 TYR   B CB    1 
ATOM   2712 C  CG    . TYR   B 1 112 ? 28.02325 45.97423 -3.58343  1.000 52.73444  ? 109 TYR   B CG    1 
ATOM   2713 C  CD1   . TYR   B 1 112 ? 27.89503 44.63553 -3.23689  1.000 49.59090  ? 109 TYR   B CD1   1 
ATOM   2714 C  CD2   . TYR   B 1 112 ? 27.17229 46.48350 -4.55817  1.000 54.84214  ? 109 TYR   B CD2   1 
ATOM   2715 C  CE1   . TYR   B 1 112 ? 26.96088 43.82372 -3.85444  1.000 48.74794  ? 109 TYR   B CE1   1 
ATOM   2716 C  CE2   . TYR   B 1 112 ? 26.23307 45.67998 -5.17947  1.000 54.19088  ? 109 TYR   B CE2   1 
ATOM   2717 C  CZ    . TYR   B 1 112 ? 26.13376 44.35080 -4.82412  1.000 54.07070  ? 109 TYR   B CZ    1 
ATOM   2718 O  OH    . TYR   B 1 112 ? 25.20085 43.54679 -5.43849  1.000 57.56737  ? 109 TYR   B OH    1 
ATOM   2719 N  N     . GLU   B 1 113 ? 31.28122 47.16510 -5.21999  1.000 58.80345  ? 110 GLU   B N     1 
ATOM   2720 C  CA    . GLU   B 1 113 ? 31.64760 46.98843 -6.61829  1.000 61.84250  ? 110 GLU   B CA    1 
ATOM   2721 C  C     . GLU   B 1 113 ? 32.95105 46.21974 -6.79032  1.000 57.46996  ? 110 GLU   B C     1 
ATOM   2722 O  O     . GLU   B 1 113 ? 33.25249 45.78762 -7.90771  1.000 57.51947  ? 110 GLU   B O     1 
ATOM   2723 C  CB    . GLU   B 1 113 ? 31.72899 48.35372 -7.30124  1.000 69.43134  ? 110 GLU   B CB    1 
ATOM   2724 C  CG    . GLU   B 1 113 ? 30.39876 49.09441 -7.30034  1.000 75.77204  ? 110 GLU   B CG    1 
ATOM   2725 C  CD    . GLU   B 1 113 ? 30.49342 50.49080 -7.88105  1.000 82.51763  ? 110 GLU   B CD    1 
ATOM   2726 O  OE1   . GLU   B 1 113 ? 31.60355 50.90145 -8.28064  1.000 85.30531  ? 110 GLU   B OE1   1 
ATOM   2727 O  OE2   . GLU   B 1 113 ? 29.45261 51.18010 -7.93650  1.000 84.80841  ? 110 GLU   B OE2   1 
ATOM   2728 N  N     . ILE   B 1 114 ? 33.72307 46.03578 -5.71806  1.000 53.12122  ? 111 ILE   B N     1 
ATOM   2729 C  CA    . ILE   B 1 114 ? 34.86915 45.13500 -5.77598  1.000 52.20177  ? 111 ILE   B CA    1 
ATOM   2730 C  C     . ILE   B 1 114 ? 34.40239 43.69322 -5.94071  1.000 51.17111  ? 111 ILE   B C     1 
ATOM   2731 O  O     . ILE   B 1 114 ? 35.01538 42.90532 -6.67204  1.000 51.21930  ? 111 ILE   B O     1 
ATOM   2732 C  CB    . ILE   B 1 114 ? 35.74521 45.31085 -4.52085  1.000 51.44372  ? 111 ILE   B CB    1 
ATOM   2733 C  CG1   . ILE   B 1 114 ? 36.43219 46.67996 -4.53020  1.000 50.71614  ? 111 ILE   B CG1   1 
ATOM   2734 C  CG2   . ILE   B 1 114 ? 36.76412 44.18660 -4.40392  1.000 51.24911  ? 111 ILE   B CG2   1 
ATOM   2735 C  CD1   . ILE   B 1 114 ? 37.18043 46.99215 -3.25080  1.000 50.42178  ? 111 ILE   B CD1   1 
ATOM   2736 N  N     . GLY   B 1 115 ? 33.30303 43.32971 -5.28388  1.000 47.74680  ? 112 GLY   B N     1 
ATOM   2737 C  CA    . GLY   B 1 115 ? 32.83720 41.95855 -5.31216  1.000 50.36325  ? 112 GLY   B CA    1 
ATOM   2738 C  C     . GLY   B 1 115 ? 31.69436 41.69152 -6.27080  1.000 53.39881  ? 112 GLY   B C     1 
ATOM   2739 O  O     . GLY   B 1 115 ? 31.38177 40.52877 -6.55073  1.000 52.96172  ? 112 GLY   B O     1 
ATOM   2740 N  N     . LEU   B 1 116 ? 31.06195 42.75114 -6.77814  1.000 51.68608  ? 113 LEU   B N     1 
ATOM   2741 C  CA    . LEU   B 1 116 ? 29.92132 42.56345 -7.67192  1.000 55.19134  ? 113 LEU   B CA    1 
ATOM   2742 C  C     . LEU   B 1 116 ? 30.24166 41.72642 -8.90693  1.000 56.51057  ? 113 LEU   B C     1 
ATOM   2743 O  O     . LEU   B 1 116 ? 29.37834 40.92567 -9.30808  1.000 57.47211  ? 113 LEU   B O     1 
ATOM   2744 C  CB    . LEU   B 1 116 ? 29.34132 43.92354 -8.08271  1.000 57.55138  ? 113 LEU   B CB    1 
ATOM   2745 C  CG    . LEU   B 1 116 ? 28.05095 43.83004 -8.90574  1.000 59.16807  ? 113 LEU   B CG    1 
ATOM   2746 C  CD1   . LEU   B 1 116 ? 26.96005 43.11258 -8.11450  1.000 58.47433  ? 113 LEU   B CD1   1 
ATOM   2747 C  CD2   . LEU   B 1 116 ? 27.57547 45.20280 -9.36203  1.000 58.63715  ? 113 LEU   B CD2   1 
ATOM   2748 N  N     . PRO   B 1 117 ? 31.40859 41.85229 -9.55754  1.000 56.39593  ? 114 PRO   B N     1 
ATOM   2749 C  CA    . PRO   B 1 117 ? 31.70027 40.94347 -10.68034 1.000 54.58554  ? 114 PRO   B CA    1 
ATOM   2750 C  C     . PRO   B 1 117 ? 31.63027 39.47211 -10.30633 1.000 51.98437  ? 114 PRO   B C     1 
ATOM   2751 O  O     . PRO   B 1 117 ? 31.17811 38.65711 -11.11917 1.000 53.91635  ? 114 PRO   B O     1 
ATOM   2752 C  CB    . PRO   B 1 117 ? 33.11521 41.36032 -11.10180 1.000 56.38815  ? 114 PRO   B CB    1 
ATOM   2753 C  CG    . PRO   B 1 117 ? 33.19648 42.78995 -10.73441 1.000 57.39219  ? 114 PRO   B CG    1 
ATOM   2754 C  CD    . PRO   B 1 117 ? 32.42272 42.92058 -9.45382  1.000 55.57698  ? 114 PRO   B CD    1 
ATOM   2755 N  N     . PHE   B 1 118 ? 32.05587 39.10937 -9.09305  1.000 48.72313  ? 115 PHE   B N     1 
ATOM   2756 C  CA    . PHE   B 1 118 ? 31.97150 37.71576 -8.66492  1.000 50.76049  ? 115 PHE   B CA    1 
ATOM   2757 C  C     . PHE   B 1 118 ? 30.53142 37.31454 -8.37275  1.000 49.95234  ? 115 PHE   B C     1 
ATOM   2758 O  O     . PHE   B 1 118 ? 30.12271 36.18544 -8.67032  1.000 50.74189  ? 115 PHE   B O     1 
ATOM   2759 C  CB    . PHE   B 1 118 ? 32.85201 37.48834 -7.43565  1.000 53.57451  ? 115 PHE   B CB    1 
ATOM   2760 C  CG    . PHE   B 1 118 ? 34.29148 37.85396 -7.64913  1.000 53.67069  ? 115 PHE   B CG    1 
ATOM   2761 C  CD1   . PHE   B 1 118 ? 35.17852 36.94132 -8.19463  1.000 54.14250  ? 115 PHE   B CD1   1 
ATOM   2762 C  CD2   . PHE   B 1 118 ? 34.75642 39.11394 -7.31002  1.000 52.98377  ? 115 PHE   B CD2   1 
ATOM   2763 C  CE1   . PHE   B 1 118 ? 36.50373 37.27828 -8.39599  1.000 56.06132  ? 115 PHE   B CE1   1 
ATOM   2764 C  CE2   . PHE   B 1 118 ? 36.07985 39.45656 -7.50749  1.000 53.55487  ? 115 PHE   B CE2   1 
ATOM   2765 C  CZ    . PHE   B 1 118 ? 36.95482 38.53785 -8.05161  1.000 55.64642  ? 115 PHE   B CZ    1 
ATOM   2766 N  N     . ILE   B 1 119 ? 29.75316 38.22178 -7.77825  1.000 51.13509  ? 116 ILE   B N     1 
ATOM   2767 C  CA    . ILE   B 1 119 ? 28.33205 37.96340 -7.56146  1.000 53.91546  ? 116 ILE   B CA    1 
ATOM   2768 C  C     . ILE   B 1 119 ? 27.62504 37.74895 -8.89320  1.000 55.96863  ? 116 ILE   B C     1 
ATOM   2769 O  O     . ILE   B 1 119 ? 26.78655 36.84854 -9.03423  1.000 55.41094  ? 116 ILE   B O     1 
ATOM   2770 C  CB    . ILE   B 1 119 ? 27.69774 39.11892 -6.76370  1.000 54.77413  ? 116 ILE   B CB    1 
ATOM   2771 C  CG1   . ILE   B 1 119 ? 28.33245 39.22547 -5.37418  1.000 55.25037  ? 116 ILE   B CG1   1 
ATOM   2772 C  CG2   . ILE   B 1 119 ? 26.18902 38.94236 -6.66741  1.000 53.76688  ? 116 ILE   B CG2   1 
ATOM   2773 C  CD1   . ILE   B 1 119 ? 27.87038 40.43105 -4.58096  1.000 54.64764  ? 116 ILE   B CD1   1 
ATOM   2774 N  N     . GLN   B 1 120 ? 27.96244 38.56435 -9.89439  1.000 56.27848  ? 117 GLN   B N     1 
ATOM   2775 C  CA    . GLN   B 1 120 ? 27.33599 38.43359 -11.20498 1.000 58.79536  ? 117 GLN   B CA    1 
ATOM   2776 C  C     . GLN   B 1 120 ? 27.75920 37.14106 -11.89254 1.000 60.58623  ? 117 GLN   B C     1 
ATOM   2777 O  O     . GLN   B 1 120 ? 26.92249 36.42295 -12.45250 1.000 59.88990  ? 117 GLN   B O     1 
ATOM   2778 C  CB    . GLN   B 1 120 ? 27.68047 39.64608 -12.06846 1.000 59.22310  ? 117 GLN   B CB    1 
ATOM   2779 C  CG    . GLN   B 1 120 ? 27.07489 40.94807 -11.57082 1.000 59.40289  ? 117 GLN   B CG    1 
ATOM   2780 C  CD    . GLN   B 1 120 ? 27.64271 42.16445 -12.27847 1.000 62.62632  ? 117 GLN   B CD    1 
ATOM   2781 O  OE1   . GLN   B 1 120 ? 28.82831 42.21077 -12.60137 1.000 64.27410  ? 117 GLN   B OE1   1 
ATOM   2782 N  NE2   . GLN   B 1 120 ? 26.79517 43.15578 -12.52582 1.000 64.51671  ? 117 GLN   B NE2   1 
ATOM   2783 N  N     . LYS   B 1 121 ? 29.05802 36.82741 -11.86105 1.000 61.92792  ? 118 LYS   B N     1 
ATOM   2784 C  CA    . LYS   B 1 121 ? 29.53396 35.59496 -12.48334 1.000 60.77908  ? 118 LYS   B CA    1 
ATOM   2785 C  C     . LYS   B 1 121 ? 28.92775 34.36923 -11.81276 1.000 60.34842  ? 118 LYS   B C     1 
ATOM   2786 O  O     . LYS   B 1 121 ? 28.64895 33.36307 -12.47669 1.000 61.68994  ? 118 LYS   B O     1 
ATOM   2787 C  CB    . LYS   B 1 121 ? 31.06067 35.53859 -12.44080 1.000 58.80298  ? 118 LYS   B CB    1 
ATOM   2788 C  CG    . LYS   B 1 121 ? 31.72756 36.53211 -13.37474 1.000 61.05797  ? 118 LYS   B CG    1 
ATOM   2789 C  CD    . LYS   B 1 121 ? 33.24191 36.47558 -13.27929 1.000 62.13834  ? 118 LYS   B CD    1 
ATOM   2790 C  CE    . LYS   B 1 121 ? 33.87842 37.49657 -14.21259 1.000 64.99194  ? 118 LYS   B CE    1 
ATOM   2791 N  NZ    . LYS   B 1 121 ? 35.35167 37.32556 -14.31142 1.000 68.06910  ? 118 LYS   B NZ    1 
ATOM   2792 N  N     . ALA   B 1 122 ? 28.70812 34.43636 -10.49718 1.000 58.23860  ? 119 ALA   B N     1 
ATOM   2793 C  CA    . ALA   B 1 122 ? 27.98174 33.37616 -9.81084  1.000 54.68294  ? 119 ALA   B CA    1 
ATOM   2794 C  C     . ALA   B 1 122 ? 26.51916 33.31311 -10.22697 1.000 55.73169  ? 119 ALA   B C     1 
ATOM   2795 O  O     . ALA   B 1 122 ? 25.85058 32.31929 -9.92449  1.000 57.01346  ? 119 ALA   B O     1 
ATOM   2796 C  CB    . ALA   B 1 122 ? 28.08291 33.56128 -8.29704  1.000 51.18203  ? 119 ALA   B CB    1 
ATOM   2797 N  N     . GLY   B 1 123 ? 26.01060 34.34038 -10.90524 1.000 55.65050  ? 120 GLY   B N     1 
ATOM   2798 C  CA    . GLY   B 1 123 ? 24.64511 34.32324 -11.39355 1.000 56.16460  ? 120 GLY   B CA    1 
ATOM   2799 C  C     . GLY   B 1 123 ? 23.58959 34.51467 -10.32916 1.000 58.54500  ? 120 GLY   B C     1 
ATOM   2800 O  O     . GLY   B 1 123 ? 22.47948 33.99082 -10.46781 1.000 62.08985  ? 120 GLY   B O     1 
ATOM   2801 N  N     . VAL   B 1 124 ? 23.90001 35.26200 -9.27083  1.000 55.96114  ? 121 VAL   B N     1 
ATOM   2802 C  CA    . VAL   B 1 124 ? 22.98757 35.45761 -8.15103  1.000 54.25890  ? 121 VAL   B CA    1 
ATOM   2803 C  C     . VAL   B 1 124 ? 22.66300 36.92223 -7.90328  1.000 52.75389  ? 121 VAL   B C     1 
ATOM   2804 O  O     . VAL   B 1 124 ? 21.97908 37.23198 -6.92144  1.000 49.46809  ? 121 VAL   B O     1 
ATOM   2805 C  CB    . VAL   B 1 124 ? 23.53830 34.81333 -6.86230  1.000 50.49238  ? 121 VAL   B CB    1 
ATOM   2806 C  CG1   . VAL   B 1 124 ? 23.70731 33.31169 -7.04618  1.000 52.27315  ? 121 VAL   B CG1   1 
ATOM   2807 C  CG2   . VAL   B 1 124 ? 24.85601 35.45589 -6.48204  1.000 45.99312  ? 121 VAL   B CG2   1 
ATOM   2808 N  N     . GLU   B 1 125 ? 23.13039 37.83748 -8.75718  1.000 53.18846  ? 122 GLU   B N     1 
ATOM   2809 C  CA    . GLU   B 1 125 ? 22.86055 39.25369 -8.53255  1.000 55.90421  ? 122 GLU   B CA    1 
ATOM   2810 C  C     . GLU   B 1 125 ? 21.36947 39.56774 -8.55606  1.000 55.19354  ? 122 GLU   B C     1 
ATOM   2811 O  O     . GLU   B 1 125 ? 20.94663 40.55918 -7.95117  1.000 53.41111  ? 122 GLU   B O     1 
ATOM   2812 C  CB    . GLU   B 1 125 ? 23.58628 40.11097 -9.57305  1.000 60.73965  ? 122 GLU   B CB    1 
ATOM   2813 C  CG    . GLU   B 1 125 ? 23.62663 41.59590 -9.22077  1.000 64.26167  ? 122 GLU   B CG    1 
ATOM   2814 C  CD    . GLU   B 1 125 ? 24.04747 42.46923 -10.38524 1.000 71.58828  ? 122 GLU   B CD    1 
ATOM   2815 O  OE1   . GLU   B 1 125 ? 23.97626 42.00016 -11.54116 1.000 74.67465  ? 122 GLU   B OE1   1 
ATOM   2816 O  OE2   . GLU   B 1 125 ? 24.44905 43.62757 -10.14438 1.000 73.75648  ? 122 GLU   B OE2   1 
ATOM   2817 N  N     . HIS   B 1 126 ? 20.56160 38.73898 -9.22336  1.000 54.90538  ? 123 HIS   B N     1 
ATOM   2818 C  CA    . HIS   B 1 126 ? 19.12418 38.98383 -9.28134  1.000 56.29772  ? 123 HIS   B CA    1 
ATOM   2819 C  C     . HIS   B 1 126 ? 18.45705 38.85921 -7.91604  1.000 51.55302  ? 123 HIS   B C     1 
ATOM   2820 O  O     . HIS   B 1 126 ? 17.33549 39.34666 -7.74006  1.000 51.02456  ? 123 HIS   B O     1 
ATOM   2821 C  CB    . HIS   B 1 126 ? 18.46556 38.02208 -10.27663 1.000 57.56360  ? 123 HIS   B CB    1 
ATOM   2822 C  CG    . HIS   B 1 126 ? 18.39006 36.60654 -9.79324  1.000 57.67778  ? 123 HIS   B CG    1 
ATOM   2823 N  ND1   . HIS   B 1 126 ? 19.41388 35.70074 -9.97219  1.000 57.05004  ? 123 HIS   B ND1   1 
ATOM   2824 C  CD2   . HIS   B 1 126 ? 17.40948 35.94089 -9.13784  1.000 57.17498  ? 123 HIS   B CD2   1 
ATOM   2825 C  CE1   . HIS   B 1 126 ? 19.06776 34.53890 -9.44620  1.000 56.92896  ? 123 HIS   B CE1   1 
ATOM   2826 N  NE2   . HIS   B 1 126 ? 17.85657 34.65836 -8.93236  1.000 56.78194  ? 123 HIS   B NE2   1 
ATOM   2827 N  N     . LYS   B 1 127 ? 19.11841 38.22620 -6.94718  1.000 53.07876  ? 124 LYS   B N     1 
ATOM   2828 C  CA    . LYS   B 1 127 ? 18.55643 38.06468 -5.61129  1.000 55.34027  ? 124 LYS   B CA    1 
ATOM   2829 C  C     . LYS   B 1 127 ? 18.78745 39.26976 -4.70745  1.000 53.91657  ? 124 LYS   B C     1 
ATOM   2830 O  O     . LYS   B 1 127 ? 18.22417 39.31261 -3.60879  1.000 55.67563  ? 124 LYS   B O     1 
ATOM   2831 C  CB    . LYS   B 1 127 ? 19.14974 36.82512 -4.93191  1.000 52.86197  ? 124 LYS   B CB    1 
ATOM   2832 C  CG    . LYS   B 1 127 ? 19.01286 35.53148 -5.71499  1.000 53.01995  ? 124 LYS   B CG    1 
ATOM   2833 C  CD    . LYS   B 1 127 ? 19.49858 34.34966 -4.88116  1.000 51.44265  ? 124 LYS   B CD    1 
ATOM   2834 C  CE    . LYS   B 1 127 ? 19.49752 33.05447 -5.67902  1.000 51.74567  ? 124 LYS   B CE    1 
ATOM   2835 N  NZ    . LYS   B 1 127 ? 19.88313 31.88493 -4.83861  1.000 50.92584  ? 124 LYS   B NZ    1 
ATOM   2836 N  N     . ILE   B 1 128 ? 19.58524 40.24462 -5.13256  1.000 54.40587  ? 125 ILE   B N     1 
ATOM   2837 C  CA    . ILE   B 1 128 ? 20.12755 41.26419 -4.24182  1.000 54.01945  ? 125 ILE   B CA    1 
ATOM   2838 C  C     . ILE   B 1 128 ? 19.51087 42.61653 -4.57232  1.000 54.93449  ? 125 ILE   B C     1 
ATOM   2839 O  O     . ILE   B 1 128 ? 19.50891 43.04389 -5.73359  1.000 56.85810  ? 125 ILE   B O     1 
ATOM   2840 C  CB    . ILE   B 1 128 ? 21.66186 41.32343 -4.33750  1.000 53.22822  ? 125 ILE   B CB    1 
ATOM   2841 C  CG1   . ILE   B 1 128 ? 22.26571 39.97826 -3.93205  1.000 49.61290  ? 125 ILE   B CG1   1 
ATOM   2842 C  CG2   . ILE   B 1 128 ? 22.20969 42.44988 -3.47392  1.000 53.62305  ? 125 ILE   B CG2   1 
ATOM   2843 C  CD1   . ILE   B 1 128 ? 23.76931 39.91654 -4.06687  1.000 48.01818  ? 125 ILE   B CD1   1 
ATOM   2844 N  N     . ASN   B 1 129 ? 18.99390 43.28753 -3.54703  1.000 52.36716  ? 126 ASN   B N     1 
ATOM   2845 C  CA    . ASN   B 1 129 ? 18.58076 44.68604 -3.61917  1.000 52.06866  ? 126 ASN   B CA    1 
ATOM   2846 C  C     . ASN   B 1 129 ? 19.53960 45.46534 -2.72442  1.000 51.39248  ? 126 ASN   B C     1 
ATOM   2847 O  O     . ASN   B 1 129 ? 19.41948 45.43422 -1.49642  1.000 50.90025  ? 126 ASN   B O     1 
ATOM   2848 C  CB    . ASN   B 1 129 ? 17.12783 44.85741 -3.18115  1.000 51.20354  ? 126 ASN   B CB    1 
ATOM   2849 C  CG    . ASN   B 1 129 ? 16.71169 46.31521 -3.09049  1.000 53.76603  ? 126 ASN   B CG    1 
ATOM   2850 O  OD1   . ASN   B 1 129 ? 17.28756 47.18100 -3.74920  1.000 58.04795  ? 126 ASN   B OD1   1 
ATOM   2851 N  ND2   . ASN   B 1 129 ? 15.70881 46.59345 -2.26591  1.000 51.67746  ? 126 ASN   B ND2   1 
ATOM   2852 N  N     . PHE   B 1 130 ? 20.49954 46.15028 -3.33918  1.000 53.69700  ? 127 PHE   B N     1 
ATOM   2853 C  CA    . PHE   B 1 130 ? 21.51577 46.88259 -2.59569  1.000 53.77019  ? 127 PHE   B CA    1 
ATOM   2854 C  C     . PHE   B 1 130 ? 21.07254 48.32126 -2.36911  1.000 53.30217  ? 127 PHE   B C     1 
ATOM   2855 O  O     . PHE   B 1 130 ? 20.57131 48.98434 -3.28156  1.000 54.15364  ? 127 PHE   B O     1 
ATOM   2856 C  CB    . PHE   B 1 130 ? 22.85575 46.85823 -3.33452  1.000 55.75647  ? 127 PHE   B CB    1 
ATOM   2857 C  CG    . PHE   B 1 130 ? 24.00566 47.38940 -2.52470  1.000 56.63825  ? 127 PHE   B CG    1 
ATOM   2858 C  CD1   . PHE   B 1 130 ? 24.30056 48.74389 -2.51798  1.000 59.22535  ? 127 PHE   B CD1   1 
ATOM   2859 C  CD2   . PHE   B 1 130 ? 24.79477 46.53275 -1.77340  1.000 55.18957  ? 127 PHE   B CD2   1 
ATOM   2860 C  CE1   . PHE   B 1 130 ? 25.35599 49.23484 -1.77231  1.000 60.89576  ? 127 PHE   B CE1   1 
ATOM   2861 C  CE2   . PHE   B 1 130 ? 25.85385 47.01715 -1.02712  1.000 56.57286  ? 127 PHE   B CE2   1 
ATOM   2862 C  CZ    . PHE   B 1 130 ? 26.13493 48.37053 -1.02645  1.000 58.48517  ? 127 PHE   B CZ    1 
ATOM   2863 N  N     . ILE   B 1 131 ? 21.27074 48.80042 -1.14502  1.000 51.64088  ? 128 ILE   B N     1 
ATOM   2864 C  CA    . ILE   B 1 131 ? 20.87620 50.14380 -0.73923  1.000 52.50616  ? 128 ILE   B CA    1 
ATOM   2865 C  C     . ILE   B 1 131 ? 22.10194 50.82196 -0.14404  1.000 50.90477  ? 128 ILE   B C     1 
ATOM   2866 O  O     . ILE   B 1 131 ? 22.60355 50.39592 0.90421   1.000 51.12274  ? 128 ILE   B O     1 
ATOM   2867 C  CB    . ILE   B 1 131 ? 19.71798 50.12635 0.26739   1.000 53.30963  ? 128 ILE   B CB    1 
ATOM   2868 C  CG1   . ILE   B 1 131 ? 18.45545 49.55195 -0.38281  1.000 55.26467  ? 128 ILE   B CG1   1 
ATOM   2869 C  CG2   . ILE   B 1 131 ? 19.46634 51.52394 0.81218   1.000 54.71761  ? 128 ILE   B CG2   1 
ATOM   2870 C  CD1   . ILE   B 1 131 ? 17.31212 49.33216 0.58466   1.000 55.72680  ? 128 ILE   B CD1   1 
ATOM   2871 N  N     . GLU   B 1 132 ? 22.58918 51.86881 -0.80752  1.000 49.65631  ? 129 GLU   B N     1 
ATOM   2872 C  CA    . GLU   B 1 132 ? 23.74985 52.61725 -0.32714  1.000 51.13821  ? 129 GLU   B CA    1 
ATOM   2873 C  C     . GLU   B 1 132 ? 23.25881 53.67816 0.64864   1.000 52.99519  ? 129 GLU   B C     1 
ATOM   2874 O  O     . GLU   B 1 132 ? 22.85073 54.76940 0.24571   1.000 56.06991  ? 129 GLU   B O     1 
ATOM   2875 C  CB    . GLU   B 1 132 ? 24.52224 53.24030 -1.48399  1.000 51.98297  ? 129 GLU   B CB    1 
ATOM   2876 C  CG    . GLU   B 1 132 ? 25.78556 53.96062 -1.03833  1.000 57.09776  ? 129 GLU   B CG    1 
ATOM   2877 C  CD    . GLU   B 1 132 ? 26.52254 54.63210 -2.18013  1.000 61.34907  ? 129 GLU   B CD    1 
ATOM   2878 O  OE1   . GLU   B 1 132 ? 25.87843 54.96393 -3.19943  1.000 63.16431  ? 129 GLU   B OE1   1 
ATOM   2879 O  OE2   . GLU   B 1 132 ? 27.75157 54.82618 -2.05614  1.000 61.71636  ? 129 GLU   B OE2   1 
ATOM   2880 N  N     . SER   B 1 133 ? 23.30441 53.35987 1.93861   1.000 53.00864  ? 130 SER   B N     1 
ATOM   2881 C  CA    . SER   B 1 133 ? 22.80637 54.25968 2.96935   1.000 53.36172  ? 130 SER   B CA    1 
ATOM   2882 C  C     . SER   B 1 133 ? 23.35597 53.81551 4.31607   1.000 54.08302  ? 130 SER   B C     1 
ATOM   2883 O  O     . SER   B 1 133 ? 23.94829 52.74071 4.44697   1.000 54.04070  ? 130 SER   B O     1 
ATOM   2884 C  CB    . SER   B 1 133 ? 21.27341 54.28358 2.99248   1.000 53.28561  ? 130 SER   B CB    1 
ATOM   2885 O  OG    . SER   B 1 133 ? 20.78655 54.86669 4.18998   1.000 54.41885  ? 130 SER   B OG    1 
ATOM   2886 N  N     . GLU   B 1 134 ? 23.16111 54.66777 5.31804   1.000 54.63187  ? 131 GLU   B N     1 
ATOM   2887 C  CA    . GLU   B 1 134 ? 23.34076 54.23073 6.69200   1.000 53.83904  ? 131 GLU   B CA    1 
ATOM   2888 C  C     . GLU   B 1 134 ? 22.21163 53.27729 7.06280   1.000 51.37673  ? 131 GLU   B C     1 
ATOM   2889 O  O     . GLU   B 1 134 ? 21.07852 53.41002 6.59126   1.000 48.41826  ? 131 GLU   B O     1 
ATOM   2890 C  CB    . GLU   B 1 134 ? 23.37845 55.42716 7.64305   1.000 58.20998  ? 131 GLU   B CB    1 
ATOM   2891 C  CG    . GLU   B 1 134 ? 24.45170 56.45086 7.29811   1.000 64.73594  ? 131 GLU   B CG    1 
ATOM   2892 C  CD    . GLU   B 1 134 ? 24.74693 57.40077 8.44161   1.000 68.33426  ? 131 GLU   B CD    1 
ATOM   2893 O  OE1   . GLU   B 1 134 ? 24.51978 57.01619 9.60646   1.000 69.72756  ? 131 GLU   B OE1   1 
ATOM   2894 O  OE2   . GLU   B 1 134 ? 25.20696 58.53104 8.17653   1.000 71.08012  ? 131 GLU   B OE2   1 
ATOM   2895 N  N     . ALA   B 1 135 ? 22.53615 52.29498 7.90520   1.000 50.52678  ? 132 ALA   B N     1 
ATOM   2896 C  CA    . ALA   B 1 135 ? 21.60760 51.19508 8.14518   1.000 49.74240  ? 132 ALA   B CA    1 
ATOM   2897 C  C     . ALA   B 1 135 ? 20.37359 51.65152 8.91409   1.000 49.30730  ? 132 ALA   B C     1 
ATOM   2898 O  O     . ALA   B 1 135 ? 19.24785 51.27955 8.56085   1.000 49.02668  ? 132 ALA   B O     1 
ATOM   2899 C  CB    . ALA   B 1 135 ? 22.31799 50.06963 8.89117   1.000 50.06900  ? 132 ALA   B CB    1 
ATOM   2900 N  N     . LEU   B 1 136 ? 20.56273 52.45466 9.96533   1.000 49.25284  ? 133 LEU   B N     1 
ATOM   2901 C  CA    . LEU   B 1 136 ? 19.44386 52.83432 10.82694  1.000 48.44981  ? 133 LEU   B CA    1 
ATOM   2902 C  C     . LEU   B 1 136 ? 18.29678 53.50818 10.08145  1.000 50.29864  ? 133 LEU   B C     1 
ATOM   2903 O  O     . LEU   B 1 136 ? 17.13854 53.11906 10.30685  1.000 49.32223  ? 133 LEU   B O     1 
ATOM   2904 C  CB    . LEU   B 1 136 ? 19.94430 53.71999 11.97265  1.000 49.29015  ? 133 LEU   B CB    1 
ATOM   2905 C  CG    . LEU   B 1 136 ? 20.30860 53.03493 13.29056  1.000 53.40015  ? 133 LEU   B CG    1 
ATOM   2906 C  CD1   . LEU   B 1 136 ? 20.55163 54.08010 14.37614  1.000 55.73557  ? 133 LEU   B CD1   1 
ATOM   2907 C  CD2   . LEU   B 1 136 ? 19.22516 52.05197 13.71962  1.000 52.12308  ? 133 LEU   B CD2   1 
ATOM   2908 N  N     . PRO   B 1 137 ? 18.52204 54.50916 9.21601   1.000 51.84683  ? 134 PRO   B N     1 
ATOM   2909 C  CA    . PRO   B 1 137 ? 17.36879 55.13306 8.54090   1.000 50.83492  ? 134 PRO   B CA    1 
ATOM   2910 C  C     . PRO   B 1 137 ? 16.58089 54.16441 7.68022   1.000 51.28160  ? 134 PRO   B C     1 
ATOM   2911 O  O     . PRO   B 1 137 ? 15.35148 54.27247 7.59968   1.000 53.78813  ? 134 PRO   B O     1 
ATOM   2912 C  CB    . PRO   B 1 137 ? 18.01568 56.24291 7.70048   1.000 51.44074  ? 134 PRO   B CB    1 
ATOM   2913 C  CG    . PRO   B 1 137 ? 19.30683 56.52487 8.37210   1.000 50.69997  ? 134 PRO   B CG    1 
ATOM   2914 C  CD    . PRO   B 1 137 ? 19.77923 55.20541 8.88645   1.000 50.38440  ? 134 PRO   B CD    1 
ATOM   2915 N  N     . VAL   B 1 138 ? 17.25672 53.21410 7.03370   1.000 53.04581  ? 135 VAL   B N     1 
ATOM   2916 C  CA    . VAL   B 1 138 ? 16.55690 52.23623 6.20715   1.000 52.69653  ? 135 VAL   B CA    1 
ATOM   2917 C  C     . VAL   B 1 138 ? 15.71067 51.31557 7.07817   1.000 51.01023  ? 135 VAL   B C     1 
ATOM   2918 O  O     . VAL   B 1 138 ? 14.54859 51.03152 6.76352   1.000 52.61800  ? 135 VAL   B O     1 
ATOM   2919 C  CB    . VAL   B 1 138 ? 17.56061 51.44187 5.35162   1.000 52.18653  ? 135 VAL   B CB    1 
ATOM   2920 C  CG1   . VAL   B 1 138 ? 16.83094 50.64092 4.28714   1.000 53.58540  ? 135 VAL   B CG1   1 
ATOM   2921 C  CG2   . VAL   B 1 138 ? 18.57696 52.37770 4.71767   1.000 51.37044  ? 135 VAL   B CG2   1 
ATOM   2922 N  N     . LEU   B 1 139 ? 16.28283 50.83692 8.18768   1.000 49.03483  ? 136 LEU   B N     1 
ATOM   2923 C  CA    . LEU   B 1 139 ? 15.53504 49.96847 9.09161   1.000 49.27024  ? 136 LEU   B CA    1 
ATOM   2924 C  C     . LEU   B 1 139 ? 14.31710 50.68469 9.65941   1.000 49.16606  ? 136 LEU   B C     1 
ATOM   2925 O  O     . LEU   B 1 139 ? 13.24665 50.08241 9.80820   1.000 46.51015  ? 136 LEU   B O     1 
ATOM   2926 C  CB    . LEU   B 1 139 ? 16.43991 49.47722 10.22126  1.000 48.91832  ? 136 LEU   B CB    1 
ATOM   2927 C  CG    . LEU   B 1 139 ? 17.69502 48.70294 9.81559   1.000 48.61946  ? 136 LEU   B CG    1 
ATOM   2928 C  CD1   . LEU   B 1 139 ? 18.46303 48.23763 11.04647  1.000 44.82105  ? 136 LEU   B CD1   1 
ATOM   2929 C  CD2   . LEU   B 1 139 ? 17.32605 47.52502 8.93163   1.000 48.83744  ? 136 LEU   B CD2   1 
ATOM   2930 N  N     . ASP   B 1 140 ? 14.46076 51.97292 9.98326   1.000 49.80581  ? 137 ASP   B N     1 
ATOM   2931 C  CA    . ASP   B 1 140 ? 13.32289 52.73696 10.48374  1.000 51.65387  ? 137 ASP   B CA    1 
ATOM   2932 C  C     . ASP   B 1 140 ? 12.25857 52.91069 9.40722   1.000 53.58259  ? 137 ASP   B C     1 
ATOM   2933 O  O     . ASP   B 1 140 ? 11.05801 52.83789 9.69625   1.000 50.78124  ? 137 ASP   B O     1 
ATOM   2934 C  CB    . ASP   B 1 140 ? 13.78912 54.09489 11.00710  1.000 51.65746  ? 137 ASP   B CB    1 
ATOM   2935 C  CG    . ASP   B 1 140 ? 14.32212 54.02147 12.42450  1.000 53.08720  ? 137 ASP   B CG    1 
ATOM   2936 O  OD1   . ASP   B 1 140 ? 14.23832 52.93668 13.03758  1.000 52.74071  ? 137 ASP   B OD1   1 
ATOM   2937 O  OD2   . ASP   B 1 140 ? 14.82071 55.05086 12.92839  1.000 56.40157  ? 137 ASP   B OD2   1 
ATOM   2938 N  N     . GLN   B 1 141 ? 12.67760 53.14519 8.16075   1.000 56.40048  ? 138 GLN   B N     1 
ATOM   2939 C  CA    . GLN   B 1 141 ? 11.71601 53.21801 7.06720   1.000 60.32780  ? 138 GLN   B CA    1 
ATOM   2940 C  C     . GLN   B 1 141 ? 11.07040 51.86362 6.80803   1.000 60.13540  ? 138 GLN   B C     1 
ATOM   2941 O  O     . GLN   B 1 141 ? 9.89616  51.80044 6.42584   1.000 60.88187  ? 138 GLN   B O     1 
ATOM   2942 C  CB    . GLN   B 1 141 ? 12.39588 53.73825 5.80078   1.000 65.13388  ? 138 GLN   B CB    1 
ATOM   2943 C  CG    . GLN   B 1 141 ? 11.45470 53.93102 4.62348   1.000 73.05692  ? 138 GLN   B CG    1 
ATOM   2944 C  CD    . GLN   B 1 141 ? 11.94199 53.23041 3.36906   1.000 79.76446  ? 138 GLN   B CD    1 
ATOM   2945 O  OE1   . GLN   B 1 141 ? 11.95039 51.99919 3.29294   1.000 79.55223  ? 138 GLN   B OE1   1 
ATOM   2946 N  NE2   . GLN   B 1 141 ? 12.35521 54.01351 2.37675   1.000 83.10371  ? 138 GLN   B NE2   1 
ATOM   2947 N  N     . MET   B 1 142 ? 11.81621 50.77374 7.01293   1.000 60.66887  ? 139 MET   B N     1 
ATOM   2948 C  CA    . MET   B 1 142 ? 11.23259 49.44400 6.87856   1.000 61.05893  ? 139 MET   B CA    1 
ATOM   2949 C  C     . MET   B 1 142 ? 10.16170 49.18987 7.93025   1.000 60.22764  ? 139 MET   B C     1 
ATOM   2950 O  O     . MET   B 1 142 ? 9.19060  48.47867 7.65794   1.000 59.98559  ? 139 MET   B O     1 
ATOM   2951 C  CB    . MET   B 1 142 ? 12.31923 48.37486 6.97342   1.000 59.69431  ? 139 MET   B CB    1 
ATOM   2952 C  CG    . MET   B 1 142 ? 13.23260 48.30272 5.76815   1.000 60.47929  ? 139 MET   B CG    1 
ATOM   2953 S  SD    . MET   B 1 142 ? 14.51247 47.05730 5.98866   1.000 58.91110  ? 139 MET   B SD    1 
ATOM   2954 C  CE    . MET   B 1 142 ? 15.46913 47.28672 4.49807   1.000 59.79361  ? 139 MET   B CE    1 
ATOM   2955 N  N     . LEU   B 1 143 ? 10.31690 49.75807 9.12933   1.000 58.92673  ? 140 LEU   B N     1 
ATOM   2956 C  CA    . LEU   B 1 143 ? 9.33935  49.52886 10.18832  1.000 59.58920  ? 140 LEU   B CA    1 
ATOM   2957 C  C     . LEU   B 1 143 ? 7.97345  50.10562 9.83799   1.000 65.41820  ? 140 LEU   B C     1 
ATOM   2958 O  O     . LEU   B 1 143 ? 6.94939  49.57150 10.27873  1.000 67.39839  ? 140 LEU   B O     1 
ATOM   2959 C  CB    . LEU   B 1 143 ? 9.84034  50.11939 11.50679  1.000 56.65360  ? 140 LEU   B CB    1 
ATOM   2960 C  CG    . LEU   B 1 143 ? 10.79966 49.25351 12.32266  1.000 56.08072  ? 140 LEU   B CG    1 
ATOM   2961 C  CD1   . LEU   B 1 143 ? 11.20713 49.96956 13.59775  1.000 56.37910  ? 140 LEU   B CD1   1 
ATOM   2962 C  CD2   . LEU   B 1 143 ? 10.15864 47.91541 12.64661  1.000 56.00170  ? 140 LEU   B CD2   1 
ATOM   2963 N  N     . GLU   B 1 144 ? 7.93224  51.18457 9.05201   1.000 69.59643  ? 141 GLU   B N     1 
ATOM   2964 C  CA    . GLU   B 1 144 ? 6.65346  51.78654 8.69180   1.000 76.39899  ? 141 GLU   B CA    1 
ATOM   2965 C  C     . GLU   B 1 144 ? 5.97021  51.05036 7.54716   1.000 80.48076  ? 141 GLU   B C     1 
ATOM   2966 O  O     . GLU   B 1 144 ? 4.73749  50.98091 7.51297   1.000 83.55182  ? 141 GLU   B O     1 
ATOM   2967 C  CB    . GLU   B 1 144 ? 6.84787  53.25653 8.32306   1.000 78.86558  ? 141 GLU   B CB    1 
ATOM   2968 C  CG    . GLU   B 1 144 ? 7.02485  54.17010 9.52338   1.000 83.06393  ? 141 GLU   B CG    1 
ATOM   2969 C  CD    . GLU   B 1 144 ? 8.27455  55.02236 9.43005   1.000 88.59244  ? 141 GLU   B CD    1 
ATOM   2970 O  OE1   . GLU   B 1 144 ? 8.56424  55.76384 10.39444  1.000 90.49049  ? 141 GLU   B OE1   1 
ATOM   2971 O  OE2   . GLU   B 1 144 ? 8.96890  54.94882 8.39319   1.000 90.49300  ? 141 GLU   B OE2   1 
ATOM   2972 N  N     . GLU   B 1 145 ? 6.73968  50.49284 6.61197   1.000 82.05102  ? 142 GLU   B N     1 
ATOM   2973 C  CA    . GLU   B 1 145 ? 6.16435  49.83026 5.44883   1.000 84.13409  ? 142 GLU   B CA    1 
ATOM   2974 C  C     . GLU   B 1 145 ? 6.00595  48.32753 5.62711   1.000 84.54295  ? 142 GLU   B C     1 
ATOM   2975 O  O     . GLU   B 1 145 ? 5.23781  47.71099 4.88023   1.000 86.49740  ? 142 GLU   B O     1 
ATOM   2976 C  CB    . GLU   B 1 145 ? 7.02688  50.08963 4.21012   1.000 86.68593  ? 142 GLU   B CB    1 
ATOM   2977 C  CG    . GLU   B 1 145 ? 7.52295  51.51561 4.07380   1.000 91.19600  ? 142 GLU   B CG    1 
ATOM   2978 C  CD    . GLU   B 1 145 ? 8.33883  51.72594 2.81088   1.000 95.29167  ? 142 GLU   B CD    1 
ATOM   2979 O  OE1   . GLU   B 1 145 ? 8.25791  52.82735 2.22834   1.000 97.33042  ? 142 GLU   B OE1   1 
ATOM   2980 O  OE2   . GLU   B 1 145 ? 9.05397  50.78802 2.39592   1.000 95.90516  ? 142 GLU   B OE2   1 
ATOM   2981 N  N     . MET   B 1 146 ? 6.70705  47.73112 6.59028   1.000 83.36340  ? 143 MET   B N     1 
ATOM   2982 C  CA    . MET   B 1 146 ? 6.71386  46.28097 6.73970   1.000 82.07548  ? 143 MET   B CA    1 
ATOM   2983 C  C     . MET   B 1 146 ? 5.31298  45.74918 7.00803   1.000 78.79905  ? 143 MET   B C     1 
ATOM   2984 O  O     . MET   B 1 146 ? 4.60093  46.24350 7.88668   1.000 76.18367  ? 143 MET   B O     1 
ATOM   2985 C  CB    . MET   B 1 146 ? 7.65042  45.87402 7.87787   1.000 84.39669  ? 143 MET   B CB    1 
ATOM   2986 C  CG    . MET   B 1 146 ? 7.85230  44.37196 8.04039   1.000 89.34922  ? 143 MET   B CG    1 
ATOM   2987 S  SD    . MET   B 1 146 ? 8.82721  43.62738 6.71461   1.000 92.24204  ? 143 MET   B SD    1 
ATOM   2988 C  CE    . MET   B 1 146 ? 10.17054 44.80321 6.56246   1.000 89.71236  ? 143 MET   B CE    1 
ATOM   2989 N  N     . LYS   B 1 147 ? 4.92120  44.74217 6.23842   1.000 79.74328  ? 144 LYS   B N     1 
ATOM   2990 C  CA    . LYS   B 1 147 ? 3.70594  43.98505 6.48343   1.000 81.35923  ? 144 LYS   B CA    1 
ATOM   2991 C  C     . LYS   B 1 147 ? 4.06174  42.68569 7.19318   1.000 80.60573  ? 144 LYS   B C     1 
ATOM   2992 O  O     . LYS   B 1 147 ? 5.16247  42.15396 7.02888   1.000 80.19029  ? 144 LYS   B O     1 
ATOM   2993 C  CB    . LYS   B 1 147 ? 2.96966  43.69964 5.17255   1.000 84.47239  ? 144 LYS   B CB    1 
ATOM   2994 C  CG    . LYS   B 1 147 ? 2.31036  44.93132 4.56472   1.000 85.06838  ? 144 LYS   B CG    1 
ATOM   2995 C  CD    . LYS   B 1 147 ? 2.47103  44.98183 3.05138   1.000 86.38185  ? 144 LYS   B CD    1 
ATOM   2996 C  CE    . LYS   B 1 147 ? 3.90184  45.31641 2.65119   1.000 86.01936  ? 144 LYS   B CE    1 
ATOM   2997 N  NZ    . LYS   B 1 147 ? 4.00511  45.70664 1.21377   1.000 87.13908  ? 144 LYS   B NZ    1 
ATOM   2998 N  N     . GLU   B 1 148 ? 3.11983  42.18466 7.99751   1.000 83.70563  ? 145 GLU   B N     1 
ATOM   2999 C  CA    . GLU   B 1 148 ? 3.39079  41.00312 8.81228   1.000 85.46766  ? 145 GLU   B CA    1 
ATOM   3000 C  C     . GLU   B 1 148 ? 3.82727  39.81949 7.95646   1.000 84.42168  ? 145 GLU   B C     1 
ATOM   3001 O  O     . GLU   B 1 148 ? 4.67927  39.02398 8.37010   1.000 81.27014  ? 145 GLU   B O     1 
ATOM   3002 C  CB    . GLU   B 1 148 ? 2.15729  40.64661 9.64423   1.000 90.36771  ? 145 GLU   B CB    1 
ATOM   3003 C  CG    . GLU   B 1 148 ? 2.29289  39.35858 10.44339  1.000 94.64430  ? 145 GLU   B CG    1 
ATOM   3004 C  CD    . GLU   B 1 148 ? 1.56033  39.41340 11.77063  1.000 98.77407  ? 145 GLU   B CD    1 
ATOM   3005 O  OE1   . GLU   B 1 148 ? 1.94588  40.23556 12.62942  1.000 99.46507  ? 145 GLU   B OE1   1 
ATOM   3006 O  OE2   . GLU   B 1 148 ? 0.59561  38.64086 11.95330  1.000 100.49048 ? 145 GLU   B OE2   1 
ATOM   3007 N  N     . GLU   B 1 149 ? 3.27283  39.69777 6.75151   1.000 86.83434  ? 146 GLU   B N     1 
ATOM   3008 C  CA    . GLU   B 1 149 ? 3.66644  38.62687 5.84544   1.000 88.57565  ? 146 GLU   B CA    1 
ATOM   3009 C  C     . GLU   B 1 149 ? 4.96653  38.92069 5.10600   1.000 83.95593  ? 146 GLU   B C     1 
ATOM   3010 O  O     . GLU   B 1 149 ? 5.39902  38.09070 4.29939   1.000 86.01607  ? 146 GLU   B O     1 
ATOM   3011 C  CB    . GLU   B 1 149 ? 2.54952  38.34875 4.83196   1.000 95.01099  ? 146 GLU   B CB    1 
ATOM   3012 C  CG    . GLU   B 1 149 ? 2.36834  39.42475 3.76760   1.000 99.93857  ? 146 GLU   B CG    1 
ATOM   3013 C  CD    . GLU   B 1 149 ? 1.42029  40.53111 4.19479   1.000 104.10393 ? 146 GLU   B CD    1 
ATOM   3014 O  OE1   . GLU   B 1 149 ? 1.01878  40.55372 5.37786   1.000 104.69007 ? 146 GLU   B OE1   1 
ATOM   3015 O  OE2   . GLU   B 1 149 ? 1.06971  41.37598 3.34228   1.000 105.56645 ? 146 GLU   B OE2   1 
ATOM   3016 N  N     . ASP   B 1 150 ? 5.59889  40.06767 5.35653   1.000 77.84807  ? 147 ASP   B N     1 
ATOM   3017 C  CA    . ASP   B 1 150 ? 6.83858  40.44194 4.68632   1.000 73.89993  ? 147 ASP   B CA    1 
ATOM   3018 C  C     . ASP   B 1 150 ? 8.05165  40.39959 5.60874   1.000 65.89108  ? 147 ASP   B C     1 
ATOM   3019 O  O     . ASP   B 1 150 ? 9.13242  40.84808 5.21180   1.000 62.09575  ? 147 ASP   B O     1 
ATOM   3020 C  CB    . ASP   B 1 150 ? 6.70998  41.83643 4.06930   1.000 78.50675  ? 147 ASP   B CB    1 
ATOM   3021 C  CG    . ASP   B 1 150 ? 5.79834  41.85759 2.86050   1.000 84.05858  ? 147 ASP   B CG    1 
ATOM   3022 O  OD1   . ASP   B 1 150 ? 5.00549  40.90782 2.69378   1.000 85.42362  ? 147 ASP   B OD1   1 
ATOM   3023 O  OD2   . ASP   B 1 150 ? 5.88358  42.82031 2.06950   1.000 85.83163  ? 147 ASP   B OD2   1 
ATOM   3024 N  N     . LEU   B 1 151 ? 7.90328  39.87246 6.82188   1.000 60.86969  ? 148 LEU   B N     1 
ATOM   3025 C  CA    . LEU   B 1 151 ? 9.00911  39.84077 7.76892   1.000 53.29659  ? 148 LEU   B CA    1 
ATOM   3026 C  C     . LEU   B 1 151 ? 10.14460 38.96315 7.25038   1.000 49.50047  ? 148 LEU   B C     1 
ATOM   3027 O  O     . LEU   B 1 151 ? 9.92758  37.98320 6.53270   1.000 49.82376  ? 148 LEU   B O     1 
ATOM   3028 C  CB    . LEU   B 1 151 ? 8.52505  39.33179 9.12662   1.000 52.36029  ? 148 LEU   B CB    1 
ATOM   3029 C  CG    . LEU   B 1 151 ? 7.56020  40.24840 9.87755   1.000 54.71955  ? 148 LEU   B CG    1 
ATOM   3030 C  CD1   . LEU   B 1 151 ? 6.93116  39.52052 11.05519  1.000 57.29582  ? 148 LEU   B CD1   1 
ATOM   3031 C  CD2   . LEU   B 1 151 ? 8.27857  41.49978 10.34861  1.000 54.05409  ? 148 LEU   B CD2   1 
ATOM   3032 N  N     . TYR   B 1 152 ? 11.36954 39.32774 7.62243   1.000 46.21464  ? 149 TYR   B N     1 
ATOM   3033 C  CA    . TYR   B 1 152 ? 12.54721 38.59660 7.18195   1.000 44.49414  ? 149 TYR   B CA    1 
ATOM   3034 C  C     . TYR   B 1 152 ? 12.73922 37.32607 8.00149   1.000 43.55663  ? 149 TYR   B C     1 
ATOM   3035 O  O     . TYR   B 1 152 ? 12.41061 37.26894 9.19039   1.000 41.97790  ? 149 TYR   B O     1 
ATOM   3036 C  CB    . TYR   B 1 152 ? 13.79806 39.47169 7.29136   1.000 43.83216  ? 149 TYR   B CB    1 
ATOM   3037 C  CG    . TYR   B 1 152 ? 13.83362 40.62364 6.31488   1.000 45.38247  ? 149 TYR   B CG    1 
ATOM   3038 C  CD1   . TYR   B 1 152 ? 14.35045 40.45689 5.03748   1.000 47.34146  ? 149 TYR   B CD1   1 
ATOM   3039 C  CD2   . TYR   B 1 152 ? 13.35442 41.87851 6.67014   1.000 50.65639  ? 149 TYR   B CD2   1 
ATOM   3040 C  CE1   . TYR   B 1 152 ? 14.38413 41.50321 4.13664   1.000 52.43455  ? 149 TYR   B CE1   1 
ATOM   3041 C  CE2   . TYR   B 1 152 ? 13.38450 42.93546 5.77526   1.000 53.94558  ? 149 TYR   B CE2   1 
ATOM   3042 C  CZ    . TYR   B 1 152 ? 13.89943 42.74077 4.50815   1.000 54.97613  ? 149 TYR   B CZ    1 
ATOM   3043 O  OH    . TYR   B 1 152 ? 13.93677 43.78425 3.60882   1.000 55.21622  ? 149 TYR   B OH    1 
ATOM   3044 N  N     . ASP   B 1 153 ? 13.28389 36.29776 7.34701   1.000 44.76028  ? 150 ASP   B N     1 
ATOM   3045 C  CA    . ASP   B 1 153 ? 13.64391 35.07058 8.04895   1.000 44.19593  ? 150 ASP   B CA    1 
ATOM   3046 C  C     . ASP   B 1 153 ? 14.96427 35.19970 8.79109   1.000 39.07215  ? 150 ASP   B C     1 
ATOM   3047 O  O     . ASP   B 1 153 ? 15.16572 34.52802 9.80829   1.000 39.67829  ? 150 ASP   B O     1 
ATOM   3048 C  CB    . ASP   B 1 153 ? 13.74943 33.90289 7.06806   1.000 44.60249  ? 150 ASP   B CB    1 
ATOM   3049 C  CG    . ASP   B 1 153 ? 12.49465 33.71237 6.24925   1.000 45.59076  ? 150 ASP   B CG    1 
ATOM   3050 O  OD1   . ASP   B 1 153 ? 11.39849 33.63775 6.84425   1.000 45.93171  ? 150 ASP   B OD1   1 
ATOM   3051 O  OD2   . ASP   B 1 153 ? 12.61126 33.64148 5.00930   1.000 45.50090  ? 150 ASP   B OD2   1 
ATOM   3052 N  N     . TYR   B 1 154 ? 15.86322 36.05219 8.30738   1.000 38.22491  ? 151 TYR   B N     1 
ATOM   3053 C  CA    . TYR   B 1 154 ? 17.26090 35.99167 8.70768   1.000 37.24900  ? 151 TYR   B CA    1 
ATOM   3054 C  C     . TYR   B 1 154 ? 17.88255 37.36891 8.53573   1.000 39.35899  ? 151 TYR   B C     1 
ATOM   3055 O  O     . TYR   B 1 154 ? 17.60910 38.05946 7.55079   1.000 39.68743  ? 151 TYR   B O     1 
ATOM   3056 C  CB    . TYR   B 1 154 ? 17.99300 34.93272 7.86855   1.000 38.03016  ? 151 TYR   B CB    1 
ATOM   3057 C  CG    . TYR   B 1 154 ? 19.50574 34.91041 7.95401   1.000 39.81767  ? 151 TYR   B CG    1 
ATOM   3058 C  CD1   . TYR   B 1 154 ? 20.27827 35.77580 7.18500   1.000 39.96861  ? 151 TYR   B CD1   1 
ATOM   3059 C  CD2   . TYR   B 1 154 ? 20.16324 33.98270 8.75372   1.000 41.13215  ? 151 TYR   B CD2   1 
ATOM   3060 C  CE1   . TYR   B 1 154 ? 21.65864 35.74759 7.24019   1.000 40.19595  ? 151 TYR   B CE1   1 
ATOM   3061 C  CE2   . TYR   B 1 154 ? 21.54840 33.94378 8.81289   1.000 42.46078  ? 151 TYR   B CE2   1 
ATOM   3062 C  CZ    . TYR   B 1 154 ? 22.28961 34.82878 8.05460   1.000 42.88012  ? 151 TYR   B CZ    1 
ATOM   3063 O  OH    . TYR   B 1 154 ? 23.66619 34.79601 8.10833   1.000 43.97862  ? 151 TYR   B OH    1 
ATOM   3064 N  N     . ALA   B 1 155 ? 18.71774 37.75768 9.49686   1.000 38.66825  ? 152 ALA   B N     1 
ATOM   3065 C  CA    . ALA   B 1 155 ? 19.39333 39.04696 9.46872   1.000 36.68422  ? 152 ALA   B CA    1 
ATOM   3066 C  C     . ALA   B 1 155 ? 20.82968 38.86824 9.93246   1.000 37.16203  ? 152 ALA   B C     1 
ATOM   3067 O  O     . ALA   B 1 155 ? 21.06718 38.34160 11.02360  1.000 35.40987  ? 152 ALA   B O     1 
ATOM   3068 C  CB    . ALA   B 1 155 ? 18.67736 40.06783 10.36032  1.000 37.07380  ? 152 ALA   B CB    1 
ATOM   3069 N  N     . PHE   B 1 156 ? 21.78029 39.30735 9.11006   1.000 37.05645  ? 153 PHE   B N     1 
ATOM   3070 C  CA    . PHE   B 1 156 ? 23.19678 39.27794 9.45472   1.000 36.96829  ? 153 PHE   B CA    1 
ATOM   3071 C  C     . PHE   B 1 156 ? 23.65807 40.70774 9.71074   1.000 37.30127  ? 153 PHE   B C     1 
ATOM   3072 O  O     . PHE   B 1 156 ? 23.56013 41.56383 8.82517   1.000 36.98411  ? 153 PHE   B O     1 
ATOM   3073 C  CB    . PHE   B 1 156 ? 24.02253 38.61961 8.34677   1.000 38.23126  ? 153 PHE   B CB    1 
ATOM   3074 C  CG    . PHE   B 1 156 ? 25.47433 38.42832 8.70205   1.000 36.10404  ? 153 PHE   B CG    1 
ATOM   3075 C  CD1   . PHE   B 1 156 ? 25.84303 37.59244 9.74501   1.000 36.51197  ? 153 PHE   B CD1   1 
ATOM   3076 C  CD2   . PHE   B 1 156 ? 26.46820 39.07529 7.98604   1.000 35.32049  ? 153 PHE   B CD2   1 
ATOM   3077 C  CE1   . PHE   B 1 156 ? 27.17779 37.41327 10.07747  1.000 36.44760  ? 153 PHE   B CE1   1 
ATOM   3078 C  CE2   . PHE   B 1 156 ? 27.80525 38.90114 8.30957   1.000 37.25464  ? 153 PHE   B CE2   1 
ATOM   3079 C  CZ    . PHE   B 1 156 ? 28.15953 38.06844 9.35855   1.000 37.79750  ? 153 PHE   B CZ    1 
ATOM   3080 N  N     . VAL   B 1 157 ? 24.14112 40.96787 10.92260  1.000 36.13231  ? 154 VAL   B N     1 
ATOM   3081 C  CA    . VAL   B 1 157 ? 24.54162 42.30588 11.34572  1.000 35.65216  ? 154 VAL   B CA    1 
ATOM   3082 C  C     . VAL   B 1 157 ? 26.06166 42.35271 11.42401  1.000 35.12231  ? 154 VAL   B C     1 
ATOM   3083 O  O     . VAL   B 1 157 ? 26.67654 41.62605 12.21903  1.000 32.73078  ? 154 VAL   B O     1 
ATOM   3084 C  CB    . VAL   B 1 157 ? 23.90434 42.68777 12.68932  1.000 35.27232  ? 154 VAL   B CB    1 
ATOM   3085 C  CG1   . VAL   B 1 157 ? 24.20245 44.14626 13.02533  1.000 31.24556  ? 154 VAL   B CG1   1 
ATOM   3086 C  CG2   . VAL   B 1 157 ? 22.41323 42.44218 12.64450  1.000 37.58112  ? 154 VAL   B CG2   1 
ATOM   3087 N  N     . ASP   B 1 158 ? 26.66364 43.21983 10.60833  1.000 35.86536  ? 155 ASP   B N     1 
ATOM   3088 C  CA    . ASP   B 1 158 ? 28.11465 43.29105 10.52759  1.000 39.09471  ? 155 ASP   B CA    1 
ATOM   3089 C  C     . ASP   B 1 158 ? 28.55033 44.68650 10.09809  1.000 40.96635  ? 155 ASP   B C     1 
ATOM   3090 O  O     . ASP   B 1 158 ? 29.44629 44.83062 9.26752   1.000 45.69325  ? 155 ASP   B O     1 
ATOM   3091 C  CB    . ASP   B 1 158 ? 28.63641 42.22733 9.55405   1.000 39.96186  ? 155 ASP   B CB    1 
ATOM   3092 C  CG    . ASP   B 1 158 ? 30.11197 41.92231 9.74353   1.000 39.43454  ? 155 ASP   B CG    1 
ATOM   3093 O  OD1   . ASP   B 1 158 ? 30.66137 42.25327 10.81081  1.000 42.78984  ? 155 ASP   B OD1   1 
ATOM   3094 O  OD2   . ASP   B 1 158 ? 30.72539 41.34891 8.81516   1.000 39.90327  ? 155 ASP   B OD2   1 
ATOM   3095 N  N     . ALA   B 1 159 ? 27.92912 45.72539 10.64869  1.000 41.89808  ? 156 ALA   B N     1 
ATOM   3096 C  CA    . ALA   B 1 159 ? 28.25600 47.08784 10.23822  1.000 44.14693  ? 156 ALA   B CA    1 
ATOM   3097 C  C     . ALA   B 1 159 ? 29.02170 47.83402 11.32371  1.000 42.32911  ? 156 ALA   B C     1 
ATOM   3098 O  O     . ALA   B 1 159 ? 29.97372 47.29880 11.89702  1.000 41.59714  ? 156 ALA   B O     1 
ATOM   3099 C  CB    . ALA   B 1 159 ? 26.97947 47.84961 9.86643   1.000 42.14957  ? 156 ALA   B CB    1 
ATOM   3100 N  N     A ASP   B 1 160 ? 28.60639 49.06696 11.60082  0.500 43.18968  ? 157 ASP   B N     1 
ATOM   3101 N  N     B ASP   B 1 160 ? 28.62602 49.07643 11.60248  0.500 43.21622  ? 157 ASP   B N     1 
ATOM   3102 C  CA    A ASP   B 1 160 ? 29.16667 49.85777 12.68739  0.500 44.17445  ? 157 ASP   B CA    1 
ATOM   3103 C  CA    B ASP   B 1 160 ? 29.28104 49.86160 12.64124  0.500 44.16942  ? 157 ASP   B CA    1 
ATOM   3104 C  C     A ASP   B 1 160 ? 28.95911 49.14251 14.01104  0.500 44.24861  ? 157 ASP   B C     1 
ATOM   3105 C  C     B ASP   B 1 160 ? 28.99569 49.24249 14.00673  0.500 44.27823  ? 157 ASP   B C     1 
ATOM   3106 O  O     A ASP   B 1 160 ? 27.81960 48.92759 14.43762  0.500 42.03755  ? 157 ASP   B O     1 
ATOM   3107 O  O     B ASP   B 1 160 ? 27.84060 49.16689 14.43855  0.500 41.84273  ? 157 ASP   B O     1 
ATOM   3108 C  CB    A ASP   B 1 160 ? 28.49338 51.22853 12.70789  0.500 46.82079  ? 157 ASP   B CB    1 
ATOM   3109 C  CB    B ASP   B 1 160 ? 28.82961 51.32271 12.58096  0.500 45.87976  ? 157 ASP   B CB    1 
ATOM   3110 C  CG    A ASP   B 1 160 ? 29.06168 52.15554 13.76425  0.500 46.14847  ? 157 ASP   B CG    1 
ATOM   3111 C  CG    B ASP   B 1 160 ? 27.33610 51.47957 12.33112  0.500 46.69411  ? 157 ASP   B CG    1 
ATOM   3112 O  OD1   A ASP   B 1 160 ? 29.95139 51.73849 14.53457  0.500 46.03348  ? 157 ASP   B OD1   1 
ATOM   3113 O  OD1   B ASP   B 1 160 ? 26.70829 50.57293 11.73910  0.500 46.86204  ? 157 ASP   B OD1   1 
ATOM   3114 O  OD2   A ASP   B 1 160 ? 28.61245 53.31761 13.81758  0.500 48.26070  ? 157 ASP   B OD2   1 
ATOM   3115 O  OD2   B ASP   B 1 160 ? 26.78967 52.53686 12.71637  0.500 48.39333  ? 157 ASP   B OD2   1 
ATOM   3116 N  N     . LYS   B 1 161 ? 30.06280 48.79193 14.67408  1.000 46.46268  ? 158 LYS   B N     1 
ATOM   3117 C  CA    . LYS   B 1 161 ? 29.93921 47.99065 15.89058  1.000 48.97977  ? 158 LYS   B CA    1 
ATOM   3118 C  C     . LYS   B 1 161 ? 29.25236 48.75247 17.01933  1.000 53.76856  ? 158 LYS   B C     1 
ATOM   3119 O  O     . LYS   B 1 161 ? 28.49525 48.16296 17.80077  1.000 58.93489  ? 158 LYS   B O     1 
ATOM   3120 C  CB    . LYS   B 1 161 ? 31.31727 47.50132 16.33654  1.000 45.15387  ? 158 LYS   B CB    1 
ATOM   3121 C  CG    . LYS   B 1 161 ? 32.15777 46.93148 15.20340  1.000 43.16083  ? 158 LYS   B CG    1 
ATOM   3122 C  CD    . LYS   B 1 161 ? 31.42058 45.82257 14.46365  1.000 38.39822  ? 158 LYS   B CD    1 
ATOM   3123 C  CE    . LYS   B 1 161 ? 32.21027 45.33909 13.25263  1.000 39.70087  ? 158 LYS   B CE    1 
ATOM   3124 N  NZ    . LYS   B 1 161 ? 31.32784 44.92201 12.11933  1.000 38.65298  ? 158 LYS   B NZ    1 
ATOM   3125 N  N     . SER   B 1 162 ? 29.50234 50.05536 17.12864  1.000 51.12473  ? 159 SER   B N     1 
ATOM   3126 C  CA    . SER   B 1 162 ? 28.92470 50.83102 18.22001  1.000 50.84365  ? 159 SER   B CA    1 
ATOM   3127 C  C     . SER   B 1 162 ? 27.41348 51.00727 18.09577  1.000 49.47527  ? 159 SER   B C     1 
ATOM   3128 O  O     . SER   B 1 162 ? 26.80226 51.58742 19.00071  1.000 51.07544  ? 159 SER   B O     1 
ATOM   3129 C  CB    . SER   B 1 162 ? 29.60318 52.20067 18.29921  1.000 51.44136  ? 159 SER   B CB    1 
ATOM   3130 O  OG    . SER   B 1 162 ? 29.31527 52.97901 17.15150  1.000 50.54788  ? 159 SER   B OG    1 
ATOM   3131 N  N     . ASN   B 1 163 ? 26.79655 50.51188 17.02207  1.000 46.88327  ? 160 ASN   B N     1 
ATOM   3132 C  CA    . ASN   B 1 163 ? 25.37646 50.71077 16.76311  1.000 42.50714  ? 160 ASN   B CA    1 
ATOM   3133 C  C     . ASN   B 1 163 ? 24.56861 49.41843 16.82084  1.000 37.48141  ? 160 ASN   B C     1 
ATOM   3134 O  O     . ASN   B 1 163 ? 23.38384 49.43178 16.47073  1.000 39.29539  ? 160 ASN   B O     1 
ATOM   3135 C  CB    . ASN   B 1 163 ? 25.18461 51.37573 15.39800  1.000 47.22424  ? 160 ASN   B CB    1 
ATOM   3136 C  CG    . ASN   B 1 163 ? 24.44860 52.69640 15.48814  1.000 51.33861  ? 160 ASN   B CG    1 
ATOM   3137 O  OD1   . ASN   B 1 163 ? 23.80388 52.99645 16.49463  1.000 51.49417  ? 160 ASN   B OD1   1 
ATOM   3138 N  ND2   . ASN   B 1 163 ? 24.53440 53.49289 14.42702  1.000 52.81271  ? 160 ASN   B ND2   1 
ATOM   3139 N  N     . TYR   B 1 164 ? 25.17413 48.30601 17.25279  1.000 34.91850  ? 161 TYR   B N     1 
ATOM   3140 C  CA    . TYR   B 1 164 ? 24.47012 47.02393 17.24769  1.000 33.63212  ? 161 TYR   B CA    1 
ATOM   3141 C  C     . TYR   B 1 164 ? 23.20238 47.07059 18.09540  1.000 32.87241  ? 161 TYR   B C     1 
ATOM   3142 O  O     . TYR   B 1 164 ? 22.16066 46.53365 17.69692  1.000 32.03465  ? 161 TYR   B O     1 
ATOM   3143 C  CB    . TYR   B 1 164 ? 25.39082 45.91080 17.74501  1.000 31.06949  ? 161 TYR   B CB    1 
ATOM   3144 C  CG    . TYR   B 1 164 ? 26.29670 45.31296 16.68925  1.000 32.83761  ? 161 TYR   B CG    1 
ATOM   3145 C  CD1   . TYR   B 1 164 ? 26.77626 46.07740 15.63022  1.000 32.02721  ? 161 TYR   B CD1   1 
ATOM   3146 C  CD2   . TYR   B 1 164 ? 26.66716 43.97654 16.75203  1.000 31.07368  ? 161 TYR   B CD2   1 
ATOM   3147 C  CE1   . TYR   B 1 164 ? 27.60657 45.52165 14.66562  1.000 33.67769  ? 161 TYR   B CE1   1 
ATOM   3148 C  CE2   . TYR   B 1 164 ? 27.49229 43.41498 15.79725  1.000 30.34579  ? 161 TYR   B CE2   1 
ATOM   3149 C  CZ    . TYR   B 1 164 ? 27.96183 44.18849 14.75922  1.000 33.61923  ? 161 TYR   B CZ    1 
ATOM   3150 O  OH    . TYR   B 1 164 ? 28.78753 43.61562 13.81492  1.000 35.36712  ? 161 TYR   B OH    1 
ATOM   3151 N  N     . ALA   B 1 165 ? 23.27417 47.69704 19.27270  1.000 30.57627  ? 162 ALA   B N     1 
ATOM   3152 C  CA    . ALA   B 1 165 ? 22.10540 47.76988 20.14432  1.000 35.10431  ? 162 ALA   B CA    1 
ATOM   3153 C  C     . ALA   B 1 165 ? 20.95390 48.50431 19.46615  1.000 37.77696  ? 162 ALA   B C     1 
ATOM   3154 O  O     . ALA   B 1 165 ? 19.78778 48.12288 19.62132  1.000 36.67627  ? 162 ALA   B O     1 
ATOM   3155 C  CB    . ALA   B 1 165 ? 22.47688 48.44691 21.46224  1.000 35.72791  ? 162 ALA   B CB    1 
ATOM   3156 N  N     . ASN   B 1 166 ? 21.26139 49.55441 18.69933  1.000 38.40339  ? 163 ASN   B N     1 
ATOM   3157 C  CA    . ASN   B 1 166 ? 20.21622 50.25489 17.95955  1.000 38.04852  ? 163 ASN   B CA    1 
ATOM   3158 C  C     . ASN   B 1 166 ? 19.65974 49.38969 16.83641  1.000 40.29147  ? 163 ASN   B C     1 
ATOM   3159 O  O     . ASN   B 1 166 ? 18.44962 49.40113 16.58163  1.000 42.13570  ? 163 ASN   B O     1 
ATOM   3160 C  CB    . ASN   B 1 166 ? 20.75038 51.57548 17.40778  1.000 40.26456  ? 163 ASN   B CB    1 
ATOM   3161 C  CG    . ASN   B 1 166 ? 20.77519 52.67150 18.45300  1.000 43.25181  ? 163 ASN   B CG    1 
ATOM   3162 O  OD1   . ASN   B 1 166 ? 19.94127 52.69958 19.35600  1.000 47.00437  ? 163 ASN   B OD1   1 
ATOM   3163 N  ND2   . ASN   B 1 166 ? 21.73490 53.57848 18.33790  1.000 40.20987  ? 163 ASN   B ND2   1 
ATOM   3164 N  N     A TYR   B 1 167 ? 20.53092 48.64981 16.14220  0.500 38.91648  ? 164 TYR   B N     1 
ATOM   3165 N  N     B TYR   B 1 167 ? 20.52381 48.63593 16.15204  0.500 38.91620  ? 164 TYR   B N     1 
ATOM   3166 C  CA    A TYR   B 1 167 ? 20.06486 47.71036 15.12638  0.500 39.11247  ? 164 TYR   B CA    1 
ATOM   3167 C  CA    B TYR   B 1 167 ? 20.04378 47.71842 15.12342  0.500 39.11706  ? 164 TYR   B CA    1 
ATOM   3168 C  C     A TYR   B 1 167 ? 19.13426 46.66693 15.73160  0.500 38.39169  ? 164 TYR   B C     1 
ATOM   3169 C  C     B TYR   B 1 167 ? 19.13956 46.64716 15.72178  0.500 38.38647  ? 164 TYR   B C     1 
ATOM   3170 O  O     A TYR   B 1 167 ? 18.09547 46.33382 15.14766  0.500 38.06517  ? 164 TYR   B O     1 
ATOM   3171 O  O     B TYR   B 1 167 ? 18.12018 46.27887 15.12537  0.500 38.19287  ? 164 TYR   B O     1 
ATOM   3172 C  CB    A TYR   B 1 167 ? 21.25516 47.02289 14.45485  0.500 40.98823  ? 164 TYR   B CB    1 
ATOM   3173 C  CB    B TYR   B 1 167 ? 21.22738 47.07840 14.39771  0.500 41.02774  ? 164 TYR   B CB    1 
ATOM   3174 C  CG    A TYR   B 1 167 ? 22.21204 47.95101 13.73698  0.500 43.18227  ? 164 TYR   B CG    1 
ATOM   3175 C  CG    B TYR   B 1 167 ? 22.08215 48.06250 13.63121  0.500 43.26368  ? 164 TYR   B CG    1 
ATOM   3176 C  CD1   A TYR   B 1 167 ? 21.77107 49.13817 13.16611  0.500 43.93538  ? 164 TYR   B CD1   1 
ATOM   3177 C  CD1   B TYR   B 1 167 ? 21.53628 49.22926 13.11209  0.500 43.79152  ? 164 TYR   B CD1   1 
ATOM   3178 C  CD2   A TYR   B 1 167 ? 23.56023 47.63247 13.62535  0.500 43.62243  ? 164 TYR   B CD2   1 
ATOM   3179 C  CD2   B TYR   B 1 167 ? 23.43549 47.82486 13.42678  0.500 43.62544  ? 164 TYR   B CD2   1 
ATOM   3180 C  CE1   A TYR   B 1 167 ? 22.64897 49.98358 12.50704  0.500 43.85935  ? 164 TYR   B CE1   1 
ATOM   3181 C  CE1   B TYR   B 1 167 ? 22.31391 50.13199 12.41138  0.500 43.72538  ? 164 TYR   B CE1   1 
ATOM   3182 C  CE2   A TYR   B 1 167 ? 24.44407 48.47019 12.96944  0.500 43.90173  ? 164 TYR   B CE2   1 
ATOM   3183 C  CE2   B TYR   B 1 167 ? 24.22188 48.72249 12.72629  0.500 44.26378  ? 164 TYR   B CE2   1 
ATOM   3184 C  CZ    A TYR   B 1 167 ? 23.98367 49.64358 12.41276  0.500 45.14045  ? 164 TYR   B CZ    1 
ATOM   3185 C  CZ    B TYR   B 1 167 ? 23.65422 49.87428 12.22115  0.500 44.89691  ? 164 TYR   B CZ    1 
ATOM   3186 O  OH    A TYR   B 1 167 ? 24.86324 50.47810 11.76005  0.500 45.55034  ? 164 TYR   B OH    1 
ATOM   3187 O  OH    B TYR   B 1 167 ? 24.42898 50.77316 11.52314  0.500 46.23674  ? 164 TYR   B OH    1 
ATOM   3188 N  N     . HIS   B 1 168 ? 19.49200 46.14738 16.90931  1.000 34.96878  ? 165 HIS   B N     1 
ATOM   3189 C  CA    . HIS   B 1 168 ? 18.70098 45.10034 17.54994  1.000 33.05385  ? 165 HIS   B CA    1 
ATOM   3190 C  C     . HIS   B 1 168 ? 17.26304 45.54037 17.80260  1.000 37.91110  ? 165 HIS   B C     1 
ATOM   3191 O  O     . HIS   B 1 168 ? 16.32297 44.76353 17.59387  1.000 37.92935  ? 165 HIS   B O     1 
ATOM   3192 C  CB    . HIS   B 1 168 ? 19.36832 44.69268 18.86490  1.000 32.89011  ? 165 HIS   B CB    1 
ATOM   3193 C  CG    . HIS   B 1 168 ? 18.68882 43.55837 19.56674  1.000 34.72690  ? 165 HIS   B CG    1 
ATOM   3194 N  ND1   . HIS   B 1 168 ? 18.74018 42.25926 19.10710  1.000 34.61797  ? 165 HIS   B ND1   1 
ATOM   3195 C  CD2   . HIS   B 1 168 ? 17.94825 43.52719 20.70048  1.000 33.70868  ? 165 HIS   B CD2   1 
ATOM   3196 C  CE1   . HIS   B 1 168 ? 18.05924 41.47763 19.92651  1.000 35.63521  ? 165 HIS   B CE1   1 
ATOM   3197 N  NE2   . HIS   B 1 168 ? 17.56765 42.22274 20.90104  1.000 35.13675  ? 165 HIS   B NE2   1 
ATOM   3198 N  N     . GLU   B 1 169 ? 17.07107 46.78464 18.24974  1.000 39.17084  ? 166 GLU   B N     1 
ATOM   3199 C  CA    . GLU   B 1 169 ? 15.72816 47.25187 18.58196  1.000 41.07982  ? 166 GLU   B CA    1 
ATOM   3200 C  C     . GLU   B 1 169 ? 14.82454 47.29208 17.35659  1.000 40.31235  ? 166 GLU   B C     1 
ATOM   3201 O  O     . GLU   B 1 169 ? 13.60663 47.12385 17.47925  1.000 40.36984  ? 166 GLU   B O     1 
ATOM   3202 C  CB    . GLU   B 1 169 ? 15.79997 48.62906 19.24755  1.000 40.59187  ? 166 GLU   B CB    1 
ATOM   3203 C  CG    . GLU   B 1 169 ? 16.36346 48.59241 20.66070  1.000 37.07746  ? 166 GLU   B CG    1 
ATOM   3204 C  CD    . GLU   B 1 169 ? 15.68365 47.53991 21.52076  1.000 40.75288  ? 166 GLU   B CD    1 
ATOM   3205 O  OE1   . GLU   B 1 169 ? 14.43812 47.46871 21.50135  1.000 42.33807  ? 166 GLU   B OE1   1 
ATOM   3206 O  OE2   . GLU   B 1 169 ? 16.39352 46.76846 22.20068  1.000 42.39842  ? 166 GLU   B OE2   1 
ATOM   3207 N  N     . ARG   B 1 170 ? 15.39577 47.50784 16.17149  1.000 39.20488  ? 167 ARG   B N     1 
ATOM   3208 C  CA    . ARG   B 1 170 ? 14.60312 47.44442 14.94947  1.000 40.50475  ? 167 ARG   B CA    1 
ATOM   3209 C  C     . ARG   B 1 170 ? 14.42797 46.00903 14.47263  1.000 40.53689  ? 167 ARG   B C     1 
ATOM   3210 O  O     . ARG   B 1 170 ? 13.33907 45.62650 14.02829  1.000 40.50562  ? 167 ARG   B O     1 
ATOM   3211 C  CB    . ARG   B 1 170 ? 15.25387 48.28457 13.84808  1.000 40.47576  ? 167 ARG   B CB    1 
ATOM   3212 C  CG    . ARG   B 1 170 ? 14.98360 49.77992 13.93201  1.000 44.63120  ? 167 ARG   B CG    1 
ATOM   3213 C  CD    . ARG   B 1 170 ? 15.79229 50.44534 15.03004  1.000 47.01722  ? 167 ARG   B CD    1 
ATOM   3214 N  NE    . ARG   B 1 170 ? 15.78027 51.89962 14.91525  1.000 49.62297  ? 167 ARG   B NE    1 
ATOM   3215 C  CZ    . ARG   B 1 170 ? 16.29130 52.72283 15.82405  1.000 51.02655  ? 167 ARG   B CZ    1 
ATOM   3216 N  NH1   . ARG   B 1 170 ? 16.85318 52.23218 16.92092  1.000 50.32261  ? 167 ARG   B NH1   1 
ATOM   3217 N  NH2   . ARG   B 1 170 ? 16.23881 54.03548 15.63724  1.000 51.18511  ? 167 ARG   B NH2   1 
ATOM   3218 N  N     . LEU   B 1 171 ? 15.48615 45.20102 14.57080  1.000 40.49170  ? 168 LEU   B N     1 
ATOM   3219 C  CA    . LEU   B 1 171 ? 15.48412 43.88720 13.94280  1.000 37.03703  ? 168 LEU   B CA    1 
ATOM   3220 C  C     . LEU   B 1 171 ? 14.59186 42.88112 14.65845  1.000 32.54255  ? 168 LEU   B C     1 
ATOM   3221 O  O     . LEU   B 1 171 ? 14.09222 41.95823 14.00834  1.000 30.65094  ? 168 LEU   B O     1 
ATOM   3222 C  CB    . LEU   B 1 171 ? 16.91268 43.35890 13.84753  1.000 34.27756  ? 168 LEU   B CB    1 
ATOM   3223 C  CG    . LEU   B 1 171 ? 17.76092 44.09503 12.80882  1.000 34.05688  ? 168 LEU   B CG    1 
ATOM   3224 C  CD1   . LEU   B 1 171 ? 19.18419 43.59634 12.83816  1.000 34.04019  ? 168 LEU   B CD1   1 
ATOM   3225 C  CD2   . LEU   B 1 171 ? 17.17622 43.94482 11.41741  1.000 32.39349  ? 168 LEU   B CD2   1 
ATOM   3226 N  N     . VAL   B 1 172 ? 14.37226 43.02915 15.96882  1.000 29.20905  ? 169 VAL   B N     1 
ATOM   3227 C  CA    . VAL   B 1 172 ? 13.44141 42.14712 16.66633  1.000 34.07312  ? 169 VAL   B CA    1 
ATOM   3228 C  C     . VAL   B 1 172 ? 12.00186 42.39854 16.24663  1.000 39.72819  ? 169 VAL   B C     1 
ATOM   3229 O  O     . VAL   B 1 172 ? 11.10253 41.65644 16.65726  1.000 41.70239  ? 169 VAL   B O     1 
ATOM   3230 C  CB    . VAL   B 1 172 ? 13.55668 42.29350 18.19892  1.000 36.73119  ? 169 VAL   B CB    1 
ATOM   3231 C  CG1   . VAL   B 1 172 ? 14.93252 41.88294 18.68619  1.000 39.97854  ? 169 VAL   B CG1   1 
ATOM   3232 C  CG2   . VAL   B 1 172 ? 13.21421 43.70796 18.62507  1.000 38.22827  ? 169 VAL   B CG2   1 
ATOM   3233 N  N     . LYS   B 1 173 ? 11.75907 43.43939 15.44469  1.000 42.27904  ? 170 LYS   B N     1 
ATOM   3234 C  CA    . LYS   B 1 173 ? 10.44924 43.69110 14.86617  1.000 48.33206  ? 170 LYS   B CA    1 
ATOM   3235 C  C     . LYS   B 1 173 ? 10.39954 43.46649 13.36228  1.000 46.53046  ? 170 LYS   B C     1 
ATOM   3236 O  O     . LYS   B 1 173 ? 9.30350  43.31798 12.81583  1.000 47.67166  ? 170 LYS   B O     1 
ATOM   3237 C  CB    . LYS   B 1 173 ? 10.00145 45.12860 15.16930  1.000 53.55928  ? 170 LYS   B CB    1 
ATOM   3238 C  CG    . LYS   B 1 173 ? 9.91888  45.45438 16.65034  1.000 58.66415  ? 170 LYS   B CG    1 
ATOM   3239 C  CD    . LYS   B 1 173 ? 9.31126  46.82287 16.87529  1.000 65.88947  ? 170 LYS   B CD    1 
ATOM   3240 C  CE    . LYS   B 1 173 ? 8.96140  47.02625 18.33694  1.000 70.23031  ? 170 LYS   B CE    1 
ATOM   3241 N  NZ    . LYS   B 1 173 ? 8.05992  45.94379 18.82702  1.000 70.72507  ? 170 LYS   B NZ    1 
ATOM   3242 N  N     . LEU   B 1 174 ? 11.54929 43.44151 12.68529  1.000 45.37621  ? 171 LEU   B N     1 
ATOM   3243 C  CA    . LEU   B 1 174 ? 11.60799 43.22933 11.24553  1.000 43.94854  ? 171 LEU   B CA    1 
ATOM   3244 C  C     . LEU   B 1 174 ? 11.84290 41.77531 10.86830  1.000 41.89515  ? 171 LEU   B C     1 
ATOM   3245 O  O     . LEU   B 1 174 ? 11.64409 41.41726 9.70410   1.000 40.94440  ? 171 LEU   B O     1 
ATOM   3246 C  CB    . LEU   B 1 174 ? 12.71039 44.09445 10.61747  1.000 42.35055  ? 171 LEU   B CB    1 
ATOM   3247 C  CG    . LEU   B 1 174 ? 12.50433 45.60903 10.63444  1.000 44.00464  ? 171 LEU   B CG    1 
ATOM   3248 C  CD1   . LEU   B 1 174 ? 13.75201 46.34088 10.15045  1.000 44.93093  ? 171 LEU   B CD1   1 
ATOM   3249 C  CD2   . LEU   B 1 174 ? 11.30845 45.97364 9.78476   1.000 44.90802  ? 171 LEU   B CD2   1 
ATOM   3250 N  N     . VAL   B 1 175 ? 12.25841 40.93809 11.81344  1.000 40.88454  ? 172 VAL   B N     1 
ATOM   3251 C  CA    . VAL   B 1 175 ? 12.46110 39.51330 11.58515  1.000 41.16860  ? 172 VAL   B CA    1 
ATOM   3252 C  C     . VAL   B 1 175 ? 11.26269 38.76643 12.14590  1.000 40.02201  ? 172 VAL   B C     1 
ATOM   3253 O  O     . VAL   B 1 175 ? 10.74312 39.12049 13.21298  1.000 42.72101  ? 172 VAL   B O     1 
ATOM   3254 C  CB    . VAL   B 1 175 ? 13.77480 39.03444 12.23249  1.000 41.77598  ? 172 VAL   B CB    1 
ATOM   3255 C  CG1   . VAL   B 1 175 ? 13.84936 37.52035 12.24700  1.000 41.08132  ? 172 VAL   B CG1   1 
ATOM   3256 C  CG2   . VAL   B 1 175 ? 14.96813 39.61426 11.49033  1.000 41.35156  ? 172 VAL   B CG2   1 
ATOM   3257 N  N     . ARG   B 1 176 ? 10.81468 37.73899 11.42548  1.000 37.93273  ? 173 ARG   B N     1 
ATOM   3258 C  CA    . ARG   B 1 176 ? 9.64482  36.98378 11.84651  1.000 39.33530  ? 173 ARG   B CA    1 
ATOM   3259 C  C     . ARG   B 1 176 ? 9.89691  36.29137 13.18263  1.000 38.90579  ? 173 ARG   B C     1 
ATOM   3260 O  O     . ARG   B 1 176 ? 11.03717 36.12629 13.62952  1.000 38.57294  ? 173 ARG   B O     1 
ATOM   3261 C  CB    . ARG   B 1 176 ? 9.27182  35.93481 10.79988  1.000 37.74837  ? 173 ARG   B CB    1 
ATOM   3262 C  CG    . ARG   B 1 176 ? 10.24821 34.76728 10.72708  1.000 38.76209  ? 173 ARG   B CG    1 
ATOM   3263 C  CD    . ARG   B 1 176 ? 9.70012  33.63092 9.87647   1.000 40.57258  ? 173 ARG   B CD    1 
ATOM   3264 N  NE    . ARG   B 1 176 ? 10.72569 32.64333 9.54603   1.000 44.62254  ? 173 ARG   B NE    1 
ATOM   3265 C  CZ    . ARG   B 1 176 ? 11.01393 31.58109 10.29304  1.000 47.52299  ? 173 ARG   B CZ    1 
ATOM   3266 N  NH1   . ARG   B 1 176 ? 11.96451 30.73752 9.91108   1.000 45.64952  ? 173 ARG   B NH1   1 
ATOM   3267 N  NH2   . ARG   B 1 176 ? 10.35200 31.36064 11.42235  1.000 46.86645  ? 173 ARG   B NH2   1 
ATOM   3268 N  N     . ILE   B 1 177 ? 8.80060  35.88406 13.82434  1.000 35.44903  ? 174 ILE   B N     1 
ATOM   3269 C  CA    . ILE   B 1 177 ? 8.90158  35.03708 15.00390  1.000 37.24652  ? 174 ILE   B CA    1 
ATOM   3270 C  C     . ILE   B 1 177 ? 9.52183  33.70853 14.60225  1.000 38.74928  ? 174 ILE   B C     1 
ATOM   3271 O  O     . ILE   B 1 177 ? 9.11132  33.08161 13.61748  1.000 38.39930  ? 174 ILE   B O     1 
ATOM   3272 C  CB    . ILE   B 1 177 ? 7.52025  34.84922 15.64826  1.000 38.18394  ? 174 ILE   B CB    1 
ATOM   3273 C  CG1   . ILE   B 1 177 ? 7.05414  36.15715 16.29442  1.000 39.10505  ? 174 ILE   B CG1   1 
ATOM   3274 C  CG2   . ILE   B 1 177 ? 7.55448  33.71258 16.66633  1.000 34.55771  ? 174 ILE   B CG2   1 
ATOM   3275 C  CD1   . ILE   B 1 177 ? 5.63319  36.10537 16.83703  1.000 42.97870  ? 174 ILE   B CD1   1 
ATOM   3276 N  N     . GLY   B 1 178 ? 10.52766 33.27719 15.35695  1.000 39.60006  ? 175 GLY   B N     1 
ATOM   3277 C  CA    . GLY   B 1 178 ? 11.29966 32.11612 14.97603  1.000 37.58284  ? 175 GLY   B CA    1 
ATOM   3278 C  C     . GLY   B 1 178 ? 12.40043 32.39195 13.97667  1.000 37.71041  ? 175 GLY   B C     1 
ATOM   3279 O  O     . GLY   B 1 178 ? 13.16151 31.47188 13.64870  1.000 41.90329  ? 175 GLY   B O     1 
ATOM   3280 N  N     . GLY   B 1 179 ? 12.49997 33.62152 13.46751  1.000 36.38809  ? 176 GLY   B N     1 
