data_9F2F
# 
_entry.id   9F2F 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9F2F         pdb_00009f2f 10.2210/pdb9f2f/pdb 
WWPDB D_1292138054 ?            ?                   
# 
_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       2025-03-05 
_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                        9F2F 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              thomas.ward@unibas.ch 
_pdbx_contact_author.name_first         Thomas 
_pdbx_contact_author.name_last          Ward 
_pdbx_contact_author.name_mi            R. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8602-5468 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Jakob, R.P.' 1 0000-0002-6451-8656 
'Ward, T.R.'  2 0000-0001-8602-5468 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            14 
_citation.language                  ? 
_citation.page_first                17171 
_citation.page_last                 17179 
_citation.title                     
'Directed Evolution of an Artificial Hydroxylase Based on a Thermostable Human Carbonic Anhydrase Protein' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c04163 
_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 'Morita, I.'     1 ? 
primary 'Faraone, A.'    2 ? 
primary 'Salvisberg, E.' 3 ? 
primary 'Zhang, K.'      4 ? 
primary 'Jakob, R.P.'    5 ? 
primary 'Maier, T.'      6 ? 
primary 'Ward, T.R.'     7 ? 
# 
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 'Carbonic anhydrase 2' 29283.895 4    4.2.1.1,4.2.1.69 ? ? ? 
2 non-polymer syn 
;4,4,7,10,10-pentamethyl-3,6,8,11-tetrakis(oxidanylidene)-N-[2-(4-sulfamoylphenyl)ethyl]-2,5,7,9,12-pentazabicyclo[11.4.0]heptadeca-1(13),14,16-triene-15-carboxamide containing iron
;
639.461   4    ?                ? ? ? 
3 non-polymer syn 'ZINC ION' 65.409    14   ?                ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL 62.068    11   ?                ? ? ? 
5 water       nat water 18.015    1632 ?                ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II,Cyanamide hydratase CA2' 
# 
_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       
;MAHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHTFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSHDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSALPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLESVTWIVLKEPISVSSEQVSKFRKLNFNGEGEPEEPM
VDNWRPTQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHTFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSHDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSALPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLESVTWIVLKEPISVSSEQVSKFRKLNFNGEGEPEEPM
VDNWRPTQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;4,4,7,10,10-pentamethyl-3,6,8,11-tetrakis(oxidanylidene)-N-[2-(4-sulfamoylphenyl)ethyl]-2,5,7,9,12-pentazabicyclo[11.4.0]heptadeca-1(13),14,16-triene-15-carboxamide containing iron
;
A1H9O 
3 'ZINC ION' ZN    
4 1,2-ETHANEDIOL EDO   
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  THR n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 HIS n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LEU n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 SER n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 SER n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 PRO n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 THR n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS 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                   260 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_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 
A1H9O non-polymer         . 
;4,4,7,10,10-pentamethyl-3,6,8,11-tetrakis(oxidanylidene)-N-[2-(4-sulfamoylphenyl)ethyl]-2,5,7,9,12-pentazabicyclo[11.4.0]heptadeca-1(13),14,16-triene-15-carboxamide containing iron
;
?                 'C26 H29 Fe N7 O7 S' 639.461 
ALA   'L-peptide linking' y ALANINE ?                 'C3 H7 N O2'         89.093  
ARG   'L-peptide linking' y ARGININE ?                 'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                 'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'         133.103 
CYS   'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'       121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'           62.068  
GLN   'L-peptide linking' y GLUTAMINE ?                 'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE ?                 'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE ?                 'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER ?                 'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                 'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE ?                 'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE ?                 'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE ?                 'C5 H11 N O2 S'      149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE ?                 'C3 H7 N O3'         105.093 
THR   'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'         119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                 'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE ?                 'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE ?                 'C5 H11 N O2'        117.146 
ZN    non-polymer         . 'ZINC ION' ?                 'Zn 2'               65.409  
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TRP 191 191 191 TRP TRP A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 THR 247 247 247 THR THR A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 GLN 254 254 254 GLN GLN A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   2   ALA ALA B . n 
B 1 3   HIS 3   3   3   HIS HIS B . n 
B 1 4   HIS 4   4   4   HIS HIS B . n 
B 1 5   TRP 5   5   5   TRP TRP B . n 
B 1 6   GLY 6   6   6   GLY GLY B . n 
B 1 7   TYR 7   7   7   TYR TYR B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  HIS 10  10  10  HIS HIS B . n 
B 1 11  ASN 11  11  11  ASN ASN B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  HIS 15  15  15  HIS HIS B . n 
B 1 16  TRP 16  16  16  TRP TRP B . n 
B 1 17  HIS 17  17  17  HIS HIS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  GLY 25  25  25  GLY GLY B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ARG 27  27  27  ARG ARG B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  ASP 32  32  32  ASP ASP B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  THR 35  35  35  THR THR B . n 
B 1 36  HIS 36  36  36  HIS HIS B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  LYS 45  45  45  LYS LYS B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  GLN 53  53  53  GLN GLN B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  ASN 62  62  62  ASN ASN B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  THR 65  65  65  THR THR B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  PRO 83  83  83  PRO PRO B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  GLN 92  92  92  GLN GLN B . n 
B 1 93  PHE 93  93  93  PHE PHE B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  TRP 97  97  97  TRP TRP B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 HIS 100 100 100 HIS HIS B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 GLN 103 103 103 GLN GLN B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 HIS 107 107 107 HIS HIS B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 HIS 122 122 122 HIS HIS B . n 
B 1 123 TRP 123 123 123 TRP TRP B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 THR 125 125 125 THR THR B . n 
B 1 126 LYS 126 126 126 LYS LYS B . n 
B 1 127 TYR 127 127 127 TYR TYR B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 PHE 130 130 130 PHE PHE B . n 
B 1 131 GLY 131 131 131 GLY GLY B . n 
B 1 132 LYS 132 132 132 LYS LYS B . n 
B 1 133 ALA 133 133 133 ALA ALA B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 GLN 136 136 136 GLN GLN B . n 
B 1 137 PRO 137 137 137 PRO PRO B . n 
B 1 138 ASP 138 138 138 ASP ASP B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ALA 141 141 141 ALA ALA B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 GLY 144 144 144 GLY GLY B . n 
B 1 145 ILE 145 145 145 ILE ILE B . n 
B 1 146 PHE 146 146 146 PHE PHE B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 VAL 149 149 149 VAL VAL B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 SER 151 151 151 SER SER B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 PRO 154 154 154 PRO PRO B . n 
B 1 155 GLY 155 155 155 GLY GLY B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 GLN 157 157 157 GLN GLN B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 VAL 160 160 160 VAL VAL B . n 
B 1 161 ASP 161 161 161 ASP ASP B . n 
B 1 162 VAL 162 162 162 VAL VAL B . n 
B 1 163 LEU 163 163 163 LEU LEU B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 SER 165 165 165 SER SER B . n 
B 1 166 ILE 166 166 166 ILE ILE B . n 
B 1 167 LYS 167 167 167 LYS LYS B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 LYS 169 169 169 LYS LYS B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 LYS 171 171 171 LYS LYS B . n 
B 1 172 SER 172 172 172 SER SER B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 ASP 174 174 174 ASP ASP B . n 
B 1 175 PHE 175 175 175 PHE PHE B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 ASN 177 177 177 ASN ASN B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 ASP 179 179 179 ASP ASP B . n 
B 1 180 PRO 180 180 180 PRO PRO B . n 
B 1 181 ARG 181 181 181 ARG ARG B . n 
B 1 182 GLY 182 182 182 GLY GLY B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 SER 187 187 187 SER SER B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 ASP 189 189 189 ASP ASP B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TRP 191 191 191 TRP TRP B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 PRO 194 194 194 PRO PRO B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 LEU 202 202 202 LEU LEU B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 GLU 204 204 204 GLU GLU B . n 
B 1 205 SER 205 205 205 SER SER B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 THR 207 207 207 THR THR B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 ILE 209 209 209 ILE ILE B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 LEU 211 211 211 LEU LEU B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 GLU 213 213 213 GLU GLU B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 ILE 215 215 215 ILE ILE B . n 
B 1 216 SER 216 216 216 SER SER B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 SER 219 219 219 SER SER B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 VAL 222 222 222 VAL VAL B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 PHE 225 225 225 PHE PHE B . n 
B 1 226 ARG 226 226 226 ARG ARG B . n 
B 1 227 LYS 227 227 227 LYS LYS B . n 
B 1 228 LEU 228 228 228 LEU LEU B . n 
B 1 229 ASN 229 229 229 ASN ASN B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 GLY 232 232 232 GLY GLY B . n 
B 1 233 GLU 233 233 233 GLU GLU B . n 
B 1 234 GLY 234 234 234 GLY GLY B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 PRO 236 236 236 PRO PRO B . n 
B 1 237 GLU 237 237 237 GLU GLU B . n 
B 1 238 GLU 238 238 238 GLU GLU B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 MET 240 240 240 MET MET B . n 
B 1 241 VAL 241 241 241 VAL VAL B . n 
B 1 242 ASP 242 242 242 ASP ASP B . n 
B 1 243 ASN 243 243 243 ASN ASN B . n 
B 1 244 TRP 244 244 244 TRP TRP B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 PRO 246 246 246 PRO PRO B . n 
B 1 247 THR 247 247 247 THR THR B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 ARG 253 253 253 ARG ARG B . n 
B 1 254 GLN 254 254 254 GLN GLN B . n 
B 1 255 ILE 255 255 255 ILE ILE B . n 
B 1 256 LYS 256 256 256 LYS LYS B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 SER 258 258 258 SER SER B . n 
B 1 259 PHE 259 259 259 PHE PHE B . n 
B 1 260 LYS 260 260 260 LYS LYS B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   ALA 2   2   2   ALA ALA C . n 
C 1 3   HIS 3   3   3   HIS HIS C . n 
C 1 4   HIS 4   4   4   HIS HIS C . n 
C 1 5   TRP 5   5   5   TRP TRP C . n 
C 1 6   GLY 6   6   6   GLY GLY C . n 
C 1 7   TYR 7   7   7   TYR TYR C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  HIS 10  10  10  HIS HIS C . n 
C 1 11  ASN 11  11  11  ASN ASN C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  GLU 14  14  14  GLU GLU C . n 
C 1 15  HIS 15  15  15  HIS HIS C . n 
C 1 16  TRP 16  16  16  TRP TRP C . n 
C 1 17  HIS 17  17  17  HIS HIS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  ASP 19  19  19  ASP ASP C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  PRO 21  21  21  PRO PRO C . n 
C 1 22  ILE 22  22  22  ILE ILE C . n 
C 1 23  ALA 23  23  23  ALA ALA C . n 
C 1 24  LYS 24  24  24  LYS LYS C . n 
C 1 25  GLY 25  25  25  GLY GLY C . n 
C 1 26  GLU 26  26  26  GLU GLU C . n 
C 1 27  ARG 27  27  27  ARG ARG C . n 
C 1 28  GLN 28  28  28  GLN GLN C . n 
C 1 29  SER 29  29  29  SER SER C . n 
C 1 30  PRO 30  30  30  PRO PRO C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  ASP 32  32  32  ASP ASP C . n 
C 1 33  ILE 33  33  33  ILE ILE C . n 
C 1 34  ASP 34  34  34  ASP ASP C . n 
C 1 35  THR 35  35  35  THR THR C . n 
C 1 36  HIS 36  36  36  HIS HIS C . n 
C 1 37  THR 37  37  37  THR THR C . n 
C 1 38  ALA 38  38  38  ALA ALA C . n 
C 1 39  LYS 39  39  39  LYS LYS C . n 
C 1 40  TYR 40  40  40  TYR TYR C . n 
C 1 41  ASP 41  41  41  ASP ASP C . n 
C 1 42  PRO 42  42  42  PRO PRO C . n 
C 1 43  SER 43  43  43  SER SER C . n 
C 1 44  LEU 44  44  44  LEU LEU C . n 
C 1 45  LYS 45  45  45  LYS LYS C . n 
C 1 46  PRO 46  46  46  PRO PRO C . n 
C 1 47  LEU 47  47  47  LEU LEU C . n 
C 1 48  SER 48  48  48  SER SER C . n 
C 1 49  VAL 49  49  49  VAL VAL C . n 
C 1 50  SER 50  50  50  SER SER C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  GLN 53  53  53  GLN GLN C . n 
C 1 54  ALA 54  54  54  ALA ALA C . n 
C 1 55  THR 55  55  55  THR THR C . n 
C 1 56  SER 56  56  56  SER SER C . n 
C 1 57  LEU 57  57  57  LEU LEU C . n 
C 1 58  ARG 58  58  58  ARG ARG C . n 
C 1 59  ILE 59  59  59  ILE ILE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  ASN 61  61  61  ASN ASN C . n 
C 1 62  ASN 62  62  62  ASN ASN C . n 
C 1 63  GLY 63  63  63  GLY GLY C . n 
C 1 64  HIS 64  64  64  HIS HIS C . n 
C 1 65  THR 65  65  65  THR THR C . n 
C 1 66  PHE 66  66  66  PHE PHE C . n 
C 1 67  ASN 67  67  67  ASN ASN C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  GLU 69  69  69  GLU GLU C . n 
C 1 70  PHE 70  70  70  PHE PHE C . n 
C 1 71  ASP 71  71  71  ASP ASP C . n 
C 1 72  ASP 72  72  72  ASP ASP C . n 
C 1 73  SER 73  73  73  SER SER C . n 
C 1 74  GLN 74  74  74  GLN GLN C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  LYS 76  76  76  LYS LYS C . n 
C 1 77  ALA 77  77  77  ALA ALA C . n 
C 1 78  VAL 78  78  78  VAL VAL C . n 
C 1 79  LEU 79  79  79  LEU LEU C . n 
C 1 80  LYS 80  80  80  LYS LYS C . n 
C 1 81  GLY 81  81  81  GLY GLY C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  PRO 83  83  83  PRO PRO C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  ASP 85  85  85  ASP ASP C . n 
C 1 86  GLY 86  86  86  GLY GLY C . n 
C 1 87  THR 87  87  87  THR THR C . n 
C 1 88  TYR 88  88  88  TYR TYR C . n 
C 1 89  ARG 89  89  89  ARG ARG C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  ILE 91  91  91  ILE ILE C . n 
C 1 92  GLN 92  92  92  GLN GLN C . n 
C 1 93  PHE 93  93  93  PHE PHE C . n 
C 1 94  HIS 94  94  94  HIS HIS C . n 
C 1 95  PHE 95  95  95  PHE PHE C . n 
C 1 96  HIS 96  96  96  HIS HIS C . n 
C 1 97  TRP 97  97  97  TRP TRP C . n 
C 1 98  GLY 98  98  98  GLY GLY C . n 
C 1 99  SER 99  99  99  SER SER C . n 
C 1 100 HIS 100 100 100 HIS HIS C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 GLN 103 103 103 GLN GLN C . n 
C 1 104 GLY 104 104 104 GLY GLY C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 GLU 106 106 106 GLU GLU C . n 
C 1 107 HIS 107 107 107 HIS HIS C . n 