ATOM   3281 C  CA    . GLY   B 1 179 ? 13.59832 33.98787 12.60409  1.000 40.79465  ? 176 GLY   B CA    1 
ATOM   3282 C  C     . GLY   B 1 179 ? 14.86680 34.25204 13.38933  1.000 40.18025  ? 176 GLY   B C     1 
ATOM   3283 O  O     . GLY   B 1 179 ? 14.86785 34.33008 14.61756  1.000 38.52079  ? 176 GLY   B O     1 
ATOM   3284 N  N     . ALA   B 1 180 ? 15.96619 34.40093 12.65772  1.000 36.08324  ? 177 ALA   B N     1 
ATOM   3285 C  CA    . ALA   B 1 180 ? 17.28907 34.49751 13.25485  1.000 30.34117  ? 177 ALA   B CA    1 
ATOM   3286 C  C     . ALA   B 1 180 ? 17.89024 35.87753 13.02637  1.000 33.11115  ? 177 ALA   B C     1 
ATOM   3287 O  O     . ALA   B 1 180 ? 17.72426 36.47149 11.95538  1.000 38.77310  ? 177 ALA   B O     1 
ATOM   3288 C  CB    . ALA   B 1 180 ? 18.22017 33.41968 12.68961  1.000 27.52923  ? 177 ALA   B CB    1 
ATOM   3289 N  N     . ILE   B 1 181 ? 18.57526 36.38582 14.04942  1.000 31.11715  ? 178 ILE   B N     1 
ATOM   3290 C  CA    . ILE   B 1 181 ? 19.39207 37.59095 13.95619  1.000 31.83277  ? 178 ILE   B CA    1 
ATOM   3291 C  C     . ILE   B 1 181 ? 20.79911 37.21011 14.39396  1.000 33.96514  ? 178 ILE   B C     1 
ATOM   3292 O  O     . ILE   B 1 181 ? 20.99138 36.69606 15.50398  1.000 32.57674  ? 178 ILE   B O     1 
ATOM   3293 C  CB    . ILE   B 1 181 ? 18.84078 38.73690 14.82041  1.000 33.48368  ? 178 ILE   B CB    1 
ATOM   3294 C  CG1   . ILE   B 1 181 ? 17.34768 38.93663 14.56428  1.000 34.19611  ? 178 ILE   B CG1   1 
ATOM   3295 C  CG2   . ILE   B 1 181 ? 19.60107 40.03638 14.53823  1.000 30.98444  ? 178 ILE   B CG2   1 
ATOM   3296 C  CD1   . ILE   B 1 181 ? 16.72540 40.00259 15.43075  1.000 33.64126  ? 178 ILE   B CD1   1 
ATOM   3297 N  N     . LEU   B 1 182 ? 21.77690 37.44612 13.52514  1.000 33.20765  ? 179 LEU   B N     1 
ATOM   3298 C  CA    . LEU   B 1 182 ? 23.16201 37.08166 13.79065  1.000 31.78604  ? 179 LEU   B CA    1 
ATOM   3299 C  C     . LEU   B 1 182 ? 24.00915 38.34112 13.88675  1.000 31.76859  ? 179 LEU   B C     1 
ATOM   3300 O  O     . LEU   B 1 182 ? 23.98505 39.18087 12.98041  1.000 34.10655  ? 179 LEU   B O     1 
ATOM   3301 C  CB    . LEU   B 1 182 ? 23.70676 36.15165 12.70434  1.000 32.09793  ? 179 LEU   B CB    1 
ATOM   3302 C  CG    . LEU   B 1 182 ? 23.43843 34.65494 12.88292  1.000 35.99516  ? 179 LEU   B CG    1 
ATOM   3303 C  CD1   . LEU   B 1 182 ? 21.97640 34.31090 12.66271  1.000 38.06550  ? 179 LEU   B CD1   1 
ATOM   3304 C  CD2   . LEU   B 1 182 ? 24.32556 33.84783 11.94750  1.000 34.47743  ? 179 LEU   B CD2   1 
ATOM   3305 N  N     . TYR   B 1 183 ? 24.74856 38.47096 14.98629  1.000 28.82688  ? 180 TYR   B N     1 
ATOM   3306 C  CA    . TYR   B 1 183 ? 25.62839 39.61036 15.22232  1.000 27.85849  ? 180 TYR   B CA    1 
ATOM   3307 C  C     . TYR   B 1 183 ? 27.07096 39.14446 15.11755  1.000 29.12402  ? 180 TYR   B C     1 
ATOM   3308 O  O     . TYR   B 1 183 ? 27.50481 38.27354 15.87884  1.000 31.16441  ? 180 TYR   B O     1 
ATOM   3309 C  CB    . TYR   B 1 183 ? 25.36256 40.24869 16.58558  1.000 25.55752  ? 180 TYR   B CB    1 
ATOM   3310 C  CG    . TYR   B 1 183 ? 23.97176 40.82352 16.68854  1.000 30.20853  ? 180 TYR   B CG    1 
ATOM   3311 C  CD1   . TYR   B 1 183 ? 23.67884 42.07444 16.16157  1.000 28.45899  ? 180 TYR   B CD1   1 
ATOM   3312 C  CD2   . TYR   B 1 183 ? 22.94657 40.10428 17.28345  1.000 29.39288  ? 180 TYR   B CD2   1 
ATOM   3313 C  CE1   . TYR   B 1 183 ? 22.40765 42.60003 16.23488  1.000 35.55059  ? 180 TYR   B CE1   1 
ATOM   3314 C  CE2   . TYR   B 1 183 ? 21.66683 40.62230 17.36417  1.000 33.65521  ? 180 TYR   B CE2   1 
ATOM   3315 C  CZ    . TYR   B 1 183 ? 21.40555 41.87163 16.83706  1.000 37.34971  ? 180 TYR   B CZ    1 
ATOM   3316 O  OH    . TYR   B 1 183 ? 20.14032 42.39654 16.90465  1.000 39.20215  ? 180 TYR   B OH    1 
ATOM   3317 N  N     . ASP   B 1 184 ? 27.80426 39.72814 14.17897  1.000 31.40932  ? 181 ASP   B N     1 
ATOM   3318 C  CA    . ASP   B 1 184 ? 29.19157 39.36426 13.95248  1.000 34.55687  ? 181 ASP   B CA    1 
ATOM   3319 C  C     . ASP   B 1 184 ? 30.10597 40.11334 14.91418  1.000 31.20873  ? 181 ASP   B C     1 
ATOM   3320 O  O     . ASP   B 1 184 ? 29.77452 41.19861 15.39406  1.000 34.57587  ? 181 ASP   B O     1 
ATOM   3321 C  CB    . ASP   B 1 184 ? 29.57648 39.66652 12.50316  1.000 39.00282  ? 181 ASP   B CB    1 
ATOM   3322 C  CG    . ASP   B 1 184 ? 30.80301 38.90227 12.05483  1.000 44.23810  ? 181 ASP   B CG    1 
ATOM   3323 O  OD1   . ASP   B 1 184 ? 30.89100 37.69745 12.36667  1.000 44.62938  ? 181 ASP   B OD1   1 
ATOM   3324 O  OD2   . ASP   B 1 184 ? 31.67025 39.50277 11.39135  1.000 48.24588  ? 181 ASP   B OD2   1 
ATOM   3325 N  N     . ASN   B 1 185 ? 31.25313 39.49693 15.21547  1.000 32.07276  ? 182 ASN   B N     1 
ATOM   3326 C  CA    . ASN   B 1 185 ? 32.34548 40.11465 15.96836  1.000 32.85426  ? 182 ASN   B CA    1 
ATOM   3327 C  C     . ASN   B 1 185 ? 32.03005 40.29528 17.45158  1.000 32.25027  ? 182 ASN   B C     1 
ATOM   3328 O  O     . ASN   B 1 185 ? 32.62758 41.14992 18.10719  1.000 31.98350  ? 182 ASN   B O     1 
ATOM   3329 C  CB    . ASN   B 1 185 ? 32.74210 41.46350 15.36180  1.000 34.98226  ? 182 ASN   B CB    1 
ATOM   3330 C  CG    . ASN   B 1 185 ? 33.20953 41.34195 13.93011  1.000 40.59730  ? 182 ASN   B CG    1 
ATOM   3331 O  OD1   . ASN   B 1 185 ? 32.52466 41.77648 13.00102  1.000 45.92791  ? 182 ASN   B OD1   1 
ATOM   3332 N  ND2   . ASN   B 1 185 ? 34.38375 40.75020 13.74118  1.000 40.13376  ? 182 ASN   B ND2   1 
ATOM   3333 N  N     . THR   B 1 186 ? 31.12285 39.49261 18.01681  1.000 29.75312  ? 183 THR   B N     1 
ATOM   3334 C  CA    . THR   B 1 186 ? 30.70294 39.75364 19.39157  1.000 30.70908  ? 183 THR   B CA    1 
ATOM   3335 C  C     . THR   B 1 186 ? 31.75407 39.36280 20.42166  1.000 31.37850  ? 183 THR   B C     1 
ATOM   3336 O  O     . THR   B 1 186 ? 31.56951 39.65394 21.60807  1.000 30.52886  ? 183 THR   B O     1 
ATOM   3337 C  CB    . THR   B 1 186 ? 29.37273 39.05385 19.70246  1.000 28.30360  ? 183 THR   B CB    1 
ATOM   3338 O  OG1   . THR   B 1 186 ? 29.47237 37.65030 19.44521  1.000 28.87171  ? 183 THR   B OG1   1 
ATOM   3339 C  CG2   . THR   B 1 186 ? 28.25469 39.64517 18.85487  1.000 25.91672  ? 183 THR   B CG2   1 
ATOM   3340 N  N     . LEU   B 1 187 ? 32.84606 38.72588 20.00742  1.000 32.11807  ? 184 LEU   B N     1 
ATOM   3341 C  CA    . LEU   B 1 187 ? 33.96550 38.46926 20.90014  1.000 29.03942  ? 184 LEU   B CA    1 
ATOM   3342 C  C     . LEU   B 1 187 ? 35.11009 39.45956 20.70800  1.000 34.32029  ? 184 LEU   B C     1 
ATOM   3343 O  O     . LEU   B 1 187 ? 36.00205 39.52401 21.56405  1.000 32.79036  ? 184 LEU   B O     1 
ATOM   3344 C  CB    . LEU   B 1 187 ? 34.47687 37.03545 20.71218  1.000 27.76206  ? 184 LEU   B CB    1 
ATOM   3345 C  CG    . LEU   B 1 187 ? 33.53774 35.91318 21.16682  1.000 28.34638  ? 184 LEU   B CG    1 
ATOM   3346 C  CD1   . LEU   B 1 187 ? 34.17193 34.54314 20.92659  1.000 28.68181  ? 184 LEU   B CD1   1 
ATOM   3347 C  CD2   . LEU   B 1 187 ? 33.15477 36.08126 22.63378  1.000 27.94998  ? 184 LEU   B CD2   1 
ATOM   3348 N  N     . TRP   B 1 188 ? 35.09953 40.21646 19.61175  1.000 33.28458  ? 185 TRP   B N     1 
ATOM   3349 C  CA    . TRP   B 1 188 ? 36.01165 41.33578 19.36183  1.000 33.70140  ? 185 TRP   B CA    1 
ATOM   3350 C  C     . TRP   B 1 188 ? 37.46300 40.97497 19.69663  1.000 34.11408  ? 185 TRP   B C     1 
ATOM   3351 O  O     . TRP   B 1 188 ? 38.11236 41.58086 20.55085  1.000 32.82256  ? 185 TRP   B O     1 
ATOM   3352 C  CB    . TRP   B 1 188 ? 35.54867 42.58321 20.12043  1.000 31.44647  ? 185 TRP   B CB    1 
ATOM   3353 C  CG    . TRP   B 1 188 ? 36.02544 43.87844 19.50886  1.000 33.86735  ? 185 TRP   B CG    1 
ATOM   3354 C  CD1   . TRP   B 1 188 ? 36.72917 44.87160 20.13320  1.000 36.16717  ? 185 TRP   B CD1   1 
ATOM   3355 C  CD2   . TRP   B 1 188 ? 35.84344 44.31318 18.15110  1.000 31.84565  ? 185 TRP   B CD2   1 
ATOM   3356 N  NE1   . TRP   B 1 188 ? 36.98937 45.89781 19.25263  1.000 33.19623  ? 185 TRP   B NE1   1 
ATOM   3357 C  CE2   . TRP   B 1 188 ? 36.45916 45.57829 18.02945  1.000 35.20024  ? 185 TRP   B CE2   1 
ATOM   3358 C  CE3   . TRP   B 1 188 ? 35.22471 43.75502 17.02776  1.000 31.87438  ? 185 TRP   B CE3   1 
ATOM   3359 C  CZ2   . TRP   B 1 188 ? 36.47218 46.29319 16.83061  1.000 36.40508  ? 185 TRP   B CZ2   1 
ATOM   3360 C  CZ3   . TRP   B 1 188 ? 35.23599 44.46546 15.83872  1.000 35.55510  ? 185 TRP   B CZ3   1 
ATOM   3361 C  CH2   . TRP   B 1 188 ? 35.85443 45.72268 15.74967  1.000 37.91806  ? 185 TRP   B CH2   1 
ATOM   3362 N  N     . PHE   B 1 189 ? 37.96239 39.95424 18.99353  1.000 34.58360  ? 186 PHE   B N     1 
ATOM   3363 C  CA    . PHE   B 1 189 ? 39.35110 39.50044 19.08888  1.000 39.04351  ? 186 PHE   B CA    1 
ATOM   3364 C  C     . PHE   B 1 189 ? 39.73036 39.08555 20.50605  1.000 42.86425  ? 186 PHE   B C     1 
ATOM   3365 O  O     . PHE   B 1 189 ? 40.91222 39.12650 20.87641  1.000 42.45559  ? 186 PHE   B O     1 
ATOM   3366 C  CB    . PHE   B 1 189 ? 40.32250 40.56947 18.56960  1.000 41.28295  ? 186 PHE   B CB    1 
ATOM   3367 C  CG    . PHE   B 1 189 ? 40.02361 41.02618 17.16900  1.000 47.93624  ? 186 PHE   B CG    1 
ATOM   3368 C  CD1   . PHE   B 1 189 ? 39.13260 42.06241 16.93740  1.000 50.52225  ? 186 PHE   B CD1   1 
ATOM   3369 C  CD2   . PHE   B 1 189 ? 40.62834 40.41570 16.08307  1.000 53.65765  ? 186 PHE   B CD2   1 
ATOM   3370 C  CE1   . PHE   B 1 189 ? 38.85114 42.48481 15.64624  1.000 56.12396  ? 186 PHE   B CE1   1 
ATOM   3371 C  CE2   . PHE   B 1 189 ? 40.35746 40.83299 14.79018  1.000 57.12210  ? 186 PHE   B CE2   1 
ATOM   3372 C  CZ    . PHE   B 1 189 ? 39.46519 41.86771 14.57006  1.000 58.86557  ? 186 PHE   B CZ    1 
ATOM   3373 N  N     . GLY   B 1 190 ? 38.74407 38.68215 21.30736  1.000 38.74269  ? 187 GLY   B N     1 
ATOM   3374 C  CA    . GLY   B 1 190 ? 38.97815 38.27055 22.67472  1.000 33.33795  ? 187 GLY   B CA    1 
ATOM   3375 C  C     . GLY   B 1 190 ? 39.03068 39.39182 23.68703  1.000 33.92864  ? 187 GLY   B C     1 
ATOM   3376 O  O     . GLY   B 1 190 ? 39.09682 39.11073 24.89055  1.000 32.61108  ? 187 GLY   B O     1 
ATOM   3377 N  N     . SER   B 1 191 ? 38.98494 40.65160 23.24606  1.000 35.68162  ? 188 SER   B N     1 
ATOM   3378 C  CA    . SER   B 1 191 ? 39.18173 41.78038 24.14803  1.000 38.62664  ? 188 SER   B CA    1 
ATOM   3379 C  C     . SER   B 1 191 ? 37.98174 42.04716 25.04907  1.000 36.04349  ? 188 SER   B C     1 
ATOM   3380 O  O     . SER   B 1 191 ? 38.12210 42.77182 26.04102  1.000 34.95137  ? 188 SER   B O     1 
ATOM   3381 C  CB    . SER   B 1 191 ? 39.50966 43.04128 23.34400  1.000 40.73220  ? 188 SER   B CB    1 
ATOM   3382 O  OG    . SER   B 1 191 ? 38.41542 43.42408 22.52752  1.000 35.80400  ? 188 SER   B OG    1 
ATOM   3383 N  N     . VAL   B 1 192 ? 36.80953 41.49087 24.73039  1.000 31.70471  ? 189 VAL   B N     1 
ATOM   3384 C  CA    . VAL   B 1 192 ? 35.63350 41.67610 25.57659  1.000 31.61777  ? 189 VAL   B CA    1 
ATOM   3385 C  C     . VAL   B 1 192 ? 35.73530 40.93338 26.89944  1.000 34.21391  ? 189 VAL   B C     1 
ATOM   3386 O  O     . VAL   B 1 192 ? 34.94080 41.19753 27.80900  1.000 32.59077  ? 189 VAL   B O     1 
ATOM   3387 C  CB    . VAL   B 1 192 ? 34.34844 41.22329 24.85050  1.000 28.90924  ? 189 VAL   B CB    1 
ATOM   3388 C  CG1   . VAL   B 1 192 ? 34.07315 42.10907 23.64090  1.000 28.33980  ? 189 VAL   B CG1   1 
ATOM   3389 C  CG2   . VAL   B 1 192 ? 34.45870 39.76298 24.43534  1.000 26.87550  ? 189 VAL   B CG2   1 
ATOM   3390 N  N     . ALA   B 1 193 ? 36.69623 40.01639 27.03303  1.000 33.25420  ? 190 ALA   B N     1 
ATOM   3391 C  CA    . ALA   B 1 193 ? 36.79358 39.15939 28.20765  1.000 36.65430  ? 190 ALA   B CA    1 
ATOM   3392 C  C     . ALA   B 1 193 ? 37.27862 39.88757 29.45424  1.000 40.64849  ? 190 ALA   B C     1 
ATOM   3393 O  O     . ALA   B 1 193 ? 37.22160 39.30917 30.54452  1.000 43.83429  ? 190 ALA   B O     1 
ATOM   3394 C  CB    . ALA   B 1 193 ? 37.72444 37.97998 27.91734  1.000 33.09618  ? 190 ALA   B CB    1 
ATOM   3395 N  N     . TYR   B 1 194 ? 37.75871 41.12386 29.32815  1.000 38.85136  ? 191 TYR   B N     1 
ATOM   3396 C  CA    . TYR   B 1 194 ? 38.27145 41.86914 30.46480  1.000 41.58253  ? 191 TYR   B CA    1 
ATOM   3397 C  C     . TYR   B 1 194 ? 37.55232 43.21408 30.55708  1.000 45.39332  ? 191 TYR   B C     1 
ATOM   3398 O  O     . TYR   B 1 194 ? 37.21731 43.80631 29.52608  1.000 45.74325  ? 191 TYR   B O     1 
ATOM   3399 C  CB    . TYR   B 1 194 ? 39.79031 42.09758 30.34630  1.000 43.25067  ? 191 TYR   B CB    1 
ATOM   3400 C  CG    . TYR   B 1 194 ? 40.56808 40.85986 29.93810  1.000 45.70516  ? 191 TYR   B CG    1 
ATOM   3401 C  CD1   . TYR   B 1 194 ? 40.80925 40.58015 28.59864  1.000 46.25045  ? 191 TYR   B CD1   1 
ATOM   3402 C  CD2   . TYR   B 1 194 ? 41.05363 39.96857 30.88983  1.000 49.45715  ? 191 TYR   B CD2   1 
ATOM   3403 C  CE1   . TYR   B 1 194 ? 41.51174 39.44923 28.21497  1.000 48.24009  ? 191 TYR   B CE1   1 
ATOM   3404 C  CE2   . TYR   B 1 194 ? 41.76229 38.83208 30.51575  1.000 50.00550  ? 191 TYR   B CE2   1 
ATOM   3405 C  CZ    . TYR   B 1 194 ? 41.98714 38.57857 29.17657  1.000 51.78343  ? 191 TYR   B CZ    1 
ATOM   3406 O  OH    . TYR   B 1 194 ? 42.68559 37.45161 28.79428  1.000 54.20075  ? 191 TYR   B OH    1 
ATOM   3407 N  N     . PRO   B 1 195 ? 37.28991 43.70117 31.77251  1.000 47.41090  ? 192 PRO   B N     1 
ATOM   3408 C  CA    . PRO   B 1 195 ? 36.68138 45.03887 31.89198  1.000 49.43963  ? 192 PRO   B CA    1 
ATOM   3409 C  C     . PRO   B 1 195 ? 37.55569 46.13917 31.31927  1.000 48.48241  ? 192 PRO   B C     1 
ATOM   3410 O  O     . PRO   B 1 195 ? 37.04467 47.05576 30.66343  1.000 48.24756  ? 192 PRO   B O     1 
ATOM   3411 C  CB    . PRO   B 1 195 ? 36.48262 45.19532 33.40708  1.000 51.68236  ? 192 PRO   B CB    1 
ATOM   3412 C  CG    . PRO   B 1 195 ? 36.49004 43.79414 33.94627  1.000 49.20008  ? 192 PRO   B CG    1 
ATOM   3413 C  CD    . PRO   B 1 195 ? 37.44458 43.04157 33.07841  1.000 47.89536  ? 192 PRO   B CD    1 
ATOM   3414 N  N     . GLU   B 1 196 ? 38.86427 46.07194 31.55106  1.000 46.02764  ? 193 GLU   B N     1 
ATOM   3415 C  CA    . GLU   B 1 196 ? 39.82336 47.01866 31.00272  1.000 51.25288  ? 193 GLU   B CA    1 
ATOM   3416 C  C     . GLU   B 1 196 ? 40.77638 46.28589 30.07033  1.000 47.88926  ? 193 GLU   B C     1 
ATOM   3417 O  O     . GLU   B 1 196 ? 41.21178 45.16827 30.36494  1.000 48.53862  ? 193 GLU   B O     1 
ATOM   3418 C  CB    . GLU   B 1 196 ? 40.61294 47.72519 32.11353  1.000 57.34996  ? 193 GLU   B CB    1 
ATOM   3419 C  CG    . GLU   B 1 196 ? 39.81239 48.76207 32.88260  1.000 65.83756  ? 193 GLU   B CG    1 
ATOM   3420 C  CD    . GLU   B 1 196 ? 40.62865 49.43979 33.96569  1.000 75.95645  ? 193 GLU   B CD    1 
ATOM   3421 O  OE1   . GLU   B 1 196 ? 40.25762 49.32378 35.15334  1.000 79.57475  ? 193 GLU   B OE1   1 
ATOM   3422 O  OE2   . GLU   B 1 196 ? 41.64861 50.07977 33.63020  1.000 79.48431  ? 193 GLU   B OE2   1 
ATOM   3423 N  N     . TYR   B 1 197 ? 41.09694 46.92248 28.94197  1.000 46.28437  ? 194 TYR   B N     1 
ATOM   3424 C  CA    . TYR   B 1 197 ? 41.95315 46.32766 27.92724  1.000 44.04332  ? 194 TYR   B CA    1 
ATOM   3425 C  C     . TYR   B 1 197 ? 42.92107 47.40859 27.45860  1.000 41.11443  ? 194 TYR   B C     1 
ATOM   3426 O  O     . TYR   B 1 197 ? 42.48705 48.53648 27.16320  1.000 43.03213  ? 194 TYR   B O     1 
ATOM   3427 C  CB    . TYR   B 1 197 ? 41.13828 45.78466 26.75285  1.000 41.74247  ? 194 TYR   B CB    1 
ATOM   3428 C  CG    . TYR   B 1 197 ? 41.87385 44.77031 25.91443  1.000 38.74449  ? 194 TYR   B CG    1 
ATOM   3429 C  CD1   . TYR   B 1 197 ? 42.62931 45.16274 24.81830  1.000 35.68990  ? 194 TYR   B CD1   1 
ATOM   3430 C  CD2   . TYR   B 1 197 ? 41.81083 43.41792 26.21928  1.000 34.35950  ? 194 TYR   B CD2   1 
ATOM   3431 C  CE1   . TYR   B 1 197 ? 43.29584 44.23868 24.04830  1.000 33.45850  ? 194 TYR   B CE1   1 
ATOM   3432 C  CE2   . TYR   B 1 197 ? 42.47356 42.48503 25.45373  1.000 33.77084  ? 194 TYR   B CE2   1 
ATOM   3433 C  CZ    . TYR   B 1 197 ? 43.21514 42.90328 24.36810  1.000 35.57875  ? 194 TYR   B CZ    1 
ATOM   3434 O  OH    . TYR   B 1 197 ? 43.88698 41.98246 23.60143  1.000 40.99407  ? 194 TYR   B OH    1 
ATOM   3435 N  N     . PRO   B 1 198 ? 44.21335 47.10497 27.35944  1.000 39.55812  ? 195 PRO   B N     1 
ATOM   3436 C  CA    . PRO   B 1 198 ? 45.19930 48.16403 27.12066  1.000 41.13796  ? 195 PRO   B CA    1 
ATOM   3437 C  C     . PRO   B 1 198 ? 45.37501 48.50075 25.64629  1.000 42.90812  ? 195 PRO   B C     1 
ATOM   3438 O  O     . PRO   B 1 198 ? 45.22842 47.64911 24.76576  1.000 43.59911  ? 195 PRO   B O     1 
ATOM   3439 C  CB    . PRO   B 1 198 ? 46.49497 47.57576 27.70395  1.000 43.52049  ? 195 PRO   B CB    1 
ATOM   3440 C  CG    . PRO   B 1 198 ? 46.18731 46.12109 28.05872  1.000 37.85266  ? 195 PRO   B CG    1 
ATOM   3441 C  CD    . PRO   B 1 198 ? 44.85050 45.78423 27.48724  1.000 38.76052  ? 195 PRO   B CD    1 
ATOM   3442 N  N     . GLY   B 1 199 ? 45.66636 49.77680 25.39348  1.000 42.00019  ? 196 GLY   B N     1 
ATOM   3443 C  CA    . GLY   B 1 199 ? 46.30159 50.21779 24.16194  1.000 41.68490  ? 196 GLY   B CA    1 
ATOM   3444 C  C     . GLY   B 1 199 ? 45.52055 50.05914 22.87747  1.000 40.69267  ? 196 GLY   B C     1 
ATOM   3445 O  O     . GLY   B 1 199 ? 46.12836 49.93935 21.81053  1.000 41.86409  ? 196 GLY   B O     1 
ATOM   3446 N  N     . LEU   B 1 200 ? 44.19472 50.08055 22.93463  1.000 37.20037  ? 197 LEU   B N     1 
ATOM   3447 C  CA    . LEU   B 1 200 ? 43.41002 49.99296 21.71217  1.000 37.49589  ? 197 LEU   B CA    1 
ATOM   3448 C  C     . LEU   B 1 200 ? 43.24347 51.36628 21.06915  1.000 39.39362  ? 197 LEU   B C     1 
ATOM   3449 O  O     . LEU   B 1 200 ? 43.28398 52.40159 21.73971  1.000 41.48102  ? 197 LEU   B O     1 
ATOM   3450 C  CB    . LEU   B 1 200 ? 42.03295 49.38439 21.99277  1.000 40.80281  ? 197 LEU   B CB    1 
ATOM   3451 C  CG    . LEU   B 1 200 ? 42.04188 47.94551 22.51193  1.000 37.94061  ? 197 LEU   B CG    1 
ATOM   3452 C  CD1   . LEU   B 1 200 ? 40.62828 47.40836 22.61727  1.000 32.26625  ? 197 LEU   B CD1   1 
ATOM   3453 C  CD2   . LEU   B 1 200 ? 42.89775 47.05442 21.62180  1.000 41.01001  ? 197 LEU   B CD2   1 
ATOM   3454 N  N     . HIS   B 1 201 ? 43.06547 51.36504 19.75152  1.000 42.29878  ? 198 HIS   B N     1 
ATOM   3455 C  CA    . HIS   B 1 201 ? 42.63859 52.57367 19.06295  1.000 43.47270  ? 198 HIS   B CA    1 
ATOM   3456 C  C     . HIS   B 1 201 ? 41.28761 53.01875 19.62721  1.000 42.86089  ? 198 HIS   B C     1 
ATOM   3457 O  O     . HIS   B 1 201 ? 40.46158 52.17136 19.98326  1.000 40.30509  ? 198 HIS   B O     1 
ATOM   3458 C  CB    . HIS   B 1 201 ? 42.53620 52.31632 17.55683  1.000 45.63854  ? 198 HIS   B CB    1 
ATOM   3459 C  CG    . HIS   B 1 201 ? 42.06998 53.49853 16.76267  1.000 53.86311  ? 198 HIS   B CG    1 
ATOM   3460 N  ND1   . HIS   B 1 201 ? 40.75020 53.89513 16.72082  1.000 54.25653  ? 198 HIS   B ND1   1 
ATOM   3461 C  CD2   . HIS   B 1 201 ? 42.74595 54.36033 15.96565  1.000 56.40728  ? 198 HIS   B CD2   1 
ATOM   3462 C  CE1   . HIS   B 1 201 ? 40.63442 54.95681 15.94292  1.000 54.98809  ? 198 HIS   B CE1   1 
ATOM   3463 N  NE2   . HIS   B 1 201 ? 41.83057 55.25885 15.47108  1.000 56.90529  ? 198 HIS   B NE2   1 
ATOM   3464 N  N     . PRO   B 1 202 ? 41.04341 54.33069 19.74792  1.000 41.53780  ? 199 PRO   B N     1 
ATOM   3465 C  CA    . PRO   B 1 202 ? 39.78027 54.79144 20.35898  1.000 38.85778  ? 199 PRO   B CA    1 
ATOM   3466 C  C     . PRO   B 1 202 ? 38.52617 54.14933 19.78506  1.000 41.27610  ? 199 PRO   B C     1 
ATOM   3467 O  O     . PRO   B 1 202 ? 37.58670 53.86982 20.53938  1.000 39.31741  ? 199 PRO   B O     1 
ATOM   3468 C  CB    . PRO   B 1 202 ? 39.81394 56.30347 20.09999  1.000 37.05615  ? 199 PRO   B CB    1 
ATOM   3469 C  CG    . PRO   B 1 202 ? 41.27634 56.63391 20.11356  1.000 38.62538  ? 199 PRO   B CG    1 
ATOM   3470 C  CD    . PRO   B 1 202 ? 41.96988 55.44730 19.48514  1.000 38.43664  ? 199 PRO   B CD    1 
ATOM   3471 N  N     . GLU   B 1 203 ? 38.48030 53.89626 18.47612  1.000 44.79289  ? 200 GLU   B N     1 
ATOM   3472 C  CA    . GLU   B 1 203 ? 37.30057 53.25057 17.90760  1.000 47.24728  ? 200 GLU   B CA    1 
ATOM   3473 C  C     . GLU   B 1 203 ? 37.24221 51.76810 18.25586  1.000 39.90489  ? 200 GLU   B C     1 
ATOM   3474 O  O     . GLU   B 1 203 ? 36.14875 51.20571 18.37211  1.000 39.14804  ? 200 GLU   B O     1 
ATOM   3475 C  CB    . GLU   B 1 203 ? 37.26341 53.44965 16.39305  1.000 54.44864  ? 200 GLU   B CB    1 
ATOM   3476 C  CG    . GLU   B 1 203 ? 36.99387 54.88554 15.99271  1.000 65.62216  ? 200 GLU   B CG    1 
ATOM   3477 C  CD    . GLU   B 1 203 ? 35.81649 55.48394 16.74892  1.000 73.56653  ? 200 GLU   B CD    1 
ATOM   3478 O  OE1   . GLU   B 1 203 ? 34.67908 54.98875 16.58154  1.000 73.26154  ? 200 GLU   B OE1   1 
ATOM   3479 O  OE2   . GLU   B 1 203 ? 36.03298 56.44279 17.52298  1.000 75.73129  ? 200 GLU   B OE2   1 
ATOM   3480 N  N     . GLU   B 1 204 ? 38.39523 51.11775 18.42279  1.000 39.79226  ? 201 GLU   B N     1 
ATOM   3481 C  CA    . GLU   B 1 204 ? 38.39021 49.72603 18.86495  1.000 36.69440  ? 201 GLU   B CA    1 
ATOM   3482 C  C     . GLU   B 1 204 ? 37.93327 49.60552 20.31053  1.000 33.77905  ? 201 GLU   B C     1 
ATOM   3483 O  O     . GLU   B 1 204 ? 37.30380 48.60673 20.67913  1.000 33.17872  ? 201 GLU   B O     1 
ATOM   3484 C  CB    . GLU   B 1 204 ? 39.77971 49.11002 18.70121  1.000 37.88134  ? 201 GLU   B CB    1 
ATOM   3485 C  CG    . GLU   B 1 204 ? 40.17876 48.85774 17.26208  1.000 42.89782  ? 201 GLU   B CG    1 
ATOM   3486 C  CD    . GLU   B 1 204 ? 41.61183 48.36701 17.13459  1.000 47.79602  ? 201 GLU   B CD    1 
ATOM   3487 O  OE1   . GLU   B 1 204 ? 42.49203 48.89948 17.84612  1.000 46.59268  ? 201 GLU   B OE1   1 
ATOM   3488 O  OE2   . GLU   B 1 204 ? 41.85533 47.43958 16.33283  1.000 49.42521  ? 201 GLU   B OE2   1 
ATOM   3489 N  N     . GLU   B 1 205 ? 38.24240 50.60891 21.13824  1.000 32.34789  ? 202 GLU   B N     1 
ATOM   3490 C  CA    . GLU   B 1 205 ? 37.78660 50.60216 22.52504  1.000 34.70568  ? 202 GLU   B CA    1 
ATOM   3491 C  C     . GLU   B 1 205 ? 36.28733 50.87790 22.62111  1.000 34.71252  ? 202 GLU   B C     1 
ATOM   3492 O  O     . GLU   B 1 205 ? 35.59779 50.29558 23.46737  1.000 34.74257  ? 202 GLU   B O     1 
ATOM   3493 C  CB    . GLU   B 1 205 ? 38.58057 51.62534 23.34138  1.000 33.81479  ? 202 GLU   B CB    1 
ATOM   3494 C  CG    . GLU   B 1 205 ? 38.15706 51.73137 24.80922  1.000 41.65026  ? 202 GLU   B CG    1 
ATOM   3495 C  CD    . GLU   B 1 205 ? 38.53742 50.51009 25.64050  1.000 46.91727  ? 202 GLU   B CD    1 
ATOM   3496 O  OE1   . GLU   B 1 205 ? 39.18015 49.58288 25.10411  1.000 49.35547  ? 202 GLU   B OE1   1 
ATOM   3497 O  OE2   . GLU   B 1 205 ? 38.19645 50.47784 26.84178  1.000 48.48817  ? 202 GLU   B OE2   1 
ATOM   3498 N  N     . VAL   B 1 206 ? 35.76723 51.76646 21.76888  1.000 33.61295  ? 203 VAL   B N     1 
ATOM   3499 C  CA    . VAL   B 1 206 ? 34.32683 52.02257 21.73741  1.000 33.76517  ? 203 VAL   B CA    1 
ATOM   3500 C  C     . VAL   B 1 206 ? 33.57498 50.75770 21.34167  1.000 33.90805  ? 203 VAL   B C     1 
ATOM   3501 O  O     . VAL   B 1 206 ? 32.56516 50.39310 21.95586  1.000 36.00791  ? 203 VAL   B O     1 
ATOM   3502 C  CB    . VAL   B 1 206 ? 34.00803 53.19021 20.78402  1.000 34.33958  ? 203 VAL   B CB    1 
ATOM   3503 C  CG1   . VAL   B 1 206 ? 32.50131 53.27160 20.50059  1.000 36.97721  ? 203 VAL   B CG1   1 
ATOM   3504 C  CG2   . VAL   B 1 206 ? 34.51163 54.50448 21.36319  1.000 32.67186  ? 203 VAL   B CG2   1 
ATOM   3505 N  N     . ALA   B 1 207 ? 34.06098 50.06745 20.30804  1.000 31.63448  ? 204 ALA   B N     1 
ATOM   3506 C  CA    . ALA   B 1 207 ? 33.43264 48.82094 19.88694  1.000 30.81143  ? 204 ALA   B CA    1 
ATOM   3507 C  C     . ALA   B 1 207 ? 33.51608 47.76167 20.98026  1.000 33.38586  ? 204 ALA   B C     1 
ATOM   3508 O  O     . ALA   B 1 207 ? 32.56252 47.00304 21.19260  1.000 33.07272  ? 204 ALA   B O     1 
ATOM   3509 C  CB    . ALA   B 1 207 ? 34.08410 48.31790 18.59715  1.000 29.83518  ? 204 ALA   B CB    1 
ATOM   3510 N  N     . ARG   B 1 208 ? 34.64853 47.69578 21.68656  1.000 31.95197  ? 205 ARG   B N     1 
ATOM   3511 C  CA    . ARG   B 1 208 ? 34.81025 46.70055 22.74385  1.000 32.52929  ? 205 ARG   B CA    1 
ATOM   3512 C  C     . ARG   B 1 208 ? 33.79913 46.91628 23.86421  1.000 32.45870  ? 205 ARG   B C     1 
ATOM   3513 O  O     . ARG   B 1 208 ? 33.12262 45.97496 24.29602  1.000 31.90362  ? 205 ARG   B O     1 
ATOM   3514 C  CB    . ARG   B 1 208 ? 36.23421 46.74689 23.29910  1.000 33.00498  ? 205 ARG   B CB    1 
ATOM   3515 C  CG    . ARG   B 1 208 ? 36.52335 45.65612 24.32352  1.000 34.33435  ? 205 ARG   B CG    1 
ATOM   3516 C  CD    . ARG   B 1 208 ? 37.90916 45.80219 24.92385  1.000 34.87834  ? 205 ARG   B CD    1 
ATOM   3517 N  NE    . ARG   B 1 208 ? 37.96348 46.86301 25.92480  1.000 35.25426  ? 205 ARG   B NE    1 
ATOM   3518 C  CZ    . ARG   B 1 208 ? 37.67738 46.68491 27.21080  1.000 34.52994  ? 205 ARG   B CZ    1 
ATOM   3519 N  NH1   . ARG   B 1 208 ? 37.32332 45.48709 27.65225  1.000 33.31011  ? 205 ARG   B NH1   1 
ATOM   3520 N  NH2   . ARG   B 1 208 ? 37.74865 47.69989 28.05727  1.000 37.47996  ? 205 ARG   B NH2   1 
ATOM   3521 N  N     . LEU   B 1 209 ? 33.70196 48.15239 24.36434  1.000 31.37371  ? 206 LEU   B N     1 
ATOM   3522 C  CA    . LEU   B 1 209 ? 32.71987 48.45923 25.39712  1.000 35.03409  ? 206 LEU   B CA    1 
ATOM   3523 C  C     . LEU   B 1 209 ? 31.30368 48.26122 24.88242  1.000 36.80957  ? 206 LEU   B C     1 
ATOM   3524 O  O     . LEU   B 1 209 ? 30.41460 47.86425 25.64227  1.000 41.08832  ? 206 LEU   B O     1 
ATOM   3525 C  CB    . LEU   B 1 209 ? 32.90415 49.89377 25.89137  1.000 34.81039  ? 206 LEU   B CB    1 
ATOM   3526 C  CG    . LEU   B 1 209 ? 34.23009 50.21890 26.58154  1.000 36.84947  ? 206 LEU   B CG    1 
ATOM   3527 C  CD1   . LEU   B 1 209 ? 34.35283 51.71974 26.83464  1.000 32.88190  ? 206 LEU   B CD1   1 
ATOM   3528 C  CD2   . LEU   B 1 209 ? 34.35055 49.43693 27.88705  1.000 37.39829  ? 206 LEU   B CD2   1 
ATOM   3529 N  N     . SER   B 1 210 ? 31.07666 48.52936 23.59688  1.000 33.09518  ? 207 SER   B N     1 
ATOM   3530 C  CA    . SER   B 1 210 ? 29.75866 48.30475 23.01992  1.000 32.18198  ? 207 SER   B CA    1 
ATOM   3531 C  C     . SER   B 1 210 ? 29.41173 46.82012 23.00446  1.000 33.18125  ? 207 SER   B C     1 
ATOM   3532 O  O     . SER   B 1 210 ? 28.26969 46.44163 23.28724  1.000 30.75705  ? 207 SER   B O     1 
ATOM   3533 C  CB    . SER   B 1 210 ? 29.70184 48.89200 21.60969  1.000 32.09310  ? 207 SER   B CB    1 
ATOM   3534 O  OG    . SER   B 1 210 ? 28.41861 48.70574 21.04237  1.000 43.32710  ? 207 SER   B OG    1 
ATOM   3535 N  N     . PHE   B 1 211 ? 30.38818 45.95899 22.69156  1.000 30.23809  ? 208 PHE   B N     1 
ATOM   3536 C  CA    . PHE   B 1 211 ? 30.10737 44.52543 22.63430  1.000 30.53467  ? 208 PHE   B CA    1 
ATOM   3537 C  C     . PHE   B 1 211 ? 29.92504 43.93302 24.02594  1.000 28.69302  ? 208 PHE   B C     1 
ATOM   3538 O  O     . PHE   B 1 211 ? 29.09889 43.03469 24.21638  1.000 30.69971  ? 208 PHE   B O     1 
ATOM   3539 C  CB    . PHE   B 1 211 ? 31.21206 43.79354 21.87482  1.000 29.51139  ? 208 PHE   B CB    1 
ATOM   3540 C  CG    . PHE   B 1 211 ? 31.03961 43.83382 20.38171  1.000 33.38645  ? 208 PHE   B CG    1 
ATOM   3541 C  CD1   . PHE   B 1 211 ? 29.92028 43.26632 19.79175  1.000 32.86298  ? 208 PHE   B CD1   1 
ATOM   3542 C  CD2   . PHE   B 1 211 ? 31.98593 44.44161 19.56896  1.000 33.13094  ? 208 PHE   B CD2   1 
ATOM   3543 C  CE1   . PHE   B 1 211 ? 29.74618 43.29549 18.41947  1.000 32.42252  ? 208 PHE   B CE1   1 
ATOM   3544 C  CE2   . PHE   B 1 211 ? 31.81878 44.47730 18.19468  1.000 35.62742  ? 208 PHE   B CE2   1 
ATOM   3545 C  CZ    . PHE   B 1 211 ? 30.69498 43.90267 17.62025  1.000 38.39881  ? 208 PHE   B CZ    1 
ATOM   3546 N  N     . ARG   B 1 212 ? 30.68733 44.41529 25.00986  1.000 29.31183  ? 209 ARG   B N     1 
ATOM   3547 C  CA    . ARG   B 1 212 ? 30.46551 43.98249 26.38574  1.000 30.52538  ? 209 ARG   B CA    1 
ATOM   3548 C  C     . ARG   B 1 212 ? 29.04717 44.30889 26.84037  1.000 35.27880  ? 209 ARG   B C     1 
ATOM   3549 O  O     . ARG   B 1 212 ? 28.38519 43.47635 27.47195  1.000 34.58338  ? 209 ARG   B O     1 
ATOM   3550 C  CB    . ARG   B 1 212 ? 31.49973 44.62279 27.31511  1.000 30.66974  ? 209 ARG   B CB    1 
ATOM   3551 C  CG    . ARG   B 1 212 ? 32.86602 43.93714 27.26196  1.000 30.33516  ? 209 ARG   B CG    1 
ATOM   3552 C  CD    . ARG   B 1 212 ? 33.87530 44.57703 28.21363  1.000 30.16772  ? 209 ARG   B CD    1 
ATOM   3553 N  NE    . ARG   B 1 212 ? 33.43220 44.54460 29.60676  1.000 32.06963  ? 209 ARG   B NE    1 
ATOM   3554 C  CZ    . ARG   B 1 212 ? 33.56920 43.50186 30.42145  1.000 33.83983  ? 209 ARG   B CZ    1 
ATOM   3555 N  NH1   . ARG   B 1 212 ? 34.13458 42.38197 29.99020  1.000 33.10326  ? 209 ARG   B NH1   1 
ATOM   3556 N  NH2   . ARG   B 1 212 ? 33.13268 43.57883 31.67190  1.000 35.18311  ? 209 ARG   B NH2   1 
ATOM   3557 N  N     . ASN   B 1 213 ? 28.55873 45.51142 26.51436  1.000 34.31744  ? 210 ASN   B N     1 
ATOM   3558 C  CA    . ASN   B 1 213 ? 27.18177 45.87440 26.84620  1.000 33.33149  ? 210 ASN   B CA    1 
ATOM   3559 C  C     . ASN   B 1 213 ? 26.17779 45.03937 26.05784  1.000 35.02365  ? 210 ASN   B C     1 
ATOM   3560 O  O     . ASN   B 1 213 ? 25.18232 44.56366 26.61937  1.000 36.46194  ? 210 ASN   B O     1 
ATOM   3561 C  CB    . ASN   B 1 213 ? 26.95472 47.36638 26.59135  1.000 33.79968  ? 210 ASN   B CB    1 
ATOM   3562 C  CG    . ASN   B 1 213 ? 27.70832 48.24890 27.57640  1.000 43.50534  ? 210 ASN   B CG    1 
ATOM   3563 O  OD1   . ASN   B 1 213 ? 27.88764 47.88546 28.74053  1.000 46.80883  ? 210 ASN   B OD1   1 
ATOM   3564 N  ND2   . ASN   B 1 213 ? 28.15585 49.41314 27.11185  1.000 42.02926  ? 210 ASN   B ND2   1 
ATOM   3565 N  N     . LEU   B 1 214 ? 26.41840 44.85106 24.75586  1.000 33.30803  ? 211 LEU   B N     1 
ATOM   3566 C  CA    . LEU   B 1 214 ? 25.48268 44.08905 23.93249  1.000 33.62152  ? 211 LEU   B CA    1 
ATOM   3567 C  C     . LEU   B 1 214 ? 25.38597 42.63697 24.39101  1.000 34.58090  ? 211 LEU   B C     1 
ATOM   3568 O  O     . LEU   B 1 214 ? 24.28818 42.07075 24.45211  1.000 31.36834  ? 211 LEU   B O     1 
ATOM   3569 C  CB    . LEU   B 1 214 ? 25.89746 44.15323 22.46419  1.000 33.54369  ? 211 LEU   B CB    1 
ATOM   3570 C  CG    . LEU   B 1 214 ? 25.05343 43.29533 21.51797  1.000 33.13640  ? 211 LEU   B CG    1 
ATOM   3571 C  CD1   . LEU   B 1 214 ? 23.73845 43.98922 21.19279  1.000 33.28047  ? 211 LEU   B CD1   1 
ATOM   3572 C  CD2   . LEU   B 1 214 ? 25.81737 42.95311 20.24834  1.000 33.68967  ? 211 LEU   B CD2   1 
ATOM   3573 N  N     . ASN   B 1 215 ? 26.52396 42.01446 24.71114  1.000 32.77615  ? 212 ASN   B N     1 
ATOM   3574 C  CA    . ASN   B 1 215 ? 26.49993 40.62418 25.15933  1.000 32.40403  ? 212 ASN   B CA    1 
ATOM   3575 C  C     . ASN   B 1 215 ? 25.70135 40.46928 26.44907  1.000 30.83887  ? 212 ASN   B C     1 
ATOM   3576 O  O     . ASN   B 1 215 ? 24.91402 39.52643 26.59008  1.000 29.39661  ? 212 ASN   B O     1 
ATOM   3577 C  CB    . ASN   B 1 215 ? 27.92518 40.10295 25.34546  1.000 33.08369  ? 212 ASN   B CB    1 
ATOM   3578 C  CG    . ASN   B 1 215 ? 28.71081 40.08653 24.04928  1.000 36.66142  ? 212 ASN   B CG    1 
ATOM   3579 O  OD1   . ASN   B 1 215 ? 28.13129 40.15102 22.96179  1.000 35.16010  ? 212 ASN   B OD1   1 
ATOM   3580 N  ND2   . ASN   B 1 215 ? 30.03693 40.00032 24.15526  1.000 32.58230  ? 212 ASN   B ND2   1 
ATOM   3581 N  N     . THR   B 1 216 ? 25.88703 41.38644 27.40064  1.000 30.94941  ? 213 THR   B N     1 
ATOM   3582 C  CA    . THR   B 1 216 ? 25.11236 41.33674 28.63759  1.000 32.07584  ? 213 THR   B CA    1 
ATOM   3583 C  C     . THR   B 1 216 ? 23.62984 41.57014 28.36734  1.000 30.99531  ? 213 THR   B C     1 
ATOM   3584 O  O     . THR   B 1 216 ? 22.77062 40.89526 28.94619  1.000 30.99842  ? 213 THR   B O     1 
ATOM   3585 C  CB    . THR   B 1 216 ? 25.65428 42.36644 29.63634  1.000 33.07099  ? 213 THR   B CB    1 
ATOM   3586 O  OG1   . THR   B 1 216 ? 26.96111 41.96644 30.07699  1.000 31.92694  ? 213 THR   B OG1   1 
ATOM   3587 C  CG2   . THR   B 1 216 ? 24.73145 42.49362 30.84731  1.000 27.56686  ? 213 THR   B CG2   1 
ATOM   3588 N  N     . PHE   B 1 217 ? 23.31194 42.50902 27.47421  1.000 32.42163  ? 214 PHE   B N     1 
ATOM   3589 C  CA    . PHE   B 1 217 ? 21.91500 42.82173 27.19464  1.000 30.47021  ? 214 PHE   B CA    1 
ATOM   3590 C  C     . PHE   B 1 217 ? 21.21719 41.65676 26.50320  1.000 36.83252  ? 214 PHE   B C     1 
ATOM   3591 O  O     . PHE   B 1 217 ? 20.11708 41.25416 26.90478  1.000 34.62387  ? 214 PHE   B O     1 
ATOM   3592 C  CB    . PHE   B 1 217 ? 21.81626 44.08923 26.34613  1.000 28.80683  ? 214 PHE   B CB    1 
ATOM   3593 C  CG    . PHE   B 1 217 ? 20.40373 44.48446 26.01743  1.000 35.92046  ? 214 PHE   B CG    1 
ATOM   3594 C  CD1   . PHE   B 1 217 ? 19.67881 45.29372 26.87902  1.000 36.41396  ? 214 PHE   B CD1   1 
ATOM   3595 C  CD2   . PHE   B 1 217 ? 19.79429 44.03755 24.85276  1.000 37.24160  ? 214 PHE   B CD2   1 
ATOM   3596 C  CE1   . PHE   B 1 217 ? 18.37971 45.65640 26.58088  1.000 36.62058  ? 214 PHE   B CE1   1 
ATOM   3597 C  CE2   . PHE   B 1 217 ? 18.49508 44.39372 24.55502  1.000 35.70282  ? 214 PHE   B CE2   1 
ATOM   3598 C  CZ    . PHE   B 1 217 ? 17.78885 45.20295 25.41920  1.000 36.95486  ? 214 PHE   B CZ    1 
ATOM   3599 N  N     . LEU   B 1 218 ? 21.84229 41.10211 25.45758  1.000 34.61828  ? 215 LEU   B N     1 
ATOM   3600 C  CA    . LEU   B 1 218 ? 21.21921 40.00633 24.71991  1.000 33.66202  ? 215 LEU   B CA    1 
ATOM   3601 C  C     . LEU   B 1 218 ? 20.97345 38.80014 25.61986  1.000 34.82328  ? 215 LEU   B C     1 
ATOM   3602 O  O     . LEU   B 1 218 ? 19.95456 38.11155 25.48571  1.000 34.00052  ? 215 LEU   B O     1 
ATOM   3603 C  CB    . LEU   B 1 218 ? 22.08707 39.61516 23.52424  1.000 29.70171  ? 215 LEU   B CB    1 
ATOM   3604 C  CG    . LEU   B 1 218 ? 22.23430 40.64514 22.40272  1.000 29.29866  ? 215 LEU   B CG    1 
ATOM   3605 C  CD1   . LEU   B 1 218 ? 23.04699 40.06006 21.26333  1.000 28.33890  ? 215 LEU   B CD1   1 
ATOM   3606 C  CD2   . LEU   B 1 218 ? 20.86673 41.11640 21.90764  1.000 28.88772  ? 215 LEU   B CD2   1 
ATOM   3607 N  N     . ALA   B 1 219 ? 21.89342 38.53455 26.55123  1.000 32.85705  ? 216 ALA   B N     1 
ATOM   3608 C  CA    . ALA   B 1 219 ? 21.73035 37.40280 27.46064  1.000 31.75310  ? 216 ALA   B CA    1 
ATOM   3609 C  C     . ALA   B 1 219 ? 20.52011 37.57145 28.37299  1.000 28.93086  ? 216 ALA   B C     1 
ATOM   3610 O  O     . ALA   B 1 219 ? 19.98039 36.57885 28.87737  1.000 31.47914  ? 216 ALA   B O     1 
ATOM   3611 C  CB    . ALA   B 1 219 ? 22.99951 37.21633 28.29333  1.000 25.64245  ? 216 ALA   B CB    1 
ATOM   3612 N  N     . ALA   B 1 220 ? 20.07410 38.80786 28.58516  1.000 28.88486  ? 217 ALA   B N     1 
ATOM   3613 C  CA    . ALA   B 1 220 ? 18.94062 39.10127 29.45104  1.000 36.03488  ? 217 ALA   B CA    1 
ATOM   3614 C  C     . ALA   B 1 220 ? 17.67329 39.46736 28.68464  1.000 37.15660  ? 217 ALA   B C     1 
ATOM   3615 O  O     . ALA   B 1 220 ? 16.63709 39.71044 29.31099  1.000 36.36778  ? 217 ALA   B O     1 
ATOM   3616 C  CB    . ALA   B 1 220 ? 19.30068 40.23482 30.41234  1.000 35.78945  ? 217 ALA   B CB    1 
ATOM   3617 N  N     . ASP   B 1 221 ? 17.72678 39.49969 27.35194  1.000 34.54126  ? 218 ASP   B N     1 
ATOM   3618 C  CA    . ASP   B 1 221 ? 16.61753 39.93511 26.51012  1.000 32.34246  ? 218 ASP   B CA    1 
ATOM   3619 C  C     . ASP   B 1 221 ? 15.58086 38.82528 26.36872  1.000 35.67401  ? 218 ASP   B C     1 
ATOM   3620 O  O     . ASP   B 1 221 ? 15.85108 37.79719 25.73475  1.000 36.73318  ? 218 ASP   B O     1 
ATOM   3621 C  CB    . ASP   B 1 221 ? 17.14314 40.35926 25.13671  1.000 33.19088  ? 218 ASP   B CB    1 
ATOM   3622 C  CG    . ASP   B 1 221 ? 16.10134 41.07504 24.29210  1.000 38.75135  ? 218 ASP   B CG    1 
ATOM   3623 O  OD1   . ASP   B 1 221 ? 14.89902 41.05906 24.64196  1.000 38.31597  ? 218 ASP   B OD1   1 
ATOM   3624 O  OD2   . ASP   B 1 221 ? 16.50104 41.66440 23.26490  1.000 37.91010  ? 218 ASP   B OD2   1 
ATOM   3625 N  N     . PRO   B 1 222 ? 14.38346 38.99731 26.93809  1.000 34.47442  ? 219 PRO   B N     1 
ATOM   3626 C  CA    . PRO   B 1 222 ? 13.36340 37.93896 26.85188  1.000 34.41563  ? 219 PRO   B CA    1 
ATOM   3627 C  C     . PRO   B 1 222 ? 12.72160 37.81068 25.48032  1.000 35.18240  ? 219 PRO   B C     1 
ATOM   3628 O  O     . PRO   B 1 222 ? 11.99601 36.83572 25.24759  1.000 38.48967  ? 219 PRO   B O     1 
ATOM   3629 C  CB    . PRO   B 1 222 ? 12.33095 38.36532 27.90127  1.000 32.73213  ? 219 PRO   B CB    1 
ATOM   3630 C  CG    . PRO   B 1 222 ? 12.44749 39.85859 27.93339  1.000 33.89951  ? 219 PRO   B CG    1 
ATOM   3631 C  CD    . PRO   B 1 222 ? 13.91136 40.16524 27.70294  1.000 34.57701  ? 219 PRO   B CD    1 
ATOM   3632 N  N     . ARG   B 1 223 ? 12.95497 38.75454 24.56832  1.000 32.86720  ? 220 ARG   B N     1 
ATOM   3633 C  CA    . ARG   B 1 223 ? 12.38181 38.64346 23.23316  1.000 30.69853  ? 220 ARG   B CA    1 
ATOM   3634 C  C     . ARG   B 1 223 ? 13.07103 37.58005 22.38929  1.000 32.72241  ? 220 ARG   B C     1 
ATOM   3635 O  O     . ARG   B 1 223 ? 12.52857 37.19085 21.34921  1.000 33.19166  ? 220 ARG   B O     1 
ATOM   3636 C  CB    . ARG   B 1 223 ? 12.44731 39.99561 22.51680  1.000 26.08323  ? 220 ARG   B CB    1 
ATOM   3637 C  CG    . ARG   B 1 223 ? 11.58346 41.08045 23.15830  1.000 31.27145  ? 220 ARG   B CG    1 
ATOM   3638 C  CD    . ARG   B 1 223 ? 11.91308 42.45873 22.60424  1.000 35.50701  ? 220 ARG   B CD    1 
ATOM   3639 N  NE    . ARG   B 1 223 ? 13.27533 42.87320 22.93978  1.000 37.95540  ? 220 ARG   B NE    1 
ATOM   3640 C  CZ    . ARG   B 1 223 ? 13.77735 44.08073 22.69158  1.000 40.32168  ? 220 ARG   B CZ    1 
ATOM   3641 N  NH1   . ARG   B 1 223 ? 13.03027 45.00844 22.10634  1.000 39.80143  ? 220 ARG   B NH1   1 
ATOM   3642 N  NH2   . ARG   B 1 223 ? 15.02825 44.36414 23.03349  1.000 37.49315  ? 220 ARG   B NH2   1 
ATOM   3643 N  N     . VAL   B 1 224 ? 14.25022 37.10321 22.80240  1.000 32.42855  ? 221 VAL   B N     1 
ATOM   3644 C  CA    . VAL   B 1 224 ? 15.04936 36.20090 21.98225  1.000 30.77905  ? 221 VAL   B CA    1 
ATOM   3645 C  C     . VAL   B 1 224 ? 15.66500 35.09594 22.83114  1.000 31.07608  ? 221 VAL   B C     1 
ATOM   3646 O  O     . VAL   B 1 224 ? 15.85901 35.23645 24.04028  1.000 30.09515  ? 221 VAL   B O     1 
ATOM   3647 C  CB    . VAL   B 1 224 ? 16.17831 36.93907 21.21685  1.000 32.61213  ? 221 VAL   B CB    1 
ATOM   3648 C  CG1   . VAL   B 1 224 ? 15.60449 37.85058 20.14233  1.000 30.60529  ? 221 VAL   B CG1   1 
ATOM   3649 C  CG2   . VAL   B 1 224 ? 17.07494 37.71878 22.18514  1.000 29.33566  ? 221 VAL   B CG2   1 
ATOM   3650 N  N     . GLU   B 1 225 ? 15.95651 33.97860 22.16858  1.000 32.47402  ? 222 GLU   B N     1 
ATOM   3651 C  CA    . GLU   B 1 225 ? 16.92979 32.99717 22.62316  1.000 36.90428  ? 222 GLU   B CA    1 
ATOM   3652 C  C     . GLU   B 1 225 ? 18.24666 33.26839 21.90805  1.000 35.06531  ? 222 GLU   B C     1 
ATOM   3653 O  O     . GLU   B 1 225 ? 18.25817 33.75615 20.77471  1.000 32.99180  ? 222 GLU   B O     1 
ATOM   3654 C  CB    . GLU   B 1 225 ? 16.46781 31.56841 22.32636  1.000 40.84641  ? 222 GLU   B CB    1 
ATOM   3655 C  CG    . GLU   B 1 225 ? 15.30696 31.08376 23.16599  1.000 52.26324  ? 222 GLU   B CG    1 
ATOM   3656 C  CD    . GLU   B 1 225 ? 14.56914 29.92071 22.51715  1.000 60.49231  ? 222 GLU   B CD    1 
ATOM   3657 O  OE1   . GLU   B 1 225 ? 14.83449 29.62449 21.33112  1.000 63.31614  ? 222 GLU   B OE1   1 
ATOM   3658 O  OE2   . GLU   B 1 225 ? 13.71574 29.31051 23.19176  1.000 63.06075  ? 222 GLU   B OE2   1 
ATOM   3659 N  N     . ILE   B 1 226 ? 19.36351 32.95099 22.56961  1.000 34.38572  ? 223 ILE   B N     1 
ATOM   3660 C  CA    . ILE   B 1 226 ? 20.66952 33.29195 22.02121  1.000 34.78178  ? 223 ILE   B CA    1 
ATOM   3661 C  C     . ILE   B 1 226 ? 21.62027 32.10421 22.08249  1.000 34.79970  ? 223 ILE   B C     1 
ATOM   3662 O  O     . ILE   B 1 226 ? 21.44492 31.16165 22.85859  1.000 34.11833  ? 223 ILE   B O     1 
ATOM   3663 C  CB    . ILE   B 1 226 ? 21.31631 34.50635 22.72782  1.000 32.22667  ? 223 ILE   B CB    1 
ATOM   3664 C  CG1   . ILE   B 1 226 ? 21.78340 34.13287 24.13527  1.000 32.38461  ? 223 ILE   B CG1   1 
ATOM   3665 C  CG2   . ILE   B 1 226 ? 20.36079 35.69200 22.76475  1.000 28.52743  ? 223 ILE   B CG2   1 
ATOM   3666 C  CD1   . ILE   B 1 226 ? 22.75719 35.13972 24.72953  1.000 31.67830  ? 223 ILE   B CD1   1 
ATOM   3667 N  N     . SER   B 1 227 ? 22.64154 32.17146 21.23070  1.000 32.10664  ? 224 SER   B N     1 
ATOM   3668 C  CA    . SER   B 1 227 ? 23.79119 31.27882 21.29788  1.000 34.08216  ? 224 SER   B CA    1 
ATOM   3669 C  C     . SER   B 1 227 ? 24.99964 32.04203 20.78043  1.000 31.68881  ? 224 SER   B C     1 
ATOM   3670 O  O     . SER   B 1 227 ? 25.04740 32.39292 19.59684  1.000 29.95903  ? 224 SER   B O     1 
ATOM   3671 C  CB    . SER   B 1 227 ? 23.56796 30.00815 20.47601  1.000 33.41885  ? 224 SER   B CB    1 
ATOM   3672 O  OG    . SER   B 1 227 ? 24.77775 29.26759 20.37528  1.000 32.13665  ? 224 SER   B OG    1 
ATOM   3673 N  N     . GLN   B 1 228 ? 25.96596 32.30791 21.65323  1.000 24.63020  ? 225 GLN   B N     1 
ATOM   3674 C  CA    . GLN   B 1 228 ? 27.21244 32.93543 21.23351  1.000 27.51940  ? 225 GLN   B CA    1 
ATOM   3675 C  C     . GLN   B 1 228 ? 28.17414 31.83404 20.80685  1.000 28.29110  ? 225 GLN   B C     1 
ATOM   3676 O  O     . GLN   B 1 228 ? 28.48355 30.93599 21.59685  1.000 28.57739  ? 225 GLN   B O     1 
ATOM   3677 C  CB    . GLN   B 1 228 ? 27.80735 33.79133 22.35149  1.000 29.06184  ? 225 GLN   B CB    1 
ATOM   3678 C  CG    . GLN   B 1 228 ? 29.04943 34.56803 21.93143  1.000 31.01420  ? 225 GLN   B CG    1 
ATOM   3679 C  CD    . GLN   B 1 228 ? 29.35182 35.72968 22.85303  1.000 34.49969  ? 225 GLN   B CD    1 
ATOM   3680 O  OE1   . GLN   B 1 228 ? 29.29665 35.59963 24.07806  1.000 37.81442  ? 225 GLN   B OE1   1 
ATOM   3681 N  NE2   . GLN   B 1 228 ? 29.65948 36.88183 22.26746  1.000 32.95747  ? 225 GLN   B NE2   1 
ATOM   3682 N  N     . VAL   B 1 229 ? 28.62145 31.88489 19.55533  1.000 28.31915  ? 226 VAL   B N     1 
ATOM   3683 C  CA    . VAL   B 1 229 ? 29.40413 30.81147 18.95362  1.000 27.47061  ? 226 VAL   B CA    1 
ATOM   3684 C  C     . VAL   B 1 229 ? 30.81085 31.33598 18.69900  1.000 31.53138  ? 226 VAL   B C     1 
ATOM   3685 O  O     . VAL   B 1 229 ? 30.98754 32.33953 17.99731  1.000 31.03114  ? 226 VAL   B O     1 
ATOM   3686 C  CB    . VAL   B 1 229 ? 28.75316 30.30069 17.65874  1.000 27.50818  ? 226 VAL   B CB    1 
ATOM   3687 C  CG1   . VAL   B 1 229 ? 29.50142 29.09422 17.12876  1.000 29.12962  ? 226 VAL   B CG1   1 
ATOM   3688 C  CG2   . VAL   B 1 229 ? 27.28787 29.95187 17.90363  1.000 28.52170  ? 226 VAL   B CG2   1 
ATOM   3689 N  N     . SER   B 1 230 ? 31.81282 30.65029 19.25525  1.000 29.94293  ? 227 SER   B N     1 
ATOM   3690 C  CA    . SER   B 1 230 ? 33.20780 31.08403 19.14965  1.000 30.11943  ? 227 SER   B CA    1 
ATOM   3691 C  C     . SER   B 1 230 ? 33.80540 30.70189 17.79131  1.000 31.60563  ? 227 SER   B C     1 
ATOM   3692 O  O     . SER   B 1 230 ? 34.82861 30.02562 17.68504  1.000 33.02608  ? 227 SER   B O     1 
ATOM   3693 C  CB    . SER   B 1 230 ? 34.01691 30.49945 20.29879  1.000 26.68831  ? 227 SER   B CB    1 
ATOM   3694 O  OG    . SER   B 1 230 ? 34.03533 29.08420 20.22072  1.000 29.79062  ? 227 SER   B OG    1 
ATOM   3695 N  N     . ILE   B 1 231 ? 33.13685 31.15755 16.73621  1.000 32.33730  ? 228 ILE   B N     1 
ATOM   3696 C  CA    . ILE   B 1 231 ? 33.58467 30.96819 15.36263  1.000 31.44812  ? 228 ILE   B CA    1 
ATOM   3697 C  C     . ILE   B 1 231 ? 33.90422 32.33464 14.77283  1.000 34.24472  ? 228 ILE   B C     1 
ATOM   3698 O  O     . ILE   B 1 231 ? 33.22451 33.32552 15.07337  1.000 35.78653  ? 228 ILE   B O     1 
ATOM   3699 C  CB    . ILE   B 1 231 ? 32.52610 30.22660 14.52028  1.000 30.28980  ? 228 ILE   B CB    1 
ATOM   3700 C  CG1   . ILE   B 1 231 ? 33.08551 29.86697 13.13857  1.000 30.81287  ? 228 ILE   B CG1   1 
ATOM   3701 C  CG2   . ILE   B 1 231 ? 31.23565 31.05296 14.39816  1.000 27.84262  ? 228 ILE   B CG2   1 
ATOM   3702 C  CD1   . ILE   B 1 231 ? 32.15840 28.98283 12.32049  1.000 31.69928  ? 228 ILE   B CD1   1 
ATOM   3703 N  N     . GLY   B 1 232 ? 34.94927 32.38919 13.95194  1.000 34.00616  ? 229 GLY   B N     1 
ATOM   3704 C  CA    . GLY   B 1 232 ? 35.37675 33.66373 13.39612  1.000 35.71872  ? 229 GLY   B CA    1 
ATOM   3705 C  C     . GLY   B 1 232 ? 35.87123 34.58581 14.49564  1.000 35.22233  ? 229 GLY   B C     1 
ATOM   3706 O  O     . GLY   B 1 232 ? 36.85423 34.29865 15.18939  1.000 34.77037  ? 229 GLY   B O     1 
ATOM   3707 N  N     . ASP   B 1 233 ? 35.18988 35.71841 14.65722  1.000 36.81388  ? 230 ASP   B N     1 
ATOM   3708 C  CA    . ASP   B 1 233 ? 35.42176 36.63391 15.76653  1.000 38.24689  ? 230 ASP   B CA    1 
ATOM   3709 C  C     . ASP   B 1 233 ? 34.27624 36.58889 16.77199  1.000 38.01766  ? 230 ASP   B C     1 
ATOM   3710 O  O     . ASP   B 1 233 ? 34.05317 37.55689 17.50726  1.000 37.86862  ? 230 ASP   B O     1 
ATOM   3711 C  CB    . ASP   B 1 233 ? 35.62027 38.05723 15.24183  1.000 42.10810  ? 230 ASP   B CB    1 
ATOM   3712 C  CG    . ASP   B 1 233 ? 36.29017 38.97171 16.25654  1.000 48.81703  ? 230 ASP   B CG    1 
ATOM   3713 O  OD1   . ASP   B 1 233 ? 37.07568 38.46522 17.08740  1.000 48.76549  ? 230 ASP   B OD1   1 
ATOM   3714 O  OD2   . ASP   B 1 233 ? 36.02038 40.19515 16.22869  1.000 46.53155  ? 230 ASP   B OD2   1 
ATOM   3715 N  N     . GLY   B 1 234 ? 33.53827 35.48249 16.80666  1.000 35.53003  ? 231 GLY   B N     1 
ATOM   3716 C  CA    . GLY   B 1 234 ? 32.36168 35.37632 17.64235  1.000 32.45695  ? 231 GLY   B CA    1 
ATOM   3717 C  C     . GLY   B 1 234 ? 31.11157 35.80276 16.90340  1.000 32.12911  ? 231 GLY   B C     1 
ATOM   3718 O  O     . GLY   B 1 234 ? 31.03260 36.92791 16.40110  1.000 31.99931  ? 231 GLY   B O     1 
ATOM   3719 N  N     . VAL   B 1 235 ? 30.13812 34.90289 16.80739  1.000 30.63069  ? 232 VAL   B N     1 
ATOM   3720 C  CA    . VAL   B 1 235 ? 28.83748 35.19683 16.22178  1.000 32.31730  ? 232 VAL   B CA    1 
ATOM   3721 C  C     . VAL   B 1 235 ? 27.77488 34.85478 17.25269  1.000 31.56545  ? 232 VAL   B C     1 
ATOM   3722 O  O     . VAL   B 1 235 ? 27.73843 33.72829 17.76246  1.000 28.77169  ? 232 VAL   B O     1 
ATOM   3723 C  CB    . VAL   B 1 235 ? 28.59940 34.41312 14.91722  1.000 35.22244  ? 232 VAL   B CB    1 
ATOM   3724 C  CG1   . VAL   B 1 235 ? 27.17482 34.63899 14.41829  1.000 33.38326  ? 232 VAL   B CG1   1 
ATOM   3725 C  CG2   . VAL   B 1 235 ? 29.61589 34.81354 13.85712  1.000 36.32984  ? 232 VAL   B CG2   1 
ATOM   3726 N  N     . THR   B 1 236 ? 26.91908 35.82249 17.56409  1.000 30.49798  ? 233 THR   B N     1 
ATOM   3727 C  CA    . THR   B 1 236 ? 25.79803 35.60575 18.46819  1.000 29.75624  ? 233 THR   B CA    1 
ATOM   3728 C  C     . THR   B 1 236 ? 24.54595 35.39876 17.62657  1.000 29.91770  ? 233 THR   B C     1 
ATOM   3729 O  O     . THR   B 1 236 ? 24.08835 36.32082 16.94316  1.000 28.86780  ? 233 THR   B O     1 
ATOM   3730 C  CB    . THR   B 1 236 ? 25.62329 36.77535 19.43341  1.000 32.74744  ? 233 THR   B CB    1 
ATOM   3731 O  OG1   . THR   B 1 236 ? 26.80585 36.92132 20.22744  1.000 34.42867  ? 233 THR   B OG1   1 
ATOM   3732 C  CG2   . THR   B 1 236 ? 24.43231 36.52689 20.35098  1.000 34.90707  ? 233 THR   B CG2   1 
ATOM   3733 N  N     . ILE   B 1 237 ? 24.00716 34.18609 17.66860  1.000 30.74018  ? 234 ILE   B N     1 
ATOM   3734 C  CA    . ILE   B 1 237 ? 22.75908 33.85798 16.99527  1.000 31.23649  ? 234 ILE   B CA    1 
ATOM   3735 C  C     . ILE   B 1 237 ? 21.61056 34.16790 17.94162  1.000 32.34973  ? 234 ILE   B C     1 
ATOM   3736 O  O     . ILE   B 1 237 ? 21.59874 33.70590 19.08859  1.000 32.28211  ? 234 ILE   B O     1 
ATOM   3737 C  CB    . ILE   B 1 237 ? 22.73316 32.38032 16.57228  1.000 32.64045  ? 234 ILE   B CB    1 
ATOM   3738 C  CG1   . ILE   B 1 237 ? 23.97591 32.03120 15.75441  1.000 30.80123  ? 234 ILE   B CG1   1 
ATOM   3739 C  CG2   . ILE   B 1 237 ? 21.47116 32.07495 15.78618  1.000 32.34628  ? 234 ILE   B CG2   1 
ATOM   3740 C  CD1   . ILE   B 1 237 ? 24.17183 30.53855 15.57546  1.000 31.45216  ? 234 ILE   B CD1   1 
ATOM   3741 N  N     . CYS   B 1 238 ? 20.65038 34.95552 17.46851  1.000 28.42361  ? 235 CYS   B N     1 
ATOM   3742 C  CA    . CYS   B 1 238 ? 19.43810 35.25541 18.21284  1.000 33.06913  ? 235 CYS   B CA    1 
ATOM   3743 C  C     . CYS   B 1 238 ? 18.24125 34.67100 17.47922  1.000 36.26452  ? 235 CYS   B C     1 
ATOM   3744 O  O     . CYS   B 1 238 ? 18.18382 34.70261 16.24724  1.000 39.31793  ? 235 CYS   B O     1 
ATOM   3745 C  CB    . CYS   B 1 238 ? 19.25380 36.76396 18.38739  1.000 35.65590  ? 235 CYS   B CB    1 
ATOM   3746 S  SG    . CYS   B 1 238 ? 20.58270 37.56678 19.29200  1.000 34.97883  ? 235 CYS   B SG    1 
ATOM   3747 N  N     . ARG   B 1 239 ? 17.28647 34.13835 18.23574  1.000 33.45720  ? 236 ARG   B N     1 
ATOM   3748 C  CA    . ARG   B 1 239 ? 16.04695 33.61177 17.67712  1.000 33.74241  ? 236 ARG   B CA    1 
ATOM   3749 C  C     . ARG   B 1 239 ? 14.88057 34.33142 18.33726  1.000 33.84819  ? 236 ARG   B C     1 
ATOM   3750 O  O     . ARG   B 1 239 ? 14.75354 34.31042 19.56499  1.000 33.00163  ? 236 ARG   B O     1 
ATOM   3751 C  CB    . ARG   B 1 239 ? 15.94321 32.10039 17.88797  1.000 34.19553  ? 236 ARG   B CB    1 
ATOM   3752 C  CG    . ARG   B 1 239 ? 14.67097 31.49025 17.33059  1.000 37.74682  ? 236 ARG   B CG    1 
ATOM   3753 C  CD    . ARG   B 1 239 ? 14.61169 29.99396 17.58690  1.000 41.05856  ? 236 ARG   B CD    1 
ATOM   3754 N  NE    . ARG   B 1 239 ? 13.36669 29.42588 17.08067  1.000 50.55696  ? 236 ARG   B NE    1 
ATOM   3755 C  CZ    . ARG   B 1 239 ? 12.24960 29.31470 17.79203  1.000 50.30718  ? 236 ARG   B CZ    1 
ATOM   3756 N  NH1   . ARG   B 1 239 ? 12.21976 29.72409 19.05402  1.000 51.09339  ? 236 ARG   B NH1   1 
ATOM   3757 N  NH2   . ARG   B 1 239 ? 11.16363 28.78881 17.24038  1.000 49.25530  ? 236 ARG   B NH2   1 
ATOM   3758 N  N     . ARG   B 1 240 ? 14.03399 34.96594 17.52821  1.000 33.12721  ? 237 ARG   B N     1 
ATOM   3759 C  CA    . ARG   B 1 240 ? 12.95022 35.77299 18.07488  1.000 34.24848  ? 237 ARG   B CA    1 
ATOM   3760 C  C     . ARG   B 1 240 ? 11.85506 34.88581 18.65604  1.000 34.37265  ? 237 ARG   B C     1 
ATOM   3761 O  O     . ARG   B 1 240 ? 11.34566 33.98341 17.98278  1.000 32.75591  ? 237 ARG   B O     1 
ATOM   3762 C  CB    . ARG   B 1 240 ? 12.36451 36.68718 17.00004  1.000 37.45143  ? 237 ARG   B CB    1 
ATOM   3763 C  CG    . ARG   B 1 240 ? 11.14245 37.45052 17.48251  1.000 37.94410  ? 237 ARG   B CG    1 
ATOM   3764 C  CD    . ARG   B 1 240 ? 10.54149 38.32551 16.40149  1.000 35.91445  ? 237 ARG   B CD    1 
ATOM   3765 N  NE    . ARG   B 1 240 ? 9.32211  38.97117 16.87507  1.000 35.94588  ? 237 ARG   B NE    1 
ATOM   3766 C  CZ    . ARG   B 1 240 ? 8.54891  39.75102 16.12822  1.000 38.57864  ? 237 ARG   B CZ    1 
ATOM   3767 N  NH1   . ARG   B 1 240 ? 8.86714  39.98347 14.86030  1.000 36.42287  ? 237 ARG   B NH1   1 
ATOM   3768 N  NH2   . ARG   B 1 240 ? 7.45657  40.29723 16.64992  1.000 37.37360  ? 237 ARG   B NH2   1 
ATOM   3769 N  N     . LEU   B 1 241 ? 11.48083 35.15887 19.90670  1.000 35.12109  ? 238 LEU   B N     1 
ATOM   3770 C  CA    . LEU   B 1 241 ? 10.45904 34.37600 20.59279  1.000 40.53270  ? 238 LEU   B CA    1 
ATOM   3771 C  C     . LEU   B 1 241 ? 9.06016  34.95992 20.44605  1.000 44.86677  ? 238 LEU   B C     1 
ATOM   3772 O  O     . LEU   B 1 241 ? 8.08522  34.20178 20.40099  1.000 43.55321  ? 238 LEU   B O     1 
ATOM   3773 C  CB    . LEU   B 1 241 ? 10.80251 34.25398 22.08003  1.000 39.29304  ? 238 LEU   B CB    1 
ATOM   3774 C  CG    . LEU   B 1 241 ? 12.17882 33.65588 22.36748  1.000 39.54625  ? 238 LEU   B CG    1 
ATOM   3775 C  CD1   . LEU   B 1 241 ? 12.43178 33.54465 23.86738  1.000 36.98343  ? 238 LEU   B CD1   1 
ATOM   3776 C  CD2   . LEU   B 1 241 ? 12.27957 32.30504 21.68918  1.000 42.53298  ? 238 LEU   B CD2   1 
ATOM   3777 N  N     . TYR   B 1 242 ? 8.93510  36.28264 20.39426  1.000 46.03155  ? 239 TYR   B N     1 
ATOM   3778 C  CA    . TYR   B 1 242 ? 7.64273  36.92688 20.17595  1.000 48.85171  ? 239 TYR   B CA    1 
ATOM   3779 C  C     . TYR   B 1 242 ? 7.83964  38.33499 19.62048  1.000 51.14667  ? 239 TYR   B C     1 
ATOM   3780 O  O     . TYR   B 1 242 ? 6.89325  38.99455 19.19155  1.000 50.40822  ? 239 TYR   B O     1 
ATOM   3781 C  CB    . TYR   B 1 242 ? 6.82362  36.97506 21.47223  1.000 44.01315  ? 239 TYR   B CB    1 
ATOM   3782 C  CG    . TYR   B 1 242 ? 7.49144  37.71725 22.61322  1.000 39.99963  ? 239 TYR   B CG    1 
ATOM   3783 C  CD1   . TYR   B 1 242 ? 7.32109  39.08646 22.77193  1.000 42.47066  ? 239 TYR   B CD1   1 
ATOM   3784 C  CD2   . TYR   B 1 242 ? 8.28483  37.04548 23.53711  1.000 38.38102  ? 239 TYR   B CD2   1 
ATOM   3785 C  CE1   . TYR   B 1 242 ? 7.92797  39.76886 23.81406  1.000 43.67438  ? 239 TYR   B CE1   1 
ATOM   3786 C  CE2   . TYR   B 1 242 ? 8.89604  37.72009 24.58566  1.000 34.98809  ? 239 TYR   B CE2   1 
ATOM   3787 C  CZ    . TYR   B 1 242 ? 8.71146  39.08020 24.71737  1.000 40.42309  ? 239 TYR   B CZ    1 
ATOM   3788 O  OH    . TYR   B 1 242 ? 9.31071  39.76367 25.75131  1.000 44.45756  ? 239 TYR   B OH    1 
ATOM   3789 O  OXT   . TYR   B 1 242 ? 8.95985  38.84498 19.59199  1.000 51.94550  ? 239 TYR   B OXT   1 
HETATM 3790 C  C1    . GOL   C 2 .   ? 33.81040 5.61109  28.98390  1.000 68.88235  ? 501 GOL   A C1    1 
HETATM 3791 O  O1    . GOL   C 2 .   ? 32.81521 4.63334  29.05192  1.000 69.71599  ? 501 GOL   A O1    1 
HETATM 3792 C  C2    . GOL   C 2 .   ? 33.10679 6.96708  28.71038  1.000 66.71738  ? 501 GOL   A C2    1 
HETATM 3793 O  O2    . GOL   C 2 .   ? 33.35842 7.89199  29.69886  1.000 67.10877  ? 501 GOL   A O2    1 
HETATM 3794 C  C3    . GOL   C 2 .   ? 33.64283 7.42589  27.34949  1.000 65.60713  ? 501 GOL   A C3    1 
HETATM 3795 O  O3    . GOL   C 2 .   ? 33.51596 8.80581  27.33376  1.000 65.34207  ? 501 GOL   A O3    1 
HETATM 3796 MG MG    . MG    D 3 .   ? 32.03516 14.96540 22.90129  1.000 34.17231  ? 502 MG    A MG    1 
HETATM 3797 N  N     . SAH   E 4 .   ? 27.00275 13.49658 24.53379  1.000 32.03150  ? 503 SAH   A N     1 
HETATM 3798 C  CA    . SAH   E 4 .   ? 27.30725 13.36317 25.95470  1.000 35.96283  ? 503 SAH   A CA    1 
HETATM 3799 C  CB    . SAH   E 4 .   ? 28.74054 12.87410 26.16934  1.000 34.04803  ? 503 SAH   A CB    1 
HETATM 3800 C  CG    . SAH   E 4 .   ? 29.15512 11.60652 25.42397  1.000 38.63641  ? 503 SAH   A CG    1 
HETATM 3801 S  SD    . SAH   E 4 .   ? 30.55559 10.80534 26.25318  1.000 42.52641  ? 503 SAH   A SD    1 
HETATM 3802 C  C     . SAH   E 4 .   ? 27.09722 14.68069 26.69691  1.000 38.42232  ? 503 SAH   A C     1 
HETATM 3803 O  O     . SAH   E 4 .   ? 26.23262 15.48466 26.34371  1.000 37.92434  ? 503 SAH   A O     1 
HETATM 3804 O  OXT   . SAH   E 4 .   ? 27.78565 14.97249 27.67681  1.000 39.47350  ? 503 SAH   A OXT   1 
HETATM 3805 C  "C5'" . SAH   E 4 .   ? 30.54806 9.36596  25.14825  1.000 43.24213  ? 503 SAH   A "C5'" 1 
HETATM 3806 C  "C4'" . SAH   E 4 .   ? 29.54224 8.27309  25.50535  1.000 43.99256  ? 503 SAH   A "C4'" 1 
HETATM 3807 O  "O4'" . SAH   E 4 .   ? 29.48305 7.31964  24.46231  1.000 43.56304  ? 503 SAH   A "O4'" 1 
HETATM 3808 C  "C3'" . SAH   E 4 .   ? 29.90938 7.50769  26.76841  1.000 44.63499  ? 503 SAH   A "C3'" 1 
HETATM 3809 O  "O3'" . SAH   E 4 .   ? 28.84801 7.61883  27.68867  1.000 43.21691  ? 503 SAH   A "O3'" 1 
HETATM 3810 C  "C2'" . SAH   E 4 .   ? 30.04729 6.05846  26.34688  1.000 42.52691  ? 503 SAH   A "C2'" 1 
HETATM 3811 O  "O2'" . SAH   E 4 .   ? 29.41506 5.20859  27.27249  1.000 44.17881  ? 503 SAH   A "O2'" 1 
HETATM 3812 C  "C1'" . SAH   E 4 .   ? 29.31836 6.02823  25.01625  1.000 43.46900  ? 503 SAH   A "C1'" 1 
HETATM 3813 N  N9    . SAH   E 4 .   ? 29.79835 4.97670  24.09838  1.000 45.63159  ? 503 SAH   A N9    1 
HETATM 3814 C  C8    . SAH   E 4 .   ? 31.07636 4.50485  23.94368  1.000 42.40300  ? 503 SAH   A C8    1 
HETATM 3815 N  N7    . SAH   E 4 .   ? 31.05827 3.54210  22.99047  1.000 42.46807  ? 503 SAH   A N7    1 
HETATM 3816 C  C5    . SAH   E 4 .   ? 29.79273 3.39271  22.53551  1.000 44.60107  ? 503 SAH   A C5    1 
HETATM 3817 C  C6    . SAH   E 4 .   ? 29.21565 2.55942  21.58015  1.000 44.64458  ? 503 SAH   A C6    1 
HETATM 3818 N  N6    . SAH   E 4 .   ? 29.95104 1.68558  20.89827  1.000 43.52374  ? 503 SAH   A N6    1 
HETATM 3819 N  N1    . SAH   E 4 .   ? 27.86155 2.64455  21.33517  1.000 42.03276  ? 503 SAH   A N1    1 
HETATM 3820 C  C2    . SAH   E 4 .   ? 27.08431 3.54564  22.03306  1.000 39.96841  ? 503 SAH   A C2    1 
HETATM 3821 N  N3    . SAH   E 4 .   ? 27.66064 4.36323  22.98152  1.000 41.09448  ? 503 SAH   A N3    1 
HETATM 3822 C  C4    . SAH   E 4 .   ? 28.99155 4.28901  23.22784  1.000 44.67111  ? 503 SAH   A C4    1 
HETATM 3823 C  C1    . GOL   F 2 .   ? 17.13198 34.79667 30.22390  1.000 73.09443  ? 504 GOL   A C1    1 
HETATM 3824 O  O1    . GOL   F 2 .   ? 17.95819 34.86250 31.33122  1.000 76.15540  ? 504 GOL   A O1    1 
HETATM 3825 C  C2    . GOL   F 2 .   ? 15.96824 35.76239 30.49156  1.000 71.12394  ? 504 GOL   A C2    1 
HETATM 3826 O  O2    . GOL   F 2 .   ? 15.73766 36.59829 29.41721  1.000 70.20307  ? 504 GOL   A O2    1 
HETATM 3827 C  C3    . GOL   F 2 .   ? 14.76907 34.84781 30.78399  1.000 73.40369  ? 504 GOL   A C3    1 
HETATM 3828 O  O3    . GOL   F 2 .   ? 14.28563 34.41975 29.55709  1.000 74.56752  ? 504 GOL   A O3    1 
HETATM 3829 C  C13   . A1LU2 G 5 .   ? 35.26807 44.74615 11.19847  1.000 70.83499  ? 701 A1LU2 B C13   1 
HETATM 3830 C  C02   . A1LU2 G 5 .   ? 36.45960 50.62539 13.43382  1.000 98.67134  ? 701 A1LU2 B C02   1 
HETATM 3831 C  C03   . A1LU2 G 5 .   ? 37.64989 50.74476 12.73150  1.000 98.55004  ? 701 A1LU2 B C03   1 
HETATM 3832 C  C04   . A1LU2 G 5 .   ? 38.62839 49.76742 12.84045  1.000 98.13252  ? 701 A1LU2 B C04   1 
HETATM 3833 C  C05   . A1LU2 G 5 .   ? 36.25016 49.52350 14.24983  1.000 97.34208  ? 701 A1LU2 B C05   1 
HETATM 3834 C  C06   . A1LU2 G 5 .   ? 37.22931 48.54833 14.36103  1.000 97.30064  ? 701 A1LU2 B C06   1 
HETATM 3835 C  C07   . A1LU2 G 5 .   ? 38.41936 48.67204 13.66184  1.000 96.88726  ? 701 A1LU2 B C07   1 
HETATM 3836 C  C08   . A1LU2 G 5 .   ? 39.48691 47.58691 13.78419  1.000 93.55795  ? 701 A1LU2 B C08   1 
HETATM 3837 C  C09   . A1LU2 G 5 .   ? 38.87738 46.21212 13.53397  1.000 91.16401  ? 701 A1LU2 B C09   1 
HETATM 3838 C  C11   . A1LU2 G 5 .   ? 37.27809 46.12550 11.80159  1.000 82.79281  ? 701 A1LU2 B C11   1 
HETATM 3839 C  C12   . A1LU2 G 5 .   ? 36.57840 44.78028 11.64206  1.000 76.44218  ? 701 A1LU2 B C12   1 
HETATM 3840 C  C14   . A1LU2 G 5 .   ? 34.62016 43.53212 11.04588  1.000 67.99769  ? 701 A1LU2 B C14   1 
HETATM 3841 C  C16   . A1LU2 G 5 .   ? 35.28798 42.35515 11.34209  1.000 66.32310  ? 701 A1LU2 B C16   1 
HETATM 3842 C  C18   . A1LU2 G 5 .   ? 36.59794 42.38817 11.79080  1.000 70.11908  ? 701 A1LU2 B C18   1 
HETATM 3843 C  C19   . A1LU2 G 5 .   ? 37.24539 43.60224 11.94045  1.000 74.67922  ? 701 A1LU2 B C19   1 
HETATM 3844 N  N10   . A1LU2 G 5 .   ? 38.68632 45.96326 12.11592  1.000 87.83695  ? 701 A1LU2 B N10   1 
HETATM 3845 O  O01   . A1LU2 G 5 .   ? 35.47003 51.61417 13.32017  1.000 100.12426 ? 701 A1LU2 B O01   1 
HETATM 3846 O  O15   . A1LU2 G 5 .   ? 33.29293 43.49098 10.59445  1.000 65.51185  ? 701 A1LU2 B O15   1 
HETATM 3847 O  O17   . A1LU2 G 5 .   ? 34.63726 41.12296 11.19342  1.000 55.70444  ? 701 A1LU2 B O17   1 
HETATM 3848 MG MG    . MG    H 3 .   ? 32.57781 41.30324 10.99303  1.000 34.83537  ? 702 MG    B MG    1 