C 1 108 THR 108 108 108 THR THR C . n 
C 1 109 VAL 109 109 109 VAL VAL C . n 
C 1 110 ASP 110 110 110 ASP ASP C . n 
C 1 111 LYS 111 111 111 LYS LYS C . n 
C 1 112 LYS 112 112 112 LYS LYS C . n 
C 1 113 LYS 113 113 113 LYS LYS C . n 
C 1 114 TYR 114 114 114 TYR TYR C . n 
C 1 115 ALA 115 115 115 ALA ALA C . n 
C 1 116 ALA 116 116 116 ALA ALA C . n 
C 1 117 GLU 117 117 117 GLU GLU C . n 
C 1 118 LEU 118 118 118 LEU LEU C . n 
C 1 119 HIS 119 119 119 HIS HIS C . n 
C 1 120 LEU 120 120 120 LEU LEU C . n 
C 1 121 VAL 121 121 121 VAL VAL C . n 
C 1 122 HIS 122 122 122 HIS HIS C . n 
C 1 123 TRP 123 123 123 TRP TRP C . n 
C 1 124 ASN 124 124 124 ASN ASN C . n 
C 1 125 THR 125 125 125 THR THR C . n 
C 1 126 LYS 126 126 126 LYS LYS C . n 
C 1 127 TYR 127 127 127 TYR TYR C . n 
C 1 128 GLY 128 128 128 GLY GLY C . n 
C 1 129 ASP 129 129 129 ASP ASP C . n 
C 1 130 PHE 130 130 130 PHE PHE C . n 
C 1 131 GLY 131 131 131 GLY GLY C . n 
C 1 132 LYS 132 132 132 LYS LYS C . n 
C 1 133 ALA 133 133 133 ALA ALA C . n 
C 1 134 VAL 134 134 134 VAL VAL C . n 
C 1 135 GLN 135 135 135 GLN GLN C . n 
C 1 136 GLN 136 136 136 GLN GLN C . n 
C 1 137 PRO 137 137 137 PRO PRO C . n 
C 1 138 ASP 138 138 138 ASP ASP C . n 
C 1 139 GLY 139 139 139 GLY GLY C . n 
C 1 140 LEU 140 140 140 LEU LEU C . n 
C 1 141 ALA 141 141 141 ALA ALA C . n 
C 1 142 VAL 142 142 142 VAL VAL C . n 
C 1 143 LEU 143 143 143 LEU LEU C . n 
C 1 144 GLY 144 144 144 GLY GLY C . n 
C 1 145 ILE 145 145 145 ILE ILE C . n 
C 1 146 PHE 146 146 146 PHE PHE C . n 
C 1 147 LEU 147 147 147 LEU LEU C . n 
C 1 148 LYS 148 148 148 LYS LYS C . n 
C 1 149 VAL 149 149 149 VAL VAL C . n 
C 1 150 GLY 150 150 150 GLY GLY C . n 
C 1 151 SER 151 151 151 SER SER C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 LEU 153 153 153 LEU LEU C . n 
C 1 154 PRO 154 154 154 PRO PRO C . n 
C 1 155 GLY 155 155 155 GLY GLY C . n 
C 1 156 LEU 156 156 156 LEU LEU C . n 
C 1 157 GLN 157 157 157 GLN GLN C . n 
C 1 158 LYS 158 158 158 LYS LYS C . n 
C 1 159 VAL 159 159 159 VAL VAL C . n 
C 1 160 VAL 160 160 160 VAL VAL C . n 
C 1 161 ASP 161 161 161 ASP ASP C . n 
C 1 162 VAL 162 162 162 VAL VAL C . n 
C 1 163 LEU 163 163 163 LEU LEU C . n 
C 1 164 ASP 164 164 164 ASP ASP C . n 
C 1 165 SER 165 165 165 SER SER C . n 
C 1 166 ILE 166 166 166 ILE ILE C . n 
C 1 167 LYS 167 167 167 LYS LYS C . n 
C 1 168 THR 168 168 168 THR THR C . n 
C 1 169 LYS 169 169 169 LYS LYS C . n 
C 1 170 GLY 170 170 170 GLY GLY C . n 
C 1 171 LYS 171 171 171 LYS LYS C . n 
C 1 172 SER 172 172 172 SER SER C . n 
C 1 173 ALA 173 173 173 ALA ALA C . n 
C 1 174 ASP 174 174 174 ASP ASP C . n 
C 1 175 PHE 175 175 175 PHE PHE C . n 
C 1 176 THR 176 176 176 THR THR C . n 
C 1 177 ASN 177 177 177 ASN ASN C . n 
C 1 178 PHE 178 178 178 PHE PHE C . n 
C 1 179 ASP 179 179 179 ASP ASP C . n 
C 1 180 PRO 180 180 180 PRO PRO C . n 
C 1 181 ARG 181 181 181 ARG ARG C . n 
C 1 182 GLY 182 182 182 GLY GLY C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 LEU 184 184 184 LEU LEU C . n 
C 1 185 PRO 185 185 185 PRO PRO C . n 
C 1 186 GLU 186 186 186 GLU GLU C . n 
C 1 187 SER 187 187 187 SER SER C . n 
C 1 188 LEU 188 188 188 LEU LEU C . n 
C 1 189 ASP 189 189 189 ASP ASP C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TRP 191 191 191 TRP TRP C . n 
C 1 192 THR 192 192 192 THR THR C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 PRO 194 194 194 PRO PRO C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 LEU 202 202 202 LEU LEU C . n 
C 1 203 LEU 203 203 203 LEU LEU C . n 
C 1 204 GLU 204 204 204 GLU GLU C . n 
C 1 205 SER 205 205 205 SER SER C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 THR 207 207 207 THR THR C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 ILE 209 209 209 ILE ILE C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 LEU 211 211 211 LEU LEU C . n 
C 1 212 LYS 212 212 212 LYS LYS C . n 
C 1 213 GLU 213 213 213 GLU GLU C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 ILE 215 215 215 ILE ILE C . n 
C 1 216 SER 216 216 216 SER SER C . n 
C 1 217 VAL 217 217 217 VAL VAL C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 SER 219 219 219 SER SER C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 VAL 222 222 222 VAL VAL C . n 
C 1 223 SER 223 223 223 SER SER C . n 
C 1 224 LYS 224 224 224 LYS LYS C . n 
C 1 225 PHE 225 225 225 PHE PHE C . n 
C 1 226 ARG 226 226 226 ARG ARG C . n 
C 1 227 LYS 227 227 227 LYS LYS C . n 
C 1 228 LEU 228 228 228 LEU LEU C . n 
C 1 229 ASN 229 229 229 ASN ASN C . n 
C 1 230 PHE 230 230 230 PHE PHE C . n 
C 1 231 ASN 231 231 231 ASN ASN C . n 
C 1 232 GLY 232 232 232 GLY GLY C . n 
C 1 233 GLU 233 233 233 GLU GLU C . n 
C 1 234 GLY 234 234 234 GLY GLY C . n 
C 1 235 GLU 235 235 235 GLU GLU C . n 
C 1 236 PRO 236 236 236 PRO PRO C . n 
C 1 237 GLU 237 237 237 GLU GLU C . n 
C 1 238 GLU 238 238 238 GLU GLU C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 MET 240 240 240 MET MET C . n 
C 1 241 VAL 241 241 241 VAL VAL C . n 
C 1 242 ASP 242 242 242 ASP ASP C . n 
C 1 243 ASN 243 243 243 ASN ASN C . n 
C 1 244 TRP 244 244 244 TRP TRP C . n 
C 1 245 ARG 245 245 245 ARG ARG C . n 
C 1 246 PRO 246 246 246 PRO PRO C . n 
C 1 247 THR 247 247 247 THR THR C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 PRO 249 249 249 PRO PRO C . n 
C 1 250 LEU 250 250 250 LEU LEU C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 ASN 252 252 252 ASN ASN C . n 
C 1 253 ARG 253 253 253 ARG ARG C . n 
C 1 254 GLN 254 254 254 GLN GLN C . n 
C 1 255 ILE 255 255 255 ILE ILE C . n 
C 1 256 LYS 256 256 256 LYS LYS C . n 
C 1 257 ALA 257 257 257 ALA ALA C . n 
C 1 258 SER 258 258 258 SER SER C . n 
C 1 259 PHE 259 259 259 PHE PHE C . n 
C 1 260 LYS 260 260 260 LYS LYS C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   ALA 2   2   2   ALA ALA D . n 
D 1 3   HIS 3   3   3   HIS HIS D . n 
D 1 4   HIS 4   4   4   HIS HIS D . n 
D 1 5   TRP 5   5   5   TRP TRP D . n 
D 1 6   GLY 6   6   6   GLY GLY D . n 
D 1 7   TYR 7   7   7   TYR TYR D . n 
D 1 8   GLY 8   8   8   GLY GLY D . n 
D 1 9   LYS 9   9   9   LYS LYS D . n 
D 1 10  HIS 10  10  10  HIS HIS D . n 
D 1 11  ASN 11  11  11  ASN ASN D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  PRO 13  13  13  PRO PRO D . n 
D 1 14  GLU 14  14  14  GLU GLU D . n 
D 1 15  HIS 15  15  15  HIS HIS D . n 
D 1 16  TRP 16  16  16  TRP TRP D . n 
D 1 17  HIS 17  17  17  HIS HIS D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  ASP 19  19  19  ASP ASP D . n 
D 1 20  PHE 20  20  20  PHE PHE D . n 
D 1 21  PRO 21  21  21  PRO PRO D . n 
D 1 22  ILE 22  22  22  ILE ILE D . n 
D 1 23  ALA 23  23  23  ALA ALA D . n 
D 1 24  LYS 24  24  24  LYS LYS D . n 
D 1 25  GLY 25  25  25  GLY GLY D . n 
D 1 26  GLU 26  26  26  GLU GLU D . n 
D 1 27  ARG 27  27  27  ARG ARG D . n 
D 1 28  GLN 28  28  28  GLN GLN D . n 
D 1 29  SER 29  29  29  SER SER D . n 
D 1 30  PRO 30  30  30  PRO PRO D . n 
D 1 31  VAL 31  31  31  VAL VAL D . n 
D 1 32  ASP 32  32  32  ASP ASP D . n 
D 1 33  ILE 33  33  33  ILE ILE D . n 
D 1 34  ASP 34  34  34  ASP ASP D . n 
D 1 35  THR 35  35  35  THR THR D . n 
D 1 36  HIS 36  36  36  HIS HIS D . n 
D 1 37  THR 37  37  37  THR THR D . n 
D 1 38  ALA 38  38  38  ALA ALA D . n 
D 1 39  LYS 39  39  39  LYS LYS D . n 
D 1 40  TYR 40  40  40  TYR TYR D . n 
D 1 41  ASP 41  41  41  ASP ASP D . n 
D 1 42  PRO 42  42  42  PRO PRO D . n 
D 1 43  SER 43  43  43  SER SER D . n 
D 1 44  LEU 44  44  44  LEU LEU D . n 
D 1 45  LYS 45  45  45  LYS LYS D . n 
D 1 46  PRO 46  46  46  PRO PRO D . n 
D 1 47  LEU 47  47  47  LEU LEU D . n 
D 1 48  SER 48  48  48  SER SER D . n 
D 1 49  VAL 49  49  49  VAL VAL D . n 
D 1 50  SER 50  50  50  SER SER D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ASP 52  52  52  ASP ASP D . n 
D 1 53  GLN 53  53  53  GLN GLN D . n 
D 1 54  ALA 54  54  54  ALA ALA D . n 
D 1 55  THR 55  55  55  THR THR D . n 
D 1 56  SER 56  56  56  SER SER D . n 
D 1 57  LEU 57  57  57  LEU LEU D . n 
D 1 58  ARG 58  58  58  ARG ARG D . n 
D 1 59  ILE 59  59  59  ILE ILE D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  ASN 61  61  61  ASN ASN D . n 
D 1 62  ASN 62  62  62  ASN ASN D . n 
D 1 63  GLY 63  63  63  GLY GLY D . n 
D 1 64  HIS 64  64  64  HIS HIS D . n 
D 1 65  THR 65  65  65  THR THR D . n 
D 1 66  PHE 66  66  66  PHE PHE D . n 
D 1 67  ASN 67  67  67  ASN ASN D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  GLU 69  69  69  GLU GLU D . n 
D 1 70  PHE 70  70  70  PHE PHE D . n 
D 1 71  ASP 71  71  71  ASP ASP D . n 
D 1 72  ASP 72  72  72  ASP ASP D . n 
D 1 73  SER 73  73  73  SER SER D . n 
D 1 74  GLN 74  74  74  GLN GLN D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  LYS 76  76  76  LYS LYS D . n 
D 1 77  ALA 77  77  77  ALA ALA D . n 
D 1 78  VAL 78  78  78  VAL VAL D . n 
D 1 79  LEU 79  79  79  LEU LEU D . n 
D 1 80  LYS 80  80  80  LYS LYS D . n 
D 1 81  GLY 81  81  81  GLY GLY D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  PRO 83  83  83  PRO PRO D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  ASP 85  85  85  ASP ASP D . n 
D 1 86  GLY 86  86  86  GLY GLY D . n 
D 1 87  THR 87  87  87  THR THR D . n 
D 1 88  TYR 88  88  88  TYR TYR D . n 
D 1 89  ARG 89  89  89  ARG ARG D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  ILE 91  91  91  ILE ILE D . n 
D 1 92  GLN 92  92  92  GLN GLN D . n 
D 1 93  PHE 93  93  93  PHE PHE D . n 
D 1 94  HIS 94  94  94  HIS HIS D . n 
D 1 95  PHE 95  95  95  PHE PHE D . n 
D 1 96  HIS 96  96  96  HIS HIS D . n 
D 1 97  TRP 97  97  97  TRP TRP D . n 
D 1 98  GLY 98  98  98  GLY GLY D . n 
D 1 99  SER 99  99  99  SER SER D . n 
D 1 100 HIS 100 100 100 HIS HIS D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 GLN 103 103 103 GLN GLN D . n 
D 1 104 GLY 104 104 104 GLY GLY D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 GLU 106 106 106 GLU GLU D . n 
D 1 107 HIS 107 107 107 HIS HIS D . n 
D 1 108 THR 108 108 108 THR THR D . n 
D 1 109 VAL 109 109 109 VAL VAL D . n 
D 1 110 ASP 110 110 110 ASP ASP D . n 
D 1 111 LYS 111 111 111 LYS LYS D . n 
D 1 112 LYS 112 112 112 LYS LYS D . n 
D 1 113 LYS 113 113 113 LYS LYS D . n 
D 1 114 TYR 114 114 114 TYR TYR D . n 
D 1 115 ALA 115 115 115 ALA ALA D . n 
D 1 116 ALA 116 116 116 ALA ALA D . n 
D 1 117 GLU 117 117 117 GLU GLU D . n 
D 1 118 LEU 118 118 118 LEU LEU D . n 
D 1 119 HIS 119 119 119 HIS HIS D . n 
D 1 120 LEU 120 120 120 LEU LEU D . n 
D 1 121 VAL 121 121 121 VAL VAL D . n 
D 1 122 HIS 122 122 122 HIS HIS D . n 
D 1 123 TRP 123 123 123 TRP TRP D . n 
D 1 124 ASN 124 124 124 ASN ASN D . n 
D 1 125 THR 125 125 125 THR THR D . n 
D 1 126 LYS 126 126 126 LYS LYS D . n 
D 1 127 TYR 127 127 127 TYR TYR D . n 
D 1 128 GLY 128 128 128 GLY GLY D . n 
D 1 129 ASP 129 129 129 ASP ASP D . n 
D 1 130 PHE 130 130 130 PHE PHE D . n 
D 1 131 GLY 131 131 131 GLY GLY D . n 
D 1 132 LYS 132 132 132 LYS LYS D . n 
D 1 133 ALA 133 133 133 ALA ALA D . n 
D 1 134 VAL 134 134 134 VAL VAL D . n 
D 1 135 GLN 135 135 135 GLN GLN D . n 
D 1 136 GLN 136 136 136 GLN GLN D . n 
D 1 137 PRO 137 137 137 PRO PRO D . n 
D 1 138 ASP 138 138 138 ASP ASP D . n 
D 1 139 GLY 139 139 139 GLY GLY D . n 
D 1 140 LEU 140 140 140 LEU LEU D . n 
D 1 141 ALA 141 141 141 ALA ALA D . n 
D 1 142 VAL 142 142 142 VAL VAL D . n 
D 1 143 LEU 143 143 143 LEU LEU D . n 
D 1 144 GLY 144 144 144 GLY GLY D . n 
D 1 145 ILE 145 145 145 ILE ILE D . n 
D 1 146 PHE 146 146 146 PHE PHE D . n 
D 1 147 LEU 147 147 147 LEU LEU D . n 
D 1 148 LYS 148 148 148 LYS LYS D . n 
D 1 149 VAL 149 149 149 VAL VAL D . n 
D 1 150 GLY 150 150 150 GLY GLY D . n 
D 1 151 SER 151 151 151 SER SER D . n 
D 1 152 ALA 152 152 152 ALA ALA D . n 
D 1 153 LEU 153 153 153 LEU LEU D . n 
D 1 154 PRO 154 154 154 PRO PRO D . n 
D 1 155 GLY 155 155 155 GLY GLY D . n 
D 1 156 LEU 156 156 156 LEU LEU D . n 
D 1 157 GLN 157 157 157 GLN GLN D . n 
D 1 158 LYS 158 158 158 LYS LYS D . n 
D 1 159 VAL 159 159 159 VAL VAL D . n 
D 1 160 VAL 160 160 160 VAL VAL D . n 
D 1 161 ASP 161 161 161 ASP ASP D . n 
D 1 162 VAL 162 162 162 VAL VAL D . n 
D 1 163 LEU 163 163 163 LEU LEU D . n 
D 1 164 ASP 164 164 164 ASP ASP D . n 
D 1 165 SER 165 165 165 SER SER D . n 
D 1 166 ILE 166 166 166 ILE ILE D . n 
D 1 167 LYS 167 167 167 LYS LYS D . n 
D 1 168 THR 168 168 168 THR THR D . n 
D 1 169 LYS 169 169 169 LYS LYS D . n 
D 1 170 GLY 170 170 170 GLY GLY D . n 
D 1 171 LYS 171 171 171 LYS LYS D . n 
D 1 172 SER 172 172 172 SER SER D . n 
D 1 173 ALA 173 173 173 ALA ALA D . n 
D 1 174 ASP 174 174 174 ASP ASP D . n 
D 1 175 PHE 175 175 175 PHE PHE D . n 
D 1 176 THR 176 176 176 THR THR D . n 
D 1 177 ASN 177 177 177 ASN ASN D . n 
D 1 178 PHE 178 178 178 PHE PHE D . n 
D 1 179 ASP 179 179 179 ASP ASP D . n 
D 1 180 PRO 180 180 180 PRO PRO D . n 
D 1 181 ARG 181 181 181 ARG ARG D . n 
D 1 182 GLY 182 182 182 GLY GLY D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 LEU 184 184 184 LEU LEU D . n 
D 1 185 PRO 185 185 185 PRO PRO D . n 
D 1 186 GLU 186 186 186 GLU GLU D . n 
D 1 187 SER 187 187 187 SER SER D . n 
D 1 188 LEU 188 188 188 LEU LEU D . n 
D 1 189 ASP 189 189 189 ASP ASP D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 TRP 191 191 191 TRP TRP D . n 
D 1 192 THR 192 192 192 THR THR D . n 
D 1 193 TYR 193 193 193 TYR TYR D . n 
D 1 194 PRO 194 194 194 PRO PRO D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 THR 199 199 199 THR THR D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 PRO 201 201 201 PRO PRO D . n 
D 1 202 LEU 202 202 202 LEU LEU D . n 
D 1 203 LEU 203 203 203 LEU LEU D . n 
D 1 204 GLU 204 204 204 GLU GLU D . n 
D 1 205 SER 205 205 205 SER SER D . n 
D 1 206 VAL 206 206 206 VAL VAL D . n 
D 1 207 THR 207 207 207 THR THR D . n 
D 1 208 TRP 208 208 208 TRP TRP D . n 
D 1 209 ILE 209 209 209 ILE ILE D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 LEU 211 211 211 LEU LEU D . n 
D 1 212 LYS 212 212 212 LYS LYS D . n 
D 1 213 GLU 213 213 213 GLU GLU D . n 
D 1 214 PRO 214 214 214 PRO PRO D . n 
D 1 215 ILE 215 215 215 ILE ILE D . n 
D 1 216 SER 216 216 216 SER SER D . n 
D 1 217 VAL 217 217 217 VAL VAL D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 SER 219 219 219 SER SER D . n 
D 1 220 GLU 220 220 220 GLU GLU D . n 
D 1 221 GLN 221 221 221 GLN GLN D . n 
D 1 222 VAL 222 222 222 VAL VAL D . n 
D 1 223 SER 223 223 223 SER SER D . n 
D 1 224 LYS 224 224 224 LYS LYS D . n 
D 1 225 PHE 225 225 225 PHE PHE D . n 
D 1 226 ARG 226 226 226 ARG ARG D . n 
D 1 227 LYS 227 227 227 LYS LYS D . n 
D 1 228 LEU 228 228 228 LEU LEU D . n 
D 1 229 ASN 229 229 229 ASN ASN D . n 
D 1 230 PHE 230 230 230 PHE PHE D . n 
D 1 231 ASN 231 231 231 ASN ASN D . n 
D 1 232 GLY 232 232 232 GLY GLY D . n 
D 1 233 GLU 233 233 233 GLU GLU D . n 
D 1 234 GLY 234 234 234 GLY GLY D . n 
D 1 235 GLU 235 235 235 GLU GLU D . n 
D 1 236 PRO 236 236 236 PRO PRO D . n 
D 1 237 GLU 237 237 237 GLU GLU D . n 
D 1 238 GLU 238 238 238 GLU GLU D . n 
D 1 239 PRO 239 239 239 PRO PRO D . n 
D 1 240 MET 240 240 240 MET MET D . n 
D 1 241 VAL 241 241 241 VAL VAL D . n 
D 1 242 ASP 242 242 242 ASP ASP D . n 
D 1 243 ASN 243 243 243 ASN ASN D . n 
D 1 244 TRP 244 244 244 TRP TRP D . n 
D 1 245 ARG 245 245 245 ARG ARG D . n 
D 1 246 PRO 246 246 246 PRO PRO D . n 
D 1 247 THR 247 247 247 THR THR D . n 
D 1 248 GLN 248 248 248 GLN GLN D . n 
D 1 249 PRO 249 249 249 PRO PRO D . n 
D 1 250 LEU 250 250 250 LEU LEU D . n 
D 1 251 LYS 251 251 251 LYS LYS D . n 
D 1 252 ASN 252 252 252 ASN ASN D . n 
D 1 253 ARG 253 253 253 ARG ARG D . n 
D 1 254 GLN 254 254 254 GLN GLN D . n 
D 1 255 ILE 255 255 255 ILE ILE D . n 
D 1 256 LYS 256 256 256 LYS LYS D . n 
D 1 257 ALA 257 257 257 ALA ALA D . n 
D 1 258 SER 258 258 258 SER SER D . n 
D 1 259 PHE 259 259 259 PHE PHE D . n 
D 1 260 LYS 260 260 260 LYS LYS D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H9O 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H9O 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 A1H9O 1   301  301  A1H9O CAT A . 