HETATM 3849 N  N     . SAH   I 4 .   ? 30.04832 41.45686 6.17124   1.000 39.92676  ? 703 SAH   B N     1 
HETATM 3850 C  CA    . SAH   I 4 .   ? 31.22574 41.83057 5.39635   1.000 38.36776  ? 703 SAH   B CA    1 
HETATM 3851 C  CB    . SAH   I 4 .   ? 32.17470 42.67939 6.24064   1.000 37.24539  ? 703 SAH   B CB    1 
HETATM 3852 C  CG    . SAH   I 4 .   ? 31.56847 43.95182 6.83538   1.000 37.28474  ? 703 SAH   B CG    1 
HETATM 3853 S  SD    . SAH   I 4 .   ? 32.85300 45.19365 7.15024   1.000 40.29174  ? 703 SAH   B SD    1 
HETATM 3854 C  C     . SAH   I 4 .   ? 31.95496 40.60459 4.85038   1.000 38.72778  ? 703 SAH   B C     1 
HETATM 3855 O  O     . SAH   I 4 .   ? 31.32933 39.60248 4.50913   1.000 39.26554  ? 703 SAH   B O     1 
HETATM 3856 O  OXT   . SAH   I 4 .   ? 33.18183 40.58330 4.72257   1.000 37.50390  ? 703 SAH   B OXT   1 
HETATM 3857 C  "C5'" . SAH   I 4 .   ? 31.65196 46.37515 7.81603   1.000 38.49075  ? 703 SAH   B "C5'" 1 
HETATM 3858 C  "C4'" . SAH   I 4 .   ? 30.91439 47.17892 6.75152   1.000 39.87400  ? 703 SAH   B "C4'" 1 
HETATM 3859 O  "O4'" . SAH   I 4 .   ? 29.88882 47.95153 7.34151   1.000 39.55397  ? 703 SAH   B "O4'" 1 
HETATM 3860 C  "C3'" . SAH   I 4 .   ? 31.82967 48.14982 6.02603   1.000 41.61763  ? 703 SAH   B "C3'" 1 
HETATM 3861 O  "O3'" . SAH   I 4 .   ? 31.80070 47.84472 4.65317   1.000 40.45125  ? 703 SAH   B "O3'" 1 
HETATM 3862 C  "C2'" . SAH   I 4 .   ? 31.22016 49.51883 6.23305   1.000 43.11385  ? 703 SAH   B "C2'" 1 
HETATM 3863 O  "O2'" . SAH   I 4 .   ? 31.21108 50.24043 5.02466   1.000 45.03078  ? 703 SAH   B "O2'" 1 
HETATM 3864 C  "C1'" . SAH   I 4 .   ? 29.80304 49.19459 6.67365   1.000 42.18145  ? 703 SAH   B "C1'" 1 
HETATM 3865 N  N9    . SAH   I 4 .   ? 29.20962 50.22896 7.54028   1.000 41.74402  ? 703 SAH   B N9    1 
HETATM 3866 C  C8    . SAH   I 4 .   ? 29.83510 51.00162 8.48539   1.000 39.15685  ? 703 SAH   B C8    1 
HETATM 3867 N  N7    . SAH   I 4 .   ? 28.90965 51.81622 9.04991   1.000 40.26235  ? 703 SAH   B N7    1 
HETATM 3868 C  C5    . SAH   I 4 .   ? 27.70591 51.57003 8.48047   1.000 42.16043  ? 703 SAH   B C5    1 
HETATM 3869 C  C6    . SAH   I 4 .   ? 26.43983 52.10937 8.67721   1.000 44.16201  ? 703 SAH   B C6    1 
HETATM 3870 N  N6    . SAH   I 4 .   ? 26.24089 53.06478 9.58195   1.000 45.88202  ? 703 SAH   B N6    1 
HETATM 3871 N  N1    . SAH   I 4 .   ? 25.38203 51.64490 7.92713   1.000 44.09870  ? 703 SAH   B N1    1 
HETATM 3872 C  C2    . SAH   I 4 .   ? 25.57900 50.64971 6.99095   1.000 44.09000  ? 703 SAH   B C2    1 
HETATM 3873 N  N3    . SAH   I 4 .   ? 26.83881 50.12128 6.79800   1.000 40.61805  ? 703 SAH   B N3    1 
HETATM 3874 C  C4    . SAH   I 4 .   ? 27.88291 50.57397 7.53036   1.000 41.28289  ? 703 SAH   B C4    1 
HETATM 3875 O  O     . HOH   J 6 .   ? 17.77565 21.53676 5.26172   1.000 54.13034  ? 601 HOH   A O     1 
HETATM 3876 O  O     . HOH   J 6 .   ? 13.11828 5.21091  19.33360  1.000 47.63008  ? 602 HOH   A O     1 
HETATM 3877 O  O     . HOH   J 6 .   ? 31.01336 15.50584 24.60779  1.000 34.21774  ? 603 HOH   A O     1 
HETATM 3878 O  O     . HOH   J 6 .   ? 37.65846 23.51765 27.01706  1.000 50.02577  ? 604 HOH   A O     1 
HETATM 3879 O  O     . HOH   J 6 .   ? 19.48882 14.16267 19.31498  1.000 51.99245  ? 605 HOH   A O     1 
HETATM 3880 O  O     . HOH   J 6 .   ? 46.83195 11.91465 9.59784   1.000 57.73277  ? 606 HOH   A O     1 
HETATM 3881 O  O     . HOH   J 6 .   ? 51.34187 10.73324 20.46165  1.000 56.12342  ? 607 HOH   A O     1 
HETATM 3882 O  O     . HOH   J 6 .   ? 34.72697 17.18757 10.18241  1.000 38.65016  ? 608 HOH   A O     1 
HETATM 3883 O  O     . HOH   J 6 .   ? 33.64098 15.50383 24.24466  1.000 53.69441  ? 609 HOH   A O     1 
HETATM 3884 O  O     . HOH   J 6 .   ? 26.32004 14.15537 29.68031  1.000 31.19167  ? 610 HOH   A O     1 
HETATM 3885 O  O     . HOH   J 6 .   ? 36.49797 9.92982  14.53531  1.000 49.59120  ? 611 HOH   A O     1 
HETATM 3886 O  O     . HOH   J 6 .   ? 25.35931 38.03817 31.04007  1.000 30.33431  ? 612 HOH   A O     1 
HETATM 3887 O  O     . HOH   J 6 .   ? 27.84804 21.07586 30.52897  1.000 42.54540  ? 613 HOH   A O     1 
HETATM 3888 O  O     . HOH   J 6 .   ? 35.85319 25.71053 23.41804  1.000 33.33904  ? 614 HOH   A O     1 
HETATM 3889 O  O     . HOH   J 6 .   ? 13.03945 28.52865 11.55966  1.000 49.49779  ? 615 HOH   A O     1 
HETATM 3890 O  O     . HOH   J 6 .   ? 30.02063 41.66217 28.91948  1.000 30.36521  ? 616 HOH   A O     1 
HETATM 3891 O  O     . HOH   J 6 .   ? 22.05243 17.26021 20.56302  1.000 42.48668  ? 617 HOH   A O     1 
HETATM 3892 O  O     . HOH   J 6 .   ? 23.67982 24.77889 27.84494  1.000 45.53403  ? 618 HOH   A O     1 
HETATM 3893 O  O     . HOH   J 6 .   ? 33.73856 23.91717 7.44396   1.000 36.19465  ? 619 HOH   A O     1 
HETATM 3894 O  O     . HOH   J 6 .   ? 35.71856 6.88965  12.38432  1.000 59.13317  ? 620 HOH   A O     1 
HETATM 3895 O  O     . HOH   J 6 .   ? 20.21145 28.61747 22.09975  1.000 35.79577  ? 621 HOH   A O     1 
HETATM 3896 O  O     . HOH   J 6 .   ? 33.01703 13.07226 23.86805  1.000 54.31188  ? 622 HOH   A O     1 
HETATM 3897 O  O     . HOH   J 6 .   ? 34.85783 4.10502  12.05242  1.000 49.74634  ? 623 HOH   A O     1 
HETATM 3898 O  O     . HOH   J 6 .   ? 35.12831 26.88573 12.60424  1.000 28.98200  ? 624 HOH   A O     1 
HETATM 3899 O  O     . HOH   J 6 .   ? 33.79431 27.15563 22.64060  1.000 31.85075  ? 625 HOH   A O     1 
HETATM 3900 O  O     . HOH   J 6 .   ? 13.39982 19.50295 10.80768  1.000 43.09077  ? 626 HOH   A O     1 
HETATM 3901 O  O     . HOH   J 6 .   ? 21.98100 23.43112 26.51348  1.000 39.14427  ? 627 HOH   A O     1 
HETATM 3902 O  O     . HOH   J 6 .   ? 17.44851 23.25926 25.05616  1.000 28.94868  ? 628 HOH   A O     1 
HETATM 3903 O  O     . HOH   J 6 .   ? 25.42970 37.33732 24.77862  1.000 25.53826  ? 629 HOH   A O     1 
HETATM 3904 O  O     . HOH   J 6 .   ? 23.49544 13.31685 26.20009  1.000 40.47929  ? 630 HOH   A O     1 
HETATM 3905 O  O     . HOH   J 6 .   ? 29.93074 39.91466 31.10851  1.000 38.30299  ? 631 HOH   A O     1 
HETATM 3906 O  O     . HOH   J 6 .   ? 23.29191 28.05837 34.89641  1.000 36.38947  ? 632 HOH   A O     1 
HETATM 3907 O  O     . HOH   J 6 .   ? 5.18286  22.14371 21.85222  1.000 41.62026  ? 633 HOH   A O     1 
HETATM 3908 O  O     . HOH   J 6 .   ? 24.48326 6.81817  29.02565  1.000 39.71630  ? 634 HOH   A O     1 
HETATM 3909 O  O     . HOH   J 6 .   ? 18.84463 26.05252 28.51488  1.000 32.86368  ? 635 HOH   A O     1 
HETATM 3910 O  O     . HOH   J 6 .   ? 33.44554 25.19157 25.10262  1.000 37.11926  ? 636 HOH   A O     1 
HETATM 3911 O  O     . HOH   J 6 .   ? 42.53310 17.38423 4.52967   1.000 45.51809  ? 637 HOH   A O     1 
HETATM 3912 O  O     . HOH   J 6 .   ? 37.74195 8.00707  10.30590  1.000 44.91059  ? 638 HOH   A O     1 
HETATM 3913 O  O     . HOH   J 6 .   ? 39.26628 21.45075 28.86286  1.000 59.65391  ? 639 HOH   A O     1 
HETATM 3914 O  O     . HOH   J 6 .   ? 36.83453 36.15881 31.97920  1.000 48.69217  ? 640 HOH   A O     1 
HETATM 3915 O  O     . HOH   J 6 .   ? 20.25352 27.93688 35.79169  1.000 51.52513  ? 641 HOH   A O     1 
HETATM 3916 O  O     . HOH   J 6 .   ? 16.26919 31.42516 27.42640  1.000 41.18957  ? 642 HOH   A O     1 
HETATM 3917 O  O     . HOH   J 6 .   ? 29.45164 22.53716 2.53163   1.000 44.27635  ? 643 HOH   A O     1 
HETATM 3918 O  O     . HOH   J 6 .   ? 27.03231 33.44446 35.07686  1.000 42.83454  ? 644 HOH   A O     1 
HETATM 3919 O  O     . HOH   J 6 .   ? 30.51710 24.23672 30.44468  1.000 33.46827  ? 645 HOH   A O     1 
HETATM 3920 O  O     . HOH   J 6 .   ? 18.10913 29.48101 26.60569  1.000 44.54702  ? 646 HOH   A O     1 
HETATM 3921 O  O     . HOH   J 6 .   ? 14.92238 26.65335 34.36759  1.000 53.36687  ? 647 HOH   A O     1 
HETATM 3922 O  O     . HOH   J 6 .   ? 28.86622 0.70644  18.05430  1.000 39.98952  ? 648 HOH   A O     1 
HETATM 3923 O  O     . HOH   J 6 .   ? 44.79688 25.45766 26.69078  1.000 53.44896  ? 649 HOH   A O     1 
HETATM 3924 O  O     . HOH   J 6 .   ? 38.23726 25.59161 24.65066  1.000 52.25145  ? 650 HOH   A O     1 
HETATM 3925 O  O     . HOH   J 6 .   ? 13.69379 12.59044 3.19456   1.000 56.27794  ? 651 HOH   A O     1 
HETATM 3926 O  O     . HOH   J 6 .   ? 30.46469 21.57675 31.34331  1.000 36.76508  ? 652 HOH   A O     1 
HETATM 3927 O  O     . HOH   J 6 .   ? 30.44610 9.13613  -0.90600  1.000 52.41326  ? 653 HOH   A O     1 
HETATM 3928 O  O     . HOH   J 6 .   ? 19.21198 20.83640 -0.90241  1.000 65.62642  ? 654 HOH   A O     1 
HETATM 3929 O  O     . HOH   J 6 .   ? 24.27606 32.09314 35.52344  1.000 51.50882  ? 655 HOH   A O     1 
HETATM 3930 O  O     . HOH   J 6 .   ? 17.16671 30.53966 31.55968  1.000 58.79936  ? 656 HOH   A O     1 
HETATM 3931 O  O     . HOH   J 6 .   ? 52.01250 8.65350  21.17114  1.000 68.42142  ? 657 HOH   A O     1 
HETATM 3932 O  O     . HOH   J 6 .   ? 33.12459 17.63748 24.61839  1.000 53.37986  ? 658 HOH   A O     1 
HETATM 3933 O  O     . HOH   J 6 .   ? 34.06575 19.79461 30.07409  1.000 71.12057  ? 659 HOH   A O     1 
HETATM 3934 O  O     . HOH   J 6 .   ? 39.13314 22.87626 30.74851  1.000 58.59886  ? 660 HOH   A O     1 
HETATM 3935 O  O     . HOH   J 6 .   ? 19.47206 24.78656 26.22145  1.000 39.09634  ? 661 HOH   A O     1 
HETATM 3936 O  O     . HOH   J 6 .   ? 35.27967 13.13885 24.87218  1.000 49.97535  ? 662 HOH   A O     1 
HETATM 3937 O  O     . HOH   J 6 .   ? 28.06283 24.38099 0.30163   1.000 61.31267  ? 663 HOH   A O     1 
HETATM 3938 O  O     . HOH   J 6 .   ? 37.11447 11.41721 26.30586  1.000 65.87953  ? 664 HOH   A O     1 
HETATM 3939 O  O     . HOH   J 6 .   ? 34.46261 23.77961 27.38983  1.000 43.46269  ? 665 HOH   A O     1 
HETATM 3940 O  O     . HOH   J 6 .   ? 33.26780 24.15473 29.76163  1.000 45.15865  ? 666 HOH   A O     1 
HETATM 3941 O  O     . HOH   K 6 .   ? 37.74645 52.33971 28.19945  1.000 43.43394  ? 801 HOH   B O     1 
HETATM 3942 O  O     . HOH   K 6 .   ? 36.13317 39.45737 10.44374  1.000 49.83527  ? 802 HOH   B O     1 
HETATM 3943 O  O     . HOH   K 6 .   ? 33.24707 40.89833 8.91523   1.000 53.14326  ? 803 HOH   B O     1 
HETATM 3944 O  O     . HOH   K 6 .   ? 32.75000 36.92606 13.72710  1.000 39.45080  ? 804 HOH   B O     1 
HETATM 3945 O  O     . HOH   K 6 .   ? 12.74690 28.78865 14.79214  1.000 48.37188  ? 805 HOH   B O     1 
HETATM 3946 O  O     . HOH   K 6 .   ? 27.33269 40.00994 31.64143  1.000 34.28184  ? 806 HOH   B O     1 
HETATM 3947 O  O     . HOH   K 6 .   ? 26.36188 38.25205 22.38043  1.000 32.07885  ? 807 HOH   B O     1 
HETATM 3948 O  O     . HOH   K 6 .   ? 33.41657 41.17173 2.00911   1.000 35.46370  ? 808 HOH   B O     1 
HETATM 3949 O  O     . HOH   K 6 .   ? 21.43048 38.13529 4.72211   1.000 56.35987  ? 809 HOH   B O     1 
HETATM 3950 O  O     . HOH   K 6 .   ? 32.23778 26.09299 8.96384   1.000 39.58292  ? 810 HOH   B O     1 
HETATM 3951 O  O     . HOH   K 6 .   ? 22.74313 39.45287 31.13554  1.000 34.18289  ? 811 HOH   B O     1 
HETATM 3952 O  O     . HOH   K 6 .   ? 16.18036 40.23583 31.83892  1.000 54.98095  ? 812 HOH   B O     1 
HETATM 3953 O  O     . HOH   K 6 .   ? 42.67522 16.14110 8.30255   1.000 42.19847  ? 813 HOH   B O     1 
HETATM 3954 O  O     . HOH   K 6 .   ? 25.50824 31.32109 24.05588  1.000 42.86890  ? 814 HOH   B O     1 
HETATM 3955 O  O     . HOH   K 6 .   ? 5.01806  40.58963 20.15363  1.000 40.69441  ? 815 HOH   B O     1 
HETATM 3956 O  O     . HOH   K 6 .   ? 36.61945 35.24991 3.36352   1.000 44.39747  ? 816 HOH   B O     1 
HETATM 3957 O  O     . HOH   K 6 .   ? 19.20011 46.98643 21.96128  1.000 42.15444  ? 817 HOH   B O     1 
HETATM 3958 O  O     . HOH   K 6 .   ? 36.78403 30.01770 13.75817  1.000 32.44080  ? 818 HOH   B O     1 
HETATM 3959 O  O     . HOH   K 6 .   ? 26.25877 29.24270 22.60119  1.000 34.21144  ? 819 HOH   B O     1 
HETATM 3960 O  O     . HOH   K 6 .   ? 23.57294 53.29118 11.15723  1.000 36.63826  ? 820 HOH   B O     1 
HETATM 3961 O  O     . HOH   K 6 .   ? 43.81677 17.91684 6.55541   1.000 43.45541  ? 821 HOH   B O     1 
HETATM 3962 O  O     . HOH   K 6 .   ? 46.98087 29.61566 22.81448  1.000 54.24638  ? 822 HOH   B O     1 
HETATM 3963 O  O     . HOH   K 6 .   ? 38.35073 32.14435 14.46379  1.000 39.98499  ? 823 HOH   B O     1 
HETATM 3964 O  O     . HOH   K 6 .   ? 26.93175 29.74684 0.46012   1.000 46.08666  ? 824 HOH   B O     1 
HETATM 3965 O  O     . HOH   K 6 .   ? 27.97081 24.76842 5.05027   1.000 53.34236  ? 825 HOH   B O     1 
HETATM 3966 O  O     . HOH   K 6 .   ? 16.04513 21.67830 7.43091   1.000 54.79903  ? 826 HOH   B O     1 
HETATM 3967 O  O     . HOH   K 6 .   ? 40.02495 18.15878 3.09676   1.000 44.16153  ? 827 HOH   B O     1 
HETATM 3968 O  O     . HOH   K 6 .   ? 12.98311 30.31170 7.14998   1.000 54.56905  ? 828 HOH   B O     1 
HETATM 3969 O  O     . HOH   K 6 .   ? 6.92823  43.12179 14.18911  1.000 50.75735  ? 829 HOH   B O     1 
HETATM 3970 O  O     . HOH   K 6 .   ? 30.45231 27.51472 -0.99344  1.000 54.08454  ? 830 HOH   B O     1 
HETATM 3971 O  O     . HOH   K 6 .   ? 9.76936  42.50633 25.53754  1.000 46.35607  ? 831 HOH   B O     1 
HETATM 3972 O  O     . HOH   K 6 .   ? 34.00186 38.07952 10.81853  1.000 53.33529  ? 832 HOH   B O     1 
HETATM 3973 O  O     . HOH   K 6 .   ? 30.97068 29.69046 21.84882  1.000 31.06204  ? 833 HOH   B O     1 
HETATM 3974 O  O     . HOH   K 6 .   ? 28.78781 40.86710 2.55313   1.000 44.11117  ? 834 HOH   B O     1 
HETATM 3975 O  O     . HOH   K 6 .   ? 16.58733 24.23906 2.77471   1.000 58.20608  ? 835 HOH   B O     1 
HETATM 3976 O  O     . HOH   K 6 .   ? 37.85113 32.14356 11.51846  1.000 44.85667  ? 836 HOH   B O     1 
HETATM 3977 O  O     . HOH   K 6 .   ? 17.97857 42.77922 27.94433  1.000 36.84866  ? 837 HOH   B O     1 
HETATM 3978 O  O     . HOH   K 6 .   ? 25.86935 47.93883 23.15435  1.000 40.02642  ? 838 HOH   B O     1 
HETATM 3979 O  O     . HOH   K 6 .   ? 39.18452 32.76605 5.50175   1.000 33.40446  ? 839 HOH   B O     1 
HETATM 3980 O  O     . HOH   K 6 .   ? 30.94782 30.96224 2.52546   1.000 43.29193  ? 840 HOH   B O     1 
HETATM 3981 O  O     . HOH   K 6 .   ? 25.60978 48.94123 20.39019  1.000 36.77573  ? 841 HOH   B O     1 
HETATM 3982 O  O     . HOH   K 6 .   ? 38.92999 36.92785 6.84535   1.000 44.26687  ? 842 HOH   B O     1 
HETATM 3983 O  O     . HOH   K 6 .   ? 11.88949 47.25416 19.81408  1.000 57.43344  ? 843 HOH   B O     1 
HETATM 3984 O  O     . HOH   K 6 .   ? 35.45846 18.22897 7.79674   1.000 39.81985  ? 844 HOH   B O     1 
HETATM 3985 O  O     . HOH   K 6 .   ? 10.45079 45.04405 20.74353  1.000 53.56300  ? 845 HOH   B O     1 
HETATM 3986 O  O     . HOH   K 6 .   ? 32.56559 49.89155 13.59846  1.000 44.93165  ? 846 HOH   B O     1 
HETATM 3987 O  O     . HOH   K 6 .   ? 31.94939 47.05275 30.11685  1.000 50.96215  ? 847 HOH   B O     1 
HETATM 3988 O  O     . HOH   K 6 .   ? 41.23974 44.41833 14.50866  1.000 95.12725  ? 848 HOH   B O     1 
HETATM 3989 O  O     . HOH   K 6 .   ? 40.09139 49.90664 29.08609  1.000 43.19078  ? 849 HOH   B O     1 
HETATM 3990 O  O     . HOH   K 6 .   ? 42.131   39.362   23.605    1.000 49.13642  ? 850 HOH   B O     1 
HETATM 3991 O  O     . HOH   K 6 .   ? 39.58178 38.75863 8.56833   1.000 66.81235  ? 851 HOH   B O     1 
HETATM 3992 O  O     . HOH   K 6 .   ? 49.73529 31.04092 16.52631  1.000 40.63501  ? 852 HOH   B O     1 
HETATM 3993 O  O     . HOH   K 6 .   ? 19.27971 31.12868 24.96274  1.000 33.29746  ? 853 HOH   B O     1 
HETATM 3994 O  O     . HOH   K 6 .   ? 10.14324 28.82815 13.08644  1.000 56.48428  ? 854 HOH   B O     1 
HETATM 3995 O  O     . HOH   K 6 .   ? 42.38910 23.32756 0.64603   1.000 53.15667  ? 855 HOH   B O     1 
HETATM 3996 O  O     . HOH   K 6 .   ? 23.77076 51.24134 19.64652  1.000 52.40572  ? 856 HOH   B O     1 
HETATM 3997 O  O     . HOH   K 6 .   ? 20.72141 46.09440 -6.46439  1.000 55.00306  ? 857 HOH   B O     1 
HETATM 3998 O  O     . HOH   K 6 .   ? 41.15602 38.44371 6.93692   1.000 52.14887  ? 858 HOH   B O     1 
HETATM 3999 O  O     . HOH   K 6 .   ? 23.14247 57.89155 4.65795   1.000 54.66705  ? 859 HOH   B O     1 
HETATM 4000 O  O     . HOH   K 6 .   ? 46.30175 49.82973 9.95328   1.000 61.09348  ? 860 HOH   B O     1 
HETATM 4001 O  O     . HOH   K 6 .   ? 21.89933 37.44814 -12.13069 1.000 56.52773  ? 861 HOH   B O     1 
HETATM 4002 O  O     . HOH   K 6 .   ? 39.79180 33.89676 10.79078  1.000 45.24812  ? 862 HOH   B O     1 
HETATM 4003 O  O     . HOH   K 6 .   ? 21.918   33.590   -14.203   1.000 63.84989  ? 863 HOH   B O     1 
HETATM 4004 O  O     . HOH   K 6 .   ? 29.16535 29.08601 1.06964   1.000 46.17010  ? 864 HOH   B O     1 
HETATM 4005 O  O     . HOH   K 6 .   ? 32.07182 17.95186 -2.71792  1.000 52.68421  ? 865 HOH   B O     1 
HETATM 4006 O  O     . HOH   K 6 .   ? 38.97026 35.23969 4.53841   1.000 46.62096  ? 866 HOH   B O     1 
HETATM 4007 O  O     . HOH   K 6 .   ? 23.10026 52.14554 22.04483  1.000 49.69422  ? 867 HOH   B O     1 
HETATM 4008 O  O     . HOH   K 6 .   ? 18.56483 44.08222 30.28172  1.000 40.31180  ? 868 HOH   B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP A 9   ? 1.35924 1.17317 1.25497 -0.01858 -0.07531 0.11529  6   ASP A N   
2    C CA  . ASP A 9   ? 1.31548 1.14863 1.22978 -0.01301 -0.06549 0.10801  6   ASP A CA  
3    C C   . ASP A 9   ? 1.29388 1.13319 1.23179 -0.00336 -0.06854 0.11129  6   ASP A C   
4    O O   . ASP A 9   ? 1.30035 1.13890 1.24764 0.00093  -0.07904 0.11845  6   ASP A O   
5    C CB  . ASP A 9   ? 1.28095 1.13231 1.20172 -0.01251 -0.06331 0.10401  6   ASP A CB  
6    N N   . ASP A 10  ? 1.25813 1.10399 1.20591 -0.00006 -0.05922 0.10558  7   ASP A N   
7    C CA  . ASP A 10  ? 1.20652 1.06027 1.17781 0.00900  -0.06039 0.10709  7   ASP A CA  
8    C C   . ASP A 10  ? 1.09240 0.97047 1.08478 0.01492  -0.05466 0.10198  7   ASP A C   
9    O O   . ASP A 10  ? 1.07145 0.95890 1.08460 0.02234  -0.05892 0.10485  7   ASP A O   
10   C CB  . ASP A 10  ? 1.23385 1.07816 1.20348 0.00921  -0.05432 0.10450  7   ASP A CB  
11   C CG  . ASP A 10  ? 1.28843 1.11211 1.25231 0.00946  -0.06390 0.11257  7   ASP A CG  
12   O OD1 . ASP A 10  ? 1.30067 1.12626 1.27984 0.01598  -0.07311 0.11852  7   ASP A OD1 
13   O OD2 . ASP A 10  ? 1.32680 1.13220 1.27073 0.00306  -0.06232 0.11287  7   ASP A OD2 
14   N N   . TYR A 11  ? 0.99751 0.88590 0.98498 0.01177  -0.04528 0.09439  8   TYR A N   
15   C CA  . TYR A 11  ? 0.91527 0.82604 0.92107 0.01702  -0.03967 0.08953  8   TYR A CA  
16   C C   . TYR A 11  ? 0.81895 0.73855 0.83233 0.01901  -0.04756 0.09400  8   TYR A C   
17   O O   . TYR A 11  ? 0.82703 0.73671 0.82832 0.01495  -0.05569 0.09912  8   TYR A O   
18   C CB  . TYR A 11  ? 0.92593 0.84439 0.92338 0.01308  -0.02804 0.08012  8   TYR A CB  
19   C CG  . TYR A 11  ? 0.95702 0.87677 0.95751 0.01423  -0.01788 0.07366  8   TYR A CG  
20   C CD1 . TYR A 11  ? 0.98809 0.89740 0.99260 0.01660  -0.01952 0.07663  8   TYR A CD1 
21   C CD2 . TYR A 11  ? 0.95941 0.89104 0.95928 0.01316  -0.00682 0.06439  8   TYR A CD2 
22   C CE1 . TYR A 11  ? 1.01220 0.92277 1.01983 0.01756  -0.01008 0.07047  8   TYR A CE1 
23   C CE2 . TYR A 11  ? 0.97662 0.91001 0.97955 0.01417  0.00256  0.05814  8   TYR A CE2 
24   C CZ  . TYR A 11  ? 1.00813 0.93100 1.01494 0.01624  0.00105  0.06118  8   TYR A CZ  
25   O OH  . TYR A 11  ? 1.02469 0.94938 1.03481 0.01712  0.01053  0.05472  8   TYR A OH  
26   N N   . SER A 12  ? 0.72398 0.66262 0.75747 0.02509  -0.04484 0.09181  9   SER A N   
27   C CA  . SER A 12  ? 0.69839 0.64689 0.74246 0.02782  -0.05183 0.09592  9   SER A CA  
28   C C   . SER A 12  ? 0.66585 0.62791 0.70864 0.02612  -0.04673 0.09099  9   SER A C   
29   O O   . SER A 12  ? 0.63664 0.60187 0.67977 0.02540  -0.05297 0.09440  9   SER A O   
30   C CB  . SER A 12  ? 0.67829 0.63819 0.74743 0.03610  -0.05394 0.09806  9   SER A CB  
31   O OG  . SER A 12  ? 0.71197 0.68074 0.79148 0.03846  -0.06098 0.10221  9   SER A OG  
32   N N   . LEU A 13  ? 0.64163 0.61145 0.68283 0.02548  -0.03580 0.08296  10  LEU A N   
33   C CA  . LEU A 13  ? 0.62836 0.61306 0.67196 0.02545  -0.03063 0.07790  10  LEU A CA  
34   C C   . LEU A 13  ? 0.65275 0.63161 0.67569 0.01817  -0.02825 0.07396  10  LEU A C   
35   O O   . LEU A 13  ? 0.66664 0.65672 0.69047 0.01794  -0.02486 0.06987  10  LEU A O   
36   C CB  . LEU A 13  ? 0.57132 0.57021 0.62720 0.02978  -0.02017 0.07095  10  LEU A CB  
37   C CG  . LEU A 13  ? 0.60477 0.61494 0.68390 0.03733  -0.02097 0.07320  10  LEU A CG  
38   C CD1 . LEU A 13  ? 0.62007 0.64216 0.70837 0.04066  -0.01004 0.06579  10  LEU A CD1 
39   C CD2 . LEU A 13  ? 0.57748 0.59898 0.66813 0.04003  -0.02642 0.07694  10  LEU A CD2 
40   N N   . VAL A 14  ? 0.66059 0.62220 0.66508 0.01215  -0.03019 0.07510  11  VAL A N   
41   C CA  . VAL A 14  ? 0.72125 0.67772 0.70609 0.00492  -0.02533 0.06925  11  VAL A CA  
42   C C   . VAL A 14  ? 0.75448 0.71712 0.73537 0.00259  -0.02827 0.06875  11  VAL A C   
43   O O   . VAL A 14  ? 0.79390 0.76048 0.76577 -0.00099 -0.02214 0.06164  11  VAL A O   
44   C CB  . VAL A 14  ? 0.72370 0.65934 0.68915 -0.00158 -0.02831 0.07190  11  VAL A CB  
45   C CG1 . VAL A 14  ? 0.71677 0.64597 0.68578 0.00060  -0.02467 0.07172  11  VAL A CG1 
46   C CG2 . VAL A 14  ? 0.74846 0.67378 0.70968 -0.00300 -0.04059 0.08109  11  VAL A CG2 
47   N N   . HIS A 15  ? 0.75157 0.71543 0.73952 0.00462  -0.03759 0.07582  12  HIS A N   
48   C CA  . HIS A 15  ? 0.76620 0.73395 0.74951 0.00193  -0.04136 0.07602  12  HIS A CA  
49   C C   . HIS A 15  ? 0.70109 0.68711 0.70132 0.00736  -0.03955 0.07445  12  HIS A C   
50   O O   . HIS A 15  ? 0.70525 0.69548 0.70297 0.00557  -0.04225 0.07424  12  HIS A O   
51   C CB  . HIS A 15  ? 0.85145 0.80835 0.82976 -0.00026 -0.05308 0.08455  12  HIS A CB  
52   C CG  . HIS A 15  ? 0.94137 0.87959 0.89867 -0.00732 -0.05556 0.08597  12  HIS A CG  
53   N ND1 . HIS A 15  ? 0.96842 0.90142 0.90724 -0.01443 -0.05041 0.07983  12  HIS A ND1 
54   C CD2 . HIS A 15  ? 0.97512 0.89845 0.92664 -0.00854 -0.06276 0.09278  12  HIS A CD2 
55   C CE1 . HIS A 15  ? 0.99570 0.91134 0.91779 -0.02012 -0.05397 0.08287  12  HIS A CE1 
56   N NE2 . HIS A 15  ? 0.99215 0.90123 0.92122 -0.01659 -0.06167 0.09096  12  HIS A NE2 
57   N N   . LYS A 16  ? 0.66115 0.65786 0.67814 0.01368  -0.03502 0.07327  13  LYS A N   
58   C CA  . LYS A 16  ? 0.65026 0.66385 0.68343 0.01875  -0.03358 0.07247  13  LYS A CA  
59   C C   . LYS A 16  ? 0.67607 0.69881 0.70485 0.01768  -0.02502 0.06396  13  LYS A C   
60   O O   . LYS A 16  ? 0.69208 0.71406 0.71494 0.01656  -0.01707 0.05756  13  LYS A O   
61   C CB  . LYS A 16  ? 0.64006 0.66194 0.69262 0.02561  -0.03179 0.07409  13  LYS A CB  
62   C CG  . LYS A 16  ? 0.61912 0.65698 0.68934 0.03065  -0.03241 0.07538  13  LYS A CG  
63   C CD  . LYS A 16  ? 0.61756 0.66382 0.70653 0.03693  -0.02991 0.07614  13  LYS A CD  
64   C CE  . LYS A 16  ? 0.63180 0.69471 0.73745 0.04136  -0.02908 0.07650  13  LYS A CE  
65   N NZ  . LYS A 16  ? 0.63359 0.70663 0.75656 0.04704  -0.02424 0.07512  13  LYS A NZ  
66   N N   . ASN A 17  ? 0.65960 0.69088 0.69150 0.01812  -0.02683 0.06379  14  ASN A N   
67   C CA  . ASN A 17  ? 0.64000 0.68084 0.66943 0.01793  -0.01994 0.05622  14  ASN A CA  
68   C C   . ASN A 17  ? 0.62169 0.67851 0.66898 0.02449  -0.01572 0.05512  14  ASN A C   
69   O O   . ASN A 17  ? 0.64306 0.70465 0.70468 0.02849  -0.01981 0.06091  14  ASN A O   
70   C CB  . ASN A 17  ? 0.63166 0.67141 0.65272 0.01417  -0.02460 0.05641  14  ASN A CB  
71   C CG  . ASN A 17  ? 0.66233 0.68785 0.66374 0.00689  -0.02688 0.05528  14  ASN A CG  
72   O OD1 . ASN A 17  ? 0.69175 0.71226 0.68236 0.00380  -0.02090 0.04949  14  ASN A OD1 
73   N ND2 . ASN A 17  ? 0.64860 0.66767 0.64512 0.00384  -0.03544 0.06062  14  ASN A ND2 
74   N N   . ILE A 18  ? 0.53300 0.59829 0.57925 0.02546  -0.00749 0.04737  15  ILE A N   
75   C CA  . ILE A 18  ? 0.50122 0.58194 0.56235 0.03110  -0.00349 0.04593  15  ILE A CA  
76   C C   . ILE A 18  ? 0.48054 0.56806 0.54130 0.03100  -0.00524 0.04512  15  ILE A C   
77   O O   . ILE A 18  ? 0.49890 0.59856 0.57158 0.03534  -0.00319 0.04514  15  ILE A O   
78   C CB  . ILE A 18  ? 0.48688 0.57434 0.54963 0.03335  0.00661  0.03823  15  ILE A CB  
79   C CG1 . ILE A 18  ? 0.46704 0.55312 0.51523 0.02965  0.01157  0.02988  15  ILE A CG1 
80   C CG2 . ILE A 18  ? 0.50836 0.58929 0.57283 0.03378  0.00849  0.03911  15  ILE A CG2 
81   C CD1 . ILE A 18  ? 0.45798 0.55297 0.50887 0.03230  0.02136  0.02178  15  ILE A CD1 
82   N N   . LEU A 19  ? 0.42358 0.50357 0.47104 0.02607  -0.00894 0.04434  16  LEU A N   
83   C CA  . LEU A 19  ? 0.44147 0.52606 0.48906 0.02575  -0.01240 0.04491  16  LEU A CA  
84   C C   . LEU A 19  ? 0.47504 0.55629 0.52832 0.02544  -0.02171 0.05382  16  LEU A C   
85   O O   . LEU A 19  ? 0.49540 0.56855 0.54874 0.02440  -0.02614 0.05889  16  LEU A O   
86   C CB  . LEU A 19  ? 0.44891 0.52791 0.48014 0.02065  -0.01161 0.03886  16  LEU A CB  
87   C CG  . LEU A 19  ? 0.44484 0.52689 0.46976 0.02051  -0.00250 0.02924  16  LEU A CG  
88   C CD1 . LEU A 19  ? 0.44085 0.51899 0.45117 0.01568  -0.00204 0.02276  16  LEU A CD1 
89   C CD2 . LEU A 19  ? 0.43480 0.53100 0.47184 0.02651  0.00330  0.02626  16  LEU A CD2 
90   N N   . HIS A 20  ? 0.48062 0.56806 0.53881 0.02641  -0.02484 0.05564  17  HIS A N   
91   C CA  . HIS A 20  ? 0.49276 0.57984 0.55981 0.02705  -0.03281 0.06384  17  HIS A CA  
92   C C   . HIS A 20  ? 0.49671 0.57156 0.55297 0.02185  -0.04066 0.06743  17  HIS A C   
93   O O   . HIS A 20  ? 0.55662 0.62956 0.61949 0.02214  -0.04775 0.07434  17  HIS A O   
94   C CB  . HIS A 20  ? 0.51854 0.61612 0.59501 0.02963  -0.03352 0.06501  17  HIS A CB  
95   C CG  . HIS A 20  ? 0.61646 0.71321 0.68310 0.02682  -0.03419 0.06125  17  HIS A CG  
96   N ND1 . HIS A 20  ? 0.66206 0.74861 0.71459 0.02152  -0.03803 0.06005  17  HIS A ND1 
97   C CD2 . HIS A 20  ? 0.62250 0.72733 0.69173 0.02865  -0.03182 0.05846  17  HIS A CD2 
98   C CE1 . HIS A 20  ? 0.65283 0.74163 0.70033 0.02033  -0.03781 0.05625  17  HIS A CE1 
99   N NE2 . HIS A 20  ? 0.63444 0.73393 0.69180 0.02473  -0.03427 0.05537  17  HIS A NE2 
100  N N   . SER A 21  ? 0.48060 0.54746 0.52062 0.01701  -0.03962 0.06273  18  SER A N   
101  C CA  . SER A 21  ? 0.47803 0.53299 0.50666 0.01161  -0.04679 0.06588  18  SER A CA  
102  C C   . SER A 21  ? 0.47569 0.52160 0.48691 0.00655  -0.04311 0.05987  18  SER A C   
103  O O   . SER A 21  ? 0.44378 0.49390 0.45099 0.00673  -0.03567 0.05225  18  SER A O   
104  C CB  . SER A 21  ? 0.47807 0.53457 0.50589 0.00975  -0.05234 0.06743  18  SER A CB  
105  O OG  . SER A 21  ? 0.48351 0.54278 0.50337 0.00807  -0.04800 0.06001  18  SER A OG  
106  N N   . GLU A 22  ? 0.47816 0.51158 0.47889 0.00187  -0.04852 0.06329  19  GLU A N   
107  C CA  . GLU A 22  ? 0.57489 0.59860 0.55736 -0.00424 -0.04591 0.05798  19  GLU A CA  
108  C C   . GLU A 22  ? 0.55474 0.58089 0.52874 -0.00762 -0.04476 0.05174  19  GLU A C   
109  O O   . GLU A 22  ? 0.50711 0.53127 0.46985 -0.01095 -0.03898 0.04397  19  GLU A O   
110  C CB  . GLU A 22  ? 0.65422 0.66384 0.62695 -0.00879 -0.05307 0.06386  19  GLU A CB  
111  C CG  . GLU A 22  ? 0.75370 0.75176 0.70851 -0.01478 -0.04964 0.05963  19  GLU A CG  
112  C CD  . GLU A 22  ? 0.88123 0.87633 0.83861 -0.01246 -0.04499 0.05984  19  GLU A CD  
113  O OE1 . GLU A 22  ? 0.93389 0.92384 0.87967 -0.01606 -0.03873 0.05389  19  GLU A OE1 
114  O OE2 . GLU A 22  ? 0.93074 0.92882 0.90209 -0.00712 -0.04750 0.06565  19  GLU A OE2 
115  N N   . ASP A 23  ? 0.51742 0.54798 0.49709 -0.00684 -0.05018 0.05470  20  ASP A N   
116  C CA  . ASP A 23  ? 0.52060 0.55343 0.49336 -0.00971 -0.04984 0.04899  20  ASP A CA  
117  C C   . ASP A 23  ? 0.45628 0.49870 0.43156 -0.00671 -0.04139 0.04063  20  ASP A C   
118  O O   . ASP A 23  ? 0.43493 0.47674 0.39998 -0.01006 -0.03829 0.03289  20  ASP A O   
119  C CB  . ASP A 23  ? 0.56163 0.59800 0.54224 -0.00863 -0.05707 0.05425  20  ASP A CB  
120  C CG  . ASP A 23  ? 0.62107 0.64735 0.59499 -0.01327 -0.06576 0.06027  20  ASP A CG  
121  O OD1 . ASP A 23  ? 0.67793 0.69396 0.64041 -0.01738 -0.06632 0.06061  20  ASP A OD1 
122  O OD2 . ASP A 23  ? 0.66024 0.68865 0.63994 -0.01297 -0.07205 0.06459  20  ASP A OD2 
123  N N   . LEU A 24  ? 0.42303 0.47471 0.41201 -0.00040 -0.03768 0.04176  21  LEU A N   
124  C CA  . LEU A 24  ? 0.41190 0.47284 0.40327 0.00275  -0.02982 0.03397  21  LEU A CA  
125  C C   . LEU A 24  ? 0.41677 0.47395 0.39796 0.00028  -0.02278 0.02678  21  LEU A C   
126  O O   . LEU A 24  ? 0.38003 0.44018 0.35470 -0.00091 -0.01783 0.01804  21  LEU A O   
127  C CB  . LEU A 24  ? 0.40369 0.47532 0.41175 0.00974  -0.02756 0.03718  21  LEU A CB  
128  C CG  . LEU A 24  ? 0.38748 0.46960 0.39908 0.01362  -0.02012 0.02987  21  LEU A CG  
129  C CD1 . LEU A 24  ? 0.33804 0.42161 0.34301 0.01180  -0.02097 0.02438  21  LEU A CD1 
130  C CD2 . LEU A 24  ? 0.35428 0.44689 0.38220 0.01996  -0.01897 0.03404  21  LEU A CD2 
131  N N   . LEU A 25  ? 0.43858 0.48907 0.41835 -0.00058 -0.02233 0.03010  22  LEU A N   
132  C CA  . LEU A 25  ? 0.47751 0.52328 0.44698 -0.00355 -0.01568 0.02359  22  LEU A CA  
133  C C   . LEU A 25  ? 0.47710 0.51462 0.42926 -0.01096 -0.01627 0.01829  22  LEU A C   
134  O O   . LEU A 25  ? 0.47017 0.50923 0.41464 -0.01306 -0.00970 0.00904  22  LEU A O   
135  C CB  . LEU A 25  ? 0.47838 0.51679 0.44914 -0.00340 -0.01626 0.02912  22  LEU A CB  
136  C CG  . LEU A 25  ? 0.47021 0.50314 0.43096 -0.00643 -0.00910 0.02292  22  LEU A CG  
137  C CD1 . LEU A 25  ? 0.42447 0.46864 0.38895 -0.00327 -0.00008 0.01372  22  LEU A CD1 
138  C CD2 . LEU A 25  ? 0.48603 0.51270 0.45081 -0.00498 -0.00974 0.02882  22  LEU A CD2 
139  N N   . LYS A 26  ? 0.47468 0.50386 0.42071 -0.01514 -0.02409 0.02369  23  LYS A N   
140  C CA  . LYS A 26  ? 0.53338 0.55475 0.46278 -0.02267 -0.02493 0.01881  23  LYS A CA  
141  C C   . LYS A 26  ? 0.47932 0.50867 0.40783 -0.02267 -0.02274 0.01076  23  LYS A C   
142  O O   . LYS A 26  ? 0.47622 0.50300 0.39253 -0.02771 -0.01909 0.00242  23  LYS A O   
143  C CB  . LYS A 26  ? 0.62884 0.64030 0.55268 -0.02680 -0.03423 0.02667  23  LYS A CB  
144  C CG  . LYS A 26  ? 0.70832 0.70771 0.62543 -0.02965 -0.03621 0.03220  23  LYS A CG  
145  C CD  . LYS A 26  ? 0.80642 0.79659 0.71839 -0.03332 -0.04603 0.04008  23  LYS A CD  
146  C CE  . LYS A 26  ? 0.86654 0.84330 0.76967 -0.03660 -0.04829 0.04519  23  LYS A CE  
147  N NZ  . LYS A 26  ? 0.90753 0.87233 0.79121 -0.04546 -0.05116 0.04391  23  LYS A NZ  
148  N N   . TYR A 27  ? 0.45584 0.49473 0.39707 -0.01719 -0.02489 0.01289  24  TYR A N   
149  C CA  . TYR A 27  ? 0.43333 0.47997 0.37476 -0.01625 -0.02273 0.00520  24  TYR A CA  
150  C C   . TYR A 27  ? 0.40329 0.45560 0.34270 -0.01493 -0.01348 -0.00480 24  TYR A C   
151  O O   . TYR A 27  ? 0.37839 0.43127 0.30906 -0.01822 -0.01056 -0.01396 24  TYR A O   
152  C CB  . TYR A 27  ? 0.39069 0.44622 0.34662 -0.01015 -0.02618 0.00987  24  TYR A CB  
153  C CG  . TYR A 27  ? 0.40496 0.46848 0.36187 -0.00825 -0.02376 0.00202  24  TYR A CG  
154  C CD1 . TYR A 27  ? 0.35778 0.41911 0.30874 -0.01179 -0.02810 -0.00059 24  TYR A CD1 
155  C CD2 . TYR A 27  ? 0.37846 0.45155 0.34201 -0.00291 -0.01724 -0.00313 24  TYR A CD2 
156  C CE1 . TYR A 27  ? 0.36672 0.43485 0.31875 -0.00980 -0.02626 -0.00802 24  TYR A CE1 
157  C CE2 . TYR A 27  ? 0.39054 0.47044 0.35466 -0.00090 -0.01551 -0.01039 24  TYR A CE2 
158  C CZ  . TYR A 27  ? 0.38497 0.46218 0.34347 -0.00424 -0.02013 -0.01280 24  TYR A CZ  
159  O OH  . TYR A 27  ? 0.35853 0.44212 0.31798 -0.00192 -0.01881 -0.02015 24  TYR A OH  
160  N N   . ILE A 28  ? 0.36155 0.41858 0.30946 -0.01009 -0.00877 -0.00357 25  ILE A N   
161  C CA  . ILE A 28  ? 0.39104 0.45433 0.33825 -0.00834 0.00012  -0.01294 25  ILE A CA  
162  C C   . ILE A 28  ? 0.41593 0.47126 0.34770 -0.01535 0.00416  -0.02002 25  ILE A C   
163  O O   . ILE A 28  ? 0.40167 0.46062 0.32751 -0.01704 0.00903  -0.03038 25  ILE A O   
164  C CB  . ILE A 28  ? 0.41021 0.47889 0.36900 -0.00252 0.00407  -0.00953 25  ILE A CB  
165  C CG1 . ILE A 28  ? 0.44402 0.52168 0.41793 0.00411  0.00087  -0.00352 25  ILE A CG1 
166  C CG2 . ILE A 28  ? 0.38990 0.46458 0.34731 -0.00115 0.01340  -0.01942 25  ILE A CG2 
167  C CD1 . ILE A 28  ? 0.41960 0.50326 0.40564 0.00970  0.00459  -0.00012 25  ILE A CD1 
168  N N   . LEU A 29  ? 0.41988 0.46407 0.34477 -0.01966 0.00208  -0.01465 26  LEU A N   
169  C CA  . LEU A 29  ? 0.45284 0.48837 0.36237 -0.02683 0.00620  -0.02064 26  LEU A CA  
170  C C   . LEU A 29  ? 0.46452 0.49674 0.36186 -0.03323 0.00421  -0.02652 26  LEU A C   
171  O O   . LEU A 29  ? 0.46533 0.49785 0.35334 -0.03730 0.01008  -0.03679 26  LEU A O   
172  C CB  . LEU A 29  ? 0.47204 0.49527 0.37672 -0.02988 0.00323  -0.01235 26  LEU A CB  
173  C CG  . LEU A 29  ? 0.45730 0.48271 0.37344 -0.02413 0.00542  -0.00712 26  LEU A CG  
174  C CD1 . LEU A 29  ? 0.42461 0.43748 0.33727 -0.02653 -0.00009 0.00252  26  LEU A CD1 
175  C CD2 . LEU A 29  ? 0.45605 0.48531 0.37085 -0.02361 0.01541  -0.01588 26  LEU A CD2 
176  N N   . GLU A 30  ? 0.46541 0.49491 0.36311 -0.03428 -0.00396 -0.02056 27  GLU A N   
177  C CA  . GLU A 30  ? 0.45127 0.47722 0.33752 -0.04068 -0.00635 -0.02578 27  GLU A CA  
178  C C   . GLU A 30  ? 0.42753 0.46434 0.31754 -0.03811 -0.00339 -0.03546 27  GLU A C   
179  O O   . GLU A 30  ? 0.42277 0.45854 0.30255 -0.04346 -0.00145 -0.04440 27  GLU A O   
180  C CB  . GLU A 30  ? 0.46098 0.48100 0.34702 -0.04245 -0.01609 -0.01652 27  GLU A CB  
181  C CG  . GLU A 30  ? 0.52679 0.53438 0.40603 -0.04630 -0.01999 -0.00787 27  GLU A CG  
182  C CD  . GLU A 30  ? 0.56865 0.57292 0.45248 -0.04560 -0.02984 0.00253  27  GLU A CD  
183  O OE1 . GLU A 30  ? 0.56847 0.58058 0.46223 -0.04160 -0.03311 0.00355  27  GLU A OE1 
184  O OE2 . GLU A 30  ? 0.59379 0.58742 0.47122 -0.04907 -0.03443 0.00963  27  GLU A OE2 
185  N N   . THR A 31  ? 0.38687 0.43400 0.29122 -0.03011 -0.00305 -0.03407 28  THR A N   
186  C CA  . THR A 31  ? 0.40237 0.45931 0.31081 -0.02699 -0.00130 -0.04234 28  THR A CA  
187  C C   . THR A 31  ? 0.45953 0.52360 0.36801 -0.02498 0.00772  -0.05283 28  THR A C   
188  O O   . THR A 31  ? 0.45052 0.51846 0.35425 -0.02670 0.01055  -0.06348 28  THR A O   
189  C CB  . THR A 31  ? 0.40395 0.46809 0.32697 -0.01963 -0.00578 -0.03562 28  THR A CB  
190  O OG1 . THR A 31  ? 0.39705 0.45498 0.32064 -0.02155 -0.01414 -0.02608 28  THR A OG1 
191  C CG2 . THR A 31  ? 0.39824 0.47111 0.32466 -0.01650 -0.00499 -0.04360 28  THR A CG2 
192  N N   . SER A 32  ? 0.43371 0.49983 0.34775 -0.02141 0.01227  -0.05042 29  SER A N   
193  C CA  . SER A 32  ? 0.43022 0.50520 0.34759 -0.01780 0.02043  -0.05935 29  SER A CA  
194  C C   . SER A 32  ? 0.52656 0.59699 0.43600 -0.02186 0.02748  -0.06383 29  SER A C   
195  O O   . SER A 32  ? 0.57024 0.64722 0.47901 -0.02095 0.03463  -0.07402 29  SER A O   
196  C CB  . SER A 32  ? 0.42574 0.50989 0.35850 -0.00898 0.02083  -0.05419 29  SER A CB  
197  O OG  . SER A 32  ? 0.43635 0.52528 0.37648 -0.00507 0.01511  -0.05086 29  SER A OG  
198  N N   . ALA A 33  ? 0.47211 0.42254 0.49948 -0.03270 -0.02629 -0.04679 30  ALA A N   
199  C CA  . ALA A 33  ? 0.42336 0.38902 0.45266 -0.03897 -0.03224 -0.03620 30  ALA A CA  
200  C C   . ALA A 33  ? 0.45178 0.42146 0.46837 -0.04357 -0.01666 -0.03858 30  ALA A C   
201  O O   . ALA A 33  ? 0.43116 0.41646 0.46688 -0.04073 -0.00808 -0.03225 30  ALA A O   
202  C CB  . ALA A 33  ? 0.37237 0.33330 0.38310 -0.04814 -0.05194 -0.03313 30  ALA A CB  
203  N N   . TYR A 34  ? 0.46508 0.42060 0.44930 -0.05103 -0.01301 -0.04766 31  TYR A N   
204  C CA  . TYR A 34  ? 0.49903 0.45613 0.46683 -0.05692 0.00134  -0.05050 31  TYR A CA  
205  C C   . TYR A 34  ? 0.46153 0.42571 0.44814 -0.04910 0.02257  -0.05312 31  TYR A C   
206  O O   . TYR A 34  ? 0.45252 0.42933 0.44380 -0.05164 0.03139  -0.04843 31  TYR A O   
207  C CB  . TYR A 34  ? 0.55285 0.49034 0.48298 -0.06499 0.00243  -0.06151 31  TYR A CB  
208  C CG  . TYR A 34  ? 0.62725 0.55885 0.53655 -0.07431 -0.01775 -0.05868 31  TYR A CG  
209  C CD1 . TYR A 34  ? 0.63739 0.58224 0.55440 -0.07840 -0.03139 -0.04674 31  TYR A CD1 
210  C CD2 . TYR A 34  ? 0.66464 0.57740 0.54713 -0.07899 -0.02325 -0.06804 31  TYR A CD2 
211  C CE1 . TYR A 34  ? 0.65218 0.59160 0.55109 -0.08671 -0.04981 -0.04424 31  TYR A CE1 
212  C CE2 . TYR A 34  ? 0.67360 0.58121 0.53836 -0.08733 -0.04190 -0.06559 31  TYR A CE2 
213  C CZ  . TYR A 34  ? 0.69944 0.62041 0.57276 -0.09103 -0.05503 -0.05371 31  TYR A CZ  
214  O OH  . TYR A 34  ? 0.75719 0.67307 0.61394 -0.09906 -0.07351 -0.05133 31  TYR A OH  
215  N N   . PRO A 35  ? 0.43566 0.39310 0.43435 -0.03973 0.03200  -0.06023 32  PRO A N   
216  C CA  . PRO A 35  ? 0.41003 0.37546 0.42926 -0.03192 0.05215  -0.06219 32  PRO A CA  
217  C C   . PRO A 35  ? 0.42663 0.41383 0.48102 -0.02617 0.05088  -0.05010 32  PRO A C   
218  O O   . PRO A 35  ? 0.42609 0.42330 0.49647 -0.02195 0.06721  -0.05007 32  PRO A O   
219  C CB  . PRO A 35  ? 0.37797 0.33028 0.40318 -0.02290 0.05809  -0.07146 32  PRO A CB  
220  C CG  . PRO A 35  ? 0.39351 0.32737 0.38957 -0.02907 0.04647  -0.07802 32  PRO A CG  
221  C CD  . PRO A 35  ? 0.35754 0.29790 0.34861 -0.03644 0.02630  -0.06829 32  PRO A CD  
222  N N   . ARG A 36  ? 0.36429 0.35904 0.43148 -0.02599 0.03225  -0.04000 33  ARG A N   
223  C CA  . ARG A 36  ? 0.37827 0.39331 0.47834 -0.02102 0.02927  -0.02795 33  ARG A CA  
224  C C   . ARG A 36  ? 0.38766 0.41520 0.48209 -0.03010 0.02057  -0.01802 33  ARG A C   
225  O O   . ARG A 36  ? 0.40468 0.44948 0.52456 -0.02731 0.01645  -0.00721 33  ARG A O   
226  C CB  . ARG A 36  ? 0.35826 0.37346 0.47979 -0.01368 0.01508  -0.02300 33  ARG A CB  
227  C CG  . ARG A 36  ? 0.35623 0.36294 0.49177 -0.00283 0.02438  -0.03047 33  ARG A CG  
228  C CD  . ARG A 36  ? 0.35049 0.37185 0.51744 0.00606  0.03897  -0.02733 33  ARG A CD  
229  N NE  . ARG A 36  ? 0.33062 0.34429 0.51339 0.01704  0.04658  -0.03350 33  ARG A NE  
230  C CZ  . ARG A 36  ? 0.31854 0.34352 0.53479 0.02710  0.05335  -0.02933 33  ARG A CZ  
231  N NH1 . ARG A 36  ? 0.34323 0.38823 0.58100 0.02747  0.05357  -0.01902 33  ARG A NH1 
232  N NH2 . ARG A 36  ? 0.28023 0.29635 0.50858 0.03674  0.05959  -0.03538 33  ARG A NH2 
233  N N   . GLU A 37  ? 0.38682 0.40575 0.44845 -0.04096 0.01745  -0.02132 34  GLU A N   
234  C CA  . GLU A 37  ? 0.39727 0.42579 0.45042 -0.05024 0.00747  -0.01217 34  GLU A CA  
235  C C   . GLU A 37  ? 0.39291 0.43326 0.44850 -0.05287 0.02358  -0.01054 34  GLU A C   
236  O O   . GLU A 37  ? 0.42017 0.45270 0.45991 -0.05473 0.03991  -0.01988 34  GLU A O   
237  C CB  . GLU A 37  ? 0.43264 0.44588 0.44929 -0.06078 -0.00357 -0.01648 34  GLU A CB  
238  C CG  . GLU A 37  ? 0.43922 0.46007 0.44568 -0.07045 -0.01715 -0.00698 34  GLU A CG  
239  C CD  . GLU A 37  ? 0.49586 0.50069 0.46596 -0.08063 -0.02704 -0.01209 34  GLU A CD  
240  O OE1 . GLU A 37  ? 0.52594 0.51662 0.47285 -0.08334 -0.01671 -0.02295 34  GLU A OE1 
241  O OE2 . GLU A 37  ? 0.49284 0.49901 0.45776 -0.08593 -0.04523 -0.00531 34  GLU A OE2 
242  N N   . HIS A 38  ? 0.33111 0.39013 0.40674 -0.05315 0.01930  0.00118  35  HIS A N   
243  C CA  . HIS A 38  ? 0.36025 0.43182 0.43881 -0.05652 0.03325  0.00376  35  HIS A CA  
244  C C   . HIS A 38  ? 0.39007 0.45098 0.43032 -0.06857 0.03687  -0.00171 35  HIS A C   
245  O O   . HIS A 38  ? 0.38431 0.43438 0.39958 -0.07607 0.02245  -0.00197 35  HIS A O   
246  C CB  . HIS A 38  ? 0.37285 0.46453 0.47387 -0.05709 0.02361  0.01799  35  HIS A CB  
247  C CG  . HIS A 38  ? 0.37915 0.48683 0.49307 -0.05781 0.03885  0.02145  35  HIS A CG  
248  N ND1 . HIS A 38  ? 0.40062 0.50784 0.49066 -0.06807 0.04614  0.02009  35  HIS A ND1 
249  C CD2 . HIS A 38  ? 0.36792 0.49263 0.51651 -0.04978 0.04785  0.02637  35  HIS A CD2 
250  C CE1 . HIS A 38  ? 0.39639 0.51972 0.50575 -0.06643 0.05957  0.02371  35  HIS A CE1 
251  N NE2 . HIS A 38  ? 0.38027 0.51483 0.52585 -0.05526 0.06077  0.02758  35  HIS A NE2 
252  N N   . GLU A 39  ? 0.44210 0.50569 0.47781 -0.07050 0.05646  -0.00631 36  GLU A N   
253  C CA  . GLU A 39  ? 0.54165 0.59424 0.54020 -0.08214 0.06186  -0.01203 36  GLU A CA  
254  C C   . GLU A 39  ? 0.51008 0.56669 0.49295 -0.09278 0.04583  -0.00282 36  GLU A C   
255  O O   . GLU A 39  ? 0.51250 0.55494 0.46184 -0.10214 0.03850  -0.00638 36  GLU A O   
256  C CB  . GLU A 39  ? 0.66560 0.72352 0.66636 -0.08247 0.08578  -0.01677 36  GLU A CB  
257  C CG  . GLU A 39  ? 0.84431 0.89043 0.80631 -0.09484 0.09312  -0.02289 36  GLU A CG  
258  C CD  . GLU A 39  ? 1.01726 1.06905 0.98261 -0.09535 0.11749  -0.02755 36  GLU A CD  
259  O OE1 . GLU A 39  ? 1.05427 1.12135 1.05409 -0.08624 0.12764  -0.02484 36  GLU A OE1 
260  O OE2 . GLU A 39  ? 1.09952 1.14024 1.03314 -0.10501 0.12650  -0.03399 36  GLU A OE2 
261  N N   . GLN A 40  ? 0.47636 0.55192 0.48312 -0.09156 0.03985  0.00915  37  GLN A N   
262  C CA  . GLN A 40  ? 0.50097 0.58092 0.49429 -0.10141 0.02473  0.01838  37  GLN A CA  
263  C C   . GLN A 40  ? 0.47951 0.55140 0.46572 -0.10252 0.00177  0.02144  37  GLN A C   
264  O O   . GLN A 40  ? 0.46464 0.53212 0.42836 -0.11215 -0.01118 0.02508  37  GLN A O   
265  C CB  . GLN A 40  ? 0.52160 0.62425 0.54304 -0.09978 0.02553  0.03018  37  GLN A CB  
266  C CG  . GLN A 40  ? 0.52982 0.64149 0.55755 -0.10008 0.04787  0.02767  37  GLN A CG  
267  C CD  . GLN A 40  ? 0.58599 0.68493 0.57578 -0.11129 0.05702  0.02037  37  GLN A CD  
268  O OE1 . GLN A 40  ? 0.59195 0.68525 0.55589 -0.12167 0.04516  0.02377  37  GLN A OE1 
269  N NE2 . GLN A 40  ? 0.62602 0.71959 0.61177 -0.10937 0.07806  0.01016  37  GLN A NE2 
270  N N   . LEU A 41  ? 0.46121 0.53082 0.46626 -0.09299 -0.00355 0.01997  38  LEU A N   
271  C CA  . LEU A 41  ? 0.44447 0.50406 0.44064 -0.09425 -0.02373 0.02082  38  LEU A CA  
272  C C   . LEU A 41  ? 0.48544 0.52365 0.44567 -0.10051 -0.02442 0.00988  38  LEU A C   
273  O O   . LEU A 41  ? 0.46186 0.49179 0.40275 -0.10732 -0.04084 0.01123  38  LEU A O   
274  C CB  . LEU A 41  ? 0.40359 0.46530 0.42834 -0.08273 -0.02816 0.02156  38  LEU A CB  
275  C CG  . LEU A 41  ? 0.41396 0.49439 0.47168 -0.07788 -0.03642 0.03429  38  LEU A CG  
276  C CD1 . LEU A 41  ? 0.37420 0.45535 0.45973 -0.06587 -0.03642 0.03335  38  LEU A CD1 
277  C CD2 . LEU A 41  ? 0.39950 0.48127 0.44879 -0.08511 -0.05772 0.04298  38  LEU A CD2 
278  N N   . LYS A 42  ? 0.51135 0.54032 0.46260 -0.09832 -0.00681 -0.00109 39  LYS A N   
279  C CA  . LYS A 42  ? 0.51176 0.52018 0.42785 -0.10472 -0.00606 -0.01184 39  LYS A CA  
280  C C   . LYS A 42  ? 0.53754 0.54253 0.42317 -0.11783 -0.00999 -0.00976 39  LYS A C   
281  O O   . LYS A 42  ? 0.52845 0.52036 0.38829 -0.12500 -0.02318 -0.01198 39  LYS A O   
282  C CB  . LYS A 42  ? 0.56960 0.57011 0.48340 -0.09993 0.01543  -0.02349 39  LYS A CB  
283  C CG  . LYS A 42  ? 0.63671 0.61552 0.51401 -0.10643 0.01832  -0.03530 39  LYS A CG  
284  C CD  . LYS A 42  ? 0.70710 0.67903 0.58527 -0.10086 0.04038  -0.04649 39  LYS A CD  
285  C CE  . LYS A 42  ? 0.77526 0.73867 0.62313 -0.11027 0.05460  -0.05311 39  LYS A CE  
286  N NZ  . LYS A 42  ? 0.79736 0.74027 0.60719 -0.11924 0.04631  -0.06029 39  LYS A NZ  
287  N N   . GLY A 43  ? 0.57517 0.59179 0.46369 -0.12126 0.00104  -0.00535 40  GLY A N   
288  C CA  . GLY A 43  ? 0.60369 0.61715 0.46338 -0.13396 -0.00241 -0.00282 40  GLY A CA  
289  C C   . GLY A 43  ? 0.62242 0.63951 0.47933 -0.13918 -0.02546 0.00727  40  GLY A C   
290  O O   . GLY A 43  ? 0.68087 0.68665 0.50776 -0.14903 -0.03563 0.00643  40  GLY A O   
291  N N   . LEU A 44  ? 0.55621 0.58877 0.44437 -0.13276 -0.03415 0.01697  41  LEU A N   
292  C CA  . LEU A 44  ? 0.55333 0.58956 0.44095 -0.13717 -0.05600 0.02660  41  LEU A CA  
293  C C   . LEU A 44  ? 0.56271 0.58276 0.43484 -0.13829 -0.07155 0.02157  41  LEU A C   
294  O O   . LEU A 44  ? 0.58098 0.59534 0.43386 -0.14652 -0.08709 0.02475  41  LEU A O   
295  C CB  . LEU A 44  ? 0.52603 0.58134 0.45112 -0.12954 -0.06116 0.03734  41  LEU A CB  
296  C CG  . LEU A 44  ? 0.53079 0.59416 0.46004 -0.13407 -0.08116 0.04923  41  LEU A CG  
297  C CD1 . LEU A 44  ? 0.53594 0.62069 0.49857 -0.12889 -0.07871 0.05991  41  LEU A CD1 
298  C CD2 . LEU A 44  ? 0.53457 0.58876 0.46464 -0.13138 -0.09911 0.04883  41  LEU A CD2 
299  N N   . ARG A 45  ? 0.54398 0.55636 0.42458 -0.13013 -0.06769 0.01365  42  ARG A N   
300  C CA  . ARG A 45  ? 0.54639 0.54344 0.41331 -0.13101 -0.08171 0.00826  42  ARG A CA  
301  C C   . ARG A 45  ? 0.62563 0.60522 0.45346 -0.14097 -0.08189 0.00029  42  ARG A C   
302  O O   . ARG A 45  ? 0.65427 0.62548 0.48293 -0.13422 -0.08728 0.00302  42  ARG A O   
303  C CB  . ARG A 45  ? 0.51807 0.51018 0.40168 -0.12030 -0.07586 0.00101  42  ARG A CB  
304  C CG  . ARG A 45  ? 0.51542 0.48976 0.38221 -0.12147 -0.08704 -0.00688 42  ARG A CG  
305  C CD  . ARG A 45  ? 0.49489 0.46528 0.38060 -0.11061 -0.08250 -0.01285 42  ARG A CD  
306  N NE  . ARG A 45  ? 0.49201 0.46223 0.38320 -0.10493 -0.06073 -0.01963 42  ARG A NE  
307  C CZ  . ARG A 45  ? 0.53801 0.49383 0.40572 -0.10755 -0.04910 -0.03088 42  ARG A CZ  
308  N NH1 . ARG A 45  ? 0.56660 0.50710 0.40359 -0.11584 -0.05770 -0.03639 42  ARG A NH1 
309  N NH2 . ARG A 45  ? 0.50860 0.46513 0.38366 -0.10197 -0.02897 -0.03668 42  ARG A NH2 
310  N N   . GLU A 46  ? 0.66737 0.64207 0.48058 -0.14326 -0.06357 -0.00665 43  GLU A N   
311  C CA  . GLU A 46  ? 0.75863 0.71520 0.53376 -0.15261 -0.06262 -0.01505 43  GLU A CA  
312  C C   . GLU A 46  ? 0.77577 0.73288 0.53868 -0.15925 -0.07113 -0.00672 43  GLU A C   
313  O O   . GLU A 46  ? 0.75191 0.69799 0.51253 -0.15415 -0.07329 -0.00659 43  GLU A O   
314  C CB  . GLU A 46  ? 0.82538 0.77715 0.59094 -0.15238 -0.03905 -0.02384 43  GLU A CB  
315  C CG  . GLU A 46  ? 0.85671 0.80260 0.63500 -0.14227 -0.02796 -0.03329 43  GLU A CG  
316  C CD  . GLU A 46  ? 0.94068 0.88237 0.71109 -0.14181 -0.00395 -0.04190 43  GLU A CD  
317  O OE1 . GLU A 46  ? 0.98028 0.92746 0.74224 -0.14790 0.00560  -0.03923 43  GLU A OE1 
318  O OE2 . GLU A 46  ? 0.95472 0.88729 0.72725 -0.13553 0.00564  -0.05150 43  GLU A OE2 
319  N N   A VAL A 47  ? 0.77298 0.74499 0.53978 -0.16516 -0.07216 0.00196  44  VAL A N   
320  N N   B VAL A 47  ? 0.76978 0.74156 0.53542 -0.16558 -0.07175 0.00162  44  VAL A N   
321  C CA  A VAL A 47  ? 0.77754 0.74969 0.54552 -0.16542 -0.07545 0.01102  44  VAL A CA  
322  C CA  B VAL A 47  ? 0.77543 0.74812 0.54389 -0.16545 -0.07551 0.01119  44  VAL A CA  
323  C C   A VAL A 47  ? 0.74263 0.71576 0.54107 -0.15118 -0.08434 0.01914  44  VAL A C   
324  C C   B VAL A 47  ? 0.74653 0.71855 0.54431 -0.15082 -0.08422 0.01831  44  VAL A C   
325  O O   A VAL A 47  ? 0.75123 0.71793 0.55028 -0.14831 -0.08590 0.02215  44  VAL A O   
326  O O   B VAL A 47  ? 0.75772 0.72145 0.55484 -0.14728 -0.08561 0.01985  44  VAL A O   
327  C CB  A VAL A 47  ? 0.79116 0.77870 0.55343 -0.17577 -0.07222 0.01760  44  VAL A CB  
328  C CB  B VAL A 47  ? 0.78642 0.77637 0.55430 -0.17434 -0.07373 0.01898  44  VAL A CB  
329  C CG1 A VAL A 47  ? 0.82906 0.81362 0.57264 -0.18101 -0.05179 0.00934  44  VAL A CG1 
330  C CG1 B VAL A 47  ? 0.78840 0.77778 0.56177 -0.17388 -0.07754 0.02796  44  VAL A CG1 
331  C CG2 A VAL A 47  ? 0.76335 0.77117 0.55746 -0.17034 -0.07674 0.02598  44  VAL A CG2 
332  C CG2 B VAL A 47  ? 0.82356 0.81333 0.57671 -0.17902 -0.05302 0.01202  44  VAL A CG2 
333  N N   . THR A 48  ? 0.68946 0.67005 0.51273 -0.14190 -0.08830 0.02166  45  THR A N   
334  C CA  . THR A 48  ? 0.68336 0.66319 0.53200 -0.12768 -0.09178 0.02700  45  THR A CA  
335  C C   . THR A 48  ? 0.72008 0.68737 0.56772 -0.11938 -0.09140 0.02046  45  THR A C   
336  O O   . THR A 48  ? 0.70500 0.66807 0.56110 -0.11335 -0.09195 0.02383  45  THR A O   
337  C CB  . THR A 48  ? 0.61791 0.60861 0.49209 -0.12004 -0.09397 0.03128  45  THR A CB  
338  O OG1 . THR A 48  ? 0.61182 0.61746 0.49031 -0.12744 -0.09457 0.03871  45  THR A OG1 
339  C CG2 . THR A 48  ? 0.59304 0.58078 0.48828 -0.10608 -0.09325 0.03452  45  THR A CG2 
340  N N   A GLU A 49  ? 0.74627 0.70697 0.58199 -0.12123 -0.09002 0.01158  46  GLU A N   
341  N N   B GLU A 49  ? 0.74615 0.70675 0.58189 -0.12115 -0.09003 0.01158  46  GLU A N   
342  C CA  A GLU A 49  ? 0.74577 0.69635 0.58005 -0.11425 -0.08940 0.00537  46  GLU A CA  
343  C CA  B GLU A 49  ? 0.74403 0.69492 0.57977 -0.11357 -0.08955 0.00584  46  GLU A CA  
344  C C   A GLU A 49  ? 0.77753 0.72092 0.59930 -0.11694 -0.08874 0.00576  46  GLU A C   
345  C C   B GLU A 49  ? 0.77700 0.72047 0.59920 -0.11674 -0.08880 0.00593  46  GLU A C   
346  O O   A GLU A 49  ? 0.78060 0.71460 0.60216 -0.11487 -0.09064 0.00657  46  GLU A O   
347  O O   B GLU A 49  ? 0.78072 0.71448 0.60213 -0.11507 -0.09075 0.00689  46  GLU A O   
348  C CB  A GLU A 49  ? 0.74341 0.68642 0.56297 -0.11792 -0.08656 -0.00509 46  GLU A CB  
349  C CB  B GLU A 49  ? 0.73879 0.68249 0.56261 -0.11571 -0.08718 -0.00442 46  GLU A CB  
350  C CG  A GLU A 49  ? 0.71216 0.65998 0.54848 -0.11228 -0.08802 -0.00714 46  GLU A CG  
351  C CG  B GLU A 49  ? 0.70790 0.65738 0.54936 -0.11017 -0.08879 -0.00560 46  GLU A CG  
352  C CD  A GLU A 49  ? 0.70687 0.64554 0.52577 -0.11853 -0.08315 -0.01900 46  GLU A CD  
353  C CD  B GLU A 49  ? 0.67573 0.62678 0.54018 -0.09587 -0.09013 -0.00470 46  GLU A CD  
354  O OE1 A GLU A 49  ? 0.71591 0.64624 0.50725 -0.12907 -0.07626 -0.02543 46  GLU A OE1 
355  O OE1 B GLU A 49  ? 0.65070 0.60266 0.52569 -0.09122 -0.09048 -0.00827 46  GLU A OE1 
356  O OE2 A GLU A 49  ? 0.64435 0.58280 0.47648 -0.11274 -0.08419 -0.02287 46  GLU A OE2 
357  O OE2 B GLU A 49  ? 0.66601 0.61368 0.53327 -0.09329 -0.09101 0.00100  46  GLU A OE2 
358  N N   . LYS A 50  ? 0.80180 0.86470 0.88637 -0.06976 -0.07834 0.08584  47  LYS A N   
359  C CA  . LYS A 50  ? 0.82336 0.89017 0.91662 -0.07157 -0.08582 0.09564  47  LYS A CA  
360  C C   . LYS A 50  ? 0.77805 0.84088 0.89036 -0.06228 -0.09398 0.09525  47  LYS A C   
361  O O   . LYS A 50  ? 0.79268 0.85995 0.91431 -0.06195 -0.10051 0.10261  47  LYS A O   
362  C CB  . LYS A 50  ? 0.87673 0.93780 0.96392 -0.08079 -0.08717 0.10550  47  LYS A CB  
363  C CG  . LYS A 50  ? 0.92565 0.98950 0.99424 -0.09085 -0.07899 0.10676  47  LYS A CG  
364  C CD  . LYS A 50  ? 0.97551 1.03397 1.03971 -0.09995 -0.08108 0.11701  47  LYS A CD  
365  C CE  . LYS A 50  ? 0.98758 1.04560 1.03387 -0.10952 -0.07222 0.11718  47  LYS A CE  
366  N NZ  . LYS A 50  ? 0.99114 1.06169 1.02684 -0.11419 -0.06653 0.11629  47  LYS A NZ  
367  N N   . HIS A 51  ? 0.73476 0.78938 0.85309 -0.05493 -0.09371 0.08705  48  HIS A N   
368  C CA  . HIS A 51  ? 0.67141 0.72105 0.80771 -0.04622 -0.10074 0.08598  48  HIS A CA  
369  C C   . HIS A 51  ? 0.65748 0.71710 0.80273 -0.03918 -0.10181 0.08132  48  HIS A C   
370  O O   . HIS A 51  ? 0.64653 0.71493 0.78374 -0.03948 -0.09609 0.07565  48  HIS A O   
371  C CB  . HIS A 51  ? 0.66310 0.70079 0.80198 -0.04141 -0.09961 0.07830  48  HIS A CB  
372  C CG  . HIS A 51  ? 0.68440 0.71411 0.84070 -0.03438 -0.10684 0.07879  48  HIS A CG  
373  N ND1 . HIS A 51  ? 0.69680 0.72788 0.86564 -0.02504 -0.10870 0.07173  48  HIS A ND1 
374  C CD2 . HIS A 51  ? 0.69503 0.71492 0.85826 -0.03549 -0.11233 0.08531  48  HIS A CD2 
375  C CE1 . HIS A 51  ? 0.69882 0.72116 0.88170 -0.02064 -0.11490 0.07391  48  HIS A CE1 
376  N NE2 . HIS A 51  ? 0.69716 0.71256 0.87686 -0.02681 -0.11727 0.08217  48  HIS A NE2 
377  N N   . GLU A 52  ? 0.66593 0.72393 0.82837 -0.03275 -0.10910 0.08376  49  GLU A N   
378  C CA  . GLU A 52  ? 0.66402 0.73145 0.83714 -0.02583 -0.11081 0.08023  49  GLU A CA  
379  C C   . GLU A 52  ? 0.63802 0.70522 0.81122 -0.01902 -0.10574 0.06690  49  GLU A C   
380  O O   . GLU A 52  ? 0.63709 0.71458 0.81128 -0.01602 -0.10345 0.06214  49  GLU A O   
381  C CB  . GLU A 52  ? 0.74894 0.81311 0.94125 -0.02009 -0.11954 0.08581  49  GLU A CB  
382  C CG  . GLU A 52  ? 0.84408 0.89292 1.04341 -0.01734 -0.12266 0.08544  49  GLU A CG  
383  C CD  . GLU A 52  ? 0.90263 0.94781 1.12173 -0.01065 -0.13058 0.08969  49  GLU A CD  
384  O OE1 . GLU A 52  ? 0.90953 0.96194 1.13969 -0.00402 -0.13213 0.08676  49  GLU A OE1 
385  O OE2 . GLU A 52  ? 0.91492 0.94990 1.13866 -0.01205 -0.13508 0.09599  49  GLU A OE2 
386  N N   . TRP A 53  ? 0.60159 0.65750 0.77365 -0.01673 -0.10392 0.06073  50  TRP A N   
387  C CA  . TRP A 53  ? 0.59679 0.65147 0.76871 -0.01050 -0.09940 0.04813  50  TRP A CA  
388  C C   . TRP A 53  ? 0.55992 0.61559 0.71339 -0.01526 -0.09107 0.04273  50  TRP A C   
389  O O   . TRP A 53  ? 0.55715 0.60798 0.70829 -0.01150 -0.08747 0.03332  50  TRP A O   
390  C CB  . TRP A 53  ? 0.65493 0.69707 0.83811 -0.00440 -0.10273 0.04394  50  TRP A CB  
391  C CG  . TRP A 53  ? 0.75095 0.79343 0.95325 0.00347  -0.10855 0.04372  50  TRP A CG  
392  C CD1 . TRP A 53  ? 0.79411 0.83067 1.00982 0.00517  -0.11573 0.05120  50  TRP A CD1 
393  C CD2 . TRP A 53  ? 0.80829 0.85738 1.01874 0.01075  -0.10740 0.03568  50  TRP A CD2 
394  N NE1 . TRP A 53  ? 0.82965 0.86858 1.06178 0.01330  -0.11907 0.04840  50  TRP A NE1 
395  C CE2 . TRP A 53  ? 0.83603 0.88277 1.06540 0.01680  -0.11404 0.03877  50  TRP A CE2 
396  C CE3 . TRP A 53  ? 0.83996 0.89650 1.04358 0.01269  -0.10122 0.02613  50  TRP A CE3 
397  C CZ2 . TRP A 53  ? 0.85511 0.90685 1.09712 0.02472  -0.11455 0.03252  50  TRP A CZ2 
398  C CZ3 . TRP A 53  ? 0.85628 0.91781 1.07200 0.02032  -0.10184 0.01982  50  TRP A CZ3 
399  C CH2 . TRP A 53  ? 0.85853 0.91774 1.09346 0.02626  -0.10840 0.02298  50  TRP A CH2 
400  N N   . SER A 54  ? 0.54401 0.60593 0.68435 -0.02352 -0.08782 0.04853  51  SER A N   
401  C CA  . SER A 54  ? 0.56669 0.62929 0.68935 -0.02845 -0.07955 0.04423  51  SER A CA  
402  C C   . SER A 54  ? 0.62474 0.69299 0.74381 -0.02365 -0.07387 0.03307  51  SER A C   
403  O O   . SER A 54  ? 0.65365 0.72071 0.75941 -0.02600 -0.06698 0.02788  51  SER A O   
404  C CB  . SER A 54  ? 0.54996 0.61956 0.66040 -0.03807 -0.07699 0.05243  51  SER A CB  
405  O OG  . SER A 54  ? 0.56120 0.64321 0.67475 -0.03782 -0.07802 0.05432  51  SER A OG  
406  N N   . THR A 55  ? 0.62584 0.70013 0.75656 -0.01702 -0.07647 0.02937  52  THR A N   
407  C CA  . THR A 55  ? 0.58577 0.66553 0.71347 -0.01249 -0.07111 0.01857  52  THR A CA  
408  C C   . THR A 55  ? 0.54003 0.61038 0.66630 -0.00809 -0.06849 0.00921  52  THR A C   
409  O O   . THR A 55  ? 0.51727 0.58979 0.63318 -0.00770 -0.06184 0.00126  52  THR A O   
410  C CB  . THR A 55  ? 0.60000 0.68737 0.74250 -0.00596 -0.07500 0.01672  52  THR A CB  
411  O OG1 . THR A 55  ? 0.66726 0.75927 0.80707 -0.00148 -0.06967 0.00562  52  THR A OG1 
412  C CG2 . THR A 55  ? 0.59586 0.67513 0.75651 0.00048  -0.08245 0.01782  52  THR A CG2 
413  N N   . ALA A 56  ? 0.51936 0.57921 0.65555 -0.00501 -0.07357 0.01011  53  ALA A N   
414  C CA  . ALA A 56  ? 0.47382 0.52496 0.61006 -0.00072 -0.07186 0.00130  53  ALA A CA  
415  C C   . ALA A 56  ? 0.45684 0.50222 0.57831 -0.00625 -0.06728 0.00157  53  ALA A C   
416  O O   . ALA A 56  ? 0.42450 0.46349 0.54408 -0.00339 -0.06533 -0.00566 53  ALA A O   
417  C CB  . ALA A 56  ? 0.45820 0.50039 0.61109 0.00456  -0.07888 0.00188  53  ALA A CB  
418  N N   . LEU A 57  ? 0.47726 0.52500 0.58845 -0.01414 -0.06544 0.00965  54  LEU A N   
419  C CA  . LEU A 57  ? 0.44643 0.48859 0.54444 -0.01973 -0.06112 0.01089  54  LEU A CA  
420  C C   . LEU A 57  ? 0.40915 0.45352 0.49492 -0.01881 -0.05331 0.00185  54  LEU A C   
421  O O   . LEU A 57  ? 0.39875 0.45200 0.47874 -0.01886 -0.04900 -0.00131 54  LEU A O   
422  C CB  . LEU A 57  ? 0.46144 0.50700 0.55097 -0.02860 -0.06011 0.02110  54  LEU A CB  
423  C CG  . LEU A 57  ? 0.47701 0.51807 0.55242 -0.03582 -0.05513 0.02417  54  LEU A CG  
424  C CD1 . LEU A 57  ? 0.46247 0.49181 0.54294 -0.03528 -0.05876 0.02558  54  LEU A CD1 
425  C CD2 . LEU A 57  ? 0.46734 0.51368 0.53543 -0.04444 -0.05407 0.03376  54  LEU A CD2 
426  N N   . VAL A 58  ? 0.40941 0.44582 0.49130 -0.01801 -0.05154 -0.00222 55  VAL A N   
427  C CA  . VAL A 58  ? 0.41309 0.45088 0.48250 -0.01752 -0.04413 -0.01000 55  VAL A CA  
428  C C   . VAL A 58  ? 0.42842 0.47093 0.48226 -0.02513 -0.03757 -0.00546 55  VAL A C   
429  O O   . VAL A 58  ? 0.43892 0.47784 0.48873 -0.03124 -0.03779 0.00225  55  VAL A O   
430  C CB  . VAL A 58  ? 0.38302 0.41140 0.45208 -0.01548 -0.04427 -0.01420 55  VAL A CB  
431  C CG1 . VAL A 58  ? 0.35883 0.38806 0.41231 -0.01741 -0.03629 -0.01877 55  VAL A CG1 
432  C CG2 . VAL A 58  ? 0.37460 0.39992 0.45626 -0.00750 -0.04844 -0.02192 55  VAL A CG2 
433  N N   . PRO A 59  ? 0.40873 0.45902 0.45351 -0.02534 -0.03144 -0.00993 56  PRO A N   
434  C CA  . PRO A 59  ? 0.40438 0.45931 0.43445 -0.03287 -0.02478 -0.00569 56  PRO A CA  
435  C C   . PRO A 59  ? 0.41803 0.46696 0.43598 -0.03609 -0.01910 -0.00634 56  PRO A C   
436  O O   . PRO A 59  ? 0.45075 0.49377 0.46963 -0.03190 -0.01910 -0.01190 56  PRO A O   
437  C CB  . PRO A 59  ? 0.36560 0.43006 0.39088 -0.03096 -0.02004 -0.01181 56  PRO A CB  
438  C CG  . PRO A 59  ? 0.39794 0.46053 0.43123 -0.02243 -0.02200 -0.02128 56  PRO A CG  
439  C CD  . PRO A 59  ? 0.36155 0.41713 0.41010 -0.01889 -0.03052 -0.01885 56  PRO A CD  
440  N N   . ALA A 60  ? 0.39323 0.44417 0.39962 -0.04383 -0.01398 -0.00050 57  ALA A N   
441  C CA  . ALA A 60  ? 0.43846 0.48332 0.43456 -0.04790 -0.00900 0.00105  57  ALA A CA  
442  C C   . ALA A 60  ? 0.46155 0.50623 0.44829 -0.04472 -0.00227 -0.00732 57  ALA A C   
443  O O   . ALA A 60  ? 0.46793 0.50602 0.45166 -0.04404 -0.00077 -0.00878 57  ALA A O   
444  C CB  . ALA A 60  ? 0.41030 0.45777 0.39623 -0.05717 -0.00447 0.00893  57  ALA A CB  
445  N N   . ASP A 61  ? 0.41856 0.47059 0.40033 -0.04294 0.00197  -0.01272 58  ASP A N   
446  C CA  . ASP A 61  ? 0.39698 0.44877 0.36925 -0.04004 0.00851  -0.02056 58  ASP A CA  
447  C C   . ASP A 61  ? 0.38866 0.43585 0.36944 -0.03220 0.00413  -0.02771 58  ASP A C   
448  O O   . ASP A 61  ? 0.35250 0.39520 0.32758 -0.03052 0.00717  -0.03152 58  ASP A O   
449  C CB  . ASP A 61  ? 0.42511 0.48580 0.38982 -0.04035 0.01425  -0.02470 58  ASP A CB  
450  C CG  . ASP A 61  ? 0.52122 0.58751 0.49730 -0.03501 0.00906  -0.02874 58  ASP A CG  
451  O OD1 . ASP A 61  ? 0.52253 0.58809 0.51155 -0.03390 0.00129  -0.02465 58  ASP A OD1 
452  O OD2 . ASP A 61  ? 0.48722 0.55858 0.45940 -0.03192 0.01295  -0.03599 58  ASP A OD2 
453  N N   . GLU A 62  ? 0.34074 0.38888 0.33540 -0.02748 -0.00306 -0.02941 59  GLU A N   
454  C CA  . GLU A 62  ? 0.35841 0.40152 0.36204 -0.02059 -0.00753 -0.03591 59  GLU A CA  
455  C C   . GLU A 62  ? 0.38080 0.41496 0.38745 -0.02160 -0.01082 -0.03237 59  GLU A C   
456  O O   . GLU A 62  ? 0.36377 0.39325 0.37093 -0.01782 -0.01122 -0.03785 59  GLU A O   
457  C CB  . GLU A 62  ? 0.33720 0.38273 0.35587 -0.01571 -0.01431 -0.03780 59  GLU A CB  
458  C CG  . GLU A 62  ? 0.37629 0.41633 0.40467 -0.00888 -0.01873 -0.04483 59  GLU A CG  
459  C CD  . GLU A 62  ? 0.45603 0.49768 0.50022 -0.00400 -0.02522 -0.04645 59  GLU A CD  
460  O OE1 . GLU A 62  ? 0.45742 0.50650 0.50374 -0.00445 -0.02509 -0.04487 59  GLU A OE1 
461  O OE2 . GLU A 62  ? 0.48467 0.52021 0.53938 0.00026  -0.03034 -0.04933 59  GLU A OE2 
462  N N   . GLY A 63  ? 0.36644 0.39833 0.37482 -0.02697 -0.01313 -0.02328 60  GLY A N   
463  C CA  . GLY A 63  ? 0.38089 0.40441 0.39217 -0.02842 -0.01609 -0.01967 60  GLY A CA  
464  C C   . GLY A 63  ? 0.41098 0.43153 0.41068 -0.02978 -0.00996 -0.02175 60  GLY A C   
465  O O   . GLY A 63  ? 0.43031 0.44515 0.43306 -0.02701 -0.01208 -0.02463 60  GLY A O   
466  N N   . LEU A 64  ? 0.41714 0.44170 0.40350 -0.03412 -0.00217 -0.02029 61  LEU A N   
467  C CA  . LEU A 64  ? 0.39032 0.41248 0.36538 -0.03511 0.00432  -0.02220 61  LEU A CA  
468  C C   . LEU A 64  ? 0.39679 0.41916 0.37083 -0.02847 0.00524  -0.03176 61  LEU A C   
469  O O   . LEU A 64  ? 0.44328 0.46172 0.41321 -0.02736 0.00712  -0.03383 61  LEU A O   
470  C CB  . LEU A 64  ? 0.37176 0.39829 0.33297 -0.04090 0.01295  -0.01915 61  LEU A CB  
471  C CG  . LEU A 64  ? 0.42751 0.45258 0.38642 -0.04875 0.01388  -0.00958 61  LEU A CG  
472  C CD1 . LEU A 64  ? 0.46099 0.49109 0.40625 -0.05428 0.02280  -0.00775 61  LEU A CD1 
473  C CD2 . LEU A 64  ? 0.36126 0.37868 0.32064 -0.05052 0.01331  -0.00619 61  LEU A CD2 
474  N N   . PHE A 65  ? 0.36858 0.39574 0.34623 -0.02415 0.00403  -0.03762 62  PHE A N   
475  C CA  . PHE A 65  ? 0.36195 0.38920 0.33932 -0.01793 0.00445  -0.04707 62  PHE A CA  
476  C C   . PHE A 65  ? 0.38420 0.40519 0.37250 -0.01392 -0.00247 -0.04951 62  PHE A C   