F  3 ZN    1   302  401  ZN    ZN  A . 
G  4 EDO   1   303  402  EDO   EDO A . 
H  4 EDO   1   304  405  EDO   EDO A . 
I  3 ZN    1   305  1    ZN    ZN  A . 
J  3 ZN    1   306  4    ZN    ZN  A . 
K  3 ZN    1   307  8    ZN    ZN  A . 
L  2 A1H9O 1   301  301  A1H9O CAT B . 
M  3 ZN    1   302  401  ZN    ZN  B . 
N  4 EDO   1   303  402  EDO   EDO B . 
O  4 EDO   1   304  404  EDO   EDO B . 
P  4 EDO   1   305  405  EDO   EDO B . 
Q  3 ZN    1   306  3    ZN    ZN  B . 
R  3 ZN    1   307  6    ZN    ZN  B . 
S  3 ZN    1   308  10   ZN    ZN  B . 
T  2 A1H9O 1   301  301  A1H9O CAT C . 
U  3 ZN    1   302  401  ZN    ZN  C . 
V  4 EDO   1   303  402  EDO   EDO C . 
W  4 EDO   1   304  403  EDO   EDO C . 
X  4 EDO   1   305  404  EDO   EDO C . 
Y  4 EDO   1   306  405  EDO   EDO C . 
Z  4 EDO   1   307  406  EDO   EDO C . 
AA 3 ZN    1   308  2    ZN    ZN  C . 
BA 2 A1H9O 1   301  301  A1H9O CAT D . 
CA 3 ZN    1   302  401  ZN    ZN  D . 
DA 4 EDO   1   303  402  EDO   EDO D . 
EA 3 ZN    1   304  5    ZN    ZN  D . 
FA 3 ZN    1   305  7    ZN    ZN  D . 
GA 3 ZN    1   306  9    ZN    ZN  D . 
HA 5 HOH   1   1701 1701 HOH   HOH A . 
HA 5 HOH   2   1702 1592 HOH   HOH A . 
HA 5 HOH   3   1703 39   HOH   HOH A . 
HA 5 HOH   4   1704 1033 HOH   HOH A . 
HA 5 HOH   5   1705 1556 HOH   HOH A . 
HA 5 HOH   6   1706 1097 HOH   HOH A . 
HA 5 HOH   7   1707 1014 HOH   HOH A . 
HA 5 HOH   8   1708 141  HOH   HOH A . 
HA 5 HOH   9   1709 1588 HOH   HOH A . 
HA 5 HOH   10  1710 1611 HOH   HOH A . 
HA 5 HOH   11  1711 110  HOH   HOH A . 
HA 5 HOH   12  1712 1332 HOH   HOH A . 
HA 5 HOH   13  1713 546  HOH   HOH A . 
HA 5 HOH   14  1714 876  HOH   HOH A . 
HA 5 HOH   15  1715 872  HOH   HOH A . 
HA 5 HOH   16  1716 104  HOH   HOH A . 
HA 5 HOH   17  1717 1407 HOH   HOH A . 
HA 5 HOH   18  1718 855  HOH   HOH A . 
HA 5 HOH   19  1719 679  HOH   HOH A . 
HA 5 HOH   20  1720 1048 HOH   HOH A . 
HA 5 HOH   21  1721 644  HOH   HOH A . 
HA 5 HOH   22  1722 24   HOH   HOH A . 
HA 5 HOH   23  1723 853  HOH   HOH A . 
HA 5 HOH   24  1724 1114 HOH   HOH A . 
HA 5 HOH   25  1725 123  HOH   HOH A . 
HA 5 HOH   26  1726 457  HOH   HOH A . 
HA 5 HOH   27  1727 1308 HOH   HOH A . 
HA 5 HOH   28  1728 642  HOH   HOH A . 
HA 5 HOH   29  1729 266  HOH   HOH A . 
HA 5 HOH   30  1730 774  HOH   HOH A . 
HA 5 HOH   31  1731 562  HOH   HOH A . 
HA 5 HOH   32  1732 567  HOH   HOH A . 
HA 5 HOH   33  1733 303  HOH   HOH A . 
HA 5 HOH   34  1734 1198 HOH   HOH A . 
HA 5 HOH   35  1735 516  HOH   HOH A . 
HA 5 HOH   36  1736 1570 HOH   HOH A . 
HA 5 HOH   37  1737 954  HOH   HOH A . 
HA 5 HOH   38  1738 1512 HOH   HOH A . 
HA 5 HOH   39  1739 1369 HOH   HOH A . 
HA 5 HOH   40  1740 212  HOH   HOH A . 
HA 5 HOH   41  1741 950  HOH   HOH A . 
HA 5 HOH   42  1742 101  HOH   HOH A . 
HA 5 HOH   43  1743 786  HOH   HOH A . 
HA 5 HOH   44  1744 1547 HOH   HOH A . 
HA 5 HOH   45  1745 1650 HOH   HOH A . 
HA 5 HOH   46  1746 201  HOH   HOH A . 
HA 5 HOH   47  1747 292  HOH   HOH A . 
HA 5 HOH   48  1748 487  HOH   HOH A . 
HA 5 HOH   49  1749 27   HOH   HOH A . 
HA 5 HOH   50  1750 715  HOH   HOH A . 
HA 5 HOH   51  1751 1353 HOH   HOH A . 
HA 5 HOH   52  1752 96   HOH   HOH A . 
HA 5 HOH   53  1753 948  HOH   HOH A . 
HA 5 HOH   54  1754 227  HOH   HOH A . 
HA 5 HOH   55  1755 883  HOH   HOH A . 
HA 5 HOH   56  1756 1017 HOH   HOH A . 
HA 5 HOH   57  1757 975  HOH   HOH A . 
HA 5 HOH   58  1758 207  HOH   HOH A . 
HA 5 HOH   59  1759 914  HOH   HOH A . 
HA 5 HOH   60  1760 64   HOH   HOH A . 
HA 5 HOH   61  1761 523  HOH   HOH A . 
HA 5 HOH   62  1762 1151 HOH   HOH A . 
HA 5 HOH   63  1763 28   HOH   HOH A . 
HA 5 HOH   64  1764 1404 HOH   HOH A . 
HA 5 HOH   65  1765 479  HOH   HOH A . 
HA 5 HOH   66  1766 353  HOH   HOH A . 
HA 5 HOH   67  1767 486  HOH   HOH A . 
HA 5 HOH   68  1768 844  HOH   HOH A . 
HA 5 HOH   69  1769 1363 HOH   HOH A . 
HA 5 HOH   70  1770 49   HOH   HOH A . 
HA 5 HOH   71  1771 402  HOH   HOH A . 
HA 5 HOH   72  1772 7    HOH   HOH A . 
HA 5 HOH   73  1773 712  HOH   HOH A . 
HA 5 HOH   74  1774 102  HOH   HOH A . 
HA 5 HOH   75  1775 209  HOH   HOH A . 
HA 5 HOH   76  1776 112  HOH   HOH A . 
HA 5 HOH   77  1777 117  HOH   HOH A . 
HA 5 HOH   78  1778 1152 HOH   HOH A . 
HA 5 HOH   79  1779 219  HOH   HOH A . 
HA 5 HOH   80  1780 286  HOH   HOH A . 
HA 5 HOH   81  1781 11   HOH   HOH A . 
HA 5 HOH   82  1782 732  HOH   HOH A . 
HA 5 HOH   83  1783 80   HOH   HOH A . 
HA 5 HOH   84  1784 1613 HOH   HOH A . 
HA 5 HOH   85  1785 99   HOH   HOH A . 
HA 5 HOH   86  1786 332  HOH   HOH A . 
HA 5 HOH   87  1787 1698 HOH   HOH A . 
HA 5 HOH   88  1788 671  HOH   HOH A . 
HA 5 HOH   89  1789 508  HOH   HOH A . 
HA 5 HOH   90  1790 1096 HOH   HOH A . 
HA 5 HOH   91  1791 400  HOH   HOH A . 
HA 5 HOH   92  1792 338  HOH   HOH A . 
HA 5 HOH   93  1793 767  HOH   HOH A . 
HA 5 HOH   94  1794 728  HOH   HOH A . 
HA 5 HOH   95  1795 778  HOH   HOH A . 
HA 5 HOH   96  1796 1580 HOH   HOH A . 
HA 5 HOH   97  1797 824  HOH   HOH A . 
HA 5 HOH   98  1798 124  HOH   HOH A . 
HA 5 HOH   99  1799 159  HOH   HOH A . 
HA 5 HOH   100 1800 284  HOH   HOH A . 
HA 5 HOH   101 1801 241  HOH   HOH A . 
HA 5 HOH   102 1802 635  HOH   HOH A . 
HA 5 HOH   103 1803 459  HOH   HOH A . 
HA 5 HOH   104 1804 462  HOH   HOH A . 
HA 5 HOH   105 1805 645  HOH   HOH A . 
HA 5 HOH   106 1806 665  HOH   HOH A . 
HA 5 HOH   107 1807 91   HOH   HOH A . 
HA 5 HOH   108 1808 1084 HOH   HOH A . 
HA 5 HOH   109 1809 348  HOH   HOH A . 
HA 5 HOH   110 1810 68   HOH   HOH A . 
HA 5 HOH   111 1811 891  HOH   HOH A . 
HA 5 HOH   112 1812 545  HOH   HOH A . 
HA 5 HOH   113 1813 165  HOH   HOH A . 
HA 5 HOH   114 1814 1079 HOH   HOH A . 
HA 5 HOH   115 1815 182  HOH   HOH A . 
HA 5 HOH   116 1816 1027 HOH   HOH A . 
HA 5 HOH   117 1817 1499 HOH   HOH A . 
HA 5 HOH   118 1818 591  HOH   HOH A . 
HA 5 HOH   119 1819 1423 HOH   HOH A . 
HA 5 HOH   120 1820 808  HOH   HOH A . 
HA 5 HOH   121 1821 367  HOH   HOH A . 
HA 5 HOH   122 1822 263  HOH   HOH A . 
HA 5 HOH   123 1823 1267 HOH   HOH A . 
HA 5 HOH   124 1824 572  HOH   HOH A . 
HA 5 HOH   125 1825 613  HOH   HOH A . 
HA 5 HOH   126 1826 803  HOH   HOH A . 
HA 5 HOH   127 1827 575  HOH   HOH A . 
HA 5 HOH   128 1828 85   HOH   HOH A . 
HA 5 HOH   129 1829 89   HOH   HOH A . 
HA 5 HOH   130 1830 589  HOH   HOH A . 
HA 5 HOH   131 1831 1143 HOH   HOH A . 
HA 5 HOH   132 1832 415  HOH   HOH A . 
HA 5 HOH   133 1833 746  HOH   HOH A . 
HA 5 HOH   134 1834 654  HOH   HOH A . 
HA 5 HOH   135 1835 217  HOH   HOH A . 
HA 5 HOH   136 1836 161  HOH   HOH A . 
HA 5 HOH   137 1837 1571 HOH   HOH A . 
HA 5 HOH   138 1838 1038 HOH   HOH A . 
HA 5 HOH   139 1839 37   HOH   HOH A . 
HA 5 HOH   140 1840 184  HOH   HOH A . 
HA 5 HOH   141 1841 682  HOH   HOH A . 
HA 5 HOH   142 1842 941  HOH   HOH A . 
HA 5 HOH   143 1843 1060 HOH   HOH A . 
HA 5 HOH   144 1844 333  HOH   HOH A . 
HA 5 HOH   145 1845 247  HOH   HOH A . 
HA 5 HOH   146 1846 685  HOH   HOH A . 
HA 5 HOH   147 1847 407  HOH   HOH A . 
HA 5 HOH   148 1848 1321 HOH   HOH A . 
HA 5 HOH   149 1849 225  HOH   HOH A . 
HA 5 HOH   150 1850 369  HOH   HOH A . 
HA 5 HOH   151 1851 1564 HOH   HOH A . 
HA 5 HOH   152 1852 903  HOH   HOH A . 
HA 5 HOH   153 1853 593  HOH   HOH A . 
HA 5 HOH   154 1854 336  HOH   HOH A . 
HA 5 HOH   155 1855 1661 HOH   HOH A . 
HA 5 HOH   156 1856 616  HOH   HOH A . 
HA 5 HOH   157 1857 1309 HOH   HOH A . 
HA 5 HOH   158 1858 1118 HOH   HOH A . 
HA 5 HOH   159 1859 52   HOH   HOH A . 
HA 5 HOH   160 1860 541  HOH   HOH A . 
HA 5 HOH   161 1861 153  HOH   HOH A . 
HA 5 HOH   162 1862 1053 HOH   HOH A . 
HA 5 HOH   163 1863 1256 HOH   HOH A . 
HA 5 HOH   164 1864 1393 HOH   HOH A . 
HA 5 HOH   165 1865 458  HOH   HOH A . 
HA 5 HOH   166 1866 703  HOH   HOH A . 
HA 5 HOH   167 1867 370  HOH   HOH A . 
HA 5 HOH   168 1868 1703 HOH   HOH A . 
HA 5 HOH   169 1869 1123 HOH   HOH A . 
HA 5 HOH   170 1870 376  HOH   HOH A . 
HA 5 HOH   171 1871 296  HOH   HOH A . 
HA 5 HOH   172 1872 811  HOH   HOH A . 
HA 5 HOH   173 1873 945  HOH   HOH A . 
HA 5 HOH   174 1874 1126 HOH   HOH A . 
HA 5 HOH   175 1875 571  HOH   HOH A . 
HA 5 HOH   176 1876 1144 HOH   HOH A . 
HA 5 HOH   177 1877 894  HOH   HOH A . 
HA 5 HOH   178 1878 422  HOH   HOH A . 
HA 5 HOH   179 1879 236  HOH   HOH A . 
HA 5 HOH   180 1880 940  HOH   HOH A . 
HA 5 HOH   181 1881 132  HOH   HOH A . 
HA 5 HOH   182 1882 587  HOH   HOH A . 
HA 5 HOH   183 1883 725  HOH   HOH A . 
HA 5 HOH   184 1884 271  HOH   HOH A . 
HA 5 HOH   185 1885 887  HOH   HOH A . 
HA 5 HOH   186 1886 1690 HOH   HOH A . 
HA 5 HOH   187 1887 680  HOH   HOH A . 
HA 5 HOH   188 1888 801  HOH   HOH A . 
HA 5 HOH   189 1889 583  HOH   HOH A . 
HA 5 HOH   190 1890 1704 HOH   HOH A . 
HA 5 HOH   191 1891 877  HOH   HOH A . 
HA 5 HOH   192 1892 350  HOH   HOH A . 
HA 5 HOH   193 1893 1654 HOH   HOH A . 
HA 5 HOH   194 1894 1456 HOH   HOH A . 
HA 5 HOH   195 1895 1093 HOH   HOH A . 
HA 5 HOH   196 1896 1042 HOH   HOH A . 
HA 5 HOH   197 1897 273  HOH   HOH A . 
HA 5 HOH   198 1898 909  HOH   HOH A . 
HA 5 HOH   199 1899 1389 HOH   HOH A . 
HA 5 HOH   200 1900 1015 HOH   HOH A . 
HA 5 HOH   201 1901 295  HOH   HOH A . 
HA 5 HOH   202 1902 900  HOH   HOH A . 
HA 5 HOH   203 1903 722  HOH   HOH A . 
HA 5 HOH   204 1904 285  HOH   HOH A . 
HA 5 HOH   205 1905 539  HOH   HOH A . 
HA 5 HOH   206 1906 698  HOH   HOH A . 
HA 5 HOH   207 1907 768  HOH   HOH A . 
HA 5 HOH   208 1908 607  HOH   HOH A . 
HA 5 HOH   209 1909 1430 HOH   HOH A . 
HA 5 HOH   210 1910 1686 HOH   HOH A . 
HA 5 HOH   211 1911 390  HOH   HOH A . 
HA 5 HOH   212 1912 474  HOH   HOH A . 
HA 5 HOH   213 1913 576  HOH   HOH A . 
HA 5 HOH   214 1914 1381 HOH   HOH A . 
HA 5 HOH   215 1915 373  HOH   HOH A . 
HA 5 HOH   216 1916 57   HOH   HOH A . 
HA 5 HOH   217 1917 629  HOH   HOH A . 
HA 5 HOH   218 1918 1527 HOH   HOH A . 
HA 5 HOH   219 1919 126  HOH   HOH A . 
HA 5 HOH   220 1920 389  HOH   HOH A . 
HA 5 HOH   221 1921 1242 HOH   HOH A . 
HA 5 HOH   222 1922 467  HOH   HOH A . 
HA 5 HOH   223 1923 1579 HOH   HOH A . 
HA 5 HOH   224 1924 186  HOH   HOH A . 
HA 5 HOH   225 1925 881  HOH   HOH A . 
HA 5 HOH   226 1926 563  HOH   HOH A . 
HA 5 HOH   227 1927 122  HOH   HOH A . 
HA 5 HOH   228 1928 978  HOH   HOH A . 
HA 5 HOH   229 1929 387  HOH   HOH A . 
HA 5 HOH   230 1930 289  HOH   HOH A . 
HA 5 HOH   231 1931 190  HOH   HOH A . 
HA 5 HOH   232 1932 1655 HOH   HOH A . 
HA 5 HOH   233 1933 1535 HOH   HOH A . 
HA 5 HOH   234 1934 26   HOH   HOH A . 
HA 5 HOH   235 1935 500  HOH   HOH A . 
HA 5 HOH   236 1936 826  HOH   HOH A . 
HA 5 HOH   237 1937 1549 HOH   HOH A . 
HA 5 HOH   238 1938 1670 HOH   HOH A . 
HA 5 HOH   239 1939 147  HOH   HOH A . 
HA 5 HOH   240 1940 743  HOH   HOH A . 
HA 5 HOH   241 1941 718  HOH   HOH A . 
HA 5 HOH   242 1942 1539 HOH   HOH A . 
HA 5 HOH   243 1943 1188 HOH   HOH A . 
HA 5 HOH   244 1944 1249 HOH   HOH A . 
HA 5 HOH   245 1945 1111 HOH   HOH A . 
HA 5 HOH   246 1946 1398 HOH   HOH A . 
HA 5 HOH   247 1947 1352 HOH   HOH A . 
HA 5 HOH   248 1948 929  HOH   HOH A . 
HA 5 HOH   249 1949 1032 HOH   HOH A . 
HA 5 HOH   250 1950 319  HOH   HOH A . 
HA 5 HOH   251 1951 1113 HOH   HOH A . 
HA 5 HOH   252 1952 1466 HOH   HOH A . 
HA 5 HOH   253 1953 987  HOH   HOH A . 
HA 5 HOH   254 1954 1482 HOH   HOH A . 
HA 5 HOH   255 1955 411  HOH   HOH A . 
HA 5 HOH   256 1956 1081 HOH   HOH A . 
HA 5 HOH   257 1957 1191 HOH   HOH A . 
HA 5 HOH   258 1958 444  HOH   HOH A . 
HA 5 HOH   259 1959 1303 HOH   HOH A . 
HA 5 HOH   260 1960 298  HOH   HOH A . 
HA 5 HOH   261 1961 229  HOH   HOH A . 
HA 5 HOH   262 1962 830  HOH   HOH A . 
HA 5 HOH   263 1963 537  HOH   HOH A . 
HA 5 HOH   264 1964 1278 HOH   HOH A . 
HA 5 HOH   265 1965 1457 HOH   HOH A . 
HA 5 HOH   266 1966 408  HOH   HOH A . 
HA 5 HOH   267 1967 1253 HOH   HOH A . 
HA 5 HOH   268 1968 1194 HOH   HOH A . 
HA 5 HOH   269 1969 736  HOH   HOH A . 
HA 5 HOH   270 1970 1621 HOH   HOH A . 
HA 5 HOH   271 1971 473  HOH   HOH A . 
HA 5 HOH   272 1972 691  HOH   HOH A . 
HA 5 HOH   273 1973 1241 HOH   HOH A . 
HA 5 HOH   274 1974 62   HOH   HOH A . 
HA 5 HOH   275 1975 1658 HOH   HOH A . 
HA 5 HOH   276 1976 1090 HOH   HOH A . 
HA 5 HOH   277 1977 1411 HOH   HOH A . 
HA 5 HOH   278 1978 1161 HOH   HOH A . 
HA 5 HOH   279 1979 1047 HOH   HOH A . 
HA 5 HOH   280 1980 1266 HOH   HOH A . 
HA 5 HOH   281 1981 1231 HOH   HOH A . 
HA 5 HOH   282 1982 150  HOH   HOH A . 
HA 5 HOH   283 1983 1652 HOH   HOH A . 
HA 5 HOH   284 1984 1251 HOH   HOH A . 
HA 5 HOH   285 1985 10   HOH   HOH A . 
HA 5 HOH   286 1986 1402 HOH   HOH A . 
HA 5 HOH   287 1987 1599 HOH   HOH A . 
HA 5 HOH   288 1988 2    HOH   HOH A . 
HA 5 HOH   289 1989 499  HOH   HOH A . 
HA 5 HOH   290 1990 757  HOH   HOH A . 
HA 5 HOH   291 1991 452  HOH   HOH A . 
HA 5 HOH   292 1992 1493 HOH   HOH A . 
HA 5 HOH   293 1993 1337 HOH   HOH A . 
HA 5 HOH   294 1994 1099 HOH   HOH A . 
HA 5 HOH   295 1995 496  HOH   HOH A . 
HA 5 HOH   296 1996 889  HOH   HOH A . 
HA 5 HOH   297 1997 1361 HOH   HOH A . 
HA 5 HOH   298 1998 1540 HOH   HOH A . 
HA 5 HOH   299 1999 1468 HOH   HOH A . 
HA 5 HOH   300 2000 549  HOH   HOH A . 
HA 5 HOH   301 2001 1001 HOH   HOH A . 
HA 5 HOH   302 2002 1306 HOH   HOH A . 
HA 5 HOH   303 2003 1620 HOH   HOH A . 
HA 5 HOH   304 2004 1372 HOH   HOH A . 
HA 5 HOH   305 2005 282  HOH   HOH A . 
HA 5 HOH   306 2006 886  HOH   HOH A . 
HA 5 HOH   307 2007 561  HOH   HOH A . 
HA 5 HOH   308 2008 1619 HOH   HOH A . 
HA 5 HOH   309 2009 1313 HOH   HOH A . 
HA 5 HOH   310 2010 19   HOH   HOH A . 
HA 5 HOH   311 2011 1223 HOH   HOH A . 
HA 5 HOH   312 2012 393  HOH   HOH A . 
HA 5 HOH   313 2013 1230 HOH   HOH A . 
HA 5 HOH   314 2014 1089 HOH   HOH A . 
HA 5 HOH   315 2015 1593 HOH   HOH A . 
HA 5 HOH   316 2016 1067 HOH   HOH A . 
HA 5 HOH   317 2017 1566 HOH   HOH A . 
HA 5 HOH   318 2018 163  HOH   HOH A . 
HA 5 HOH   319 2019 1051 HOH   HOH A . 
HA 5 HOH   320 2020 1127 HOH   HOH A . 
HA 5 HOH   321 2021 628  HOH   HOH A . 
HA 5 HOH   322 2022 1288 HOH   HOH A . 
HA 5 HOH   323 2023 1633 HOH   HOH A . 
HA 5 HOH   324 2024 1415 HOH   HOH A . 
HA 5 HOH   325 2025 871  HOH   HOH A . 
HA 5 HOH   326 2026 1521 HOH   HOH A . 
HA 5 HOH   327 2027 980  HOH   HOH A . 
HA 5 HOH   328 2028 1102 HOH   HOH A . 
HA 5 HOH   329 2029 1498 HOH   HOH A . 
HA 5 HOH   330 2030 1022 HOH   HOH A . 
HA 5 HOH   331 2031 848  HOH   HOH A . 
HA 5 HOH   332 2032 1222 HOH   HOH A . 
HA 5 HOH   333 2033 556  HOH   HOH A . 
HA 5 HOH   334 2034 755  HOH   HOH A . 
HA 5 HOH   335 2035 53   HOH   HOH A . 
HA 5 HOH   336 2036 1214 HOH   HOH A . 
HA 5 HOH   337 2037 989  HOH   HOH A . 
HA 5 HOH   338 2038 1597 HOH   HOH A . 
HA 5 HOH   339 2039 1514 HOH   HOH A . 
HA 5 HOH   340 2040 1572 HOH   HOH A . 
HA 5 HOH   341 2041 1395 HOH   HOH A . 
HA 5 HOH   342 2042 1392 HOH   HOH A . 
HA 5 HOH   343 2043 1678 HOH   HOH A . 
HA 5 HOH   344 2044 700  HOH   HOH A . 
HA 5 HOH   345 2045 917  HOH   HOH A . 
HA 5 HOH   346 2046 1469 HOH   HOH A . 
HA 5 HOH   347 2047 1465 HOH   HOH A . 
HA 5 HOH   348 2048 1486 HOH   HOH A . 
HA 5 HOH   349 2049 1018 HOH   HOH A . 
HA 5 HOH   350 2050 1427 HOH   HOH A . 
HA 5 HOH   351 2051 1229 HOH   HOH A . 
HA 5 HOH   352 2052 1371 HOH   HOH A . 
HA 5 HOH   353 2053 752  HOH   HOH A . 
HA 5 HOH   354 2054 643  HOH   HOH A . 
HA 5 HOH   355 2055 869  HOH   HOH A . 
HA 5 HOH   356 2056 748  HOH   HOH A . 
HA 5 HOH   357 2057 1632 HOH   HOH A . 
HA 5 HOH   358 2058 194  HOH   HOH A . 
HA 5 HOH   359 2059 856  HOH   HOH A . 
HA 5 HOH   360 2060 1419 HOH   HOH A . 
HA 5 HOH   361 2061 761  HOH   HOH A . 
HA 5 HOH   362 2062 1614 HOH   HOH A . 
HA 5 HOH   363 2063 992  HOH   HOH A . 
HA 5 HOH   364 2064 777  HOH   HOH A . 
HA 5 HOH   365 2065 1666 HOH   HOH A . 
HA 5 HOH   366 2066 1505 HOH   HOH A . 
HA 5 HOH   367 2067 661  HOH   HOH A . 
HA 5 HOH   368 2068 1631 HOH   HOH A . 
HA 5 HOH   369 2069 964  HOH   HOH A . 
HA 5 HOH   370 2070 724  HOH   HOH A . 
HA 5 HOH   371 2071 1236 HOH   HOH A . 
HA 5 HOH   372 2072 1515 HOH   HOH A . 
HA 5 HOH   373 2073 1683 HOH   HOH A . 
HA 5 HOH   374 2074 1255 HOH   HOH A . 
HA 5 HOH   375 2075 1710 HOH   HOH A . 
HA 5 HOH   376 2076 1314 HOH   HOH A . 
HA 5 HOH   377 2077 839  HOH   HOH A . 
HA 5 HOH   378 2078 973  HOH   HOH A . 
HA 5 HOH   379 2079 1318 HOH   HOH A . 
HA 5 HOH   380 2080 1072 HOH   HOH A . 
HA 5 HOH   381 2081 1331 HOH   HOH A . 
HA 5 HOH   382 2082 1121 HOH   HOH A . 
HA 5 HOH   383 2083 1529 HOH   HOH A . 
HA 5 HOH   384 2084 1438 HOH   HOH A . 
HA 5 HOH   385 2085 639  HOH   HOH A . 
HA 5 HOH   386 2086 727  HOH   HOH A . 
HA 5 HOH   387 2087 1409 HOH   HOH A . 
HA 5 HOH   388 2088 1634 HOH   HOH A . 
HA 5 HOH   389 2089 1201 HOH   HOH A . 
HA 5 HOH   390 2090 1437 HOH   HOH A . 
HA 5 HOH   391 2091 1612 HOH   HOH A . 
HA 5 HOH   392 2092 1506 HOH   HOH A . 
HA 5 HOH   393 2093 1217 HOH   HOH A . 
HA 5 HOH   394 2094 814  HOH   HOH A . 
HA 5 HOH   395 2095 785  HOH   HOH A . 
HA 5 HOH   396 2096 1302 HOH   HOH A . 
HA 5 HOH   397 2097 1445 HOH   HOH A . 
HA 5 HOH   398 2098 1640 HOH   HOH A . 
HA 5 HOH   399 2099 1665 HOH   HOH A . 
HA 5 HOH   400 2100 711  HOH   HOH A . 
HA 5 HOH   401 2101 1532 HOH   HOH A . 
HA 5 HOH   402 2102 354  HOH   HOH A . 
HA 5 HOH   403 2103 1197 HOH   HOH A . 
HA 5 HOH   404 2104 598  HOH   HOH A . 
HA 5 HOH   405 2105 1237 HOH   HOH A . 
HA 5 HOH   406 2106 686  HOH   HOH A . 
HA 5 HOH   407 2107 1622 HOH   HOH A . 
HA 5 HOH   408 2108 1366 HOH   HOH A . 
HA 5 HOH   409 2109 1347 HOH   HOH A . 
HA 5 HOH   410 2110 522  HOH   HOH A . 
HA 5 HOH   411 2111 1340 HOH   HOH A . 
HA 5 HOH   412 2112 416  HOH   HOH A . 
HA 5 HOH   413 2113 1442 HOH   HOH A . 
IA 5 HOH   1   401  1444 HOH   HOH B . 
IA 5 HOH   2   402  40   HOH   HOH B . 
IA 5 HOH   3   403  939  HOH   HOH B . 
IA 5 HOH   4   404  962  HOH   HOH B . 
IA 5 HOH   5   405  120  HOH   HOH B . 
IA 5 HOH   6   406  641  HOH   HOH B . 
IA 5 HOH   7   407  1024 HOH   HOH B . 
IA 5 HOH   8   408  911  HOH   HOH B . 
IA 5 HOH   9   409  1105 HOH   HOH B . 
IA 5 HOH   10  410  106  HOH   HOH B . 
IA 5 HOH   11  411  825  HOH   HOH B . 
IA 5 HOH   12  412  550  HOH   HOH B . 
IA 5 HOH   13  413  1156 HOH   HOH B . 
IA 5 HOH   14  414  1394 HOH   HOH B . 
IA 5 HOH   15  415  699  HOH   HOH B . 
IA 5 HOH   16  416  753  HOH   HOH B . 
IA 5 HOH   17  417  737  HOH   HOH B . 
IA 5 HOH   18  418  119  HOH   HOH B . 
IA 5 HOH   19  419  847  HOH   HOH B . 
IA 5 HOH   20  420  1328 HOH   HOH B . 
IA 5 HOH   21  421  1700 HOH   HOH B . 
IA 5 HOH   22  422  660  HOH   HOH B . 
IA 5 HOH   23  423  1492 HOH   HOH B . 
IA 5 HOH   24  424  216  HOH   HOH B . 
IA 5 HOH   25  425  1212 HOH   HOH B . 