477  O O   . PHE A 65  ? 0.38649 0.40474 0.37147 -0.01128 -0.00138 -0.05435 62  PHE A O   
478  C CB  . PHE A 65  ? 0.40465 0.43843 0.38458 -0.01459 0.00454  -0.05256 62  PHE A CB  
479  C CG  . PHE A 65  ? 0.46050 0.49435 0.44145 -0.00826 0.00442  -0.06258 62  PHE A CG  
480  C CD1 . PHE A 65  ? 0.53602 0.56923 0.50547 -0.00744 0.01012  -0.06707 62  PHE A CD1 
481  C CD2 . PHE A 65  ? 0.53014 0.56467 0.52352 -0.00323 -0.00122 -0.06745 62  PHE A CD2 
482  C CE1 . PHE A 65  ? 0.61340 0.64674 0.58320 -0.00202 0.00998  -0.07628 62  PHE A CE1 
483  C CE2 . PHE A 65  ? 0.56900 0.60350 0.56307 0.00217  -0.00103 -0.07699 62  PHE A CE2 
484  C CZ  . PHE A 65  ? 0.61305 0.64703 0.59501 0.00261  0.00449  -0.08142 62  PHE A CZ  
485  N N   . LEU A 66  ? 0.36100 0.37972 0.36233 -0.01352 -0.00963 -0.04616 63  LEU A N   
486  C CA  . LEU A 66  ? 0.41280 0.42505 0.42478 -0.01035 -0.01611 -0.04800 63  LEU A CA  
487  C C   . LEU A 66  ? 0.38491 0.39172 0.39237 -0.01335 -0.01512 -0.04444 63  LEU A C   
488  O O   . LEU A 66  ? 0.36673 0.36982 0.37608 -0.01037 -0.01688 -0.04902 63  LEU A O   
489  C CB  . LEU A 66  ? 0.45006 0.46041 0.47613 -0.01018 -0.02339 -0.04365 63  LEU A CB  
490  C CG  . LEU A 66  ? 0.46481 0.48054 0.49792 -0.00705 -0.02535 -0.04615 63  LEU A CG  
491  C CD1 . LEU A 66  ? 0.45519 0.46809 0.50260 -0.00695 -0.03282 -0.04077 63  LEU A CD1 
492  C CD2 . LEU A 66  ? 0.32779 0.34478 0.36311 -0.00066 -0.02508 -0.05678 63  LEU A CD2 
493  N N   . SER A 67  ? 0.40413 0.41065 0.40571 -0.01944 -0.01222 -0.03636 64  SER A N   
494  C CA  . SER A 67  ? 0.43189 0.43356 0.42930 -0.02265 -0.01073 -0.03252 64  SER A CA  
495  C C   . SER A 67  ? 0.45278 0.45548 0.43931 -0.02101 -0.00479 -0.03748 64  SER A C   
496  O O   . SER A 67  ? 0.43827 0.43698 0.42509 -0.02021 -0.00573 -0.03836 64  SER A O   
497  C CB  . SER A 67  ? 0.42236 0.42401 0.41499 -0.02984 -0.00791 -0.02318 64  SER A CB  
498  O OG  . SER A 67  ? 0.44704 0.44442 0.43507 -0.03307 -0.00549 -0.01964 64  SER A OG  
499  N N   . MET A 68  ? 0.41706 0.42522 0.39387 -0.02057 0.00136  -0.04060 65  MET A N   
500  C CA  . MET A 68  ? 0.38346 0.39264 0.34945 -0.01883 0.00723  -0.04524 65  MET A CA  
501  C C   . MET A 68  ? 0.42313 0.43100 0.39390 -0.01270 0.00342  -0.05354 65  MET A C   
502  O O   . MET A 68  ? 0.48159 0.48752 0.44793 -0.01151 0.00488  -0.05558 65  MET A O   
503  C CB  . MET A 68  ? 0.40942 0.42455 0.36442 -0.01971 0.01451  -0.04709 65  MET A CB  
504  C CG  . MET A 68  ? 0.43370 0.44995 0.37702 -0.01765 0.02087  -0.05207 65  MET A CG  
505  S SD  . MET A 68  ? 0.49239 0.50507 0.42616 -0.02189 0.02669  -0.04594 65  MET A SD  
506  C CE  . MET A 68  ? 0.31414 0.32955 0.24008 -0.02901 0.03335  -0.03873 65  MET A CE  
507  N N   . LEU A 69  ? 0.39724 0.40631 0.37712 -0.00886 -0.00138 -0.05839 66  LEU A N   
508  C CA  . LEU A 69  ? 0.43534 0.44294 0.42033 -0.00341 -0.00504 -0.06663 66  LEU A CA  
509  C C   . LEU A 69  ? 0.43377 0.43538 0.42578 -0.00342 -0.01023 -0.06512 66  LEU A C   
510  O O   . LEU A 69  ? 0.38115 0.38148 0.37093 -0.00104 -0.01038 -0.06986 66  LEU A O   
511  C CB  . LEU A 69  ? 0.45226 0.46172 0.44729 0.00028  -0.00925 -0.07136 66  LEU A CB  
512  C CG  . LEU A 69  ? 0.53788 0.55376 0.52703 0.00191  -0.00463 -0.07604 66  LEU A CG  
513  C CD1 . LEU A 69  ? 0.54635 0.56380 0.54768 0.00531  -0.00942 -0.07947 66  LEU A CD1 
514  C CD2 . LEU A 69  ? 0.56798 0.58528 0.54762 0.00479  -0.00034 -0.08372 66  LEU A CD2 
515  N N   . LEU A 70  ? 0.43788 0.43595 0.43844 -0.00624 -0.01462 -0.05853 67  LEU A N   
516  C CA  . LEU A 70  ? 0.41000 0.40224 0.41771 -0.00674 -0.01957 -0.05675 67  LEU A CA  
517  C C   . LEU A 70  ? 0.43391 0.42524 0.43262 -0.00875 -0.01564 -0.05491 67  LEU A C   
518  O O   . LEU A 70  ? 0.47739 0.46644 0.47812 -0.00674 -0.01802 -0.05847 67  LEU A O   
519  C CB  . LEU A 70  ? 0.42154 0.41034 0.43782 -0.01037 -0.02373 -0.04885 67  LEU A CB  
520  C CG  . LEU A 70  ? 0.46100 0.44929 0.48941 -0.00793 -0.02938 -0.05004 67  LEU A CG  
521  C CD1 . LEU A 70  ? 0.49940 0.48614 0.53226 -0.01246 -0.03151 -0.04086 67  LEU A CD1 
522  C CD2 . LEU A 70  ? 0.42868 0.41218 0.46790 -0.00410 -0.03550 -0.05535 67  LEU A CD2 
523  N N   . LYS A 71  ? 0.36902 0.36232 0.35782 -0.01279 -0.00942 -0.04937 68  LYS A N   
524  C CA  . LYS A 71  ? 0.44708 0.43923 0.42824 -0.01490 -0.00545 -0.04661 68  LYS A CA  
525  C C   . LYS A 71  ? 0.47444 0.46933 0.44742 -0.01108 -0.00199 -0.05338 68  LYS A C   
526  O O   . LYS A 71  ? 0.51469 0.50800 0.48676 -0.01027 -0.00258 -0.05422 68  LYS A O   
527  C CB  . LYS A 71  ? 0.45730 0.45044 0.43030 -0.02044 0.00076  -0.03898 68  LYS A CB  
528  C CG  . LYS A 71  ? 0.53733 0.52746 0.51764 -0.02497 -0.00265 -0.03159 68  LYS A CG  
529  C CD  . LYS A 71  ? 0.57156 0.56136 0.54396 -0.03116 0.00340  -0.02387 68  LYS A CD  
530  C CE  . LYS A 71  ? 0.67345 0.65917 0.65355 -0.03585 -0.00068 -0.01657 68  LYS A CE  
531  N NZ  . LYS A 71  ? 0.72368 0.70829 0.69656 -0.04226 0.00519  -0.00923 68  LYS A NZ  
532  N N   . LEU A 72  ? 0.45622 0.45541 0.42323 -0.00878 0.00153  -0.05823 69  LEU A N   
533  C CA  . LEU A 72  ? 0.48831 0.49007 0.44657 -0.00540 0.00517  -0.06455 69  LEU A CA  
534  C C   . LEU A 72  ? 0.50819 0.50843 0.47316 -0.00115 -0.00067 -0.07144 69  LEU A C   
535  O O   . LEU A 72  ? 0.53423 0.53531 0.49322 0.00077  0.00096  -0.07487 69  LEU A O   
536  C CB  . LEU A 72  ? 0.46746 0.47395 0.41857 -0.00406 0.00995  -0.06861 69  LEU A CB  
537  C CG  . LEU A 72  ? 0.46746 0.47632 0.40813 -0.00817 0.01767  -0.06325 69  LEU A CG  
538  C CD1 . LEU A 72  ? 0.48240 0.49614 0.41779 -0.00673 0.02143  -0.06798 69  LEU A CD1 
539  C CD2 . LEU A 72  ? 0.43618 0.44440 0.36612 -0.00943 0.02364  -0.06081 69  LEU A CD2 
540  N N   . MET A 73  ? 0.49492 0.49297 0.47216 0.00026  -0.00733 -0.07352 70  MET A N   
541  C CA  . MET A 73  ? 0.54222 0.53831 0.52661 0.00373  -0.01291 -0.08006 70  MET A CA  
542  C C   . MET A 73  ? 0.50462 0.49604 0.49680 0.00186  -0.01787 -0.07616 70  MET A C   
543  O O   . MET A 73  ? 0.53920 0.52864 0.53789 0.00412  -0.02275 -0.08119 70  MET A O   
544  C CB  . MET A 73  ? 0.55801 0.55413 0.55161 0.00681  -0.01692 -0.08572 70  MET A CB  
545  C CG  . MET A 73  ? 0.57253 0.56507 0.57857 0.00524  -0.02215 -0.08093 70  MET A CG  
546  S SD  . MET A 73  ? 0.53682 0.52946 0.55432 0.00955  -0.02654 -0.08787 70  MET A SD  
547  C CE  . MET A 73  ? 0.51757 0.50811 0.53812 0.01328  -0.02987 -0.09748 70  MET A CE  
548  N N   . ASN A 74  ? 0.49424 0.66243 0.59699 0.10382  0.02000  -0.13278 71  ASN A N   
549  C CA  . ASN A 74  ? 0.50646 0.70261 0.61850 0.09616  0.01916  -0.12957 71  ASN A CA  
550  C C   . ASN A 74  ? 0.48755 0.67985 0.60941 0.08028  0.01681  -0.12620 71  ASN A C   
551  O O   . ASN A 74  ? 0.48125 0.68796 0.61041 0.07303  0.01432  -0.12689 71  ASN A O   
552  C CB  . ASN A 74  ? 0.55083 0.76689 0.66307 0.10180  0.01756  -0.13419 71  ASN A CB  
553  C CG  . ASN A 74  ? 0.62940 0.87721 0.74910 0.09768  0.01777  -0.13102 71  ASN A CG  
554  O OD1 . ASN A 74  ? 0.67161 0.92970 0.79212 0.09767  0.02045  -0.12647 71  ASN A OD1 
555  N ND2 . ASN A 74  ? 0.65833 0.92209 0.78354 0.09396  0.01496  -0.13347 71  ASN A ND2 
556  N N   . ALA A 75  ? 0.41345 0.58582 0.53539 0.07488  0.01770  -0.12254 72  ALA A N   
557  C CA  . ALA A 75  ? 0.40918 0.57647 0.54027 0.05991  0.01589  -0.11875 72  ALA A CA  
558  C C   . ALA A 75  ? 0.42042 0.61402 0.56012 0.05164  0.01628  -0.11350 72  ALA A C   
559  O O   . ALA A 75  ? 0.39293 0.60159 0.53099 0.05625  0.01883  -0.11066 72  ALA A O   
560  C CB  . ALA A 75  ? 0.40528 0.54628 0.53423 0.05691  0.01706  -0.11555 72  ALA A CB  
561  N N   . LYS A 76  ? 0.42285 0.62215 0.57174 0.03929  0.01382  -0.11241 73  LYS A N   
562  C CA  . LYS A 76  ? 0.41609 0.63887 0.57385 0.02977  0.01396  -0.10746 73  LYS A CA  
563  C C   . LYS A 76  ? 0.38544 0.59820 0.55099 0.01520  0.01325  -0.10230 73  LYS A C   
564  O O   . LYS A 76  ? 0.38948 0.61469 0.56003 0.00865  0.01454  -0.09646 73  LYS A O   
565  C CB  . LYS A 76  ? 0.40579 0.65203 0.56838 0.02818  0.01182  -0.11087 73  LYS A CB  
566  C CG  . LYS A 76  ? 0.43963 0.70085 0.59583 0.04199  0.01255  -0.11529 73  LYS A CG  
567  N N   . ARG A 77  ? 0.35861 0.54918 0.52532 0.00994  0.01132  -0.10425 74  ARG A N   
568  C CA  . ARG A 77  ? 0.49745 0.67639 0.67145 -0.00365 0.01069  -0.09954 74  ARG A CA  
569  C C   . ARG A 77  ? 0.45401 0.60089 0.62292 -0.00163 0.01102  -0.09984 74  ARG A C   
570  O O   . ARG A 77  ? 0.40248 0.53368 0.56641 0.00399  0.00982  -0.10553 74  ARG A O   
571  C CB  . ARG A 77  ? 0.53064 0.71527 0.71308 -0.01458 0.00790  -0.10140 74  ARG A CB  
572  C CG  . ARG A 77  ? 0.62602 0.80770 0.81760 -0.02954 0.00773  -0.09544 74  ARG A CG  
573  C CD  . ARG A 77  ? 0.74793 0.92852 0.94695 -0.04021 0.00513  -0.09789 74  ARG A CD  
574  N NE  . ARG A 77  ? 0.84506 1.02503 1.05309 -0.05460 0.00525  -0.09191 74  ARG A NE  
575  C CZ  . ARG A 77  ? 0.93047 1.10395 1.14562 -0.06596 0.00353  -0.09258 74  ARG A CZ  
576  N NH1 . ARG A 77  ? 0.96465 1.13779 1.18770 -0.07861 0.00395  -0.08676 74  ARG A NH1 
577  N NH2 . ARG A 77  ? 0.95664 1.12375 1.17094 -0.06475 0.00147  -0.09906 74  ARG A NH2 
578  N N   . THR A 78  ? 0.36242 0.49992 0.53249 -0.00607 0.01267  -0.09372 75  THR A N   
579  C CA  . THR A 78  ? 0.46011 0.56830 0.62526 -0.00383 0.01329  -0.09333 75  THR A CA  
580  C C   . THR A 78  ? 0.45869 0.55517 0.63145 -0.01720 0.01291  -0.08750 75  THR A C   
581  O O   . THR A 78  ? 0.42158 0.53363 0.60251 -0.02725 0.01277  -0.08288 75  THR A O   
582  C CB  . THR A 78  ? 0.41771 0.52324 0.57424 0.00709  0.01625  -0.09177 75  THR A CB  
583  O OG1 . THR A 78  ? 0.46001 0.57698 0.62060 0.00142  0.01804  -0.08443 75  THR A OG1 
584  C CG2 . THR A 78  ? 0.38859 0.50996 0.53837 0.01996  0.01709  -0.09660 75  THR A CG2 
585  N N   . ILE A 79  ? 0.42815 0.49668 0.59807 -0.01711 0.01281  -0.08778 76  ILE A N   
586  C CA  . ILE A 79  ? 0.48156 0.53527 0.65739 -0.02807 0.01279  -0.08202 76  ILE A CA  
587  C C   . ILE A 79  ? 0.44067 0.47433 0.60951 -0.02173 0.01470  -0.07990 76  ILE A C   
588  O O   . ILE A 79  ? 0.38014 0.40078 0.54030 -0.01102 0.01508  -0.08484 76  ILE A O   
589  C CB  . ILE A 79  ? 0.52856 0.56677 0.71001 -0.03695 0.01031  -0.08467 76  ILE A CB  
590  C CG1 . ILE A 79  ? 0.55546 0.57402 0.74177 -0.04658 0.01051  -0.07906 76  ILE A CG1 
591  C CG2 . ILE A 79  ? 0.51731 0.53963 0.69175 -0.02821 0.00916  -0.09259 76  ILE A CG2 
592  C CD1 . ILE A 79  ? 0.61593 0.62571 0.81048 -0.05832 0.00840  -0.08003 76  ILE A CD1 
593  N N   . GLU A 80  ? 0.47958 0.51152 0.65203 -0.02827 0.01596  -0.07252 77  GLU A N   
594  C CA  . GLU A 80  ? 0.51446 0.53024 0.68098 -0.02322 0.01795  -0.06948 77  GLU A CA  
595  C C   . GLU A 80  ? 0.52135 0.51806 0.69386 -0.03398 0.01736  -0.06435 77  GLU A C   
596  O O   . GLU A 80  ? 0.49127 0.49765 0.67194 -0.04472 0.01726  -0.05838 77  GLU A O   
597  C CB  . GLU A 80  ? 0.57766 0.61269 0.74180 -0.01926 0.02051  -0.06494 77  GLU A CB  
598  C CG  . GLU A 80  ? 0.68206 0.70315 0.83806 -0.01120 0.02288  -0.06323 77  GLU A CG  
599  C CD  . GLU A 80  ? 0.76685 0.79562 0.91304 0.00320  0.02465  -0.06809 77  GLU A CD  
600  O OE1 . GLU A 80  ? 0.76468 0.78282 0.90347 0.01069  0.02680  -0.06747 77  GLU A OE1 
601  O OE2 . GLU A 80  ? 0.80551 0.85106 0.95141 0.00701  0.02397  -0.07251 77  GLU A OE2 
602  N N   . ILE A 81  ? 0.50238 0.47212 0.67087 -0.03109 0.01704  -0.06664 78  ILE A N   
603  C CA  . ILE A 81  ? 0.51066 0.45955 0.68444 -0.04042 0.01640  -0.06248 78  ILE A CA  
604  C C   . ILE A 81  ? 0.47064 0.40583 0.63866 -0.03538 0.01844  -0.05867 78  ILE A C   
605  O O   . ILE A 81  ? 0.44503 0.36542 0.60440 -0.02532 0.01910  -0.06298 78  ILE A O   
606  C CB  . ILE A 81  ? 0.55276 0.48070 0.72744 -0.04226 0.01428  -0.06819 78  ILE A CB  
607  C CG1 . ILE A 81  ? 0.58918 0.53202 0.76967 -0.04761 0.01232  -0.07193 78  ILE A CG1 
608  C CG2 . ILE A 81  ? 0.52732 0.43285 0.70726 -0.05128 0.01385  -0.06383 78  ILE A CG2 
609  C CD1 . ILE A 81  ? 0.60803 0.53290 0.78847 -0.04816 0.01029  -0.07863 78  ILE A CD1 
610  N N   . GLY A 82  ? 0.45804 0.39815 0.63074 -0.04244 0.01946  -0.05060 79  GLY A N   
611  C CA  . GLY A 82  ? 0.42980 0.36090 0.59733 -0.03802 0.02154  -0.04633 79  GLY A CA  
612  C C   . GLY A 82  ? 0.43665 0.39041 0.59986 -0.03170 0.02380  -0.04436 79  GLY A C   
613  O O   . GLY A 82  ? 0.45527 0.41234 0.60994 -0.02003 0.02497  -0.04935 79  GLY A O   
614  N N   . VAL A 83  ? 0.43668 0.40612 0.60574 -0.03941 0.02453  -0.03713 80  VAL A N   
615  C CA  . VAL A 83  ? 0.41778 0.41194 0.58438 -0.03526 0.02657  -0.03499 80  VAL A CA  
616  C C   . VAL A 83  ? 0.45578 0.44527 0.61733 -0.03144 0.02905  -0.03001 80  VAL A C   
617  O O   . VAL A 83  ? 0.44811 0.44620 0.60207 -0.02145 0.03119  -0.03186 80  VAL A O   
618  C CB  . VAL A 83  ? 0.40909 0.42602 0.58519 -0.04613 0.02590  -0.03053 80  VAL A CB  
619  C CG1 . VAL A 83  ? 0.36674 0.40898 0.54065 -0.04242 0.02814  -0.02783 80  VAL A CG1 
620  C CG2 . VAL A 83  ? 0.41433 0.43797 0.59474 -0.04900 0.02363  -0.03607 80  VAL A CG2 
621  N N   . TYR A 84  ? 0.45264 0.42882 0.61840 -0.03941 0.02887  -0.02361 81  TYR A N   
622  C CA  . TYR A 84  ? 0.46788 0.43988 0.62997 -0.03755 0.03106  -0.01786 81  TYR A CA  
623  C C   . TYR A 84  ? 0.47236 0.47251 0.63508 -0.03783 0.03292  -0.01399 81  TYR A C   
624  O O   . TYR A 84  ? 0.52149 0.53810 0.69206 -0.04673 0.03203  -0.01092 81  TYR A O   
625  C CB  . TYR A 84  ? 0.44496 0.39870 0.59670 -0.02570 0.03229  -0.02252 81  TYR A CB  
626  C CG  . TYR A 84  ? 0.46905 0.41563 0.61674 -0.02378 0.03446  -0.01706 81  TYR A CG  
627  C CD1 . TYR A 84  ? 0.49371 0.43554 0.64780 -0.03391 0.03414  -0.00883 81  TYR A CD1 
628  C CD2 . TYR A 84  ? 0.47818 0.42269 0.61561 -0.01188 0.03690  -0.02012 81  TYR A CD2 
629  C CE1 . TYR A 84  ? 0.51911 0.45479 0.66950 -0.03225 0.03604  -0.00371 81  TYR A CE1 
630  C CE2 . TYR A 84  ? 0.52460 0.46291 0.65824 -0.01026 0.03896  -0.01526 81  TYR A CE2 
631  C CZ  . TYR A 84  ? 0.55867 0.49279 0.69883 -0.02048 0.03844  -0.00702 81  TYR A CZ  
632  O OH  . TYR A 84  ? 0.55970 0.48812 0.69606 -0.01893 0.04041  -0.00209 81  TYR A OH  
633  N N   . THR A 85  ? 0.45324 0.45940 0.60799 -0.02853 0.03557  -0.01421 82  THR A N   
634  C CA  . THR A 85  ? 0.45657 0.48933 0.61190 -0.02874 0.03748  -0.01071 82  THR A CA  
635  C C   . THR A 85  ? 0.44527 0.49869 0.59931 -0.02318 0.03753  -0.01661 82  THR A C   
636  O O   . THR A 85  ? 0.42470 0.50213 0.58058 -0.02441 0.03881  -0.01410 82  THR A O   
637  C CB  . THR A 85  ? 0.45787 0.48959 0.60554 -0.02167 0.04054  -0.00816 82  THR A CB  
638  O OG1 . THR A 85  ? 0.44074 0.46134 0.57861 -0.00885 0.04166  -0.01522 82  THR A OG1 
639  C CG2 . THR A 85  ? 0.39279 0.40771 0.54271 -0.02835 0.04049  -0.00113 82  THR A CG2 
640  N N   . GLY A 86  ? 0.46152 0.50648 0.61250 -0.01711 0.03621  -0.02427 83  GLY A N   
641  C CA  . GLY A 86  ? 0.42825 0.49193 0.57922 -0.01304 0.03572  -0.02978 83  GLY A CA  
642  C C   . GLY A 86  ? 0.40002 0.46900 0.54118 0.00123  0.03780  -0.03565 83  GLY A C   
643  O O   . GLY A 86  ? 0.35644 0.44682 0.49775 0.00463  0.03812  -0.03847 83  GLY A O   
644  N N   . TYR A 87  ? 0.35695 0.32441 0.43911 -0.03123 -0.01956 -0.02796 84  TYR A N   
645  C CA  . TYR A 87  ? 0.37889 0.35648 0.47190 -0.02610 -0.01382 -0.03479 84  TYR A CA  
646  C C   . TYR A 87  ? 0.38597 0.36352 0.49022 -0.02195 -0.01360 -0.03643 84  TYR A C   
647  O O   . TYR A 87  ? 0.41395 0.40302 0.52765 -0.02199 -0.00839 -0.03954 84  TYR A O   
648  C CB  . TYR A 87  ? 0.33542 0.30939 0.42632 -0.02003 -0.01396 -0.03897 84  TYR A CB  
649  C CG  . TYR A 87  ? 0.32368 0.30930 0.42468 -0.01563 -0.00726 -0.04607 84  TYR A CG  
650  C CD1 . TYR A 87  ? 0.29159 0.27647 0.40287 -0.00875 -0.00603 -0.05011 84  TYR A CD1 
651  C CD2 . TYR A 87  ? 0.33769 0.33501 0.43788 -0.01832 -0.00202 -0.04871 84  TYR A CD2 
652  C CE1 . TYR A 87  ? 0.29363 0.28899 0.41410 -0.00468 0.00033  -0.05659 84  TYR A CE1 
653  C CE2 . TYR A 87  ? 0.32695 0.33510 0.43653 -0.01438 0.00424  -0.05522 84  TYR A CE2 
654  C CZ  . TYR A 87  ? 0.30604 0.31311 0.42573 -0.00760 0.00543  -0.05913 84  TYR A CZ  
655  O OH  . TYR A 87  ? 0.29505 0.31271 0.42400 -0.00365 0.01187  -0.06557 84  TYR A OH  
656  N N   . SER A 88  ? 0.37046 0.33506 0.47376 -0.01815 -0.01926 -0.03444 85  SER A N   
657  C CA  . SER A 88  ? 0.38273 0.34649 0.49607 -0.01405 -0.01944 -0.03569 85  SER A CA  
658  C C   . SER A 88  ? 0.37428 0.34250 0.49016 -0.01995 -0.01943 -0.03207 85  SER A C   
659  O O   . SER A 88  ? 0.39441 0.36863 0.52043 -0.01786 -0.01686 -0.03439 85  SER A O   
660  C CB  . SER A 88  ? 0.41104 0.35941 0.52225 -0.00864 -0.02566 -0.03425 85  SER A CB  
661  O OG  . SER A 88  ? 0.40867 0.34686 0.51060 -0.01327 -0.03185 -0.02769 85  SER A OG  
662  N N   . LEU A 89  ? 0.36465 0.33003 0.47148 -0.02720 -0.02215 -0.02654 86  LEU A N   
663  C CA  . LEU A 89  ? 0.34794 0.31785 0.45697 -0.03337 -0.02186 -0.02319 86  LEU A CA  
664  C C   . LEU A 89  ? 0.37409 0.36050 0.49031 -0.03618 -0.01463 -0.02666 86  LEU A C   
665  O O   . LEU A 89  ? 0.39892 0.39186 0.52394 -0.03669 -0.01262 -0.02763 86  LEU A O   
666  C CB  . LEU A 89  ? 0.38338 0.34640 0.48048 -0.04053 -0.02587 -0.01668 86  LEU A CB  
667  C CG  . LEU A 89  ? 0.40178 0.36877 0.49985 -0.04781 -0.02563 -0.01281 86  LEU A CG  
668  C CD1 . LEU A 89  ? 0.40329 0.36734 0.50988 -0.04502 -0.02806 -0.01261 86  LEU A CD1 
669  C CD2 . LEU A 89  ? 0.41143 0.37005 0.49670 -0.05429 -0.02962 -0.00639 86  LEU A CD2 
670  N N   . LEU A 90  ? 0.36895 0.36238 0.48155 -0.03791 -0.01068 -0.02868 87  LEU A N   
671  C CA  . LEU A 90  ? 0.35385 0.36311 0.47341 -0.04005 -0.00357 -0.03243 87  LEU A CA  
672  C C   . LEU A 90  ? 0.36133 0.37669 0.49329 -0.03298 0.00006  -0.03844 87  LEU A C   
673  O O   . LEU A 90  ? 0.37275 0.39898 0.51339 -0.03421 0.00433  -0.04058 87  LEU A O   
674  C CB  . LEU A 90  ? 0.32411 0.33869 0.43699 -0.04248 -0.00040 -0.03361 87  LEU A CB  
675  C CG  . LEU A 90  ? 0.35577 0.38681 0.47465 -0.04533 0.00700  -0.03719 87  LEU A CG  
676  C CD1 . LEU A 90  ? 0.30038 0.33805 0.42341 -0.05150 0.00853  -0.03479 87  LEU A CD1 
677  C CD2 . LEU A 90  ? 0.33642 0.37102 0.44660 -0.04876 0.00910  -0.03705 87  LEU A CD2 
678  N N   . THR A 91  ? 0.34342 0.35181 0.47630 -0.02548 -0.00144 -0.04130 88  THR A N   
679  C CA  . THR A 91  ? 0.33991 0.35210 0.48408 -0.01814 0.00166  -0.04675 88  THR A CA  
680  C C   . THR A 91  ? 0.36246 0.37403 0.51387 -0.01750 0.00019  -0.04556 88  THR A C   
681  O O   . THR A 91  ? 0.38851 0.41008 0.54983 -0.01574 0.00477  -0.04921 88  THR A O   
682  C CB  . THR A 91  ? 0.35273 0.35455 0.49550 -0.01047 -0.00085 -0.04904 88  THR A CB  
683  O OG1 . THR A 91  ? 0.38036 0.38436 0.51768 -0.01057 0.00115  -0.05112 88  THR A OG1 
684  C CG2 . THR A 91  ? 0.29593 0.30024 0.45008 -0.00258 0.00221  -0.05438 88  THR A CG2 
685  N N   . THR A 92  ? 0.39500 0.39494 0.54155 -0.01883 -0.00622 -0.04051 89  THR A N   
686  C CA  . THR A 92  ? 0.41047 0.40917 0.56351 -0.01820 -0.00816 -0.03922 89  THR A CA  
687  C C   . THR A 92  ? 0.43191 0.44260 0.58876 -0.02500 -0.00477 -0.03842 89  THR A C   
688  O O   . THR A 92  ? 0.41746 0.43476 0.58396 -0.02312 -0.00248 -0.04084 89  THR A O   
689  C CB  . THR A 92  ? 0.37999 0.36365 0.52623 -0.01881 -0.01586 -0.03372 89  THR A CB  
690  O OG1 . THR A 92  ? 0.36944 0.34198 0.51328 -0.01190 -0.01894 -0.03489 89  THR A OG1 
691  C CG2 . THR A 92  ? 0.34364 0.32641 0.49648 -0.01855 -0.01800 -0.03230 89  THR A CG2 
692  N N   . ALA A 93  ? 0.41525 0.42885 0.56461 -0.03281 -0.00430 -0.03516 90  ALA A N   
693  C CA  . ALA A 93  ? 0.42246 0.44695 0.57494 -0.03978 -0.00108 -0.03421 90  ALA A CA  
694  C C   . ALA A 93  ? 0.46460 0.50438 0.62619 -0.03847 0.00629  -0.03992 90  ALA A C   
695  O O   . ALA A 93  ? 0.47148 0.52038 0.64065 -0.04069 0.00902  -0.04103 90  ALA A O   
696  C CB  . ALA A 93  ? 0.43714 0.46051 0.57880 -0.04812 -0.00196 -0.02949 90  ALA A CB  
697  N N   . LEU A 94  ? 0.48800 0.53089 0.64918 -0.03482 0.00960  -0.04375 91  LEU A N   
698  C CA  . LEU A 94  ? 0.44941 0.50671 0.61920 -0.03333 0.01672  -0.04930 91  LEU A CA  
699  C C   . LEU A 94  ? 0.44009 0.49935 0.62114 -0.02607 0.01810  -0.05346 91  LEU A C   
700  O O   . LEU A 94  ? 0.40863 0.48019 0.59827 -0.02597 0.02335  -0.05710 91  LEU A O   
701  C CB  . LEU A 94  ? 0.42027 0.48006 0.58648 -0.03132 0.01979  -0.05233 91  LEU A CB  
702  C CG  . LEU A 94  ? 0.38163 0.44415 0.53829 -0.03859 0.02062  -0.04957 91  LEU A CG  
703  C CD1 . LEU A 94  ? 0.33358 0.39552 0.48589 -0.03528 0.02217  -0.05244 91  LEU A CD1 
704  C CD2 . LEU A 94  ? 0.37779 0.45488 0.53880 -0.04462 0.02612  -0.05044 91  LEU A CD2 
705  N N   . ALA A 95  ? 0.43183 0.47905 0.61284 -0.01989 0.01350  -0.05299 92  ALA A N   
706  C CA  . ALA A 95  ? 0.36536 0.41323 0.55640 -0.01242 0.01463  -0.05682 92  ALA A CA  
707  C C   . ALA A 95  ? 0.34258 0.39251 0.53912 -0.01437 0.01308  -0.05513 92  ALA A C   
708  O O   . ALA A 95  ? 0.35214 0.40909 0.55835 -0.01043 0.01632  -0.05897 92  ALA A O   
709  C CB  . ALA A 95  ? 0.28324 0.31710 0.47212 -0.00493 0.01037  -0.05697 92  ALA A CB  
710  N N   . LEU A 96  ? 0.33016 0.37401 0.52076 -0.02021 0.00820  -0.04960 93  LEU A N   
711  C CA  . LEU A 96  ? 0.39006 0.43460 0.58557 -0.02193 0.00606  -0.04788 93  LEU A CA  
712  C C   . LEU A 96  ? 0.39932 0.45957 0.60163 -0.02662 0.01159  -0.05009 93  LEU A C   
713  O O   . LEU A 96  ? 0.36436 0.43363 0.56502 -0.03077 0.01615  -0.05126 93  LEU A O   
714  C CB  . LEU A 96  ? 0.39755 0.43187 0.58456 -0.02758 -0.00019 -0.04139 93  LEU A CB  
715  C CG  . LEU A 96  ? 0.41967 0.43761 0.60045 -0.02316 -0.00658 -0.03867 93  LEU A CG  
716  C CD1 . LEU A 96  ? 0.41663 0.42574 0.59051 -0.02896 -0.01248 -0.03235 93  LEU A CD1 
717  C CD2 . LEU A 96  ? 0.38108 0.39472 0.56946 -0.01393 -0.00762 -0.04185 93  LEU A CD2 
718  N N   . PRO A 97  ? 0.36304 0.42687 0.57311 -0.02595 0.01125  -0.05083 94  PRO A N   
719  C CA  . PRO A 97  ? 0.39411 0.47240 0.61036 -0.03112 0.01594  -0.05255 94  PRO A CA  
720  C C   . PRO A 97  ? 0.40733 0.48702 0.61668 -0.04128 0.01515  -0.04794 94  PRO A C   
721  O O   . PRO A 97  ? 0.43516 0.50444 0.63496 -0.04430 0.01076  -0.04322 94  PRO A O   
722  C CB  . PRO A 97  ? 0.37404 0.45285 0.59897 -0.02759 0.01420  -0.05378 94  PRO A CB  
723  C CG  . PRO A 97  ? 0.39013 0.45316 0.61061 -0.02391 0.00719  -0.05037 94  PRO A CG  
724  C CD  . PRO A 97  ? 0.34120 0.39630 0.55508 -0.02005 0.00667  -0.05047 94  PRO A CD  
725  N N   . GLU A 98  ? 0.41589 0.50871 0.63020 -0.04659 0.01968  -0.04943 95  GLU A N   
726  C CA  . GLU A 98  ? 0.47023 0.56565 0.67861 -0.05644 0.01996  -0.04551 95  GLU A CA  
727  C C   . GLU A 98  ? 0.45683 0.54200 0.66093 -0.06006 0.01378  -0.04020 95  GLU A C   
728  O O   . GLU A 98  ? 0.47204 0.55278 0.66721 -0.06678 0.01210  -0.03561 95  GLU A O   
729  C CB  . GLU A 98  ? 0.51013 0.62144 0.72606 -0.06093 0.02583  -0.04846 95  GLU A CB  
730  C CG  . GLU A 98  ? 0.61554 0.73770 0.83317 -0.06029 0.03235  -0.05253 95  GLU A CG  
731  C CD  . GLU A 98  ? 0.74689 0.86824 0.95424 -0.06639 0.03343  -0.04959 95  GLU A CD  
732  O OE1 . GLU A 98  ? 0.79354 0.91939 0.99977 -0.06436 0.03720  -0.05230 95  GLU A OE1 
733  O OE2 . GLU A 98  ? 0.79545 0.91165 0.99579 -0.07310 0.03059  -0.04463 95  GLU A OE2 
734  N N   . ASP A 99  ? 0.40016 0.48134 0.61031 -0.05563 0.01040  -0.04074 96  ASP A N   
735  C CA  . ASP A 99  ? 0.44155 0.51358 0.64880 -0.05874 0.00459  -0.03607 96  ASP A CA  
736  C C   . ASP A 99  ? 0.46679 0.52304 0.66864 -0.05316 -0.00168 -0.03350 96  ASP A C   
737  O O   . ASP A 99  ? 0.45051 0.49884 0.65229 -0.05319 -0.00681 -0.03065 96  ASP A O   
738  C CB  . ASP A 99  ? 0.42581 0.50447 0.64348 -0.05849 0.00478  -0.03815 96  ASP A CB  
739  C CG  . ASP A 99  ? 0.42828 0.50736 0.65453 -0.04865 0.00475  -0.04269 96  ASP A CG  
740  O OD1 . ASP A 99  ? 0.47515 0.55442 0.70151 -0.04281 0.00709  -0.04563 96  ASP A OD1 
741  O OD2 . ASP A 99  ? 0.41962 0.49877 0.65249 -0.04664 0.00249  -0.04341 96  ASP A OD2 
742  N N   . GLY A 100 ? 0.45394 0.50556 0.65148 -0.04838 -0.00134 -0.03460 97  GLY A N   
743  C CA  . GLY A 100 ? 0.43017 0.46654 0.62158 -0.04381 -0.00721 -0.03194 97  GLY A CA  
744  C C   . GLY A 100 ? 0.43974 0.46659 0.61977 -0.05035 -0.01150 -0.02571 97  GLY A C   
745  O O   . GLY A 100 ? 0.42730 0.45910 0.60269 -0.05807 -0.00924 -0.02365 97  GLY A O   
746  N N   . LYS A 101 ? 0.40997 0.42260 0.58521 -0.04709 -0.01774 -0.02262 98  LYS A N   
747  C CA  . LYS A 101 ? 0.47233 0.47438 0.63671 -0.05257 -0.02249 -0.01649 98  LYS A CA  
748  C C   . LYS A 101 ? 0.46912 0.45762 0.62635 -0.04721 -0.02691 -0.01507 98  LYS A C   
749  O O   . LYS A 101 ? 0.44061 0.42434 0.60238 -0.03930 -0.02865 -0.01749 98  LYS A O   
750  C CB  . LYS A 101 ? 0.54133 0.53946 0.70758 -0.05595 -0.02661 -0.01306 98  LYS A CB  
751  C CG  . LYS A 101 ? 0.66522 0.66779 0.82762 -0.06605 -0.02528 -0.00960 98  LYS A CG  
752  C CD  . LYS A 101 ? 0.72690 0.72162 0.87600 -0.07067 -0.02694 -0.00499 98  LYS A CD  
753  C CE  . LYS A 101 ? 0.75939 0.75844 0.90444 -0.08065 -0.02507 -0.00161 98  LYS A CE  
754  N NZ  . LYS A 101 ? 0.78339 0.77820 0.91602 -0.08494 -0.02474 0.00169  98  LYS A NZ  
755  N N   . ILE A 102 ? 0.45501 0.43725 0.60092 -0.05150 -0.02863 -0.01122 99  ILE A N   
756  C CA  . ILE A 102 ? 0.44818 0.41766 0.58608 -0.04733 -0.03283 -0.00965 99  ILE A CA  
757  C C   . ILE A 102 ? 0.45852 0.41688 0.58577 -0.05289 -0.03822 -0.00304 99  ILE A C   
758  O O   . ILE A 102 ? 0.41170 0.37361 0.53395 -0.06073 -0.03677 -0.00011 99  ILE A O   
759  C CB  . ILE A 102 ? 0.45225 0.42563 0.58618 -0.04594 -0.02896 -0.01245 99  ILE A CB  
760  C CG1 . ILE A 102 ? 0.41522 0.40103 0.55964 -0.04138 -0.02280 -0.01899 99  ILE A CG1 
761  C CG2 . ILE A 102 ? 0.45914 0.41931 0.58572 -0.04094 -0.03342 -0.01142 99  ILE A CG2 
762  C CD1 . ILE A 102 ? 0.42534 0.41784 0.56665 -0.04167 -0.01804 -0.02180 99  ILE A CD1 
763  N N   . THR A 103 ? 0.44647 0.39116 0.57009 -0.04880 -0.04430 -0.00069 100 THR A N   
764  C CA  . THR A 103 ? 0.46997 0.40254 0.58213 -0.05293 -0.04965 0.00539  100 THR A CA  
765  C C   . THR A 103 ? 0.48613 0.41117 0.58989 -0.04938 -0.05112 0.00520  100 THR A C   
766  O O   . THR A 103 ? 0.49291 0.41180 0.59893 -0.04184 -0.05320 0.00289  100 THR A O   
767  C CB  . THR A 103 ? 0.47473 0.39685 0.58816 -0.05140 -0.05584 0.00857  100 THR A CB  
768  O OG1 . THR A 103 ? 0.46386 0.39365 0.58585 -0.05432 -0.05437 0.00817  100 THR A OG1 
769  C CG2 . THR A 103 ? 0.47627 0.38654 0.57760 -0.05627 -0.06094 0.01495  100 THR A CG2 
770  N N   . ALA A 104 ? 0.47317 0.39870 0.56730 -0.05469 -0.04994 0.00746  101 ALA A N   
771  C CA  . ALA A 104 ? 0.46776 0.38715 0.55323 -0.05206 -0.05108 0.00722  101 ALA A CA  
772  C C   . ALA A 104 ? 0.50522 0.41106 0.57845 -0.05544 -0.05710 0.01348  101 ALA A C   
773  O O   . ALA A 104 ? 0.51028 0.41613 0.57838 -0.06279 -0.05744 0.01785  101 ALA A O   
774  C CB  . ALA A 104 ? 0.43611 0.36653 0.51946 -0.05491 -0.04505 0.00467  101 ALA A CB  
775  N N   . ILE A 105 ? 0.50402 0.39825 0.57259 -0.05008 -0.06170 0.01383  102 ILE A N   
776  C CA  . ILE A 105 ? 0.55343 0.43358 0.61080 -0.05220 -0.06803 0.01958  102 ILE A CA  
777  C C   . ILE A 105 ? 0.53990 0.41457 0.58816 -0.04953 -0.06911 0.01884  102 ILE A C   
778  O O   . ILE A 105 ? 0.56416 0.43843 0.61626 -0.04256 -0.06855 0.01433  102 ILE A O   
779  C CB  . ILE A 105 ? 0.56688 0.43619 0.62753 -0.04815 -0.07389 0.02134  102 ILE A CB  
780  C CG1 . ILE A 105 ? 0.54405 0.42041 0.61609 -0.04885 -0.07225 0.02034  102 ILE A CG1 
781  C CG2 . ILE A 105 ? 0.58632 0.44229 0.63574 -0.05192 -0.08011 0.02795  102 ILE A CG2 
782  C CD1 . ILE A 105 ? 0.55507 0.42248 0.63220 -0.04346 -0.07722 0.02077  102 ILE A CD1 
783  N N   . ASP A 106 ? 0.51920 0.38956 0.55539 -0.05495 -0.07057 0.02316  103 ASP A N   
784  C CA  . ASP A 106 ? 0.54917 0.41340 0.57542 -0.05283 -0.07227 0.02300  103 ASP A CA  
785  C C   . ASP A 106 ? 0.60318 0.45791 0.61597 -0.05865 -0.07634 0.02964  103 ASP A C   
786  O O   . ASP A 106 ? 0.56572 0.42296 0.57661 -0.06552 -0.07534 0.03342  103 ASP A O   
787  C CB  . ASP A 106 ? 0.53478 0.41084 0.56176 -0.05263 -0.06605 0.01835  103 ASP A CB  
788  C CG  . ASP A 106 ? 0.59121 0.46179 0.61117 -0.04805 -0.06764 0.01627  103 ASP A CG  
789  O OD1 . ASP A 106 ? 0.61243 0.47496 0.61998 -0.05072 -0.07099 0.02020  103 ASP A OD1 
790  O OD2 . ASP A 106 ? 0.54587 0.42008 0.57279 -0.04165 -0.06551 0.01057  103 ASP A OD2 
791  N N   . VAL A 107 ? 0.58460 0.42821 0.58809 -0.05578 -0.08089 0.03095  104 VAL A N   
792  C CA  . VAL A 107 ? 0.62026 0.45386 0.61016 -0.06068 -0.08503 0.03722  104 VAL A CA  
793  C C   . VAL A 107 ? 0.64855 0.48794 0.62952 -0.06569 -0.08130 0.03802  104 VAL A C   
794  O O   . VAL A 107 ? 0.70891 0.54266 0.67936 -0.07133 -0.08318 0.04351  104 VAL A O   
795  C CB  . VAL A 107 ? 0.61364 0.43286 0.59634 -0.05575 -0.09150 0.03840  104 VAL A CB  
796  C CG1 . VAL A 107 ? 0.61320 0.42460 0.60278 -0.05186 -0.09598 0.03908  104 VAL A CG1 
797  C CG2 . VAL A 107 ? 0.54902 0.37076 0.53174 -0.04973 -0.08982 0.03276  104 VAL A CG2 
798  N N   . ASN A 108 ? 0.64759 0.49798 0.63235 -0.06374 -0.07598 0.03275  105 ASN A N   
799  C CA  . ASN A 108 ? 0.69157 0.54703 0.66751 -0.06720 -0.07266 0.03280  105 ASN A CA  
800  C C   . ASN A 108 ? 0.67735 0.54867 0.66125 -0.07060 -0.06531 0.02990  105 ASN A C   
801  O O   . ASN A 108 ? 0.68883 0.56965 0.68099 -0.06659 -0.06121 0.02400  105 ASN A O   
802  C CB  . ASN A 108 ? 0.72567 0.57873 0.69751 -0.06116 -0.07357 0.02888  105 ASN A CB  
803  C CG  . ASN A 108 ? 0.80106 0.65651 0.76141 -0.06434 -0.07158 0.02968  105 ASN A CG  
804  O OD1 . ASN A 108 ? 0.82431 0.68959 0.78451 -0.06944 -0.06652 0.02992  105 ASN A OD1 
805  N ND2 . ASN A 108 ? 0.82298 0.66937 0.77354 -0.06117 -0.07559 0.02998  105 ASN A ND2 
806  N N   . LYS A 109 ? 0.72954 0.68403 0.74237 -0.06087 0.01146  0.11867  106 LYS A N   
807  C CA  . LYS A 109 ? 0.74079 0.68723 0.72877 -0.06816 0.03044  0.11269  106 LYS A CA  
808  C C   . LYS A 109 ? 0.71624 0.63367 0.66399 -0.07662 0.02316  0.11367  106 LYS A C   
809  O O   . LYS A 109 ? 0.71133 0.62585 0.64347 -0.08124 0.03619  0.10797  106 LYS A O   
810  C CB  . LYS A 109 ? 0.80277 0.74187 0.77675 -0.07271 0.04533  0.11261  106 LYS A CB  
811  C CG  . LYS A 109 ? 0.87527 0.81387 0.83288 -0.07842 0.06833  0.10544  106 LYS A CG  
812  C CD  . LYS A 109 ? 0.90586 0.84996 0.86659 -0.07925 0.08474  0.10434  106 LYS A CD  
813  C CE  . LYS A 109 ? 0.91812 0.86994 0.87315 -0.08263 0.10895  0.09633  106 LYS A CE  
814  N NZ  . LYS A 109 ? 0.95441 0.87672 0.86281 -0.09369 0.11454  0.09547  106 LYS A NZ  
815  N N   . SER A 110 ? 0.72527 0.62150 0.65625 -0.07867 0.00264  0.12070  107 SER A N   
816  C CA  . SER A 110 ? 0.76632 0.63375 0.65787 -0.08694 -0.00484 0.12197  107 SER A CA  
817  C C   . SER A 110 ? 0.72174 0.59928 0.62180 -0.08478 -0.00644 0.11745  107 SER A C   
818  O O   . SER A 110 ? 0.72233 0.58328 0.59281 -0.09179 -0.00221 0.11475  107 SER A O   
819  C CB  . SER A 110 ? 0.80882 0.65339 0.68402 -0.08875 -0.02734 0.13063  107 SER A CB  
820  O OG  . SER A 110 ? 0.87097 0.73092 0.77692 -0.08026 -0.04441 0.13356  107 SER A OG  
821  N N   . TYR A 111 ? 0.66371 0.56827 0.60387 -0.07515 -0.01267 0.11661  108 TYR A N   
822  C CA  . TYR A 111 ? 0.64045 0.55879 0.59306 -0.07238 -0.01146 0.11146  108 TYR A CA  
823  C C   . TYR A 111 ? 0.60807 0.53593 0.55769 -0.07507 0.01243  0.10319  108 TYR A C   
824  O O   . TYR A 111 ? 0.57089 0.49103 0.50239 -0.07945 0.01658  0.09925  108 TYR A O   
825  C CB  . TYR A 111 ? 0.57832 0.52697 0.57776 -0.06109 -0.02002 0.11167  108 TYR A CB  
826  C CG  . TYR A 111 ? 0.58313 0.52520 0.58905 -0.05754 -0.04442 0.11935  108 TYR A CG  
827  C CD1 . TYR A 111 ? 0.65222 0.56300 0.62300 -0.06419 -0.05957 0.12480  108 TYR A CD1 
828  C CD2 . TYR A 111 ? 0.57216 0.53958 0.61967 -0.04747 -0.05235 0.12110  108 TYR A CD2 
829  C CE1 . TYR A 111 ? 0.67222 0.57711 0.64915 -0.06088 -0.08198 0.13182  108 TYR A CE1 
830  C CE2 . TYR A 111 ? 0.61902 0.58085 0.67298 -0.04408 -0.07469 0.12808  108 TYR A CE2 
831  C CZ  . TYR A 111 ? 0.65479 0.58531 0.67337 -0.05081 -0.08942 0.13341  108 TYR A CZ  
832  O OH  . TYR A 111 ? 0.69650 0.62147 0.72151 -0.04744 -0.11161 0.14034  108 TYR A OH  
833  N N   . TYR A 112 ? 0.60765 0.55252 0.57523 -0.07240 0.02835  0.10047  109 TYR A N   
834  C CA  . TYR A 112 ? 0.61259 0.56869 0.58034 -0.07434 0.05180  0.09258  109 TYR A CA  
835  C C   . TYR A 112 ? 0.62606 0.55342 0.54727 -0.08556 0.06060  0.09118  109 TYR A C   
836  O O   . TYR A 112 ? 0.63311 0.56336 0.54617 -0.08851 0.07466  0.08472  109 TYR A O   
837  C CB  . TYR A 112 ? 0.59443 0.57169 0.58845 -0.06964 0.06552  0.09101  109 TYR A CB  
838  C CG  . TYR A 112 ? 0.61428 0.60204 0.60738 -0.07197 0.09051  0.08334  109 TYR A CG  
839  C CD1 . TYR A 112 ? 0.57884 0.58878 0.59255 -0.06812 0.10050  0.07638  109 TYR A CD1 
840  C CD2 . TYR A 112 ? 0.59503 0.57104 0.56742 -0.07788 0.10417  0.08309  109 TYR A CD2 
841  C CE1 . TYR A 112 ? 0.52552 0.54530 0.53875 -0.07016 0.12339  0.06936  109 TYR A CE1 
842  C CE2 . TYR A 112 ? 0.57759 0.56339 0.54939 -0.07996 0.12706  0.07612  109 TYR A CE2 
843  C CZ  . TYR A 112 ? 0.56176 0.56942 0.55401 -0.07607 0.13658  0.06926  109 TYR A CZ  
844  O OH  . TYR A 112 ? 0.56641 0.58374 0.55797 -0.07814 0.15937  0.06230  109 TYR A OH  
845  N N   . GLU A 113 ? 0.63977 0.53922 0.53003 -0.09191 0.05234  0.09717  110 GLU A N   
846  C CA  . GLU A 113 ? 0.72444 0.59488 0.56891 -0.10283 0.05927  0.09643  110 GLU A CA  
847  C C   . GLU A 113 ? 0.71487 0.57162 0.53827 -0.10686 0.05231  0.09492  110 GLU A C   
848  O O   . GLU A 113 ? 0.74902 0.58851 0.53993 -0.11498 0.06244  0.09180  110 GLU A O   
849  C CB  . GLU A 113 ? 0.85188 0.69551 0.66931 -0.10826 0.04951  0.10381  110 GLU A CB  
850  C CG  . GLU A 113 ? 0.96352 0.81860 0.80087 -0.10424 0.05361  0.10632  110 GLU A CG  
851  C CD  . GLU A 113 ? 1.07725 0.92749 0.89793 -0.10991 0.07461  0.10308  110 GLU A CD  
852  O OE1 . GLU A 113 ? 1.14230 0.97078 0.93772 -0.11561 0.07247  0.10770  110 GLU A OE1 
853  O OE2 . GLU A 113 ? 1.09481 0.96290 0.92752 -0.10871 0.09319  0.09595  110 GLU A OE2 
854  N N   . ILE A 114 ? 0.68631 0.55012 0.52709 -0.10144 0.03521  0.09708  111 ILE A N   
855  C CA  . ILE A 114 ? 0.70905 0.56048 0.53105 -0.10495 0.02792  0.09573  111 ILE A CA  
856  C C   . ILE A 114 ? 0.68374 0.55160 0.51377 -0.10449 0.04555  0.08700  111 ILE A C   
857  O O   . ILE A 114 ? 0.73911 0.59082 0.53981 -0.11138 0.05036  0.08400  111 ILE A O   
858  C CB  . ILE A 114 ? 0.69345 0.54986 0.53440 -0.09877 0.00513  0.10032  111 ILE A CB  
859  C CG1 . ILE A 114 ? 0.69874 0.53622 0.52813 -0.09997 -0.01267 0.10909  111 ILE A CG1 
860  C CG2 . ILE A 114 ? 0.68550 0.53160 0.51003 -0.10177 -0.00192 0.09849  111 ILE A CG2 
861  C CD1 . ILE A 114 ? 0.68194 0.52514 0.53170 -0.09348 -0.03528 0.11400  111 ILE A CD1 
862  N N   . GLY A 115 ? 0.61270 0.51273 0.48226 -0.09644 0.05550  0.08278  112 GLY A N   
863  C CA  . GLY A 115 ? 0.58155 0.49963 0.46253 -0.09513 0.07179  0.07451  112 GLY A CA  
864  C C   . GLY A 115 ? 0.61585 0.53785 0.48979 -0.09872 0.09584  0.06919  112 GLY A C   
865  O O   . GLY A 115 ? 0.60181 0.53340 0.47669 -0.09964 0.11088  0.06215  112 GLY A O   
866  N N   . LEU A 116 ? 0.63725 0.55197 0.50418 -0.10074 0.09963  0.07249  113 LEU A N   
867  C CA  . LEU A 116 ? 0.66486 0.58300 0.52517 -0.10416 0.12229  0.06786  113 LEU A CA  
868  C C   . LEU A 116 ? 0.69473 0.59483 0.51858 -0.11327 0.13494  0.06313  113 LEU A C   
869  O O   . LEU A 116 ? 0.68633 0.60058 0.51701 -0.11334 0.15497  0.05632  113 LEU A O   
870  C CB  . LEU A 116 ? 0.68171 0.58871 0.53326 -0.10625 0.12148  0.07325  113 LEU A CB  
871  C CG  . LEU A 116 ? 0.70356 0.61109 0.54520 -0.11045 0.14386  0.06939  113 LEU A CG  
872  C CD1 . LEU A 116 ? 0.67161 0.61344 0.55071 -0.10341 0.16088  0.06253  113 LEU A CD1 
873  C CD2 . LEU A 116 ? 0.66270 0.55799 0.49531 -0.11245 0.14078  0.07538  113 LEU A CD2 
874  N N   . PRO A 117 ? 0.71901 0.58894 0.50447 -0.12101 0.12497  0.06615  114 PRO A N   
875  C CA  . PRO A 117 ? 0.75529 0.60993 0.50784 -0.12930 0.13780  0.06109  114 PRO A CA  
876  C C   . PRO A 117 ? 0.69720 0.57220 0.46740 -0.12590 0.14733  0.05352  114 PRO A C   
877  O O   . PRO A 117 ? 0.67894 0.55637 0.43943 -0.12956 0.16654  0.04721  114 PRO A O   
878  C CB  . PRO A 117 ? 0.82197 0.64394 0.53733 -0.13620 0.12058  0.06643  114 PRO A CB  
879  C CG  . PRO A 117 ? 0.82948 0.64400 0.54889 -0.13418 0.10451  0.07456  114 PRO A CG  
880  C CD  . PRO A 117 ? 0.74936 0.59641 0.51741 -0.12315 0.10269  0.07431  114 PRO A CD  
881  N N   . PHE A 118 ? 0.64553 0.53536 0.44158 -0.11897 0.13437  0.05398  115 PHE A N   
882  C CA  . PHE A 118 ? 0.66065 0.57138 0.47606 -0.11516 0.14286  0.04689  115 PHE A CA  
883  C C   . PHE A 118 ? 0.63196 0.57301 0.48042 -0.10935 0.16167  0.04139  115 PHE A C   
884  O O   . PHE A 118 ? 0.63786 0.58962 0.48846 -0.11009 0.17818  0.03417  115 PHE A O   
885  C CB  . PHE A 118 ? 0.67738 0.59770 0.51464 -0.10868 0.12387  0.04916  115 PHE A CB  
886  C CG  . PHE A 118 ? 0.70903 0.60066 0.51651 -0.11368 0.10396  0.05508  115 PHE A CG  
887  C CD1 . PHE A 118 ? 0.70276 0.58321 0.50864 -0.11278 0.08674  0.06308  115 PHE A CD1 
888  C CD2 . PHE A 118 ? 0.74112 0.61671 0.52188 -0.11935 0.10250  0.05266  115 PHE A CD2 
889  C CE1 . PHE A 118 ? 0.75028 0.60424 0.52867 -0.11742 0.06845  0.06857  115 PHE A CE1 
890  C CE2 . PHE A 118 ? 0.77639 0.62540 0.52950 -0.12402 0.08419  0.05813  115 PHE A CE2 
891  C CZ  . PHE A 118 ? 0.77832 0.61655 0.53029 -0.12306 0.06716  0.06610  115 PHE A CZ  
892  N N   . ILE A 119 ? 0.61694 0.57207 0.49135 -0.10356 0.15945  0.04470  116 ILE A N   
893  C CA  . ILE A 119 ? 0.61515 0.59850 0.52075 -0.09810 0.17708  0.03994  116 ILE A CA  
894  C C   . ILE A 119 ? 0.66333 0.63781 0.54472 -0.10527 0.19855  0.03563  116 ILE A C   
895  O O   . ILE A 119 ? 0.64335 0.63691 0.53922 -0.10349 0.21688  0.02869  116 ILE A O   
896  C CB  . ILE A 119 ? 0.58491 0.58120 0.51868 -0.09134 0.16931  0.04512  116 ILE A CB  
897  C CG1 . ILE A 119 ? 0.55622 0.56508 0.51802 -0.08343 0.14939  0.04860  116 ILE A CG1 
898  C CG2 . ILE A 119 ? 0.55487 0.57772 0.51723 -0.08661 0.18836  0.04051  116 ILE A CG2 
899  C CD1 . ILE A 119 ? 0.55143 0.57225 0.54049 -0.07670 0.14029  0.05397  116 ILE A CD1 
900  N N   . GLN A 120 ? 0.67894 0.62432 0.52297 -0.11355 0.19660  0.03964  117 GLN A N   
901  C CA  . GLN A 120 ? 0.69878 0.63422 0.51807 -0.12074 0.21641  0.03597  117 GLN A CA  
902  C C   . GLN A 120 ? 0.73610 0.66698 0.53719 -0.12499 0.22634  0.02920  117 GLN A C   
903  O O   . GLN A 120 ? 0.69043 0.63829 0.50918 -0.11640 0.22856  0.02191  117 GLN A O   
904  C CB  . GLN A 120 ? 0.74688 0.65132 0.52991 -0.12853 0.21017  0.04220  117 GLN A CB  
905  C CG  . GLN A 120 ? 0.81826 0.72851 0.61812 -0.12471 0.20623  0.04742  117 GLN A CG  
906  C CD  . GLN A 120 ? 0.91491 0.79397 0.68120 -0.13145 0.19442  0.05478  117 GLN A CD  
907  O OE1 . GLN A 120 ? 0.96078 0.81557 0.69730 -0.13709 0.18286  0.05743  117 GLN A OE1 
908  N NE2 . GLN A 120 ? 0.93633 0.81581 0.70721 -0.13092 0.19723  0.05813  117 GLN A NE2 
909  N N   . LYS A 121 ? 0.79100 0.70473 0.57125 -0.12887 0.21453  0.03067  118 LYS A N   
910  C CA  . LYS A 121 ? 0.80962 0.71744 0.57046 -0.13370 0.22409  0.02453  118 LYS A CA  
911  C C   . LYS A 121 ? 0.70405 0.64538 0.50597 -0.12265 0.22686  0.01720  118 LYS A C   
912  O O   . LYS A 121 ? 0.68453 0.63080 0.48746 -0.11905 0.22837  0.01053  118 LYS A O   
913  C CB  . LYS A 121 ? 0.91981 0.80273 0.65271 -0.13836 0.20643  0.02804  118 LYS A CB  
914  C CG  . LYS A 121 ? 1.03001 0.89786 0.73120 -0.14591 0.21585  0.02286  118 LYS A CG  
915  C CD  . LYS A 121 ? 1.13586 0.97672 0.80723 -0.15096 0.19752  0.02716  118 LYS A CD  
916  C CE  . LYS A 121 ? 1.18412 1.01719 0.83456 -0.15582 0.20437  0.02137  118 LYS A CE  
917  N NZ  . LYS A 121 ? 1.21752 1.03162 0.84984 -0.15814 0.18458  0.02514  118 LYS A NZ  
918  N N   . ALA A 122 ? 0.46701 0.51481 0.54019 0.00305  0.10851  0.08742  119 ALA A N   
919  C CA  . ALA A 122 ? 0.47783 0.53869 0.55030 0.00418  0.09156  0.07470  119 ALA A CA  
920  C C   . ALA A 122 ? 0.48600 0.56503 0.60710 -0.00096 0.08843  0.06601  119 ALA A C   
921  O O   . ALA A 122 ? 0.48043 0.57230 0.60617 0.00012  0.07640  0.05652  119 ALA A O   
922  C CB  . ALA A 122 ? 0.48213 0.53904 0.53085 0.00255  0.07339  0.06523  119 ALA A CB  
923  N N   . GLY A 123 ? 0.49806 0.57847 0.65520 -0.00668 0.09864  0.06924  120 GLY A N   
924  C CA  . GLY A 123 ? 0.52106 0.61837 0.72570 -0.01186 0.09740  0.06288  120 GLY A CA  
925  C C   . GLY A 123 ? 0.51367 0.62032 0.73615 -0.01859 0.07844  0.04715  120 GLY A C   
926  O O   . GLY A 123 ? 0.52252 0.64538 0.77579 -0.02150 0.07226  0.03962  120 GLY A O   
927  N N   . VAL A 124 ? 0.47770 0.57444 0.68184 -0.02122 0.06912  0.04220  121 VAL A N   
928  C CA  . VAL A 124 ? 0.45691 0.56048 0.67253 -0.02709 0.05045  0.02696  121 VAL A CA  
929  C C   . VAL A 124 ? 0.46489 0.56046 0.69644 -0.03451 0.05105  0.02503  121 VAL A C   
930  O O   . VAL A 124 ? 0.48751 0.58446 0.72190 -0.03911 0.03610  0.01312  121 VAL A O   
931  C CB  . VAL A 124 ? 0.45845 0.55949 0.63405 -0.02264 0.03434  0.01979  121 VAL A CB  
932  C CG1 . VAL A 124 ? 0.48218 0.59367 0.64806 -0.01644 0.03107  0.01888  121 VAL A CG1 
933  C CG2 . VAL A 124 ? 0.43662 0.51921 0.57076 -0.01843 0.03914  0.02859  121 VAL A CG2 
934  N N   . GLU A 125 ? 0.46528 0.55219 0.70737 -0.03575 0.06824  0.03653  122 GLU A N   
935  C CA  . GLU A 125 ? 0.50698 0.58542 0.76382 -0.04258 0.06968  0.03532  122 GLU A CA  
936  C C   . GLU A 125 ? 0.47114 0.56137 0.77186 -0.05138 0.06214  0.02433  122 GLU A C   
937  O O   . GLU A 125 ? 0.39816 0.48315 0.70662 -0.05736 0.05519  0.01732  122 GLU A O   
938  C CB  . GLU A 125 ? 0.55409 0.62158 0.81455 -0.04201 0.09030  0.05047  122 GLU A CB  
939  C CG  . GLU A 125 ? 0.56403 0.62094 0.83585 -0.04834 0.09276  0.05045  122 GLU A CG  
940  C CD  . GLU A 125 ? 0.61007 0.66064 0.89981 -0.04973 0.11304  0.06380  122 GLU A CD  
941  O OE1 . GLU A 125 ? 0.63259 0.68940 0.93392 -0.04695 0.12471  0.07166  122 GLU A OE1 
942  O OE2 . GLU A 125 ? 0.62763 0.66691 0.91991 -0.05345 0.11748  0.06657  122 GLU A OE2 
943  N N   . HIS A 126 ? 0.40046 0.50635 0.72974 -0.05231 0.06323  0.02283  123 HIS A N   
944  C CA  . HIS A 126 ? 0.39632 0.51425 0.76817 -0.06107 0.05582  0.01298  123 HIS A CA  
945  C C   . HIS A 126 ? 0.40929 0.53040 0.77532 -0.06472 0.03433  -0.00311 123 HIS A C   
946  O O   . HIS A 126 ? 0.43917 0.56506 0.83530 -0.07316 0.02707  -0.01201 123 HIS A O   
947  C CB  . HIS A 126 ? 0.36914 0.50439 0.76889 -0.06036 0.05989  0.01487  123 HIS A CB  
948  C CG  . HIS A 126 ? 0.35609 0.50199 0.73914 -0.05518 0.04765  0.00826  123 HIS A CG  
949  N ND1 . HIS A 126 ? 0.37516 0.51679 0.72161 -0.04561 0.05158  0.01490  123 HIS A ND1 
950  C CD2 . HIS A 126 ? 0.32563 0.48584 0.72300 -0.05840 0.03131  -0.00440 123 HIS A CD2 
951  C CE1 . HIS A 126 ? 0.33302 0.48594 0.67220 -0.04296 0.03835  0.00657  123 HIS A CE1 
952  N NE2 . HIS A 126 ? 0.35782 0.52248 0.72776 -0.05055 0.02593  -0.00512 123 HIS A NE2 
953  N N   . LYS A 127 ? 0.41004 0.52834 0.73789 -0.05873 0.02393  -0.00699 124 LYS A N   
954  C CA  . LYS A 127 ? 0.40560 0.52648 0.72508 -0.06154 0.00356  -0.02199 124 LYS A CA  
955  C C   . LYS A 127 ? 0.40046 0.50623 0.70668 -0.06476 -0.00032 -0.02524 124 LYS A C   
956  O O   . LYS A 127 ? 0.35504 0.46184 0.65800 -0.06812 -0.01658 -0.03803 124 LYS A O   
957  C CB  . LYS A 127 ? 0.39465 0.51873 0.67813 -0.05375 -0.00641 -0.02482 124 LYS A CB  
958  C CG  . LYS A 127 ? 0.39661 0.53412 0.68632 -0.04894 -0.00253 -0.02103 124 LYS A CG  
959  C CD  . LYS A 127 ? 0.34829 0.48844 0.60227 -0.04209 -0.01490 -0.02586 124 LYS A CD  
960  C CE  . LYS A 127 ? 0.30479 0.45411 0.55639 -0.03544 -0.00806 -0.01931 124 LYS A CE  
961  N NZ  . LYS A 127 ? 0.29046 0.44248 0.50803 -0.02914 -0.02091 -0.02468 124 LYS A NZ  
962  N N   . ILE A 128 ? 0.39670 0.48851 0.69529 -0.06374 0.01416  -0.01397 125 ILE A N   
963  C CA  . ILE A 128 ? 0.43564 0.51170 0.71369 -0.06459 0.01197  -0.01458 125 ILE A CA  
964  C C   . ILE A 128 ? 0.45205 0.52286 0.76262 -0.07288 0.01821  -0.01495 125 ILE A C   
965  O O   . ILE A 128 ? 0.43244 0.50381 0.76678 -0.07474 0.03332  -0.00573 125 ILE A O   
966  C CB  . ILE A 128 ? 0.41468 0.47758 0.65534 -0.05691 0.02297  -0.00102 125 ILE A CB  
967  C CG1 . ILE A 128 ? 0.43664 0.50355 0.64270 -0.04901 0.01541  -0.00139 125 ILE A CG1 
968  C CG2 . ILE A 128 ? 0.42391 0.47087 0.64709 -0.05814 0.02215  -0.00033 125 ILE A CG2 
969  C CD1 . ILE A 128 ? 0.47601 0.53196 0.64819 -0.04155 0.02751  0.01315  125 ILE A CD1 
970  N N   . ASN A 129 ? 0.44427 0.50953 0.75530 -0.07775 0.00677  -0.02546 126 ASN A N   
971  C CA  . ASN A 129 ? 0.49714 0.55330 0.83100 -0.08501 0.01194  -0.02591 126 ASN A CA  
972  C C   . ASN A 129 ? 0.49183 0.53071 0.79329 -0.08186 0.01277  -0.02253 126 ASN A C   
973  O O   . ASN A 129 ? 0.46159 0.49703 0.74440 -0.08161 -0.00131 -0.03219 126 ASN A O   
974  C CB  . ASN A 129 ? 0.49383 0.55699 0.85636 -0.09374 -0.00188 -0.04110 126 ASN A CB  
975  C CG  . ASN A 129 ? 0.51485 0.56696 0.89840 -0.10132 0.00248  -0.04239 126 ASN A CG  
976  O OD1 . ASN A 129 ? 0.53366 0.57753 0.92452 -0.10153 0.01845  -0.03098 126 ASN A OD1 
977  N ND2 . ASN A 129 ? 0.51187 0.56320 0.90460 -0.10761 -0.01169 -0.05631 126 ASN A ND2 
978  N N   . PHE A 130 ? 0.48301 0.51130 0.77751 -0.07928 0.02930  -0.00843 127 PHE A N   
979  C CA  . PHE A 130 ? 0.50695 0.51917 0.77068 -0.07588 0.03169  -0.00302 127 PHE A CA  
980  C C   . PHE A 130 ? 0.50750 0.50927 0.79018 -0.08271 0.03378  -0.00600 127 PHE A C   
981  O O   . PHE A 130 ? 0.54516 0.54660 0.85926 -0.08790 0.04474  -0.00192 127 PHE A O   
982  C CB  . PHE A 130 ? 0.49747 0.50273 0.74146 -0.06958 0.04807  0.01414  127 PHE A CB  
983  C CG  . PHE A 130 ? 0.51251 0.50249 0.72172 -0.06547 0.04956  0.02054  127 PHE A CG  
984  C CD1 . PHE A 130 ? 0.52436 0.50146 0.74074 -0.06846 0.05929  0.02656  127 PHE A CD1 
985  C CD2 . PHE A 130 ? 0.50160 0.49027 0.67133 -0.05874 0.04095  0.02069  127 PHE A CD2 
986  C CE1 . PHE A 130 ? 0.52088 0.48451 0.70620 -0.06468 0.06059  0.03292  127 PHE A CE1 
987  C CE2 . PHE A 130 ? 0.52607 0.50131 0.66448 -0.05517 0.04200  0.02714  127 PHE A CE2 
988  C CZ  . PHE A 130 ? 0.49807 0.46099 0.64456 -0.05808 0.05192  0.03341  127 PHE A CZ  
989  N N   . ILE A 131 ? 0.49880 0.49170 0.76189 -0.08251 0.02353  -0.01281 128 ILE A N   
990  C CA  . ILE A 131 ? 0.49651 0.47794 0.77313 -0.08833 0.02418  -0.01659 128 ILE A CA  
991  C C   . ILE A 131 ? 0.50173 0.46771 0.74633 -0.08319 0.02979  -0.00739 128 ILE A C   
992  O O   . ILE A 131 ? 0.44854 0.41205 0.66067 -0.07816 0.01983  -0.01016 128 ILE A O   
993  C CB  . ILE A 131 ? 0.47489 0.45936 0.75998 -0.09345 0.00625  -0.03425 128 ILE A CB  
994  C CG1 . ILE A 131 ? 0.50507 0.50568 0.82255 -0.09889 0.00036  -0.04275 128 ILE A CG1 
995  C CG2 . ILE A 131 ? 0.43176 0.40231 0.72783 -0.09899 0.00747  -0.03783 128 ILE A CG2 
996  C CD1 . ILE A 131 ? 0.49666 0.50141 0.82148 -0.10401 -0.01823 -0.06027 128 ILE A CD1 
997  N N   . GLU A 132 ? 0.52619 0.48214 0.77996 -0.08444 0.04565  0.00397  129 GLU A N   
998  C CA  . GLU A 132 ? 0.58754 0.52865 0.81391 -0.08009 0.05230  0.01398  129 GLU A CA  
999  C C   . GLU A 132 ? 0.58574 0.51617 0.81642 -0.08419 0.04618  0.00564  129 GLU A C   
1000 O O   . GLU A 132 ? 0.61805 0.54196 0.87469 -0.08994 0.05403  0.00632  129 GLU A O   
1001 C CB  . GLU A 132 ? 0.62680 0.56190 0.86015 -0.07937 0.07223  0.03037  129 GLU A CB  
1002 C CG  . GLU A 132 ? 0.71656 0.63692 0.92112 -0.07482 0.07933  0.04187  129 GLU A CG  
1003 C CD  . GLU A 132 ? 0.80892 0.72251 1.02244 -0.07492 0.09906  0.05771  129 GLU A CD  
1004 O OE1 . GLU A 132 ? 0.80364 0.72057 1.05187 -0.08036 0.10732  0.05794  129 GLU A OE1 
1005 O OE2 . GLU A 132 ? 0.84925 0.75427 1.03489 -0.06967 0.10613  0.07018  129 GLU A OE2 
1006 N N   . SER A 133 ? 0.57471 0.50295 0.77954 -0.08112 0.03232  -0.00210 130 SER A N   
1007 C CA  . SER A 133 ? 0.62782 0.54572 0.83349 -0.08424 0.02538  -0.01084 130 SER A CA  
1008 C C   . SER A 133 ? 0.64951 0.56597 0.81922 -0.07854 0.01169  -0.01583 130 SER A C   
1009 O O   . SER A 133 ? 0.64301 0.56776 0.79055 -0.07318 0.00606  -0.01437 130 SER A O   
1010 C CB  . SER A 133 ? 0.64537 0.56804 0.88512 -0.09277 0.01750  -0.02566 130 SER A CB  
1011 O OG  . SER A 133 ? 0.66114 0.57543 0.89389 -0.09452 0.00639  -0.03676 130 SER A OG  
1012 N N   . GLU A 134 ? 0.69965 0.60516 0.86382 -0.07970 0.00653  -0.02166 131 GLU A N   
1013 C CA  . GLU A 134 ? 0.68578 0.59076 0.82136 -0.07560 -0.00855 -0.02958 131 GLU A CA  
1014 C C   . GLU A 134 ? 0.63188 0.54923 0.77833 -0.07897 -0.02457 -0.04609 131 GLU A C   
1015 O O   . GLU A 134 ? 0.60122 0.52262 0.78008 -0.08622 -0.02557 -0.05432 131 GLU A O   
1016 C CB  . GLU A 134 ? 0.68322 0.57289 0.81244 -0.07612 -0.00917 -0.03173 131 GLU A CB  
1017 C CG  . GLU A 134 ? 0.73647 0.61333 0.86048 -0.07396 0.00722  -0.01592 131 GLU A CG  
1018 C CD  . GLU A 134 ? 0.83714 0.69930 0.95051 -0.07313 0.00579  -0.01757 131 GLU A CD  
1019 O OE1 . GLU A 134 ? 0.87958 0.74155 0.97154 -0.06999 -0.00741 -0.02543 131 GLU A OE1 
1020 O OE2 . GLU A 134 ? 0.89568 0.74640 1.02217 -0.07548 0.01800  -0.01094 131 GLU A OE2 
1021 N N   . ALA A 135 ? 0.62569 0.54909 0.74462 -0.07384 -0.03747 -0.05070 132 ALA A N   
1022 C CA  . ALA A 135 ? 0.65029 0.58732 0.77697 -0.07614 -0.05233 -0.06472 132 ALA A CA  
1023 C C   . ALA A 135 ? 0.64050 0.57403 0.78218 -0.08229 -0.06374 -0.08077 132 ALA A C   
1024 O O   . ALA A 135 ? 0.62876 0.57123 0.79619 -0.08843 -0.07021 -0.09133 132 ALA A O   
1025 C CB  . ALA A 135 ? 0.64155 0.58552 0.73340 -0.06876 -0.06272 -0.06467 132 ALA A CB  
1026 N N   . LEU A 136 ? 0.65794 0.57840 0.78362 -0.08077 -0.06647 -0.08269 133 LEU A N   
1027 C CA  . LEU A 136 ? 0.69720 0.61304 0.83277 -0.08598 -0.07806 -0.09834 133 LEU A CA  
1028 C C   . LEU A 136 ? 0.65982 0.57343 0.83489 -0.09550 -0.07347 -0.10396 133 LEU A C   
1029 O O   . LEU A 136 ? 0.66727 0.58663 0.85851 -0.10131 -0.08528 -0.11818 133 LEU A O   
1030 C CB  . LEU A 136 ? 0.75721 0.65785 0.86889 -0.08211 -0.07907 -0.09736 133 LEU A CB  
1031 C CG  . LEU A 136 ? 0.81478 0.71803 0.89119 -0.07531 -0.09245 -0.10118 133 LEU A CG  
1032 C CD1 . LEU A 136 ? 0.83972 0.72728 0.89704 -0.07207 -0.09189 -0.09968 133 LEU A CD1 
1033 C CD2 . LEU A 136 ? 0.83181 0.74775 0.91059 -0.07727 -0.10680 -0.11519 133 LEU A CD2 
1034 N N   . PRO A 137 ? 0.64602 0.55150 0.83777 -0.09777 -0.05727 -0.09358 134 PRO A N   
1035 C CA  . PRO A 137 ? 0.63481 0.53946 0.86534 -0.10733 -0.05377 -0.09919 134 PRO A CA  
1036 C C   . PRO A 137 ? 0.64283 0.56497 0.89660 -0.11148 -0.05775 -0.10352 134 PRO A C   
1037 O O   . PRO A 137 ? 0.63582 0.56102 0.91566 -0.11956 -0.06481 -0.11508 134 PRO A O   
1038 C CB  . PRO A 137 ? 0.63728 0.53156 0.87675 -0.10725 -0.03447 -0.08441 134 PRO A CB  
1039 C CG  . PRO A 137 ? 0.64438 0.52870 0.84942 -0.09903 -0.03092 -0.07533 134 PRO A CG  
1040 C CD  . PRO A 137 ? 0.63664 0.53202 0.81355 -0.09249 -0.04218 -0.07712 134 PRO A CD  
1041 N N   . VAL A 138 ? 0.62315 0.55664 0.86797 -0.10620 -0.05338 -0.09430 135 VAL A N   
1042 C CA  . VAL A 138 ? 0.61948 0.57006 0.88590 -0.10934 -0.05636 -0.09740 135 VAL A CA  
1043 C C   . VAL A 138 ? 0.60217 0.56259 0.86435 -0.11076 -0.07593 -0.11305 135 VAL A C   
1044 O O   . VAL A 138 ? 0.59159 0.56163 0.87886 -0.11691 -0.08178 -0.12120 135 VAL A O   
1045 C CB  . VAL A 138 ? 0.61590 0.57465 0.87053 -0.10256 -0.04644 -0.08337 135 VAL A CB  
1046 C CG1 . VAL A 138 ? 0.59248 0.56861 0.87138 -0.10559 -0.04800 -0.08569 135 VAL A CG1 
1047 C CG2 . VAL A 138 ? 0.63083 0.57894 0.88780 -0.10113 -0.02725 -0.06772 135 VAL A CG2 
1048 N N   . LEU A 139 ? 0.56828 0.52680 0.79631 -0.10436 -0.08579 -0.11616 136 LEU A N   
1049 C CA  . LEU A 139 ? 0.59446 0.56294 0.80548 -0.10158 -0.10018 -0.12525 136 LEU A CA  
1050 C C   . LEU A 139 ? 0.66805 0.63239 0.88338 -0.10479 -0.10267 -0.13111 136 LEU A C   
1051 O O   . LEU A 139 ? 0.67127 0.64602 0.88707 -0.10506 -0.10846 -0.13491 136 LEU A O   
1052 C CB  . LEU A 139 ? 0.54072 0.50683 0.70978 -0.09275 -0.10643 -0.12356 136 LEU A CB  
1053 C CG  . LEU A 139 ? 0.52420 0.49599 0.67992 -0.08797 -0.10734 -0.11820 136 LEU A CG  
1054 C CD1 . LEU A 139 ? 0.51778 0.48755 0.62874 -0.07869 -0.11278 -0.11520 136 LEU A CD1 
1055 C CD2 . LEU A 139 ? 0.48525 0.47509 0.65281 -0.08812 -0.10941 -0.11875 136 LEU A CD2 
1056 N N   . ASP A 140 ? 0.71460 0.66284 0.93242 -0.10733 -0.09806 -0.13142 137 ASP A N   
1057 C CA  . ASP A 140 ? 0.73334 0.67628 0.95446 -0.11068 -0.10045 -0.13706 137 ASP A CA  
1058 C C   . ASP A 140 ? 0.79218 0.74136 1.04801 -0.11820 -0.09769 -0.13890 137 ASP A C   
1059 O O   . ASP A 140 ? 0.84344 0.79689 1.10034 -0.12028 -0.10361 -0.14412 137 ASP A O   
1060 C CB  . ASP A 140 ? 0.73042 0.65402 0.94668 -0.11146 -0.09529 -0.13644 137 ASP A CB  
1061 C CG  . ASP A 140 ? 0.74867 0.66655 0.92776 -0.10395 -0.10007 -0.13611 137 ASP A CG  
1062 O OD1 . ASP A 140 ? 0.74719 0.67529 0.90387 -0.09923 -0.10760 -0.13777 137 ASP A OD1 
1063 O OD2 . ASP A 140 ? 0.76644 0.66951 0.93901 -0.10271 -0.09500 -0.13297 137 ASP A OD2 
1064 N N   . GLN A 141 ? 0.79193 0.74149 1.07631 -0.12253 -0.08780 -0.13358 138 GLN A N   
1065 C CA  . GLN A 141 ? 0.81729 0.77455 1.13501 -0.12925 -0.08442 -0.13392 138 GLN A CA  
1066 C C   . GLN A 141 ? 0.81034 0.78656 1.12995 -0.12783 -0.09186 -0.13609 138 GLN A C   
1067 O O   . GLN A 141 ? 0.82046 0.80372 1.15784 -0.13223 -0.09433 -0.13917 138 GLN A O   
1068 C CB  . GLN A 141 ? 0.85073 0.80416 1.19720 -0.13359 -0.06945 -0.12512 138 GLN A CB  
1069 C CG  . GLN A 141 ? 0.88468 0.84499 1.26638 -0.14047 -0.06417 -0.12391 138 GLN A CG  
1070 C CD  . GLN A 141 ? 0.93640 0.88675 1.32483 -0.14524 -0.06547 -0.12886 138 GLN A CD  
1071 O OE1 . GLN A 141 ? 0.96643 0.90290 1.33571 -0.14372 -0.06772 -0.13202 138 GLN A OE1 
1072 N NE2 . GLN A 141 ? 0.93450 0.89180 1.35017 -0.15108 -0.06397 -0.12929 138 GLN A NE2 
1073 N N   . MET A 142 ? 0.78094 0.76507 1.08150 -0.12165 -0.09551 -0.13423 139 MET A N   
1074 C CA  . MET A 142 ? 0.78041 0.78161 1.07868 -0.11929 -0.10246 -0.13585 139 MET A CA  
1075 C C   . MET A 142 ? 0.79572 0.79850 1.07455 -0.11768 -0.11229 -0.14172 139 MET A C   
1076 O O   . MET A 142 ? 0.80448 0.81799 1.09412 -0.11981 -0.11619 -0.14389 139 MET A O   
1077 C CB  . MET A 142 ? 0.76905 0.77669 1.04725 -0.11250 -0.10401 -0.13216 139 MET A CB  
1078 C CG  . MET A 142 ? 0.76673 0.77765 1.06792 -0.11478 -0.09416 -0.12546 139 MET A CG  
1079 S SD  . MET A 142 ? 0.77252 0.78947 1.04504 -0.10662 -0.09785 -0.12195 139 MET A SD  
1080 C CE  . MET A 142 ? 0.80149 0.81899 1.08826 -0.10517 -0.07714 -0.10496 139 MET A CE  
1081 N N   . LEU A 143 ? 0.83088 0.82304 1.08124 -0.11410 -0.11548 -0.14341 140 LEU A N   
1082 C CA  . LEU A 143 ? 0.89369 0.88649 1.12558 -0.11305 -0.12260 -0.14737 140 LEU A CA  
1083 C C   . LEU A 143 ? 0.98927 0.97854 1.24306 -0.12077 -0.12318 -0.15213 140 LEU A C   
1084 O O   . LEU A 143 ? 1.00304 0.99788 1.25326 -0.12211 -0.12885 -0.15510 140 LEU A O   
1085 C CB  . LEU A 143 ? 0.90282 0.88518 1.10134 -0.10777 -0.12388 -0.14681 140 LEU A CB  
1086 C CG  . LEU A 143 ? 0.92722 0.91722 1.09388 -0.10036 -0.12753 -0.14342 140 LEU A CG  
1087 C CD1 . LEU A 143 ? 0.94598 0.92619 1.08352 -0.09629 -0.12734 -0.14229 140 LEU A CD1 
1088 C CD2 . LEU A 143 ? 0.94230 0.94321 1.11086 -0.10179 -0.13206 -0.14496 140 LEU A CD2 
1089 N N   . GLU A 144 ? 1.05220 1.03174 1.32819 -0.12612 -0.11682 -0.15220 141 GLU A N   
1090 C CA  . GLU A 144 ? 1.08751 1.06356 1.38541 -0.13382 -0.11677 -0.15602 141 GLU A CA  
1091 C C   . GLU A 144 ? 1.07033 1.06043 1.39705 -0.13836 -0.11671 -0.15549 141 GLU A C   
1092 O O   . GLU A 144 ? 1.11664 1.10739 1.45713 -0.14420 -0.11946 -0.15903 141 GLU A O   
1093 C CB  . GLU A 144 ? 1.14529 1.10613 1.45776 -0.13796 -0.10845 -0.15484 141 GLU A CB  
1094 C CG  . GLU A 144 ? 1.21848 1.16344 1.50879 -0.13680 -0.11013 -0.15811 141 GLU A CG  
1095 C CD  . GLU A 144 ? 1.27205 1.20129 1.57189 -0.13884 -0.10062 -0.15519 141 GLU A CD  
1096 O OE1 . GLU A 144 ? 1.29376 1.20891 1.57694 -0.13782 -0.10093 -0.15741 141 GLU A OE1 
1097 O OE2 . GLU A 144 ? 1.28146 1.21217 1.60530 -0.14138 -0.09185 -0.14984 141 GLU A OE2 
1098 N N   . GLU A 145 ? 0.99487 0.99621 1.33077 -0.13593 -0.11364 -0.15095 142 GLU A N   
1099 C CA  . GLU A 145 ? 0.98467 0.99972 1.35016 -0.13999 -0.11205 -0.14931 142 GLU A CA  
1100 C C   . GLU A 145 ? 0.95605 0.98644 1.31143 -0.13595 -0.11900 -0.14972 142 GLU A C   
1101 O O   . GLU A 145 ? 0.95631 0.99810 1.33386 -0.13958 -0.11972 -0.14953 142 GLU A O   
1102 C CB  . GLU A 145 ? 0.99408 1.01092 1.38416 -0.14138 -0.10068 -0.14235 142 GLU A CB  
1103 C CG  . GLU A 145 ? 1.03523 1.04141 1.45038 -0.14803 -0.09122 -0.13996 142 GLU A CG  
1104 C CD  . GLU A 145 ? 1.05110 1.05573 1.48295 -0.14819 -0.07774 -0.13099 142 GLU A CD  
1105 O OE1 . GLU A 145 ? 1.06663 1.05689 1.50209 -0.15019 -0.06933 -0.12785 142 GLU A OE1 
1106 O OE2 . GLU A 145 ? 1.03339 1.05071 1.47394 -0.14622 -0.07475 -0.12632 142 GLU A OE2 
1107 N N   . MET A 146 ? 1.32869 1.03721 1.39035 -0.12592 -0.19279 -0.05269 143 MET A N   
1108 C CA  . MET A 146 ? 1.32178 1.06288 1.38186 -0.12061 -0.18191 -0.05856 143 MET A CA  
1109 C C   . MET A 146 ? 1.32048 1.04959 1.37111 -0.11888 -0.19017 -0.07237 143 MET A C   
1110 O O   . MET A 146 ? 1.31072 1.00343 1.34552 -0.10966 -0.19635 -0.08542 143 MET A O   
1111 C CB  . MET A 146 ? 1.33024 1.07771 1.37820 -0.10188 -0.16471 -0.06600 143 MET A CB  
1112 C CG  . MET A 146 ? 1.34650 1.13472 1.39666 -0.09811 -0.15070 -0.06767 143 MET A CG  
1113 S SD  . MET A 146 ? 1.37025 1.18884 1.42562 -0.09275 -0.13146 -0.05777 143 MET A SD  
1114 C CE  . MET A 146 ? 1.38647 1.21071 1.46327 -0.11307 -0.13986 -0.03573 143 MET A CE  
1115 N N   . LYS A 147 ? 1.31686 1.07685 1.37740 -0.12793 -0.19019 -0.06925 144 LYS A N   
1116 C CA  . LYS A 147 ? 1.33880 1.09563 1.39100 -0.12523 -0.19503 -0.08209 144 LYS A CA  
1117 C C   . LYS A 147 ? 1.40335 1.17999 1.44521 -0.10916 -0.17906 -0.09297 144 LYS A C   
1118 O O   . LYS A 147 ? 1.39009 1.19185 1.43545 -0.10403 -0.16433 -0.08786 144 LYS A O   
1119 C CB  . LYS A 147 ? 1.30029 1.07970 1.36905 -0.14382 -0.20409 -0.07279 144 LYS A CB  
1120 C CG  . LYS A 147 ? 1.27504 1.03551 1.35419 -0.16062 -0.22067 -0.06232 144 LYS A CG  
1121 N N   . GLU A 148 ? 1.48069 1.24547 1.50942 -0.10135 -0.18216 -0.10820 145 GLU A N   
1122 C CA  . GLU A 148 ? 1.52468 1.30600 1.54255 -0.08573 -0.16788 -0.11978 145 GLU A CA  
1123 C C   . GLU A 148 ? 1.51708 1.34698 1.54943 -0.09157 -0.15672 -0.11053 145 GLU A C   
1124 O O   . GLU A 148 ? 1.53406 1.38408 1.56142 -0.07966 -0.14076 -0.11459 145 GLU A O   
1125 C CB  . GLU A 148 ? 1.59522 1.35718 1.59882 -0.07931 -0.17513 -0.13625 145 GLU A CB  
1126 C CG  . GLU A 148 ? 1.66217 1.41230 1.64520 -0.05774 -0.16448 -0.15332 145 GLU A CG  
1127 C CD  . GLU A 148 ? 1.68160 1.46953 1.66527 -0.05035 -0.14905 -0.15630 145 GLU A CD  
1128 O OE1 . GLU A 148 ? 1.68444 1.46814 1.65305 -0.03272 -0.13775 -0.16820 145 GLU A OE1 
1129 O OE2 . GLU A 148 ? 1.67775 1.49938 1.67693 -0.06210 -0.14809 -0.14679 145 GLU A OE2 
1130 N N   . GLU A 149 ? 1.41905 1.26820 1.46936 -0.10990 -0.16461 -0.09797 146 GLU A N   
1131 C CA  . GLU A 149 ? 1.29813 1.19332 1.36344 -0.11685 -0.15464 -0.08825 146 GLU A CA  
1132 C C   . GLU A 149 ? 1.19635 1.11260 1.27240 -0.11985 -0.14373 -0.07444 146 GLU A C   
1133 O O   . GLU A 149 ? 1.16716 1.12210 1.25546 -0.12524 -0.13395 -0.06592 146 GLU A O   
1134 C CB  . GLU A 149 ? 1.30632 1.21427 1.38720 -0.13564 -0.16730 -0.07961 146 GLU A CB  
1135 N N   . ASP A 150 ? 1.13357 1.02576 1.20540 -0.11660 -0.14495 -0.07192 147 ASP A N   
1136 C CA  . ASP A 150 ? 1.05158 0.96140 1.13398 -0.12070 -0.13620 -0.05791 147 ASP A CA  
1137 C C   . ASP A 150 ? 0.94869 0.85545 1.01810 -0.10306 -0.12111 -0.06425 147 ASP A C   
1138 O O   . ASP A 150 ? 0.92468 0.84528 1.00137 -0.10519 -0.11299 -0.05329 147 ASP A O   
1139 C CB  . ASP A 150 ? 1.12280 1.01104 1.21410 -0.13353 -0.14968 -0.04649 147 ASP A CB  