IA 5 HOH   26  426  1656 HOH   HOH B . 
IA 5 HOH   27  427  245  HOH   HOH B . 
IA 5 HOH   28  428  258  HOH   HOH B . 
IA 5 HOH   29  429  544  HOH   HOH B . 
IA 5 HOH   30  430  961  HOH   HOH B . 
IA 5 HOH   31  431  1405 HOH   HOH B . 
IA 5 HOH   32  432  22   HOH   HOH B . 
IA 5 HOH   33  433  670  HOH   HOH B . 
IA 5 HOH   34  434  334  HOH   HOH B . 
IA 5 HOH   35  435  435  HOH   HOH B . 
IA 5 HOH   36  436  1301 HOH   HOH B . 
IA 5 HOH   37  437  195  HOH   HOH B . 
IA 5 HOH   38  438  505  HOH   HOH B . 
IA 5 HOH   39  439  510  HOH   HOH B . 
IA 5 HOH   40  440  999  HOH   HOH B . 
IA 5 HOH   41  441  342  HOH   HOH B . 
IA 5 HOH   42  442  83   HOH   HOH B . 
IA 5 HOH   43  443  299  HOH   HOH B . 
IA 5 HOH   44  444  1135 HOH   HOH B . 
IA 5 HOH   45  445  243  HOH   HOH B . 
IA 5 HOH   46  446  719  HOH   HOH B . 
IA 5 HOH   47  447  509  HOH   HOH B . 
IA 5 HOH   48  448  1279 HOH   HOH B . 
IA 5 HOH   49  449  187  HOH   HOH B . 
IA 5 HOH   50  450  1021 HOH   HOH B . 
IA 5 HOH   51  451  793  HOH   HOH B . 
IA 5 HOH   52  452  34   HOH   HOH B . 
IA 5 HOH   53  453  277  HOH   HOH B . 
IA 5 HOH   54  454  92   HOH   HOH B . 
IA 5 HOH   55  455  203  HOH   HOH B . 
IA 5 HOH   56  456  215  HOH   HOH B . 
IA 5 HOH   57  457  75   HOH   HOH B . 
IA 5 HOH   58  458  33   HOH   HOH B . 
IA 5 HOH   59  459  1133 HOH   HOH B . 
IA 5 HOH   60  460  321  HOH   HOH B . 
IA 5 HOH   61  461  684  HOH   HOH B . 
IA 5 HOH   62  462  1166 HOH   HOH B . 
IA 5 HOH   63  463  1507 HOH   HOH B . 
IA 5 HOH   64  464  1647 HOH   HOH B . 
IA 5 HOH   65  465  1100 HOH   HOH B . 
IA 5 HOH   66  466  95   HOH   HOH B . 
IA 5 HOH   67  467  1446 HOH   HOH B . 
IA 5 HOH   68  468  113  HOH   HOH B . 
IA 5 HOH   69  469  705  HOH   HOH B . 
IA 5 HOH   70  470  377  HOH   HOH B . 
IA 5 HOH   71  471  143  HOH   HOH B . 
IA 5 HOH   72  472  414  HOH   HOH B . 
IA 5 HOH   73  473  114  HOH   HOH B . 
IA 5 HOH   74  474  1125 HOH   HOH B . 
IA 5 HOH   75  475  697  HOH   HOH B . 
IA 5 HOH   76  476  1625 HOH   HOH B . 
IA 5 HOH   77  477  901  HOH   HOH B . 
IA 5 HOH   78  478  288  HOH   HOH B . 
IA 5 HOH   79  479  8    HOH   HOH B . 
IA 5 HOH   80  480  577  HOH   HOH B . 
IA 5 HOH   81  481  1086 HOH   HOH B . 
IA 5 HOH   82  482  742  HOH   HOH B . 
IA 5 HOH   83  483  1023 HOH   HOH B . 
IA 5 HOH   84  484  683  HOH   HOH B . 
IA 5 HOH   85  485  802  HOH   HOH B . 
IA 5 HOH   86  486  166  HOH   HOH B . 
IA 5 HOH   87  487  137  HOH   HOH B . 
IA 5 HOH   88  488  1699 HOH   HOH B . 
IA 5 HOH   89  489  79   HOH   HOH B . 
IA 5 HOH   90  490  160  HOH   HOH B . 
IA 5 HOH   91  491  56   HOH   HOH B . 
IA 5 HOH   92  492  630  HOH   HOH B . 
IA 5 HOH   93  493  744  HOH   HOH B . 
IA 5 HOH   94  494  1602 HOH   HOH B . 
IA 5 HOH   95  495  399  HOH   HOH B . 
IA 5 HOH   96  496  261  HOH   HOH B . 
IA 5 HOH   97  497  86   HOH   HOH B . 
IA 5 HOH   98  498  1560 HOH   HOH B . 
IA 5 HOH   99  499  13   HOH   HOH B . 
IA 5 HOH   100 500  864  HOH   HOH B . 
IA 5 HOH   101 501  231  HOH   HOH B . 
IA 5 HOH   102 502  466  HOH   HOH B . 
IA 5 HOH   103 503  246  HOH   HOH B . 
IA 5 HOH   104 504  175  HOH   HOH B . 
IA 5 HOH   105 505  318  HOH   HOH B . 
IA 5 HOH   106 506  456  HOH   HOH B . 
IA 5 HOH   107 507  441  HOH   HOH B . 
IA 5 HOH   108 508  362  HOH   HOH B . 
IA 5 HOH   109 509  453  HOH   HOH B . 
IA 5 HOH   110 510  1474 HOH   HOH B . 
IA 5 HOH   111 511  1380 HOH   HOH B . 
IA 5 HOH   112 512  490  HOH   HOH B . 
IA 5 HOH   113 513  213  HOH   HOH B . 
IA 5 HOH   114 514  78   HOH   HOH B . 
IA 5 HOH   115 515  860  HOH   HOH B . 
IA 5 HOH   116 516  828  HOH   HOH B . 
IA 5 HOH   117 517  274  HOH   HOH B . 
IA 5 HOH   118 518  565  HOH   HOH B . 
IA 5 HOH   119 519  72   HOH   HOH B . 
IA 5 HOH   120 520  1346 HOH   HOH B . 
IA 5 HOH   121 521  899  HOH   HOH B . 
IA 5 HOH   122 522  582  HOH   HOH B . 
IA 5 HOH   123 523  1648 HOH   HOH B . 
IA 5 HOH   124 524  1276 HOH   HOH B . 
IA 5 HOH   125 525  35   HOH   HOH B . 
IA 5 HOH   126 526  1406 HOH   HOH B . 
IA 5 HOH   127 527  244  HOH   HOH B . 
IA 5 HOH   128 528  356  HOH   HOH B . 
IA 5 HOH   129 529  827  HOH   HOH B . 
IA 5 HOH   130 530  1338 HOH   HOH B . 
IA 5 HOH   131 531  530  HOH   HOH B . 
IA 5 HOH   132 532  721  HOH   HOH B . 
IA 5 HOH   133 533  798  HOH   HOH B . 
IA 5 HOH   134 534  482  HOH   HOH B . 
IA 5 HOH   135 535  495  HOH   HOH B . 
IA 5 HOH   136 536  256  HOH   HOH B . 
IA 5 HOH   137 537  471  HOH   HOH B . 
IA 5 HOH   138 538  192  HOH   HOH B . 
IA 5 HOH   139 539  406  HOH   HOH B . 
IA 5 HOH   140 540  51   HOH   HOH B . 
IA 5 HOH   141 541  863  HOH   HOH B . 
IA 5 HOH   142 542  1208 HOH   HOH B . 
IA 5 HOH   143 543  716  HOH   HOH B . 
IA 5 HOH   144 544  223  HOH   HOH B . 
IA 5 HOH   145 545  988  HOH   HOH B . 
IA 5 HOH   146 546  1616 HOH   HOH B . 
IA 5 HOH   147 547  652  HOH   HOH B . 
IA 5 HOH   148 548  1228 HOH   HOH B . 
IA 5 HOH   149 549  325  HOH   HOH B . 
IA 5 HOH   150 550  1518 HOH   HOH B . 
IA 5 HOH   151 551  386  HOH   HOH B . 
IA 5 HOH   152 552  423  HOH   HOH B . 
IA 5 HOH   153 553  164  HOH   HOH B . 
IA 5 HOH   154 554  749  HOH   HOH B . 
IA 5 HOH   155 555  1684 HOH   HOH B . 
IA 5 HOH   156 556  655  HOH   HOH B . 
IA 5 HOH   157 557  1294 HOH   HOH B . 
IA 5 HOH   158 558  426  HOH   HOH B . 
IA 5 HOH   159 559  1124 HOH   HOH B . 
IA 5 HOH   160 560  1146 HOH   HOH B . 
IA 5 HOH   161 561  862  HOH   HOH B . 
IA 5 HOH   162 562  806  HOH   HOH B . 
IA 5 HOH   163 563  1216 HOH   HOH B . 
IA 5 HOH   164 564  364  HOH   HOH B . 
IA 5 HOH   165 565  810  HOH   HOH B . 
IA 5 HOH   166 566  1062 HOH   HOH B . 
IA 5 HOH   167 567  121  HOH   HOH B . 
IA 5 HOH   168 568  926  HOH   HOH B . 
IA 5 HOH   169 569  1101 HOH   HOH B . 
IA 5 HOH   170 570  1513 HOH   HOH B . 
IA 5 HOH   171 571  100  HOH   HOH B . 
IA 5 HOH   172 572  1238 HOH   HOH B . 
IA 5 HOH   173 573  600  HOH   HOH B . 
IA 5 HOH   174 574  220  HOH   HOH B . 
IA 5 HOH   175 575  604  HOH   HOH B . 
IA 5 HOH   176 576  1013 HOH   HOH B . 
IA 5 HOH   177 577  1056 HOH   HOH B . 
IA 5 HOH   178 578  1006 HOH   HOH B . 
IA 5 HOH   179 579  836  HOH   HOH B . 
IA 5 HOH   180 580  395  HOH   HOH B . 
IA 5 HOH   181 581  502  HOH   HOH B . 
IA 5 HOH   182 582  1707 HOH   HOH B . 
IA 5 HOH   183 583  533  HOH   HOH B . 
IA 5 HOH   184 584  924  HOH   HOH B . 
IA 5 HOH   185 585  612  HOH   HOH B . 
IA 5 HOH   186 586  335  HOH   HOH B . 
IA 5 HOH   187 587  789  HOH   HOH B . 
IA 5 HOH   188 588  262  HOH   HOH B . 
IA 5 HOH   189 589  235  HOH   HOH B . 
IA 5 HOH   190 590  267  HOH   HOH B . 
IA 5 HOH   191 591  1074 HOH   HOH B . 
IA 5 HOH   192 592  484  HOH   HOH B . 
IA 5 HOH   193 593  781  HOH   HOH B . 
IA 5 HOH   194 594  893  HOH   HOH B . 
IA 5 HOH   195 595  23   HOH   HOH B . 
IA 5 HOH   196 596  1160 HOH   HOH B . 
IA 5 HOH   197 597  465  HOH   HOH B . 
IA 5 HOH   198 598  578  HOH   HOH B . 
IA 5 HOH   199 599  965  HOH   HOH B . 
IA 5 HOH   200 600  986  HOH   HOH B . 
IA 5 HOH   201 601  1157 HOH   HOH B . 
IA 5 HOH   202 602  1000 HOH   HOH B . 
IA 5 HOH   203 603  859  HOH   HOH B . 
IA 5 HOH   204 604  620  HOH   HOH B . 
IA 5 HOH   205 605  341  HOH   HOH B . 
IA 5 HOH   206 606  281  HOH   HOH B . 
IA 5 HOH   207 607  1692 HOH   HOH B . 
IA 5 HOH   208 608  647  HOH   HOH B . 
IA 5 HOH   209 609  58   HOH   HOH B . 
IA 5 HOH   210 610  1037 HOH   HOH B . 
IA 5 HOH   211 611  1550 HOH   HOH B . 
IA 5 HOH   212 612  570  HOH   HOH B . 
IA 5 HOH   213 613  1087 HOH   HOH B . 
IA 5 HOH   214 614  1165 HOH   HOH B . 
IA 5 HOH   215 615  771  HOH   HOH B . 
IA 5 HOH   216 616  865  HOH   HOH B . 
IA 5 HOH   217 617  329  HOH   HOH B . 
IA 5 HOH   218 618  1681 HOH   HOH B . 
IA 5 HOH   219 619  310  HOH   HOH B . 
IA 5 HOH   220 620  1150 HOH   HOH B . 
IA 5 HOH   221 621  852  HOH   HOH B . 
IA 5 HOH   222 622  1594 HOH   HOH B . 
IA 5 HOH   223 623  478  HOH   HOH B . 
IA 5 HOH   224 624  1705 HOH   HOH B . 
IA 5 HOH   225 625  912  HOH   HOH B . 
IA 5 HOH   226 626  1120 HOH   HOH B . 
IA 5 HOH   227 627  130  HOH   HOH B . 
IA 5 HOH   228 628  1339 HOH   HOH B . 
IA 5 HOH   229 629  1408 HOH   HOH B . 
IA 5 HOH   230 630  1490 HOH   HOH B . 
IA 5 HOH   231 631  519  HOH   HOH B . 
IA 5 HOH   232 632  745  HOH   HOH B . 
IA 5 HOH   233 633  832  HOH   HOH B . 
IA 5 HOH   234 634  392  HOH   HOH B . 
IA 5 HOH   235 635  383  HOH   HOH B . 
IA 5 HOH   236 636  363  HOH   HOH B . 
IA 5 HOH   237 637  196  HOH   HOH B . 
IA 5 HOH   238 638  1440 HOH   HOH B . 
IA 5 HOH   239 639  1582 HOH   HOH B . 
IA 5 HOH   240 640  133  HOH   HOH B . 
IA 5 HOH   241 641  1432 HOH   HOH B . 
IA 5 HOH   242 642  779  HOH   HOH B . 
IA 5 HOH   243 643  608  HOH   HOH B . 
IA 5 HOH   244 644  740  HOH   HOH B . 
IA 5 HOH   245 645  634  HOH   HOH B . 
IA 5 HOH   246 646  536  HOH   HOH B . 
IA 5 HOH   247 647  1213 HOH   HOH B . 
IA 5 HOH   248 648  204  HOH   HOH B . 
IA 5 HOH   249 649  1489 HOH   HOH B . 
IA 5 HOH   250 650  868  HOH   HOH B . 
IA 5 HOH   251 651  1578 HOH   HOH B . 
IA 5 HOH   252 652  308  HOH   HOH B . 
IA 5 HOH   253 653  568  HOH   HOH B . 
IA 5 HOH   254 654  569  HOH   HOH B . 
IA 5 HOH   255 655  1059 HOH   HOH B . 
IA 5 HOH   256 656  1689 HOH   HOH B . 
IA 5 HOH   257 657  1375 HOH   HOH B . 
IA 5 HOH   258 658  1455 HOH   HOH B . 
IA 5 HOH   259 659  584  HOH   HOH B . 
IA 5 HOH   260 660  1045 HOH   HOH B . 
IA 5 HOH   261 661  309  HOH   HOH B . 
IA 5 HOH   262 662  230  HOH   HOH B . 
IA 5 HOH   263 663  1080 HOH   HOH B . 
IA 5 HOH   264 664  1122 HOH   HOH B . 
IA 5 HOH   265 665  1589 HOH   HOH B . 
IA 5 HOH   266 666  391  HOH   HOH B . 
IA 5 HOH   267 667  316  HOH   HOH B . 
IA 5 HOH   268 668  1559 HOH   HOH B . 
IA 5 HOH   269 669  1179 HOH   HOH B . 
IA 5 HOH   270 670  518  HOH   HOH B . 
IA 5 HOH   271 671  148  HOH   HOH B . 
IA 5 HOH   272 672  440  HOH   HOH B . 
IA 5 HOH   273 673  1706 HOH   HOH B . 
IA 5 HOH   274 674  1636 HOH   HOH B . 
IA 5 HOH   275 675  1316 HOH   HOH B . 
IA 5 HOH   276 676  963  HOH   HOH B . 
IA 5 HOH   277 677  1171 HOH   HOH B . 
IA 5 HOH   278 678  1479 HOH   HOH B . 
IA 5 HOH   279 679  158  HOH   HOH B . 
IA 5 HOH   280 680  861  HOH   HOH B . 
IA 5 HOH   281 681  580  HOH   HOH B . 
IA 5 HOH   282 682  404  HOH   HOH B . 
IA 5 HOH   283 683  1702 HOH   HOH B . 
IA 5 HOH   284 684  4    HOH   HOH B . 
IA 5 HOH   285 685  1370 HOH   HOH B . 
IA 5 HOH   286 686  1627 HOH   HOH B . 
IA 5 HOH   287 687  765  HOH   HOH B . 
IA 5 HOH   288 688  1517 HOH   HOH B . 
IA 5 HOH   289 689  1269 HOH   HOH B . 
IA 5 HOH   290 690  9    HOH   HOH B . 
IA 5 HOH   291 691  494  HOH   HOH B . 
IA 5 HOH   292 692  1181 HOH   HOH B . 
IA 5 HOH   293 693  1307 HOH   HOH B . 
IA 5 HOH   294 694  1315 HOH   HOH B . 
IA 5 HOH   295 695  1358 HOH   HOH B . 
IA 5 HOH   296 696  1609 HOH   HOH B . 