1140 C CG  . ASP A 150 ? 1.14344 1.04356 1.25200 -0.15375 -0.16235 -0.03556 147 ASP A CG  
1141 O OD1 . ASP A 150 ? 1.10883 1.04482 1.22825 -0.16047 -0.15694 -0.03046 147 ASP A OD1 
1142 O OD2 . ASP A 150 ? 1.16391 1.03738 1.27519 -0.16294 -0.17756 -0.03199 147 ASP A OD2 
1143 N N   . LEU A 151 ? 0.88967 0.77917 0.94016 -0.08597 -0.11713 -0.08141 148 LEU A N   
1144 C CA  . LEU A 151 ? 0.83940 0.72176 0.87625 -0.06866 -0.10395 -0.08829 148 LEU A CA  
1145 C C   . LEU A 151 ? 0.75825 0.68168 0.80187 -0.06689 -0.08583 -0.08137 148 LEU A C   
1146 O O   . LEU A 151 ? 0.72451 0.68070 0.77686 -0.07254 -0.08067 -0.07851 148 LEU A O   
1147 C CB  . LEU A 151 ? 0.85151 0.71149 0.86740 -0.05126 -0.10275 -0.10840 148 LEU A CB  
1148 C CG  . LEU A 151 ? 0.89078 0.70583 0.89637 -0.05008 -0.11903 -0.11732 148 LEU A CG  
1149 C CD1 . LEU A 151 ? 0.88898 0.68941 0.87620 -0.03551 -0.11806 -0.13664 148 LEU A CD1 
1150 C CD2 . LEU A 151 ? 0.89843 0.68336 0.89858 -0.04535 -0.12095 -0.11517 148 LEU A CD2 
1151 N N   . TYR A 152 ? 0.70254 0.62389 0.74206 -0.05908 -0.07600 -0.07854 149 TYR A N   
1152 C CA  . TYR A 152 ? 0.62896 0.58708 0.67422 -0.05758 -0.05862 -0.07137 149 TYR A CA  
1153 C C   . TYR A 152 ? 0.53822 0.50785 0.56925 -0.04071 -0.04426 -0.08560 149 TYR A C   
1154 O O   . TYR A 152 ? 0.53612 0.47943 0.54974 -0.02636 -0.04560 -0.10115 149 TYR A O   
1155 C CB  . TYR A 152 ? 0.66943 0.62087 0.71537 -0.05570 -0.05363 -0.06277 149 TYR A CB  
1156 C CG  . TYR A 152 ? 0.76101 0.70765 0.82307 -0.07303 -0.06518 -0.04636 149 TYR A CG  
1157 C CD1 . TYR A 152 ? 0.74653 0.72756 0.82733 -0.08813 -0.06149 -0.02995 149 TYR A CD1 
1158 C CD2 . TYR A 152 ? 0.81906 0.72658 0.87751 -0.07428 -0.07951 -0.04727 149 TYR A CD2 
1159 C CE1 . TYR A 152 ? 0.75673 0.73365 0.85229 -0.10397 -0.07199 -0.01490 149 TYR A CE1 
1160 C CE2 . TYR A 152 ? 0.80919 0.71213 0.88239 -0.09003 -0.08995 -0.03223 149 TYR A CE2 
1161 C CZ  . TYR A 152 ? 0.79741 0.73531 0.88917 -0.10482 -0.08624 -0.01606 149 TYR A CZ  
1162 O OH  . TYR A 152 ? 0.82347 0.75724 0.93001 -0.12056 -0.09657 -0.00099 149 TYR A OH  
1163 N N   . ASP A 153 ? 0.46319 0.47268 0.50180 -0.04267 -0.03017 -0.08009 150 ASP A N   
1164 C CA  . ASP A 153 ? 0.48252 0.50638 0.50863 -0.02699 -0.01459 -0.09210 150 ASP A CA  
1165 C C   . ASP A 153 ? 0.49770 0.51654 0.51266 -0.01334 -0.00175 -0.09463 150 ASP A C   
1166 O O   . ASP A 153 ? 0.47516 0.48673 0.47349 0.00369  0.00684  -0.10889 150 ASP A O   
1167 C CB  . ASP A 153 ? 0.44521 0.51402 0.48363 -0.03428 -0.00375 -0.08534 150 ASP A CB  
1168 C CG  . ASP A 153 ? 0.44467 0.52205 0.49401 -0.04684 -0.01485 -0.08328 150 ASP A CG  
1169 O OD1 . ASP A 153 ? 0.46763 0.52371 0.50762 -0.04158 -0.02395 -0.09550 150 ASP A OD1 
1170 O OD2 . ASP A 153 ? 0.40021 0.50598 0.46756 -0.06217 -0.01440 -0.06926 150 ASP A OD2 
1171 N N   . TYR A 154 ? 0.52886 0.55174 0.55275 -0.02058 -0.00032 -0.08092 151 TYR A N   
1172 C CA  . TYR A 154 ? 0.49751 0.52732 0.51467 -0.01047 0.01455  -0.07988 151 TYR A CA  
1173 C C   . TYR A 154 ? 0.45903 0.47048 0.48126 -0.01620 0.00793  -0.06883 151 TYR A C   
1174 O O   . TYR A 154 ? 0.46657 0.47990 0.50432 -0.03271 -0.00268 -0.05575 151 TYR A O   
1175 C CB  . TYR A 154 ? 0.49931 0.57466 0.52583 -0.01503 0.03059  -0.07188 151 TYR A CB  
1176 C CG  . TYR A 154 ? 0.51197 0.60097 0.53558 -0.00902 0.04601  -0.06679 151 TYR A CG  
1177 C CD1 . TYR A 154 ? 0.53386 0.62982 0.56985 -0.02048 0.04515  -0.05039 151 TYR A CD1 
1178 C CD2 . TYR A 154 ? 0.51992 0.61684 0.52888 0.00748  0.06176  -0.07796 151 TYR A CD2 
1179 C CE1 . TYR A 154 ? 0.56306 0.67255 0.59652 -0.01557 0.05924  -0.04534 151 TYR A CE1 
1180 C CE2 . TYR A 154 ? 0.54639 0.65669 0.55255 0.01254  0.07601  -0.07316 151 TYR A CE2 
1181 C CZ  . TYR A 154 ? 0.57814 0.69484 0.59662 0.00084  0.07463  -0.05676 151 TYR A CZ  
1182 O OH  . TYR A 154 ? 0.59955 0.72996 0.61531 0.00535  0.08860  -0.05161 151 TYR A OH  
1183 N N   . ALA A 155 ? 0.45310 0.44688 0.46230 -0.00245 0.01424  -0.07403 152 ALA A N   
1184 C CA  . ALA A 155 ? 0.45552 0.43089 0.46803 -0.00570 0.00932  -0.06432 152 ALA A CA  
1185 C C   . ALA A 155 ? 0.46956 0.45556 0.47494 0.00511  0.02562  -0.06332 152 ALA A C   
1186 O O   . ALA A 155 ? 0.51627 0.49602 0.50507 0.02213  0.03490  -0.07706 152 ALA A O   
1187 C CB  . ALA A 155 ? 0.48815 0.41689 0.49029 0.00047  -0.00504 -0.07321 152 ALA A CB  
1188 N N   . PHE A 156 ? 0.46613 0.46816 0.48385 -0.00489 0.02900  -0.04710 153 PHE A N   
1189 C CA  . PHE A 156 ? 0.44835 0.46063 0.46080 0.00340  0.04357  -0.04397 153 PHE A CA  
1190 C C   . PHE A 156 ? 0.46789 0.45285 0.48134 0.00257  0.03584  -0.03658 153 PHE A C   
1191 O O   . PHE A 156 ? 0.44338 0.42840 0.47206 -0.01289 0.02609  -0.02244 153 PHE A O   
1192 C CB  . PHE A 156 ? 0.36705 0.42395 0.39253 -0.00711 0.05600  -0.03103 153 PHE A CB  
1193 C CG  . PHE A 156 ? 0.38253 0.45319 0.40149 0.00171  0.07244  -0.02888 153 PHE A CG  
1194 C CD1 . PHE A 156 ? 0.41420 0.48345 0.41540 0.01997  0.08470  -0.04348 153 PHE A CD1 
1195 C CD2 . PHE A 156 ? 0.38737 0.47276 0.41789 -0.00845 0.07565  -0.01219 153 PHE A CD2 
1196 C CE1 . PHE A 156 ? 0.43378 0.51567 0.42865 0.02795  0.09980  -0.04155 153 PHE A CE1 
1197 C CE2 . PHE A 156 ? 0.44289 0.54133 0.46723 -0.00070 0.09073  -0.01001 153 PHE A CE2 
1198 C CZ  . PHE A 156 ? 0.45488 0.55149 0.46127 0.01752  0.10281  -0.02476 153 PHE A CZ  
1199 N N   . VAL A 157 ? 0.46810 0.42974 0.46553 0.01919  0.04022  -0.04605 154 VAL A N   
1200 C CA  . VAL A 157 ? 0.51133 0.44253 0.50729 0.02122  0.03294  -0.04143 154 VAL A CA  
1201 C C   . VAL A 157 ? 0.54139 0.48769 0.53590 0.02625  0.04703  -0.03412 154 VAL A C   
1202 O O   . VAL A 157 ? 0.47991 0.42954 0.46009 0.04163  0.05986  -0.04423 154 VAL A O   
1203 C CB  . VAL A 157 ? 0.55903 0.44795 0.53773 0.03624  0.02562  -0.05791 154 VAL A CB  
1204 C CG1 . VAL A 157 ? 0.58476 0.44179 0.56332 0.03728  0.01753  -0.05221 154 VAL A CG1 
1205 C CG2 . VAL A 157 ? 0.58988 0.46620 0.56887 0.03160  0.01278  -0.06607 154 VAL A CG2 
1206 N N   . ASP A 158 ? 0.56423 0.51922 0.57339 0.01323  0.04447  -0.01651 155 ASP A N   
1207 C CA  . ASP A 158 ? 0.53871 0.51229 0.54890 0.01518  0.05758  -0.00725 155 ASP A CA  
1208 C C   . ASP A 158 ? 0.51578 0.47678 0.53725 0.00558  0.04912  0.00834  155 ASP A C   
1209 O O   . ASP A 158 ? 0.45770 0.44433 0.49092 -0.00462 0.05499  0.02348  155 ASP A O   
1210 C CB  . ASP A 158 ? 0.51930 0.53918 0.53853 0.00635  0.07022  0.00018  155 ASP A CB  
1211 C CG  . ASP A 158 ? 0.53646 0.57740 0.55171 0.01225  0.08709  0.00497  155 ASP A CG  
1212 O OD1 . ASP A 158 ? 0.60234 0.62304 0.60483 0.02632  0.09075  -0.00086 155 ASP A OD1 
1213 O OD2 . ASP A 158 ? 0.51030 0.58830 0.53527 0.00248  0.09677  0.01480  155 ASP A OD2 
1214 N N   . ALA A 159 ? 0.55086 0.47263 0.56897 0.00855  0.03553  0.00501  156 ALA A N   
1215 C CA  . ALA A 159 ? 0.55900 0.46719 0.58855 -0.00110 0.02640  0.01986  156 ALA A CA  
1216 C C   . ALA A 159 ? 0.58679 0.46718 0.60530 0.01285  0.02837  0.01709  156 ALA A C   
1217 O O   . ALA A 159 ? 0.59589 0.48747 0.60543 0.02394  0.04239  0.01455  156 ALA A O   
1218 C CB  . ALA A 159 ? 0.56226 0.44801 0.60033 -0.01236 0.00765  0.02159  156 ALA A CB  
1219 N N   . ASP A 160 ? 0.64300 0.48761 0.66269 0.01177  0.01441  0.01827  157 ASP A N   
1220 C CA  . ASP A 160 ? 0.70501 0.51888 0.71479 0.02472  0.01442  0.01552  157 ASP A CA  
1221 C C   . ASP A 160 ? 0.65437 0.45223 0.64282 0.04517  0.02115  -0.00462 157 ASP A C   
1222 O O   . ASP A 160 ? 0.65548 0.43170 0.63579 0.04975  0.01328  -0.01808 157 ASP A O   
1223 C CB  . ASP A 160 ? 0.85286 0.63063 0.86826 0.01873  -0.00276 0.01960  157 ASP A CB  
1224 C CG  . ASP A 160 ? 0.99829 0.74515 1.00547 0.03087  -0.00278 0.01881  157 ASP A CG  
1225 O OD1 . ASP A 160 ? 1.02568 0.78518 1.02754 0.03984  0.01027  0.02048  157 ASP A OD1 
1226 O OD2 . ASP A 160 ? 1.07230 0.78252 1.07808 0.03155  -0.01551 0.01632  157 ASP A OD2 
1227 N N   . LYS A 161 ? 0.51673 0.47472 0.56613 0.04948  -0.02377 -0.04567 158 LYS A N   
1228 C CA  . LYS A 161 ? 0.54338 0.50900 0.59789 0.05114  -0.01862 -0.05035 158 LYS A CA  
1229 C C   . LYS A 161 ? 0.61899 0.57890 0.68223 0.05499  -0.00881 -0.05568 158 LYS A C   
1230 O O   . LYS A 161 ? 0.68167 0.64148 0.73803 0.05348  -0.00201 -0.06255 158 LYS A O   
1231 C CB  . LYS A 161 ? 0.52201 0.49830 0.58906 0.05299  -0.02419 -0.04496 158 LYS A CB  
1232 C CG  . LYS A 161 ? 0.51005 0.49093 0.56729 0.04816  -0.03336 -0.04001 158 LYS A CG  
1233 C CD  . LYS A 161 ? 0.47895 0.46047 0.51789 0.04279  -0.03159 -0.04534 158 LYS A CD  
1234 C CE  . LYS A 161 ? 0.44583 0.43000 0.47479 0.03729  -0.03902 -0.04137 158 LYS A CE  
1235 N NZ  . LYS A 161 ? 0.40332 0.38608 0.41679 0.03228  -0.03692 -0.04653 158 LYS A NZ  
1236 N N   . SER A 162 ? 0.62568 0.57982 0.70357 0.05953  -0.00778 -0.05267 159 SER A N   
1237 C CA  . SER A 162 ? 0.64681 0.59501 0.73505 0.06308  0.00289  -0.05830 159 SER A CA  
1238 C C   . SER A 162 ? 0.67131 0.60847 0.74376 0.05961  0.01007  -0.06556 159 SER A C   
1239 O O   . SER A 162 ? 0.69791 0.62839 0.77542 0.06114  0.02005  -0.07140 159 SER A O   
1240 C CB  . SER A 162 ? 0.65218 0.59679 0.76285 0.06926  0.00189  -0.05287 159 SER A CB  
1241 O OG  . SER A 162 ? 0.68338 0.61827 0.78841 0.06854  -0.00277 -0.04855 159 SER A OG  
1242 N N   . ASN A 163 ? 0.67643 0.61153 0.73042 0.05449  0.00568  -0.06579 160 ASN A N   
1243 C CA  . ASN A 163 ? 0.65472 0.58007 0.69414 0.05057  0.01099  -0.07220 160 ASN A CA  
1244 C C   . ASN A 163 ? 0.60859 0.53800 0.63138 0.04536  0.01166  -0.07770 160 ASN A C   
1245 O O   . ASN A 163 ? 0.62864 0.55148 0.63824 0.04114  0.01406  -0.08258 160 ASN A O   
1246 C CB  . ASN A 163 ? 0.69491 0.61327 0.72780 0.04847  0.00596  -0.06854 160 ASN A CB  
1247 C CG  . ASN A 163 ? 0.76038 0.66514 0.79672 0.04987  0.01240  -0.07086 160 ASN A CG  
1248 O OD1 . ASN A 163 ? 0.78696 0.68684 0.82728 0.05120  0.02163  -0.07688 160 ASN A OD1 
1249 N ND2 . ASN A 163 ? 0.76157 0.65913 0.79543 0.04894  0.00818  -0.06640 160 ASN A ND2 
1250 N N   . TYR A 164 ? 0.53658 0.47641 0.56019 0.04540  0.00915  -0.07678 161 TYR A N   
1251 C CA  . TYR A 164 ? 0.50698 0.45030 0.51578 0.04076  0.00855  -0.08089 161 TYR A CA  
1252 C C   . TYR A 164 ? 0.52308 0.45853 0.52294 0.03820  0.01669  -0.08842 161 TYR A C   
1253 O O   . TYR A 164 ? 0.55557 0.48820 0.54096 0.03340  0.01558  -0.09195 161 TYR A O   
1254 C CB  . TYR A 164 ? 0.48363 0.43790 0.49615 0.04160  0.00580  -0.07876 161 TYR A CB  
1255 C CG  . TYR A 164 ? 0.48148 0.44381 0.49412 0.04077  -0.00308 -0.07315 161 TYR A CG  
1256 C CD1 . TYR A 164 ? 0.51123 0.47152 0.52642 0.04099  -0.00806 -0.06827 161 TYR A CD1 
1257 C CD2 . TYR A 164 ? 0.43607 0.40684 0.44506 0.03908  -0.00603 -0.07290 161 TYR A CD2 
1258 C CE1 . TYR A 164 ? 0.45492 0.42135 0.46797 0.03888  -0.01536 -0.06371 161 TYR A CE1 
1259 C CE2 . TYR A 164 ? 0.40173 0.37896 0.41019 0.03755  -0.01295 -0.06865 161 TYR A CE2 
1260 C CZ  . TYR A 164 ? 0.42276 0.39778 0.43270 0.03713  -0.01739 -0.06429 161 TYR A CZ  
1261 O OH  . TYR A 164 ? 0.42187 0.40222 0.42919 0.03435  -0.02349 -0.06062 161 TYR A OH  
1262 N N   . ALA A 165 ? 0.53756 0.46929 0.54606 0.04081  0.02500  -0.09115 162 ALA A N   
1263 C CA  . ALA A 165 ? 0.55972 0.48252 0.55773 0.03716  0.03380  -0.09884 162 ALA A CA  
1264 C C   . ALA A 165 ? 0.59493 0.50695 0.58333 0.03388  0.03552  -0.10227 162 ALA A C   
1265 O O   . ALA A 165 ? 0.59165 0.49768 0.56422 0.02826  0.03836  -0.10796 162 ALA A O   
1266 C CB  . ALA A 165 ? 0.51444 0.43432 0.52579 0.04045  0.04401  -0.10166 162 ALA A CB  
1267 N N   . ASN A 166 ? 0.60738 0.51633 0.60432 0.03674  0.03339  -0.09866 163 ASN A N   
1268 C CA  . ASN A 166 ? 0.58257 0.48124 0.57056 0.03329  0.03485  -0.10170 163 ASN A CA  
1269 C C   . ASN A 166 ? 0.59975 0.50229 0.57343 0.02811  0.02692  -0.10148 163 ASN A C   
1270 O O   . ASN A 166 ? 0.62546 0.52192 0.58597 0.02265  0.02849  -0.10672 163 ASN A O   
1271 C CB  . ASN A 166 ? 0.60355 0.49687 0.60487 0.03778  0.03472  -0.09724 163 ASN A CB  
1272 C CG  . ASN A 166 ? 0.67468 0.56025 0.69014 0.04204  0.04475  -0.09974 163 ASN A CG  
1273 O OD1 . ASN A 166 ? 0.70014 0.57717 0.70917 0.03903  0.05423  -0.10741 163 ASN A OD1 
1274 N ND2 . ASN A 166 ? 0.68739 0.57569 0.72264 0.04868  0.04270  -0.09336 163 ASN A ND2 
1275 N N   . TYR A 167 ? 0.57808 0.49074 0.55492 0.02936  0.01853  -0.09573 164 TYR A N   
1276 C CA  . TYR A 167 ? 0.60799 0.52560 0.57419 0.02471  0.01183  -0.09600 164 TYR A CA  
1277 C C   . TYR A 167 ? 0.60061 0.51995 0.55549 0.02072  0.01217  -0.10075 164 TYR A C   
1278 O O   . TYR A 167 ? 0.57862 0.49668 0.52335 0.01572  0.00949  -0.10383 164 TYR A O   
1279 C CB  . TYR A 167 ? 0.60732 0.53533 0.57923 0.02649  0.00445  -0.08982 164 TYR A CB  
1280 C CG  . TYR A 167 ? 0.64955 0.57561 0.63026 0.02935  0.00225  -0.08398 164 TYR A CG  
1281 C CD1 . TYR A 167 ? 0.65788 0.57413 0.63698 0.02817  0.00388  -0.08422 164 TYR A CD1 
1282 C CD2 . TYR A 167 ? 0.63573 0.56914 0.62556 0.03268  -0.00197 -0.07791 164 TYR A CD2 
1283 C CE1 . TYR A 167 ? 0.64635 0.55945 0.63214 0.03037  0.00102  -0.07799 164 TYR A CE1 
1284 C CE2 . TYR A 167 ? 0.62433 0.55526 0.62076 0.03456  -0.00541 -0.07171 164 TYR A CE2 
1285 C CZ  . TYR A 167 ? 0.66120 0.58162 0.65532 0.03347  -0.00407 -0.07150 164 TYR A CZ  
1286 O OH  . TYR A 167 ? 0.73767 0.65426 0.73712 0.03497  -0.00827 -0.06449 164 TYR A OH  
1287 N N   . HIS A 168 ? 0.57490 0.49690 0.53159 0.02252  0.01514  -0.10115 165 HIS A N   
1288 C CA  . HIS A 168 ? 0.59573 0.51855 0.54040 0.01846  0.01470  -0.10452 165 HIS A CA  
1289 C C   . HIS A 168 ? 0.62089 0.53324 0.55187 0.01270  0.01838  -0.11074 165 HIS A C   
1290 O O   . HIS A 168 ? 0.63886 0.55200 0.55827 0.00771  0.01341  -0.11246 165 HIS A O   
1291 C CB  . HIS A 168 ? 0.57501 0.49984 0.52361 0.02087  0.01943  -0.10443 165 HIS A CB  
1292 C CG  . HIS A 168 ? 0.57931 0.50405 0.51438 0.01644  0.01857  -0.10686 165 HIS A CG  
1293 N ND1 . HIS A 168 ? 0.55448 0.48686 0.48537 0.01504  0.01012  -0.10417 165 HIS A ND1 
1294 C CD2 . HIS A 168 ? 0.58201 0.49887 0.50618 0.01264  0.02513  -0.11159 165 HIS A CD2 
1295 C CE1 . HIS A 168 ? 0.56736 0.49659 0.48565 0.01098  0.01048  -0.10633 165 HIS A CE1 
1296 N NE2 . HIS A 168 ? 0.58706 0.50662 0.49971 0.00898  0.01953  -0.11087 165 HIS A NE2 
1297 N N   . GLU A 169 ? 0.65645 0.55866 0.58907 0.01305  0.02688  -0.11417 166 GLU A N   
1298 C CA  . GLU A 169 ? 0.69313 0.58413 0.61139 0.00665  0.03145  -0.12080 166 GLU A CA  
1299 C C   . GLU A 169 ? 0.69279 0.58326 0.60472 0.00248  0.02523  -0.12149 166 GLU A C   
1300 O O   . GLU A 169 ? 0.71501 0.60050 0.61254 -0.00432 0.02426  -0.12593 166 GLU A O   
1301 C CB  . GLU A 169 ? 0.71180 0.59154 0.63532 0.00820  0.04302  -0.12469 166 GLU A CB  
1302 C CG  . GLU A 169 ? 0.73179 0.61119 0.66174 0.01109  0.05099  -0.12579 166 GLU A CG  
1303 C CD  . GLU A 169 ? 0.79640 0.67403 0.70932 0.00496  0.05220  -0.12949 166 GLU A CD  
1304 O OE1 . GLU A 169 ? 0.84611 0.71624 0.74085 -0.00260 0.05172  -0.13396 166 GLU A OE1 
1305 O OE2 . GLU A 169 ? 0.81047 0.69387 0.72756 0.00719  0.05316  -0.12767 166 GLU A OE2 
1306 N N   . ARG A 170 ? 0.65724 0.55256 0.57924 0.00571  0.02089  -0.11723 167 ARG A N   
1307 C CA  . ARG A 170 ? 0.67210 0.56816 0.58955 0.00145  0.01534  -0.11808 167 ARG A CA  
1308 C C   . ARG A 170 ? 0.65732 0.56433 0.57205 -0.00065 0.00612  -0.11635 167 ARG A C   
1309 O O   . ARG A 170 ? 0.67622 0.58323 0.58323 -0.00624 0.00191  -0.11928 167 ARG A O   
1310 C CB  . ARG A 170 ? 0.72141 0.61713 0.64900 0.00462  0.01486  -0.11438 167 ARG A CB  
1311 C CG  . ARG A 170 ? 0.77027 0.65309 0.69945 0.00508  0.02264  -0.11666 167 ARG A CG  
1312 C CD  . ARG A 170 ? 0.79246 0.67162 0.73120 0.01098  0.02946  -0.11533 167 ARG A CD  
1313 N NE  . ARG A 170 ? 0.81840 0.68528 0.76219 0.01248  0.03661  -0.11666 167 ARG A NE  
1314 C CZ  . ARG A 170 ? 0.83276 0.69466 0.78789 0.01771  0.04366  -0.11617 167 ARG A CZ  
1315 N NH1 . ARG A 170 ? 0.81697 0.68569 0.77910 0.02151  0.04467  -0.11466 167 ARG A NH1 
1316 N NH2 . ARG A 170 ? 0.85967 0.70970 0.82044 0.01915  0.04994  -0.11731 167 ARG A NH2 
1317 N N   . LEU A 171 ? 0.61057 0.52693 0.53260 0.00365  0.00282  -0.11168 168 LEU A N   
1318 C CA  . LEU A 171 ? 0.58047 0.50719 0.50326 0.00251  -0.00548 -0.10965 168 LEU A CA  
1319 C C   . LEU A 171 ? 0.58206 0.50896 0.49436 -0.00135 -0.00875 -0.11175 168 LEU A C   
1320 O O   . LEU A 171 ? 0.57200 0.50484 0.48365 -0.00403 -0.01612 -0.11152 168 LEU A O   
1321 C CB  . LEU A 171 ? 0.55427 0.48974 0.48742 0.00772  -0.00739 -0.10432 168 LEU A CB  
1322 C CG  . LEU A 171 ? 0.59157 0.52816 0.53312 0.00972  -0.00755 -0.10131 168 LEU A CG  
1323 C CD1 . LEU A 171 ? 0.57439 0.51725 0.52460 0.01445  -0.00839 -0.09609 168 LEU A CD1 
1324 C CD2 . LEU A 171 ? 0.56070 0.50156 0.50237 0.00586  -0.01244 -0.10228 168 LEU A CD2 
1325 N N   . VAL A 172 ? 0.55338 0.47342 0.45765 -0.00206 -0.00344 -0.11373 169 VAL A N   
1326 C CA  . VAL A 172 ? 0.60074 0.51827 0.49138 -0.00717 -0.00662 -0.11558 169 VAL A CA  
1327 C C   . VAL A 172 ? 0.65371 0.56602 0.53407 -0.01416 -0.00993 -0.11959 169 VAL A C   
1328 O O   . VAL A 172 ? 0.69103 0.60187 0.55979 -0.01933 -0.01534 -0.12035 169 VAL A O   
1329 C CB  . VAL A 172 ? 0.63569 0.54514 0.51808 -0.00773 0.00153  -0.11767 169 VAL A CB  
1330 C CG1 . VAL A 172 ? 0.63244 0.54874 0.52501 -0.00170 0.00315  -0.11358 169 VAL A CG1 
1331 C CG2 . VAL A 172 ? 0.67167 0.57018 0.55273 -0.00845 0.01173  -0.12232 169 VAL A CG2 
1332 N N   . LYS A 173 ? 0.67819 0.58726 0.56220 -0.01486 -0.00725 -0.12190 170 LYS A N   
1333 C CA  . LYS A 173 ? 0.68392 0.58923 0.56026 -0.02169 -0.01063 -0.12584 170 LYS A CA  
1334 C C   . LYS A 173 ? 0.65680 0.57146 0.54430 -0.02145 -0.01739 -0.12437 170 LYS A C   
1335 O O   . LYS A 173 ? 0.69490 0.60923 0.57861 -0.02724 -0.02194 -0.12728 170 LYS A O   
1336 C CB  . LYS A 173 ? 0.67861 0.57110 0.54907 -0.02421 -0.00122 -0.13088 170 LYS A CB  
1337 C CG  . LYS A 173 ? 0.69414 0.57650 0.55568 -0.02453 0.00800  -0.13349 170 LYS A CG  
1338 C CD  . LYS A 173 ? 0.74009 0.60963 0.59913 -0.02621 0.01838  -0.13867 170 LYS A CD  
1339 N N   . LEU A 174 ? 0.64759 0.57041 0.54856 -0.01561 -0.01791 -0.12027 171 LEU A N   
1340 C CA  . LEU A 174 ? 0.62762 0.55837 0.53922 -0.01584 -0.02228 -0.11950 171 LEU A CA  
1341 C C   . LEU A 174 ? 0.61775 0.56044 0.53743 -0.01429 -0.02993 -0.11644 171 LEU A C   
1342 O O   . LEU A 174 ? 0.62554 0.57521 0.55444 -0.01560 -0.03363 -0.11688 171 LEU A O   
1343 C CB  . LEU A 174 ? 0.62323 0.55260 0.54282 -0.01183 -0.01676 -0.11749 171 LEU A CB  
1344 C CG  . LEU A 174 ? 0.70196 0.61948 0.61685 -0.01352 -0.00979 -0.12045 171 LEU A CG  
1345 C CD1 . LEU A 174 ? 0.72911 0.64337 0.65064 -0.00797 -0.00452 -0.11668 171 LEU A CD1 
1346 C CD2 . LEU A 174 ? 0.67994 0.59671 0.59487 -0.01916 -0.01151 -0.12398 171 LEU A CD2 
1347 N N   . VAL A 175 ? 0.61483 0.55961 0.53205 -0.01174 -0.03167 -0.11368 172 VAL A N   
1348 C CA  . VAL A 175 ? 0.59026 0.54484 0.51446 -0.01052 -0.03902 -0.11089 172 VAL A CA  
1349 C C   . VAL A 175 ? 0.60948 0.56240 0.52466 -0.01514 -0.04609 -0.11171 172 VAL A C   
1350 O O   . VAL A 175 ? 0.63323 0.57686 0.53369 -0.01822 -0.04388 -0.11333 172 VAL A O   
1351 C CB  . VAL A 175 ? 0.60139 0.55925 0.52897 -0.00503 -0.03697 -0.10679 172 VAL A CB  
1352 C CG1 . VAL A 175 ? 0.57673 0.53575 0.51213 -0.00127 -0.03132 -0.10538 172 VAL A CG1 
1353 C CG2 . VAL A 175 ? 0.67256 0.62298 0.58787 -0.00508 -0.03381 -0.10660 172 VAL A CG2 
1354 N N   . ARG A 176 ? 0.58548 0.54689 0.50959 -0.01607 -0.05460 -0.11064 173 ARG A N   
1355 C CA  . ARG A 176 ? 0.60895 0.56937 0.52592 -0.02061 -0.06359 -0.11030 173 ARG A CA  
1356 C C   . ARG A 176 ? 0.65452 0.60997 0.55937 -0.01983 -0.06442 -0.10706 173 ARG A C   
1357 O O   . ARG A 176 ? 0.66049 0.61668 0.56736 -0.01494 -0.05931 -0.10477 173 ARG A O   
1358 C CB  . ARG A 176 ? 0.55637 0.52802 0.48987 -0.02044 -0.07275 -0.10905 173 ARG A CB  
1359 C CG  . ARG A 176 ? 0.53000 0.50926 0.47564 -0.01461 -0.07362 -0.10516 173 ARG A CG  
1360 C CD  . ARG A 176 ? 0.53924 0.52859 0.50212 -0.01461 -0.08271 -0.10421 173 ARG A CD  
1361 N NE  . ARG A 176 ? 0.55641 0.55234 0.53177 -0.00932 -0.08233 -0.10126 173 ARG A NE  
1362 C CZ  . ARG A 176 ? 0.57463 0.56954 0.54670 -0.00715 -0.08659 -0.09689 173 ARG A CZ  
1363 N NH1 . ARG A 176 ? 0.54116 0.54182 0.52541 -0.00267 -0.08533 -0.09488 173 ARG A NH1 
1364 N NH2 . ARG A 176 ? 0.56814 0.55530 0.52357 -0.01015 -0.09168 -0.09469 173 ARG A NH2 
1365 N N   . ILE A 177 ? 0.65265 0.60251 0.54392 -0.02552 -0.07113 -0.10688 174 ILE A N   
1366 C CA  . ILE A 177 ? 0.65267 0.59769 0.53188 -0.02595 -0.07366 -0.10329 174 ILE A CA  
1367 C C   . ILE A 177 ? 0.64413 0.59902 0.53843 -0.02088 -0.07997 -0.09841 174 ILE A C   
1368 O O   . ILE A 177 ? 0.66098 0.62456 0.57010 -0.02047 -0.08793 -0.09754 174 ILE A O   
1369 C CB  . ILE A 177 ? 0.66549 0.60181 0.52566 -0.03439 -0.08107 -0.10363 174 ILE A CB  
1370 C CG1 . ILE A 177 ? 0.69598 0.62206 0.54190 -0.03996 -0.07352 -0.10955 174 ILE A CG1 
1371 C CG2 . ILE A 177 ? 0.62900 0.55826 0.47380 -0.03585 -0.08300 -0.09979 174 ILE A CG2 
1372 C CD1 . ILE A 177 ? 0.70160 0.61656 0.52416 -0.04978 -0.07891 -0.11069 174 ILE A CD1 
1373 N N   . GLY A 178 ? 0.61397 0.56764 0.50598 -0.01706 -0.07576 -0.09562 175 GLY A N   
1374 C CA  . GLY A 178 ? 0.58267 0.54512 0.48983 -0.01174 -0.07900 -0.09175 175 GLY A CA  
1375 C C   . GLY A 178 ? 0.58416 0.55497 0.50846 -0.00638 -0.07244 -0.09305 175 GLY A C   
1376 O O   . GLY A 178 ? 0.55804 0.53529 0.49389 -0.00225 -0.07314 -0.09050 175 GLY A O   
1377 N N   . GLY A 179 ? 0.56882 0.53878 0.49419 -0.00689 -0.06615 -0.09686 176 GLY A N   
1378 C CA  . GLY A 179 ? 0.57033 0.54609 0.50835 -0.00282 -0.05989 -0.09759 176 GLY A CA  
1379 C C   . GLY A 179 ? 0.55718 0.53069 0.49180 0.00089  -0.05248 -0.09590 176 GLY A C   
1380 O O   . GLY A 179 ? 0.53837 0.50508 0.46080 0.00020  -0.05004 -0.09528 176 GLY A O   
1381 N N   . ALA A 180 ? 0.53328 0.51252 0.47898 0.00427  -0.04870 -0.09534 177 ALA A N   
1382 C CA  . ALA A 180 ? 0.53999 0.51954 0.48605 0.00789  -0.04330 -0.09313 177 ALA A CA  
1383 C C   . ALA A 180 ? 0.53899 0.51652 0.48655 0.00916  -0.03676 -0.09406 177 ALA A C   
1384 O O   . ALA A 180 ? 0.55601 0.53535 0.50915 0.00823  -0.03648 -0.09543 177 ALA A O   
1385 C CB  . ALA A 180 ? 0.49489 0.48242 0.45179 0.01034  -0.04530 -0.09081 177 ALA A CB  
1386 N N   . ILE A 181 ? 0.51928 0.49274 0.46251 0.01114  -0.03150 -0.09317 178 ILE A N   
1387 C CA  . ILE A 181 ? 0.48952 0.46138 0.43656 0.01338  -0.02605 -0.09271 178 ILE A CA  
1388 C C   . ILE A 181 ? 0.49877 0.47520 0.45132 0.01685  -0.02432 -0.08939 178 ILE A C   
1389 O O   . ILE A 181 ? 0.50835 0.48369 0.45730 0.01760  -0.02276 -0.08885 178 ILE A O   
1390 C CB  . ILE A 181 ? 0.54456 0.50714 0.48442 0.01264  -0.02071 -0.09520 178 ILE A CB  
1391 C CG1 . ILE A 181 ? 0.57311 0.53066 0.50547 0.00809  -0.02277 -0.09887 178 ILE A CG1 
1392 C CG2 . ILE A 181 ? 0.54967 0.51045 0.49614 0.01546  -0.01611 -0.09404 178 ILE A CG2 
1393 C CD1 . ILE A 181 ? 0.58433 0.53144 0.50804 0.00636  -0.01670 -0.10220 178 ILE A CD1 
1394 N N   . LEU A 182 ? 0.46429 0.44536 0.42460 0.01816  -0.02459 -0.08726 179 LEU A N   
1395 C CA  . LEU A 182 ? 0.45833 0.44444 0.42423 0.02063  -0.02390 -0.08399 179 LEU A CA  
1396 C C   . LEU A 182 ? 0.48470 0.46897 0.45506 0.02281  -0.02100 -0.08187 179 LEU A C   
1397 O O   . LEU A 182 ? 0.52229 0.50420 0.49349 0.02188  -0.02136 -0.08161 179 LEU A O   
1398 C CB  . LEU A 182 ? 0.47758 0.47044 0.44818 0.01942  -0.02728 -0.08294 179 LEU A CB  
1399 C CG  . LEU A 182 ? 0.49307 0.48933 0.46357 0.01870  -0.03025 -0.08358 179 LEU A CG  
1400 C CD1 . LEU A 182 ? 0.47171 0.46565 0.43921 0.01659  -0.03331 -0.08628 179 LEU A CD1 
1401 C CD2 . LEU A 182 ? 0.47810 0.48054 0.45499 0.01788  -0.03146 -0.08269 179 LEU A CD2 
1402 N N   . TYR A 183 ? 0.44938 0.43457 0.42339 0.02555  -0.01829 -0.08019 180 TYR A N   
1403 C CA  . TYR A 183 ? 0.40891 0.39345 0.39049 0.02831  -0.01648 -0.07739 180 TYR A CA  
1404 C C   . TYR A 183 ? 0.42851 0.42072 0.41679 0.02912  -0.01927 -0.07335 180 TYR A C   
1405 O O   . TYR A 183 ? 0.45081 0.44753 0.43996 0.02938  -0.01897 -0.07330 180 TYR A O   
1406 C CB  . TYR A 183 ? 0.40488 0.38474 0.38847 0.03071  -0.01054 -0.07909 180 TYR A CB  
1407 C CG  . TYR A 183 ? 0.48255 0.45363 0.45795 0.02891  -0.00729 -0.08347 180 TYR A CG  
1408 C CD1 . TYR A 183 ? 0.55002 0.51492 0.52695 0.02935  -0.00574 -0.08383 180 TYR A CD1 
1409 C CD2 . TYR A 183 ? 0.50225 0.47046 0.46736 0.02613  -0.00629 -0.08702 180 TYR A CD2 
1410 C CE1 . TYR A 183 ? 0.56293 0.51943 0.53174 0.02695  -0.00253 -0.08831 180 TYR A CE1 
1411 C CE2 . TYR A 183 ? 0.49607 0.45595 0.45220 0.02337  -0.00394 -0.09110 180 TYR A CE2 
1412 C CZ  . TYR A 183 ? 0.53915 0.49342 0.49734 0.02373  -0.00173 -0.09206 180 TYR A CZ  
1413 O OH  . TYR A 183 ? 0.54972 0.49539 0.49844 0.02031  0.00088  -0.09657 180 TYR A OH  
1414 N N   . ASP A 184 ? 0.44494 0.43781 0.43680 0.02886  -0.02213 -0.06987 181 ASP A N   
1415 C CA  . ASP A 184 ? 0.40821 0.40756 0.40472 0.02835  -0.02565 -0.06580 181 ASP A CA  
1416 C C   . ASP A 184 ? 0.36746 0.36883 0.37481 0.03213  -0.02505 -0.06243 181 ASP A C   
1417 O O   . ASP A 184 ? 0.39471 0.39122 0.40701 0.03513  -0.02230 -0.06243 181 ASP A O   
1418 C CB  . ASP A 184 ? 0.39806 0.39605 0.39098 0.02487  -0.02948 -0.06349 181 ASP A CB  
1419 C CG  . ASP A 184 ? 0.44457 0.44861 0.43744 0.02191  -0.03299 -0.06088 181 ASP A CG  
1420 O OD1 . ASP A 184 ? 0.46918 0.47810 0.46169 0.02123  -0.03220 -0.06290 181 ASP A OD1 
1421 O OD2 . ASP A 184 ? 0.51814 0.52117 0.51033 0.01972  -0.03662 -0.05677 181 ASP A OD2 
1422 N N   . ASN A 185 ? 0.37474 0.38346 0.38701 0.03184  -0.02736 -0.05988 182 ASN A N   
1423 C CA  . ASN A 185 ? 0.42627 0.43930 0.45144 0.03484  -0.02830 -0.05604 182 ASN A CA  
1424 C C   . ASN A 185 ? 0.38818 0.40108 0.42105 0.03864  -0.02178 -0.05892 182 ASN A C   
1425 O O   . ASN A 185 ? 0.40492 0.41952 0.45147 0.04211  -0.02102 -0.05662 182 ASN A O   
1426 C CB  . ASN A 185 ? 0.46348 0.47318 0.49426 0.03609  -0.03233 -0.05105 182 ASN A CB  
1427 C CG  . ASN A 185 ? 0.57776 0.58619 0.59924 0.03118  -0.03826 -0.04804 182 ASN A CG  
1428 O OD1 . ASN A 185 ? 0.63906 0.64107 0.65132 0.02900  -0.03762 -0.04980 182 ASN A OD1 
1429 N ND2 . ASN A 185 ? 0.59261 0.60681 0.61597 0.02866  -0.04374 -0.04380 182 ASN A ND2 
1430 N N   . THR A 186 ? 0.36856 0.37923 0.39341 0.03769  -0.01702 -0.06386 183 THR A N   
1431 C CA  . THR A 186 ? 0.42524 0.43341 0.45412 0.03992  -0.00963 -0.06733 183 THR A CA  
1432 C C   . THR A 186 ? 0.43942 0.45504 0.47978 0.04120  -0.00776 -0.06632 183 THR A C   
1433 O O   . THR A 186 ? 0.46388 0.47784 0.51088 0.04308  -0.00072 -0.06912 183 THR A O   
1434 C CB  . THR A 186 ? 0.41835 0.42092 0.43284 0.03736  -0.00608 -0.07226 183 THR A CB  
1435 O OG1 . THR A 186 ? 0.41989 0.42666 0.42749 0.03461  -0.00972 -0.07182 183 THR A OG1 
1436 C CG2 . THR A 186 ? 0.41865 0.41357 0.42461 0.03633  -0.00662 -0.07409 183 THR A CG2 
1437 N N   . LEU A 187 ? 0.40697 0.43042 0.44988 0.03966  -0.01318 -0.06294 184 LEU A N   
1438 C CA  . LEU A 187 ? 0.42719 0.45871 0.48295 0.04055  -0.01237 -0.06151 184 LEU A CA  
1439 C C   . LEU A 187 ? 0.42692 0.46379 0.49891 0.04296  -0.01757 -0.05611 184 LEU A C   
1440 O O   . LEU A 187 ? 0.48184 0.52593 0.56862 0.04437  -0.01682 -0.05492 184 LEU A O   
1441 C CB  . LEU A 187 ? 0.40689 0.44368 0.45601 0.03679  -0.01499 -0.06126 184 LEU A CB  
1442 C CG  . LEU A 187 ? 0.40599 0.43819 0.44180 0.03468  -0.01047 -0.06565 184 LEU A CG  
1443 C CD1 . LEU A 187 ? 0.41405 0.45108 0.44569 0.03138  -0.01307 -0.06497 184 LEU A CD1 
1444 C CD2 . LEU A 187 ? 0.35991 0.38891 0.39845 0.03597  -0.00194 -0.06936 184 LEU A CD2 
1445 N N   . TRP A 188 ? 0.42272 0.45605 0.49245 0.04313  -0.02313 -0.05262 185 TRP A N   
1446 C CA  . TRP A 188 ? 0.40736 0.44352 0.49070 0.04520  -0.02954 -0.04637 185 TRP A CA  
1447 C C   . TRP A 188 ? 0.42086 0.46777 0.51497 0.04395  -0.03496 -0.04237 185 TRP A C   
1448 O O   . TRP A 188 ? 0.40640 0.45885 0.52007 0.04747  -0.03451 -0.04062 185 TRP A O   
1449 C CB  . TRP A 188 ? 0.43951 0.47191 0.53795 0.05078  -0.02452 -0.04704 185 TRP A CB  
1450 C CG  . TRP A 188 ? 0.49548 0.52633 0.60431 0.05320  -0.03169 -0.04030 185 TRP A CG  
1451 C CD1 . TRP A 188 ? 0.48271 0.51805 0.61453 0.05766  -0.03395 -0.03610 185 TRP A CD1 
1452 C CD2 . TRP A 188 ? 0.49635 0.52020 0.59335 0.05103  -0.03785 -0.03662 185 TRP A CD2 
1453 N NE1 . TRP A 188 ? 0.48291 0.51387 0.61731 0.05861  -0.04201 -0.02933 185 TRP A NE1 
1454 C CE2 . TRP A 188 ? 0.48199 0.50541 0.59406 0.05423  -0.04414 -0.02967 185 TRP A CE2 
1455 C CE3 . TRP A 188 ? 0.51206 0.52988 0.58814 0.04652  -0.03851 -0.03857 185 TRP A CE3 
1456 C CZ2 . TRP A 188 ? 0.45634 0.47228 0.56059 0.05257  -0.05100 -0.02437 185 TRP A CZ2 
1457 C CZ3 . TRP A 188 ? 0.51909 0.53031 0.58847 0.04473  -0.04433 -0.03414 185 TRP A CZ3 
1458 C CH2 . TRP A 188 ? 0.48901 0.49872 0.57114 0.04751  -0.05048 -0.02698 185 TRP A CH2 
1459 N N   . PHE A 189 ? 0.41670 0.46667 0.49911 0.03867  -0.03971 -0.04133 186 PHE A N   
1460 C CA  . PHE A 189 ? 0.42694 0.48642 0.51614 0.03584  -0.04563 -0.03765 186 PHE A CA  
1461 C C   . PHE A 189 ? 0.47561 0.54252 0.57782 0.03759  -0.04004 -0.04056 186 PHE A C   
1462 O O   . PHE A 189 ? 0.50911 0.58507 0.62324 0.03645  -0.04451 -0.03739 186 PHE A O   
1463 C CB  . PHE A 189 ? 0.45169 0.51346 0.55163 0.03637  -0.05532 -0.02985 186 PHE A CB  
1464 C CG  . PHE A 189 ? 0.52173 0.57498 0.60784 0.03384  -0.06064 -0.02662 186 PHE A CG  
1465 C CD1 . PHE A 189 ? 0.54148 0.59415 0.61210 0.02665  -0.06659 -0.02453 186 PHE A CD1 
1466 C CD2 . PHE A 189 ? 0.52051 0.56549 0.60847 0.03796  -0.05874 -0.02620 186 PHE A CD2 
1467 C CE1 . PHE A 189 ? 0.54047 0.58458 0.59755 0.02340  -0.07042 -0.02205 186 PHE A CE1 
1468 C CE2 . PHE A 189 ? 0.53603 0.57258 0.61075 0.03505  -0.06307 -0.02340 186 PHE A CE2 
1469 C CZ  . PHE A 189 ? 0.52312 0.55925 0.58224 0.02765  -0.06882 -0.02133 186 PHE A CZ  
1470 N N   . GLY A 190 ? 0.45275 0.51560 0.55210 0.03959  -0.03034 -0.04660 187 GLY A N   
1471 C CA  . GLY A 190 ? 0.42642 0.49434 0.53575 0.04046  -0.02342 -0.05009 187 GLY A CA  
1472 C C   . GLY A 190 ? 0.44970 0.51991 0.58088 0.04562  -0.01881 -0.05047 187 GLY A C   
1473 O O   . GLY A 190 ? 0.41855 0.49133 0.55750 0.04612  -0.01063 -0.05471 187 GLY A O   
1474 N N   . SER A 191 ? 0.46784 0.53641 0.60946 0.04929  -0.02315 -0.04641 188 SER A N   
1475 C CA  . SER A 191 ? 0.47488 0.54643 0.64166 0.05468  -0.01932 -0.04628 188 SER A CA  
1476 C C   . SER A 191 ? 0.49453 0.55781 0.66046 0.05710  -0.00611 -0.05362 188 SER A C   
1477 O O   . SER A 191 ? 0.42791 0.49348 0.61519 0.06096  0.00038  -0.05562 188 SER A O   
1478 C CB  . SER A 191 ? 0.43335 0.50401 0.61114 0.05795  -0.02841 -0.03915 188 SER A CB  
1479 O OG  . SER A 191 ? 0.40334 0.46229 0.56485 0.05814  -0.02810 -0.03961 188 SER A OG  
1480 N N   . VAL A 192 ? 0.46054 0.51416 0.60290 0.05450  -0.00198 -0.05781 189 VAL A N   
1481 C CA  . VAL A 192 ? 0.44644 0.49101 0.58420 0.05525  0.01005  -0.06487 189 VAL A CA  
1482 C C   . VAL A 192 ? 0.46002 0.50744 0.60084 0.05328  0.01960  -0.07022 189 VAL A C   
1483 O O   . VAL A 192 ? 0.43047 0.47130 0.57215 0.05358  0.03095  -0.07629 189 VAL A O   
1484 C CB  . VAL A 192 ? 0.42402 0.45804 0.53536 0.05224  0.01018  -0.06730 189 VAL A CB  
1485 C CG1 . VAL A 192 ? 0.42356 0.45356 0.53191 0.05371  0.00251  -0.06289 189 VAL A CG1 
1486 C CG2 . VAL A 192 ? 0.40886 0.44521 0.50320 0.04746  0.00693  -0.06744 189 VAL A CG2 
1487 N N   . ALA A 193 ? 0.44904 0.50530 0.59064 0.05055  0.01586  -0.06843 190 ALA A N   
1488 C CA  . ALA A 193 ? 0.47308 0.53076 0.61338 0.04751  0.02469  -0.07340 190 ALA A CA  
1489 C C   . ALA A 193 ? 0.49600 0.55887 0.66206 0.05014  0.03345  -0.07641 190 ALA A C   
1490 O O   . ALA A 193 ? 0.50252 0.56446 0.66719 0.04721  0.04339  -0.08177 190 ALA A O   
1491 C CB  . ALA A 193 ? 0.46190 0.52734 0.59676 0.04372  0.01812  -0.07056 190 ALA A CB  
1492 N N   . TYR A 194 ? 0.49812 0.56597 0.68808 0.05536  0.03026  -0.07312 191 TYR A N   
1493 C CA  . TYR A 194 ? 0.54677 0.62096 0.76597 0.05843  0.03822  -0.07584 191 TYR A CA  
1494 C C   . TYR A 194 ? 0.57838 0.64520 0.80973 0.06342  0.04431  -0.07797 191 TYR A C   
1495 O O   . TYR A 194 ? 0.63049 0.69116 0.85419 0.06558  0.03775  -0.07433 191 TYR A O   
1496 C CB  . TYR A 194 ? 0.55800 0.64772 0.80242 0.06044  0.02797  -0.06929 191 TYR A CB  
1497 C CG  . TYR A 194 ? 0.55944 0.65613 0.79146 0.05522  0.02035  -0.06647 191 TYR A CG  
1498 C CD1 . TYR A 194 ? 0.56922 0.66600 0.78593 0.05349  0.00720  -0.06015 191 TYR A CD1 
1499 C CD2 . TYR A 194 ? 0.53942 0.64173 0.77469 0.05148  0.02720  -0.07060 191 TYR A CD2 
1500 C CE1 . TYR A 194 ? 0.58898 0.69118 0.79449 0.04833  0.00133  -0.05829 191 TYR A CE1 
1501 C CE2 . TYR A 194 ? 0.54023 0.64799 0.76424 0.04653  0.02078  -0.06831 191 TYR A CE2 
1502 C CZ  . TYR A 194 ? 0.61441 0.72208 0.82391 0.04506  0.00797  -0.06229 191 TYR A CZ  
1503 O OH  . TYR A 194 ? 0.71712 0.82933 0.91558 0.03976  0.00265  -0.06071 191 TYR A OH  
1504 N N   . PRO A 195 ? 0.59351 0.66005 0.84379 0.06491  0.05774  -0.08436 192 PRO A N   
1505 C CA  . PRO A 195 ? 0.57599 0.63521 0.84072 0.06983  0.06455  -0.08686 192 PRO A CA  
1506 C C   . PRO A 195 ? 0.51050 0.57607 0.79919 0.07655  0.05249  -0.07836 192 PRO A C   
1507 O O   . PRO A 195 ? 0.48069 0.53724 0.76878 0.07990  0.05200  -0.07732 192 PRO A O   
1508 C CB  . PRO A 195 ? 0.60110 0.66185 0.88613 0.06955  0.08125  -0.09530 192 PRO A CB  
1509 C CG  . PRO A 195 ? 0.61985 0.68155 0.88551 0.06239  0.08576  -0.09909 192 PRO A CG  
1510 C CD  . PRO A 195 ? 0.59399 0.66464 0.85035 0.06127  0.06914  -0.09067 192 PRO A CD  
1511 N N   . GLU A 196 ? 0.47424 0.55449 0.78316 0.07807  0.04225  -0.07194 193 GLU A N   
1512 C CA  . GLU A 196 ? 0.51251 0.59911 0.84380 0.08366  0.02879  -0.06258 193 GLU A CA  
1513 C C   . GLU A 196 ? 0.46932 0.56506 0.79121 0.08043  0.01201  -0.05407 193 GLU A C   
1514 O O   . GLU A 196 ? 0.44624 0.54782 0.75719 0.07522  0.01224  -0.05589 193 GLU A O   
1515 C CB  . GLU A 196 ? 0.59215 0.68860 0.96716 0.08944  0.03306  -0.06296 193 GLU A CB  
1516 C CG  . GLU A 196 ? 0.69806 0.78489 1.09016 0.09524  0.04361  -0.06701 193 GLU A CG  
1517 C CD  . GLU A 196 ? 0.81517 0.89475 1.20511 0.09948  0.03201  -0.05888 193 GLU A CD  
1518 O OE1 . GLU A 196 ? 0.85700 0.92428 1.24826 0.10254  0.04074  -0.06276 193 GLU A OE1 
1519 O OE2 . GLU A 196 ? 0.85696 0.94221 1.24270 0.09907  0.01456  -0.04880 193 GLU A OE2 
1520 N N   . TYR A 197 ? 0.48274 0.57861 0.80802 0.08297  -0.00222 -0.04486 194 TYR A N   
1521 C CA  . TYR A 197 ? 0.45581 0.55843 0.76974 0.07888  -0.01817 -0.03679 194 TYR A CA  
1522 C C   . TYR A 197 ? 0.44261 0.55012 0.77798 0.08285  -0.03304 -0.02614 194 TYR A C   
1523 O O   . TYR A 197 ? 0.42447 0.52226 0.75375 0.08524  -0.03795 -0.02181 194 TYR A O   
1524 C CB  . TYR A 197 ? 0.40898 0.50104 0.68427 0.07383  -0.02074 -0.03711 194 TYR A CB  
1525 C CG  . TYR A 197 ? 0.39043 0.48885 0.64978 0.06759  -0.03202 -0.03249 194 TYR A CG  
1526 C CD1 . TYR A 197 ? 0.38544 0.48580 0.64365 0.06636  -0.04746 -0.02306 194 TYR A CD1 
1527 C CD2 . TYR A 197 ? 0.37723 0.47871 0.62210 0.06235  -0.02692 -0.03762 194 TYR A CD2 
1528 C CE1 . TYR A 197 ? 0.39032 0.49551 0.63294 0.05965  -0.05671 -0.01962 194 TYR A CE1 
1529 C CE2 . TYR A 197 ? 0.39723 0.50381 0.62832 0.05643  -0.03617 -0.03405 194 TYR A CE2 
1530 C CZ  . TYR A 197 ? 0.40883 0.51732 0.63873 0.05489  -0.05067 -0.02542 194 TYR A CZ  
1531 O OH  . TYR A 197 ? 0.40939 0.52190 0.62431 0.04800  -0.05890 -0.02261 194 TYR A OH  
1532 N N   . PRO A 198 ? 0.42023 0.54223 0.78039 0.08323  -0.04105 -0.02135 195 PRO A N   
1533 C CA  . PRO A 198 ? 0.39735 0.52409 0.78024 0.08706  -0.05638 -0.01037 195 PRO A CA  
1534 C C   . PRO A 198 ? 0.40341 0.52625 0.76075 0.08176  -0.07288 -0.00130 195 PRO A C   
1535 O O   . PRO A 198 ? 0.44059 0.56110 0.76724 0.07467  -0.07362 -0.00329 195 PRO A O   
1536 C CB  . PRO A 198 ? 0.41360 0.55820 0.82881 0.08759  -0.05962 -0.00900 195 PRO A CB  
1537 C CG  . PRO A 198 ? 0.40328 0.55045 0.81710 0.08567  -0.04178 -0.02092 195 PRO A CG  
1538 C CD  . PRO A 198 ? 0.33903 0.47356 0.71073 0.08046  -0.03561 -0.02608 195 PRO A CD  
1539 N N   . GLY A 199 ? 0.40306 0.52436 0.77397 0.08512  -0.08591 0.00878  196 GLY A N   
1540 C CA  . GLY A 199 ? 0.44728 0.56556 0.79852 0.07961  -0.10320 0.01885  196 GLY A CA  
1541 C C   . GLY A 199 ? 0.54637 0.64800 0.86464 0.07711  -0.10281 0.01912  196 GLY A C   
1542 O O   . GLY A 199 ? 0.58626 0.68452 0.88064 0.07015  -0.11406 0.02494  196 GLY A O   
1543 N N   . LEU A 200 ? 0.55246 0.64334 0.86858 0.08187  -0.09004 0.01278  197 LEU A N   
1544 C CA  . LEU A 200 ? 0.51808 0.59375 0.80292 0.07907  -0.08785 0.01141  197 LEU A CA  
1545 C C   . LEU A 200 ? 0.56229 0.62735 0.85458 0.08353  -0.09438 0.01893  197 LEU A C   
1546 O O   . LEU A 200 ? 0.59750 0.66387 0.92086 0.09124  -0.09322 0.02097  197 LEU A O   
1547 C CB  . LEU A 200 ? 0.42477 0.49413 0.69764 0.07993  -0.06984 -0.00078 197 LEU A CB  
1548 C CG  . LEU A 200 ? 0.43716 0.51354 0.69701 0.07496  -0.06263 -0.00841 197 LEU A CG  
1549 C CD1 . LEU A 200 ? 0.43197 0.49918 0.67459 0.07474  -0.04744 -0.01880 197 LEU A CD1 
1550 C CD2 . LEU A 200 ? 0.41979 0.49865 0.65608 0.06686  -0.07330 -0.00422 197 LEU A CD2 
1551 N N   . HIS A 201 ? 0.56948 0.62354 0.83362 0.07843  -0.10072 0.02284  198 HIS A N   
1552 C CA  . HIS A 201 ? 0.60563 0.64599 0.86973 0.08174  -0.10369 0.02798  198 HIS A CA  
1553 C C   . HIS A 201 ? 0.62368 0.65644 0.89554 0.08802  -0.08706 0.01870  198 HIS A C   
1554 O O   . HIS A 201 ? 0.63912 0.67297 0.90062 0.08663  -0.07402 0.00812  198 HIS A O   
1555 C CB  . HIS A 201 ? 0.61114 0.64055 0.83928 0.07364  -0.10977 0.03099  198 HIS A CB  
1556 C CG  . HIS A 201 ? 0.67915 0.69402 0.90477 0.07544  -0.11533 0.03806  198 HIS A CG  
1557 N ND1 . HIS A 201 ? 0.69789 0.70099 0.92286 0.07982  -0.10431 0.03271  198 HIS A ND1 
1558 C CD2 . HIS A 201 ? 0.71826 0.72738 0.94009 0.07269  -0.13083 0.05018  198 HIS A CD2 
1559 C CE1 . HIS A 201 ? 0.72621 0.71710 0.94839 0.08018  -0.11235 0.04112  198 HIS A CE1 
1560 N NE2 . HIS A 201 ? 0.72857 0.72250 0.94836 0.07588  -0.12866 0.05207  198 HIS A NE2 
1561 N N   . PRO A 202 ? 0.61257 0.63702 0.90283 0.09465  -0.08726 0.02252  199 PRO A N   
1562 C CA  . PRO A 202 ? 0.58044 0.59635 0.87739 0.09985  -0.07067 0.01312  199 PRO A CA  
1563 C C   . PRO A 202 ? 0.57941 0.58613 0.84312 0.09461  -0.06013 0.00383  199 PRO A C   
1564 O O   . PRO A 202 ? 0.58803 0.59567 0.85109 0.09520  -0.04587 -0.00679 199 PRO A O   
1565 C CB  . PRO A 202 ? 0.55374 0.55889 0.86700 0.10563  -0.07634 0.02112  199 PRO A CB  
1566 C CG  . PRO A 202 ? 0.56231 0.57735 0.89715 0.10724  -0.09330 0.03334  199 PRO A CG  
1567 C CD  . PRO A 202 ? 0.58277 0.60657 0.89372 0.09827  -0.10230 0.03545  199 PRO A CD  
1568 N N   . GLU A 203 ? 0.58237 0.58010 0.81851 0.08900  -0.06679 0.00750  200 GLU A N   
1569 C CA  . GLU A 203 ? 0.59403 0.58393 0.80130 0.08413  -0.05752 -0.00113 200 GLU A CA  
1570 C C   . GLU A 203 ? 0.55034 0.54965 0.74019 0.07817  -0.05564 -0.00648 200 GLU A C   
1571 O O   . GLU A 203 ? 0.51736 0.51249 0.68804 0.07502  -0.04677 -0.01472 200 GLU A O   
1572 C CB  . GLU A 203 ? 0.70200 0.67891 0.88770 0.08003  -0.06397 0.00382  200 GLU A CB  
1573 C CG  . GLU A 203 ? 0.81353 0.79276 0.98875 0.07458  -0.07963 0.01408  200 GLU A CG  
1574 C CD  . GLU A 203 ? 0.91417 0.87861 1.07549 0.07196  -0.08612 0.02072  200 GLU A CD  
1575 O OE1 . GLU A 203 ? 0.94867 0.90159 1.10866 0.07455  -0.07810 0.01688  200 GLU A OE1 
1576 O OE2 . GLU A 203 ? 0.94695 0.91051 1.09765 0.06664  -0.09897 0.02963  200 GLU A OE2 
1577 N N   . GLU A 204 ? 0.54570 0.55728 0.74218 0.07640  -0.06408 -0.00183 201 GLU A N   
1578 C CA  . GLU A 204 ? 0.51243 0.53352 0.69893 0.07224  -0.06000 -0.00787 201 GLU A CA  
1579 C C   . GLU A 204 ? 0.50387 0.52868 0.70462 0.07642  -0.04629 -0.01680 201 GLU A C   
1580 O O   . GLU A 204 ? 0.44698 0.47229 0.63260 0.07325  -0.03800 -0.02466 201 GLU A O   
1581 C CB  . GLU A 204 ? 0.52716 0.56019 0.71933 0.06920  -0.07176 -0.00104 201 GLU A CB  
1582 C CG  . GLU A 204 ? 0.52397 0.55541 0.68919 0.06068  -0.08032 0.00229  201 GLU A CG  
1583 C CD  . GLU A 204 ? 0.52450 0.56749 0.69474 0.05682  -0.09111 0.00817  201 GLU A CD  
1584 O OE1 . GLU A 204 ? 0.48030 0.53018 0.67581 0.06095  -0.09759 0.01414  201 GLU A OE1 
1585 O OE2 . GLU A 204 ? 0.51884 0.56409 0.66880 0.04951  -0.09297 0.00659  201 GLU A OE2 
1586 N N   . GLU A 205 ? 0.51016 0.53699 0.74034 0.08326  -0.04360 -0.01565 202 GLU A N   
1587 C CA  . GLU A 205 ? 0.52582 0.55507 0.77056 0.08666  -0.02916 -0.02465 202 GLU A CA  
1588 C C   . GLU A 205 ? 0.53123 0.54711 0.76219 0.08670  -0.01641 -0.03306 202 GLU A C   
1589 O O   . GLU A 205 ? 0.51527 0.53081 0.74142 0.08538  -0.00419 -0.04217 202 GLU A O   
1590 C CB  . GLU A 205 ? 0.53053 0.56590 0.81344 0.09390  -0.02951 -0.02128 202 GLU A CB  
1591 C CG  . GLU A 205 ? 0.57009 0.60756 0.87099 0.09713  -0.01313 -0.03109 202 GLU A CG  
1592 C CD  . GLU A 205 ? 0.59802 0.64650 0.89504 0.09303  -0.00872 -0.03622 202 GLU A CD  
1593 O OE1 . GLU A 205 ? 0.61676 0.67289 0.90192 0.08855  -0.01913 -0.03159 202 GLU A OE1 
1594 O OE2 . GLU A 205 ? 0.60638 0.65494 0.91153 0.09377  0.00578  -0.04516 202 GLU A OE2 
1595 N N   . VAL A 206 ? 0.56203 0.56618 0.78543 0.08748  -0.01915 -0.03013 203 VAL A N   
1596 C CA  . VAL A 206 ? 0.54048 0.53165 0.74871 0.08644  -0.00802 -0.03802 203 VAL A CA  
1597 C C   . VAL A 206 ? 0.50315 0.49374 0.68079 0.07943  -0.00590 -0.04347 203 VAL A C   
1598 O O   . VAL A 206 ? 0.49347 0.47960 0.66140 0.07761  0.00534  -0.05232 203 VAL A O   
1599 C CB  . VAL A 206 ? 0.54292 0.52173 0.74910 0.08815  -0.01241 -0.03308 203 VAL A CB  
1600 C CG1 . VAL A 206 ? 0.52898 0.49474 0.71467 0.08526  -0.00242 -0.04120 203 VAL A CG1 
1601 C CG2 . VAL A 206 ? 0.52645 0.50404 0.76534 0.09595  -0.01255 -0.02867 203 VAL A CG2 
1602 N N   . ALA A 207 ? 0.50729 0.50190 0.66958 0.07505  -0.01679 -0.03819 204 ALA A N   
1603 C CA  . ALA A 207 ? 0.51621 0.51097 0.65256 0.06884  -0.01552 -0.04285 204 ALA A CA  
1604 C C   . ALA A 207 ? 0.48403 0.48691 0.62178 0.06778  -0.00909 -0.04842 204 ALA A C   
1605 O O   . ALA A 207 ? 0.49641 0.49571 0.61806 0.06459  -0.00211 -0.05531 204 ALA A O   
1606 C CB  . ALA A 207 ? 0.48615 0.48394 0.60898 0.06428  -0.02751 -0.03637 204 ALA A CB  
1607 N N   . ARG A 208 ? 0.49578 0.50938 0.65266 0.07005  -0.01184 -0.04520 205 ARG A N   
1608 C CA  . ARG A 208 ? 0.47095 0.49218 0.63032 0.06874  -0.00549 -0.05023 205 ARG A CA  
1609 C C   . ARG A 208 ? 0.45912 0.47349 0.61957 0.06979  0.00904  -0.05914 205 ARG A C   
1610 O O   . ARG A 208 ? 0.42715 0.43977 0.57149 0.06582  0.01532  -0.06515 205 ARG A O   
1611 C CB  . ARG A 208 ? 0.42649 0.46020 0.61060 0.07142  -0.01039 -0.04537 205 ARG A CB  
1612 C CG  . ARG A 208 ? 0.41667 0.45933 0.60145 0.06881  -0.00587 -0.04941 205 ARG A CG  
1613 C CD  . ARG A 208 ? 0.43777 0.49310 0.65049 0.07161  -0.00986 -0.04526 205 ARG A CD  
1614 N NE  . ARG A 208 ? 0.46800 0.52292 0.70731 0.07741  -0.00130 -0.04799 205 ARG A NE  
1615 C CZ  . ARG A 208 ? 0.49625 0.55163 0.74291 0.07758  0.01229  -0.05608 205 ARG A CZ  
1616 N NH1 . ARG A 208 ? 0.47305 0.52889 0.70127 0.07232  0.01773  -0.06136 205 ARG A NH1 
1617 N NH2 . ARG A 208 ? 0.50581 0.56040 0.77831 0.08271  0.02082  -0.05895 205 ARG A NH2 
1618 N N   . LEU A 209 ? 0.49403 0.50352 0.67297 0.07472  0.01461  -0.06004 206 LEU A N   
1619 C CA  . LEU A 209 ? 0.51308 0.51447 0.69245 0.07487  0.02963  -0.06921 206 LEU A CA  
1620 C C   . LEU A 209 ? 0.51395 0.50306 0.66542 0.07045  0.03316  -0.07404 206 LEU A C   
1621 O O   . LEU A 209 ? 0.53908 0.52269 0.67794 0.06684  0.04323  -0.08180 206 LEU A O   
1622 C CB  . LEU A 209 ? 0.49826 0.49664 0.70560 0.08128  0.03493  -0.06910 206 LEU A CB  
1623 C CG  . LEU A 209 ? 0.51537 0.52643 0.75517 0.08599  0.03304  -0.06546 206 LEU A CG  
1624 C CD1 . LEU A 209 ? 0.50527 0.51295 0.77429 0.09316  0.03497  -0.06319 206 LEU A CD1 
1625 C CD2 . LEU A 209 ? 0.50812 0.52425 0.75227 0.08373  0.04484  -0.07324 206 LEU A CD2 
1626 N N   . SER A 210 ? 0.49716 0.48155 0.63835 0.07006  0.02480  -0.06949 207 SER A N   
1627 C CA  . SER A 210 ? 0.49308 0.46700 0.60943 0.06563  0.02715  -0.07386 207 SER A CA  
1628 C C   . SER A 210 ? 0.51276 0.49002 0.60767 0.05996  0.02569  -0.07643 207 SER A C   
1629 O O   . SER A 210 ? 0.55888 0.52859 0.63622 0.05592  0.03149  -0.08256 207 SER A O   
1630 C CB  . SER A 210 ? 0.53107 0.50028 0.64215 0.06595  0.01831  -0.06821 207 SER A CB  
1631 O OG  . SER A 210 ? 0.61456 0.57490 0.70317 0.06135  0.02017  -0.07255 207 SER A OG  
1632 N N   . PHE A 211 ? 0.47526 0.46328 0.57141 0.05931  0.01770  -0.07169 208 PHE A N   
1633 C CA  . PHE A 211 ? 0.47406 0.46499 0.55213 0.05444  0.01639  -0.07381 208 PHE A CA  
1634 C C   . PHE A 211 ? 0.50279 0.49420 0.58125 0.05309  0.02596  -0.07953 208 PHE A C   
1635 O O   . PHE A 211 ? 0.50738 0.49462 0.56731 0.04864  0.02871  -0.08362 208 PHE A O   
1636 C CB  . PHE A 211 ? 0.47031 0.47135 0.54908 0.05358  0.00585  -0.06756 208 PHE A CB  
1637 C CG  . PHE A 211 ? 0.47785 0.47637 0.54463 0.05144  -0.00237 -0.06409 208 PHE A CG  
1638 C CD1 . PHE A 211 ? 0.42677 0.42000 0.47440 0.04753  -0.00200 -0.06763 208 PHE A CD1 
1639 C CD2 . PHE A 211 ? 0.50161 0.50277 0.57637 0.05282  -0.01053 -0.05728 208 PHE A CD2 
1640 C CE1 . PHE A 211 ? 0.43580 0.42699 0.47397 0.04518  -0.00835 -0.06526 208 PHE A CE1 
1641 C CE2 . PHE A 211 ? 0.47441 0.47218 0.53679 0.04982  -0.01686 -0.05467 208 PHE A CE2 
1642 C CZ  . PHE A 211 ? 0.44940 0.44250 0.49425 0.04607  -0.01513 -0.05908 208 PHE A CZ  
1643 N N   . ARG A 212 ? 0.48742 0.48360 0.58713 0.05655  0.03102  -0.07977 209 ARG A N   
1644 C CA  . ARG A 212 ? 0.49572 0.49100 0.59612 0.05464  0.04206  -0.08606 209 ARG A CA  
1645 C C   . ARG A 212 ? 0.50411 0.48574 0.59018 0.05161  0.05238  -0.09353 209 ARG A C   
1646 O O   . ARG A 212 ? 0.50987 0.48687 0.57897 0.04647  0.05786  -0.09831 209 ARG A O   
1647 C CB  . ARG A 212 ? 0.51273 0.51556 0.64220 0.05914  0.04655  -0.08557 209 ARG A CB  
1648 C CG  . ARG A 212 ? 0.52405 0.54073 0.66389 0.05951  0.03919  -0.08054 209 ARG A CG  
1649 C CD  . ARG A 212 ? 0.52846 0.55384 0.70035 0.06419  0.04228  -0.07954 209 ARG A CD  
1650 N NE  . ARG A 212 ? 0.54640 0.56845 0.72558 0.06331  0.05758  -0.08772 209 ARG A NE  
1651 C CZ  . ARG A 212 ? 0.54152 0.56716 0.71704 0.05939  0.06359  -0.09152 209 ARG A CZ  
1652 N NH1 . ARG A 212 ? 0.46979 0.50260 0.63520 0.05647  0.05536  -0.08778 209 ARG A NH1 
1653 N NH2 . ARG A 212 ? 0.57261 0.59378 0.75410 0.05788  0.07858  -0.09940 209 ARG A NH2 
1654 N N   . ASN A 213 ? 0.51623 0.49038 0.60768 0.05413  0.05486  -0.09446 210 ASN A N   
1655 C CA  . ASN A 213 ? 0.54403 0.50433 0.61998 0.05034  0.06416  -0.10172 210 ASN A CA  
1656 C C   . ASN A 213 ? 0.56670 0.52217 0.61480 0.04492  0.05787  -0.10185 210 ASN A C   
1657 O O   . ASN A 213 ? 0.58000 0.52708 0.60904 0.03920  0.06369  -0.10750 210 ASN A O   
1658 C CB  . ASN A 213 ? 0.56375 0.51695 0.65306 0.05441  0.06798  -0.10243 210 ASN A CB  
1659 C CG  . ASN A 213 ? 0.60532 0.56100 0.72333 0.05940  0.07708  -0.10426 210 ASN A CG  
1660 O OD1 . ASN A 213 ? 0.61059 0.56835 0.73309 0.05769  0.08606  -0.10896 210 ASN A OD1 
1661 N ND2 . ASN A 213 ? 0.57108 0.52626 0.70950 0.06548  0.07489  -0.10049 210 ASN A ND2 
1662 N N   . LEU A 214 ? 0.57012 0.53059 0.61573 0.04617  0.04593  -0.09567 211 LEU A N   
1663 C CA  . LEU A 214 ? 0.55044 0.50748 0.57355 0.04149  0.03981  -0.09583 211 LEU A CA  
1664 C C   . LEU A 214 ? 0.54946 0.50905 0.55857 0.03716  0.03891  -0.09699 211 LEU A C   
1665 O O   . LEU A 214 ? 0.59076 0.54321 0.58035 0.03204  0.03944  -0.10033 211 LEU A O   
1666 C CB  . LEU A 214 ? 0.53239 0.49500 0.55780 0.04337  0.02843  -0.08937 211 LEU A CB  
1667 C CG  . LEU A 214 ? 0.53038 0.49121 0.53670 0.03894  0.02193  -0.08950 211 LEU A CG  
1668 C CD1 . LEU A 214 ? 0.50903 0.45875 0.50538 0.03651  0.02513  -0.09365 211 LEU A CD1 
1669 C CD2 . LEU A 214 ? 0.55036 0.51899 0.55977 0.03995  0.01176  -0.08343 211 LEU A CD2 
1670 N N   . ASN A 215 ? 0.50626 0.47560 0.52504 0.03885  0.03701  -0.09396 212 ASN A N   
1671 C CA  . ASN A 215 ? 0.50040 0.47173 0.50647 0.03492  0.03572  -0.09438 212 ASN A CA  
1672 C C   . ASN A 215 ? 0.49873 0.46071 0.49321 0.03041  0.04611  -0.10070 212 ASN A C   
1673 O O   . ASN A 215 ? 0.56448 0.52155 0.53947 0.02532  0.04459  -0.10192 212 ASN A O   
1674 C CB  . ASN A 215 ? 0.48620 0.46942 0.50600 0.03734  0.03244  -0.09023 212 ASN A CB  
1675 C CG  . ASN A 215 ? 0.48005 0.47131 0.50696 0.03998  0.02181  -0.08406 212 ASN A CG  
1676 O OD1 . ASN A 215 ? 0.46670 0.45498 0.48488 0.03915  0.01632  -0.08293 212 ASN A OD1 
1677 N ND2 . ASN A 215 ? 0.43166 0.43288 0.47401 0.04243  0.01904  -0.08027 212 ASN A ND2 
1678 N N   . THR A 216 ? 0.51251 0.47132 0.51879 0.03181  0.05682  -0.10474 213 THR A N   
1679 C CA  . THR A 216 ? 0.54049 0.48860 0.53436 0.02637  0.06847  -0.11175 213 THR A CA  
1680 C C   . THR A 216 ? 0.58236 0.51766 0.55505 0.02145  0.06922  -0.11546 213 THR A C   
1681 O O   . THR A 216 ? 0.64542 0.57188 0.59624 0.01452  0.07194  -0.11879 213 THR A O   
1682 C CB  . THR A 216 ? 0.55125 0.49914 0.56585 0.02917  0.08093  -0.11596 213 THR A CB  
1683 O OG1 . THR A 216 ? 0.55557 0.51605 0.58970 0.03285  0.07976  -0.11264 213 THR A OG1 
1684 C CG2 . THR A 216 ? 0.53378 0.46890 0.53407 0.02236  0.09487  -0.12434 213 THR A CG2 
1685 N N   . PHE A 217 ? 0.56191 0.49559 0.53994 0.02437  0.06628  -0.11467 214 PHE A N   
1686 C CA  . PHE A 217 ? 0.59655 0.51852 0.55572 0.01944  0.06683  -0.11842 214 PHE A CA  
1687 C C   . PHE A 217 ? 0.62991 0.55227 0.56911 0.01515  0.05585  -0.11559 214 PHE A C   
1688 O O   . PHE A 217 ? 0.64432 0.55680 0.56204 0.00821  0.05700  -0.11913 214 PHE A O   
1689 C CB  . PHE A 217 ? 0.61525 0.53593 0.58608 0.02373  0.06574  -0.11766 214 PHE A CB  
1690 C CG  . PHE A 217 ? 0.69705 0.60613 0.64989 0.01850  0.06628  -0.12172 214 PHE A CG  
1691 C CD1 . PHE A 217 ? 0.69167 0.60257 0.63327 0.01665  0.05504  -0.11858 214 PHE A CD1 
1692 C CD2 . PHE A 217 ? 0.70810 0.60444 0.65601 0.01499  0.07852  -0.12917 214 PHE A CD2 
1693 C CE1 . PHE A 217 ? 0.71728 0.61833 0.64335 0.01140  0.05505  -0.12240 214 PHE A CE1 
1694 C CE2 . PHE A 217 ? 0.71989 0.60533 0.65041 0.00934  0.07886  -0.13316 214 PHE A CE2 
1695 C CZ  . PHE A 217 ? 0.72005 0.60826 0.63979 0.00756  0.06663  -0.12957 214 PHE A CZ  
1696 N N   . LEU A 218 ? 0.59747 0.53092 0.54387 0.01888  0.04500  -0.10924 215 LEU A N   
1697 C CA  . LEU A 218 ? 0.57753 0.51221 0.50930 0.01567  0.03463  -0.10657 215 LEU A CA  
1698 C C   . LEU A 218 ? 0.59322 0.52469 0.50970 0.01065  0.03501  -0.10716 215 LEU A C   
1699 O O   . LEU A 218 ? 0.56521 0.49128 0.46395 0.00557  0.02963  -0.10729 215 LEU A O   
1700 C CB  . LEU A 218 ? 0.49277 0.43947 0.43681 0.02039  0.02494  -0.10049 215 LEU A CB  
1701 C CG  . LEU A 218 ? 0.49970 0.44792 0.45296 0.02357  0.02176  -0.09900 215 LEU A CG  
1702 C CD1 . LEU A 218 ? 0.47423 0.43342 0.43730 0.02682  0.01315  -0.09330 215 LEU A CD1 
1703 C CD2 . LEU A 218 ? 0.46442 0.40479 0.40376 0.01931  0.01952  -0.10185 215 LEU A CD2 
1704 N N   . ALA A 219 ? 0.59756 0.53200 0.52087 0.01170  0.04096  -0.10728 216 ALA A N   
1705 C CA  . ALA A 219 ? 0.59296 0.52311 0.50102 0.00651  0.04204  -0.10764 216 ALA A CA  
1706 C C   . ALA A 219 ? 0.66176 0.57679 0.54832 -0.00129 0.04912  -0.11329 216 ALA A C   
1707 O O   . ALA A 219 ? 0.71049 0.61889 0.57726 -0.00736 0.04627  -0.11273 216 ALA A O   
1708 C CB  . ALA A 219 ? 0.55348 0.49003 0.47477 0.00891  0.04815  -0.10721 216 ALA A CB  
1709 N N   . ALA A 220 ? 0.65413 0.56263 0.54347 -0.00174 0.05826  -0.11865 217 ALA A N   
1710 C CA  . ALA A 220 ? 0.68132 0.57426 0.54929 -0.01016 0.06632  -0.12500 217 ALA A CA  
1711 C C   . ALA A 220 ? 0.67249 0.55873 0.52655 -0.01380 0.06011  -0.12596 217 ALA A C   
1712 O O   . ALA A 220 ? 0.69869 0.57141 0.53071 -0.02231 0.06429  -0.13061 217 ALA A O   
1713 C CB  . ALA A 220 ? 0.67835 0.56641 0.55743 -0.00956 0.08243  -0.13174 217 ALA A CB  
1714 N N   . ASP A 221 ? 0.63547 0.53034 0.50094 -0.00845 0.05055  -0.12194 218 ASP A N   
1715 C CA  . ASP A 221 ? 0.64193 0.53190 0.49783 -0.01146 0.04500  -0.12310 218 ASP A CA  
1716 C C   . ASP A 221 ? 0.65476 0.54035 0.48844 -0.01848 0.03507  -0.12117 218 ASP A C   
1717 O O   . ASP A 221 ? 0.63075 0.52519 0.46809 -0.01593 0.02429  -0.11534 218 ASP A O   
1718 C CB  . ASP A 221 ? 0.66259 0.56357 0.53739 -0.00412 0.03764  -0.11899 218 ASP A CB  
1719 C CG  . ASP A 221 ? 0.67871 0.57459 0.54748 -0.00675 0.03453  -0.12120 218 ASP A CG  
1720 O OD1 . ASP A 221 ? 0.70973 0.59494 0.55859 -0.01457 0.03523  -0.12508 218 ASP A OD1 
1721 O OD2 . ASP A 221 ? 0.67481 0.57691 0.55810 -0.00159 0.03135  -0.11904 218 ASP A OD2 
1722 N N   . PRO A 222 ? 0.68216 0.55404 0.49313 -0.02753 0.03791  -0.12572 219 PRO A N   
1723 C CA  . PRO A 222 ? 0.70178 0.56910 0.49140 -0.03464 0.02686  -0.12293 219 PRO A CA  
1724 C C   . PRO A 222 ? 0.72208 0.59560 0.51497 -0.03362 0.01354  -0.11975 219 PRO A C   
1725 O O   . PRO A 222 ? 0.73651 0.60955 0.51782 -0.03767 0.00203  -0.11598 219 PRO A O   
1726 C CB  . PRO A 222 ? 0.70264 0.55235 0.46661 -0.04549 0.03523  -0.12947 219 PRO A CB  
1727 C CG  . PRO A 222 ? 0.72203 0.56839 0.49612 -0.04351 0.04718  -0.13597 219 PRO A CG  
1728 C CD  . PRO A 222 ? 0.70399 0.56328 0.50767 -0.03216 0.05118  -0.13364 219 PRO A CD  
1729 N N   . ARG A 223 ? 0.69978 0.57887 0.50874 -0.02853 0.01464  -0.12099 220 ARG A N   
1730 C CA  . ARG A 223 ? 0.67413 0.55931 0.48755 -0.02794 0.00337  -0.11873 220 ARG A CA  
1731 C C   . ARG A 223 ? 0.69719 0.59619 0.52516 -0.02192 -0.00708 -0.11210 220 ARG A C   
1732 O O   . ARG A 223 ? 0.71666 0.62109 0.54845 -0.02209 -0.01693 -0.11017 220 ARG A O   
1733 C CB  . ARG A 223 ? 0.65599 0.54175 0.48152 -0.02473 0.00870  -0.12206 220 ARG A CB  
1734 C CG  . ARG A 223 ? 0.68974 0.56119 0.50119 -0.03138 0.01808  -0.12925 220 ARG A CG  
1735 C CD  . ARG A 223 ? 0.67749 0.54904 0.50437 -0.02648 0.02551  -0.13196 220 ARG A CD  
1736 N NE  . ARG A 223 ? 0.67621 0.55344 0.52192 -0.01820 0.03257  -0.13018 220 ARG A NE  
1737 C CZ  . ARG A 223 ? 0.70201 0.57937 0.56363 -0.01276 0.03925  -0.13127 220 ARG A CZ  
1738 N NH1 . ARG A 223 ? 0.67892 0.55021 0.53917 -0.01472 0.04078  -0.13449 220 ARG A NH1 
1739 N NH2 . ARG A 223 ? 0.69757 0.58087 0.57679 -0.00557 0.04397  -0.12888 220 ARG A NH2 
1740 N N   . VAL A 224 ? 0.67168 0.57642 0.50855 -0.01703 -0.00466 -0.10906 221 VAL A N   
1741 C CA  . VAL A 224 ? 0.67476 0.59222 0.52674 -0.01123 -0.01269 -0.10357 221 VAL A CA  
1742 C C   . VAL A 224 ? 0.68462 0.60301 0.53412 -0.01056 -0.01229 -0.10043 221 VAL A C   
1743 O O   . VAL A 224 ? 0.68544 0.59721 0.52770 -0.01248 -0.00332 -0.10270 221 VAL A O   
1744 C CB  . VAL A 224 ? 0.66531 0.59201 0.53836 -0.00391 -0.00953 -0.10298 221 VAL A CB  
1745 C CG1 . VAL A 224 ? 0.67733 0.60405 0.55404 -0.00438 -0.01148 -0.10508 221 VAL A CG1 
1746 C CG2 . VAL A 224 ? 0.62307 0.54754 0.50179 -0.00107 0.00205  -0.10502 221 VAL A CG2 
1747 N N   A GLU A 225 ? 0.67756 0.60390 0.53390 -0.00807 -0.02136 -0.09559 222 GLU A N   
1748 N N   B GLU A 225 ? 0.67695 0.60317 0.53300 -0.00818 -0.02150 -0.09558 222 GLU A N   
1749 C CA  A GLU A 225 ? 0.68603 0.61589 0.54581 -0.00566 -0.02086 -0.09219 222 GLU A CA  
1750 C CA  B GLU A 225 ? 0.68564 0.61580 0.54578 -0.00557 -0.02123 -0.09208 222 GLU A CA  
1751 C C   A GLU A 225 ? 0.65290 0.59498 0.53408 0.00152  -0.01980 -0.09052 222 GLU A C   
1752 C C   B GLU A 225 ? 0.65260 0.59460 0.53402 0.00159  -0.01933 -0.09074 222 GLU A C   
1753 O O   A GLU A 225 ? 0.64487 0.59349 0.53668 0.00402  -0.02419 -0.09007 222 GLU A O   
1754 O O   B GLU A 225 ? 0.64046 0.58864 0.53258 0.00415  -0.02277 -0.09067 222 GLU A O   
1755 C CB  A GLU A 225 ? 0.71459 0.64345 0.56692 -0.00816 -0.03147 -0.08777 222 GLU A CB  
1756 C CB  B GLU A 225 ? 0.71065 0.64119 0.56566 -0.00739 -0.03233 -0.08748 222 GLU A CB  
1757 C CG  A GLU A 225 ? 0.73689 0.67218 0.59779 -0.00703 -0.04223 -0.08590 222 GLU A CG  
1758 C CG  B GLU A 225 ? 0.76617 0.68411 0.59792 -0.01528 -0.03593 -0.08735 222 GLU A CG  
1759 C CD  A GLU A 225 ? 0.77265 0.70384 0.62368 -0.01094 -0.05332 -0.08195 222 GLU A CD  
1760 C CD  B GLU A 225 ? 0.79880 0.71799 0.62904 -0.01669 -0.04990 -0.08243 222 GLU A CD  
1761 O OE1 A GLU A 225 ? 0.77022 0.70733 0.63070 -0.00991 -0.06266 -0.08020 222 GLU A OE1 
1762 O OE1 B GLU A 225 ? 0.77633 0.70635 0.62487 -0.01167 -0.05579 -0.08051 222 GLU A OE1 
1763 O OE2 A GLU A 225 ? 0.79472 0.71645 0.62892 -0.01529 -0.05276 -0.08048 222 GLU A OE2 
1764 O OE2 B GLU A 225 ? 0.82799 0.73689 0.63898 -0.02315 -0.05498 -0.08048 222 GLU A OE2 
1765 N N   . ILE A 226 ? 0.61815 0.56289 0.50495 0.00406  -0.01376 -0.08979 223 ILE A N   
1766 C CA  . ILE A 226 ? 0.55708 0.51212 0.46239 0.00984  -0.01179 -0.08852 223 ILE A CA  
1767 C C   . ILE A 226 ? 0.52265 0.48400 0.43380 0.01173  -0.01436 -0.08492 223 ILE A C   
1768 O O   . ILE A 226 ? 0.53007 0.48697 0.43146 0.00904  -0.01545 -0.08359 223 ILE A O   
1769 C CB  . ILE A 226 ? 0.57010 0.52417 0.48171 0.01177  -0.00174 -0.09124 223 ILE A CB  
1770 C CG1 . ILE A 226 ? 0.57622 0.52669 0.48304 0.01009  0.00531  -0.09212 223 ILE A CG1 
1771 C CG2 . ILE A 226 ? 0.59161 0.53789 0.49729 0.00967  0.00198  -0.09531 223 ILE A CG2 
1772 C CD1 . ILE A 226 ? 0.57940 0.53283 0.49968 0.01339  0.01442  -0.09395 223 ILE A CD1 
1773 N N   . SER A 227 ? 0.50150 0.47243 0.42780 0.01584  -0.01529 -0.08332 224 SER A N   
1774 C CA  . SER A 227 ? 0.51436 0.49180 0.44798 0.01759  -0.01607 -0.08062 224 SER A CA  
1775 C C   . SER A 227 ? 0.50994 0.49559 0.45812 0.02107  -0.01381 -0.08003 224 SER A C   
1776 O O   . SER A 227 ? 0.45479 0.44424 0.40911 0.02229  -0.01710 -0.07966 224 SER A O   
1777 C CB  . SER A 227 ? 0.51272 0.49272 0.44710 0.01728  -0.02394 -0.07831 224 SER A CB  
1778 O OG  . SER A 227 ? 0.51000 0.49624 0.45253 0.01884  -0.02388 -0.07629 224 SER A OG  
1779 N N   . GLN A 228 ? 0.48259 0.47070 0.43613 0.02216  -0.00845 -0.07982 225 GLN A N   
1780 C CA  . GLN A 228 ? 0.46098 0.45716 0.42859 0.02505  -0.00768 -0.07833 225 GLN A CA  
1781 C C   . GLN A 228 ? 0.46347 0.46654 0.43583 0.02490  -0.01121 -0.07585 225 GLN A C   
1782 O O   . GLN A 228 ? 0.45919 0.46198 0.42890 0.02366  -0.00957 -0.07551 225 GLN A O   
1783 C CB  . GLN A 228 ? 0.46450 0.46078 0.43859 0.02635  -0.00041 -0.07951 225 GLN A CB  
1784 C CG  . GLN A 228 ? 0.47066 0.47465 0.46035 0.02950  -0.00104 -0.07731 225 GLN A CG  
1785 C CD  . GLN A 228 ? 0.50531 0.50874 0.50458 0.03157  0.00599  -0.07884 225 GLN A CD  
1786 O OE1 . GLN A 228 ? 0.58199 0.58227 0.57886 0.03025  0.01262  -0.08149 225 GLN A OE1 
1787 N NE2 . GLN A 228 ? 0.43143 0.43730 0.44203 0.03459  0.00486  -0.07720 225 GLN A NE2 
1788 N N   . VAL A 229 ? 0.42977 0.43804 0.40818 0.02550  -0.01541 -0.07441 226 VAL A N   
1789 C CA  . VAL A 229 ? 0.40171 0.41534 0.38336 0.02443  -0.01844 -0.07290 226 VAL A CA  
1790 C C   . VAL A 229 ? 0.38702 0.40759 0.37817 0.02490  -0.01854 -0.07095 226 VAL A C   
1791 O O   . VAL A 229 ? 0.37872 0.40023 0.37342 0.02563  -0.02003 -0.07007 226 VAL A O   
1792 C CB  . VAL A 229 ? 0.43897 0.45210 0.41874 0.02333  -0.02288 -0.07348 226 VAL A CB  
1793 C CG1 . VAL A 229 ? 0.37658 0.39404 0.35988 0.02182  -0.02448 -0.07283 226 VAL A CG1 
1794 C CG2 . VAL A 229 ? 0.43838 0.44494 0.40989 0.02283  -0.02437 -0.07482 226 VAL A CG2 
1795 N N   . SER A 230 ? 0.37514 0.40009 0.36988 0.02398  -0.01751 -0.06998 227 SER A N   
1796 C CA  . SER A 230 ? 0.38083 0.41291 0.38451 0.02362  -0.01860 -0.06776 227 SER A CA  
1797 C C   . SER A 230 ? 0.41178 0.44670 0.41478 0.02079  -0.02275 -0.06687 227 SER A C   
1798 O O   . SER A 230 ? 0.40215 0.44143 0.40715 0.01822  -0.02350 -0.06616 227 SER A O   
1799 C CB  . SER A 230 ? 0.38485 0.42050 0.39264 0.02299  -0.01550 -0.06760 227 SER A CB  
1800 O OG  . SER A 230 ? 0.40666 0.44036 0.40823 0.02085  -0.01509 -0.06859 227 SER A OG  
1801 N N   . ILE A 231 ? 0.36099 0.39285 0.36061 0.02060  -0.02481 -0.06742 228 ILE A N   