IA 5 HOH   297 697  922  HOH   HOH B . 
IA 5 HOH   298 698  1063 HOH   HOH B . 
IA 5 HOH   299 699  1563 HOH   HOH B . 
IA 5 HOH   300 700  1562 HOH   HOH B . 
IA 5 HOH   301 701  1471 HOH   HOH B . 
IA 5 HOH   302 702  538  HOH   HOH B . 
IA 5 HOH   303 703  280  HOH   HOH B . 
IA 5 HOH   304 704  867  HOH   HOH B . 
IA 5 HOH   305 705  1367 HOH   HOH B . 
IA 5 HOH   306 706  1473 HOH   HOH B . 
IA 5 HOH   307 707  1004 HOH   HOH B . 
IA 5 HOH   308 708  1173 HOH   HOH B . 
IA 5 HOH   309 709  1617 HOH   HOH B . 
IA 5 HOH   310 710  17   HOH   HOH B . 
IA 5 HOH   311 711  1250 HOH   HOH B . 
IA 5 HOH   312 712  1094 HOH   HOH B . 
IA 5 HOH   313 713  1336 HOH   HOH B . 
IA 5 HOH   314 714  1224 HOH   HOH B . 
IA 5 HOH   315 715  512  HOH   HOH B . 
IA 5 HOH   316 716  396  HOH   HOH B . 
IA 5 HOH   317 717  167  HOH   HOH B . 
IA 5 HOH   318 718  1286 HOH   HOH B . 
IA 5 HOH   319 719  1211 HOH   HOH B . 
IA 5 HOH   320 720  1334 HOH   HOH B . 
IA 5 HOH   321 721  648  HOH   HOH B . 
IA 5 HOH   322 722  1064 HOH   HOH B . 
IA 5 HOH   323 723  1098 HOH   HOH B . 
IA 5 HOH   324 724  1019 HOH   HOH B . 
IA 5 HOH   325 725  1453 HOH   HOH B . 
IA 5 HOH   326 726  1475 HOH   HOH B . 
IA 5 HOH   327 727  1129 HOH   HOH B . 
IA 5 HOH   328 728  1503 HOH   HOH B . 
IA 5 HOH   329 729  636  HOH   HOH B . 
IA 5 HOH   330 730  1577 HOH   HOH B . 
IA 5 HOH   331 731  833  HOH   HOH B . 
IA 5 HOH   332 732  1646 HOH   HOH B . 
IA 5 HOH   333 733  787  HOH   HOH B . 
IA 5 HOH   334 734  1174 HOH   HOH B . 
IA 5 HOH   335 735  892  HOH   HOH B . 
IA 5 HOH   336 736  984  HOH   HOH B . 
IA 5 HOH   337 737  46   HOH   HOH B . 
IA 5 HOH   338 738  1583 HOH   HOH B . 
IA 5 HOH   339 739  1476 HOH   HOH B . 
IA 5 HOH   340 740  1576 HOH   HOH B . 
IA 5 HOH   341 741  1397 HOH   HOH B . 
IA 5 HOH   342 742  1436 HOH   HOH B . 
IA 5 HOH   343 743  1355 HOH   HOH B . 
IA 5 HOH   344 744  1533 HOH   HOH B . 
IA 5 HOH   345 745  1488 HOH   HOH B . 
IA 5 HOH   346 746  1153 HOH   HOH B . 
IA 5 HOH   347 747  866  HOH   HOH B . 
IA 5 HOH   348 748  741  HOH   HOH B . 
IA 5 HOH   349 749  681  HOH   HOH B . 
IA 5 HOH   350 750  1688 HOH   HOH B . 
IA 5 HOH   351 751  1280 HOH   HOH B . 
IA 5 HOH   352 752  1239 HOH   HOH B . 
IA 5 HOH   353 753  1043 HOH   HOH B . 
IA 5 HOH   354 754  758  HOH   HOH B . 
IA 5 HOH   355 755  1429 HOH   HOH B . 
IA 5 HOH   356 756  1272 HOH   HOH B . 
IA 5 HOH   357 757  1192 HOH   HOH B . 
IA 5 HOH   358 758  850  HOH   HOH B . 
IA 5 HOH   359 759  172  HOH   HOH B . 
IA 5 HOH   360 760  663  HOH   HOH B . 
IA 5 HOH   361 761  1519 HOH   HOH B . 
IA 5 HOH   362 762  734  HOH   HOH B . 
IA 5 HOH   363 763  1368 HOH   HOH B . 
IA 5 HOH   364 764  1182 HOH   HOH B . 
IA 5 HOH   365 765  1452 HOH   HOH B . 
IA 5 HOH   366 766  674  HOH   HOH B . 
IA 5 HOH   367 767  1364 HOH   HOH B . 
IA 5 HOH   368 768  1643 HOH   HOH B . 
IA 5 HOH   369 769  1439 HOH   HOH B . 
IA 5 HOH   370 770  969  HOH   HOH B . 
IA 5 HOH   371 771  1660 HOH   HOH B . 
IA 5 HOH   372 772  1291 HOH   HOH B . 
IA 5 HOH   373 773  1356 HOH   HOH B . 
IA 5 HOH   374 774  1175 HOH   HOH B . 
IA 5 HOH   375 775  1664 HOH   HOH B . 
IA 5 HOH   376 776  735  HOH   HOH B . 
IA 5 HOH   377 777  1002 HOH   HOH B . 
IA 5 HOH   378 778  1708 HOH   HOH B . 
IA 5 HOH   379 779  1012 HOH   HOH B . 
IA 5 HOH   380 780  1459 HOH   HOH B . 
IA 5 HOH   381 781  1531 HOH   HOH B . 
IA 5 HOH   382 782  1177 HOH   HOH B . 
IA 5 HOH   383 783  1061 HOH   HOH B . 
IA 5 HOH   384 784  1491 HOH   HOH B . 
IA 5 HOH   385 785  657  HOH   HOH B . 
IA 5 HOH   386 786  956  HOH   HOH B . 
IA 5 HOH   387 787  1141 HOH   HOH B . 
IA 5 HOH   388 788  817  HOH   HOH B . 
IA 5 HOH   389 789  1497 HOH   HOH B . 
IA 5 HOH   390 790  1388 HOH   HOH B . 
IA 5 HOH   391 791  1284 HOH   HOH B . 
IA 5 HOH   392 792  1196 HOH   HOH B . 
IA 5 HOH   393 793  1653 HOH   HOH B . 
IA 5 HOH   394 794  1377 HOH   HOH B . 
IA 5 HOH   395 795  772  HOH   HOH B . 
IA 5 HOH   396 796  931  HOH   HOH B . 
IA 5 HOH   397 797  1030 HOH   HOH B . 
IA 5 HOH   398 798  1626 HOH   HOH B . 
IA 5 HOH   399 799  1310 HOH   HOH B . 
IA 5 HOH   400 800  1304 HOH   HOH B . 
IA 5 HOH   401 801  1295 HOH   HOH B . 
IA 5 HOH   402 802  1206 HOH   HOH B . 
IA 5 HOH   403 803  701  HOH   HOH B . 
IA 5 HOH   404 804  664  HOH   HOH B . 
IA 5 HOH   405 805  1642 HOH   HOH B . 
IA 5 HOH   406 806  1226 HOH   HOH B . 
IA 5 HOH   407 807  1450 HOH   HOH B . 
IA 5 HOH   408 808  352  HOH   HOH B . 
IA 5 HOH   409 809  1240 HOH   HOH B . 
IA 5 HOH   410 810  594  HOH   HOH B . 
IA 5 HOH   411 811  693  HOH   HOH B . 
IA 5 HOH   412 812  1373 HOH   HOH B . 
IA 5 HOH   413 813  553  HOH   HOH B . 
IA 5 HOH   414 814  431  HOH   HOH B . 
IA 5 HOH   415 815  1545 HOH   HOH B . 
JA 5 HOH   1   401  42   HOH   HOH C . 
JA 5 HOH   2   402  1091 HOH   HOH C . 
JA 5 HOH   3   403  136  HOH   HOH C . 
JA 5 HOH   4   404  1029 HOH   HOH C . 
JA 5 HOH   5   405  197  HOH   HOH C . 
JA 5 HOH   6   406  603  HOH   HOH C . 
JA 5 HOH   7   407  1219 HOH   HOH C . 
JA 5 HOH   8   408  897  HOH   HOH C . 
JA 5 HOH   9   409  662  HOH   HOH C . 
JA 5 HOH   10  410  424  HOH   HOH C . 
JA 5 HOH   11  411  135  HOH   HOH C . 
JA 5 HOH   12  412  239  HOH   HOH C . 
JA 5 HOH   13  413  1149 HOH   HOH C . 
JA 5 HOH   14  414  127  HOH   HOH C . 
JA 5 HOH   15  415  485  HOH   HOH C . 
JA 5 HOH   16  416  18   HOH   HOH C . 
JA 5 HOH   17  417  908  HOH   HOH C . 
JA 5 HOH   18  418  250  HOH   HOH C . 
JA 5 HOH   19  419  1341 HOH   HOH C . 
JA 5 HOH   20  420  1049 HOH   HOH C . 
JA 5 HOH   21  421  729  HOH   HOH C . 
JA 5 HOH   22  422  1357 HOH   HOH C . 
JA 5 HOH   23  423  928  HOH   HOH C . 
JA 5 HOH   24  424  206  HOH   HOH C . 
JA 5 HOH   25  425  307  HOH   HOH C . 
JA 5 HOH   26  426  653  HOH   HOH C . 
JA 5 HOH   27  427  1484 HOH   HOH C . 
JA 5 HOH   28  428  1207 HOH   HOH C . 
JA 5 HOH   29  429  1203 HOH   HOH C . 
JA 5 HOH   30  430  632  HOH   HOH C . 
JA 5 HOH   31  431  658  HOH   HOH C . 
JA 5 HOH   32  432  202  HOH   HOH C . 
JA 5 HOH   33  433  1069 HOH   HOH C . 
JA 5 HOH   34  434  472  HOH   HOH C . 
JA 5 HOH   35  435  762  HOH   HOH C . 
JA 5 HOH   36  436  73   HOH   HOH C . 
JA 5 HOH   37  437  1273 HOH   HOH C . 
JA 5 HOH   38  438  67   HOH   HOH C . 
JA 5 HOH   39  439  1674 HOH   HOH C . 
JA 5 HOH   40  440  1553 HOH   HOH C . 
JA 5 HOH   41  441  328  HOH   HOH C . 
JA 5 HOH   42  442  841  HOH   HOH C . 
JA 5 HOH   43  443  1225 HOH   HOH C . 
JA 5 HOH   44  444  32   HOH   HOH C . 
JA 5 HOH   45  445  278  HOH   HOH C . 
JA 5 HOH   46  446  29   HOH   HOH C . 
JA 5 HOH   47  447  898  HOH   HOH C . 
JA 5 HOH   48  448  714  HOH   HOH C . 
JA 5 HOH   49  449  764  HOH   HOH C . 
JA 5 HOH   50  450  776  HOH   HOH C . 
JA 5 HOH   51  451  43   HOH   HOH C . 
JA 5 HOH   52  452  1574 HOH   HOH C . 
JA 5 HOH   53  453  211  HOH   HOH C . 
JA 5 HOH   54  454  170  HOH   HOH C . 
JA 5 HOH   55  455  171  HOH   HOH C . 
JA 5 HOH   56  456  65   HOH   HOH C . 
JA 5 HOH   57  457  1147 HOH   HOH C . 
JA 5 HOH   58  458  951  HOH   HOH C . 
JA 5 HOH   59  459  297  HOH   HOH C . 
JA 5 HOH   60  460  1575 HOH   HOH C . 
JA 5 HOH   61  461  1510 HOH   HOH C . 
JA 5 HOH   62  462  675  HOH   HOH C . 
JA 5 HOH   63  463  672  HOH   HOH C . 
JA 5 HOH   64  464  403  HOH   HOH C . 
JA 5 HOH   65  465  343  HOH   HOH C . 
JA 5 HOH   66  466  6    HOH   HOH C . 
JA 5 HOH   67  467  676  HOH   HOH C . 
JA 5 HOH   68  468  1431 HOH   HOH C . 
JA 5 HOH   69  469  1530 HOH   HOH C . 
JA 5 HOH   70  470  437  HOH   HOH C . 
JA 5 HOH   71  471  14   HOH   HOH C . 
JA 5 HOH   72  472  191  HOH   HOH C . 
JA 5 HOH   73  473  527  HOH   HOH C . 
JA 5 HOH   74  474  442  HOH   HOH C . 
JA 5 HOH   75  475  555  HOH   HOH C . 
JA 5 HOH   76  476  131  HOH   HOH C . 
JA 5 HOH   77  477  183  HOH   HOH C . 
JA 5 HOH   78  478  214  HOH   HOH C . 
JA 5 HOH   79  479  470  HOH   HOH C . 
JA 5 HOH   80  480  103  HOH   HOH C . 
JA 5 HOH   81  481  656  HOH   HOH C . 
JA 5 HOH   82  482  1590 HOH   HOH C . 
JA 5 HOH   83  483  371  HOH   HOH C . 
JA 5 HOH   84  484  71   HOH   HOH C . 
JA 5 HOH   85  485  88   HOH   HOH C . 
JA 5 HOH   86  486  1083 HOH   HOH C . 
JA 5 HOH   87  487  249  HOH   HOH C . 
JA 5 HOH   88  488  251  HOH   HOH C . 
JA 5 HOH   89  489  1142 HOH   HOH C . 
JA 5 HOH   90  490  469  HOH   HOH C . 
JA 5 HOH   91  491  491  HOH   HOH C . 
JA 5 HOH   92  492  626  HOH   HOH C . 
JA 5 HOH   93  493  97   HOH   HOH C . 
JA 5 HOH   94  494  481  HOH   HOH C . 
JA 5 HOH   95  495  535  HOH   HOH C . 
JA 5 HOH   96  496  105  HOH   HOH C . 
JA 5 HOH   97  497  345  HOH   HOH C . 
JA 5 HOH   98  498  995  HOH   HOH C . 
JA 5 HOH   99  499  809  HOH   HOH C . 
JA 5 HOH   100 500  794  HOH   HOH C . 
JA 5 HOH   101 501  181  HOH   HOH C . 
JA 5 HOH   102 502  640  HOH   HOH C . 
JA 5 HOH   103 503  290  HOH   HOH C . 
JA 5 HOH   104 504  1185 HOH   HOH C . 
JA 5 HOH   105 505  179  HOH   HOH C . 
JA 5 HOH   106 506  355  HOH   HOH C . 
JA 5 HOH   107 507  1417 HOH   HOH C . 
JA 5 HOH   108 508  107  HOH   HOH C . 
JA 5 HOH   109 509  849  HOH   HOH C . 
JA 5 HOH   110 510  831  HOH   HOH C . 
JA 5 HOH   111 511  174  HOH   HOH C . 
JA 5 HOH   112 512  551  HOH   HOH C . 
JA 5 HOH   113 513  623  HOH   HOH C . 
JA 5 HOH   114 514  1587 HOH   HOH C . 
JA 5 HOH   115 515  455  HOH   HOH C . 
JA 5 HOH   116 516  720  HOH   HOH C . 
JA 5 HOH   117 517  200  HOH   HOH C . 
JA 5 HOH   118 518  952  HOH   HOH C . 
JA 5 HOH   119 519  1509 HOH   HOH C . 
JA 5 HOH   120 520  264  HOH   HOH C . 
JA 5 HOH   121 521  677  HOH   HOH C . 
JA 5 HOH   122 522  937  HOH   HOH C . 
JA 5 HOH   123 523  694  HOH   HOH C . 
JA 5 HOH   124 524  317  HOH   HOH C . 
JA 5 HOH   125 525  805  HOH   HOH C . 
JA 5 HOH   126 526  834  HOH   HOH C . 
JA 5 HOH   127 527  259  HOH   HOH C . 
JA 5 HOH   128 528  61   HOH   HOH C . 
JA 5 HOH   129 529  36   HOH   HOH C . 
JA 5 HOH   130 530  375  HOH   HOH C . 
JA 5 HOH   131 531  678  HOH   HOH C . 
JA 5 HOH   132 532  77   HOH   HOH C . 
JA 5 HOH   133 533  323  HOH   HOH C . 
JA 5 HOH   134 534  820  HOH   HOH C . 
JA 5 HOH   135 535  1145 HOH   HOH C . 
JA 5 HOH   136 536  226  HOH   HOH C . 
JA 5 HOH   137 537  1162 HOH   HOH C . 
JA 5 HOH   138 538  493  HOH   HOH C . 
JA 5 HOH   139 539  997  HOH   HOH C . 
JA 5 HOH   140 540  625  HOH   HOH C . 
JA 5 HOH   141 541  176  HOH   HOH C . 
JA 5 HOH   142 542  710  HOH   HOH C . 
JA 5 HOH   143 543  169  HOH   HOH C . 
JA 5 HOH   144 544  63   HOH   HOH C . 
JA 5 HOH   145 545  770  HOH   HOH C . 
JA 5 HOH   146 546  419  HOH   HOH C . 
JA 5 HOH   147 547  463  HOH   HOH C . 
JA 5 HOH   148 548  45   HOH   HOH C . 
JA 5 HOH   149 549  812  HOH   HOH C . 
JA 5 HOH   150 550  605  HOH   HOH C . 
JA 5 HOH   151 551  1480 HOH   HOH C . 