1802 C CA  . ILE A 231 ? 0.30816 0.34141 0.30632 0.01716  -0.02752 -0.06727 228 ILE A CA  
1803 C C   . ILE A 231 ? 0.34689 0.38003 0.34647 0.01702  -0.03002 -0.06484 228 ILE A C   
1804 O O   . ILE A 231 ? 0.39229 0.42229 0.39295 0.02005  -0.02950 -0.06446 228 ILE A O   
1805 C CB  . ILE A 231 ? 0.37505 0.40467 0.36893 0.01618  -0.02743 -0.07027 228 ILE A CB  
1806 C CG1 . ILE A 231 ? 0.34344 0.37437 0.33645 0.01170  -0.02825 -0.07121 228 ILE A CG1 
1807 C CG2 . ILE A 231 ? 0.31276 0.33776 0.30429 0.01831  -0.02769 -0.07126 228 ILE A CG2 
1808 C CD1 . ILE A 231 ? 0.38112 0.40984 0.37394 0.01075  -0.02738 -0.07466 228 ILE A CD1 
1809 N N   . GLY A 232 ? 0.33675 0.37234 0.33548 0.01297  -0.03274 -0.06310 229 GLY A N   
1810 C CA  . GLY A 232 ? 0.33646 0.37103 0.33537 0.01212  -0.03624 -0.05966 229 GLY A CA  
1811 C C   . GLY A 232 ? 0.38964 0.42713 0.39774 0.01606  -0.03748 -0.05614 229 GLY A C   
1812 O O   . GLY A 232 ? 0.34696 0.39018 0.36096 0.01583  -0.03816 -0.05465 229 GLY A O   
1813 N N   . ASP A 233 ? 0.41137 0.44491 0.42207 0.01957  -0.03741 -0.05504 230 ASP A N   
1814 C CA  . ASP A 233 ? 0.45321 0.48849 0.47513 0.02425  -0.03687 -0.05280 230 ASP A CA  
1815 C C   . ASP A 233 ? 0.46663 0.49879 0.48955 0.02815  -0.03054 -0.05686 230 ASP A C   
1816 O O   . ASP A 233 ? 0.43919 0.47008 0.47034 0.03204  -0.02813 -0.05645 230 ASP A O   
1817 C CB  . ASP A 233 ? 0.50222 0.53406 0.52736 0.02539  -0.04078 -0.04858 230 ASP A CB  
1818 C CG  . ASP A 233 ? 0.57861 0.61373 0.61942 0.03003  -0.04137 -0.04532 230 ASP A CG  
1819 O OD1 . ASP A 233 ? 0.60711 0.64924 0.65623 0.03068  -0.04049 -0.04533 230 ASP A OD1 
1820 O OD2 . ASP A 233 ? 0.58092 0.61152 0.62690 0.03306  -0.04221 -0.04304 230 ASP A OD2 
1821 N N   . GLY A 234 ? 0.44638 0.47664 0.46106 0.02681  -0.02782 -0.06073 231 GLY A N   
1822 C CA  . GLY A 234 ? 0.40158 0.42730 0.41348 0.02904  -0.02276 -0.06429 231 GLY A CA  
1823 C C   . GLY A 234 ? 0.44316 0.46195 0.44766 0.02897  -0.02259 -0.06640 231 GLY A C   
1824 O O   . GLY A 234 ? 0.43615 0.45209 0.44259 0.02993  -0.02365 -0.06506 231 GLY A O   
1825 N N   . VAL A 235 ? 0.45890 0.47480 0.45533 0.02764  -0.02177 -0.06943 232 VAL A N   
1826 C CA  . VAL A 235 ? 0.42634 0.43633 0.41619 0.02707  -0.02195 -0.07186 232 VAL A CA  
1827 C C   . VAL A 235 ? 0.45191 0.45702 0.43567 0.02743  -0.01879 -0.07464 232 VAL A C   
1828 O O   . VAL A 235 ? 0.45545 0.46154 0.43640 0.02665  -0.01845 -0.07496 232 VAL A O   
1829 C CB  . VAL A 235 ? 0.43556 0.44679 0.42206 0.02417  -0.02533 -0.07273 232 VAL A CB  
1830 C CG1 . VAL A 235 ? 0.45051 0.45660 0.43188 0.02338  -0.02577 -0.07550 232 VAL A CG1 
1831 C CG2 . VAL A 235 ? 0.44889 0.46320 0.43835 0.02229  -0.02767 -0.07041 232 VAL A CG2 
1832 N N   . THR A 236 ? 0.43840 0.43725 0.41896 0.02799  -0.01636 -0.07659 233 THR A N   
1833 C CA  . THR A 236 ? 0.45772 0.45010 0.42933 0.02686  -0.01346 -0.07957 233 THR A CA  
1834 C C   . THR A 236 ? 0.46983 0.45843 0.43374 0.02449  -0.01708 -0.08143 233 THR A C   
1835 O O   . THR A 236 ? 0.48913 0.47524 0.45352 0.02434  -0.01733 -0.08235 233 THR A O   
1836 C CB  . THR A 236 ? 0.43354 0.42072 0.40664 0.02827  -0.00701 -0.08139 233 THR A CB  
1837 O OG1 . THR A 236 ? 0.44901 0.44094 0.43218 0.03056  -0.00380 -0.07979 233 THR A OG1 
1838 C CG2 . THR A 236 ? 0.40711 0.38609 0.36769 0.02547  -0.00356 -0.08497 233 THR A CG2 
1839 N N   . ILE A 237 ? 0.44819 0.43631 0.40590 0.02256  -0.02018 -0.08174 234 ILE A N   
1840 C CA  . ILE A 237 ? 0.41500 0.40045 0.36719 0.02019  -0.02468 -0.08325 234 ILE A CA  
1841 C C   . ILE A 237 ? 0.48268 0.45934 0.42295 0.01777  -0.02280 -0.08562 234 ILE A C   
1842 O O   . ILE A 237 ? 0.49213 0.46506 0.42536 0.01672  -0.02049 -0.08555 234 ILE A O   
1843 C CB  . ILE A 237 ? 0.46977 0.45917 0.42349 0.01950  -0.02997 -0.08182 234 ILE A CB  
1844 C CG1 . ILE A 237 ? 0.44528 0.44221 0.40894 0.02104  -0.02988 -0.08002 234 ILE A CG1 
1845 C CG2 . ILE A 237 ? 0.47470 0.46373 0.42812 0.01757  -0.03538 -0.08318 234 ILE A CG2 
1846 C CD1 . ILE A 237 ? 0.40554 0.40577 0.37235 0.02057  -0.03361 -0.07908 234 ILE A CD1 
1847 N N   . CYS A 238 ? 0.49072 0.46331 0.42759 0.01608  -0.02333 -0.08799 235 CYS A N   
1848 C CA  . CYS A 238 ? 0.53857 0.50207 0.46231 0.01238  -0.02222 -0.09077 235 CYS A CA  
1849 C C   . CYS A 238 ? 0.56778 0.53114 0.48751 0.00921  -0.03006 -0.09116 235 CYS A C   
1850 O O   . CYS A 238 ? 0.59754 0.56651 0.52620 0.00999  -0.03364 -0.09102 235 CYS A O   
1851 C CB  . CYS A 238 ? 0.57599 0.53369 0.49899 0.01240  -0.01572 -0.09380 235 CYS A CB  
1852 S SG  . CYS A 238 ? 0.57997 0.53897 0.51306 0.01693  -0.00723 -0.09308 235 CYS A SG  
1853 N N   . ARG A 239 ? 0.52414 0.48096 0.43061 0.00514  -0.03282 -0.09161 236 ARG A N   
1854 C CA  . ARG A 239 ? 0.54556 0.50179 0.44813 0.00160  -0.04142 -0.09164 236 ARG A CA  
1855 C C   . ARG A 239 ? 0.53781 0.48344 0.42411 -0.00401 -0.03996 -0.09494 236 ARG A C   
1856 O O   . ARG A 239 ? 0.58393 0.52130 0.45634 -0.00693 -0.03629 -0.09549 236 ARG A O   
1857 C CB  . ARG A 239 ? 0.54720 0.50537 0.44888 0.00129  -0.04887 -0.08778 236 ARG A CB  
1858 C CG  . ARG A 239 ? 0.60375 0.56202 0.50398 -0.00206 -0.05929 -0.08700 236 ARG A CG  
1859 C CD  . ARG A 239 ? 0.67212 0.63274 0.57532 -0.00119 -0.06700 -0.08240 236 ARG A CD  
1860 N NE  . ARG A 239 ? 0.77705 0.73749 0.67989 -0.00440 -0.07819 -0.08093 236 ARG A NE  
1861 C CZ  . ARG A 239 ? 0.83929 0.79065 0.72481 -0.00991 -0.08409 -0.07931 236 ARG A CZ  
1862 N NH1 . ARG A 239 ? 0.82642 0.76743 0.69265 -0.01316 -0.07839 -0.07967 236 ARG A NH1 
1863 N NH2 . ARG A 239 ? 0.88393 0.83635 0.77152 -0.01269 -0.09571 -0.07739 236 ARG A NH2 
1864 N N   . ARG A 240 ? 0.54174 0.48701 0.42905 -0.00623 -0.04211 -0.09756 237 ARG A N   
1865 C CA  . ARG A 240 ? 0.58425 0.51900 0.45611 -0.01214 -0.03977 -0.10150 237 ARG A CA  
1866 C C   . ARG A 240 ? 0.60459 0.53345 0.46059 -0.01837 -0.04774 -0.10023 237 ARG A C   
1867 O O   . ARG A 240 ? 0.59732 0.53169 0.45829 -0.01899 -0.05839 -0.09738 237 ARG A O   
1868 C CB  . ARG A 240 ? 0.58768 0.52376 0.46519 -0.01331 -0.04039 -0.10460 237 ARG A CB  
1869 C CG  . ARG A 240 ? 0.58822 0.51299 0.44949 -0.02013 -0.03787 -0.10921 237 ARG A CG  
1870 C CD  . ARG A 240 ? 0.57096 0.49699 0.43775 -0.02191 -0.03902 -0.11229 237 ARG A CD  
1871 N NE  . ARG A 240 ? 0.59581 0.51043 0.44582 -0.02936 -0.03688 -0.11700 237 ARG A NE  
1872 C CZ  . ARG A 240 ? 0.59273 0.50584 0.44282 -0.03320 -0.03811 -0.12050 237 ARG A CZ  
1873 N NH1 . ARG A 240 ? 0.55604 0.47836 0.42237 -0.03029 -0.04119 -0.11984 237 ARG A NH1 
1874 N NH2 . ARG A 240 ? 0.60390 0.50565 0.43699 -0.04072 -0.03567 -0.12509 237 ARG A NH2 
1875 N N   . LEU A 241 ? 0.64146 0.55855 0.47849 -0.02342 -0.04252 -0.10237 238 LEU A N   
1876 C CA  . LEU A 241 ? 0.68844 0.59734 0.50603 -0.03078 -0.04982 -0.10086 238 LEU A CA  
1877 C C   . LEU A 241 ? 0.74104 0.64277 0.54556 -0.03860 -0.05341 -0.10445 238 LEU A C   
1878 O O   . LEU A 241 ? 0.76479 0.66552 0.56178 -0.04359 -0.06535 -0.10181 238 LEU A O   
1879 C CB  . LEU A 241 ? 0.65147 0.55015 0.45284 -0.03359 -0.04178 -0.10144 238 LEU A CB  
1880 C CG  . LEU A 241 ? 0.67023 0.57534 0.48211 -0.02732 -0.03987 -0.09743 238 LEU A CG  
1881 C CD1 . LEU A 241 ? 0.66040 0.55518 0.45683 -0.03076 -0.03035 -0.09894 238 LEU A CD1 
1882 C CD2 . LEU A 241 ? 0.63373 0.54504 0.45072 -0.02607 -0.05315 -0.09121 238 LEU A CD2 
1883 N N   . TYR A 242 ? 0.75921 0.65565 0.56135 -0.03997 -0.04371 -0.11025 239 TYR A N   
1884 C CA  . TYR A 242 ? 0.82209 0.71144 0.61214 -0.04777 -0.04600 -0.11444 239 TYR A CA  
1885 C C   . TYR A 242 ? 0.84246 0.73093 0.64096 -0.04559 -0.03594 -0.11982 239 TYR A C   
1886 O O   . TYR A 242 ? 0.87438 0.75930 0.66813 -0.05074 -0.03751 -0.12351 239 TYR A O   
1887 C CB  . TYR A 242 ? 0.84615 0.71979 0.60750 -0.05785 -0.04403 -0.11677 239 TYR A CB  
1888 C CG  . TYR A 242 ? 0.87119 0.73533 0.62460 -0.05779 -0.02821 -0.12085 239 TYR A CG  
1889 C CD1 . TYR A 242 ? 0.89900 0.75560 0.65049 -0.05932 -0.01575 -0.12784 239 TYR A CD1 
1890 C CD2 . TYR A 242 ? 0.85976 0.72231 0.60890 -0.05632 -0.02531 -0.11795 239 TYR A CD2 
1891 C CE1 . TYR A 242 ? 0.91746 0.76594 0.66508 -0.05894 -0.00079 -0.13194 239 TYR A CE1 
1892 C CE2 . TYR A 242 ? 0.87245 0.72714 0.61672 -0.05646 -0.01026 -0.12221 239 TYR A CE2 
1893 C CZ  . TYR A 242 ? 0.90257 0.75057 0.64706 -0.05758 0.00198  -0.12927 239 TYR A CZ  
1894 O OH  . TYR A 242 ? 0.91539 0.75608 0.65833 -0.05738 0.01748  -0.13391 239 TYR A OH  
1895 O OXT . TYR A 242 ? 0.82902 0.71995 0.63941 -0.03883 -0.02643 -0.12034 239 TYR A OXT 
1896 N N   . ASP B 9   ? 1.12042 1.30245 1.34003 -0.15254 0.01339  0.07434  6   ASP B N   
1897 C CA  . ASP B 9   ? 1.13110 1.31945 1.37080 -0.17101 0.00980  0.07821  6   ASP B CA  
1898 C C   . ASP B 9   ? 1.12141 1.27791 1.33182 -0.18066 -0.00107 0.07444  6   ASP B C   
1899 O O   . ASP B 9   ? 1.12491 1.28167 1.34660 -0.19674 -0.00977 0.07557  6   ASP B O   
1900 C CB  . ASP B 9   ? 1.14574 1.34172 1.39939 -0.17651 0.03011  0.08534  6   ASP B CB  
1901 N N   . ASP B 10  ? 1.08148 1.21017 1.25457 -0.17081 -0.00037 0.07004  7   ASP B N   
1902 C CA  . ASP B 10  ? 1.05534 1.15209 1.19824 -0.17621 -0.01013 0.06603  7   ASP B CA  
1903 C C   . ASP B 10  ? 0.97403 1.05898 1.09727 -0.16530 -0.02218 0.05918  7   ASP B C   
1904 O O   . ASP B 10  ? 0.94368 1.00972 1.05193 -0.17144 -0.03445 0.05562  7   ASP B O   
1905 C CB  . ASP B 10  ? 1.09258 1.16212 1.20677 -0.17542 0.00235  0.06782  7   ASP B CB  
1906 C CG  . ASP B 10  ? 1.13077 1.18928 1.24638 -0.19304 0.00538  0.07188  7   ASP B CG  
1907 O OD1 . ASP B 10  ? 1.13666 1.21201 1.27932 -0.20676 -0.00117 0.07358  7   ASP B OD1 
1908 O OD2 . ASP B 10  ? 1.15449 1.18698 1.24408 -0.19336 0.01386  0.07347  7   ASP B OD2 
1909 N N   . TYR B 11  ? 0.92789 1.02162 1.04962 -0.14967 -0.01817 0.05722  8   TYR B N   
1910 C CA  . TYR B 11  ? 0.89292 0.97791 0.99920 -0.13900 -0.02784 0.05100  8   TYR B CA  
1911 C C   . TYR B 11  ? 0.80194 0.91438 0.93332 -0.13355 -0.03337 0.05060  8   TYR B C   
1912 O O   . TYR B 11  ? 0.77337 0.91065 0.92918 -0.13112 -0.02464 0.05476  8   TYR B O   
1913 C CB  . TYR B 11  ? 0.91769 0.98725 0.99914 -0.12537 -0.01938 0.04862  8   TYR B CB  
1914 C CG  . TYR B 11  ? 0.98281 1.02359 1.03766 -0.12861 -0.01583 0.04904  8   TYR B CG  
1915 C CD1 . TYR B 11  ? 0.99984 1.03707 1.05143 -0.13138 -0.00327 0.05400  8   TYR B CD1 
1916 C CD2 . TYR B 11  ? 1.01212 1.02776 1.04410 -0.12829 -0.02430 0.04484  8   TYR B CD2 
1917 C CE1 . TYR B 11  ? 1.02688 1.03662 1.05307 -0.13341 -0.00041 0.05490  8   TYR B CE1 
1918 C CE2 . TYR B 11  ? 1.03199 1.02117 1.04041 -0.13001 -0.02077 0.04576  8   TYR B CE2 
1919 C CZ  . TYR B 11  ? 1.04906 1.03561 1.05469 -0.13242 -0.00941 0.05087  8   TYR B CZ  
1920 O OH  . TYR B 11  ? 1.08609 1.04519 1.06718 -0.13321 -0.00627 0.05226  8   TYR B OH  
1921 N N   . SER B 12  ? 0.77039 0.87666 0.89442 -0.13097 -0.04714 0.04586  9   SER B N   
1922 C CA  . SER B 12  ? 0.77513 0.90464 0.92235 -0.12873 -0.05639 0.04599  9   SER B CA  
1923 C C   . SER B 12  ? 0.76092 0.89790 0.90637 -0.11194 -0.05271 0.04344  9   SER B C   
1924 O O   . SER B 12  ? 0.75969 0.92101 0.92912 -0.10776 -0.05493 0.04547  9   SER B O   
1925 C CB  . SER B 12  ? 0.77766 0.89412 0.91601 -0.13654 -0.07478 0.04259  9   SER B CB  
1926 O OG  . SER B 12  ? 0.81020 0.91278 0.94324 -0.15225 -0.07830 0.04384  9   SER B OG  
1927 N N   . LEU B 13  ? 0.75817 0.87524 0.87711 -0.10234 -0.04727 0.03928  10  LEU B N   
1928 C CA  . LEU B 13  ? 0.75698 0.87668 0.87077 -0.08773 -0.04509 0.03585  10  LEU B CA  
1929 C C   . LEU B 13  ? 0.77911 0.91298 0.90148 -0.07904 -0.03007 0.03825  10  LEU B C   
1930 O O   . LEU B 13  ? 0.80377 0.94086 0.92338 -0.06735 -0.02731 0.03566  10  LEU B O   
1931 C CB  . LEU B 13  ? 0.75008 0.84175 0.83281 -0.08215 -0.04699 0.02995  10  LEU B CB  
1932 C CG  . LEU B 13  ? 0.76505 0.83593 0.83162 -0.08765 -0.05983 0.02644  10  LEU B CG  
1933 C CD1 . LEU B 13  ? 0.72502 0.76922 0.76365 -0.08187 -0.05683 0.02193  10  LEU B CD1 
1934 C CD2 . LEU B 13  ? 0.77995 0.85839 0.85319 -0.08424 -0.07046 0.02468  10  LEU B CD2 
1935 N N   . VAL B 14  ? 0.78779 0.92799 0.91857 -0.08461 -0.01974 0.04308  11  VAL B N   
1936 C CA  . VAL B 14  ? 0.79247 0.93683 0.92118 -0.07649 -0.00425 0.04472  11  VAL B CA  
1937 C C   . VAL B 14  ? 0.73369 0.90113 0.88304 -0.06740 0.00119  0.04635  11  VAL B C   
1938 O O   . VAL B 14  ? 0.70743 0.87331 0.84832 -0.05770 0.01228  0.04558  11  VAL B O   
1939 C CB  . VAL B 14  ? 0.85444 0.99829 0.98623 -0.08513 0.00625  0.05014  11  VAL B CB  
1940 C CG1 . VAL B 14  ? 0.90788 1.02512 1.01461 -0.09161 0.00265  0.04856  11  VAL B CG1 
1941 C CG2 . VAL B 14  ? 0.82250 0.98930 0.98691 -0.09550 0.00535  0.05576  11  VAL B CG2 
1942 N N   . HIS B 15  ? 0.71397 0.90190 0.88946 -0.06996 -0.00656 0.04871  12  HIS B N   
1943 C CA  . HIS B 15  ? 0.70867 0.91950 0.90617 -0.06052 -0.00111 0.05121  12  HIS B CA  
1944 C C   . HIS B 15  ? 0.71742 0.92673 0.90990 -0.05119 -0.01144 0.04681  12  HIS B C   
1945 O O   . HIS B 15  ? 0.73393 0.96318 0.94760 -0.04440 -0.01137 0.04935  12  HIS B O   
1946 C CB  . HIS B 15  ? 0.70458 0.94358 0.93996 -0.06833 -0.00112 0.05828  12  HIS B CB  
1947 C CG  . HIS B 15  ? 0.71516 0.95766 0.95832 -0.07613 0.01298  0.06344  12  HIS B CG  
1948 N ND1 . HIS B 15  ? 0.70894 0.95041 0.94654 -0.06865 0.03196  0.06542  12  HIS B ND1 
1949 C CD2 . HIS B 15  ? 0.71890 0.96361 0.97293 -0.09102 0.01142  0.06706  12  HIS B CD2 
1950 C CE1 . HIS B 15  ? 0.71474 0.95737 0.95897 -0.07808 0.04201  0.07028  12  HIS B CE1 
1951 N NE2 . HIS B 15  ? 0.72655 0.97174 0.98181 -0.09193 0.03007  0.07141  12  HIS B NE2 
1952 N N   . LYS B 16  ? 0.68550 0.87099 0.85048 -0.05014 -0.01933 0.04065  13  LYS B N   
1953 C CA  . LYS B 16  ? 0.64180 0.82139 0.79813 -0.04200 -0.02830 0.03627  13  LYS B CA  
1954 C C   . LYS B 16  ? 0.63164 0.79680 0.76602 -0.03064 -0.01955 0.03140  13  LYS B C   
1955 O O   . LYS B 16  ? 0.62134 0.77296 0.73888 -0.03118 -0.01209 0.02960  13  LYS B O   
1956 C CB  . LYS B 16  ? 0.62861 0.79039 0.77005 -0.04940 -0.04350 0.03280  13  LYS B CB  
1957 C CG  . LYS B 16  ? 0.63520 0.81076 0.79689 -0.05798 -0.05725 0.03617  13  LYS B CG  
1958 C CD  . LYS B 16  ? 0.65361 0.81278 0.80392 -0.07173 -0.06624 0.03518  13  LYS B CD  
1959 C CE  . LYS B 16  ? 0.69020 0.84249 0.83606 -0.07556 -0.08437 0.03328  13  LYS B CE  
1960 N NZ  . LYS B 16  ? 0.70812 0.88751 0.88278 -0.07325 -0.09215 0.03741  13  LYS B NZ  
1961 N N   . ASN B 17  ? 0.61666 0.78433 0.75119 -0.02052 -0.02118 0.02940  14  ASN B N   
1962 C CA  . ASN B 17  ? 0.58757 0.74098 0.70195 -0.01042 -0.01439 0.02425  14  ASN B CA  
1963 C C   . ASN B 17  ? 0.56066 0.70309 0.66445 -0.00575 -0.02438 0.02011  14  ASN B C   
1964 O O   . ASN B 17  ? 0.57269 0.72284 0.68755 -0.00730 -0.03508 0.02219  14  ASN B O   
1965 C CB  . ASN B 17  ? 0.65181 0.81783 0.77547 -0.00100 -0.00094 0.02648  14  ASN B CB  
1966 C CG  . ASN B 17  ? 0.74323 0.89224 0.84356 0.00574  0.00818  0.02130  14  ASN B CG  
1967 O OD1 . ASN B 17  ? 0.74330 0.88629 0.83552 0.01456  0.00951  0.01783  14  ASN B OD1 
1968 N ND2 . ASN B 17  ? 0.75569 0.89588 0.84439 0.00128  0.01394  0.02079  14  ASN B ND2 
1969 N N   . ILE B 18  ? 0.53958 0.66304 0.62130 -0.00036 -0.02110 0.01430  15  ILE B N   
1970 C CA  . ILE B 18  ? 0.49394 0.60296 0.56231 0.00378  -0.02855 0.01013  15  ILE B CA  
1971 C C   . ILE B 18  ? 0.42611 0.54013 0.49749 0.01518  -0.02512 0.00992  15  ILE B C   
1972 O O   . ILE B 18  ? 0.43032 0.53438 0.49297 0.01906  -0.03197 0.00783  15  ILE B O   
1973 C CB  . ILE B 18  ? 0.46806 0.55369 0.51305 0.00339  -0.02668 0.00411  15  ILE B CB  
1974 C CG1 . ILE B 18  ? 0.46247 0.54614 0.50115 0.00900  -0.01482 0.00161  15  ILE B CG1 
1975 C CG2 . ILE B 18  ? 0.44583 0.52348 0.48598 -0.00678 -0.03113 0.00455  15  ILE B CG2 
1976 C CD1 . ILE B 18  ? 0.42444 0.48808 0.44421 0.00986  -0.01350 -0.00433 15  ILE B CD1 
1977 N N   . LEU B 19  ? 0.39036 0.51694 0.47148 0.02105  -0.01409 0.01211  16  LEU B N   
1978 C CA  . LEU B 19  ? 0.41618 0.54753 0.50107 0.03245  -0.01010 0.01270  16  LEU B CA  
1979 C C   . LEU B 19  ? 0.45400 0.60702 0.56380 0.03375  -0.01743 0.01920  16  LEU B C   
1980 O O   . LEU B 19  ? 0.39976 0.56745 0.52716 0.02524  -0.02279 0.02354  16  LEU B O   
1981 C CB  . LEU B 19  ? 0.39827 0.53176 0.48149 0.03870  0.00533  0.01240  16  LEU B CB  
1982 C CG  . LEU B 19  ? 0.40579 0.51958 0.46586 0.03728  0.01149  0.00613  16  LEU B CG  
1983 C CD1 . LEU B 19  ? 0.40588 0.51849 0.46063 0.04459  0.02544  0.00531  16  LEU B CD1 
1984 C CD2 . LEU B 19  ? 0.39957 0.49319 0.44125 0.03825  0.00567  0.00012  16  LEU B CD2 
1985 N N   . HIS B 20  ? 0.50718 0.66216 0.61906 0.04452  -0.01789 0.02005  17  HIS B N   
1986 C CA  . HIS B 20  ? 0.54057 0.71486 0.67526 0.04648  -0.02833 0.02609  17  HIS B CA  
1987 C C   . HIS B 20  ? 0.48970 0.69316 0.65629 0.04770  -0.02112 0.03333  17  HIS B C   
1988 O O   . HIS B 20  ? 0.44945 0.67389 0.64148 0.04602  -0.03092 0.03915  17  HIS B O   
1989 C CB  . HIS B 20  ? 0.64008 0.80589 0.76582 0.05861  -0.03188 0.02534  17  HIS B CB  
1990 C CG  . HIS B 20  ? 0.74419 0.90948 0.86786 0.07145  -0.01669 0.02525  17  HIS B CG  
1991 N ND1 . HIS B 20  ? 0.78138 0.92861 0.88595 0.08178  -0.01501 0.02210  17  HIS B ND1 
1992 C CD2 . HIS B 20  ? 0.77349 0.95163 0.90974 0.07572  -0.00189 0.02797  17  HIS B CD2 
1993 C CE1 . HIS B 20  ? 0.78141 0.93023 0.88683 0.09154  -0.00025 0.02263  17  HIS B CE1 
1994 N NE2 . HIS B 20  ? 0.77374 0.94083 0.89766 0.08830  0.00801  0.02613  17  HIS B NE2 
1995 N N   . SER B 21  ? 0.46001 0.66488 0.62595 0.05036  -0.00436 0.03325  18  SER B N   
1996 C CA  . SER B 21  ? 0.46142 0.69177 0.65622 0.05231  0.00547  0.04029  18  SER B CA  
1997 C C   . SER B 21  ? 0.45028 0.67395 0.63506 0.04908  0.02125  0.03881  18  SER B C   
1998 O O   . SER B 21  ? 0.41175 0.61282 0.56836 0.05093  0.02718  0.03256  18  SER B O   
1999 C CB  . SER B 21  ? 0.51238 0.75351 0.71975 0.06764  0.01219  0.04403  18  SER B CB  
2000 O OG  . SER B 21  ? 0.53460 0.75948 0.72131 0.07637  0.02856  0.04028  18  SER B OG  
2001 N N   . GLU B 22  ? 0.47568 0.71894 0.68388 0.04388  0.02766  0.04481  19  GLU B N   
2002 C CA  . GLU B 22  ? 0.50568 0.74283 0.70457 0.04222  0.04416  0.04468  19  GLU B CA  
2003 C C   . GLU B 22  ? 0.45916 0.68928 0.64759 0.05569  0.06047  0.04375  19  GLU B C   
2004 O O   . GLU B 22  ? 0.46654 0.67928 0.63174 0.05587  0.07162  0.04024  19  GLU B O   
2005 C CB  . GLU B 22  ? 0.60065 0.86062 0.82872 0.03461  0.04920  0.05216  19  GLU B CB  
2006 C CG  . GLU B 22  ? 0.74250 0.99456 0.95954 0.03208  0.06645  0.05285  19  GLU B CG  
2007 C CD  . GLU B 22  ? 0.87985 1.11912 1.08213 0.01846  0.06069  0.05056  19  GLU B CD  
2008 O OE1 . GLU B 22  ? 0.91598 1.16434 1.13275 0.00831  0.04760  0.05234  19  GLU B OE1 
2009 O OE2 . GLU B 22  ? 0.92640 1.14534 1.10152 0.01804  0.06874  0.04702  19  GLU B OE2 
2010 N N   . ASP B 23  ? 0.39885 0.64072 0.60262 0.06720  0.06159  0.04689  20  ASP B N   
2011 C CA  . ASP B 23  ? 0.38796 0.62157 0.58128 0.08071  0.07799  0.04629  20  ASP B CA  
2012 C C   . ASP B 23  ? 0.40378 0.60631 0.55862 0.08327  0.07798  0.03721  20  ASP B C   
2013 O O   . ASP B 23  ? 0.40163 0.58835 0.53620 0.08801  0.09224  0.03431  20  ASP B O   
2014 C CB  . ASP B 23  ? 0.39556 0.64790 0.61401 0.09322  0.07780  0.05201  20  ASP B CB  
2015 C CG  . ASP B 23  ? 0.46617 0.75230 0.72736 0.09167  0.07996  0.06165  20  ASP B CG  
2016 O OD1 . ASP B 23  ? 0.47087 0.76304 0.73921 0.08323  0.08846  0.06406  20  ASP B OD1 
2017 O OD2 . ASP B 23  ? 0.46888 0.77541 0.75690 0.09890  0.07309  0.06705  20  ASP B OD2 
2018 N N   . LEU B 24  ? 0.40990 0.60240 0.55386 0.07986  0.06242  0.03262  21  LEU B N   
2019 C CA  . LEU B 24  ? 0.40690 0.57133 0.51761 0.08114  0.06238  0.02413  21  LEU B CA  
2020 C C   . LEU B 24  ? 0.44159 0.59153 0.53244 0.07205  0.06611  0.01969  21  LEU B C   
2021 O O   . LEU B 24  ? 0.46938 0.60025 0.53652 0.07493  0.07459  0.01456  21  LEU B O   
2022 C CB  . LEU B 24  ? 0.37025 0.52715 0.47498 0.07909  0.04612  0.02089  21  LEU B CB  
2023 C CG  . LEU B 24  ? 0.41691 0.54601 0.49074 0.07980  0.04598  0.01238  21  LEU B CG  
2024 C CD1 . LEU B 24  ? 0.40559 0.52317 0.46655 0.09121  0.05939  0.01036  21  LEU B CD1 
2025 C CD2 . LEU B 24  ? 0.40281 0.52431 0.47167 0.07869  0.03183  0.01024  21  LEU B CD2 
2026 N N   . LEU B 25  ? 0.39711 0.55493 0.49661 0.06089  0.05918  0.02167  22  LEU B N   
2027 C CA  . LEU B 25  ? 0.38476 0.52935 0.46611 0.05297  0.06205  0.01847  22  LEU B CA  
2028 C C   . LEU B 25  ? 0.40389 0.54629 0.47921 0.05679  0.07903  0.02034  22  LEU B C   
2029 O O   . LEU B 25  ? 0.42446 0.54749 0.47425 0.05605  0.08391  0.01547  22  LEU B O   
2030 C CB  . LEU B 25  ? 0.39483 0.54808 0.48744 0.04111  0.05269  0.02130  22  LEU B CB  
2031 C CG  . LEU B 25  ? 0.45482 0.59424 0.52899 0.03331  0.05448  0.01887  22  LEU B CG  
2032 C CD1 . LEU B 25  ? 0.44829 0.56561 0.49661 0.03382  0.04989  0.01095  22  LEU B CD1 
2033 C CD2 . LEU B 25  ? 0.46663 0.61334 0.55188 0.02213  0.04592  0.02214  22  LEU B CD2 
2034 N N   . LYS B 26  ? 0.36750 0.52906 0.46595 0.06088  0.08822  0.02752  23  LYS B N   
2035 C CA  . LYS B 26  ? 0.42009 0.57773 0.51178 0.06578  0.10676  0.02975  23  LYS B CA  
2036 C C   . LYS B 26  ? 0.44015 0.57845 0.50833 0.07616  0.11556  0.02470  23  LYS B C   
2037 O O   . LYS B 26  ? 0.49682 0.61682 0.54048 0.07697  0.12623  0.02192  23  LYS B O   
2038 C CB  . LYS B 26  ? 0.44200 0.62582 0.56732 0.06934  0.11596  0.03891  23  LYS B CB  
2039 C CG  . LYS B 26  ? 0.47767 0.67703 0.62246 0.05778  0.11317  0.04423  23  LYS B CG  
2040 C CD  . LYS B 26  ? 0.51756 0.74440 0.69886 0.06127  0.12375  0.05350  23  LYS B CD  
2041 N N   . TYR B 27  ? 0.39080 0.53081 0.46404 0.08399  0.11111  0.02346  24  TYR B N   
2042 C CA  . TYR B 27  ? 0.43224 0.55124 0.48147 0.09304  0.11885  0.01813  24  TYR B CA  
2043 C C   . TYR B 27  ? 0.43276 0.52625 0.44972 0.08626  0.11409  0.00939  24  TYR B C   
2044 O O   . TYR B 27  ? 0.46456 0.53820 0.45659 0.08894  0.12414  0.00541  24  TYR B O   
2045 C CB  . TYR B 27  ? 0.43846 0.56172 0.49709 0.10156  0.11278  0.01825  24  TYR B CB  
2046 C CG  . TYR B 27  ? 0.49163 0.59014 0.52333 0.10955  0.11969  0.01205  24  TYR B CG  
2047 C CD1 . TYR B 27  ? 0.54455 0.63810 0.57230 0.12145  0.13638  0.01420  24  TYR B CD1 
2048 C CD2 . TYR B 27  ? 0.49601 0.57510 0.50626 0.10499  0.11055  0.00410  24  TYR B CD2 
2049 C CE1 . TYR B 27  ? 0.55737 0.62571 0.55847 0.12806  0.14304  0.00827  24  TYR B CE1 
2050 C CE2 . TYR B 27  ? 0.53589 0.59172 0.52199 0.11094  0.11712  -0.00174 24  TYR B CE2 
2051 C CZ  . TYR B 27  ? 0.53310 0.58282 0.51364 0.12219  0.13300  0.00019  24  TYR B CZ  
2052 O OH  . TYR B 27  ? 0.50424 0.52836 0.45885 0.12744  0.13969  -0.00588 24  TYR B OH  
2053 N N   . ILE B 28  ? 0.42380 0.51704 0.44093 0.07748  0.09862  0.00637  25  ILE B N   
2054 C CA  . ILE B 28  ? 0.44950 0.52187 0.44112 0.07102  0.09302  -0.00133 25  ILE B CA  
2055 C C   . ILE B 28  ? 0.49324 0.55694 0.46943 0.06611  0.09935  -0.00155 25  ILE B C   
2056 O O   . ILE B 28  ? 0.56071 0.60409 0.51121 0.06631  0.10332  -0.00704 25  ILE B O   
2057 C CB  . ILE B 28  ? 0.40897 0.48463 0.40702 0.06302  0.07685  -0.00312 25  ILE B CB  
2058 C CG1 . ILE B 28  ? 0.41169 0.48999 0.41808 0.06821  0.07066  -0.00369 25  ILE B CG1 
2059 C CG2 . ILE B 28  ? 0.44748 0.50502 0.42394 0.05623  0.07150  -0.00999 25  ILE B CG2 
2060 C CD1 . ILE B 28  ? 0.40293 0.48261 0.41426 0.06104  0.05614  -0.00494 25  ILE B CD1 
2061 N N   . LEU B 29  ? 0.46711 0.54473 0.45751 0.06114  0.09984  0.00440  26  LEU B N   
2062 C CA  . LEU B 29  ? 0.50099 0.56876 0.47501 0.05638  0.10553  0.00489  26  LEU B CA  
2063 C C   . LEU B 29  ? 0.52507 0.58030 0.48199 0.06387  0.12255  0.00496  26  LEU B C   
2064 O O   . LEU B 29  ? 0.49476 0.52896 0.42304 0.06192  0.12532  0.00087  26  LEU B O   
2065 C CB  . LEU B 29  ? 0.47809 0.56303 0.47209 0.05013  0.10501  0.01206  26  LEU B CB  
2066 C CG  . LEU B 29  ? 0.45248 0.54626 0.45959 0.04154  0.08896  0.01222  26  LEU B CG  
2067 C CD1 . LEU B 29  ? 0.35886 0.47068 0.38853 0.03572  0.09028  0.01987  26  LEU B CD1 
2068 C CD2 . LEU B 29  ? 0.45878 0.53455 0.44302 0.03538  0.07999  0.00664  26  LEU B CD2 
2069 N N   . GLU B 30  ? 0.51979 0.58672 0.49318 0.07281  0.13391  0.00970  27  GLU B N   
2070 C CA  . GLU B 30  ? 0.56958 0.62439 0.52778 0.08081  0.15268  0.01082  27  GLU B CA  
2071 C C   . GLU B 30  ? 0.60756 0.63847 0.53849 0.08652  0.15530  0.00329  27  GLU B C   
2072 O O   . GLU B 30  ? 0.61405 0.62243 0.51600 0.08845  0.16585  0.00048  27  GLU B O   
2073 C CB  . GLU B 30  ? 0.54784 0.62495 0.53633 0.08920  0.16484  0.01924  27  GLU B CB  
2074 C CG  . GLU B 30  ? 0.60594 0.70289 0.61771 0.08347  0.16824  0.02715  27  GLU B CG  
2075 C CD  . GLU B 30  ? 0.69417 0.81779 0.74265 0.09116  0.17813  0.03573  27  GLU B CD  
2076 O OE1 . GLU B 30  ? 0.72556 0.85122 0.77975 0.10224  0.18261  0.03580  27  GLU B OE1 
2077 O OE2 . GLU B 30  ? 0.74310 0.88586 0.81572 0.08610  0.18132  0.04266  27  GLU B OE2 
2078 N N   . THR B 31  ? 0.59235 0.62556 0.53000 0.08889  0.14614  -0.00014 28  THR B N   
2079 C CA  . THR B 31  ? 0.62915 0.63931 0.54220 0.09398  0.14958  -0.00712 28  THR B CA  
2080 C C   . THR B 31  ? 0.64631 0.63572 0.53253 0.08470  0.13941  -0.01555 28  THR B C   
2081 O O   . THR B 31  ? 0.65031 0.61532 0.50692 0.08547  0.14565  -0.02084 28  THR B O   
2082 C CB  . THR B 31  ? 0.64394 0.66218 0.57265 0.10039  0.14474  -0.00727 28  THR B CB  
2083 O OG1 . THR B 31  ? 0.64536 0.68378 0.60018 0.10997  0.15341  0.00097  28  THR B OG1 
2084 C CG2 . THR B 31  ? 0.68004 0.67233 0.58225 0.10505  0.14924  -0.01456 28  THR B CG2 
2085 N N   . SER B 32  ? 0.60247 0.60086 0.49879 0.07584  0.12362  -0.01678 29  SER B N   
2086 C CA  . SER B 32  ? 0.63077 0.61367 0.50889 0.06802  0.11234  -0.02452 29  SER B CA  
2087 C C   . SER B 32  ? 0.65110 0.63232 0.52163 0.05893  0.10493  -0.02437 29  SER B C   
2088 O O   . SER B 32  ? 0.70741 0.67145 0.55608 0.05397  0.09954  -0.03033 29  SER B O   
2089 C CB  . SER B 32  ? 0.60133 0.59178 0.49444 0.06604  0.10036  -0.02695 29  SER B CB  
2090 O OG  . SER B 32  ? 0.62776 0.61715 0.52511 0.07476  0.10621  -0.02714 29  SER B OG  
2091 N N   . ALA B 33  ? 0.60271 0.60079 0.49061 0.05644  0.10400  -0.01763 30  ALA B N   
2092 C CA  . ALA B 33  ? 0.63106 0.62744 0.51289 0.04802  0.09566  -0.01703 30  ALA B CA  
2093 C C   . ALA B 33  ? 0.65745 0.64086 0.51762 0.04815  0.10568  -0.01487 30  ALA B C   
2094 O O   . ALA B 33  ? 0.65409 0.61886 0.48845 0.04438  0.10127  -0.01922 30  ALA B O   
2095 C CB  . ALA B 33  ? 0.63883 0.65662 0.54779 0.04399  0.08871  -0.01133 30  ALA B CB  
2096 N N   . TYR B 34  ? 0.68592 0.67865 0.55635 0.05236  0.11903  -0.00797 31  TYR B N   
2097 C CA  . TYR B 34  ? 0.69662 0.67566 0.54586 0.05290  0.13101  -0.00514 31  TYR B CA  
2098 C C   . TYR B 34  ? 0.69215 0.64265 0.50488 0.05625  0.13765  -0.01109 31  TYR B C   
2099 O O   . TYR B 34  ? 0.70168 0.63325 0.48658 0.05293  0.13821  -0.01193 31  TYR B O   
2100 C CB  . TYR B 34  ? 0.71568 0.71105 0.58628 0.05802  0.14694  0.00336  31  TYR B CB  
2101 C CG  . TYR B 34  ? 0.71197 0.73280 0.61505 0.05260  0.14072  0.00965  31  TYR B CG  
2102 C CD1 . TYR B 34  ? 0.71418 0.73525 0.61622 0.04354  0.12605  0.00879  31  TYR B CD1 
2103 C CD2 . TYR B 34  ? 0.69517 0.73940 0.63022 0.05649  0.14923  0.01655  31  TYR B CD2 
2104 C CE1 . TYR B 34  ? 0.72064 0.76181 0.64955 0.03799  0.12061  0.01416  31  TYR B CE1 
2105 C CE2 . TYR B 34  ? 0.67641 0.74282 0.64041 0.05017  0.14250  0.02191  31  TYR B CE2 
2106 C CZ  . TYR B 34  ? 0.70414 0.76755 0.66341 0.04068  0.12850  0.02046  31  TYR B CZ  
2107 O OH  . TYR B 34  ? 0.72690 0.80935 0.71227 0.03387  0.12210  0.02544  31  TYR B OH  
2108 N N   . PRO B 35  ? 0.69936 0.64330 0.50809 0.06258  0.14260  -0.01530 32  PRO B N   
2109 C CA  . PRO B 35  ? 0.73632 0.64960 0.50685 0.06420  0.14768  -0.02178 32  PRO B CA  
2110 C C   . PRO B 35  ? 0.70342 0.60142 0.45301 0.05547  0.13056  -0.02926 32  PRO B C   
2111 O O   . PRO B 35  ? 0.73680 0.60795 0.45163 0.05452  0.13236  -0.03432 32  PRO B O   
2112 C CB  . PRO B 35  ? 0.73654 0.64901 0.51276 0.07241  0.15511  -0.02432 32  PRO B CB  
2113 C CG  . PRO B 35  ? 0.74712 0.68881 0.56165 0.07788  0.16013  -0.01658 32  PRO B CG  
2114 C CD  . PRO B 35  ? 0.68868 0.65025 0.52462 0.06943  0.14609  -0.01347 32  PRO B CD  
2115 N N   . ARG B 36  ? 0.63043 0.54400 0.39982 0.04918  0.11411  -0.03005 33  ARG B N   
2116 C CA  . ARG B 36  ? 0.68439 0.58756 0.44000 0.04127  0.09745  -0.03628 33  ARG B CA  
2117 C C   . ARG B 36  ? 0.70940 0.61744 0.46583 0.03533  0.08780  -0.03245 33  ARG B C   
2118 O O   . ARG B 36  ? 0.70546 0.61016 0.45746 0.02922  0.07238  -0.03622 33  ARG B O   
2119 C CB  . ARG B 36  ? 0.64031 0.55423 0.41608 0.03928  0.08685  -0.04078 33  ARG B CB  
2120 C CG  . ARG B 36  ? 0.66077 0.56469 0.43040 0.04425  0.09455  -0.04571 33  ARG B CG  
2121 C CD  . ARG B 36  ? 0.67838 0.55468 0.41407 0.04089  0.09275  -0.05342 33  ARG B CD  
2122 N NE  . ARG B 36  ? 0.70518 0.56969 0.43396 0.04487  0.10000  -0.05856 33  ARG B NE  
2123 C CZ  . ARG B 36  ? 0.73162 0.57752 0.44207 0.03972  0.09406  -0.06692 33  ARG B CZ  
2124 N NH1 . ARG B 36  ? 0.72819 0.56744 0.42760 0.03058  0.07958  -0.07092 33  ARG B NH1 
2125 N NH2 . ARG B 36  ? 0.73462 0.56863 0.43851 0.04359  0.10218  -0.07110 33  ARG B NH2 
2126 N N   . GLU B 37  ? 0.69384 0.60965 0.45674 0.03709  0.09689  -0.02478 34  GLU B N   
2127 C CA  . GLU B 37  ? 0.65809 0.57793 0.42234 0.03186  0.08938  -0.02030 34  GLU B CA  
2128 C C   . GLU B 37  ? 0.66315 0.55695 0.38904 0.03054  0.09095  -0.02085 34  GLU B C   
2129 O O   . GLU B 37  ? 0.67678 0.55621 0.38301 0.03499  0.10658  -0.01930 34  GLU B O   
2130 C CB  . GLU B 37  ? 0.68801 0.62782 0.47789 0.03321  0.09855  -0.01179 34  GLU B CB  
2131 C CG  . GLU B 37  ? 0.72656 0.67255 0.52275 0.02723  0.09017  -0.00710 34  GLU B CG  
2132 C CD  . GLU B 37  ? 0.75733 0.72146 0.57782 0.02720  0.10003  0.00114  34  GLU B CD  
2133 O OE1 . GLU B 37  ? 0.74835 0.71414 0.57093 0.03205  0.11658  0.00460  34  GLU B OE1 
2134 O OE2 . GLU B 37  ? 0.72599 0.70256 0.56418 0.02218  0.09143  0.00419  34  GLU B OE2 
2135 N N   . HIS B 38  ? 0.65724 0.54395 0.37173 0.02498  0.07485  -0.02288 35  HIS B N   
2136 C CA  . HIS B 38  ? 0.70702 0.56850 0.38390 0.02341  0.07322  -0.02278 35  HIS B CA  
2137 C C   . HIS B 38  ? 0.75848 0.61662 0.42862 0.02563  0.08856  -0.01453 35  HIS B C   
2138 O O   . HIS B 38  ? 0.77017 0.64914 0.46894 0.02553  0.09352  -0.00840 35  HIS B O   
2139 C CB  . HIS B 38  ? 0.73185 0.59277 0.40644 0.01780  0.05215  -0.02427 35  HIS B CB  
2140 C CG  . HIS B 38  ? 0.78913 0.62218 0.42267 0.01597  0.04515  -0.02625 35  HIS B CG  
2141 N ND1 . HIS B 38  ? 0.83254 0.65116 0.44309 0.01639  0.04942  -0.02029 35  HIS B ND1 
2142 C CD2 . HIS B 38  ? 0.79684 0.61274 0.40724 0.01328  0.03325  -0.03351 35  HIS B CD2 
2143 C CE1 . HIS B 38  ? 0.86519 0.65794 0.43822 0.01471  0.03998  -0.02369 35  HIS B CE1 
2144 N NE2 . HIS B 38  ? 0.85770 0.64906 0.43071 0.01244  0.02941  -0.03183 35  HIS B NE2 
2145 N N   B GLU B 39  ? 0.77292 0.60311 0.40377 0.02718  0.09643  -0.01451 36  GLU B N   
2146 N N   C GLU B 39  ? 0.77066 0.60086 0.40147 0.02711  0.09628  -0.01443 36  GLU B N   
2147 C CA  B GLU B 39  ? 0.78661 0.60984 0.40751 0.02952  0.11393  -0.00672 36  GLU B CA  
2148 C CA  C GLU B 39  ? 0.78473 0.60862 0.40657 0.02957  0.11420  -0.00661 36  GLU B CA  
2149 C C   B GLU B 39  ? 0.78862 0.62146 0.42095 0.02517  0.10693  -0.00031 36  GLU B C   
2150 C C   C GLU B 39  ? 0.79105 0.62284 0.42192 0.02522  0.10728  -0.00020 36  GLU B C   
2151 O O   B GLU B 39  ? 0.79217 0.63768 0.44311 0.02552  0.11969  0.00693  36  GLU B O   
2152 O O   C GLU B 39  ? 0.80250 0.64476 0.44894 0.02562  0.12058  0.00717  36  GLU B O   
2153 C CB  B GLU B 39  ? 0.82587 0.61195 0.39600 0.03154  0.12167  -0.00844 36  GLU B CB  
2154 C CB  C GLU B 39  ? 0.82395 0.61132 0.39620 0.03211  0.12378  -0.00822 36  GLU B CB  
2155 C CG  B GLU B 39  ? 0.84045 0.61456 0.39510 0.03385  0.14094  -0.00033 36  GLU B CG  
2156 C CG  C GLU B 39  ? 0.84974 0.61247 0.38520 0.02775  0.10584  -0.01154 36  GLU B CG  
2157 N N   . GLN B 40  ? 0.77691 0.60410 0.39952 0.02100  0.08671  -0.00269 37  GLN B N   
2158 C CA  . GLN B 40  ? 0.75484 0.58798 0.38530 0.01756  0.07979  0.00340  37  GLN B CA  
2159 C C   . GLN B 40  ? 0.70634 0.57146 0.38292 0.01544  0.07624  0.00557  37  GLN B C   
2160 O O   . GLN B 40  ? 0.69806 0.57101 0.38708 0.01297  0.07874  0.01211  37  GLN B O   
2161 C CB  . GLN B 40  ? 0.75940 0.57700 0.36635 0.01504  0.05893  0.00066  37  GLN B CB  
2162 C CG  . GLN B 40  ? 0.79690 0.57940 0.35336 0.01641  0.06007  -0.00108 37  GLN B CG  
2163 C CD  . GLN B 40  ? 0.83333 0.59807 0.36647 0.01842  0.07951  0.00624  37  GLN B CD  
2164 O OE1 . GLN B 40  ? 0.85559 0.62976 0.40355 0.01709  0.08480  0.01346  37  GLN B OE1 
2165 N NE2 . GLN B 40  ? 0.83449 0.57176 0.33001 0.02136  0.09123  0.00438  37  GLN B NE2 
2166 N N   . LEU B 41  ? 0.70011 0.58160 0.40016 0.01604  0.07061  0.00015  38  LEU B N   
2167 C CA  . LEU B 41  ? 0.63976 0.54900 0.38053 0.01463  0.06941  0.00218  38  LEU B CA  
2168 C C   . LEU B 41  ? 0.65473 0.57603 0.41276 0.01649  0.08812  0.00793  38  LEU B C   
2169 O O   . LEU B 41  ? 0.64104 0.57946 0.42452 0.01349  0.08907  0.01304  38  LEU B O   
2170 C CB  . LEU B 41  ? 0.59325 0.51356 0.35097 0.01543  0.06061  -0.00489 38  LEU B CB  
2171 C CG  . LEU B 41  ? 0.61814 0.53849 0.37756 0.01242  0.04099  -0.00948 38  LEU B CG  
2172 C CD1 . LEU B 41  ? 0.58072 0.50934 0.35464 0.01335  0.03676  -0.01642 38  LEU B CD1 
2173 C CD2 . LEU B 41  ? 0.61931 0.55243 0.39897 0.00930  0.03353  -0.00480 38  LEU B CD2 
2174 N N   . LYS B 42  ? 0.72604 0.63833 0.47097 0.02136  0.10317  0.00727  39  LYS B N   
2175 C CA  . LYS B 42  ? 0.80056 0.72473 0.56301 0.02403  0.12232  0.01339  39  LYS B CA  
2176 C C   . LYS B 42  ? 0.79824 0.71823 0.55591 0.02053  0.13049  0.02129  39  LYS B C   
2177 O O   . LYS B 42  ? 0.79641 0.73621 0.58331 0.01845  0.13806  0.02729  39  LYS B O   
2178 C CB  . LYS B 42  ? 0.87928 0.78973 0.62333 0.03101  0.13794  0.01121  39  LYS B CB  
2179 C CG  . LYS B 42  ? 0.93844 0.85966 0.69935 0.03529  0.16007  0.01800  39  LYS B CG  
2180 C CD  . LYS B 42  ? 1.00103 0.89969 0.73284 0.04262  0.17696  0.01618  39  LYS B CD  
2181 C CE  . LYS B 42  ? 1.04595 0.95576 0.79632 0.04806  0.20094  0.02356  39  LYS B CE  
2182 N NZ  . LYS B 42  ? 1.04707 0.98438 0.83613 0.05299  0.20304  0.02383  39  LYS B NZ  
2183 N N   . GLY B 43  ? 0.77198 0.66553 0.49250 0.01942  0.12853  0.02148  40  GLY B N   
2184 C CA  . GLY B 43  ? 0.77616 0.66167 0.48784 0.01623  0.13716  0.02911  40  GLY B CA  
2185 C C   . GLY B 43  ? 0.76021 0.66115 0.49528 0.00980  0.12539  0.03247  40  GLY B C   
2186 O O   . GLY B 43  ? 0.72490 0.63694 0.47890 0.00620  0.13511  0.03920  40  GLY B O   
2187 N N   . LEU B 44  ? 0.75452 0.65569 0.48880 0.00810  0.10483  0.02786  41  LEU B N   
2188 C CA  . LEU B 44  ? 0.73644 0.64978 0.49099 0.00278  0.09362  0.03057  41  LEU B CA  
2189 C C   . LEU B 44  ? 0.67556 0.61734 0.47181 0.00022  0.09786  0.03266  41  LEU B C   
2190 O O   . LEU B 44  ? 0.64877 0.59862 0.46065 -0.00520 0.09927  0.03804  41  LEU B O   
2191 C CB  . LEU B 44  ? 0.74483 0.65590 0.49552 0.00288  0.07238  0.02478  41  LEU B CB  
2192 C CG  . LEU B 44  ? 0.77834 0.69380 0.53982 -0.00102 0.05897  0.02694  41  LEU B CG  
2193 C CD1 . LEU B 44  ? 0.75273 0.65850 0.49975 0.00089  0.04087  0.02209  41  LEU B CD1 
2194 C CD2 . LEU B 44  ? 0.78330 0.72354 0.58284 -0.00399 0.05668  0.02684  41  LEU B CD2 
2195 N N   . ARG B 45  ? 0.67054 0.62647 0.48398 0.00386  0.09930  0.02849  42  ARG B N   
2196 C CA  . ARG B 45  ? 0.66225 0.64476 0.51413 0.00206  0.10131  0.03037  42  ARG B CA  
2197 C C   . ARG B 45  ? 0.70301 0.69413 0.56857 0.00013  0.11884  0.03799  42  ARG B C   
2198 O O   . ARG B 45  ? 0.66414 0.67217 0.55652 -0.00564 0.11795  0.04218  42  ARG B O   
2199 C CB  . ARG B 45  ? 0.63924 0.63176 0.50242 0.00768  0.10022  0.02474  42  ARG B CB  
2200 C CG  . ARG B 45  ? 0.63416 0.65298 0.53465 0.00745  0.10342  0.02720  42  ARG B CG  
2201 C CD  . ARG B 45  ? 0.61662 0.64216 0.52487 0.01369  0.10103  0.02159  42  ARG B CD  
2202 N NE  . ARG B 45  ? 0.63906 0.64993 0.52492 0.02050  0.11215  0.01910  42  ARG B NE  
2203 C CZ  . ARG B 45  ? 0.64297 0.65820 0.53437 0.02560  0.12931  0.02279  42  ARG B CZ  
2204 N NH1 . ARG B 45  ? 0.62612 0.66298 0.54819 0.02430  0.13650  0.02939  42  ARG B NH1 
2205 N NH2 . ARG B 45  ? 0.63616 0.63373 0.50271 0.03193  0.13938  0.01994  42  ARG B NH2 
2206 N N   . GLU B 46  ? 0.72065 0.69924 0.56761 0.00446  0.13528  0.03994  43  GLU B N   
2207 C CA  . GLU B 46  ? 0.73604 0.72529 0.60035 0.00360  0.15446  0.04728  43  GLU B CA  
2208 C C   . GLU B 46  ? 0.73224 0.71478 0.59247 -0.00405 0.15855  0.05391  43  GLU B C   
2209 O O   . GLU B 46  ? 0.70592 0.70519 0.59319 -0.00844 0.16909  0.06019  43  GLU B O   
2210 C CB  . GLU B 46  ? 0.76664 0.74242 0.61117 0.01147  0.17293  0.04741  43  GLU B CB  
2211 C CG  . GLU B 46  ? 0.78294 0.77391 0.64608 0.01879  0.17587  0.04400  43  GLU B CG  
2212 C CD  . GLU B 46  ? 0.84263 0.81441 0.67934 0.02739  0.19270  0.04272  43  GLU B CD  
2213 O OE1 . GLU B 46  ? 0.88687 0.83054 0.68577 0.02750  0.19929  0.04313  43  GLU B OE1 
2214 O OE2 . GLU B 46  ? 0.84022 0.82306 0.69196 0.03438  0.19935  0.04136  43  GLU B OE2 
2215 N N   . VAL B 47  ? 0.78777 0.74633 0.61568 -0.00589 0.15017  0.05293  44  VAL B N   
2216 C CA  . VAL B 47  ? 0.82550 0.77683 0.64980 -0.01328 0.15239  0.05919  44  VAL B CA  
2217 C C   . VAL B 47  ? 0.81348 0.78302 0.66653 -0.02033 0.13776  0.05923  44  VAL B C   
2218 O O   . VAL B 47  ? 0.83917 0.81590 0.70875 -0.02797 0.14277  0.06500  44  VAL B O   
2219 C CB  . VAL B 47  ? 0.84677 0.76459 0.62508 -0.01190 0.14842  0.05897  44  VAL B CB  
2220 C CG1 . VAL B 47  ? 0.89638 0.79285 0.64225 -0.00518 0.16260  0.05843  44  VAL B CG1 
2221 C CG2 . VAL B 47  ? 0.83213 0.74490 0.60052 -0.01059 0.12521  0.05268  44  VAL B CG2 
2222 N N   . THR B 48  ? 0.71687 0.69297 0.57587 -0.01825 0.12027  0.05275  45  THR B N   
2223 C CA  . THR B 48  ? 0.68589 0.67554 0.56806 -0.02424 0.10663  0.05227  45  THR B CA  
2224 C C   . THR B 48  ? 0.69835 0.71522 0.61971 -0.02850 0.11172  0.05506  45  THR B C   
2225 O O   . THR B 48  ? 0.70854 0.73345 0.64735 -0.03659 0.10685  0.05785  45  THR B O   
2226 C CB  . THR B 48  ? 0.62292 0.61260 0.50236 -0.02022 0.08918  0.04474  45  THR B CB  
2227 O OG1 . THR B 48  ? 0.65491 0.62135 0.50069 -0.01664 0.08303  0.04247  45  THR B OG1 
2228 C CG2 . THR B 48  ? 0.54980 0.54915 0.44879 -0.02584 0.07621  0.04424  45  THR B CG2 
2229 N N   . GLU B 49  ? 0.71405 0.74456 0.64917 -0.02314 0.12113  0.05451  46  GLU B N   
2230 C CA  . GLU B 49  ? 0.73013 0.78860 0.70459 -0.02603 0.12459  0.05745  46  GLU B CA  
2231 C C   . GLU B 49  ? 0.75895 0.82414 0.74913 -0.03476 0.13595  0.06544  46  GLU B C   
2232 O O   . GLU B 49  ? 0.76112 0.84919 0.78547 -0.04076 0.13361  0.06814  46  GLU B O   
2233 C CB  . GLU B 49  ? 0.75425 0.82345 0.73767 -0.01687 0.13459  0.05624  46  GLU B CB  
2234 C CG  . GLU B 49  ? 0.83219 0.89886 0.80737 -0.00962 0.12288  0.04832  46  GLU B CG  
2235 C CD  . GLU B 49  ? 0.93301 1.00196 0.90701 0.00032  0.13467  0.04689  46  GLU B CD  
2236 O OE1 . GLU B 49  ? 0.93719 1.01107 0.91546 0.00570  0.12694  0.04160  46  GLU B OE1 
2237 O OE2 . GLU B 49  ? 0.98328 1.04725 0.95078 0.00300  0.15269  0.05117  46  GLU B OE2 
2238 N N   . LYS B 50  ? 0.77600 0.82088 0.74145 -0.03608 0.14773  0.06929  47  LYS B N   
2239 C CA  . LYS B 50  ? 0.75929 0.80672 0.73636 -0.04520 0.15973  0.07699  47  LYS B CA  
2240 C C   . LYS B 50  ? 0.72762 0.76281 0.69587 -0.05454 0.14872  0.07799  47  LYS B C   
2241 O O   . LYS B 50  ? 0.72935 0.76554 0.70757 -0.06382 0.15707  0.08409  47  LYS B O   
2242 C CB  . LYS B 50  ? 0.82196 0.85098 0.77482 -0.04150 0.18106  0.08133  47  LYS B CB  
2243 C CG  . LYS B 50  ? 0.83635 0.87203 0.79216 -0.03121 0.19421  0.08038  47  LYS B CG  
2244 C CD  . LYS B 50  ? 0.84212 0.91364 0.84678 -0.03203 0.19795  0.08294  47  LYS B CD  
2245 N N   . HIS B 51  ? 0.72944 0.75268 0.67990 -0.05227 0.13117  0.07239  48  HIS B N   
2246 C CA  . HIS B 51  ? 0.72018 0.73106 0.66232 -0.05967 0.12050  0.07318  48  HIS B CA  
2247 C C   . HIS B 51  ? 0.70718 0.73894 0.68293 -0.06809 0.11061  0.07286  48  HIS B C   
2248 O O   . HIS B 51  ? 0.66883 0.72241 0.66920 -0.06586 0.10583  0.07001  48  HIS B O   
2249 C CB  . HIS B 51  ? 0.72171 0.71315 0.63462 -0.05310 0.10612  0.06770  48  HIS B CB  
2250 C CG  . HIS B 51  ? 0.75914 0.73253 0.65706 -0.05828 0.09783  0.06942  48  HIS B CG  
2251 N ND1 . HIS B 51  ? 0.74742 0.72535 0.65749 -0.06224 0.08361  0.06682  48  HIS B ND1 
2252 C CD2 . HIS B 51  ? 0.78383 0.73239 0.65355 -0.05941 0.10228  0.07367  48  HIS B CD2 
2253 C CE1 . HIS B 51  ? 0.76805 0.72530 0.65924 -0.06538 0.08014  0.06941  48  HIS B CE1 
2254 N NE2 . HIS B 51  ? 0.79476 0.73432 0.66163 -0.06365 0.09087  0.07372  48  HIS B NE2 
2255 N N   . GLU B 52  ? 0.74210 0.76467 0.71633 -0.07787 0.10722  0.07586  49  GLU B N   
2256 C CA  . GLU B 52  ? 0.75895 0.79800 0.76227 -0.08782 0.09850  0.07601  49  GLU B CA  
2257 C C   . GLU B 52  ? 0.73165 0.77536 0.73854 -0.08392 0.08036  0.06908  49  GLU B C   
2258 O O   . GLU B 52  ? 0.67482 0.73778 0.70845 -0.08836 0.07325  0.06793  49  GLU B O   
2259 C CB  . GLU B 52  ? 0.83170 0.85465 0.82725 -0.09926 0.09902  0.08025  49  GLU B CB  
2260 C CG  . GLU B 52  ? 0.91496 0.90953 0.87700 -0.09593 0.08970  0.07801  49  GLU B CG  
2261 C CD  . GLU B 52  ? 0.99097 0.97220 0.95057 -0.10746 0.08579  0.08068  49  GLU B CD  
2262 O OE1 . GLU B 52  ? 1.02192 0.98236 0.96148 -0.11079 0.09459  0.08562  49  GLU B OE1 
2263 O OE2 . GLU B 52  ? 0.98845 0.97782 0.96408 -0.11323 0.07413  0.07783  49  GLU B OE2 
2264 N N   . TRP B 53  ? 0.75831 0.78452 0.73896 -0.07574 0.07268  0.06464  50  TRP B N   
2265 C CA  . TRP B 53  ? 0.74655 0.77458 0.72858 -0.07151 0.05744  0.05819  50  TRP B CA  
2266 C C   . TRP B 53  ? 0.67880 0.71696 0.66277 -0.06080 0.05703  0.05345  50  TRP B C   
2267 O O   . TRP B 53  ? 0.69352 0.72495 0.66671 -0.05447 0.04745  0.04803  50  TRP B O   
2268 C CB  . TRP B 53  ? 0.76955 0.77344 0.72563 -0.06953 0.04894  0.05644  50  TRP B CB  
2269 C CG  . TRP B 53  ? 0.84252 0.83493 0.79708 -0.07954 0.04583  0.05951  50  TRP B CG  
2270 C CD1 . TRP B 53  ? 0.88285 0.85721 0.82110 -0.08428 0.05249  0.06478  50  TRP B CD1 
2271 C CD2 . TRP B 53  ? 0.88540 0.88037 0.85224 -0.08611 0.03552  0.05738  50  TRP B CD2 
2272 N NE1 . TRP B 53  ? 0.90130 0.86714 0.84185 -0.09364 0.04727  0.06599  50  TRP B NE1 
2273 C CE2 . TRP B 53  ? 0.91524 0.89309 0.87264 -0.09509 0.03663  0.06135  50  TRP B CE2 
2274 C CE3 . TRP B 53  ? 0.89038 0.89790 0.87260 -0.08525 0.02568  0.05253  50  TRP B CE3 
2275 C CZ2 . TRP B 53  ? 0.94287 0.91539 0.90534 -0.10357 0.02811  0.06025  50  TRP B CZ2 
2276 C CZ3 . TRP B 53  ? 0.90583 0.90787 0.89222 -0.09338 0.01695  0.05160  50  TRP B CZ3 
2277 C CH2 . TRP B 53  ? 0.93953 0.92405 0.91593 -0.10262 0.01813  0.05526  50  TRP B CH2 
2278 N N   . SER B 54  ? 0.63501 0.68873 0.63308 -0.05862 0.06810  0.05554  51  SER B N   
2279 C CA  . SER B 54  ? 0.61719 0.67737 0.61410 -0.04822 0.06958  0.05130  51  SER B CA  
2280 C C   . SER B 54  ? 0.60697 0.67902 0.61881 -0.04573 0.05730  0.04609  51  SER B C   
2281 O O   . SER B 54  ? 0.57748 0.64962 0.58338 -0.03713 0.05573  0.04134  51  SER B O   
2282 C CB  . SER B 54  ? 0.58795 0.66190 0.59836 -0.04610 0.08558  0.05538  51  SER B CB  
2283 O OG  . SER B 54  ? 0.59249 0.69045 0.63739 -0.05170 0.08563  0.05843  51  SER B OG  
2284 N N   . THR B 55  ? 0.59894 0.67882 0.62792 -0.05337 0.04869  0.04679  52  THR B N   
2285 C CA  . THR B 55  ? 0.59296 0.68064 0.63245 -0.05109 0.03692  0.04205  52  THR B CA  
2286 C C   . THR B 55  ? 0.54171 0.61229 0.55992 -0.04554 0.02827  0.03604  52  THR B C   
2287 O O   . THR B 55  ? 0.56294 0.63712 0.58417 -0.04018 0.02223  0.03132  52  THR B O   
2288 C CB  . THR B 55  ? 0.66257 0.75741 0.71959 -0.06146 0.02858  0.04402  52  THR B CB  
2289 O OG1 . THR B 55  ? 0.72544 0.80051 0.76576 -0.06755 0.02335  0.04398  52  THR B OG1 
2290 C CG2 . THR B 55  ? 0.71140 0.82445 0.79251 -0.06840 0.03710  0.05052  52  THR B CG2 
2291 N N   . ALA B 56  ? 0.47577 0.52781 0.47322 -0.04645 0.02788  0.03647  53  ALA B N   
2292 C CA  . ALA B 56  ? 0.49759 0.53502 0.47809 -0.04126 0.01985  0.03155  53  ALA B CA  
2293 C C   . ALA B 56  ? 0.50179 0.53675 0.47044 -0.03215 0.02273  0.02793  53  ALA B C   
2294 O O   . ALA B 56  ? 0.45863 0.48466 0.41714 -0.02772 0.01593  0.02351  53  ALA B O   
2295 C CB  . ALA B 56  ? 0.48103 0.49999 0.44501 -0.04488 0.01766  0.03406  53  ALA B CB  
2296 N N   . LEU B 57  ? 0.48936 0.53132 0.45925 -0.02952 0.03297  0.02968  54  LEU B N   
2297 C CA  . LEU B 57  ? 0.48977 0.52558 0.44415 -0.02183 0.03627  0.02626  54  LEU B CA  
2298 C C   . LEU B 57  ? 0.48313 0.52443 0.44344 -0.01629 0.03083  0.01998  54  LEU B C   
2299 O O   . LEU B 57  ? 0.46181 0.51679 0.44036 -0.01605 0.03096  0.01967  54  LEU B O   
2300 C CB  . LEU B 57  ? 0.55104 0.59126 0.50476 -0.02024 0.05038  0.02987  54  LEU B CB  
2301 C CG  . LEU B 57  ? 0.57707 0.60942 0.51303 -0.01264 0.05596  0.02649  54  LEU B CG  
2302 C CD1 . LEU B 57  ? 0.55358 0.56535 0.46154 -0.01145 0.05069  0.02479  54  LEU B CD1 
2303 C CD2 . LEU B 57  ? 0.58636 0.62349 0.52450 -0.01107 0.07217  0.03087  54  LEU B CD2 
2304 N N   . VAL B 58  ? 0.50800 0.53831 0.45303 -0.01199 0.02577  0.01520  55  VAL B N   
2305 C CA  . VAL B 58  ? 0.49772 0.53059 0.44567 -0.00692 0.02234  0.00902  55  VAL B CA  
2306 C C   . VAL B 58  ? 0.50492 0.54395 0.45392 -0.00234 0.03228  0.00856  55  VAL B C   
2307 O O   . VAL B 58  ? 0.52494 0.55665 0.45888 -0.00054 0.03944  0.00960  55  VAL B O   
2308 C CB  . VAL B 58  ? 0.44406 0.46456 0.37707 -0.00440 0.01516  0.00439  55  VAL B CB  
2309 C CG1 . VAL B 58  ? 0.37084 0.39247 0.30420 0.00041  0.01486  -0.00193 55  VAL B CG1 
2310 C CG2 . VAL B 58  ? 0.45097 0.46727 0.38760 -0.00708 0.00598  0.00446  55  VAL B CG2 
2311 N N   . PRO B 59  ? 0.46514 0.51551 0.42960 0.00021  0.03330  0.00723  56  PRO B N   
2312 C CA  . PRO B 59  ? 0.48312 0.53974 0.45032 0.00558  0.04392  0.00774  56  PRO B CA  
2313 C C   . PRO B 59  ? 0.52857 0.57262 0.47651 0.01095  0.04627  0.00214  56  PRO B C   
2314 O O   . PRO B 59  ? 0.50208 0.53587 0.43902 0.01046  0.03830  -0.00269 56  PRO B O   
2315 C CB  . PRO B 59  ? 0.46116 0.53180 0.44942 0.00723  0.04128  0.00773  56  PRO B CB  
2316 C CG  . PRO B 59  ? 0.44174 0.50699 0.42973 0.00454  0.02927  0.00409  56  PRO B CG  
2317 C CD  . PRO B 59  ? 0.42818 0.48446 0.40676 -0.00117 0.02506  0.00563  56  PRO B CD  
2318 N N   . ALA B 60  ? 0.52138 0.56632 0.46619 0.01606  0.05783  0.00294  57  ALA B N   
2319 C CA  . ALA B 60  ? 0.51357 0.54325 0.43589 0.02036  0.06173  -0.00203 57  ALA B CA  
2320 C C   . ALA B 60  ? 0.50630 0.53334 0.42914 0.02346  0.05634  -0.00866 57  ALA B C   
2321 O O   . ALA B 60  ? 0.49543 0.50860 0.40069 0.02349  0.05275  -0.01426 57  ALA B O   
2322 C CB  . ALA B 60  ? 0.52896 0.55788 0.44629 0.02549  0.07748  0.00097  57  ALA B CB  
2323 N N   . ASP B 61  ? 0.46800 0.50735 0.41020 0.02582  0.05554  -0.00807 58  ASP B N   
2324 C CA  . ASP B 61  ? 0.49746 0.53213 0.43856 0.02899  0.05186  -0.01402 58  ASP B CA  
2325 C C   . ASP B 61  ? 0.52408 0.55347 0.46385 0.02410  0.03988  -0.01791 58  ASP B C   
2326 O O   . ASP B 61  ? 0.57944 0.59885 0.51016 0.02472  0.03720  -0.02392 58  ASP B O   
2327 C CB  . ASP B 61  ? 0.50473 0.55206 0.46453 0.03358  0.05381  -0.01177 58  ASP B CB  
2328 C CG  . ASP B 61  ? 0.54286 0.60245 0.52110 0.02899  0.04516  -0.00810 58  ASP B CG  
2329 O OD1 . ASP B 61  ? 0.54404 0.60726 0.52525 0.02314  0.04288  -0.00440 58  ASP B OD1 
2330 O OD2 . ASP B 61  ? 0.51372 0.57711 0.50129 0.03113  0.04068  -0.00897 58  ASP B OD2 
2331 N N   . GLU B 62  ? 0.48953 0.52494 0.43863 0.01911  0.03330  -0.01444 59  GLU B N   
2332 C CA  . GLU B 62  ? 0.49599 0.52557 0.44365 0.01527  0.02340  -0.01736 59  GLU B CA  
2333 C C   . GLU B 62  ? 0.49323 0.51191 0.42442 0.01354  0.02076  -0.01976 59  GLU B C   
2334 O O   . GLU B 62  ? 0.49440 0.50693 0.42269 0.01266  0.01455  -0.02444 59  GLU B O   
2335 C CB  . GLU B 62  ? 0.44679 0.48261 0.40560 0.01068  0.01805  -0.01278 59  GLU B CB  
2336 C CG  . GLU B 62  ? 0.47209 0.50083 0.42923 0.00769  0.00936  -0.01498 59  GLU B CG  
2337 C CD  . GLU B 62  ? 0.47984 0.51082 0.44370 0.00305  0.00508  -0.01038 59  GLU B CD  
2338 O OE1 . GLU B 62  ? 0.45196 0.49114 0.42587 0.00154  0.00651  -0.00688 59  GLU B OE1 
2339 O OE2 . GLU B 62  ? 0.47393 0.49814 0.43319 0.00088  -0.00001 -0.01015 59  GLU B OE2 
2340 N N   . GLY B 63  ? 0.49762 0.51348 0.41794 0.01303  0.02535  -0.01640 60  GLY B N   
2341 C CA  . GLY B 63  ? 0.52872 0.53236 0.43019 0.01160  0.02154  -0.01831 60  GLY B CA  
2342 C C   . GLY B 63  ? 0.55837 0.55262 0.44830 0.01342  0.02083  -0.02524 60  GLY B C   
2343 O O   . GLY B 63  ? 0.54577 0.53374 0.43000 0.01118  0.01198  -0.02893 60  GLY B O   
2344 N N   . LEU B 64  ? 0.53268 0.52582 0.41981 0.01745  0.03012  -0.02696 61  LEU B N   
2345 C CA  . LEU B 64  ? 0.55180 0.53416 0.42741 0.01864  0.03029  -0.03392 61  LEU B CA  
2346 C C   . LEU B 64  ? 0.52034 0.50553 0.40891 0.01708  0.02308  -0.03846 61  LEU B C   
2347 O O   . LEU B 64  ? 0.48401 0.46049 0.36503 0.01520  0.01906  -0.04440 61  LEU B O   
2348 C CB  . LEU B 64  ? 0.52823 0.50795 0.39891 0.02432  0.04301  -0.03421 61  LEU B CB  
2349 C CG  . LEU B 64  ? 0.60840 0.57721 0.45785 0.02643  0.05233  -0.03247 61  LEU B CG  
2350 C CD1 . LEU B 64  ? 0.65714 0.62533 0.50637 0.03342  0.06602  -0.03198 61  LEU B CD1 
2351 C CD2 . LEU B 64  ? 0.63768 0.58777 0.46166 0.02317  0.04666  -0.03807 61  LEU B CD2 
2352 N N   . PHE B 65  ? 0.50379 0.49990 0.41114 0.01745  0.02171  -0.03579 62  PHE B N   
2353 C CA  . PHE B 65  ? 0.52510 0.52181 0.44334 0.01627  0.01646  -0.03957 62  PHE B CA  
2354 C C   . PHE B 65  ? 0.51028 0.50571 0.43043 0.01191  0.00647  -0.04070 62  PHE B C   
2355 O O   . PHE B 65  ? 0.51539 0.50725 0.43845 0.01026  0.00270  -0.04569 62  PHE B O   
2356 C CB  . PHE B 65  ? 0.53494 0.54049 0.46860 0.01794  0.01753  -0.03617 62  PHE B CB  
2357 C CG  . PHE B 65  ? 0.59087 0.59463 0.53356 0.01690  0.01326  -0.03921 62  PHE B CG  
2358 C CD1 . PHE B 65  ? 0.63204 0.62846 0.57246 0.01817  0.01583  -0.04485 62  PHE B CD1 
2359 C CD2 . PHE B 65  ? 0.64842 0.65581 0.60056 0.01465  0.00795  -0.03634 62  PHE B CD2 
2360 C CE1 . PHE B 65  ? 0.67420 0.66763 0.62250 0.01729  0.01384  -0.04736 62  PHE B CE1 
2361 C CE2 . PHE B 65  ? 0.66050 0.66400 0.61930 0.01428  0.00590  -0.03893 62  PHE B CE2 
2362 C CZ  . PHE B 65  ? 0.68979 0.68666 0.64713 0.01565  0.00920  -0.04433 62  PHE B CZ  
2363 N N   . LEU B 66  ? 0.50474 0.50312 0.42430 0.01019  0.00247  -0.03580 63  LEU B N   
2364 C CA  . LEU B 66  ? 0.50858 0.50529 0.42875 0.00736  -0.00722 -0.03605 63  LEU B CA  
2365 C C   . LEU B 66  ? 0.55209 0.54057 0.45844 0.00585  -0.01148 -0.04058 63  LEU B C   
2366 O O   . LEU B 66  ? 0.52951 0.51783 0.44177 0.00371  -0.01927 -0.04396 63  LEU B O   
2367 C CB  . LEU B 66  ? 0.48414 0.48253 0.40203 0.00641  -0.00957 -0.02949 63  LEU B CB  
2368 C CG  . LEU B 66  ? 0.44926 0.45449 0.37810 0.00642  -0.00579 -0.02460 63  LEU B CG  
2369 C CD1 . LEU B 66  ? 0.43982 0.44394 0.36387 0.00447  -0.00780 -0.01846 63  LEU B CD1 
2370 C CD2 . LEU B 66  ? 0.44044 0.44825 0.38415 0.00641  -0.00842 -0.02628 63  LEU B CD2 
2371 N N   . SER B 67  ? 0.55434 0.53543 0.44219 0.00676  -0.00636 -0.04060 64  SER B N   
2372 C CA  . SER B 67  ? 0.57392 0.54361 0.44381 0.00479  -0.01062 -0.04530 64  SER B CA  
2373 C C   . SER B 67  ? 0.55361 0.52111 0.42901 0.00317  -0.01140 -0.05252 64  SER B C   
2374 O O   . SER B 67  ? 0.51243 0.47608 0.38552 -0.00067 -0.02057 -0.05675 64  SER B O   
2375 C CB  . SER B 67  ? 0.61673 0.57588 0.46366 0.00687  -0.00178 -0.04415 64  SER B CB  
2376 O OG  . SER B 67  ? 0.72223 0.66667 0.54752 0.00462  -0.00588 -0.04924 64  SER B OG  
2377 N N   . MET B 68  ? 0.51860 0.48827 0.40159 0.00588  -0.00218 -0.05384 65  MET B N   
2378 C CA  . MET B 68  ? 0.51658 0.48217 0.40387 0.00439  -0.00112 -0.06041 65  MET B CA  
2379 C C   . MET B 68  ? 0.51697 0.48994 0.42423 0.00115  -0.00911 -0.06196 65  MET B C   
2380 O O   . MET B 68  ? 0.50324 0.47280 0.41264 -0.00305 -0.01392 -0.06739 65  MET B O   
2381 C CB  . MET B 68  ? 0.51307 0.47868 0.40363 0.00918  0.01036  -0.06029 65  MET B CB  
2382 C CG  . MET B 68  ? 0.51542 0.47426 0.40848 0.00811  0.01328  -0.06666 65  MET B CG  
2383 S SD  . MET B 68  ? 0.56637 0.50749 0.43614 0.00466  0.01405  -0.07382 65  MET B SD  
2384 C CE  . MET B 68  ? 0.55318 0.48700 0.40373 0.01191  0.02659  -0.07050 65  MET B CE  
2385 N N   . LEU B 69  ? 0.52040 0.50296 0.44285 0.00287  -0.01002 -0.05720 66  LEU B N   
2386 C CA  . LEU B 69  ? 0.53834 0.52686 0.47981 0.00098  -0.01552 -0.05797 66  LEU B CA  
2387 C C   . LEU B 69  ? 0.52761 0.51779 0.47050 -0.00266 -0.02719 -0.05889 66  LEU B C   
2388 O O   . LEU B 69  ? 0.49107 0.48380 0.44710 -0.00570 -0.03146 -0.06270 66  LEU B O   
2389 C CB  . LEU B 69  ? 0.58477 0.57979 0.53720 0.00360  -0.01442 -0.05229 66  LEU B CB  
2390 C CG  . LEU B 69  ? 0.69678 0.69134 0.65188 0.00678  -0.00569 -0.05125 66  LEU B CG  
2391 C CD1 . LEU B 69  ? 0.72621 0.72508 0.68988 0.00785  -0.00694 -0.04601 66  LEU B CD1 
2392 C CD2 . LEU B 69  ? 0.72678 0.71660 0.68780 0.00664  -0.00112 -0.05653 66  LEU B CD2 
2393 N N   . LEU B 70  ? 0.48442 0.47321 0.41446 -0.00231 -0.03254 -0.05508 67  LEU B N   
2394 C CA  . LEU B 70  ? 0.51132 0.50082 0.44048 -0.00494 -0.04536 -0.05516 67  LEU B CA  
2395 C C   . LEU B 70  ? 0.54296 0.52679 0.46632 -0.00975 -0.05031 -0.06218 67  LEU B C   
2396 O O   . LEU B 70  ? 0.53770 0.52705 0.47446 -0.01304 -0.06046 -0.06429 67  LEU B O   
2397 C CB  . LEU B 70  ? 0.52728 0.51161 0.43711 -0.00343 -0.04864 -0.04999 67  LEU B CB  
2398 C CG  . LEU B 70  ? 0.51003 0.49958 0.42648 -0.00028 -0.04750 -0.04271 67  LEU B CG  
2399 C CD1 . LEU B 70  ? 0.54175 0.52340 0.43584 0.00081  -0.04606 -0.03804 67  LEU B CD1 
2400 C CD2 . LEU B 70  ? 0.50222 0.49859 0.43516 0.00002  -0.05783 -0.04073 67  LEU B CD2 
2401 N N   . LYS B 71  ? 0.56197 0.53461 0.46614 -0.01033 -0.04319 -0.06580 68  LYS B N   
2402 C CA  . LYS B 71  ? 0.59416 0.55765 0.48814 -0.01576 -0.04788 -0.07284 68  LYS B CA  
2403 C C   . LYS B 71  ? 0.59970 0.56715 0.51359 -0.01905 -0.04501 -0.07821 68  LYS B C   
2404 O O   . LYS B 71  ? 0.57167 0.53968 0.49232 -0.02521 -0.05389 -0.08295 68  LYS B O   
2405 C CB  . LYS B 71  ? 0.62713 0.57426 0.49155 -0.01464 -0.03962 -0.07479 68  LYS B CB  
2406 C CG  . LYS B 71  ? 0.65556 0.59499 0.49653 -0.01271 -0.04258 -0.07041 68  LYS B CG  
2407 C CD  . LYS B 71  ? 0.71533 0.63702 0.52700 -0.01109 -0.03235 -0.07243 68  LYS B CD  
2408 C CE  . LYS B 71  ? 0.78021 0.69109 0.56577 -0.00964 -0.03457 -0.06836 68  LYS B CE  
2409 N NZ  . LYS B 71  ? 0.86516 0.75912 0.62365 -0.00637 -0.02083 -0.06896 68  LYS B NZ  
2410 N N   . LEU B 72  ? 0.56886 0.53853 0.49219 -0.01533 -0.03291 -0.07742 69  LEU B N   
2411 C CA  . LEU B 72  ? 0.55166 0.52199 0.49098 -0.01803 -0.02813 -0.08221 69  LEU B CA  
2412 C C   . LEU B 72  ? 0.53072 0.51393 0.49734 -0.02104 -0.03613 -0.08192 69  LEU B C   
2413 O O   . LEU B 72  ? 0.55121 0.53504 0.53052 -0.02650 -0.03719 -0.08704 69  LEU B O   
2414 C CB  . LEU B 72  ? 0.53122 0.50003 0.47298 -0.01243 -0.01462 -0.08040 69  LEU B CB  
2415 C CG  . LEU B 72  ? 0.51610 0.47206 0.43630 -0.00945 -0.00457 -0.08218 69  LEU B CG  
2416 C CD1 . LEU B 72  ? 0.50330 0.45985 0.42847 -0.00331 0.00621  -0.07946 69  LEU B CD1 
2417 C CD2 . LEU B 72  ? 0.51401 0.45733 0.42490 -0.01493 -0.00343 -0.08985 69  LEU B CD2 
2418 N N   . MET B 73  ? 0.51640 0.50966 0.49315 -0.01751 -0.04108 -0.07579 70  MET B N   
2419 C CA  . MET B 73  ? 0.52577 0.53149 0.52932 -0.01870 -0.04778 -0.07450 70  MET B CA  
2420 C C   . MET B 73  ? 0.54640 0.55753 0.55148 -0.02213 -0.06404 -0.07430 70  MET B C   
2421 O O   . MET B 73  ? 0.54424 0.56755 0.57352 -0.02247 -0.07106 -0.07259 70  MET B O   
2422 C CB  . MET B 73  ? 0.49311 0.50476 0.50691 -0.01250 -0.04385 -0.06791 70  MET B CB  
2423 C CG  . MET B 73  ? 0.53563 0.54852 0.53811 -0.00918 -0.05079 -0.06176 70  MET B CG  
2424 S SD  . MET B 73  ? 0.53370 0.55043 0.54680 -0.00314 -0.04559 -0.05473 70  MET B SD  
2425 C CE  . MET B 73  ? 0.49166 0.51901 0.53620 -0.00316 -0.04969 -0.05474 70  MET B CE  
2426 N N   . ASN B 74  ? 0.54668 0.54817 0.52589 -0.02415 -0.07005 -0.07571 71  ASN B N   
2427 C CA  . ASN B 74  ? 0.60749 0.61046 0.58236 -0.02777 -0.08702 -0.07598 71  ASN B CA  
2428 C C   . ASN B 74  ? 0.58187 0.59501 0.56724 -0.02275 -0.09550 -0.06851 71  ASN B C   
2429 O O   . ASN B 74  ? 0.59369 0.61759 0.59767 -0.02424 -0.10823 -0.06767 71  ASN B O   
2430 C CB  . ASN B 74  ? 0.65852 0.66705 0.65175 -0.03573 -0.09479 -0.08223 71  ASN B CB  
2431 C CG  . ASN B 74  ? 0.77669 0.78273 0.75866 -0.04095 -0.11352 -0.08403 71  ASN B CG  
2432 O OD1 . ASN B 74  ? 0.84275 0.83375 0.79159 -0.04080 -0.11673 -0.08416 71  ASN B OD1 
2433 N ND2 . ASN B 74  ? 0.79048 0.81087 0.79999 -0.04549 -0.12606 -0.08519 71  ASN B ND2 
2434 N N   . ALA B 75  ? 0.53113 0.54081 0.50527 -0.01669 -0.08830 -0.06281 72  ALA B N   
2435 C CA  . ALA B 75  ? 0.53036 0.54621 0.51081 -0.01171 -0.09465 -0.05549 72  ALA B CA  
2436 C C   . ALA B 75  ? 0.59222 0.60334 0.55542 -0.01260 -0.11036 -0.05379 72  ALA B C   
2437 O O   . ALA B 75  ? 0.61915 0.61697 0.55427 -0.01531 -0.11209 -0.05643 72  ALA B O   
2438 C CB  . ALA B 75  ? 0.51438 0.52557 0.48439 -0.00660 -0.08326 -0.05024 72  ALA B CB  
2439 N N   . LYS B 76  ? 0.61049 0.63098 0.58930 -0.00974 -0.12164 -0.04917 73  LYS B N   
2440 C CA  . LYS B 76  ? 0.65657 0.67283 0.62035 -0.00935 -0.13846 -0.04640 73  LYS B CA  
2441 C C   . LYS B 76  ? 0.67895 0.69386 0.63821 -0.00210 -0.14016 -0.03762 73  LYS B C   
2442 O O   . LYS B 76  ? 0.72373 0.72583 0.65451 -0.00070 -0.14606 -0.03438 73  LYS B O   
2443 C CB  . LYS B 76  ? 0.63609 0.66551 0.62409 -0.01287 -0.15467 -0.04897 73  LYS B CB  
2444 C CG  . LYS B 76  ? 0.75019 0.77879 0.73999 -0.02176 -0.15619 -0.05795 73  LYS B CG  
2445 C CD  . LYS B 76  ? 0.84701 0.86202 0.80664 -0.02673 -0.17143 -0.06097 73  LYS B CD  
2446 C CE  . LYS B 76  ? 0.88777 0.90914 0.86251 -0.03607 -0.18263 -0.06839 73  LYS B CE  
2447 N NZ  . LYS B 76  ? 0.93393 0.96495 0.91982 -0.03709 -0.20637 -0.06609 73  LYS B NZ  
2448 N N   . ARG B 77  ? 0.64709 0.67251 0.63174 0.00254  -0.13438 -0.03369 74  ARG B N   
2449 C CA  . ARG B 77  ? 0.64640 0.66947 0.62840 0.00939  -0.13518 -0.02540 74  ARG B CA  
2450 C C   . ARG B 77  ? 0.59362 0.61441 0.57840 0.01146  -0.11775 -0.02354 74  ARG B C   
2451 O O   . ARG B 77  ? 0.56502 0.59401 0.57271 0.01129  -0.10952 -0.02594 74  ARG B O   
2452 C CB  . ARG B 77  ? 0.67371 0.71026 0.68383 0.01380  -0.14668 -0.02174 74  ARG B CB  
2453 C CG  . ARG B 77  ? 0.76201 0.79360 0.76663 0.02156  -0.14924 -0.01288 74  ARG B CG  
2454 C CD  . ARG B 77  ? 0.83257 0.87791 0.86544 0.02699  -0.16165 -0.00899 74  ARG B CD  
2455 N NE  . ARG B 77  ? 0.90042 0.93921 0.92802 0.03540  -0.16240 -0.00023 74  ARG B NE  
2456 C CZ  . ARG B 77  ? 0.93886 0.96682 0.94260 0.03881  -0.17394 0.00503  74  ARG B CZ  
2457 N NH1 . ARG B 77  ? 0.95697 0.97756 0.95634 0.04662  -0.17297 0.01306  74  ARG B NH1 
2458 N NH2 . ARG B 77  ? 0.93388 0.95580 0.91559 0.03447  -0.18607 0.00228  74  ARG B NH2 
2459 N N   . THR B 78  ? 0.57776 0.58652 0.53856 0.01293  -0.11215 -0.01932 75  THR B N   
2460 C CA  . THR B 78  ? 0.57206 0.57793 0.53288 0.01351  -0.09715 -0.01773 75  THR B CA  
2461 C C   . THR B 78  ? 0.55621 0.55455 0.50795 0.01767  -0.09657 -0.00986 75  THR B C   
2462 O O   . THR B 78  ? 0.58640 0.57880 0.52524 0.02019  -0.10626 -0.00556 75  THR B O   
2463 C CB  . THR B 78  ? 0.55672 0.55581 0.49860 0.00955  -0.08747 -0.02108 75  THR B CB  
2464 O OG1 . THR B 78  ? 0.58029 0.56756 0.49431 0.00964  -0.08938 -0.01751 75  THR B OG1 
2465 C CG2 . THR B 78  ? 0.54012 0.54234 0.48461 0.00541  -0.08872 -0.02882 75  THR B CG2 
2466 N N   . ILE B 79  ? 0.52130 0.51814 0.47814 0.01811  -0.08533 -0.00802 76  ILE B N   
2467 C CA  . ILE B 79  ? 0.54767 0.53533 0.49488 0.02054  -0.08249 -0.00109 76  ILE B CA  
2468 C C   . ILE B 79  ? 0.55930 0.54250 0.49733 0.01662  -0.07019 -0.00117 76  ILE B C   
2469 O O   . ILE B 79  ? 0.50489 0.49352 0.45326 0.01441  -0.06309 -0.00549 76  ILE B O   
2470 C CB  . ILE B 79  ? 0.58283 0.57248 0.54906 0.02553  -0.08298 0.00215  76  ILE B CB  
2471 C CG1 . ILE B 79  ? 0.64045 0.61764 0.59469 0.02702  -0.07822 0.00873  76  ILE B CG1 
2472 C CG2 . ILE B 79  ? 0.56639 0.56360 0.55385 0.02468  -0.07539 -0.00261 76  ILE B CG2 
2473 C CD1 . ILE B 79  ? 0.67802 0.65308 0.64578 0.03323  -0.07939 0.01284  76  ILE B CD1 
2474 N N   . GLU B 80  ? 0.59923 0.57249 0.51806 0.01574  -0.06790 0.00387  77  GLU B N   
2475 C CA  . GLU B 80  ? 0.59416 0.56483 0.50518 0.01146  -0.05716 0.00456  77  GLU B CA  
2476 C C   . GLU B 80  ? 0.58546 0.54742 0.49251 0.01116  -0.05373 0.01080  77  GLU B C   
2477 O O   . GLU B 80  ? 0.61662 0.56853 0.50902 0.01273  -0.05705 0.01607  77  GLU B O   
2478 C CB  . GLU B 80  ? 0.60570 0.57189 0.49630 0.00936  -0.05533 0.00445  77  GLU B CB  
2479 C CG  . GLU B 80  ? 0.69930 0.66783 0.58796 0.00542  -0.04366 0.00393  77  GLU B CG  
2480 C CD  . GLU B 80  ? 0.79037 0.76513 0.68054 0.00477  -0.04090 -0.00234 77  GLU B CD  
2481 O OE1 . GLU B 80  ? 0.78602 0.76534 0.67969 0.00282  -0.03176 -0.00319 77  GLU B OE1 
2482 O OE2 . GLU B 80  ? 0.81607 0.79089 0.70423 0.00615  -0.04821 -0.00631 77  GLU B OE2 
2483 N N   . ILE B 81  ? 0.53353 0.49724 0.45144 0.00893  -0.04735 0.01020  78  ILE B N   
2484 C CA  . ILE B 81  ? 0.54822 0.50215 0.46288 0.00754  -0.04414 0.01526  78  ILE B CA  
2485 C C   . ILE B 81  ? 0.51732 0.47159 0.42709 0.00097  -0.03612 0.01636  78  ILE B C   
2486 O O   . ILE B 81  ? 0.49511 0.45702 0.41496 -0.00176 -0.03207 0.01281  78  ILE B O   
2487 C CB  . ILE B 81  ? 0.58728 0.54002 0.51619 0.00971  -0.04364 0.01393  78  ILE B CB  
2488 C CG1 . ILE B 81  ? 0.63482 0.59034 0.57338 0.01659  -0.05072 0.01321  78  ILE B CG1 
2489 C CG2 . ILE B 81  ? 0.58947 0.52865 0.51148 0.00771  -0.04033 0.01886  78  ILE B CG2 
2490 C CD1 . ILE B 81  ? 0.66968 0.62330 0.62279 0.01976  -0.04822 0.01206  78  ILE B CD1 
2491 N N   . GLY B 82  ? 0.55250 0.49843 0.44739 -0.00146 -0.03379 0.02163  79  GLY B N   
2492 C CA  . GLY B 82  ? 0.58763 0.53576 0.48012 -0.00793 -0.02569 0.02337  79  GLY B CA  
2493 C C   . GLY B 82  ? 0.59023 0.54314 0.47453 -0.00778 -0.02243 0.02240  79  GLY B C   
2494 O O   . GLY B 82  ? 0.56781 0.53160 0.46037 -0.00729 -0.02074 0.01761  79  GLY B O   
2495 N N   . VAL B 83  ? 0.58254 0.52499 0.44835 -0.00785 -0.02075 0.02700  80  VAL B N   
2496 C CA  . VAL B 83  ? 0.61077 0.55256 0.46302 -0.00654 -0.01788 0.02612  80  VAL B CA  
2497 C C   . VAL B 83  ? 0.56019 0.50478 0.41128 -0.01154 -0.00550 0.02884  80  VAL B C   
2498 O O   . VAL B 83  ? 0.53493 0.48707 0.38768 -0.01104 -0.00008 0.02597  80  VAL B O   
2499 C CB  . VAL B 83  ? 0.65183 0.57803 0.48106 -0.00255 -0.02418 0.02934  80  VAL B CB  
2500 C CG1 . VAL B 83  ? 0.65954 0.58006 0.46894 -0.00181 -0.02016 0.02879  80  VAL B CG1 
2501 C CG2 . VAL B 83  ? 0.61604 0.54380 0.45134 0.00288  -0.03701 0.02645  80  VAL B CG2 
2502 N N   . TYR B 84  ? 0.56271 0.50095 0.41152 -0.01634 -0.00029 0.03460  81  TYR B N   
2503 C CA  . TYR B 84  ? 0.57093 0.51220 0.42089 -0.02185 0.01225  0.03834  81  TYR B CA  
2504 C C   . TYR B 84  ? 0.61938 0.55129 0.44709 -0.01873 0.01796  0.03955  81  TYR B C   
2505 O O   . TYR B 84  ? 0.65876 0.57404 0.46384 -0.01527 0.01288  0.04143  81  TYR B O   
2506 C CB  . TYR B 84  ? 0.54519 0.50607 0.42018 -0.02481 0.01582  0.03528  81  TYR B CB  
2507 C CG  . TYR B 84  ? 0.58999 0.55823 0.47352 -0.03082 0.02793  0.03960  81  TYR B CG  
2508 C CD1 . TYR B 84  ? 0.57834 0.53566 0.45226 -0.03600 0.03459  0.04607  81  TYR B CD1 
2509 C CD2 . TYR B 84  ? 0.58381 0.57004 0.48598 -0.03107 0.03320  0.03757  81  TYR B CD2 
2510 C CE1 . TYR B 84  ? 0.54675 0.51252 0.43192 -0.04215 0.04659  0.05029  81  TYR B CE1 
2511 C CE2 . TYR B 84  ? 0.56416 0.55987 0.47834 -0.03617 0.04431  0.04202  81  TYR B CE2 
2512 C CZ  . TYR B 84  ? 0.55384 0.54006 0.46063 -0.04209 0.05117  0.04831  81  TYR B CZ  
2513 O OH  . TYR B 84  ? 0.56759 0.56502 0.48980 -0.04776 0.06300  0.05294  81  TYR B OH  
2514 N N   . THR B 85  ? 0.62831 0.56853 0.45974 -0.01920 0.02826  0.03874  82  THR B N   
2515 C CA  . THR B 85  ? 0.65237 0.58013 0.45907 -0.01593 0.03493  0.03963  82  THR B CA  
2516 C C   . THR B 85  ? 0.69441 0.61889 0.48967 -0.00979 0.02609  0.03331  82  THR B C   
2517 O O   . THR B 85  ? 0.75920 0.66944 0.52904 -0.00694 0.02924  0.03330  82  THR B O   
2518 C CB  . THR B 85  ? 0.61041 0.54686 0.42512 -0.01807 0.05131  0.04167  82  THR B CB  
2519 O OG1 . THR B 85  ? 0.56974 0.52583 0.40778 -0.01666 0.05101  0.03674  82  THR B OG1 
2520 C CG2 . THR B 85  ? 0.60577 0.54538 0.43234 -0.02550 0.06019  0.04834  82  THR B CG2 
2521 N N   . GLY B 86  ? 0.63630 0.57204 0.44846 -0.00820 0.01563  0.02794  83  GLY B N   
2522 C CA  . GLY B 86  ? 0.63476 0.56717 0.43817 -0.00367 0.00538  0.02214  83  GLY B CA  
2523 C C   . GLY B 86  ? 0.64272 0.58399 0.45249 -0.00185 0.00890  0.01602  83  GLY B C   
2524 O O   . GLY B 86  ? 0.62326 0.55755 0.41938 0.00092  0.00250  0.01144  83  GLY B O   
2525 N N   . TYR B 87  ? 0.59322 0.54900 0.42302 -0.00336 0.01811  0.01584  84  TYR B N   
2526 C CA  . TYR B 87  ? 0.55614 0.51855 0.39046 -0.00063 0.02254  0.01056  84  TYR B CA  
2527 C C   . TYR B 87  ? 0.55049 0.51667 0.39223 0.00115  0.01095  0.00376  84  TYR B C   
2528 O O   . TYR B 87  ? 0.59054 0.55004 0.41958 0.00341  0.00869  -0.00120 84  TYR B O   
2529 C CB  . TYR B 87  ? 0.51376 0.49251 0.37095 -0.00183 0.03288  0.01244  84  TYR B CB  
2530 C CG  . TYR B 87  ? 0.50892 0.49208 0.36778 0.00225  0.03996  0.00831  84  TYR B CG  
2531 C CD1 . TYR B 87  ? 0.52229 0.49765 0.36555 0.00476  0.05265  0.00988  84  TYR B CD1 
2532 C CD2 . TYR B 87  ? 0.47429 0.46689 0.34822 0.00407  0.03501  0.00297  84  TYR B CD2 
2533 C CE1 . TYR B 87  ? 0.49343 0.47061 0.33663 0.00932  0.06004  0.00625  84  TYR B CE1 
2534 C CE2 . TYR B 87  ? 0.44535 0.43975 0.31903 0.00830  0.04189  -0.00062 84  TYR B CE2 
2535 C CZ  . TYR B 87  ? 0.47010 0.45688 0.32863 0.01108  0.05428  0.00104  84  TYR B CZ  
2536 O OH  . TYR B 87  ? 0.49887 0.48543 0.35580 0.01603  0.06202  -0.00236 84  TYR B OH  
2537 N N   . SER B 88  ? 0.50015 0.47559 0.36170 -0.00024 0.00415  0.00338  85  SER B N   
2538 C CA  . SER B 88  ? 0.50443 0.48319 0.37461 0.00130  -0.00528 -0.00258 85  SER B CA  
2539 C C   . SER B 88  ? 0.50690 0.47526 0.36253 0.00245  -0.01626 -0.00392 85  SER B C   
2540 O O   . SER B 88  ? 0.49884 0.46757 0.35548 0.00351  -0.02252 -0.00959 85  SER B O   
2541 C CB  . SER B 88  ? 0.50054 0.48845 0.39240 -0.00008 -0.00862 -0.00214 85  SER B CB  
2542 O OG  . SER B 88  ? 0.50767 0.49033 0.39771 -0.00157 -0.01323 0.00258  85  SER B OG  
2543 N N   . LEU B 89  ? 0.51912 0.47793 0.36139 0.00211  -0.01908 0.00138  86  LEU B N   
2544 C CA  . LEU B 89  ? 0.54828 0.49667 0.37506 0.00389  -0.03077 0.00094  86  LEU B CA  
2545 C C   . LEU B 89  ? 0.61503 0.55316 0.41927 0.00455  -0.03066 -0.00278 86  LEU B C   
2546 O O   . LEU B 89  ? 0.63412 0.57096 0.43610 0.00503  -0.04084 -0.00778 86  LEU B O   
2547 C CB  . LEU B 89  ? 0.57522 0.51292 0.38918 0.00406  -0.03257 0.00817  86  LEU B CB  
2548 C CG  . LEU B 89  ? 0.61116 0.53655 0.40664 0.00680  -0.04561 0.00923  86  LEU B CG  
2549 C CD1 . LEU B 89  ? 0.47760 0.41266 0.29259 0.00878  -0.05862 0.00591  86  LEU B CD1 
2550 C CD2 . LEU B 89  ? 0.56988 0.48204 0.34967 0.00743  -0.04485 0.01712  86  LEU B CD2 
2551 N N   . LEU B 90  ? 0.61077 0.54068 0.39802 0.00429  -0.01872 -0.00040 87  LEU B N   
2552 C CA  . LEU B 90  ? 0.61690 0.53349 0.37912 0.00519  -0.01636 -0.00400 87  LEU B CA  
2553 C C   . LEU B 90  ? 0.62063 0.54494 0.39395 0.00525  -0.01571 -0.01153 87  LEU B C   
2554 O O   . LEU B 90  ? 0.65497 0.56931 0.41216 0.00507  -0.02169 -0.01677 87  LEU B O   
2555 C CB  . LEU B 90  ? 0.59033 0.49739 0.33541 0.00555  -0.00023 0.00052  87  LEU B CB  
2556 C CG  . LEU B 90  ? 0.64467 0.53470 0.36082 0.00711  0.00631  -0.00272 87  LEU B CG  
2557 C CD1 . LEU B 90  ? 0.67154 0.54247 0.35853 0.00716  -0.00800 -0.00504 87  LEU B CD1 
2558 C CD2 . LEU B 90  ? 0.61904 0.50068 0.32174 0.00801  0.02468  0.00294  87  LEU B CD2 
2559 N N   . THR B 91  ? 0.56682 0.50719 0.36601 0.00524  -0.00886 -0.01216 88  THR B N   
2560 C CA  . THR B 91  ? 0.58176 0.52882 0.39255 0.00564  -0.00844 -0.01892 88  THR B CA  
2561 C C   . THR B 91  ? 0.57828 0.52641 0.39485 0.00423  -0.02319 -0.02391 88  THR B C   
2562 O O   . THR B 91  ? 0.56478 0.50770 0.37425 0.00341  -0.02608 -0.03015 88  THR B O   
2563 C CB  . THR B 91  ? 0.56724 0.53067 0.40482 0.00614  -0.00125 -0.01780 88  THR B CB  
2564 O OG1 . THR B 91  ? 0.55715 0.52208 0.39277 0.00734  0.01238  -0.01347 88  THR B OG1 
2565 C CG2 . THR B 91  ? 0.55310 0.52155 0.40172 0.00694  -0.00134 -0.02448 88  THR B CG2 
2566 N N   . THR B 92  ? 0.58000 0.53462 0.41022 0.00383  -0.03219 -0.02106 89  THR B N   
2567 C CA  . THR B 92  ? 0.58983 0.54810 0.43031 0.00299  -0.04571 -0.02477 89  THR B CA  
2568 C C   . THR B 92  ? 0.63724 0.58259 0.45461 0.00207  -0.05653 -0.02663 89  THR B C   
2569 O O   . THR B 92  ? 0.65823 0.60381 0.47781 -0.00003 -0.06449 -0.03262 89  THR B O   
2570 C CB  . THR B 92  ? 0.53129 0.49760 0.38992 0.00404  -0.05124 -0.02023 89  THR B CB  
2571 O OG1 . THR B 92  ? 0.52181 0.49761 0.39902 0.00418  -0.04222 -0.01912 89  THR B OG1 
2572 C CG2 . THR B 92  ? 0.45814 0.43030 0.33147 0.00399  -0.06404 -0.02335 89  THR B CG2 
2573 N N   . ALA B 93  ? 0.62713 0.55985 0.42104 0.00315  -0.05722 -0.02154 90  ALA B N   
2574 C CA  . ALA B 93  ? 0.68462 0.60240 0.45281 0.00254  -0.06921 -0.02273 90  ALA B CA  
2575 C C   . ALA B 93  ? 0.72725 0.63321 0.47515 0.00039  -0.06615 -0.02932 90  ALA B C   
2576 O O   . ALA B 93  ? 0.72503 0.62350 0.46143 -0.00204 -0.07908 -0.03383 90  ALA B O   
2577 C CB  . ALA B 93  ? 0.69413 0.59737 0.43753 0.00460  -0.06825 -0.01547 90  ALA B CB  
2578 N N   . LEU B 94  ? 0.69792 0.60163 0.44131 0.00124  -0.04937 -0.02988 91  LEU B N   
2579 C CA  . LEU B 94  ? 0.68868 0.57946 0.41238 0.00006  -0.04412 -0.03606 91  LEU B CA  
2580 C C   . LEU B 94  ? 0.68914 0.58953 0.43252 -0.00263 -0.04809 -0.04355 91  LEU B C   
2581 O O   . LEU B 94  ? 0.75164 0.63920 0.47751 -0.00508 -0.04944 -0.04982 91  LEU B O   
2582 C CB  . LEU B 94  ? 0.68672 0.57330 0.40235 0.00310  -0.02382 -0.03355 91  LEU B CB  
2583 C CG  . LEU B 94  ? 0.75013 0.61998 0.43703 0.00510  -0.01599 -0.02758 91  LEU B CG  
2584 C CD1 . LEU B 94  ? 0.73151 0.60639 0.42512 0.00819  0.00464  -0.02376 91  LEU B CD1 
2585 C CD2 . LEU B 94  ? 0.82024 0.66307 0.46629 0.00418  -0.01987 -0.03136 91  LEU B CD2 
2586 N N   . ALA B 95  ? 0.64780 0.56807 0.42507 -0.00249 -0.04921 -0.04311 92  ALA B N   
2587 C CA  . ALA B 95  ? 0.65830 0.58680 0.45475 -0.00499 -0.05100 -0.04975 92  ALA B CA  
2588 C C   . ALA B 95  ? 0.67998 0.61223 0.48560 -0.00902 -0.06859 -0.05320 92  ALA B C   
2589 O O   . ALA B 95  ? 0.71988 0.65231 0.53155 -0.01292 -0.07148 -0.05997 92  ALA B O   
2590 C CB  . ALA B 95  ? 0.62870 0.57437 0.45521 -0.00277 -0.04287 -0.04779 92  ALA B CB  
2591 N N   . LEU B 96  ? 0.66986 0.60530 0.47773 -0.00813 -0.08020 -0.04845 93  LEU B N   
2592 C CA  . LEU B 96  ? 0.67084 0.61325 0.49229 -0.01095 -0.09771 -0.05043 93  LEU B CA  
2593 C C   . LEU B 96  ? 0.67055 0.59701 0.46495 -0.01535 -0.10964 -0.05510 93  LEU B C   
2594 O O   . LEU B 96  ? 0.71408 0.62108 0.47407 -0.01485 -0.10522 -0.05486 93  LEU B O   
2595 C CB  . LEU B 96  ? 0.67498 0.62463 0.50618 -0.00711 -0.10577 -0.04295 93  LEU B CB  
2596 C CG  . LEU B 96  ? 0.64225 0.60666 0.50124 -0.00364 -0.09692 -0.03881 93  LEU B CG  
2597 C CD1 . LEU B 96  ? 0.63822 0.60577 0.50246 0.00028  -0.10506 -0.03153 93  LEU B CD1 
2598 C CD2 . LEU B 96  ? 0.59279 0.57133 0.48243 -0.00571 -0.09598 -0.04375 93  LEU B CD2 
2599 N N   . PRO B 97  ? 0.66479 0.59837 0.47387 -0.02000 -0.12475 -0.05940 94  PRO B N   
2600 C CA  . PRO B 97  ? 0.70164 0.61993 0.48482 -0.02504 -0.13999 -0.06356 94  PRO B CA  
2601 C C   . PRO B 97  ? 0.73926 0.64643 0.49780 -0.02152 -0.15072 -0.05725 94  PRO B C   
2602 O O   . PRO B 97  ? 0.71079 0.62443 0.47696 -0.01561 -0.14794 -0.04967 94  PRO B O   
2603 C CB  . PRO B 97  ? 0.68028 0.61526 0.49515 -0.03057 -0.15452 -0.06794 94  PRO B CB  
2604 C CG  . PRO B 97  ? 0.66479 0.62303 0.51956 -0.02600 -0.14937 -0.06325 94  PRO B CG  
2605 C CD  . PRO B 97  ? 0.61213 0.56751 0.46245 -0.02134 -0.12810 -0.06082 94  PRO B CD  
2606 N N   . GLU B 98  ? 0.79402 0.68169 0.52000 -0.02549 -0.16339 -0.06059 95  GLU B N   
2607 C CA  . GLU B 98  ? 0.88048 0.75182 0.57503 -0.02211 -0.17343 -0.05490 95  GLU B CA  
2608 C C   . GLU B 98  ? 0.90697 0.79560 0.62651 -0.01812 -0.18845 -0.04830 95  GLU B C   
2609 O O   . GLU B 98  ? 0.92139 0.80102 0.62340 -0.01248 -0.19012 -0.04089 95  GLU B O   
2610 C CB  . GLU B 98  ? 0.94041 0.78726 0.59631 -0.02789 -0.18749 -0.06049 95  GLU B CB  
2611 C CG  . GLU B 98  ? 0.98083 0.80381 0.60294 -0.03032 -0.17135 -0.06607 95  GLU B CG  
2612 N N   . ASP B 99  ? 0.89395 0.80647 0.65429 -0.02053 -0.19818 -0.05049 96  ASP B N   
2613 C CA  . ASP B 99  ? 0.87902 0.80959 0.66736 -0.01594 -0.21173 -0.04425 96  ASP B CA  
2614 C C   . ASP B 99  ? 0.78507 0.73357 0.60583 -0.01005 -0.19674 -0.03914 96  ASP B C   
2615 O O   . ASP B 99  ? 0.75133 0.71664 0.60110 -0.00593 -0.20507 -0.03451 96  ASP B O   
2616 C CB  . ASP B 99  ? 0.90759 0.85486 0.72449 -0.02166 -0.23106 -0.04892 96  ASP B CB  
2617 C CG  . ASP B 99  ? 0.95822 0.91826 0.80246 -0.02807 -0.22070 -0.05658 96  ASP B CG  
2618 O OD1 . ASP B 99  ? 1.00656 0.95163 0.82872 -0.03189 -0.20756 -0.06207 96  ASP B OD1 
2619 O OD2 . ASP B 99  ? 0.97637 0.96046 0.86387 -0.02876 -0.22464 -0.05680 96  ASP B OD2 
2620 N N   . GLY B 100 ? 0.75355 0.69820 0.56971 -0.00935 -0.17529 -0.03973 97  GLY B N   
2621 C CA  . GLY B 100 ? 0.71817 0.67742 0.56205 -0.00474 -0.16195 -0.03547 97  GLY B CA  
2622 C C   . GLY B 100 ? 0.70863 0.66374 0.54487 0.00218  -0.16271 -0.02620 97  GLY B C   
2623 O O   . GLY B 100 ? 0.72707 0.66362 0.52916 0.00377  -0.16544 -0.02273 97  GLY B O   
2624 N N   . LYS B 101 ? 0.67486 0.64523 0.54163 0.00637  -0.15923 -0.02212 98  LYS B N   
2625 C CA  . LYS B 101 ? 0.68856 0.65516 0.55153 0.01298  -0.15940 -0.01331 98  LYS B CA  
2626 C C   . LYS B 101 ? 0.65053 0.62212 0.52769 0.01471  -0.14133 -0.01098 98  LYS B C   
2627 O O   . LYS B 101 ? 0.63281 0.61819 0.53773 0.01345  -0.13485 -0.01449 98  LYS B O   
2628 C CB  . LYS B 101 ? 0.72077 0.69891 0.60582 0.01753  -0.17621 -0.00952 98  LYS B CB  
2629 C CG  . LYS B 101 ? 0.81670 0.78674 0.68210 0.01718  -0.19708 -0.00926 98  LYS B CG  
2630 C CD  . LYS B 101 ? 0.86383 0.85314 0.76099 0.01496  -0.21292 -0.01310 98  LYS B CD  
2631 N N   . ILE B 102 ? 0.62824 0.58736 0.48536 0.01713  -0.13341 -0.00507 99  ILE B N   
2632 C CA  . ILE B 102 ? 0.60583 0.56740 0.47265 0.01774  -0.11761 -0.00250 99  ILE B CA  
2633 C C   . ILE B 102 ? 0.62452 0.57991 0.48839 0.02296  -0.11935 0.00588  99  ILE B C   
2634 O O   . ILE B 102 ? 0.67117 0.61233 0.50970 0.02509  -0.12542 0.01055  99  ILE B O   
2635 C CB  . ILE B 102 ? 0.62242 0.57482 0.46893 0.01413  -0.10320 -0.00366 99  ILE B CB  
2636 C CG1 . ILE B 102 ? 0.56119 0.51606 0.40609 0.00988  -0.10111 -0.01167 99  ILE B CG1 
2637 C CG2 . ILE B 102 ? 0.59865 0.55551 0.45806 0.01393  -0.08913 -0.00108 99  ILE B CG2 
2638 C CD1 . ILE B 102 ? 0.53794 0.48218 0.36014 0.00775  -0.08801 -0.01224 99  ILE B CD1 
2639 N N   . THR B 103 ? 0.57868 0.54203 0.46565 0.02512  -0.11347 0.00782  100 THR B N   
2640 C CA  . THR B 103 ? 0.60232 0.55713 0.48511 0.02929  -0.11106 0.01546  100 THR B CA  
2641 C C   . THR B 103 ? 0.61604 0.56574 0.49281 0.02522  -0.09506 0.01630  100 THR B C   
2642 O O   . THR B 103 ? 0.59056 0.54916 0.48551 0.02294  -0.08684 0.01286  100 THR B O   
2643 C CB  . THR B 103 ? 0.63602 0.60020 0.54638 0.03474  -0.11504 0.01739  100 THR B CB  
2644 O OG1 . THR B 103 ? 0.66243 0.63689 0.58598 0.03737  -0.12968 0.01551  100 THR B OG1 
2645 C CG2 . THR B 103 ? 0.64752 0.59897 0.54831 0.04010  -0.11496 0.02580  100 THR B CG2 
2646 N N   . ALA B 104 ? 0.61605 0.55113 0.46728 0.02409  -0.09084 0.02099  101 ALA B N   
2647 C CA  . ALA B 104 ? 0.65982 0.59092 0.50578 0.01935  -0.07643 0.02238  101 ALA B CA  
2648 C C   . ALA B 104 ? 0.69321 0.61371 0.53550 0.02086  -0.07341 0.02941  101 ALA B C   
2649 O O   . ALA B 104 ? 0.70934 0.61745 0.53601 0.02502  -0.07990 0.03487  101 ALA B O   
2650 C CB  . ALA B 104 ? 0.67191 0.59409 0.49293 0.01601  -0.07089 0.02245  101 ALA B CB  
2651 N N   . ILE B 105 ? 0.67065 0.59431 0.52559 0.01743  -0.06406 0.02928  102 ILE B N   
2652 C CA  . ILE B 105 ? 0.66252 0.57517 0.51545 0.01784  -0.06065 0.03497  102 ILE B CA  
2653 C C   . ILE B 105 ? 0.67148 0.58137 0.52066 0.01005  -0.04861 0.03607  102 ILE B C   
2654 O O   . ILE B 105 ? 0.63270 0.55431 0.49440 0.00576  -0.04326 0.03147  102 ILE B O   
2655 C CB  . ILE B 105 ? 0.61382 0.53150 0.48825 0.02170  -0.06292 0.03368  102 ILE B CB  
2656 C CG1 . ILE B 105 ? 0.60958 0.53474 0.49434 0.02899  -0.07459 0.03235  102 ILE B CG1 
2657 C CG2 . ILE B 105 ? 0.55505 0.45729 0.42337 0.02267  -0.05943 0.03967  102 ILE B CG2 
2658 C CD1 . ILE B 105 ? 0.58487 0.51676 0.49370 0.03317  -0.07477 0.03072  102 ILE B CD1 
2659 N N   . ASP B 106 ? 0.66877 0.56315 0.50142 0.00818  -0.04459 0.04243  103 ASP B N   
2660 C CA  . ASP B 106 ? 0.66115 0.55274 0.49171 -0.00015 -0.03359 0.04437  103 ASP B CA  
2661 C C   . ASP B 106 ? 0.66843 0.53967 0.48159 -0.00103 -0.03100 0.05176  103 ASP B C   
2662 O O   . ASP B 106 ? 0.67769 0.53615 0.47172 0.00391  -0.03515 0.05594  103 ASP B O   
2663 C CB  . ASP B 106 ? 0.64976 0.54767 0.47426 -0.00417 -0.02705 0.04300  103 ASP B CB  
2664 C CG  . ASP B 106 ? 0.65937 0.56272 0.49249 -0.01288 -0.01623 0.04369  103 ASP B CG  
2665 O OD1 . ASP B 106 ? 0.68139 0.57312 0.50632 -0.01764 -0.01074 0.04907  103 ASP B OD1 
2666 O OD2 . ASP B 106 ? 0.64838 0.56762 0.49715 -0.01506 -0.01359 0.03901  103 ASP B OD2 
2667 N N   . VAL B 107 ? 0.67399 0.54071 0.49230 -0.00756 -0.02461 0.05333  104 VAL B N   
2668 C CA  . VAL B 107 ? 0.69621 0.54157 0.49803 -0.00943 -0.02121 0.06009  104 VAL B CA  
2669 C C   . VAL B 107 ? 0.71490 0.55082 0.49748 -0.01378 -0.01376 0.06486  104 VAL B C   
2670 O O   . VAL B 107 ? 0.77491 0.59003 0.53810 -0.01351 -0.01156 0.07111  104 VAL B O   
2671 C CB  . VAL B 107 ? 0.71616 0.55782 0.52745 -0.01703 -0.01643 0.05987  104 VAL B CB  
2672 C CG1 . VAL B 107 ? 0.75212 0.59282 0.57387 -0.01110 -0.02231 0.05717  104 VAL B CG1 
2673 C CG2 . VAL B 107 ? 0.68117 0.54028 0.50835 -0.02617 -0.01088 0.05600  104 VAL B CG2 
2674 N N   . ASN B 108 ? 0.69753 0.54653 0.48392 -0.01737 -0.00865 0.06236  105 ASN B N   
2675 C CA  . ASN B 108 ? 0.73883 0.57994 0.51002 -0.02268 0.00193  0.06680  105 ASN B CA  
2676 C C   . ASN B 108 ? 0.73588 0.57989 0.49507 -0.01752 0.00100  0.06509  105 ASN B C   
2677 O O   . ASN B 108 ? 0.73138 0.59270 0.50369 -0.01880 0.00362  0.06030  105 ASN B O   
2678 C CB  . ASN B 108 ? 0.74085 0.59442 0.53022 -0.03355 0.01208  0.06616  105 ASN B CB  
2679 C CG  . ASN B 108 ? 0.78076 0.62342 0.55729 -0.04055 0.02487  0.07228  105 ASN B CG  
2680 O OD1 . ASN B 108 ? 0.82277 0.65096 0.57533 -0.03673 0.02804  0.07591  105 ASN B OD1 
2681 N ND2 . ASN B 108 ? 0.76353 0.61237 0.55564 -0.05123 0.03229  0.07355  105 ASN B ND2 
2682 N N   . LYS B 109 ? 0.75166 0.57676 0.48390 -0.01155 -0.00291 0.06908  106 LYS B N   
2683 C CA  . LYS B 109 ? 0.81855 0.64126 0.53345 -0.00702 -0.00466 0.06758  106 LYS B CA  
2684 C C   . LYS B 109 ? 0.82818 0.64559 0.53054 -0.01252 0.01084  0.07018  106 LYS B C   
2685 O O   . LYS B 109 ? 0.81974 0.63658 0.50965 -0.00986 0.01228  0.06788  106 LYS B O   
2686 C CB  . LYS B 109 ? 0.89549 0.69842 0.58406 0.00151  -0.01600 0.07117  106 LYS B CB  
2687 C CG  . LYS B 109 ? 0.93278 0.73414 0.60495 0.00691  -0.02351 0.06796  106 LYS B CG  
2688 C CD  . LYS B 109 ? 0.96669 0.75233 0.61834 0.01570  -0.03886 0.07112  106 LYS B CD  
2689 N N   . SER B 110 ? 0.82983 0.64268 0.53531 -0.02035 0.02301  0.07492  107 SER B N   
2690 C CA  . SER B 110 ? 0.82292 0.63403 0.52248 -0.02605 0.03973  0.07766  107 SER B CA  
2691 C C   . SER B 110 ? 0.79007 0.62538 0.51152 -0.02720 0.04402  0.07185  107 SER B C   
2692 O O   . SER B 110 ? 0.83207 0.66459 0.54147 -0.02618 0.05357  0.07202  107 SER B O   
2693 C CB  . SER B 110 ? 0.88022 0.68726 0.58767 -0.03587 0.05109  0.08309  107 SER B CB  
2694 O OG  . SER B 110 ? 0.97013 0.75688 0.66279 -0.03467 0.04527  0.08741  107 SER B OG  
2695 N N   . TYR B 111 ? 0.72044 0.57753 0.47217 -0.02877 0.03768  0.06684  108 TYR B N   
2696 C CA  . TYR B 111 ? 0.69324 0.57221 0.46475 -0.02835 0.03997  0.06117  108 TYR B CA  
2697 C C   . TYR B 111 ? 0.73331 0.60847 0.48836 -0.02022 0.03349  0.05672  108 TYR B C   
2698 O O   . TYR B 111 ? 0.77117 0.65154 0.52460 -0.01914 0.04132  0.05455  108 TYR B O   
2699 C CB  . TYR B 111 ? 0.65004 0.54859 0.45205 -0.03049 0.03240  0.05668  108 TYR B CB  
2700 C CG  . TYR B 111 ? 0.64987 0.55265 0.46888 -0.03956 0.03677  0.05996  108 TYR B CG  
2701 C CD1 . TYR B 111 ? 0.67991 0.58059 0.49929 -0.04700 0.05035  0.06548  108 TYR B CD1 
2702 C CD2 . TYR B 111 ? 0.60477 0.51266 0.43916 -0.04117 0.02761  0.05742  108 TYR B CD2 
2703 C CE1 . TYR B 111 ? 0.63950 0.54428 0.47543 -0.05673 0.05316  0.06817  108 TYR B CE1 
2704 C CE2 . TYR B 111 ? 0.60490 0.51426 0.45218 -0.05028 0.03040  0.05989  108 TYR B CE2 
2705 C CZ  . TYR B 111 ? 0.63062 0.53901 0.47927 -0.05851 0.04241  0.06515  108 TYR B CZ  
2706 O OH  . TYR B 111 ? 0.64237 0.55234 0.50469 -0.06891 0.04397  0.06730  108 TYR B OH  
2707 N N   . TYR B 112 ? 0.72728 0.59305 0.47044 -0.01451 0.01909  0.05540  109 TYR B N   
2708 C CA  . TYR B 112 ? 0.78378 0.64690 0.51353 -0.00796 0.01011  0.05064  109 TYR B CA  
2709 C C   . TYR B 112 ? 0.87009 0.71366 0.56638 -0.00618 0.01739  0.05319  109 TYR B C   
2710 O O   . TYR B 112 ? 0.85216 0.69583 0.53934 -0.00336 0.01701  0.04863  109 TYR B O   
2711 C CB  . TYR B 112 ? 0.78278 0.64085 0.50953 -0.00262 -0.00711 0.04994  109 TYR B CB  
2712 C CG  . TYR B 112 ? 0.81222 0.66655 0.52489 0.00322  -0.01897 0.04558  109 TYR B CG  
2713 C CD1 . TYR B 112 ? 0.76324 0.63226 0.48872 0.00353  -0.02061 0.03827  109 TYR B CD1 
2714 C CD2 . TYR B 112 ? 0.85404 0.68939 0.54032 0.00819  -0.02947 0.04882  109 TYR B CD2 
2715 C CE1 . TYR B 112 ? 0.75823 0.62306 0.47091 0.00743  -0.03205 0.03391  109 TYR B CE1 
2716 C CE2 . TYR B 112 ? 0.85089 0.68318 0.52493 0.01252  -0.04232 0.04469  109 TYR B CE2 
2717 C CZ  . TYR B 112 ? 0.83990 0.68702 0.52751 0.01152  -0.04344 0.03703  109 TYR B CZ  
2718 O OH  . TYR B 112 ? 0.88949 0.73284 0.56497 0.01443  -0.05666 0.03255  109 TYR B OH  
2719 N N   . GLU B 113 ? 0.91147 0.73577 0.58702 -0.00793 0.02490  0.06037  110 GLU B N   
2720 C CA  . GLU B 113 ? 0.96936 0.77110 0.60927 -0.00615 0.03352  0.06338  110 GLU B CA  
2721 C C   . GLU B 113 ? 0.90961 0.71854 0.55544 -0.00953 0.05258  0.06301  110 GLU B C   
2722 O O   . GLU B 113 ? 0.92606 0.71690 0.54252 -0.00725 0.06115  0.06412  110 GLU B O   
2723 C CB  . GLU B 113 ? 1.08187 0.85904 0.69716 -0.00690 0.03699  0.07164  110 GLU B CB  
2724 C CG  . GLU B 113 ? 1.16878 0.93590 0.77431 -0.00148 0.01819  0.07287  110 GLU B CG  
2725 C CD  . GLU B 113 ? 1.27063 1.01244 0.85223 -0.00174 0.02195  0.08142  110 GLU B CD  
2726 O OE1 . GLU B 113 ? 1.31222 1.04402 0.88497 -0.00720 0.03980  0.08627  110 GLU B OE1 
2727 O OE2 . GLU B 113 ? 1.30607 1.03784 0.87842 0.00372  0.00753  0.08357  110 GLU B OE2 
2728 N N   . ILE B 114 ? 0.83407 0.66799 0.51631 -0.01440 0.05929  0.06170  111 ILE B N   
2729 C CA  . ILE B 114 ? 0.81491 0.66022 0.50830 -0.01597 0.07554  0.06084  111 ILE B CA  
2730 C C   . ILE B 114 ? 0.80276 0.65120 0.49031 -0.01020 0.07076  0.05362  111 ILE B C   
2731 O O   . ILE B 114 ? 0.81035 0.65186 0.48389 -0.00813 0.08356  0.05333  111 ILE B O   
2732 C CB  . ILE B 114 ? 0.78233 0.65473 0.51756 -0.02233 0.08071  0.06134  111 ILE B CB  
2733 C CG1 . ILE B 114 ? 0.77401 0.64062 0.51236 -0.02972 0.08898  0.06880  111 ILE B CG1 
2734 C CG2 . ILE B 114 ? 0.76847 0.65767 0.52109 -0.02194 0.09397  0.05955  111 ILE B CG2 
2735 C CD1 . ILE B 114 ? 0.74883 0.64021 0.52676 -0.03721 0.09029  0.06912  111 ILE B CD1 
2736 N N   . GLY B 115 ? 0.75325 0.61048 0.45043 -0.00760 0.05326  0.04777  112 GLY B N   
2737 C CA  . GLY B 115 ? 0.78587 0.64709 0.48061 -0.00344 0.04828  0.04046  112 GLY B CA  
2738 C C   . GLY B 115 ? 0.84249 0.68267 0.50374 0.00094  0.03545  0.03778  112 GLY B C   
2739 O O   . GLY B 115 ? 0.84092 0.67866 0.49272 0.00358  0.03292  0.03189  112 GLY B O   
2740 N N   . LEU B 116 ? 0.83235 0.65650 0.47499 0.00169  0.02666  0.04211  113 LEU B N   
2741 C CA  . LEU B 116 ? 0.89328 0.69842 0.50532 0.00593  0.01149  0.04003  113 LEU B CA  
2742 C C   . LEU B 116 ? 0.92976 0.71263 0.50476 0.00788  0.01904  0.03859  113 LEU B C   
2743 O O   . LEU B 116 ? 0.94942 0.72521 0.50904 0.01022  0.00629  0.03293  113 LEU B O   
2744 C CB  . LEU B 116 ? 0.93364 0.72323 0.52983 0.00736  0.00255  0.04643  113 LEU B CB  
2745 C CG  . LEU B 116 ? 0.96879 0.74170 0.53763 0.01222  -0.01699 0.04487  113 LEU B CG  
2746 C CD1 . LEU B 116 ? 0.94441 0.73806 0.53929 0.01335  -0.03381 0.03760  113 LEU B CD1 
2747 C CD2 . LEU B 116 ? 0.97359 0.72937 0.52498 0.01491  -0.02456 0.05231  113 LEU B CD2 
2748 N N   . PRO B 117 ? 0.93808 0.70800 0.49671 0.00686  0.03924  0.04327  114 PRO B N   
2749 C CA  . PRO B 117 ? 0.93501 0.68195 0.45705 0.00936  0.04786  0.04122  114 PRO B CA  
2750 C C   . PRO B 117 ? 0.89444 0.65319 0.42754 0.01035  0.04746  0.03287  114 PRO B C   
2751 O O   . PRO B 117 ? 0.93615 0.67504 0.43738 0.01259  0.04267  0.02839  114 PRO B O   
2752 C CB  . PRO B 117 ? 0.96233 0.70152 0.47865 0.00766  0.07333  0.04812  114 PRO B CB  
2753 C CG  . PRO B 117 ? 0.96916 0.71269 0.49879 0.00447  0.07212  0.05494  114 PRO B CG  
2754 C CD  . PRO B 117 ? 0.92462 0.69526 0.49180 0.00332  0.05473  0.05115  114 PRO B CD  
2755 N N   . PHE B 118 ? 0.82904 0.61769 0.40453 0.00863  0.05187  0.03060  115 PHE B N   
2756 C CA  . PHE B 118 ? 0.84770 0.64689 0.43408 0.00996  0.05163  0.02288  115 PHE B CA  
2757 C C   . PHE B 118 ? 0.83566 0.63821 0.42409 0.01010  0.02851  0.01613  115 PHE B C   
2758 O O   . PHE B 118 ? 0.85291 0.64770 0.42735 0.01114  0.02452  0.00948  115 PHE B O   
2759 C CB  . PHE B 118 ? 0.85885 0.68791 0.48882 0.00859  0.06226  0.02309  115 PHE B CB  
2760 C CG  . PHE B 118 ? 0.85791 0.68841 0.49293 0.00784  0.08458  0.02989  115 PHE B CG  
2761 C CD1 . PHE B 118 ? 0.87016 0.69316 0.49385 0.01096  0.10291  0.02960  115 PHE B CD1 
2762 C CD2 . PHE B 118 ? 0.84086 0.67974 0.49254 0.00386  0.08787  0.03672  115 PHE B CD2 
2763 C CE1 . PHE B 118 ? 0.89054 0.71691 0.52262 0.01040  0.12439  0.03636  115 PHE B CE1 
2764 C CE2 . PHE B 118 ? 0.84456 0.68632 0.50396 0.00207  0.10843  0.04311  115 PHE B CE2 
2765 C CZ  . PHE B 118 ? 0.87546 0.71222 0.52663 0.00547  0.12685  0.04312  115 PHE B CZ  
2766 N N   . ILE B 119 ? 0.84077 0.65467 0.44747 0.00892  0.01381  0.01780  116 ILE B N   
2767 C CA  . ILE B 119 ? 0.87335 0.69111 0.48408 0.00925  -0.00799 0.01246  116 ILE B CA  
2768 C C   . ILE B 119 ? 0.92289 0.71288 0.49079 0.01073  -0.01879 0.01108  116 ILE B C   
2769 O O   . ILE B 119 ? 0.91855 0.70633 0.48048 0.01025  -0.03123 0.00422  116 ILE B O   
2770 C CB  . ILE B 119 ? 0.87085 0.70324 0.50708 0.00886  -0.01927 0.01594  116 ILE B CB  
2771 C CG1 . ILE B 119 ? 0.85494 0.71298 0.53134 0.00679  -0.01048 0.01616  116 ILE B CG1 
2772 C CG2 . ILE B 119 ? 0.85544 0.69137 0.49609 0.00989  -0.04133 0.01157  116 ILE B CG2 
2773 C CD1 . ILE B 119 ? 0.83660 0.70513 0.53463 0.00627  -0.01831 0.02001  116 ILE B CD1 
2774 N N   . GLN B 120 ? 0.94509 0.71203 0.48120 0.01208  -0.01434 0.01755  117 GLN B N   
2775 C CA  . GLN B 120 ? 1.00218 0.73909 0.49268 0.01375  -0.02521 0.01687  117 GLN B CA  
2776 C C   . GLN B 120 ? 1.04018 0.75929 0.50253 0.01361  -0.01590 0.01135  117 GLN B C   
2777 O O   . GLN B 120 ? 1.04335 0.74891 0.48329 0.01312  -0.03050 0.00555  117 GLN B O   
2778 C CB  . GLN B 120 ? 1.02498 0.73903 0.48620 0.01564  -0.02052 0.02574  117 GLN B CB  
2779 C CG  . GLN B 120 ? 1.01715 0.74202 0.49787 0.01659  -0.03242 0.03118  117 GLN B CG  
2780 C CD  . GLN B 120 ? 1.07379 0.77681 0.52892 0.01792  -0.02302 0.04049  117 GLN B CD  
2781 O OE1 . GLN B 120 ? 1.10153 0.79494 0.54565 0.01652  -0.00119 0.04388  117 GLN B OE1 
2782 N NE2 . GLN B 120 ? 1.10345 0.79826 0.54963 0.02087  -0.03889 0.04501  117 GLN B NE2 
2783 N N   . LYS B 121 ? 1.05699 0.77553 0.52046 0.01399  0.00844  0.01313  118 LYS B N   
2784 C CA  . LYS B 121 ? 1.05737 0.75776 0.49420 0.01494  0.02014  0.00828  118 LYS B CA  
2785 C C   . LYS B 121 ? 1.04078 0.75578 0.49641 0.01336  0.01083  -0.00105 118 LYS B C   
2786 O O   . LYS B 121 ? 1.07473 0.76902 0.50019 0.01315  0.00827  -0.00711 118 LYS B O   
2787 C CB  . LYS B 121 ? 1.02967 0.73194 0.47263 0.01650  0.04896  0.01283  118 LYS B CB  
2788 C CG  . LYS B 121 ? 1.07544 0.75488 0.48960 0.01763  0.06184  0.02144  118 LYS B CG  
2789 C CD  . LYS B 121 ? 1.08295 0.76826 0.50976 0.01865  0.09096  0.02627  118 LYS B CD  
2790 C CE  . LYS B 121 ? 1.13638 0.79805 0.53497 0.01901  0.10492  0.03508  118 LYS B CE  
2791 N NZ  . LYS B 121 ? 1.17168 0.83577 0.57887 0.02012  0.13501  0.03976  118 LYS B NZ  
2792 N N   . ALA B 122 ? 0.98711 0.73536 0.49034 0.01193  0.00598  -0.00242 119 ALA B N   
2793 C CA  . ALA B 122 ? 0.93131 0.69309 0.45330 0.01002  -0.00440 -0.01095 119 ALA B CA  
2794 C C   . ALA B 122 ? 0.95170 0.70547 0.46038 0.00763  -0.02991 -0.01532 119 ALA B C   
2795 O O   . ALA B 122 ? 0.96400 0.72247 0.47978 0.00503  -0.03885 -0.02306 119 ALA B O   
2796 C CB  . ALA B 122 ? 0.85812 0.65485 0.43171 0.00932  -0.00317 -0.01068 119 ALA B CB  
2797 N N   . GLY B 123 ? 0.96065 0.70266 0.45116 0.00840  -0.04193 -0.01035 120 GLY B N   
2798 C CA  . GLY B 123 ? 0.97399 0.70846 0.45155 0.00668  -0.06743 -0.01361 120 GLY B CA  
2799 C C   . GLY B 123 ? 0.97934 0.74397 0.50113 0.00508  -0.08394 -0.01571 120 GLY B C   
2800 O O   . GLY B 123 ? 1.02391 0.78933 0.54589 0.00226  -0.10295 -0.02126 120 GLY B O   
2801 N N   . VAL B 124 ? 0.92614 0.71486 0.48526 0.00650  -0.07700 -0.01136 121 VAL B N   
2802 C CA  . VAL B 124 ? 0.88107 0.69758 0.48294 0.00564  -0.08896 -0.01302 121 VAL B CA  
2803 C C   . VAL B 124 ? 0.85478 0.67909 0.47054 0.00874  -0.09543 -0.00530 121 VAL B C   
2804 O O   . VAL B 124 ? 0.79382 0.64028 0.44546 0.00898  -0.10275 -0.00560 121 VAL B O   
2805 C CB  . VAL B 124 ? 0.81442 0.65300 0.45106 0.00432  -0.07526 -0.01654 121 VAL B CB  
2806 C CG1 . VAL B 124 ? 0.84371 0.67437 0.46806 0.00180  -0.07019 -0.02452 121 VAL B CG1 
2807 C CG2 . VAL B 124 ? 0.75377 0.59641 0.39735 0.00623  -0.05565 -0.01036 121 VAL B CG2 
2808 N N   . GLU B 125 ? 0.87629 0.68116 0.46347 0.01135  -0.09186 0.00176  122 GLU B N   
2809 C CA  . GLU B 125 ? 0.90558 0.71497 0.50356 0.01455  -0.09685 0.00939  122 GLU B CA  
2810 C C   . GLU B 125 ? 0.89073 0.70701 0.49937 0.01662  -0.12098 0.00908  122 GLU B C   
2811 O O   . GLU B 125 ? 0.85648 0.68481 0.48808 0.01961  -0.12549 0.01380  122 GLU B O   
2812 C CB  . GLU B 125 ? 0.98817 0.77118 0.54848 0.01677  -0.08878 0.01693  122 GLU B CB  
2813 C CG  . GLU B 125 ? 1.02789 0.81414 0.59962 0.01949  -0.08788 0.02528  122 GLU B CG  
2814 C CD  . GLU B 125 ? 1.14439 0.90087 0.67477 0.02199  -0.08407 0.03283  122 GLU B CD  
2815 O OE1 . GLU B 125 ? 1.20473 0.93700 0.69557 0.02266  -0.08803 0.03167  122 GLU B OE1 
2816 O OE2 . GLU B 125 ? 1.17063 0.92575 0.70603 0.02304  -0.07682 0.03990  122 GLU B OE2 
2817 N N   . HIS B 126 ? 0.89452 0.70356 0.48807 0.01503  -0.13654 0.00366  123 HIS B N   
2818 C CA  . HIS B 126 ? 0.90466 0.72273 0.51168 0.01673  -0.16070 0.00351  123 HIS B CA  
2819 C C   . HIS B 126 ? 0.81667 0.66676 0.47535 0.01600  -0.16320 0.00059  123 HIS B C   
2820 O O   . HIS B 126 ? 0.79913 0.66133 0.47823 0.01886  -0.17970 0.00253  123 HIS B O   
2821 C CB  . HIS B 126 ? 0.93453 0.73803 0.51459 0.01349  -0.17713 -0.00244 123 HIS B CB  
2822 C CG  . HIS B 126 ? 0.92762 0.74159 0.52229 0.00721  -0.17421 -0.01219 123 HIS B CG  
2823 N ND1 . HIS B 126 ? 0.93102 0.73170 0.50492 0.00417  -0.15674 -0.01649 123 HIS B ND1 
2824 C CD2 . HIS B 126 ? 0.90297 0.73848 0.53094 0.00361  -0.18568 -0.01821 123 HIS B CD2 
2825 C CE1 . HIS B 126 ? 0.91962 0.73186 0.51155 -0.00084 -0.15801 -0.02481 123 HIS B CE1 
2826 N NE2 . HIS B 126 ? 0.89979 0.73310 0.52456 -0.00179 -0.17526 -0.02612 123 HIS B NE2 
2827 N N   . LYS B 127 ? 0.82454 0.68781 0.50440 0.01281  -0.14688 -0.00362 124 LYS B N   
2828 C CA  . LYS B 127 ? 0.82902 0.71932 0.55434 0.01208  -0.14701 -0.00651 124 LYS B CA  
2829 C C   . LYS B 127 ? 0.79988 0.70075 0.54796 0.01609  -0.13919 0.00000  124 LYS B C   
2830 O O   . LYS B 127 ? 0.80366 0.72435 0.58741 0.01656  -0.13985 -0.00142 124 LYS B O   
2831 C CB  . LYS B 127 ? 0.79178 0.68929 0.52745 0.00733  -0.13349 -0.01385 124 LYS B CB  
2832 C CG  . LYS B 127 ? 0.80564 0.69070 0.51818 0.00276  -0.13836 -0.02114 124 LYS B CG  
2833 C CD  . LYS B 127 ? 0.77789 0.67152 0.50517 -0.00090 -0.12488 -0.02797 124 LYS B CD  
2834 C CE  . LYS B 127 ? 0.79637 0.67341 0.49632 -0.00540 -0.12703 -0.03522 124 LYS B CE  
2835 N NZ  . LYS B 127 ? 0.77855 0.66311 0.49329 -0.00830 -0.11442 -0.04173 124 LYS B NZ  
2836 N N   . ILE B 128 ? 0.81779 0.70425 0.54513 0.01865  -0.13128 0.00698  125 ILE B N   
2837 C CA  . ILE B 128 ? 0.80493 0.69799 0.54958 0.02046  -0.11976 0.01226  125 ILE B CA  
2838 C C   . ILE B 128 ? 0.82021 0.70647 0.56058 0.02625  -0.12965 0.02006  125 ILE B C   
2839 O O   . ILE B 128 ? 0.86186 0.72839 0.57009 0.02860  -0.13588 0.02431  125 ILE B O   
2840 C CB  . ILE B 128 ? 0.80366 0.68685 0.53192 0.01775  -0.10022 0.01426  125 ILE B CB  
2841 C CG1 . ILE B 128 ? 0.75299 0.64399 0.48808 0.01347  -0.09012 0.00704  125 ILE B CG1 
2842 C CG2 . ILE B 128 ? 0.80156 0.68990 0.54597 0.01836  -0.09027 0.01980  125 ILE B CG2 
2843 C CD1 . ILE B 128 ? 0.73951 0.62328 0.46168 0.01138  -0.07104 0.00906  125 ILE B CD1 
2844 N N   . ASN B 129 ? 0.77283 0.67329 0.54360 0.02909  -0.13045 0.02213  126 ASN B N   
2845 C CA  . ASN B 129 ? 0.77162 0.66543 0.54132 0.03526  -0.13541 0.03020  126 ASN B CA  
2846 C C   . ASN B 129 ? 0.76065 0.65383 0.53820 0.03364  -0.11839 0.03342  126 ASN B C   
2847 O O   . ASN B 129 ? 0.73972 0.64788 0.54637 0.03287  -0.11320 0.03104  126 ASN B O   
2848 C CB  . ASN B 129 ? 0.74592 0.65521 0.54438 0.04050  -0.15018 0.03027  126 ASN B CB  
2849 C CG  . ASN B 129 ? 0.77979 0.68272 0.58035 0.04809  -0.15324 0.03883  126 ASN B CG  
2850 O OD1 . ASN B 129 ? 0.85004 0.73288 0.62264 0.04991  -0.14990 0.04511  126 ASN B OD1 
2851 N ND2 . ASN B 129 ? 0.73714 0.65587 0.57049 0.05280  -0.15838 0.03931  126 ASN B ND2 
2852 N N   . PHE B 130 ? 0.80499 0.67964 0.55561 0.03258  -0.10959 0.03872  127 PHE B N   
2853 C CA  . PHE B 130 ? 0.80470 0.67753 0.56079 0.02931  -0.09387 0.04175  127 PHE B CA  
2854 C C   . PHE B 130 ? 0.80117 0.66546 0.55861 0.03441  -0.09659 0.04893  127 PHE B C   
2855 O O   . PHE B 130 ? 0.82379 0.67301 0.56079 0.03990  -0.10554 0.05445  127 PHE B O   
2856 C CB  . PHE B 130 ? 0.84361 0.70185 0.57303 0.02449  -0.08076 0.04384  127 PHE B CB  
2857 C CG  . PHE B 130 ? 0.85059 0.71117 0.59023 0.01907  -0.06475 0.04580  127 PHE B CG  
2858 C CD1 . PHE B 130 ? 0.89067 0.73763 0.62199 0.01922  -0.06023 0.05292  127 PHE B CD1 
2859 C CD2 . PHE B 130 ? 0.82134 0.69706 0.57856 0.01365  -0.05487 0.04062  127 PHE B CD2 
2860 C CE1 . PHE B 130 ? 0.90782 0.75688 0.64905 0.01286  -0.04680 0.05443  127 PHE B CE1 
2861 C CE2 . PHE B 130 ? 0.83420 0.71323 0.60208 0.00820  -0.04222 0.04252  127 PHE B CE2 
2862 C CZ  . PHE B 130 ? 0.86530 0.73129 0.62557 0.00720  -0.03848 0.04923  127 PHE B CZ  
2863 N N   . ILE B 131 ? 0.77026 0.64215 0.54971 0.03283  -0.08880 0.04892  128 ILE B N   
2864 C CA  . ILE B 131 ? 0.78328 0.64617 0.56555 0.03745  -0.08931 0.05507  128 ILE B CA  
2865 C C   . ILE B 131 ? 0.76643 0.62179 0.54593 0.03062  -0.07395 0.05719  128 ILE B C   
2866 O O   . ILE B 131 ? 0.75863 0.62648 0.55732 0.02525  -0.06644 0.05262  128 ILE B O   
2867 C CB  . ILE B 131 ? 0.77833 0.65608 0.59111 0.04275  -0.09584 0.05283  128 ILE B CB  
2868 C CG1 . ILE B 131 ? 0.79842 0.68476 0.61662 0.04909  -0.11243 0.05154  128 ILE B CG1 
2869 C CG2 . ILE B 131 ? 0.79944 0.66551 0.61407 0.04732  -0.09294 0.05901  128 ILE B CG2 
2870 C CD1 . ILE B 131 ? 0.78680 0.69123 0.63934 0.05361  -0.11756 0.04874  128 ILE B CD1 
2871 N N   . GLU B 132 ? 0.76570 0.60003 0.52098 0.03043  -0.06967 0.06418  129 GLU B N   
2872 C CA  . GLU B 132 ? 0.78837 0.61413 0.54052 0.02282  -0.05570 0.06678  129 GLU B CA  
2873 C C   . GLU B 132 ? 0.81003 0.63029 0.57326 0.02561  -0.05573 0.06935  129 GLU B C   
2874 O O   . GLU B 132 ? 0.86030 0.66189 0.60821 0.03091  -0.05811 0.07591  129 GLU B O   
2875 C CB  . GLU B 132 ? 0.81679 0.62087 0.53745 0.02043  -0.04930 0.07307  129 GLU B CB  
2876 C CG  . GLU B 132 ? 0.88427 0.68114 0.60405 0.01085  -0.03451 0.07566  129 GLU B CG  
2877 C CD  . GLU B 132 ? 0.95596 0.72997 0.64506 0.00822  -0.02641 0.08240  129 GLU B CD  
2878 O OE1 . GLU B 132 ? 0.99276 0.74987 0.65733 0.01570  -0.03346 0.08681  129 GLU B OE1 
2879 O OE2 . GLU B 132 ? 0.96081 0.73358 0.65056 -0.00140 -0.01298 0.08350  129 GLU B OE2 
2880 N N   . SER B 133 ? 0.79741 0.63159 0.58508 0.02246  -0.05257 0.06431  130 SER B N   
2881 C CA  . SER B 133 ? 0.80071 0.62849 0.59831 0.02525  -0.05166 0.06580  130 SER B CA  
2882 C C   . SER B 133 ? 0.79927 0.63899 0.61665 0.01812  -0.04509 0.05992  130 SER B C   
2883 O O   . SER B 133 ? 0.79045 0.64597 0.61688 0.01280  -0.04296 0.05476  130 SER B O   
2884 C CB  . SER B 133 ? 0.79481 0.62673 0.60307 0.03714  -0.06266 0.06645  130 SER B CB  
2885 O OG  . SER B 133 ? 0.80525 0.63455 0.62787 0.03994  -0.05971 0.06621  130 SER B OG  
2886 N N   . GLU B 134 ? 0.80802 0.63785 0.62989 0.01847  -0.04186 0.06094  131 GLU B N   
2887 C CA  . GLU B 134 ? 0.78881 0.62808 0.62874 0.01430  -0.03820 0.05514  131 GLU B CA  
2888 C C   . GLU B 134 ? 0.74534 0.60152 0.60522 0.02186  -0.04430 0.05043  131 GLU B C   
2889 O O   . GLU B 134 ? 0.70692 0.56336 0.56940 0.03141  -0.05123 0.05277  131 GLU B O   
2890 C CB  . GLU B 134 ? 0.85219 0.67213 0.68739 0.01283  -0.03304 0.05739  131 GLU B CB  
2891 C CG  . GLU B 134 ? 0.94745 0.74895 0.76327 0.00427  -0.02693 0.06216  131 GLU B CG  
2892 C CD  . GLU B 134 ? 1.00018 0.78401 0.81220 -0.00094 -0.02151 0.06224  131 GLU B CD  
2893 O OE1 . GLU B 134 ? 1.01183 0.80096 0.83654 -0.00107 -0.02123 0.05721  131 GLU B OE1 
2894 O OE2 . GLU B 134 ? 1.04796 0.81046 0.84230 -0.00519 -0.01729 0.06724  131 GLU B OE2 
2895 N N   . ALA B 135 ? 0.72480 0.59544 0.59955 0.01739  -0.04185 0.04397  132 ALA B N   
2896 C CA  . ALA B 135 ? 0.70294 0.59079 0.59626 0.02270  -0.04654 0.03896  132 ALA B CA  
2897 C C   . ALA B 135 ? 0.69473 0.57861 0.60012 0.03102  -0.04731 0.03950  132 ALA B C   
2898 O O   . ALA B 135 ? 0.68394 0.57745 0.60140 0.03869  -0.05382 0.03935  132 ALA B O   
2899 C CB  . ALA B 135 ? 0.69915 0.60038 0.60286 0.01610  -0.04258 0.03239  132 ALA B CB  
2900 N N   . LEU B 136 ? 0.69983 0.56917 0.60239 0.02953  -0.04058 0.04017  133 LEU B N   
2901 C CA  . LEU B 136 ? 0.68772 0.55164 0.60151 0.03766  -0.03851 0.04034  133 LEU B CA  
2902 C C   . LEU B 136 ? 0.71158 0.57213 0.62741 0.04881  -0.04405 0.04622  133 LEU B C   
2903 O O   . LEU B 136 ? 0.68892 0.56040 0.62470 0.05679  -0.04645 0.04519  133 LEU B O   
2904 C CB  . LEU B 136 ? 0.70883 0.55181 0.61216 0.03369  -0.03012 0.04057  133 LEU B CB  
2905 C CG  . LEU B 136 ? 0.75787 0.60328 0.66780 0.02844  -0.02486 0.03412  133 LEU B CG  
2906 C CD1 . LEU B 136 ? 0.80052 0.62034 0.69684 0.02620  -0.01790 0.03498  133 LEU B CD1 
2907 C CD2 . LEU B 136 ? 0.72944 0.59000 0.66100 0.03530  -0.02493 0.03009  133 LEU B CD2 
2908 N N   . PRO B 137 ? 0.74227 0.58820 0.63948 0.05022  -0.04619 0.05271  134 PRO B N   
2909 C CA  . PRO B 137 ? 0.72965 0.57244 0.62941 0.06235  -0.05261 0.05878  134 PRO B CA  
2910 C C   . PRO B 137 ? 0.72291 0.58797 0.63758 0.06709  -0.06395 0.05753  134 PRO B C   
2911 O O   . PRO B 137 ? 0.74691 0.61874 0.67806 0.07749  -0.06943 0.06000  134 PRO B O   
2912 C CB  . PRO B 137 ? 0.75360 0.57511 0.62580 0.06084  -0.05244 0.06548  134 PRO B CB  
2913 C CG  . PRO B 137 ? 0.75252 0.56201 0.61183 0.04883  -0.04301 0.06321  134 PRO B CG  
2914 C CD  . PRO B 137 ? 0.73687 0.56688 0.61062 0.04142  -0.04223 0.05539  134 PRO B CD  
2915 N N   . VAL B 138 ? 0.74313 0.61951 0.65285 0.05964  -0.06763 0.05380  135 VAL B N   
2916 C CA  . VAL B 138 ? 0.72879 0.62393 0.64951 0.06265  -0.07892 0.05180  135 VAL B CA  
2917 C C   . VAL B 138 ? 0.69121 0.60517 0.64178 0.06458  -0.07860 0.04608  135 VAL B C   
2918 O O   . VAL B 138 ? 0.70119 0.62804 0.67002 0.07162  -0.08739 0.04673  135 VAL B O   
2919 C CB  . VAL B 138 ? 0.72642 0.62523 0.63121 0.05403  -0.08070 0.04894  135 VAL B CB  
2920 C CG1 . VAL B 138 ? 0.73884 0.65029 0.64687 0.05734  -0.09391 0.04793  135 VAL B CG1 
2921 C CG2 . VAL B 138 ? 0.73235 0.61097 0.60852 0.05037  -0.07657 0.05432  135 VAL B CG2 
2922 N N   . LEU B 139 ? 0.66382 0.57934 0.61995 0.05817  -0.06863 0.04059  136 LEU B N   
2923 C CA  . LEU B 139 ? 0.65329 0.58347 0.63528 0.05960  -0.06611 0.03518  136 LEU B CA  
2924 C C   . LEU B 139 ? 0.64690 0.57481 0.64637 0.06996  -0.06425 0.03885  136 LEU B C   
2925 O O   . LEU B 139 ? 0.59932 0.54347 0.62439 0.07457  -0.06734 0.03704  136 LEU B O   
2926 C CB  . LEU B 139 ? 0.65054 0.57786 0.63028 0.05160  -0.05545 0.02959  136 LEU B CB  
2927 C CG  . LEU B 139 ? 0.64987 0.58117 0.61628 0.04199  -0.05546 0.02599  136 LEU B CG  
2928 C CD1 . LEU B 139 ? 0.60207 0.53150 0.56942 0.03571  -0.04621 0.02101  136 LEU B CD1 
2929 C CD2 . LEU B 139 ? 0.64441 0.59296 0.61823 0.04150  -0.06384 0.02260  136 LEU B CD2 
2930 N N   . ASP B 140 ? 0.66614 0.57353 0.65273 0.07368  -0.05849 0.04415  137 ASP B N   
2931 C CA  . ASP B 140 ? 0.68611 0.58886 0.68764 0.08495  -0.05532 0.04847  137 ASP B CA  
2932 C C   . ASP B 140 ? 0.70246 0.61685 0.71658 0.09460  -0.06817 0.05381  137 ASP B C   
2933 O O   . ASP B 140 ? 0.65393 0.58015 0.69537 0.10328  -0.06901 0.05509  137 ASP B O   
2934 C CB  . ASP B 140 ? 0.70261 0.57712 0.68302 0.08637  -0.04619 0.05291  137 ASP B CB  
2935 C CG  . ASP B 140 ? 0.72601 0.58878 0.70228 0.08055  -0.03321 0.04800  137 ASP B CG  
2936 O OD1 . ASP B 140 ? 0.71208 0.58867 0.70315 0.07694  -0.03061 0.04169  137 ASP B OD1 
2937 O OD2 . ASP B 140 ? 0.78286 0.62080 0.73934 0.07940  -0.02590 0.05045  137 ASP B OD2 
2938 N N   . GLN B 141 ? 0.74581 0.65670 0.74046 0.09335  -0.07830 0.05726  138 GLN B N   
2939 C CA  . GLN B 141 ? 0.78898 0.71054 0.79266 0.10189  -0.09313 0.06208  138 GLN B CA  
2940 C C   . GLN B 141 ? 0.76926 0.71800 0.79761 0.09954  -0.10239 0.05649  138 GLN B C   
2941 O O   . GLN B 141 ? 0.76613 0.72973 0.81737 0.10763  -0.11272 0.05928  138 GLN B O   
2942 C CB  . GLN B 141 ? 0.86513 0.77274 0.83692 0.10038  -0.10103 0.06674  138 GLN B CB  
2943 C CG  . GLN B 141 ? 0.96220 0.87632 0.93731 0.10977  -0.11789 0.07254  138 GLN B CG  
2944 C CD  . GLN B 141 ? 1.05268 0.96974 1.00826 0.10336  -0.12953 0.07066  138 GLN B CD  
2945 O OE1 . GLN B 141 ? 1.04078 0.97504 1.00680 0.09657  -0.13344 0.06369  138 GLN B OE1 
2946 N NE2 . GLN B 141 ? 1.11168 1.00939 1.03649 0.10557  -0.13418 0.07692  138 GLN B NE2 
2947 N N   . MET B 142 ? 0.77496 0.73041 0.79976 0.08850  -0.09907 0.04878  139 MET B N   
2948 C CA  . MET B 142 ? 0.76474 0.74341 0.81181 0.08521  -0.10604 0.04274  139 MET B CA  
2949 C C   . MET B 142 ? 0.73785 0.72994 0.82058 0.09003  -0.09995 0.04105  139 MET B C   
2950 O O   . MET B 142 ? 0.71926 0.73191 0.82801 0.09153  -0.10883 0.03933  139 MET B O   
2951 C CB  . MET B 142 ? 0.75146 0.73128 0.78537 0.07324  -0.10142 0.03518  139 MET B CB  
2952 C CG  . MET B 142 ? 0.77429 0.74583 0.77783 0.06819  -0.10823 0.03598  139 MET B CG  
2953 S SD  . MET B 142 ? 0.75776 0.73125 0.74935 0.05580  -0.10044 0.02770  139 MET B SD  
2954 C CE  . MET B 142 ? 0.78534 0.74566 0.74088 0.05256  -0.10646 0.03095  139 MET B CE  
2955 N N   . LEU B 143 ? 0.72510 0.70486 0.80899 0.09210  -0.08464 0.04149  140 LEU B N   
2956 C CA  . LEU B 143 ? 0.71981 0.70911 0.83519 0.09691  -0.07592 0.04000  140 LEU B CA  
2957 C C   . LEU B 143 ? 0.78108 0.78147 0.92304 0.10929  -0.08309 0.04667  140 LEU B C   
2958 O O   . LEU B 143 ? 0.78864 0.80721 0.96498 0.11241  -0.08145 0.04516  140 LEU B O   
2959 C CB  . LEU B 143 ? 0.69320 0.66160 0.79778 0.09694  -0.05802 0.03948  140 LEU B CB  
2960 C CG  . LEU B 143 ? 0.69101 0.65519 0.78461 0.08608  -0.04881 0.03168  140 LEU B CG  
2961 C CD1 . LEU B 143 ? 0.70680 0.64775 0.78760 0.08685  -0.03329 0.03188  140 LEU B CD1 
2962 C CD2 . LEU B 143 ? 0.67421 0.65912 0.79448 0.08317  -0.04827 0.02552  140 LEU B CD2 
2963 N N   . GLU B 144 ? 0.84222 0.83218 0.96994 0.11663  -0.09079 0.05438  141 GLU B N   
2964 C CA  . GLU B 144 ? 0.91643 0.91689 1.06949 0.12982  -0.09859 0.06170  141 GLU B CA  
2965 C C   . GLU B 144 ? 0.95439 0.97924 1.12427 0.12931  -0.11923 0.06151  141 GLU B C   
2966 O O   . GLU B 144 ? 0.97449 1.01954 1.18055 0.13711  -0.12546 0.06442  141 GLU B O   
2967 C CB  . GLU B 144 ? 0.96320 0.94050 1.09283 0.13888  -0.09868 0.07053  141 GLU B CB  
2968 C CG  . GLU B 144 ? 1.02623 0.98085 1.14896 0.14342  -0.07915 0.07247  141 GLU B CG  
2969 C CD  . GLU B 144 ? 1.12068 1.04497 1.20046 0.13864  -0.07394 0.07406  141 GLU B CD  
2970 O OE1 . GLU B 144 ? 1.15586 1.05804 1.22433 0.14018  -0.05877 0.07485  141 GLU B OE1 
2971 O OE2 . GLU B 144 ? 1.15335 1.07486 1.21012 0.13291  -0.08463 0.07445  141 GLU B OE2 
2972 N N   . GLU B 145 ? 0.98329 1.00634 1.12794 0.12015  -0.12992 0.05816  142 GLU B N   
2973 C CA  . GLU B 145 ? 1.00068 1.04195 1.15407 0.11890  -0.15080 0.05776  142 GLU B CA  
2974 C C   . GLU B 145 ? 0.99305 1.05418 1.16502 0.10829  -0.15258 0.04849  142 GLU B C   
2975 O O   . GLU B 145 ? 1.00574 1.08569 1.19508 0.10740  -0.16940 0.04762  142 GLU B O   
2976 C CB  . GLU B 145 ? 1.05241 1.07710 1.16416 0.11571  -0.16171 0.05981  142 GLU B CB  
2977 C CG  . GLU B 145 ? 1.12728 1.12621 1.21155 0.12304  -0.15654 0.06782  142 GLU B CG  
2978 C CD  . GLU B 145 ? 1.19841 1.18047 1.24177 0.11965  -0.16632 0.07003  142 GLU B CD  
2979 O OE1 . GLU B 145 ? 1.23523 1.20155 1.26134 0.12837  -0.17116 0.07842  142 GLU B OE1 
2980 O OE2 . GLU B 145 ? 1.21112 1.19420 1.23863 0.10872  -0.16832 0.06361  142 GLU B OE2 
2981 N N   . MET B 146 ? 0.98114 1.03739 1.14890 0.10016  -0.13636 0.04169  143 MET B N   
2982 C CA  . MET B 146 ? 0.95624 1.02688 1.13537 0.08958  -0.13675 0.03273  143 MET B CA  
2983 C C   . MET B 146 ? 0.89080 0.98722 1.11598 0.09222  -0.14120 0.03190  143 MET B C   
2984 O O   . MET B 146 ? 0.84725 0.94825 1.09913 0.09998  -0.13082 0.03516  143 MET B O   
2985 C CB  . MET B 146 ? 0.99313 1.05246 1.16110 0.08271  -0.11735 0.02686  143 MET B CB  
2986 C CG  . MET B 146 ? 1.05080 1.12024 1.22382 0.07177  -0.11608 0.01764  143 MET B CG  
2987 S SD  . MET B 146 ? 1.10077 1.16485 1.23916 0.06241  -0.12865 0.01374  143 MET B SD  
2988 C CE  . MET B 146 ? 1.09057 1.12890 1.18919 0.06434  -0.12188 0.01895  143 MET B CE  
2989 N N   . LYS B 147 ? 0.89444 1.00682 1.12862 0.08545  -0.15624 0.02756  144 LYS B N   
2990 C CA  . LYS B 147 ? 0.89150 1.02985 1.16993 0.08414  -0.16050 0.02498  144 LYS B CA  
2991 C C   . LYS B 147 ? 0.88024 1.02080 1.16161 0.07254  -0.14887 0.01526  144 LYS B C   
2992 O O   . LYS B 147 ? 0.89072 1.01709 1.13906 0.06452  -0.14587 0.01015  144 LYS B O   
2993 C CB  . LYS B 147 ? 0.92271 1.07685 1.21001 0.08328  -0.18642 0.02630  144 LYS B CB  
2994 C CG  . LYS B 147 ? 0.92704 1.08368 1.22149 0.09661  -0.19907 0.03672  144 LYS B CG  
2995 C CD  . LYS B 147 ? 0.95481 1.10609 1.22122 0.09539  -0.22296 0.03867  144 LYS B CD  
2996 C CE  . LYS B 147 ? 0.97828 1.09967 1.19039 0.09248  -0.21736 0.03829  144 LYS B CE  
2997 N NZ  . LYS B 147 ? 1.00589 1.11706 1.18794 0.09494  -0.23821 0.04274  144 LYS B NZ  
2998 N N   . GLU B 148 ? 0.90024 1.05822 1.22197 0.07220  -0.14136 0.01315  145 GLU B N   
2999 C CA  . GLU B 148 ? 0.92142 1.07928 1.24669 0.06230  -0.12786 0.00452  145 GLU B CA  
3000 C C   . GLU B 148 ? 0.91387 1.07275 1.22102 0.05016  -0.14001 -0.00281 145 GLU B C   
3001 O O   . GLU B 148 ? 0.88456 1.03190 1.17143 0.04247  -0.12955 -0.00933 145 GLU B O   
3002 C CB  . GLU B 148 ? 0.96055 1.13833 1.33468 0.06371  -0.11949 0.00404  145 GLU B CB  
3003 C CG  . GLU B 148 ? 1.01284 1.19064 1.39258 0.05329  -0.10612 -0.00474 145 GLU B CG  
3004 C CD  . GLU B 148 ? 1.05267 1.23505 1.46524 0.05766  -0.08565 -0.00388 145 GLU B CD  
3005 O OE1 . GLU B 148 ? 1.07127 1.23641 1.47153 0.06531  -0.06970 -0.00044 145 GLU B OE1 
3006 O OE2 . GLU B 148 ? 1.05544 1.25738 1.50536 0.05311  -0.08512 -0.00664 145 GLU B OE2 
3007 N N   . GLU B 149 ? 0.93882 1.10961 1.25088 0.04872  -0.16235 -0.00169 146 GLU B N   
3008 C CA  . GLU B 149 ? 0.96889 1.13712 1.25946 0.03750  -0.17476 -0.00852 146 GLU B CA  
3009 C C   . GLU B 149 ? 0.93514 1.07997 1.17483 0.03693  -0.17737 -0.00801 146 GLU B C   
3010 O O   . GLU B 149 ? 0.97110 1.10979 1.18734 0.02857  -0.18630 -0.01329 146 GLU B O   
3011 C CB  . GLU B 149 ? 1.03607 1.22433 1.34959 0.03525  -0.19903 -0.00793 146 GLU B CB  
3012 C CG  . GLU B 149 ? 1.10305 1.28953 1.40463 0.04410  -0.21783 0.00031  146 GLU B CG  
3013 C CD  . GLU B 149 ? 1.13891 1.33986 1.47671 0.05710  -0.21711 0.00931  146 GLU B CD  
3014 O OE1 . GLU B 149 ? 1.13326 1.34265 1.50183 0.05977  -0.19923 0.00934  146 GLU B OE1 
3015 O OE2 . GLU B 149 ? 1.15811 1.36053 1.49241 0.06523  -0.23397 0.01659  146 GLU B OE2 
3016 N N   . ASP B 150 ? 0.86846 0.99909 1.09032 0.04524  -0.16902 -0.00183 147 ASP B N   
3017 C CA  . ASP B 150 ? 0.84086 0.94983 1.01718 0.04477  -0.16979 -0.00052 147 ASP B CA  
3018 C C   . ASP B 150 ? 0.75126 0.84447 0.90784 0.04252  -0.14911 -0.00303 147 ASP B C   
3019 O O   . ASP B 150 ? 0.72018 0.79627 0.84291 0.04266  -0.14681 -0.00105 147 ASP B O   
3020 C CB  . ASP B 150 ? 0.90453 1.00715 1.07122 0.05509  -0.17856 0.00897  147 ASP B CB  
3021 C CG  . ASP B 150 ? 0.96908 1.08229 1.14248 0.05686  -0.20283 0.01170  147 ASP B CG  
3022 O OD1 . ASP B 150 ? 0.97285 1.10325 1.16961 0.05085  -0.21258 0.00682  147 ASP B OD1 
3023 O OD2 . ASP B 150 ? 1.00126 1.10453 1.15543 0.06392  -0.21267 0.01875  147 ASP B OD2 
3024 N N   . LEU B 151 ? 0.67924 0.77747 0.85606 0.04034  -0.13427 -0.00711 148 LEU B N   
3025 C CA  . LEU B 151 ? 0.59415 0.67761 0.75326 0.03861  -0.11612 -0.00924 148 LEU B CA  
3026 C C   . LEU B 151 ? 0.55969 0.63320 0.68791 0.03054  -0.11611 -0.01457 148 LEU B C   
3027 O O   . LEU B 151 ? 0.56259 0.64144 0.68905 0.02439  -0.12544 -0.01938 148 LEU B O   
3028 C CB  . LEU B 151 ? 0.57151 0.66097 0.75697 0.03783  -0.10134 -0.01284 148 LEU B CB  
3029 C CG  . LEU B 151 ? 0.58989 0.68527 0.80393 0.04681  -0.09547 -0.00736 148 LEU B CG  
3030 C CD1 . LEU B 151 ? 0.61112 0.71340 0.85246 0.04488  -0.08169 -0.01165 148 LEU B CD1 
3031 C CD2 . LEU B 151 ? 0.59417 0.67141 0.78823 0.05333  -0.08647 -0.00184 148 LEU B CD2 
3032 N N   . TYR B 152 ? 0.53118 0.58962 0.63515 0.03055  -0.10535 -0.01359 149 TYR B N   
3033 C CA  . TYR B 152 ? 0.52189 0.57093 0.59776 0.02434  -0.10319 -0.01754 149 TYR B CA  
3034 C C   . TYR B 152 ? 0.50710 0.55823 0.58963 0.01868  -0.09304 -0.02492 149 TYR B C   
3035 O O   . TYR B 152 ? 0.48024 0.53379 0.58094 0.01998  -0.08258 -0.02605 149 TYR B O   
3036 C CB  . TYR B 152 ? 0.52657 0.56094 0.57790 0.02613  -0.09557 -0.01329 149 TYR B CB  
3037 C CG  . TYR B 152 ? 0.55330 0.58109 0.58994 0.03061  -0.10471 -0.00624 149 TYR B CG  
3038 C CD1 . TYR B 152 ? 0.58889 0.60988 0.59999 0.02819  -0.11283 -0.00580 149 TYR B CD1 
3039 C CD2 . TYR B 152 ? 0.61765 0.64345 0.66362 0.03770  -0.10428 0.00013  149 TYR B CD2 
3040 C CE1 . TYR B 152 ? 0.66168 0.67403 0.65656 0.03247  -0.12064 0.00090  149 TYR B CE1 
3041 C CE2 . TYR B 152 ? 0.66710 0.68476 0.69783 0.04227  -0.11230 0.00692  149 TYR B CE2 
3042 C CZ  . TYR B 152 ? 0.69098 0.70191 0.69595 0.03952  -0.12065 0.00732  149 TYR B CZ  
3043 O OH  . TYR B 152 ? 0.70357 0.70383 0.69056 0.04422  -0.12807 0.01431  149 TYR B OH  
3044 N N   . ASP B 153 ? 0.52922 0.57699 0.59448 0.01278  -0.09549 -0.02983 150 ASP B N   
3045 C CA  . ASP B 153 ? 0.52230 0.56865 0.58830 0.00788  -0.08527 -0.03650 150 ASP B CA  
3046 C C   . ASP B 153 ? 0.46630 0.50212 0.51615 0.00874  -0.07204 -0.03577 150 ASP B C   
3047 O O   . ASP B 153 ? 0.47269 0.50687 0.52804 0.00736  -0.06141 -0.03945 150 ASP B O   
3048 C CB  . ASP B 153 ? 0.53286 0.57722 0.58461 0.00168  -0.09213 -0.04204 150 ASP B CB  
3049 C CG  . ASP B 153 ? 0.53743 0.59170 0.60311 -0.00063 -0.10785 -0.04322 150 ASP B CG  
3050 O OD1 . ASP B 153 ? 0.52733 0.59407 0.62380 -0.00067 -0.10850 -0.04407 150 ASP B OD1 
3051 O OD2 . ASP B 153 ? 0.54466 0.59381 0.59036 -0.00245 -0.11955 -0.04315 150 ASP B OD2 
3052 N N   . TYR B 154 ? 0.46456 0.49295 0.49486 0.01082  -0.07277 -0.03088 151 TYR B N   
3053 C CA  . TYR B 154 ? 0.46063 0.48068 0.47398 0.00996  -0.06272 -0.03059 151 TYR B CA  
3054 C C   . TYR B 154 ? 0.49296 0.50690 0.49560 0.01289  -0.06275 -0.02365 151 TYR B C   
3055 O O   . TYR B 154 ? 0.49997 0.51252 0.49545 0.01458  -0.07152 -0.01971 151 TYR B O   
3056 C CB  . TYR B 154 ? 0.47813 0.49440 0.47244 0.00614  -0.06294 -0.03436 151 TYR B CB  
3057 C CG  . TYR B 154 ? 0.50881 0.51843 0.48566 0.00582  -0.05413 -0.03289 151 TYR B CG  
3058 C CD1 . TYR B 154 ? 0.51790 0.52230 0.47843 0.00667  -0.05540 -0.02754 151 TYR B CD1 
3059 C CD2 . TYR B 154 ? 0.52569 0.53436 0.50279 0.00474  -0.04456 -0.03662 151 TYR B CD2 
3060 C CE1 . TYR B 154 ? 0.52604 0.52671 0.47452 0.00595  -0.04702 -0.02586 151 TYR B CE1 
3061 C CE2 . TYR B 154 ? 0.54786 0.55301 0.51245 0.00488  -0.03733 -0.03479 151 TYR B CE2 
3062 C CZ  . TYR B 154 ? 0.55835 0.56063 0.51027 0.00521  -0.03847 -0.02942 151 TYR B CZ  
3063 O OH  . TYR B 154 ? 0.57552 0.57655 0.51892 0.00496  -0.03086 -0.02724 151 TYR B OH  
3064 N N   . ALA B 155 ? 0.48658 0.49562 0.48701 0.01315  -0.05338 -0.02217 152 ALA B N   
3065 C CA  . ALA B 155 ? 0.46717 0.46905 0.45760 0.01448  -0.05218 -0.01602 152 ALA B CA  
3066 C C   . ALA B 155 ? 0.47804 0.47607 0.45788 0.01147  -0.04393 -0.01613 152 ALA B C   
3067 O O   . ALA B 155 ? 0.45365 0.45192 0.43984 0.01078  -0.03749 -0.01922 152 ALA B O   
3068 C CB  . ALA B 155 ? 0.46882 0.46786 0.47196 0.01834  -0.05065 -0.01301 152 ALA B CB  
3069 N N   . PHE B 156 ? 0.48315 0.47750 0.44732 0.00984  -0.04408 -0.01247 153 PHE B N   
3070 C CA  . PHE B 156 ? 0.48481 0.47779 0.44202 0.00686  -0.03685 -0.01139 153 PHE B CA  
3071 C C   . PHE B 156 ? 0.49265 0.47862 0.44600 0.00596  -0.03588 -0.00560 153 PHE B C   
3072 O O   . PHE B 156 ? 0.49344 0.47421 0.43757 0.00654  -0.03943 -0.00111 153 PHE B O   
3073 C CB  . PHE B 156 ? 0.50496 0.49902 0.44864 0.00517  -0.03533 -0.01159 153 PHE B CB  
3074 C CG  . PHE B 156 ? 0.47809 0.47422 0.41948 0.00268  -0.02739 -0.01046 153 PHE B CG  
3075 C CD1 . PHE B 156 ? 0.47881 0.47948 0.42900 0.00265  -0.02286 -0.01407 153 PHE B CD1 
3076 C CD2 . PHE B 156 ? 0.47239 0.46605 0.40358 0.00054  -0.02440 -0.00545 153 PHE B CD2 
3077 C CE1 . PHE B 156 ? 0.47660 0.48109 0.42715 0.00094  -0.01696 -0.01252 153 PHE B CE1 
3078 C CE2 . PHE B 156 ? 0.49455 0.49296 0.42800 -0.00189 -0.01731 -0.00397 153 PHE B CE2 
3079 C CZ  . PHE B 156 ? 0.49580 0.50054 0.43979 -0.00147 -0.01433 -0.00743 153 PHE B CZ  
3080 N N   . VAL B 157 ? 0.47688 0.46066 0.43533 0.00436  -0.03140 -0.00573 154 VAL B N   
3081 C CA  . VAL B 157 ? 0.47512 0.44995 0.42955 0.00247  -0.03048 -0.00104 154 VAL B CA  
3082 C C   . VAL B 157 ? 0.46928 0.44607 0.41914 -0.00293 -0.02643 0.00078  154 VAL B C   
3083 O O   . VAL B 157 ? 0.43557 0.41729 0.39076 -0.00441 -0.02359 -0.00205 154 VAL B O   
3084 C CB  . VAL B 157 ? 0.47024 0.43808 0.43187 0.00422  -0.02906 -0.00241 154 VAL B CB  
3085 C CG1 . VAL B 157 ? 0.42599 0.38096 0.38024 0.00224  -0.02853 0.00236  154 VAL B CG1 
3086 C CG2 . VAL B 157 ? 0.49561 0.46525 0.46705 0.00975  -0.03165 -0.00442 154 VAL B CG2 
3087 N N   . ASP B 158 ? 0.48304 0.45592 0.42376 -0.00573 -0.02610 0.00588  155 ASP B N   
3088 C CA  . ASP B 158 ? 0.52303 0.49995 0.46244 -0.01133 -0.02170 0.00830  155 ASP B CA  
3089 C C   . ASP B 158 ? 0.55287 0.52010 0.48357 -0.01544 -0.02100 0.01432  155 ASP B C   
3090 O O   . ASP B 158 ? 0.61368 0.58304 0.53942 -0.01883 -0.01713 0.01774  155 ASP B O   
3091 C CB  . ASP B 158 ? 0.53165 0.51790 0.46882 -0.01046 -0.01849 0.00726  155 ASP B CB  
3092 C CG  . ASP B 158 ? 0.52011 0.51527 0.46296 -0.01473 -0.01279 0.00869  155 ASP B CG  
3093 O OD1 . ASP B 158 ? 0.55945 0.55604 0.51032 -0.01832 -0.01324 0.00903  155 ASP B OD1 
3094 O OD2 . ASP B 158 ? 0.52554 0.52587 0.46472 -0.01435 -0.00792 0.00963  155 ASP B OD2 
3095 N N   . ALA B 159 ? 0.56962 0.52468 0.49764 -0.01508 -0.02352 0.01585  156 ALA B N   
3096 C CA  . ALA B 159 ? 0.60570 0.54838 0.52330 -0.01881 -0.02256 0.02159  156 ALA B CA  
3097 C C   . ALA B 159 ? 0.58419 0.52051 0.50361 -0.02595 -0.02131 0.02247  156 ALA B C   
3098 O O   . ALA B 159 ? 0.56880 0.51492 0.49678 -0.03069 -0.02010 0.02075  156 ALA B O   
3099 C CB  . ALA B 159 ? 0.58701 0.51743 0.49704 -0.01257 -0.02637 0.02371  156 ALA B CB  
3100 N N   A ASP B 160 ? 0.60374 0.52281 0.51446 -0.02657 -0.02211 0.02525  157 ASP B N   
3101 N N   B ASP B 160 ? 0.60410 0.52314 0.51478 -0.02672 -0.02207 0.02529  157 ASP B N   
3102 C CA  A ASP B 160 ? 0.62045 0.52873 0.52925 -0.03356 -0.02191 0.02554  157 ASP B CA  
3103 C CA  B ASP B 160 ? 0.62011 0.52909 0.52904 -0.03427 -0.02172 0.02577  157 ASP B CA  
3104 C C   A ASP B 160 ? 0.61795 0.52899 0.53430 -0.03215 -0.02379 0.02007  157 ASP B C   
3105 C C   B ASP B 160 ? 0.61894 0.52889 0.53454 -0.03264 -0.02374 0.02040  157 ASP B C   
3106 O O   A ASP B 160 ? 0.59138 0.49756 0.50829 -0.02479 -0.02440 0.01748  157 ASP B O   
3107 O O   B ASP B 160 ? 0.59058 0.49374 0.50552 -0.02545 -0.02430 0.01819  157 ASP B O   
3108 C CB  A ASP B 160 ? 0.66588 0.55180 0.56131 -0.03217 -0.02177 0.02905  157 ASP B CB  
3109 C CB  B ASP B 160 ? 0.65393 0.54052 0.54877 -0.03463 -0.02120 0.02990  157 ASP B CB  
3110 C CG  A ASP B 160 ? 0.66478 0.53486 0.55380 -0.04030 -0.02152 0.02934  157 ASP B CG  
3111 C CG  B ASP B 160 ? 0.66790 0.54701 0.55925 -0.02368 -0.02277 0.03015  157 ASP B CG  
3112 O OD1 A ASP B 160 ? 0.65866 0.53597 0.55444 -0.04716 -0.02293 0.02674  157 ASP B OD1 
3113 O OD1 B ASP B 160 ? 0.66346 0.55551 0.56157 -0.01696 -0.02471 0.02840  157 ASP B OD1 
3114 O OD2 A ASP B 160 ? 0.70282 0.55192 0.57895 -0.03973 -0.02038 0.03229  157 ASP B OD2 
3115 O OD2 B ASP B 160 ? 0.69896 0.55873 0.58103 -0.02187 -0.02213 0.03230  157 ASP B OD2 
3116 N N   . LYS B 161 ? 0.55493 0.57637 0.63407 -0.00087 0.02501  -0.00389 158 LYS B N   
3117 C CA  . LYS B 161 ? 0.58825 0.60878 0.66399 -0.00156 0.02323  -0.01020 158 LYS B CA  
3118 C C   . LYS B 161 ? 0.64996 0.66544 0.72756 -0.00337 0.01838  -0.01571 158 LYS B C   
3119 O O   . LYS B 161 ? 0.71811 0.73177 0.78938 -0.00264 0.01771  -0.02149 158 LYS B O   
3120 C CB  . LYS B 161 ? 0.53657 0.56116 0.61791 -0.00262 0.02396  -0.00752 158 LYS B CB  
3121 C CG  . LYS B 161 ? 0.50966 0.53962 0.59064 0.00003  0.02953  -0.00081 158 LYS B CG  
3122 C CD  . LYS B 161 ? 0.45433 0.48326 0.52137 0.00404  0.03267  -0.00321 158 LYS B CD  
3123 C CE  . LYS B 161 ? 0.47066 0.50323 0.53456 0.00818  0.03845  0.00330  158 LYS B CE  
3124 N NZ  . LYS B 161 ? 0.46328 0.49174 0.51362 0.01243  0.04012  0.00264  158 LYS B NZ  
3125 N N   . SER B 162 ? 0.61452 0.62742 0.70057 -0.00529 0.01490  -0.01371 159 SER B N   
3126 C CA  . SER B 162 ? 0.61296 0.61952 0.69935 -0.00599 0.00994  -0.01921 159 SER B CA  