JA 5 HOH   152 552  796  HOH   HOH C . 
JA 5 HOH   153 553  1274 HOH   HOH C . 
JA 5 HOH   154 554  1607 HOH   HOH C . 
JA 5 HOH   155 555  385  HOH   HOH C . 
JA 5 HOH   156 556  790  HOH   HOH C . 
JA 5 HOH   157 557  797  HOH   HOH C . 
JA 5 HOH   158 558  397  HOH   HOH C . 
JA 5 HOH   159 559  870  HOH   HOH C . 
JA 5 HOH   160 560  1508 HOH   HOH C . 
JA 5 HOH   161 561  930  HOH   HOH C . 
JA 5 HOH   162 562  468  HOH   HOH C . 
JA 5 HOH   163 563  1657 HOH   HOH C . 
JA 5 HOH   164 564  574  HOH   HOH C . 
JA 5 HOH   165 565  1131 HOH   HOH C . 
JA 5 HOH   166 566  1687 HOH   HOH C . 
JA 5 HOH   167 567  503  HOH   HOH C . 
JA 5 HOH   168 568  614  HOH   HOH C . 
JA 5 HOH   169 569  1138 HOH   HOH C . 
JA 5 HOH   170 570  434  HOH   HOH C . 
JA 5 HOH   171 571  511  HOH   HOH C . 
JA 5 HOH   172 572  1193 HOH   HOH C . 
JA 5 HOH   173 573  1058 HOH   HOH C . 
JA 5 HOH   174 574  564  HOH   HOH C . 
JA 5 HOH   175 575  1210 HOH   HOH C . 
JA 5 HOH   176 576  301  HOH   HOH C . 
JA 5 HOH   177 577  1025 HOH   HOH C . 
JA 5 HOH   178 578  543  HOH   HOH C . 
JA 5 HOH   179 579  1552 HOH   HOH C . 
JA 5 HOH   180 580  476  HOH   HOH C . 
JA 5 HOH   181 581  552  HOH   HOH C . 
JA 5 HOH   182 582  515  HOH   HOH C . 
JA 5 HOH   183 583  109  HOH   HOH C . 
JA 5 HOH   184 584  269  HOH   HOH C . 
JA 5 HOH   185 585  1569 HOH   HOH C . 
JA 5 HOH   186 586  542  HOH   HOH C . 
JA 5 HOH   187 587  938  HOH   HOH C . 
JA 5 HOH   188 588  275  HOH   HOH C . 
JA 5 HOH   189 589  1232 HOH   HOH C . 
JA 5 HOH   190 590  586  HOH   HOH C . 
JA 5 HOH   191 591  769  HOH   HOH C . 
JA 5 HOH   192 592  840  HOH   HOH C . 
JA 5 HOH   193 593  874  HOH   HOH C . 
JA 5 HOH   194 594  312  HOH   HOH C . 
JA 5 HOH   195 595  47   HOH   HOH C . 
JA 5 HOH   196 596  265  HOH   HOH C . 
JA 5 HOH   197 597  1257 HOH   HOH C . 
JA 5 HOH   198 598  1543 HOH   HOH C . 
JA 5 HOH   199 599  1041 HOH   HOH C . 
JA 5 HOH   200 600  904  HOH   HOH C . 
JA 5 HOH   201 601  382  HOH   HOH C . 
JA 5 HOH   202 602  733  HOH   HOH C . 
JA 5 HOH   203 603  857  HOH   HOH C . 
JA 5 HOH   204 604  689  HOH   HOH C . 
JA 5 HOH   205 605  129  HOH   HOH C . 
JA 5 HOH   206 606  324  HOH   HOH C . 
JA 5 HOH   207 607  783  HOH   HOH C . 
JA 5 HOH   208 608  1104 HOH   HOH C . 
JA 5 HOH   209 609  1615 HOH   HOH C . 
JA 5 HOH   210 610  993  HOH   HOH C . 
JA 5 HOH   211 611  627  HOH   HOH C . 
JA 5 HOH   212 612  633  HOH   HOH C . 
JA 5 HOH   213 613  372  HOH   HOH C . 
JA 5 HOH   214 614  617  HOH   HOH C . 
JA 5 HOH   215 615  1694 HOH   HOH C . 
JA 5 HOH   216 616  1639 HOH   HOH C . 
JA 5 HOH   217 617  972  HOH   HOH C . 
JA 5 HOH   218 618  1108 HOH   HOH C . 
JA 5 HOH   219 619  953  HOH   HOH C . 
JA 5 HOH   220 620  1235 HOH   HOH C . 
JA 5 HOH   221 621  754  HOH   HOH C . 
JA 5 HOH   222 622  780  HOH   HOH C . 
JA 5 HOH   223 623  566  HOH   HOH C . 
JA 5 HOH   224 624  573  HOH   HOH C . 
JA 5 HOH   225 625  713  HOH   HOH C . 
JA 5 HOH   226 626  413  HOH   HOH C . 
JA 5 HOH   227 627  547  HOH   HOH C . 
JA 5 HOH   228 628  1434 HOH   HOH C . 
JA 5 HOH   229 629  20   HOH   HOH C . 
JA 5 HOH   230 630  1695 HOH   HOH C . 
JA 5 HOH   231 631  125  HOH   HOH C . 
JA 5 HOH   232 632  477  HOH   HOH C . 
JA 5 HOH   233 633  430  HOH   HOH C . 
JA 5 HOH   234 634  1697 HOH   HOH C . 
JA 5 HOH   235 635  918  HOH   HOH C . 
JA 5 HOH   236 636  1054 HOH   HOH C . 
JA 5 HOH   237 637  1546 HOH   HOH C . 
JA 5 HOH   238 638  750  HOH   HOH C . 
JA 5 HOH   239 639  233  HOH   HOH C . 
JA 5 HOH   240 640  878  HOH   HOH C . 
JA 5 HOH   241 641  890  HOH   HOH C . 
JA 5 HOH   242 642  232  HOH   HOH C . 
JA 5 HOH   243 643  315  HOH   HOH C . 
JA 5 HOH   244 644  162  HOH   HOH C . 
JA 5 HOH   245 645  1504 HOH   HOH C . 
JA 5 HOH   246 646  142  HOH   HOH C . 
JA 5 HOH   247 647  751  HOH   HOH C . 
JA 5 HOH   248 648  1645 HOH   HOH C . 
JA 5 HOH   249 649  1359 HOH   HOH C . 
JA 5 HOH   250 650  1675 HOH   HOH C . 
JA 5 HOH   251 651  1117 HOH   HOH C . 
JA 5 HOH   252 652  425  HOH   HOH C . 
JA 5 HOH   253 653  851  HOH   HOH C . 
JA 5 HOH   254 654  1447 HOH   HOH C . 
JA 5 HOH   255 655  1483 HOH   HOH C . 
JA 5 HOH   256 656  1668 HOH   HOH C . 
JA 5 HOH   257 657  935  HOH   HOH C . 
JA 5 HOH   258 658  1082 HOH   HOH C . 
JA 5 HOH   259 659  1494 HOH   HOH C . 
JA 5 HOH   260 660  351  HOH   HOH C . 
JA 5 HOH   261 661  344  HOH   HOH C . 
JA 5 HOH   262 662  534  HOH   HOH C . 
JA 5 HOH   263 663  313  HOH   HOH C . 
JA 5 HOH   264 664  723  HOH   HOH C . 
JA 5 HOH   265 665  1420 HOH   HOH C . 
JA 5 HOH   266 666  1076 HOH   HOH C . 
JA 5 HOH   267 667  1220 HOH   HOH C . 
JA 5 HOH   268 668  1382 HOH   HOH C . 
JA 5 HOH   269 669  1354 HOH   HOH C . 
JA 5 HOH   270 670  1329 HOH   HOH C . 
JA 5 HOH   271 671  1555 HOH   HOH C . 
JA 5 HOH   272 672  525  HOH   HOH C . 
JA 5 HOH   273 673  1416 HOH   HOH C . 
JA 5 HOH   274 674  823  HOH   HOH C . 
JA 5 HOH   275 675  1312 HOH   HOH C . 
JA 5 HOH   276 676  1565 HOH   HOH C . 
JA 5 HOH   277 677  15   HOH   HOH C . 
JA 5 HOH   278 678  1669 HOH   HOH C . 
JA 5 HOH   279 679  1    HOH   HOH C . 
JA 5 HOH   280 680  529  HOH   HOH C . 
JA 5 HOH   281 681  454  HOH   HOH C . 
JA 5 HOH   282 682  1277 HOH   HOH C . 
JA 5 HOH   283 683  985  HOH   HOH C . 
JA 5 HOH   284 684  818  HOH   HOH C . 
JA 5 HOH   285 685  1467 HOH   HOH C . 
JA 5 HOH   286 686  1628 HOH   HOH C . 
JA 5 HOH   287 687  1073 HOH   HOH C . 
JA 5 HOH   288 688  1170 HOH   HOH C . 
JA 5 HOH   289 689  907  HOH   HOH C . 
JA 5 HOH   290 690  981  HOH   HOH C . 
JA 5 HOH   291 691  983  HOH   HOH C . 
JA 5 HOH   292 692  1418 HOH   HOH C . 
JA 5 HOH   293 693  1523 HOH   HOH C . 
JA 5 HOH   294 694  1333 HOH   HOH C . 
JA 5 HOH   295 695  302  HOH   HOH C . 
JA 5 HOH   296 696  1204 HOH   HOH C . 
JA 5 HOH   297 697  1461 HOH   HOH C . 
JA 5 HOH   298 698  1641 HOH   HOH C . 
JA 5 HOH   299 699  1663 HOH   HOH C . 
JA 5 HOH   300 700  16   HOH   HOH C . 
JA 5 HOH   301 701  1470 HOH   HOH C . 
JA 5 HOH   302 702  521  HOH   HOH C . 
JA 5 HOH   303 703  1428 HOH   HOH C . 
JA 5 HOH   304 704  1403 HOH   HOH C . 
JA 5 HOH   305 705  717  HOH   HOH C . 
JA 5 HOH   306 706  960  HOH   HOH C . 
JA 5 HOH   307 707  1075 HOH   HOH C . 
JA 5 HOH   308 708  168  HOH   HOH C . 
JA 5 HOH   309 709  517  HOH   HOH C . 
JA 5 HOH   310 710  405  HOH   HOH C . 
JA 5 HOH   311 711  1685 HOH   HOH C . 
JA 5 HOH   312 712  1293 HOH   HOH C . 
JA 5 HOH   313 713  696  HOH   HOH C . 
JA 5 HOH   314 714  1088 HOH   HOH C . 
JA 5 HOH   315 715  1158 HOH   HOH C . 
JA 5 HOH   316 716  1107 HOH   HOH C . 
JA 5 HOH   317 717  1172 HOH   HOH C . 
JA 5 HOH   318 718  1202 HOH   HOH C . 
JA 5 HOH   319 719  1164 HOH   HOH C . 
JA 5 HOH   320 720  1245 HOH   HOH C . 
JA 5 HOH   321 721  609  HOH   HOH C . 
JA 5 HOH   322 722  1215 HOH   HOH C . 
JA 5 HOH   323 723  1386 HOH   HOH C . 
JA 5 HOH   324 724  747  HOH   HOH C . 
JA 5 HOH   325 725  1522 HOH   HOH C . 
JA 5 HOH   326 726  970  HOH   HOH C . 
JA 5 HOH   327 727  1608 HOH   HOH C . 
JA 5 HOH   328 728  50   HOH   HOH C . 
JA 5 HOH   329 729  1155 HOH   HOH C . 
JA 5 HOH   330 730  1391 HOH   HOH C . 
JA 5 HOH   331 731  1495 HOH   HOH C . 
JA 5 HOH   332 732  610  HOH   HOH C . 
JA 5 HOH   333 733  971  HOH   HOH C . 
JA 5 HOH   334 734  1026 HOH   HOH C . 
JA 5 HOH   335 735  966  HOH   HOH C . 
JA 5 HOH   336 736  927  HOH   HOH C . 
JA 5 HOH   337 737  976  HOH   HOH C . 
JA 5 HOH   338 738  1472 HOH   HOH C . 
JA 5 HOH   339 739  1292 HOH   HOH C . 
JA 5 HOH   340 740  1384 HOH   HOH C . 
JA 5 HOH   341 741  1283 HOH   HOH C . 
JA 5 HOH   342 742  1422 HOH   HOH C . 
JA 5 HOH   343 743  690  HOH   HOH C . 
JA 5 HOH   344 744  921  HOH   HOH C . 
JA 5 HOH   345 745  1396 HOH   HOH C . 
JA 5 HOH   346 746  1296 HOH   HOH C . 
JA 5 HOH   347 747  821  HOH   HOH C . 
JA 5 HOH   348 748  1199 HOH   HOH C . 
JA 5 HOH   349 749  1477 HOH   HOH C . 
JA 5 HOH   350 750  884  HOH   HOH C . 
JA 5 HOH   351 751  996  HOH   HOH C . 
JA 5 HOH   352 752  1618 HOH   HOH C . 
JA 5 HOH   353 753  1342 HOH   HOH C . 
JA 5 HOH   354 754  910  HOH   HOH C . 
JA 5 HOH   355 755  1362 HOH   HOH C . 
JA 5 HOH   356 756  193  HOH   HOH C . 
JA 5 HOH   357 757  1335 HOH   HOH C . 
JA 5 HOH   358 758  1285 HOH   HOH C . 
JA 5 HOH   359 759  1040 HOH   HOH C . 
JA 5 HOH   360 760  1605 HOH   HOH C . 
JA 5 HOH   361 761  1260 HOH   HOH C . 
JA 5 HOH   362 762  1538 HOH   HOH C . 
JA 5 HOH   363 763  339  HOH   HOH C . 
JA 5 HOH   364 764  916  HOH   HOH C . 
JA 5 HOH   365 765  1500 HOH   HOH C . 
JA 5 HOH   366 766  895  HOH   HOH C . 
JA 5 HOH   367 767  707  HOH   HOH C . 
JA 5 HOH   368 768  1065 HOH   HOH C . 
JA 5 HOH   369 769  957  HOH   HOH C . 
JA 5 HOH   370 770  1544 HOH   HOH C . 
JA 5 HOH   371 771  1068 HOH   HOH C . 
JA 5 HOH   372 772  829  HOH   HOH C . 
JA 5 HOH   373 773  943  HOH   HOH C . 
JA 5 HOH   374 774  991  HOH   HOH C . 
JA 5 HOH   375 775  1233 HOH   HOH C . 
JA 5 HOH   376 776  695  HOH   HOH C . 
JA 5 HOH   377 777  977  HOH   HOH C . 
JA 5 HOH   378 778  1137 HOH   HOH C . 
JA 5 HOH   379 779  815  HOH   HOH C . 
JA 5 HOH   380 780  1448 HOH   HOH C . 
JA 5 HOH   381 781  1262 HOH   HOH C . 
JA 5 HOH   382 782  1458 HOH   HOH C . 
JA 5 HOH   383 783  597  HOH   HOH C . 
JA 5 HOH   384 784  1258 HOH   HOH C . 
JA 5 HOH   385 785  1326 HOH   HOH C . 
JA 5 HOH   386 786  905  HOH   HOH C . 
JA 5 HOH   387 787  902  HOH   HOH C . 
JA 5 HOH   388 788  1425 HOH   HOH C . 
JA 5 HOH   389 789  1031 HOH   HOH C . 
JA 5 HOH   390 790  1501 HOH   HOH C . 
JA 5 HOH   391 791  692  HOH   HOH C . 
JA 5 HOH   392 792  1460 HOH   HOH C . 
JA 5 HOH   393 793  1190 HOH   HOH C . 
JA 5 HOH   394 794  1644 HOH   HOH C . 
JA 5 HOH   395 795  1525 HOH   HOH C . 
JA 5 HOH   396 796  1330 HOH   HOH C . 
JA 5 HOH   397 797  590  HOH   HOH C . 
JA 5 HOH   398 798  1390 HOH   HOH C . 
JA 5 HOH   399 799  1463 HOH   HOH C . 
JA 5 HOH   400 800  1264 HOH   HOH C . 
JA 5 HOH   401 801  650  HOH   HOH C . 
JA 5 HOH   402 802  1449 HOH   HOH C . 
JA 5 HOH   403 803  1234 HOH   HOH C . 
JA 5 HOH   404 804  294  HOH   HOH C . 
JA 5 HOH   405 805  557  HOH   HOH C . 
JA 5 HOH   406 806  1623 HOH   HOH C . 
KA 5 HOH   1   401  48   HOH   HOH D . 
KA 5 HOH   2   402  1052 HOH   HOH D . 
KA 5 HOH   3   403  585  HOH   HOH D . 
KA 5 HOH   4   404  139  HOH   HOH D . 
KA 5 HOH   5   405  1136 HOH   HOH D . 
KA 5 HOH   6   406  1298 HOH   HOH D . 
KA 5 HOH   7   407  559  HOH   HOH D . 
KA 5 HOH   8   408  1066 HOH   HOH D . 
KA 5 HOH   9   409  967  HOH   HOH D . 
KA 5 HOH   10  410  880  HOH   HOH D . 
KA 5 HOH   11  411  140  HOH   HOH D . 
KA 5 HOH   12  412  1183 HOH   HOH D . 
KA 5 HOH   13  413  1324 HOH   HOH D . 
KA 5 HOH   14  414  1299 HOH   HOH D . 
KA 5 HOH   15  415  946  HOH   HOH D . 