3127 C C   . SER B 162 ? 0.59865 0.60238 0.67881 -0.00387 0.01056  -0.02321 159 SER B C   
3128 O O   . SER B 162 ? 0.62107 0.61959 0.69998 -0.00319 0.00752  -0.02799 159 SER B O   
3129 C CB  . SER B 162 ? 0.61800 0.62130 0.71524 -0.00844 0.00484  -0.01577 159 SER B CB  
3130 O OG  . SER B 162 ? 0.60498 0.60928 0.70633 -0.00847 0.00581  -0.01100 159 SER B OG  
3131 N N   . ASN B 163 ? 0.56632 0.57274 0.64229 -0.00237 0.01415  -0.02124 160 ASN B N   
3132 C CA  . ASN B 163 ? 0.51291 0.51692 0.58525 -0.00072 0.01420  -0.02365 160 ASN B CA  
3133 C C   . ASN B 163 ? 0.45122 0.45702 0.51589 0.00111  0.01648  -0.02624 160 ASN B C   
3134 O O   . ASN B 163 ? 0.47524 0.47974 0.53807 0.00239  0.01643  -0.02701 160 ASN B O   
3135 C CB  . ASN B 163 ? 0.57196 0.57575 0.64660 -0.00075 0.01466  -0.01869 160 ASN B CB  
3136 C CG  . ASN B 163 ? 0.62396 0.62330 0.70337 -0.00108 0.01140  -0.01976 160 ASN B CG  
3137 O OD1 . ASN B 163 ? 0.62711 0.62327 0.70616 -0.00022 0.00952  -0.02478 160 ASN B OD1 
3138 N ND2 . ASN B 163 ? 0.64144 0.64035 0.72485 -0.00184 0.01092  -0.01484 160 ASN B ND2 
3139 N N   . TYR B 164 ? 0.41895 0.42760 0.48020 0.00109  0.01788  -0.02716 161 TYR B N   
3140 C CA  . TYR B 164 ? 0.40427 0.41449 0.45911 0.00255  0.01917  -0.02887 161 TYR B CA  
3141 C C   . TYR B 164 ? 0.39515 0.40417 0.44968 0.00359  0.01843  -0.03257 161 TYR B C   
3142 O O   . TYR B 164 ? 0.38504 0.39440 0.43773 0.00472  0.01849  -0.03220 161 TYR B O   
3143 C CB  . TYR B 164 ? 0.37171 0.38490 0.42389 0.00218  0.02022  -0.02955 161 TYR B CB  
3144 C CG  . TYR B 164 ? 0.39419 0.40947 0.44402 0.00288  0.02226  -0.02553 161 TYR B CG  
3145 C CD1 . TYR B 164 ? 0.38314 0.39827 0.43548 0.00317  0.02342  -0.02079 161 TYR B CD1 
3146 C CD2 . TYR B 164 ? 0.37286 0.39018 0.41762 0.00381  0.02327  -0.02617 161 TYR B CD2 
3147 C CE1 . TYR B 164 ? 0.40447 0.42161 0.45352 0.00505  0.02636  -0.01659 161 TYR B CE1 
3148 C CE2 . TYR B 164 ? 0.36433 0.38299 0.40568 0.00563  0.02560  -0.02265 161 TYR B CE2 
3149 C CZ  . TYR B 164 ? 0.40520 0.42386 0.44832 0.00659  0.02756  -0.01778 161 TYR B CZ  
3150 O OH  . TYR B 164 ? 0.42835 0.44845 0.46699 0.00958  0.03091  -0.01381 161 TYR B OH  
3151 N N   . ALA B 165 ? 0.36609 0.37330 0.42237 0.00364  0.01754  -0.03574 162 ALA B N   
3152 C CA  . ALA B 165 ? 0.42400 0.43042 0.47938 0.00581  0.01803  -0.03875 162 ALA B CA  
3153 C C   . ALA B 165 ? 0.45722 0.46220 0.51594 0.00697  0.01778  -0.03741 162 ALA B C   
3154 O O   . ALA B 165 ? 0.44255 0.44917 0.50181 0.00870  0.01891  -0.03739 162 ALA B O   
3155 C CB  . ALA B 165 ? 0.43353 0.43614 0.48782 0.00671  0.01680  -0.04257 162 ALA B CB  
3156 N N   . ASN B 166 ? 0.46492 0.46716 0.52707 0.00590  0.01613  -0.03558 163 ASN B N   
3157 C CA  . ASN B 166 ? 0.45986 0.46042 0.52540 0.00668  0.01542  -0.03401 163 ASN B CA  
3158 C C   . ASN B 166 ? 0.48824 0.49056 0.55209 0.00644  0.01562  -0.03082 163 ASN B C   
3159 O O   . ASN B 166 ? 0.51093 0.51292 0.57712 0.00753  0.01509  -0.03002 163 ASN B O   
3160 C CB  . ASN B 166 ? 0.48767 0.48475 0.55745 0.00533  0.01313  -0.03239 163 ASN B CB  
3161 C CG  . ASN B 166 ? 0.52629 0.51890 0.59818 0.00647  0.01110  -0.03595 163 ASN B CG  
3162 O OD1 . ASN B 166 ? 0.57475 0.56626 0.64493 0.00941  0.01209  -0.03934 163 ASN B OD1 
3163 N ND2 . ASN B 166 ? 0.48755 0.47715 0.56309 0.00457  0.00804  -0.03481 163 ASN B ND2 
3164 N N   A TYR B 167 ? 0.47183 0.47528 0.53154 0.00539  0.01597  -0.02875 164 TYR B N   
3165 N N   B TYR B 167 ? 0.47183 0.47531 0.53150 0.00540  0.01598  -0.02878 164 TYR B N   
3166 C CA  A TYR B 167 ? 0.47589 0.47894 0.53126 0.00594  0.01519  -0.02639 164 TYR B CA  
3167 C CA  B TYR B 167 ? 0.47594 0.47896 0.53137 0.00595  0.01517  -0.02639 164 TYR B CA  
3168 C C   A TYR B 167 ? 0.46619 0.47120 0.52132 0.00678  0.01478  -0.02770 164 TYR B C   
3169 C C   B TYR B 167 ? 0.46615 0.47117 0.52119 0.00678  0.01477  -0.02767 164 TYR B C   
3170 O O   A TYR B 167 ? 0.46230 0.46580 0.51820 0.00730  0.01253  -0.02589 164 TYR B O   
3171 O O   B TYR B 167 ? 0.46403 0.46752 0.51961 0.00730  0.01248  -0.02586 164 TYR B O   
3172 C CB  A TYR B 167 ? 0.50147 0.50506 0.55084 0.00590  0.01626  -0.02450 164 TYR B CB  
3173 C CB  B TYR B 167 ? 0.50200 0.50540 0.55146 0.00591  0.01619  -0.02435 164 TYR B CB  
3174 C CG  A TYR B 167 ? 0.52901 0.53193 0.57978 0.00532  0.01727  -0.02133 164 TYR B CG  
3175 C CG  B TYR B 167 ? 0.53013 0.53257 0.58112 0.00535  0.01702  -0.02111 164 TYR B CG  
3176 C CD1 A TYR B 167 ? 0.53809 0.53837 0.59288 0.00488  0.01598  -0.01944 164 TYR B CD1 
3177 C CD1 B TYR B 167 ? 0.53635 0.53606 0.59147 0.00494  0.01557  -0.01950 164 TYR B CD1 
3178 C CD2 A TYR B 167 ? 0.53425 0.53970 0.58350 0.00524  0.01953  -0.01945 164 TYR B CD2 
3179 C CD2 B TYR B 167 ? 0.53443 0.53921 0.58392 0.00529  0.01930  -0.01891 164 TYR B CD2 
3180 C CE1 A TYR B 167 ? 0.53629 0.53658 0.59358 0.00419  0.01680  -0.01549 164 TYR B CE1 
3181 C CE1 B TYR B 167 ? 0.53481 0.53415 0.59241 0.00425  0.01616  -0.01563 164 TYR B CE1 
3182 C CE2 A TYR B 167 ? 0.53651 0.54253 0.58903 0.00479  0.02081  -0.01506 164 TYR B CE2 
3183 C CE2 B TYR B 167 ? 0.54134 0.54638 0.59410 0.00485  0.02040  -0.01449 164 TYR B CE2 
3184 C CZ  A TYR B 167 ? 0.55169 0.55520 0.60824 0.00417  0.01937  -0.01295 164 TYR B CZ  
3185 C CZ  B TYR B 167 ? 0.54894 0.55125 0.60569 0.00421  0.01872  -0.01278 164 TYR B CZ  
3186 O OH  A TYR B 167 ? 0.55502 0.55968 0.61600 0.00356  0.02054  -0.00760 164 TYR B OH  
3187 O OH  B TYR B 167 ? 0.56425 0.56728 0.62526 0.00359  0.01964  -0.00752 164 TYR B OH  
3188 N N   . HIS B 168 ? 0.42190 0.43011 0.47664 0.00681  0.01648  -0.03025 165 HIS B N   
3189 C CA  . HIS B 168 ? 0.39649 0.40760 0.45180 0.00752  0.01644  -0.03057 165 HIS B CA  
3190 C C   . HIS B 168 ? 0.45558 0.46734 0.51753 0.00885  0.01635  -0.02953 165 HIS B C   
3191 O O   . HIS B 168 ? 0.45445 0.46752 0.51918 0.00908  0.01460  -0.02705 165 HIS B O   
3192 C CB  . HIS B 168 ? 0.39400 0.40807 0.44761 0.00752  0.01861  -0.03345 165 HIS B CB  
3193 C CG  . HIS B 168 ? 0.41577 0.43360 0.47009 0.00814  0.01891  -0.03306 165 HIS B CG  
3194 N ND1 . HIS B 168 ? 0.41493 0.43362 0.46677 0.00734  0.01673  -0.03150 165 HIS B ND1 
3195 C CD2 . HIS B 168 ? 0.40085 0.42176 0.45817 0.00983  0.02112  -0.03354 165 HIS B CD2 
3196 C CE1 . HIS B 168 ? 0.42556 0.44814 0.48027 0.00780  0.01708  -0.03069 165 HIS B CE1 
3197 N NE2 . HIS B 168 ? 0.41749 0.44198 0.47556 0.00946  0.02030  -0.03159 165 HIS B NE2 
3198 N N   . GLU B 169 ? 0.47081 0.48142 0.53608 0.00994  0.01781  -0.03101 166 GLU B N   
3199 C CA  . GLU B 169 ? 0.49237 0.50408 0.56439 0.01207  0.01865  -0.02990 166 GLU B CA  
3200 C C   . GLU B 169 ? 0.48181 0.49166 0.55821 0.01129  0.01536  -0.02608 166 GLU B C   
3201 O O   . GLU B 169 ? 0.47942 0.49152 0.56293 0.01249  0.01516  -0.02341 166 GLU B O   
3202 C CB  . GLU B 169 ? 0.48669 0.49587 0.55975 0.01404  0.02031  -0.03282 166 GLU B CB  
3203 C CG  . GLU B 169 ? 0.44358 0.45321 0.51198 0.01592  0.02291  -0.03663 166 GLU B CG  
3204 C CD  . GLU B 169 ? 0.48816 0.50319 0.55708 0.01789  0.02585  -0.03554 166 GLU B CD  
3205 O OE1 . GLU B 169 ? 0.50499 0.52313 0.58053 0.01984  0.02722  -0.03242 166 GLU B OE1 
3206 O OE2 . GLU B 169 ? 0.51022 0.52675 0.57398 0.01737  0.02667  -0.03712 166 GLU B OE2 
3207 N N   . ARG B 170 ? 0.47050 0.47613 0.54298 0.00954  0.01268  -0.02522 167 ARG B N   
3208 C CA  . ARG B 170 ? 0.48755 0.48968 0.56176 0.00895  0.00861  -0.02172 167 ARG B CA  
3209 C C   . ARG B 170 ? 0.48940 0.49085 0.55997 0.00840  0.00526  -0.01976 167 ARG B C   
3210 O O   . ARG B 170 ? 0.48790 0.48791 0.56322 0.00833  0.00133  -0.01660 167 ARG B O   
3211 C CB  . ARG B 170 ? 0.49020 0.48737 0.56032 0.00800  0.00723  -0.02114 167 ARG B CB  
3212 C CG  . ARG B 170 ? 0.54128 0.53716 0.61735 0.00824  0.00785  -0.02159 167 ARG B CG  
3213 C CD  . ARG B 170 ? 0.57079 0.56848 0.64717 0.00871  0.01102  -0.02514 167 ARG B CD  
3214 N NE  . ARG B 170 ? 0.60342 0.59805 0.68397 0.00874  0.01024  -0.02554 167 ARG B NE  
3215 C CZ  . ARG B 170 ? 0.62112 0.61495 0.70271 0.00951  0.01121  -0.02865 167 ARG B CZ  
3216 N NH1 . ARG B 170 ? 0.61270 0.60848 0.69085 0.01034  0.01327  -0.03163 167 ARG B NH1 
3217 N NH2 . ARG B 170 ? 0.62300 0.61313 0.70868 0.00949  0.00935  -0.02879 167 ARG B NH2 
3218 N N   . LEU B 171 ? 0.49125 0.49322 0.55403 0.00807  0.00611  -0.02141 168 LEU B N   
3219 C CA  . LEU B 171 ? 0.45033 0.44955 0.50736 0.00800  0.00204  -0.02002 168 LEU B CA  
3220 C C   . LEU B 171 ? 0.39004 0.39302 0.45340 0.00782  0.00027  -0.01846 168 LEU B C   
3221 O O   . LEU B 171 ? 0.36780 0.36695 0.42985 0.00761  -0.00551 -0.01611 168 LEU B O   
3222 C CB  . LEU B 171 ? 0.41870 0.41764 0.46605 0.00823  0.00392  -0.02207 168 LEU B CB  
3223 C CG  . LEU B 171 ? 0.41944 0.41427 0.46030 0.00881  0.00484  -0.02152 168 LEU B CG  
3224 C CD1 . LEU B 171 ? 0.42115 0.41735 0.45488 0.00942  0.00773  -0.02264 168 LEU B CD1 
3225 C CD2 . LEU B 171 ? 0.40286 0.38989 0.43806 0.00995  -0.00015 -0.01894 168 LEU B CD2 
3226 N N   . VAL B 172 ? 0.34337 0.35315 0.41328 0.00820  0.00467  -0.01928 169 VAL B N   
3227 C CA  . VAL B 172 ? 0.40076 0.41536 0.47851 0.00830  0.00375  -0.01635 169 VAL B CA  
3228 C C   . VAL B 172 ? 0.46891 0.48312 0.55745 0.00842  0.00045  -0.01158 169 VAL B C   
3229 O O   . VAL B 172 ? 0.48953 0.50784 0.58713 0.00832  -0.00124 -0.00738 169 VAL B O   
3230 C CB  . VAL B 172 ? 0.43107 0.45280 0.51175 0.00964  0.01014  -0.01801 169 VAL B CB  
3231 C CG1 . VAL B 172 ? 0.47520 0.49722 0.54657 0.00908  0.01222  -0.02212 169 VAL B CG1 
3232 C CG2 . VAL B 172 ? 0.44851 0.47094 0.53306 0.01164  0.01437  -0.01920 169 VAL B CG2 
3233 N N   . LYS B 173 ? 0.50258 0.51225 0.59158 0.00852  -0.00068 -0.01148 170 LYS B N   
3234 C CA  . LYS B 173 ? 0.57646 0.58441 0.67553 0.00833  -0.00496 -0.00678 170 LYS B CA  
3235 C C   . LYS B 173 ? 0.55900 0.55713 0.65182 0.00708  -0.01288 -0.00550 170 LYS B C   
3236 O O   . LYS B 173 ? 0.57175 0.56703 0.67253 0.00641  -0.01886 -0.00100 170 LYS B O   
3237 C CB  . LYS B 173 ? 0.63979 0.64972 0.74550 0.00985  -0.00057 -0.00720 170 LYS B CB  
3238 C CG  . LYS B 173 ? 0.70029 0.71809 0.81059 0.01244  0.00704  -0.00851 170 LYS B CG  
3239 C CD  . LYS B 173 ? 0.78943 0.80778 0.90629 0.01479  0.01031  -0.00865 170 LYS B CD  
3240 C CE  . LYS B 173 ? 0.84063 0.86597 0.96183 0.01878  0.01754  -0.00897 170 LYS B CE  
3241 N NZ  . LYS B 173 ? 0.84127 0.87371 0.97225 0.01938  0.01800  -0.00306 170 LYS B NZ  
3242 N N   . LEU B 174 ? 0.55090 0.54350 0.62969 0.00715  -0.01313 -0.00890 171 LEU B N   
3243 C CA  . LEU B 174 ? 0.53946 0.52159 0.60879 0.00720  -0.01992 -0.00799 171 LEU B CA  
3244 C C   . LEU B 174 ? 0.51791 0.49502 0.57889 0.00752  -0.02571 -0.00782 171 LEU B C   
3245 O O   . LEU B 174 ? 0.51204 0.47873 0.56493 0.00823  -0.03311 -0.00663 171 LEU B O   
3246 C CB  . LEU B 174 ? 0.52393 0.50272 0.58247 0.00803  -0.01637 -0.01072 171 LEU B CB  
3247 C CG  . LEU B 174 ? 0.54221 0.52263 0.60714 0.00766  -0.01304 -0.01066 171 LEU B CG  
3248 C CD1 . LEU B 174 ? 0.55761 0.53623 0.61333 0.00816  -0.00935 -0.01251 171 LEU B CD1 
3249 C CD2 . LEU B 174 ? 0.55382 0.52842 0.62406 0.00717  -0.01925 -0.00708 171 LEU B CD2 
3250 N N   . VAL B 175 ? 0.50278 0.48601 0.56463 0.00731  -0.02307 -0.00909 172 VAL B N   
3251 C CA  . VAL B 175 ? 0.51007 0.48895 0.56520 0.00762  -0.02888 -0.00901 172 VAL B CA  
3252 C C   . VAL B 175 ? 0.48964 0.47208 0.55893 0.00596  -0.03379 -0.00439 172 VAL B C   
3253 O O   . VAL B 175 ? 0.51606 0.50856 0.59858 0.00519  -0.02855 -0.00252 172 VAL B O   
3254 C CB  . VAL B 175 ? 0.51890 0.50219 0.56621 0.00830  -0.02317 -0.01300 172 VAL B CB  
3255 C CG1 . VAL B 175 ? 0.51243 0.49277 0.55571 0.00846  -0.02907 -0.01272 172 VAL B CG1 
3256 C CG2 . VAL B 175 ? 0.51932 0.49844 0.55340 0.01018  -0.01951 -0.01596 172 VAL B CG2 
3257 N N   . ARG B 176 ? 0.46697 0.44077 0.53353 0.00581  -0.04408 -0.00209 173 ARG B N   
3258 C CA  . ARG B 176 ? 0.47865 0.45531 0.56061 0.00385  -0.05034 0.00374  173 ARG B CA  
3259 C C   . ARG B 176 ? 0.46723 0.45509 0.55592 0.00306  -0.04518 0.00406  173 ARG B C   
3260 O O   . ARG B 176 ? 0.46538 0.45595 0.54427 0.00394  -0.03932 -0.00077 173 ARG B O   
3261 C CB  . ARG B 176 ? 0.46509 0.42821 0.54096 0.00390  -0.06403 0.00563  173 ARG B CB  
3262 C CG  . ARG B 176 ? 0.48434 0.44253 0.54592 0.00534  -0.06670 0.00183  173 ARG B CG  
3263 C CD  . ARG B 176 ? 0.51315 0.45760 0.57082 0.00553  -0.08177 0.00425  173 ARG B CD  
3264 N NE  . ARG B 176 ? 0.57312 0.50961 0.61273 0.00828  -0.08467 -0.00049 173 ARG B NE  
3265 C CZ  . ARG B 176 ? 0.60740 0.54835 0.64990 0.00740  -0.08572 -0.00050 173 ARG B CZ  
3266 N NH1 . ARG B 176 ? 0.59213 0.52494 0.61740 0.01048  -0.08839 -0.00508 173 ARG B NH1 
3267 N NH2 . ARG B 176 ? 0.58819 0.54182 0.65071 0.00386  -0.08380 0.00440  173 ARG B NH2 
3268 N N   . ILE B 177 ? 0.41527 0.40990 0.52173 0.00142  -0.04747 0.01057  174 ILE B N   
3269 C CA  . ILE B 177 ? 0.43257 0.43684 0.54579 0.00067  -0.04435 0.01232  174 ILE B CA  
3270 C C   . ILE B 177 ? 0.45771 0.45425 0.56033 0.00028  -0.05238 0.01037  174 ILE B C   
3271 O O   . ILE B 177 ? 0.45785 0.44317 0.55798 -0.00013 -0.06414 0.01228  174 ILE B O   
3272 C CB  . ILE B 177 ? 0.43400 0.44710 0.56972 -0.00064 -0.04558 0.02139  174 ILE B CB  
3273 C CG1 . ILE B 177 ? 0.43960 0.46186 0.58436 0.00102  -0.03515 0.02250  174 ILE B CG1 
3274 C CG2 . ILE B 177 ? 0.38312 0.40431 0.52561 -0.00166 -0.04512 0.02462  174 ILE B CG2 
3275 C CD1 . ILE B 177 ? 0.47790 0.50932 0.64577 0.00073  -0.03522 0.03241  174 ILE B CD1 
3276 N N   . GLY B 178 ? 0.46920 0.47062 0.56481 0.00069  -0.04665 0.00636  175 GLY B N   
3277 C CA  . GLY B 178 ? 0.45019 0.44410 0.53369 0.00104  -0.05296 0.00334  175 GLY B CA  
3278 C C   . GLY B 178 ? 0.46198 0.44564 0.52520 0.00374  -0.05262 -0.00335 175 GLY B C   
3279 O O   . GLY B 178 ? 0.52120 0.49842 0.57252 0.00509  -0.05666 -0.00644 175 GLY B O   
3280 N N   . GLY B 179 ? 0.44711 0.42913 0.50634 0.00491  -0.04790 -0.00519 176 GLY B N   
3281 C CA  . GLY B 179 ? 0.51138 0.48586 0.55276 0.00774  -0.04564 -0.01042 176 GLY B CA  
3282 C C   . GLY B 179 ? 0.50252 0.48490 0.53924 0.00822  -0.03537 -0.01470 176 GLY B C   
3283 O O   . GLY B 179 ? 0.47483 0.46782 0.52096 0.00646  -0.02962 -0.01430 176 GLY B O   
3284 N N   . ALA B 180 ? 0.45748 0.43421 0.47931 0.01097  -0.03315 -0.01841 177 ALA B N   
3285 C CA  . ALA B 180 ? 0.38432 0.36704 0.40146 0.01153  -0.02502 -0.02192 177 ALA B CA  
3286 C C   . ALA B 180 ? 0.41939 0.40419 0.43449 0.01220  -0.01751 -0.02316 177 ALA B C   
3287 O O   . ALA B 180 ? 0.49527 0.47326 0.50466 0.01389  -0.01909 -0.02237 177 ALA B O   
3288 C CB  . ALA B 180 ? 0.35563 0.33154 0.35882 0.01455  -0.02801 -0.02432 177 ALA B CB  
3289 N N   . ILE B 181 ? 0.38961 0.38319 0.40951 0.01081  -0.01005 -0.02481 178 ILE B N   
3290 C CA  . ILE B 181 ? 0.39840 0.39415 0.41695 0.01118  -0.00350 -0.02592 178 ILE B CA  
3291 C C   . ILE B 181 ? 0.42575 0.42489 0.43988 0.01168  0.00076  -0.02809 178 ILE B C   
3292 O O   . ILE B 181 ? 0.40489 0.40952 0.42336 0.01002  0.00194  -0.02936 178 ILE B O   
3293 C CB  . ILE B 181 ? 0.41360 0.41540 0.44323 0.00910  0.00033  -0.02566 178 ILE B CB  
3294 C CG1 . ILE B 181 ? 0.42089 0.42083 0.45758 0.00857  -0.00389 -0.02285 178 ILE B CG1 
3295 C CG2 . ILE B 181 ? 0.38221 0.38428 0.41078 0.00936  0.00506  -0.02626 178 ILE B CG2 
3296 C CD1 . ILE B 181 ? 0.40846 0.41412 0.45563 0.00759  0.00015  -0.02250 178 ILE B CD1 
3297 N N   . LEU B 182 ? 0.41993 0.41599 0.42581 0.01415  0.00314  -0.02795 179 LEU B N   
3298 C CA  . LEU B 182 ? 0.40196 0.40121 0.40456 0.01507  0.00719  -0.02899 179 LEU B CA  
3299 C C   . LEU B 182 ? 0.39890 0.40229 0.40588 0.01428  0.01305  -0.02797 179 LEU B C   
3300 O O   . LEU B 182 ? 0.43012 0.43069 0.43508 0.01561  0.01418  -0.02580 179 LEU B O   
3301 C CB  . LEU B 182 ? 0.41248 0.40504 0.40206 0.01960  0.00539  -0.02872 179 LEU B CB  
3302 C CG  . LEU B 182 ? 0.46441 0.45367 0.44958 0.02041  -0.00030 -0.03037 179 LEU B CG  
3303 C CD1 . LEU B 182 ? 0.49196 0.47582 0.47854 0.01944  -0.00802 -0.02969 179 LEU B CD1 
3304 C CD2 . LEU B 182 ? 0.45187 0.43492 0.42319 0.02586  -0.00043 -0.03071 179 LEU B CD2 
3305 N N   . TYR B 183 ? 0.35753 0.36702 0.37074 0.01202  0.01603  -0.02921 180 TYR B N   
3306 C CA  . TYR B 183 ? 0.34217 0.35516 0.36116 0.01076  0.02012  -0.02800 180 TYR B CA  
3307 C C   . TYR B 183 ? 0.35794 0.37346 0.37518 0.01207  0.02317  -0.02670 180 TYR B C   
3308 O O   . TYR B 183 ? 0.38290 0.40078 0.40042 0.01131  0.02273  -0.02858 180 TYR B O   
3309 C CB  . TYR B 183 ? 0.30910 0.32547 0.33650 0.00746  0.02019  -0.03023 180 TYR B CB  
3310 C CG  . TYR B 183 ? 0.36760 0.38229 0.39789 0.00692  0.01832  -0.03081 180 TYR B CG  
3311 C CD1 . TYR B 183 ? 0.34508 0.35793 0.37830 0.00686  0.01882  -0.02932 180 TYR B CD1 
3312 C CD2 . TYR B 183 ? 0.35679 0.37213 0.38788 0.00659  0.01608  -0.03210 180 TYR B CD2 
3313 C CE1 . TYR B 183 ? 0.43425 0.44569 0.47083 0.00667  0.01723  -0.02959 180 TYR B CE1 
3314 C CE2 . TYR B 183 ? 0.40957 0.42424 0.44493 0.00649  0.01487  -0.03164 180 TYR B CE2 
3315 C CZ  . TYR B 183 ? 0.45622 0.46879 0.49411 0.00663  0.01550  -0.03062 180 TYR B CZ  
3316 O OH  . TYR B 183 ? 0.47821 0.49023 0.52106 0.00679  0.01442  -0.02996 180 TYR B OH  
3317 N N   . ASP B 184 ? 0.38728 0.40269 0.40344 0.01416  0.02643  -0.02290 181 ASP B N   
3318 C CA  . ASP B 184 ? 0.42616 0.44479 0.44205 0.01615  0.03028  -0.02018 181 ASP B CA  
3319 C C   . ASP B 184 ? 0.37784 0.40207 0.40588 0.01243  0.03180  -0.01901 181 ASP B C   
3320 O O   . ASP B 184 ? 0.41808 0.44247 0.45318 0.00935  0.03051  -0.01934 181 ASP B O   
3321 C CB  . ASP B 184 ? 0.48526 0.50178 0.49488 0.02077  0.03380  -0.01539 181 ASP B CB  
3322 C CG  . ASP B 184 ? 0.55219 0.57092 0.55773 0.02507  0.03810  -0.01252 181 ASP B CG  
3323 O OD1 . ASP B 184 ? 0.55929 0.57689 0.55953 0.02639  0.03646  -0.01562 181 ASP B OD1 
3324 O OD2 . ASP B 184 ? 0.60102 0.62287 0.60923 0.02734  0.04321  -0.00671 181 ASP B OD2 
3325 N N   . ASN B 185 ? 0.38676 0.41475 0.41711 0.01290  0.03380  -0.01774 182 ASN B N   
3326 C CA  . ASN B 185 ? 0.39110 0.42380 0.43341 0.00978  0.03466  -0.01534 182 ASN B CA  
3327 C C   . ASN B 185 ? 0.38204 0.41415 0.42917 0.00523  0.03041  -0.02007 182 ASN B C   
3328 O O   . ASN B 185 ? 0.37521 0.40838 0.43164 0.00221  0.02911  -0.01881 182 ASN B O   
3329 C CB  . ASN B 185 ? 0.41498 0.44919 0.46500 0.00934  0.03672  -0.00969 182 ASN B CB  
3330 C CG  . ASN B 185 ? 0.48729 0.52268 0.53254 0.01448  0.04199  -0.00385 182 ASN B CG  
3331 O OD1 . ASN B 185 ? 0.55790 0.58997 0.59718 0.01662  0.04267  -0.00269 182 ASN B OD1 
3332 N ND2 . ASN B 185 ? 0.47918 0.51908 0.52664 0.01696  0.04593  0.00014  182 ASN B ND2 
3333 N N   . THR B 186 ? 0.35323 0.38320 0.39405 0.00497  0.02789  -0.02511 183 THR B N   
3334 C CA  . THR B 186 ? 0.36471 0.39371 0.40839 0.00171  0.02470  -0.02919 183 THR B CA  
3335 C C   . THR B 186 ? 0.37110 0.40203 0.41911 -0.00046 0.02352  -0.02985 183 THR B C   
3336 O O   . THR B 186 ? 0.36052 0.38959 0.40985 -0.00273 0.02072  -0.03304 183 THR B O   
3337 C CB  . THR B 186 ? 0.33699 0.36419 0.37424 0.00224  0.02288  -0.03300 183 THR B CB  
3338 O OG1 . THR B 186 ? 0.34577 0.37370 0.37752 0.00385  0.02263  -0.03345 183 THR B OG1 
3339 C CG2 . THR B 186 ? 0.30837 0.33294 0.34341 0.00364  0.02289  -0.03230 183 THR B CG2 
3340 N N   . LEU B 187 ? 0.37880 0.41292 0.42862 0.00063  0.02554  -0.02680 184 LEU B N   
3341 C CA  . LEU B 187 ? 0.33708 0.37312 0.39317 -0.00170 0.02410  -0.02638 184 LEU B CA  
3342 C C   . LEU B 187 ? 0.39946 0.43753 0.46703 -0.00307 0.02465  -0.02085 184 LEU B C   
3343 O O   . LEU B 187 ? 0.37753 0.41596 0.45240 -0.00585 0.02188  -0.02019 184 LEU B O   
3344 C CB  . LEU B 187 ? 0.32128 0.35989 0.37367 0.00028  0.02550  -0.02633 184 LEU B CB  
3345 C CG  . LEU B 187 ? 0.33221 0.36901 0.37581 0.00061  0.02330  -0.03129 184 LEU B CG  
3346 C CD1 . LEU B 187 ? 0.33684 0.37550 0.37744 0.00272  0.02398  -0.03097 184 LEU B CD1 
3347 C CD2 . LEU B 187 ? 0.32747 0.36251 0.37199 -0.00291 0.01963  -0.03521 184 LEU B CD2 
3348 N N   . TRP B 188 ? 0.38520 0.42441 0.45506 -0.00131 0.02766  -0.01636 185 TRP B N   
3349 C CA  . TRP B 188 ? 0.38560 0.42694 0.46797 -0.00285 0.02783  -0.00999 185 TRP B CA  
3350 C C   . TRP B 188 ? 0.38584 0.43163 0.47870 -0.00403 0.02796  -0.00544 185 TRP B C   
3351 O O   . TRP B 188 ? 0.36651 0.41104 0.46956 -0.00794 0.02319  -0.00427 185 TRP B O   
3352 C CB  . TRP B 188 ? 0.35745 0.39364 0.44373 -0.00631 0.02251  -0.01240 185 TRP B CB  
3353 C CG  . TRP B 188 ? 0.38412 0.42136 0.48132 -0.00731 0.02241  -0.00585 185 TRP B CG  
3354 C CD1 . TRP B 188 ? 0.40990 0.44512 0.51917 -0.01097 0.01712  -0.00318 185 TRP B CD1 
3355 C CD2 . TRP B 188 ? 0.35759 0.39760 0.45480 -0.00462 0.02715  -0.00067 185 TRP B CD2 
3356 N NE1 . TRP B 188 ? 0.36857 0.40595 0.48678 -0.01107 0.01829  0.00374  185 TRP B NE1 
3357 C CE2 . TRP B 188 ? 0.39537 0.43602 0.50606 -0.00710 0.02492  0.00545  185 TRP B CE2 
3358 C CE3 . TRP B 188 ? 0.36111 0.40219 0.44777 -0.00025 0.03237  -0.00046 185 TRP B CE3 
3359 C CZ2 . TRP B 188 ? 0.40847 0.45197 0.52279 -0.00541 0.02860  0.01211  185 TRP B CZ2 
3360 C CZ3 . TRP B 188 ? 0.40652 0.44932 0.49510 0.00179  0.03587  0.00559  185 TRP B CZ3 
3361 C CH2 . TRP B 188 ? 0.43121 0.47578 0.53372 -0.00082 0.03441  0.01198  185 TRP B CH2 
3362 N N   . PHE B 189 ? 0.39125 0.44155 0.48122 -0.00021 0.03307  -0.00278 186 PHE B N   
3363 C CA  . PHE B 189 ? 0.44244 0.49830 0.54274 -0.00010 0.03477  0.00269  186 PHE B CA  
3364 C C   . PHE B 189 ? 0.49032 0.54405 0.59428 -0.00441 0.02877  -0.00132 186 PHE B C   
3365 O O   . PHE B 189 ? 0.47973 0.53675 0.59664 -0.00640 0.02749  0.00359  186 PHE B O   
3366 C CB  . PHE B 189 ? 0.46385 0.52460 0.58012 -0.00080 0.03667  0.01250  186 PHE B CB  
3367 C CG  . PHE B 189 ? 0.54856 0.61154 0.66126 0.00364  0.04290  0.01738  186 PHE B CG  
3368 C CD1 . PHE B 189 ? 0.58345 0.64237 0.69380 0.00225  0.04084  0.01596  186 PHE B CD1 
3369 C CD2 . PHE B 189 ? 0.61981 0.68837 0.73056 0.00975  0.05086  0.02338  186 PHE B CD2 
3370 C CE1 . PHE B 189 ? 0.65518 0.71558 0.76170 0.00624  0.04618  0.02057  186 PHE B CE1 
3371 C CE2 . PHE B 189 ? 0.66507 0.73471 0.77060 0.01446  0.05663  0.02799  186 PHE B CE2 
3372 C CZ  . PHE B 189 ? 0.68918 0.75472 0.79273 0.01239  0.05407  0.02662  186 PHE B CZ  
3373 N N   . GLY B 190 ? 0.44353 0.49184 0.53668 -0.00574 0.02501  -0.00958 187 GLY B N   
3374 C CA  . GLY B 190 ? 0.37585 0.42115 0.46969 -0.00931 0.01940  -0.01382 187 GLY B CA  
3375 C C   . GLY B 190 ? 0.38342 0.42294 0.48277 -0.01360 0.01267  -0.01514 187 GLY B C   
3376 O O   . GLY B 190 ? 0.36898 0.40407 0.46602 -0.01610 0.00747  -0.01943 187 GLY B O   
3377 N N   . SER B 191 ? 0.40393 0.44237 0.50944 -0.01421 0.01212  -0.01174 188 SER B N   
3378 C CA  . SER B 191 ? 0.44147 0.47314 0.55303 -0.01792 0.00457  -0.01241 188 SER B CA  
3379 C C   . SER B 191 ? 0.41581 0.43917 0.51451 -0.01795 0.00090  -0.02091 188 SER B C   
3380 O O   . SER B 191 ? 0.40427 0.41974 0.50398 -0.02021 -0.00623 -0.02327 188 SER B O   
3381 C CB  . SER B 191 ? 0.46380 0.49697 0.58687 -0.01849 0.00473  -0.00553 188 SER B CB  
3382 O OG  . SER B 191 ? 0.40402 0.43721 0.51917 -0.01583 0.00882  -0.00709 188 SER B OG  
3383 N N   . VAL B 192 ? 0.36448 0.38894 0.45122 -0.01509 0.00532  -0.02515 189 VAL B N   
3384 C CA  . VAL B 192 ? 0.36924 0.38731 0.44478 -0.01441 0.00309  -0.03214 189 VAL B CA  
3385 C C   . VAL B 192 ? 0.40539 0.41981 0.47477 -0.01540 -0.00043 -0.03676 189 VAL B C   
3386 O O   . VAL B 192 ? 0.38986 0.39810 0.45034 -0.01454 -0.00274 -0.04195 189 VAL B O   
3387 C CB  . VAL B 192 ? 0.33688 0.35789 0.40365 -0.01131 0.00845  -0.03412 189 VAL B CB  
3388 C CG1 . VAL B 192 ? 0.32783 0.35042 0.39853 -0.01016 0.01112  -0.03036 189 VAL B CG1 
3389 C CG2 . VAL B 192 ? 0.31034 0.33702 0.37378 -0.01001 0.01209  -0.03363 189 VAL B CG2 
3390 N N   . ALA B 193 ? 0.39062 0.40863 0.46426 -0.01677 -0.00067 -0.03472 190 ALA B N   
3391 C CA  . ALA B 193 ? 0.43666 0.45188 0.50415 -0.01774 -0.00370 -0.03872 190 ALA B CA  
3392 C C   . ALA B 193 ? 0.49045 0.49610 0.55791 -0.01992 -0.01161 -0.04091 190 ALA B C   
3393 O O   . ALA B 193 ? 0.53477 0.53624 0.59450 -0.02025 -0.01452 -0.04485 190 ALA B O   
3394 C CB  . ALA B 193 ? 0.38764 0.40934 0.46052 -0.01848 -0.00194 -0.03564 190 ALA B CB  
3395 N N   . TYR B 194 ? 0.46649 0.46777 0.54192 -0.02129 -0.01578 -0.03830 191 TYR B N   
3396 C CA  . TYR B 194 ? 0.50491 0.49494 0.58009 -0.02318 -0.02505 -0.04029 191 TYR B CA  
3397 C C   . TYR B 194 ? 0.55730 0.53925 0.62819 -0.02154 -0.02784 -0.04281 191 TYR B C   
3398 O O   . TYR B 194 ? 0.55842 0.54488 0.63474 -0.02082 -0.02405 -0.03980 191 TYR B O   
3399 C CB  . TYR B 194 ? 0.52018 0.51096 0.61220 -0.02710 -0.03030 -0.03369 191 TYR B CB  
3400 C CG  . TYR B 194 ? 0.54549 0.54628 0.64481 -0.02809 -0.02603 -0.02963 191 TYR B CG  
3401 C CD1 . TYR B 194 ? 0.54565 0.55776 0.65390 -0.02693 -0.01836 -0.02360 191 TYR B CD1 
3402 C CD2 . TYR B 194 ? 0.59487 0.59314 0.69113 -0.02962 -0.02969 -0.03188 191 TYR B CD2 
3403 C CE1 . TYR B 194 ? 0.56627 0.58672 0.67991 -0.02674 -0.01426 -0.02016 191 TYR B CE1 
3404 C CE2 . TYR B 194 ? 0.59658 0.60374 0.69966 -0.03020 -0.02596 -0.02832 191 TYR B CE2 
3405 C CZ  . TYR B 194 ? 0.61260 0.63072 0.72422 -0.02849 -0.01816 -0.02258 191 TYR B CZ  
3406 O OH  . TYR B 194 ? 0.63868 0.66484 0.75586 -0.02802 -0.01427 -0.01929 191 TYR B OH  
3407 N N   . PRO B 195 ? 0.59060 0.56005 0.65074 -0.02041 -0.03444 -0.04842 192 PRO B N   
3408 C CA  . PRO B 195 ? 0.62074 0.58108 0.67666 -0.01830 -0.03796 -0.05100 192 PRO B CA  
3409 C C   . PRO B 195 ? 0.60407 0.56231 0.67573 -0.02147 -0.04392 -0.04530 192 PRO B C   
3410 O O   . PRO B 195 ? 0.60021 0.55842 0.67456 -0.02037 -0.04275 -0.04430 192 PRO B O   
3411 C CB  . PRO B 195 ? 0.65916 0.60512 0.69942 -0.01595 -0.04472 -0.05785 192 PRO B CB  
3412 C CG  . PRO B 195 ? 0.62840 0.57906 0.66193 -0.01592 -0.04114 -0.05944 192 PRO B CG  
3413 C CD  . PRO B 195 ? 0.60266 0.56511 0.65204 -0.02017 -0.03858 -0.05296 192 PRO B CD  
3414 N N   . GLU B 196 ? 0.56957 0.52632 0.65295 -0.02552 -0.05056 -0.04090 193 GLU B N   
3415 C CA  . GLU B 196 ? 0.62969 0.58607 0.73162 -0.02912 -0.05646 -0.03349 193 GLU B CA  
3416 C C   . GLU B 196 ? 0.57659 0.54748 0.69551 -0.03189 -0.05089 -0.02470 193 GLU B C   
3417 O O   . GLU B 196 ? 0.58362 0.55886 0.70177 -0.03258 -0.04881 -0.02476 193 GLU B O   
3418 C CB  . GLU B 196 ? 0.71164 0.65226 0.81513 -0.03143 -0.07091 -0.03458 193 GLU B CB  
3419 C CG  . GLU B 196 ? 0.82960 0.75394 0.91799 -0.02800 -0.07778 -0.04210 193 GLU B CG  
3420 C CD  . GLU B 196 ? 0.96371 0.87019 1.05210 -0.02987 -0.09355 -0.04341 193 GLU B CD  
3421 O OE1 . GLU B 196 ? 1.02051 0.91350 1.08946 -0.02653 -0.09827 -0.05150 193 GLU B OE1 
3422 O OE2 . GLU B 196 ? 1.00220 0.90776 1.11008 -0.03448 -0.10151 -0.03589 193 GLU B OE2 
3423 N N   . TYR B 197 ? 0.54879 0.52706 0.68275 -0.03301 -0.04826 -0.01688 194 TYR B N   
3424 C CA  . TYR B 197 ? 0.51047 0.50297 0.66000 -0.03422 -0.04147 -0.00766 194 TYR B CA  
3425 C C   . TYR B 197 ? 0.46591 0.45922 0.63702 -0.03760 -0.04707 0.00230  194 TYR B C   
3426 O O   . TYR B 197 ? 0.49115 0.48009 0.66378 -0.03753 -0.04989 0.00279  194 TYR B O   
3427 C CB  . TYR B 197 ? 0.47970 0.48330 0.62302 -0.03046 -0.02883 -0.00747 194 TYR B CB  
3428 C CG  . TYR B 197 ? 0.43458 0.45119 0.58635 -0.02976 -0.02073 -0.00079 194 TYR B CG  
3429 C CD1 . TYR B 197 ? 0.38734 0.41300 0.55571 -0.02996 -0.01679 0.00977  194 TYR B CD1 
3430 C CD2 . TYR B 197 ? 0.38098 0.40068 0.52384 -0.02835 -0.01689 -0.00475 194 TYR B CD2 
3431 C CE1 . TYR B 197 ? 0.35322 0.39027 0.52778 -0.02799 -0.00865 0.01589  194 TYR B CE1 
3432 C CE2 . TYR B 197 ? 0.36776 0.39828 0.51710 -0.02686 -0.00971 0.00086  194 TYR B CE2 
3433 C CZ  . TYR B 197 ? 0.38276 0.42173 0.54734 -0.02630 -0.00533 0.01104  194 TYR B CZ  
3434 O OH  . TYR B 197 ? 0.44616 0.49546 0.61597 -0.02358 0.00250  0.01677  194 TYR B OH  
3435 N N   . PRO B 198 ? 0.43821 0.43748 0.62733 -0.04052 -0.04874 0.01096  195 PRO B N   
3436 C CA  . PRO B 198 ? 0.45073 0.44964 0.66268 -0.04440 -0.05621 0.02131  195 PRO B CA  
3437 C C   . PRO B 198 ? 0.46398 0.47668 0.68965 -0.04320 -0.04686 0.03170  195 PRO B C   
3438 O O   . PRO B 198 ? 0.46989 0.49457 0.69211 -0.03966 -0.03443 0.03359  195 PRO B O   
3439 C CB  . PRO B 198 ? 0.47585 0.47590 0.70183 -0.04784 -0.06163 0.02662  195 PRO B CB  
3440 C CG  . PRO B 198 ? 0.40828 0.41146 0.61849 -0.04528 -0.05484 0.01942  195 PRO B CG  
3441 C CD  . PRO B 198 ? 0.42509 0.43171 0.61593 -0.04046 -0.04437 0.01229  195 PRO B CD  
3442 N N   . GLY B 199 ? 0.44857 0.45840 0.68885 -0.04584 -0.05355 0.03835  196 GLY B N   
3443 C CA  . GLY B 199 ? 0.43338 0.45620 0.69426 -0.04612 -0.04762 0.05209  196 GLY B CA  
3444 C C   . GLY B 199 ? 0.42034 0.45318 0.67262 -0.04131 -0.03387 0.05285  196 GLY B C   
3445 O O   . GLY B 199 ? 0.42630 0.47242 0.69192 -0.03979 -0.02522 0.06409  196 GLY B O   
3446 N N   . LEU B 200 ? 0.38542 0.41200 0.61603 -0.03854 -0.03172 0.04181  197 LEU B N   
3447 C CA  . LEU B 200 ? 0.38934 0.42368 0.61165 -0.03424 -0.02025 0.04249  197 LEU B CA  
3448 C C   . LEU B 200 ? 0.41034 0.44385 0.64258 -0.03556 -0.02300 0.04846  197 LEU B C   
3449 O O   . LEU B 200 ? 0.43818 0.46144 0.67647 -0.03915 -0.03467 0.04744  197 LEU B O   
3450 C CB  . LEU B 200 ? 0.44155 0.47042 0.63835 -0.03084 -0.01675 0.02919  197 LEU B CB  
3451 C CG  . LEU B 200 ? 0.40853 0.43899 0.59405 -0.02913 -0.01308 0.02324  197 LEU B CG  
3452 C CD1 . LEU B 200 ? 0.34539 0.37211 0.50847 -0.02574 -0.00907 0.01227  197 LEU B CD1 
3453 C CD2 . LEU B 200 ? 0.44030 0.48384 0.63405 -0.02690 -0.00373 0.03177  197 LEU B CD2 
3454 N N   . HIS B 201 ? 0.44345 0.48704 0.67667 -0.03233 -0.01258 0.05478  198 HIS B N   
3455 C CA  . HIS B 201 ? 0.45698 0.49959 0.69519 -0.03288 -0.01386 0.05882  198 HIS B CA  
3456 C C   . HIS B 201 ? 0.45940 0.48954 0.67958 -0.03248 -0.01897 0.04590  198 HIS B C   
3457 O O   . HIS B 201 ? 0.43440 0.46160 0.63541 -0.02968 -0.01545 0.03555  198 HIS B O   
3458 C CB  . HIS B 201 ? 0.48084 0.53534 0.71788 -0.02836 -0.00076 0.06623  198 HIS B CB  
3459 C CG  . HIS B 201 ? 0.58368 0.63781 0.82506 -0.02872 -0.00126 0.07078  198 HIS B CG  
3460 N ND1 . HIS B 201 ? 0.59661 0.64282 0.82207 -0.02759 -0.00254 0.06137  198 HIS B ND1 
3461 C CD2 . HIS B 201 ? 0.60715 0.66830 0.86777 -0.03004 -0.00051 0.08437  198 HIS B CD2 
3462 C CE1 . HIS B 201 ? 0.60250 0.65021 0.83659 -0.02837 -0.00304 0.06832  198 HIS B CE1 
3463 N NE2 . HIS B 201 ? 0.61671 0.67348 0.87196 -0.02990 -0.00181 0.08241  198 HIS B NE2 
3464 N N   . PRO B 202 ? 0.44303 0.46566 0.66956 -0.03502 -0.02747 0.04661  199 PRO B N   
3465 C CA  . PRO B 202 ? 0.41880 0.42909 0.62853 -0.03393 -0.03240 0.03440  199 PRO B CA  
3466 C C   . PRO B 202 ? 0.45496 0.46802 0.64533 -0.02928 -0.02238 0.02740  199 PRO B C   
3467 O O   . PRO B 202 ? 0.43819 0.44350 0.61219 -0.02747 -0.02382 0.01628  199 PRO B O   
3468 C CB  . PRO B 202 ? 0.39332 0.39875 0.61589 -0.03667 -0.04044 0.03964  199 PRO B CB  
3469 C CG  . PRO B 202 ? 0.40371 0.41334 0.65054 -0.04098 -0.04601 0.05193  199 PRO B CG  
3470 C CD  . PRO B 202 ? 0.39528 0.41939 0.64575 -0.03913 -0.03436 0.05864  199 PRO B CD  
3471 N N   . GLU B 203 ? 0.49560 0.51908 0.68724 -0.02698 -0.01249 0.03401  200 GLU B N   
3472 C CA  . GLU B 203 ? 0.53230 0.55713 0.70575 -0.02270 -0.00438 0.02766  200 GLU B CA  
3473 C C   . GLU B 203 ? 0.44247 0.46991 0.60382 -0.02025 0.00088  0.02215  200 GLU B C   
3474 O O   . GLU B 203 ? 0.43921 0.46372 0.58451 -0.01766 0.00355  0.01373  200 GLU B O   
3475 C CB  . GLU B 203 ? 0.61978 0.65283 0.79619 -0.02049 0.00358  0.03616  200 GLU B CB  
3476 C CG  . GLU B 203 ? 0.75947 0.78925 0.94462 -0.02254 -0.00126 0.04011  200 GLU B CG  
3477 C CD  . GLU B 203 ? 0.86724 0.88550 1.04245 -0.02293 -0.00806 0.02928  200 GLU B CD  
3478 O OE1 . GLU B 203 ? 0.86921 0.88578 1.02861 -0.01980 -0.00373 0.02193  200 GLU B OE1 
3479 O OE2 . GLU B 203 ? 0.89455 0.90500 1.07789 -0.02603 -0.01806 0.02837  200 GLU B OE2 
3480 N N   . GLU B 204 ? 0.43634 0.46940 0.60619 -0.02109 0.00215  0.02725  201 GLU B N   
3481 C CA  . GLU B 204 ? 0.40013 0.43481 0.55928 -0.01915 0.00583  0.02176  201 GLU B CA  
3482 C C   . GLU B 204 ? 0.36930 0.39418 0.51997 -0.02078 -0.00157 0.01148  201 GLU B C   
3483 O O   . GLU B 204 ? 0.36664 0.39066 0.50333 -0.01866 0.00130  0.00418  201 GLU B O   
3484 C CB  . GLU B 204 ? 0.40820 0.45131 0.57980 -0.01950 0.00880  0.03022  201 GLU B CB  
3485 C CG  . GLU B 204 ? 0.46709 0.52065 0.64219 -0.01568 0.01888  0.03965  201 GLU B CG  
3486 C CD  . GLU B 204 ? 0.52123 0.58371 0.71109 -0.01557 0.02207  0.04928  201 GLU B CD  
3487 O OE1 . GLU B 204 ? 0.50062 0.56232 0.70736 -0.02016 0.01479  0.05380  201 GLU B OE1 
3488 O OE2 . GLU B 204 ? 0.54128 0.61090 0.72576 -0.01060 0.03143  0.05237  201 GLU B OE2 
3489 N N   . GLU B 205 ? 0.35122 0.36811 0.50974 -0.02419 -0.01140 0.01109  202 GLU B N   
3490 C CA  . GLU B 205 ? 0.38820 0.39402 0.53644 -0.02469 -0.01861 0.00126  202 GLU B CA  
3491 C C   . GLU B 205 ? 0.39529 0.39541 0.52822 -0.02176 -0.01738 -0.00715 202 GLU B C   
3492 O O   . GLU B 205 ? 0.40178 0.39729 0.52099 -0.01990 -0.01743 -0.01549 202 GLU B O   
3493 C CB  . GLU B 205 ? 0.37601 0.37291 0.53589 -0.02852 -0.03060 0.00335  202 GLU B CB  
3494 C CG  . GLU B 205 ? 0.48409 0.46713 0.63130 -0.02813 -0.03893 -0.00686 202 GLU B CG  
3495 C CD  . GLU B 205 ? 0.55292 0.53626 0.69347 -0.02808 -0.03830 -0.01056 202 GLU B CD  
3496 O OE1 . GLU B 205 ? 0.57812 0.57224 0.72493 -0.02857 -0.03200 -0.00532 202 GLU B OE1 
3497 O OE2 . GLU B 205 ? 0.58052 0.55288 0.70892 -0.02712 -0.04411 -0.01866 202 GLU B OE2 
3498 N N   . VAL B 206 ? 0.38018 0.38090 0.51606 -0.02122 -0.01618 -0.00445 203 VAL B N   
3499 C CA  . VAL B 206 ? 0.38774 0.38423 0.51095 -0.01830 -0.01440 -0.01137 203 VAL B CA  
3500 C C   . VAL B 206 ? 0.39146 0.39411 0.50278 -0.01525 -0.00569 -0.01452 203 VAL B C   
3501 O O   . VAL B 206 ? 0.42334 0.42224 0.52255 -0.01299 -0.00499 -0.02198 203 VAL B O   
3502 C CB  . VAL B 206 ? 0.39261 0.38925 0.52288 -0.01867 -0.01486 -0.00678 203 VAL B CB  
3503 C CG1 . VAL B 206 ? 0.43067 0.42534 0.54896 -0.01542 -0.01123 -0.01260 203 VAL B CG1 
3504 C CG2 . VAL B 206 ? 0.37113 0.35889 0.51136 -0.02144 -0.02548 -0.00543 203 VAL B CG2 
3505 N N   . ALA B 207 ? 0.35846 0.37034 0.47316 -0.01475 0.00085  -0.00844 204 ALA B N   
3506 C CA  . ALA B 207 ? 0.35028 0.36670 0.45371 -0.01177 0.00772  -0.01114 204 ALA B CA  
3507 C C   . ALA B 207 ? 0.38557 0.40077 0.48217 -0.01173 0.00681  -0.01672 204 ALA B C   
3508 O O   . ALA B 207 ? 0.38542 0.40021 0.47098 -0.00964 0.00923  -0.02209 204 ALA B O   
3509 C CB  . ALA B 207 ? 0.33386 0.35871 0.44104 -0.01036 0.01425  -0.00346 204 ALA B CB  
3510 N N   . ARG B 208 ? 0.36517 0.37977 0.46908 -0.01420 0.00290  -0.01494 205 ARG B N   
3511 C CA  . ARG B 208 ? 0.37507 0.38818 0.47272 -0.01439 0.00158  -0.01984 205 ARG B CA  
3512 C C   . ARG B 208 ? 0.38058 0.38538 0.46732 -0.01334 -0.00199 -0.02816 205 ARG B C   
3513 O O   . ARG B 208 ? 0.37671 0.38221 0.45327 -0.01155 0.00065  -0.03286 205 ARG B O   
3514 C CB  . ARG B 208 ? 0.37745 0.39029 0.48629 -0.01756 -0.00324 -0.01587 205 ARG B CB  
3515 C CG  . ARG B 208 ? 0.39663 0.40829 0.49963 -0.01797 -0.00464 -0.02018 205 ARG B CG  
3516 C CD  . ARG B 208 ? 0.40005 0.41013 0.51503 -0.02145 -0.01079 -0.01616 205 ARG B CD  
3517 N NE  . ARG B 208 ? 0.40842 0.40700 0.52408 -0.02335 -0.02050 -0.01911 205 ARG B NE  
3518 C CZ  . ARG B 208 ? 0.40594 0.39534 0.51070 -0.02303 -0.02570 -0.02641 205 ARG B CZ  
3519 N NH1 . ARG B 208 ? 0.39324 0.38497 0.48743 -0.02153 -0.02187 -0.03081 205 ARG B NH1 
3520 N NH2 . ARG B 208 ? 0.44767 0.42493 0.55147 -0.02387 -0.03503 -0.02915 205 ARG B NH2 
3521 N N   . LEU B 209 ? 0.36886 0.36551 0.45769 -0.01403 -0.00815 -0.02966 206 LEU B N   
3522 C CA  . LEU B 209 ? 0.42190 0.41000 0.49923 -0.01167 -0.01085 -0.03731 206 LEU B CA  
3523 C C   . LEU B 209 ? 0.44593 0.43711 0.51556 -0.00847 -0.00475 -0.03976 206 LEU B C   
3524 O O   . LEU B 209 ? 0.50436 0.49313 0.56368 -0.00579 -0.00342 -0.04511 206 LEU B O   
3525 C CB  . LEU B 209 ? 0.42145 0.39907 0.50211 -0.01230 -0.01909 -0.03826 206 LEU B CB  
3526 C CG  . LEU B 209 ? 0.44669 0.41835 0.53507 -0.01559 -0.02774 -0.03619 206 LEU B CG  
3527 C CD1 . LEU B 209 ? 0.39855 0.35935 0.49146 -0.01622 -0.03681 -0.03627 206 LEU B CD1 
3528 C CD2 . LEU B 209 ? 0.45904 0.42523 0.53670 -0.01467 -0.03023 -0.04189 206 LEU B CD2 
3529 N N   . SER B 210 ? 0.39537 0.39185 0.47025 -0.00855 -0.00112 -0.03531 207 SER B N   
3530 C CA  . SER B 210 ? 0.38498 0.38405 0.45374 -0.00589 0.00378  -0.03692 207 SER B CA  
3531 C C   . SER B 210 ? 0.39796 0.40261 0.46017 -0.00475 0.00841  -0.03816 207 SER B C   
3532 O O   . SER B 210 ? 0.36954 0.37413 0.42496 -0.00248 0.01047  -0.04150 207 SER B O   
3533 C CB  . SER B 210 ? 0.38059 0.38307 0.45574 -0.00632 0.00588  -0.03152 207 SER B CB  
3534 O OG  . SER B 210 ? 0.52424 0.52810 0.59389 -0.00399 0.00943  -0.03292 207 SER B OG  
3535 N N   . PHE B 211 ? 0.35813 0.36769 0.42309 -0.00614 0.00984  -0.03504 208 PHE B N   
3536 C CA  . PHE B 211 ? 0.36241 0.37649 0.42128 -0.00503 0.01329  -0.03616 208 PHE B CA  
3537 C C   . PHE B 211 ? 0.34188 0.35352 0.39480 -0.00488 0.01153  -0.04105 208 PHE B C   
3538 O O   . PHE B 211 ? 0.36858 0.38238 0.41549 -0.00340 0.01373  -0.04310 208 PHE B O   
3539 C CB  . PHE B 211 ? 0.34631 0.36581 0.40918 -0.00569 0.01552  -0.03150 208 PHE B CB  
3540 C CG  . PHE B 211 ? 0.39421 0.41688 0.45745 -0.00395 0.01931  -0.02717 208 PHE B CG  
3541 C CD1 . PHE B 211 ? 0.39004 0.41287 0.44574 -0.00166 0.02134  -0.02871 208 PHE B CD1 
3542 C CD2 . PHE B 211 ? 0.38753 0.41260 0.45870 -0.00441 0.02051  -0.02103 208 PHE B CD2 
3543 C CE1 . PHE B 211 ? 0.38471 0.40857 0.43863 0.00038  0.02401  -0.02507 208 PHE B CE1 
3544 C CE2 . PHE B 211 ? 0.41895 0.44625 0.48847 -0.00204 0.02438  -0.01689 208 PHE B CE2 
3545 C CZ  . PHE B 211 ? 0.45775 0.48368 0.51755 0.00048  0.02588  -0.01935 208 PHE B CZ  
3546 N N   . ARG B 212 ? 0.35083 0.35752 0.40536 -0.00635 0.00706  -0.04253 209 ARG B N   
3547 C CA  . ARG B 212 ? 0.37007 0.37283 0.41692 -0.00555 0.00518  -0.04734 209 ARG B CA  
3548 C C   . ARG B 212 ? 0.43370 0.43369 0.47305 -0.00215 0.00685  -0.05102 209 ARG B C   
3549 O O   . ARG B 212 ? 0.42650 0.42818 0.45933 -0.00045 0.00907  -0.05316 209 ARG B O   
3550 C CB  . ARG B 212 ? 0.37369 0.36906 0.42256 -0.00734 -0.00131 -0.04838 209 ARG B CB  
3551 C CG  . ARG B 212 ? 0.36602 0.36480 0.42178 -0.01049 -0.00286 -0.04501 209 ARG B CG  
3552 C CD  . ARG B 212 ? 0.36566 0.35608 0.42449 -0.01265 -0.01076 -0.04560 209 ARG B CD  
3553 N NE  . ARG B 212 ? 0.39669 0.37846 0.44334 -0.01070 -0.01413 -0.05183 209 ARG B NE  
3554 C CZ  . ARG B 212 ? 0.42117 0.40321 0.46138 -0.01069 -0.01404 -0.05411 209 ARG B CZ  
3555 N NH1 . ARG B 212 ? 0.40736 0.39777 0.45265 -0.01272 -0.01118 -0.05109 209 ARG B NH1 
3556 N NH2 . ARG B 212 ? 0.44512 0.41864 0.47304 -0.00816 -0.01674 -0.05936 209 ARG B NH2 
3557 N N   . ASN B 213 ? 0.42218 0.41842 0.46330 -0.00097 0.00599  -0.05116 210 ASN B N   
3558 C CA  . ASN B 213 ? 0.41225 0.40655 0.44765 0.00281  0.00824  -0.05393 210 ASN B CA  
3559 C C   . ASN B 213 ? 0.43089 0.43297 0.46688 0.00364  0.01337  -0.05179 210 ASN B C   
3560 O O   . ASN B 213 ? 0.45011 0.45378 0.48150 0.00627  0.01608  -0.05318 210 ASN B O   
3561 C CB  . ASN B 213 ? 0.41927 0.40756 0.45740 0.00378  0.00560  -0.05435 210 ASN B CB  
3562 C CG  . ASN B 213 ? 0.54647 0.52438 0.58216 0.00392  -0.00101 -0.05734 210 ASN B CG  
3563 O OD1 . ASN B 213 ? 0.59252 0.56582 0.62018 0.00539  -0.00270 -0.06083 210 ASN B OD1 
3564 N ND2 . ASN B 213 ? 0.52702 0.50045 0.56945 0.00241  -0.00546 -0.05573 210 ASN B ND2 
3565 N N   . LEU B 214 ? 0.40583 0.41235 0.44738 0.00174  0.01447  -0.04794 211 LEU B N   
3566 C CA  . LEU B 214 ? 0.40811 0.41983 0.44953 0.00258  0.01765  -0.04596 211 LEU B CA  
3567 C C   . LEU B 214 ? 0.42009 0.43586 0.45797 0.00254  0.01883  -0.04635 211 LEU B C   
3568 O O   . LEU B 214 ? 0.37889 0.39734 0.41562 0.00405  0.02051  -0.04598 211 LEU B O   
3569 C CB  . LEU B 214 ? 0.40507 0.41890 0.45053 0.00128  0.01809  -0.04199 211 LEU B CB  
3570 C CG  . LEU B 214 ? 0.39940 0.41644 0.44320 0.00225  0.01977  -0.04004 211 LEU B CG  
3571 C CD1 . LEU B 214 ? 0.40122 0.41685 0.44644 0.00380  0.02006  -0.03981 211 LEU B CD1 
3572 C CD2 . LEU B 214 ? 0.40588 0.42430 0.44987 0.00180  0.02036  -0.03656 211 LEU B CD2 
3573 N N   . ASN B 215 ? 0.39717 0.41364 0.43454 0.00068  0.01762  -0.04652 212 ASN B N   
3574 C CA  . ASN B 215 ? 0.39228 0.41231 0.42661 0.00042  0.01815  -0.04687 212 ASN B CA  
3575 C C   . ASN B 215 ? 0.37418 0.39350 0.40406 0.00226  0.01889  -0.04928 212 ASN B C   
3576 O O   . ASN B 215 ? 0.35485 0.37819 0.38389 0.00301  0.02030  -0.04824 212 ASN B O   
3577 C CB  . ASN B 215 ? 0.40044 0.42089 0.43570 -0.00181 0.01651  -0.04664 212 ASN B CB  
3578 C CG  . ASN B 215 ? 0.44367 0.46615 0.48315 -0.00259 0.01716  -0.04318 212 ASN B CG  
3579 O OD1 . ASN B 215 ? 0.42429 0.44781 0.46382 -0.00135 0.01869  -0.04124 212 ASN B OD1 
3580 N ND2 . ASN B 215 ? 0.39071 0.41359 0.43368 -0.00428 0.01605  -0.04194 212 ASN B ND2 
3581 N N   . THR B 216 ? 0.37846 0.39223 0.40525 0.00342  0.01773  -0.05212 213 THR B N   
3582 C CA  . THR B 216 ? 0.39531 0.40757 0.41586 0.00657  0.01928  -0.05426 213 THR B CA  
3583 C C   . THR B 216 ? 0.38010 0.39527 0.40232 0.00960  0.02286  -0.05266 213 THR B C   
3584 O O   . THR B 216 ? 0.37932 0.39841 0.40007 0.01166  0.02568  -0.05145 213 THR B O   
3585 C CB  . THR B 216 ? 0.41283 0.41606 0.42766 0.00807  0.01638  -0.05808 213 THR B CB  
3586 O OG1 . THR B 216 ? 0.39948 0.40024 0.41336 0.00515  0.01255  -0.05903 213 THR B OG1 
3587 C CG2 . THR B 216 ? 0.34692 0.34741 0.35309 0.01310  0.01894  -0.06029 213 THR B CG2 
3588 N N   . PHE B 217 ? 0.39722 0.41097 0.42368 0.00980  0.02272  -0.05188 214 PHE B N   
3589 C CA  . PHE B 217 ? 0.37076 0.38689 0.40009 0.01260  0.02565  -0.05008 214 PHE B CA  
3590 C C   . PHE B 217 ? 0.44735 0.47056 0.48155 0.01135  0.02667  -0.04602 214 PHE B C   
3591 O O   . PHE B 217 ? 0.41740 0.44466 0.45349 0.01360  0.02927  -0.04379 214 PHE B O   
3592 C CB  . PHE B 217 ? 0.34969 0.36214 0.38270 0.01263  0.02445  -0.05012 214 PHE B CB  
3593 C CG  . PHE B 217 ? 0.43776 0.45228 0.47477 0.01538  0.02702  -0.04812 214 PHE B CG  
3594 C CD1 . PHE B 217 ? 0.44594 0.45747 0.48015 0.02008  0.02927  -0.04996 214 PHE B CD1 
3595 C CD2 . PHE B 217 ? 0.45102 0.46977 0.49422 0.01374  0.02689  -0.04429 214 PHE B CD2 
3596 C CE1 . PHE B 217 ? 0.44598 0.46008 0.48536 0.02284  0.03196  -0.04750 214 PHE B CE1 
3597 C CE2 . PHE B 217 ? 0.42922 0.44976 0.47757 0.01595  0.02857  -0.04190 214 PHE B CE2 
3598 C CZ  . PHE B 217 ? 0.44594 0.46487 0.49332 0.02038  0.03142  -0.04325 214 PHE B CZ  
3599 N N   . LEU B 218 ? 0.41820 0.44257 0.45456 0.00815  0.02436  -0.04460 215 LEU B N   
3600 C CA  . LEU B 218 ? 0.40354 0.43225 0.44322 0.00723  0.02364  -0.04116 215 LEU B CA  
3601 C C   . LEU B 218 ? 0.41709 0.45005 0.45598 0.00730  0.02417  -0.04021 215 LEU B C   
3602 O O   . LEU B 218 ? 0.40385 0.44077 0.44724 0.00770  0.02406  -0.03667 215 LEU B O   
3603 C CB  . LEU B 218 ? 0.35398 0.38150 0.39304 0.00498  0.02114  -0.04048 215 LEU B CB  
3604 C CG  . LEU B 218 ? 0.34951 0.37374 0.38996 0.00492  0.02070  -0.03983 215 LEU B CG  
3605 C CD1 . LEU B 218 ? 0.33832 0.36185 0.37658 0.00392  0.01924  -0.03841 215 LEU B CD1 
3606 C CD2 . LEU B 218 ? 0.34303 0.36713 0.38744 0.00631  0.02078  -0.03779 215 LEU B CD2 
3607 N N   . ALA B 219 ? 0.39413 0.42618 0.42811 0.00673  0.02420  -0.04282 216 ALA B N   
3608 C CA  . ALA B 219 ? 0.37924 0.41520 0.41204 0.00669  0.02464  -0.04177 216 ALA B CA  
3609 C C   . ALA B 219 ? 0.34215 0.38111 0.37598 0.01017  0.02845  -0.03980 216 ALA B C   
3610 O O   . ALA B 219 ? 0.37194 0.41609 0.40803 0.01035  0.02920  -0.03658 216 ALA B O   
3611 C CB  . ALA B 219 ? 0.30471 0.33799 0.33159 0.00545  0.02354  -0.04511 216 ALA B CB  
3612 N N   . ALA B 220 ? 0.34296 0.37891 0.37562 0.01331  0.03098  -0.04115 217 ALA B N   
3613 C CA  . ALA B 220 ? 0.43256 0.47107 0.46553 0.01796  0.03569  -0.03915 217 ALA B CA  
3614 C C   . ALA B 220 ? 0.44257 0.48447 0.48474 0.01930  0.03711  -0.03501 217 ALA B C   
3615 O O   . ALA B 220 ? 0.43067 0.47591 0.47523 0.02359  0.04166  -0.03219 217 ALA B O   
3616 C CB  . ALA B 220 ? 0.43500 0.46639 0.45845 0.02187  0.03748  -0.04395 217 ALA B CB  
3617 N N   . ASP B 221 ? 0.40805 0.44905 0.45530 0.01613  0.03341  -0.03417 218 ASP B N   
3618 C CA  . ASP B 221 ? 0.37688 0.41942 0.43257 0.01689  0.03343  -0.03059 218 ASP B CA  
3619 C C   . ASP B 221 ? 0.41364 0.46310 0.47872 0.01624  0.03267  -0.02403 218 ASP B C   
3620 O O   . ASP B 221 ? 0.42637 0.47631 0.49301 0.01278  0.02799  -0.02258 218 ASP B O   
3621 C CB  . ASP B 221 ? 0.38918 0.42694 0.44498 0.01394  0.02925  -0.03210 218 ASP B CB  
3622 C CG  . ASP B 221 ? 0.45734 0.49472 0.52032 0.01487  0.02887  -0.02934 218 ASP B CG  
3623 O OD1 . ASP B 221 ? 0.44795 0.48976 0.51812 0.01728  0.03128  -0.02531 218 ASP B OD1 
3624 O OD2 . ASP B 221 ? 0.44855 0.48138 0.51048 0.01327  0.02625  -0.03068 218 ASP B OD2 
3625 N N   . PRO B 222 ? 0.39440 0.44908 0.46639 0.01979  0.03688  -0.01949 219 PRO B N   
3626 C CA  . PRO B 222 ? 0.38732 0.44933 0.47099 0.01892  0.03567  -0.01177 219 PRO B CA  
3627 C C   . PRO B 222 ? 0.39436 0.45514 0.48727 0.01615  0.02979  -0.00819 219 PRO B C   
3628 O O   . PRO B 222 ? 0.43148 0.49657 0.53439 0.01444  0.02625  -0.00182 219 PRO B O   
3629 C CB  . PRO B 222 ? 0.36236 0.43046 0.45084 0.02450  0.04315  -0.00756 219 PRO B CB  
3630 C CG  . PRO B 222 ? 0.38119 0.44344 0.46340 0.02801  0.04630  -0.01271 219 PRO B CG  
3631 C CD  . PRO B 222 ? 0.39668 0.45062 0.46647 0.02524  0.04286  -0.02074 219 PRO B CD  
3632 N N   . ARG B 223 ? 0.36812 0.42259 0.45810 0.01563  0.02798  -0.01169 220 ARG B N   
3633 C CA  . ARG B 223 ? 0.33935 0.39104 0.43601 0.01327  0.02181  -0.00859 220 ARG B CA  
3634 C C   . ARG B 223 ? 0.36798 0.41539 0.45993 0.00955  0.01469  -0.00957 220 ARG B C   
3635 O O   . ARG B 223 ? 0.37344 0.41768 0.47001 0.00787  0.00823  -0.00636 220 ARG B O   
3636 C CB  . ARG B 223 ? 0.28363 0.32964 0.37778 0.01407  0.02219  -0.01182 220 ARG B CB  
3637 C CG  . ARG B 223 ? 0.34644 0.39548 0.44625 0.01826  0.02812  -0.01047 220 ARG B CG  
3638 C CD  . ARG B 223 ? 0.40373 0.44633 0.49905 0.01892  0.02832  -0.01493 220 ARG B CD  
3639 N NE  . ARG B 223 ? 0.44034 0.47836 0.52343 0.01861  0.02940  -0.02166 220 ARG B NE  
3640 C CZ  . ARG B 223 ? 0.47364 0.50612 0.55228 0.01916  0.02961  -0.02576 220 ARG B CZ  
3641 N NH1 . ARG B 223 ? 0.46573 0.49644 0.55011 0.02021  0.02920  -0.02437 220 ARG B NH1 
3642 N NH2 . ARG B 223 ? 0.44214 0.47077 0.51165 0.01847  0.02970  -0.03078 220 ARG B NH2 
3643 N N   . VAL B 224 ? 0.36778 0.41417 0.45019 0.00863  0.01530  -0.01392 221 VAL B N   
3644 C CA  . VAL B 224 ? 0.35060 0.39216 0.42670 0.00612  0.00936  -0.01567 221 VAL B CA  
3645 C C   . VAL B 224 ? 0.35419 0.39908 0.42749 0.00513  0.00942  -0.01626 221 VAL B C   
3646 O O   . VAL B 224 ? 0.34058 0.38996 0.41294 0.00630  0.01471  -0.01720 221 VAL B O   
3647 C CB  . VAL B 224 ? 0.37940 0.41438 0.44533 0.00597  0.00958  -0.02106 221 VAL B CB  
3648 C CG1 . VAL B 224 ? 0.35477 0.38533 0.42276 0.00646  0.00788  -0.02003 221 VAL B CG1 
3649 C CG2 . VAL B 224 ? 0.33924 0.37544 0.39994 0.00692  0.01547  -0.02552 221 VAL B CG2 
3650 N N   . GLU B 225 ? 0.37368 0.41537 0.44481 0.00330  0.00297  -0.01575 222 GLU B N   
3651 C CA  . GLU B 225 ? 0.43158 0.47371 0.49690 0.00215  0.00195  -0.01807 222 GLU B CA  
3652 C C   . GLU B 225 ? 0.41402 0.45003 0.46827 0.00227  0.00184  -0.02350 222 GLU B C   
3653 O O   . GLU B 225 ? 0.39068 0.42109 0.44176 0.00298  -0.00008 -0.02415 222 GLU B O   
3654 C CB  . GLU B 225 ? 0.48018 0.52189 0.54991 0.00056  -0.00565 -0.01408 222 GLU B CB  
3655 C CG  . GLU B 225 ? 0.61789 0.66737 0.70050 0.00006  -0.00559 -0.00728 222 GLU B CG  
3656 C CD  . GLU B 225 ? 0.72044 0.76759 0.81041 -0.00174 -0.01540 -0.00197 222 GLU B CD  
3657 O OE1 . GLU B 225 ? 0.76141 0.79935 0.84496 -0.00191 -0.02240 -0.00413 222 GLU B OE1 
3658 O OE2 . GLU B 225 ? 0.74663 0.80070 0.84869 -0.00266 -0.01639 0.00474  222 GLU B OE2 
3659 N N   . ILE B 226 ? 0.40682 0.44405 0.45563 0.00174  0.00401  -0.02679 223 ILE B N   
3660 C CA  . ILE B 226 ? 0.41598 0.44903 0.45654 0.00205  0.00506  -0.03087 223 ILE B CA  
3661 C C   . ILE B 226 ? 0.41799 0.45036 0.45388 0.00136  0.00248  -0.03234 223 ILE B C   
3662 O O   . ILE B 226 ? 0.40736 0.44309 0.44589 0.00017  0.00081  -0.03115 223 ILE B O   
3663 C CB  . ILE B 226 ? 0.38365 0.41793 0.42288 0.00231  0.01079  -0.03377 223 ILE B CB  
3664 C CG1 . ILE B 226 ? 0.38461 0.42261 0.42325 0.00152  0.01288  -0.03517 223 ILE B CG1 
3665 C CG2 . ILE B 226 ? 0.33522 0.36986 0.37883 0.00350  0.01333  -0.03265 223 ILE B CG2 
3666 C CD1 . ILE B 226 ? 0.37729 0.41378 0.41257 0.00160  0.01619  -0.03867 223 ILE B CD1 
3667 N N   . SER B 227 ? 0.38753 0.41567 0.41671 0.00243  0.00243  -0.03448 224 SER B N   
3668 C CA  . SER B 227 ? 0.41428 0.44192 0.43876 0.00244  0.00152  -0.03632 224 SER B CA  
3669 C C   . SER B 227 ? 0.38584 0.41190 0.40629 0.00365  0.00536  -0.03798 224 SER B C   
3670 O O   . SER B 227 ? 0.36671 0.38854 0.38306 0.00590  0.00526  -0.03732 224 SER B O   
3671 C CB  . SER B 227 ? 0.40878 0.43170 0.42928 0.00373  -0.00492 -0.03547 224 SER B CB  
3672 O OG  . SER B 227 ? 0.39480 0.41649 0.40976 0.00474  -0.00513 -0.03750 224 SER B OG  
3673 N N   . GLN B 228 ? 0.29488 0.32411 0.31684 0.00224  0.00845  -0.03952 225 GLN B N   
3674 C CA  . GLN B 228 ? 0.33204 0.36075 0.35282 0.00300  0.01161  -0.03985 225 GLN B CA  
3675 C C   . GLN B 228 ? 0.34344 0.37137 0.36013 0.00455  0.01054  -0.04000 225 GLN B C   
3676 O O   . GLN B 228 ? 0.34618 0.37603 0.36360 0.00314  0.00880  -0.04108 225 GLN B O   
3677 C CB  . GLN B 228 ? 0.34928 0.38049 0.37445 0.00072  0.01410  -0.04102 225 GLN B CB  
3678 C CG  . GLN B 228 ? 0.37342 0.40451 0.40047 0.00095  0.01666  -0.04004 225 GLN B CG  
3679 C CD  . GLN B 228 ? 0.41605 0.44715 0.44763 -0.00114 0.01745  -0.04093 225 GLN B CD  
3680 O OE1 . GLN B 228 ? 0.45790 0.48923 0.48965 -0.00274 0.01625  -0.04302 225 GLN B OE1 
3681 N NE2 . GLN B 228 ? 0.39587 0.42589 0.43047 -0.00085 0.01900  -0.03922 225 GLN B NE2 
3682 N N   . VAL B 229 ? 0.34645 0.37128 0.35827 0.00793  0.01168  -0.03875 226 VAL B N   
3683 C CA  . VAL B 229 ? 0.33835 0.36116 0.34425 0.01109  0.01087  -0.03880 226 VAL B CA  
3684 C C   . VAL B 229 ? 0.38814 0.41371 0.39619 0.01243  0.01612  -0.03698 226 VAL B C   
3685 O O   . VAL B 229 ? 0.38169 0.40707 0.39028 0.01382  0.01959  -0.03466 226 VAL B O   
3686 C CB  . VAL B 229 ? 0.34439 0.36000 0.34079 0.01537  0.00764  -0.03845 226 VAL B CB  
3687 C CG1 . VAL B 229 ? 0.36872 0.38084 0.35723 0.01952  0.00614  -0.03916 226 VAL B CG1 
3688 C CG2 . VAL B 229 ? 0.35759 0.37094 0.35517 0.01337  0.00187  -0.03889 226 VAL B CG2 
3689 N N   . SER B 230 ? 0.36630 0.39472 0.37668 0.01195  0.01651  -0.03735 227 SER B N   
3690 C CA  . SER B 230 ? 0.36558 0.39776 0.38106 0.01275  0.02118  -0.03458 227 SER B CA  
3691 C C   . SER B 230 ? 0.38752 0.41755 0.39579 0.01928  0.02443  -0.03210 227 SER B C   
3692 O O   . SER B 230 ? 0.40490 0.43670 0.41324 0.02189  0.02635  -0.03094 227 SER B O   
3693 C CB  . SER B 230 ? 0.31893 0.35471 0.34040 0.00967  0.01989  -0.03562 227 SER B CB  
3694 O OG  . SER B 230 ? 0.36079 0.39469 0.37643 0.01175  0.01704  -0.03745 227 SER B OG  
3695 N N   . ILE B 231 ? 0.40052 0.42626 0.40189 0.02243  0.02516  -0.03115 228 ILE B N   
3696 C CA  . ILE B 231 ? 0.39354 0.41585 0.38550 0.02962  0.02871  -0.02856 228 ILE B CA  
3697 C C   . ILE B 231 ? 0.42649 0.45164 0.42302 0.03016  0.03422  -0.02386 228 ILE B C   
3698 O O   . ILE B 231 ? 0.44405 0.46979 0.44588 0.02599  0.03306  -0.02404 228 ILE B O   
3699 C CB  . ILE B 231 ? 0.38684 0.39956 0.36447 0.03363  0.02366  -0.03127 228 ILE B CB  
3700 C CG1 . ILE B 231 ? 0.39967 0.40696 0.36412 0.04251  0.02706  -0.02921 228 ILE B CG1 
3701 C CG2 . ILE B 231 ? 0.35664 0.36653 0.33473 0.03071  0.02078  -0.03181 228 ILE B CG2 
3702 C CD1 . ILE B 231 ? 0.42024 0.41555 0.36864 0.04717  0.02035  -0.03236 228 ILE B CD1 
3703 N N   . GLY B 232 ? 0.42328 0.45047 0.41833 0.03556  0.04036  -0.01917 229 GLY B N   
3704 C CA  . GLY B 232 ? 0.44161 0.47265 0.44288 0.03604  0.04588  -0.01331 229 GLY B CA  
3705 C C   . GLY B 232 ? 0.42705 0.46532 0.44593 0.02888  0.04585  -0.01150 229 GLY B C   
3706 O O   . GLY B 232 ? 0.41653 0.46000 0.44459 0.02714  0.04673  -0.01006 229 GLY B O   
3707 N N   . ASP B 233 ? 0.44587 0.48356 0.46933 0.02488  0.04416  -0.01157 230 ASP B N   
3708 C CA  . ASP B 233 ? 0.45805 0.49956 0.49560 0.01823  0.04208  -0.01130 230 ASP B CA  
3709 C C   . ASP B 233 ? 0.45695 0.49487 0.49268 0.01373  0.03614  -0.01792 230 ASP B C   
3710 O O   . ASP B 233 ? 0.45250 0.49068 0.49565 0.00936  0.03395  -0.01863 230 ASP B O   
3711 C CB  . ASP B 233 ? 0.50369 0.54726 0.54897 0.01750  0.04469  -0.00574 230 ASP B CB  
3712 C CG  . ASP B 233 ? 0.58215 0.62940 0.64327 0.01172  0.04251  -0.00371 230 ASP B CG  
3713 O OD1 . ASP B 233 ? 0.57855 0.62844 0.64587 0.00971  0.04120  -0.00401 230 ASP B OD1 
3714 O OD2 . ASP B 233 ? 0.55146 0.59801 0.61852 0.00922  0.04129  -0.00195 230 ASP B OD2 
3715 N N   . GLY B 234 ? 0.42991 0.46420 0.45588 0.01517  0.03337  -0.02235 231 GLY B N   
3716 C CA  . GLY B 234 ? 0.39233 0.42405 0.41684 0.01177  0.02859  -0.02727 231 GLY B CA  
3717 C C   . GLY B 234 ? 0.39161 0.41885 0.41030 0.01306  0.02736  -0.02785 231 GLY B C   
3718 O O   . GLY B 234 ? 0.38907 0.41619 0.41057 0.01304  0.02927  -0.02530 231 GLY B O   
3719 N N   . VAL B 235 ? 0.37634 0.39971 0.38778 0.01404  0.02360  -0.03069 232 VAL B N   
3720 C CA  . VAL B 235 ? 0.40064 0.41938 0.40790 0.01470  0.02104  -0.03117 232 VAL B CA  
3721 C C   . VAL B 235 ? 0.38987 0.40914 0.40033 0.01137  0.01702  -0.03403 232 VAL B C   
3722 O O   . VAL B 235 ? 0.35489 0.37449 0.36382 0.01097  0.01433  -0.03570 232 VAL B O   
3723 C CB  . VAL B 235 ? 0.44368 0.45576 0.43885 0.01992  0.01934  -0.03061 232 VAL B CB  
3724 C CG1 . VAL B 235 ? 0.42327 0.42981 0.41532 0.01987  0.01503  -0.03105 232 VAL B CG1 
3725 C CG2 . VAL B 235 ? 0.45918 0.47102 0.45016 0.02437  0.02464  -0.02694 232 VAL B CG2 
3726 N N   . THR B 236 ? 0.37464 0.39426 0.38988 0.00930  0.01686  -0.03412 233 THR B N   
3727 C CA  . THR B 236 ? 0.36373 0.38443 0.38245 0.00710  0.01418  -0.03567 233 THR B CA  
3728 C C   . THR B 236 ? 0.36815 0.38445 0.38413 0.00849  0.01052  -0.03452 233 THR B C   
3729 O O   . THR B 236 ? 0.35554 0.36947 0.37183 0.00917  0.01107  -0.03322 233 THR B O   
3730 C CB  . THR B 236 ? 0.39848 0.42187 0.42390 0.00481  0.01634  -0.03648 233 THR B CB  
3731 O OG1 . THR B 236 ? 0.41818 0.44405 0.44591 0.00336  0.01813  -0.03748 233 THR B OG1 
3732 C CG2 . THR B 236 ? 0.42428 0.44932 0.45271 0.00376  0.01482  -0.03728 233 THR B CG2 
3733 N N   . ILE B 237 ? 0.37978 0.39454 0.39367 0.00874  0.00602  -0.03467 234 ILE B N   
3734 C CA  . ILE B 237 ? 0.38795 0.39799 0.40091 0.00951  0.00073  -0.03308 234 ILE B CA  
3735 C C   . ILE B 237 ? 0.39725 0.41184 0.42005 0.00695  0.00048  -0.03192 234 ILE B C   
3736 O O   . ILE B 237 ? 0.39319 0.41296 0.42042 0.00523  0.00128  -0.03231 234 ILE B O   
3737 C CB  . ILE B 237 ? 0.40941 0.41464 0.41615 0.01111  -0.00531 -0.03326 234 ILE B CB  
3738 C CG1 . ILE B 237 ? 0.39099 0.39220 0.38712 0.01481  -0.00377 -0.03450 234 ILE B CG1 
3739 C CG2 . ILE B 237 ? 0.40818 0.40674 0.41409 0.01185  -0.01243 -0.03122 234 ILE B CG2 
3740 C CD1 . ILE B 237 ? 0.40293 0.39963 0.39248 0.01674  -0.00928 -0.03559 234 ILE B CD1 
3741 N N   . CYS B 238 ? 0.34703 0.35978 0.37315 0.00711  -0.00029 -0.03013 235 CYS B N   
3742 C CA  . CYS B 238 ? 0.40119 0.41813 0.43715 0.00568  -0.00027 -0.02806 235 CYS B CA  
3743 C C   . CYS B 238 ? 0.44216 0.45490 0.48083 0.00584  -0.00722 -0.02464 235 CYS B C   
3744 O O   . CYS B 238 ? 0.48547 0.49056 0.51787 0.00733  -0.01112 -0.02435 235 CYS B O   
3745 C CB  . CYS B 238 ? 0.43215 0.45072 0.47189 0.00576  0.00447  -0.02846 235 CYS B CB  
3746 S SG  . CYS B 238 ? 0.42313 0.44493 0.46098 0.00531  0.01066  -0.03203 235 CYS B SG  
3747 N N   . ARG B 239 ? 0.40190 0.41930 0.45002 0.00448  -0.00907 -0.02151 236 ARG B N   
3748 C CA  . ARG B 239 ? 0.40447 0.41873 0.45886 0.00403  -0.01647 -0.01698 236 ARG B CA  
3749 C C   . ARG B 239 ? 0.39916 0.42010 0.46681 0.00346  -0.01337 -0.01304 236 ARG B C   
3750 O O   . ARG B 239 ? 0.38364 0.41285 0.45742 0.00317  -0.00835 -0.01205 236 ARG B O   
3751 C CB  . ARG B 239 ? 0.40995 0.42373 0.46559 0.00301  -0.02291 -0.01515 236 ARG B CB  
3752 C CG  . ARG B 239 ? 0.45358 0.46337 0.51726 0.00214  -0.03230 -0.00969 236 ARG B CG  
3753 C CD  . ARG B 239 ? 0.49508 0.50413 0.56083 0.00090  -0.03956 -0.00762 236 ARG B CD  
3754 N NE  . ARG B 239 ? 0.61356 0.61839 0.68898 -0.00032 -0.04986 -0.00153 236 ARG B NE  
3755 C CZ  . ARG B 239 ? 0.60174 0.61488 0.69483 -0.00239 -0.05033 0.00557  236 ARG B CZ  
3756 N NH1 . ARG B 239 ? 0.60498 0.63060 0.70574 -0.00273 -0.04045 0.00693  236 ARG B NH1 
3757 N NH2 . ARG B 239 ? 0.58664 0.59518 0.68966 -0.00375 -0.06091 0.01174  236 ARG B NH2 
3758 N N   . ARG B 240 ? 0.39002 0.40709 0.46157 0.00378  -0.01619 -0.01062 237 ARG B N   
3759 C CA  . ARG B 240 ? 0.39790 0.42118 0.48220 0.00394  -0.01256 -0.00683 237 ARG B CA  
3760 C C   . ARG B 240 ? 0.39289 0.42200 0.49111 0.00286  -0.01584 -0.00004 237 ARG B C   
3761 O O   . ARG B 240 ? 0.37297 0.39724 0.47437 0.00151  -0.02508 0.00353  237 ARG B O   
3762 C CB  . ARG B 240 ? 0.44014 0.45740 0.52544 0.00440  -0.01522 -0.00585 237 ARG B CB  
3763 C CG  . ARG B 240 ? 0.43948 0.46289 0.53933 0.00489  -0.01218 -0.00125 237 ARG B CG  
3764 C CD  . ARG B 240 ? 0.41529 0.43242 0.51687 0.00503  -0.01558 -0.00008 237 ARG B CD  
3765 N NE  . ARG B 240 ? 0.40843 0.43189 0.52545 0.00578  -0.01285 0.00494  237 ARG B NE  
3766 C CZ  . ARG B 240 ? 0.44108 0.46091 0.56383 0.00583  -0.01556 0.00729  237 ARG B CZ  
3767 N NH1 . ARG B 240 ? 0.42043 0.42983 0.53365 0.00510  -0.02126 0.00503  237 ARG B NH1 
3768 N NH2 . ARG B 240 ? 0.41855 0.44514 0.55634 0.00702  -0.01230 0.01221  237 ARG B NH2 
3769 N N   . LEU B 241 ? 0.39628 0.43535 0.50281 0.00381  -0.00851 0.00220  238 LEU B N   
3770 C CA  . LEU B 241 ? 0.45731 0.50412 0.57863 0.00323  -0.00980 0.00996  238 LEU B CA  
3771 C C   . LEU B 241 ? 0.50583 0.55615 0.64275 0.00400  -0.00986 0.01689  238 LEU B C   
3772 O O   . LEU B 241 ? 0.48344 0.53679 0.63459 0.00258  -0.01546 0.02491  238 LEU B O   
3773 C CB  . LEU B 241 ? 0.43862 0.49459 0.55974 0.00468  -0.00126 0.00955  238 LEU B CB  
3774 C CG  . LEU B 241 ? 0.44721 0.50064 0.55473 0.00373  -0.00107 0.00328  238 LEU B CG  
3775 C CD1 . LEU B 241 ? 0.41215 0.47373 0.51932 0.00523  0.00664  0.00330  238 LEU B CD1 
3776 C CD2 . LEU B 241 ? 0.48664 0.53540 0.59402 0.00104  -0.01105 0.00498  238 LEU B CD2 
3777 N N   . TYR B 242 ? 0.52102 0.57116 0.65680 0.00620  -0.00411 0.01451  239 TYR B N   
3778 C CA  . TYR B 242 ? 0.55091 0.60383 0.70140 0.00722  -0.00408 0.02075  239 TYR B CA  
3779 C C   . TYR B 242 ? 0.58392 0.63150 0.72792 0.00870  -0.00124 0.01569  239 TYR B C   
3780 O O   . TYR B 242 ? 0.57123 0.61872 0.72533 0.00931  -0.00229 0.01959  239 TYR B O   
3781 C CB  . TYR B 242 ? 0.48102 0.54648 0.64480 0.01014  0.00408  0.02716  239 TYR B CB  
3782 C CG  . TYR B 242 ? 0.43227 0.50153 0.58600 0.01407  0.01521  0.02152  239 TYR B CG  
3783 C CD1 . TYR B 242 ? 0.46431 0.53308 0.61630 0.01768  0.02155  0.01870  239 TYR B CD1 
3784 C CD2 . TYR B 242 ? 0.41346 0.48573 0.55912 0.01428  0.01848  0.01897  239 TYR B CD2 
3785 C CE1 . TYR B 242 ? 0.48259 0.55266 0.62418 0.02164  0.03023  0.01326  239 TYR B CE1 
3786 C CE2 . TYR B 242 ? 0.37338 0.44725 0.50876 0.01801  0.02736  0.01372  239 TYR B CE2 
3787 C CZ  . TYR B 242 ? 0.44353 0.51580 0.57656 0.02181  0.03289  0.01080  239 TYR B CZ  
3788 O OH  . TYR B 242 ? 0.49858 0.57034 0.62027 0.02590  0.04028  0.00529  239 TYR B OH  
3789 O OXT . TYR B 242 ? 0.60028 0.64365 0.72976 0.00917  0.00185  0.00804  239 TYR B OXT 
# 