KA 5 HOH   16  416  1410 HOH   HOH D . 
KA 5 HOH   17  417  959  HOH   HOH D . 
KA 5 HOH   18  418  1601 HOH   HOH D . 
KA 5 HOH   19  419  666  HOH   HOH D . 
KA 5 HOH   20  420  443  HOH   HOH D . 
KA 5 HOH   21  421  854  HOH   HOH D . 
KA 5 HOH   22  422  1524 HOH   HOH D . 
KA 5 HOH   23  423  979  HOH   HOH D . 
KA 5 HOH   24  424  1103 HOH   HOH D . 
KA 5 HOH   25  425  151  HOH   HOH D . 
KA 5 HOH   26  426  1573 HOH   HOH D . 
KA 5 HOH   27  427  611  HOH   HOH D . 
KA 5 HOH   28  428  1134 HOH   HOH D . 
KA 5 HOH   29  429  218  HOH   HOH D . 
KA 5 HOH   30  430  306  HOH   HOH D . 
KA 5 HOH   31  431  188  HOH   HOH D . 
KA 5 HOH   32  432  340  HOH   HOH D . 
KA 5 HOH   33  433  488  HOH   HOH D . 
KA 5 HOH   34  434  25   HOH   HOH D . 
KA 5 HOH   35  435  619  HOH   HOH D . 
KA 5 HOH   36  436  990  HOH   HOH D . 
KA 5 HOH   37  437  506  HOH   HOH D . 
KA 5 HOH   38  438  581  HOH   HOH D . 
KA 5 HOH   39  439  445  HOH   HOH D . 
KA 5 HOH   40  440  1008 HOH   HOH D . 
KA 5 HOH   41  441  240  HOH   HOH D . 
KA 5 HOH   42  442  210  HOH   HOH D . 
KA 5 HOH   43  443  293  HOH   HOH D . 
KA 5 HOH   44  444  896  HOH   HOH D . 
KA 5 HOH   45  445  115  HOH   HOH D . 
KA 5 HOH   46  446  76   HOH   HOH D . 
KA 5 HOH   47  447  501  HOH   HOH D . 
KA 5 HOH   48  448  706  HOH   HOH D . 
KA 5 HOH   49  449  1167 HOH   HOH D . 
KA 5 HOH   50  450  1259 HOH   HOH D . 
KA 5 HOH   51  451  270  HOH   HOH D . 
KA 5 HOH   52  452  30   HOH   HOH D . 
KA 5 HOH   53  453  410  HOH   HOH D . 
KA 5 HOH   54  454  198  HOH   HOH D . 
KA 5 HOH   55  455  31   HOH   HOH D . 
KA 5 HOH   56  456  5    HOH   HOH D . 
KA 5 HOH   57  457  70   HOH   HOH D . 
KA 5 HOH   58  458  374  HOH   HOH D . 
KA 5 HOH   59  459  237  HOH   HOH D . 
KA 5 HOH   60  460  1016 HOH   HOH D . 
KA 5 HOH   61  461  1595 HOH   HOH D . 
KA 5 HOH   62  462  982  HOH   HOH D . 
KA 5 HOH   63  463  791  HOH   HOH D . 
KA 5 HOH   64  464  368  HOH   HOH D . 
KA 5 HOH   65  465  108  HOH   HOH D . 
KA 5 HOH   66  466  255  HOH   HOH D . 
KA 5 HOH   67  467  111  HOH   HOH D . 
KA 5 HOH   68  468  704  HOH   HOH D . 
KA 5 HOH   69  469  118  HOH   HOH D . 
KA 5 HOH   70  470  1487 HOH   HOH D . 
KA 5 HOH   71  471  54   HOH   HOH D . 
KA 5 HOH   72  472  82   HOH   HOH D . 
KA 5 HOH   73  473  1478 HOH   HOH D . 
KA 5 HOH   74  474  98   HOH   HOH D . 
KA 5 HOH   75  475  87   HOH   HOH D . 
KA 5 HOH   76  476  1586 HOH   HOH D . 
KA 5 HOH   77  477  1106 HOH   HOH D . 
KA 5 HOH   78  478  222  HOH   HOH D . 
KA 5 HOH   79  479  380  HOH   HOH D . 
KA 5 HOH   80  480  702  HOH   HOH D . 
KA 5 HOH   81  481  279  HOH   HOH D . 
KA 5 HOH   82  482  224  HOH   HOH D . 
KA 5 HOH   83  483  189  HOH   HOH D . 
KA 5 HOH   84  484  134  HOH   HOH D . 
KA 5 HOH   85  485  94   HOH   HOH D . 
KA 5 HOH   86  486  782  HOH   HOH D . 
KA 5 HOH   87  487  379  HOH   HOH D . 
KA 5 HOH   88  488  1281 HOH   HOH D . 
KA 5 HOH   89  489  1036 HOH   HOH D . 
KA 5 HOH   90  490  1426 HOH   HOH D . 
KA 5 HOH   91  491  800  HOH   HOH D . 
KA 5 HOH   92  492  1227 HOH   HOH D . 
KA 5 HOH   93  493  1649 HOH   HOH D . 
KA 5 HOH   94  494  606  HOH   HOH D . 
KA 5 HOH   95  495  320  HOH   HOH D . 
KA 5 HOH   96  496  327  HOH   HOH D . 
KA 5 HOH   97  497  180  HOH   HOH D . 
KA 5 HOH   98  498  1542 HOH   HOH D . 
KA 5 HOH   99  499  450  HOH   HOH D . 
KA 5 HOH   100 500  646  HOH   HOH D . 
KA 5 HOH   101 501  349  HOH   HOH D . 
KA 5 HOH   102 502  637  HOH   HOH D . 
KA 5 HOH   103 503  84   HOH   HOH D . 
KA 5 HOH   104 504  1128 HOH   HOH D . 
KA 5 HOH   105 505  1629 HOH   HOH D . 
KA 5 HOH   106 506  460  HOH   HOH D . 
KA 5 HOH   107 507  592  HOH   HOH D . 
KA 5 HOH   108 508  513  HOH   HOH D . 
KA 5 HOH   109 509  1005 HOH   HOH D . 
KA 5 HOH   110 510  659  HOH   HOH D . 
KA 5 HOH   111 511  531  HOH   HOH D . 
KA 5 HOH   112 512  152  HOH   HOH D . 
KA 5 HOH   113 513  731  HOH   HOH D . 
KA 5 HOH   114 514  228  HOH   HOH D . 
KA 5 HOH   115 515  622  HOH   HOH D . 
KA 5 HOH   116 516  38   HOH   HOH D . 
KA 5 HOH   117 517  807  HOH   HOH D . 
KA 5 HOH   118 518  1323 HOH   HOH D . 
KA 5 HOH   119 519  507  HOH   HOH D . 
KA 5 HOH   120 520  1189 HOH   HOH D . 
KA 5 HOH   121 521  1584 HOH   HOH D . 
KA 5 HOH   122 522  205  HOH   HOH D . 
KA 5 HOH   123 523  687  HOH   HOH D . 
KA 5 HOH   124 524  66   HOH   HOH D . 
KA 5 HOH   125 525  361  HOH   HOH D . 
KA 5 HOH   126 526  420  HOH   HOH D . 
KA 5 HOH   127 527  257  HOH   HOH D . 
KA 5 HOH   128 528  357  HOH   HOH D . 
KA 5 HOH   129 529  59   HOH   HOH D . 
KA 5 HOH   130 530  221  HOH   HOH D . 
KA 5 HOH   131 531  1148 HOH   HOH D . 
KA 5 HOH   132 532  254  HOH   HOH D . 
KA 5 HOH   133 533  947  HOH   HOH D . 
KA 5 HOH   134 534  1682 HOH   HOH D . 
KA 5 HOH   135 535  1092 HOH   HOH D . 
KA 5 HOH   136 536  913  HOH   HOH D . 
KA 5 HOH   137 537  624  HOH   HOH D . 
KA 5 HOH   138 538  1659 HOH   HOH D . 
KA 5 HOH   139 539  730  HOH   HOH D . 
KA 5 HOH   140 540  41   HOH   HOH D . 
KA 5 HOH   141 541  81   HOH   HOH D . 
KA 5 HOH   142 542  813  HOH   HOH D . 
KA 5 HOH   143 543  601  HOH   HOH D . 
KA 5 HOH   144 544  944  HOH   HOH D . 
KA 5 HOH   145 545  1400 HOH   HOH D . 
KA 5 HOH   146 546  788  HOH   HOH D . 
KA 5 HOH   147 547  378  HOH   HOH D . 
KA 5 HOH   148 548  311  HOH   HOH D . 
KA 5 HOH   149 549  346  HOH   HOH D . 
KA 5 HOH   150 550  178  HOH   HOH D . 
KA 5 HOH   151 551  421  HOH   HOH D . 
KA 5 HOH   152 552  994  HOH   HOH D . 
KA 5 HOH   153 553  688  HOH   HOH D . 
KA 5 HOH   154 554  475  HOH   HOH D . 
KA 5 HOH   155 555  709  HOH   HOH D . 
KA 5 HOH   156 556  448  HOH   HOH D . 
KA 5 HOH   157 557  1696 HOH   HOH D . 
KA 5 HOH   158 558  738  HOH   HOH D . 
KA 5 HOH   159 559  116  HOH   HOH D . 
KA 5 HOH   160 560  177  HOH   HOH D . 
KA 5 HOH   161 561  1109 HOH   HOH D . 
KA 5 HOH   162 562  1200 HOH   HOH D . 
KA 5 HOH   163 563  649  HOH   HOH D . 
KA 5 HOH   164 564  1007 HOH   HOH D . 
KA 5 HOH   165 565  875  HOH   HOH D . 
KA 5 HOH   166 566  835  HOH   HOH D . 
KA 5 HOH   167 567  427  HOH   HOH D . 
KA 5 HOH   168 568  429  HOH   HOH D . 
KA 5 HOH   169 569  497  HOH   HOH D . 
KA 5 HOH   170 570  276  HOH   HOH D . 
KA 5 HOH   171 571  936  HOH   HOH D . 
KA 5 HOH   172 572  365  HOH   HOH D . 
KA 5 HOH   173 573  858  HOH   HOH D . 
KA 5 HOH   174 574  919  HOH   HOH D . 
KA 5 HOH   175 575  602  HOH   HOH D . 
KA 5 HOH   176 576  347  HOH   HOH D . 
KA 5 HOH   177 577  1028 HOH   HOH D . 
KA 5 HOH   178 578  1424 HOH   HOH D . 
KA 5 HOH   179 579  146  HOH   HOH D . 
KA 5 HOH   180 580  1451 HOH   HOH D . 
KA 5 HOH   181 581  759  HOH   HOH D . 
KA 5 HOH   182 582  480  HOH   HOH D . 
KA 5 HOH   183 583  1119 HOH   HOH D . 
KA 5 HOH   184 584  596  HOH   HOH D . 
KA 5 HOH   185 585  283  HOH   HOH D . 
KA 5 HOH   186 586  1637 HOH   HOH D . 
KA 5 HOH   187 587  1275 HOH   HOH D . 
KA 5 HOH   188 588  1010 HOH   HOH D . 
KA 5 HOH   189 589  483  HOH   HOH D . 
KA 5 HOH   190 590  526  HOH   HOH D . 
KA 5 HOH   191 591  1604 HOH   HOH D . 
KA 5 HOH   192 592  300  HOH   HOH D . 
KA 5 HOH   193 593  673  HOH   HOH D . 
KA 5 HOH   194 594  326  HOH   HOH D . 
KA 5 HOH   195 595  1009 HOH   HOH D . 
KA 5 HOH   196 596  1516 HOH   HOH D . 
KA 5 HOH   197 597  1071 HOH   HOH D . 
KA 5 HOH   198 598  933  HOH   HOH D . 
KA 5 HOH   199 599  305  HOH   HOH D . 
KA 5 HOH   200 600  615  HOH   HOH D . 
KA 5 HOH   201 601  804  HOH   HOH D . 
KA 5 HOH   202 602  998  HOH   HOH D . 
KA 5 HOH   203 603  579  HOH   HOH D . 
KA 5 HOH   204 604  55   HOH   HOH D . 
KA 5 HOH   205 605  1709 HOH   HOH D . 
KA 5 HOH   206 606  1596 HOH   HOH D . 
KA 5 HOH   207 607  845  HOH   HOH D . 
KA 5 HOH   208 608  955  HOH   HOH D . 
KA 5 HOH   209 609  433  HOH   HOH D . 
KA 5 HOH   210 610  799  HOH   HOH D . 
KA 5 HOH   211 611  287  HOH   HOH D . 
KA 5 HOH   212 612  1110 HOH   HOH D . 
KA 5 HOH   213 613  520  HOH   HOH D . 
KA 5 HOH   214 614  128  HOH   HOH D . 
KA 5 HOH   215 615  1548 HOH   HOH D . 
KA 5 HOH   216 616  21   HOH   HOH D . 
KA 5 HOH   217 617  260  HOH   HOH D . 
KA 5 HOH   218 618  1676 HOH   HOH D . 
KA 5 HOH   219 619  846  HOH   HOH D . 
KA 5 HOH   220 620  708  HOH   HOH D . 
KA 5 HOH   221 621  331  HOH   HOH D . 
KA 5 HOH   222 622  934  HOH   HOH D . 
KA 5 HOH   223 623  428  HOH   HOH D . 
KA 5 HOH   224 624  154  HOH   HOH D . 
KA 5 HOH   225 625  651  HOH   HOH D . 
KA 5 HOH   226 626  766  HOH   HOH D . 
KA 5 HOH   227 627  1421 HOH   HOH D . 
KA 5 HOH   228 628  932  HOH   HOH D . 
KA 5 HOH   229 629  185  HOH   HOH D . 
KA 5 HOH   230 630  1247 HOH   HOH D . 
KA 5 HOH   231 631  554  HOH   HOH D . 
KA 5 HOH   232 632  528  HOH   HOH D . 
KA 5 HOH   233 633  1271 HOH   HOH D . 
KA 5 HOH   234 634  1297 HOH   HOH D . 
KA 5 HOH   235 635  1070 HOH   HOH D . 
KA 5 HOH   236 636  1414 HOH   HOH D . 
KA 5 HOH   237 637  588  HOH   HOH D . 
KA 5 HOH   238 638  548  HOH   HOH D . 
KA 5 HOH   239 639  1187 HOH   HOH D . 
KA 5 HOH   240 640  1680 HOH   HOH D . 
KA 5 HOH   241 641  763  HOH   HOH D . 
KA 5 HOH   242 642  451  HOH   HOH D . 
KA 5 HOH   243 643  272  HOH   HOH D . 
KA 5 HOH   244 644  1551 HOH   HOH D . 
KA 5 HOH   245 645  942  HOH   HOH D . 
KA 5 HOH   246 646  792  HOH   HOH D . 
KA 5 HOH   247 647  156  HOH   HOH D . 
KA 5 HOH   248 648  366  HOH   HOH D . 
KA 5 HOH   249 649  498  HOH   HOH D . 
KA 5 HOH   250 650  1154 HOH   HOH D . 
KA 5 HOH   251 651  314  HOH   HOH D . 
KA 5 HOH   252 652  1290 HOH   HOH D . 
KA 5 HOH   253 653  330  HOH   HOH D . 
KA 5 HOH   254 654  1322 HOH   HOH D . 
KA 5 HOH   255 655  1050 HOH   HOH D . 
KA 5 HOH   256 656  816  HOH   HOH D . 
KA 5 HOH   257 657  1317 HOH   HOH D . 
KA 5 HOH   258 658  1244 HOH   HOH D . 
KA 5 HOH   259 659  1345 HOH   HOH D . 
KA 5 HOH   260 660  1585 HOH   HOH D . 
KA 5 HOH   261 661  93   HOH   HOH D . 
KA 5 HOH   262 662  739  HOH   HOH D . 
KA 5 HOH   263 663  199  HOH   HOH D . 
KA 5 HOH   264 664  838  HOH   HOH D . 
KA 5 HOH   265 665  1195 HOH   HOH D . 
KA 5 HOH   266 666  1325 HOH   HOH D . 
KA 5 HOH   267 667  12   HOH   HOH D . 
KA 5 HOH   268 668  1085 HOH   HOH D . 
KA 5 HOH   269 669  412  HOH   HOH D . 
KA 5 HOH   270 670  337  HOH   HOH D . 
KA 5 HOH   271 671  1554 HOH   HOH D . 
KA 5 HOH   272 672  3    HOH   HOH D . 
KA 5 HOH   273 673  1537 HOH   HOH D . 
KA 5 HOH   274 674  461  HOH   HOH D . 
KA 5 HOH   275 675  1520 HOH   HOH D . 
KA 5 HOH   276 676  504  HOH   HOH D . 
KA 5 HOH   277 677  1039 HOH   HOH D . 
KA 5 HOH   278 678  560  HOH   HOH D . 
KA 5 HOH   279 679  1603 HOH   HOH D . 
KA 5 HOH   280 680  1528 HOH   HOH D . 
KA 5 HOH   281 681  1178 HOH   HOH D . 
KA 5 HOH   282 682  968  HOH   HOH D . 
KA 5 HOH   283 683  1677 HOH   HOH D . 
KA 5 HOH   284 684  1344 HOH   HOH D . 
KA 5 HOH   285 685  906  HOH   HOH D . 
KA 5 HOH   286 686  1221 HOH   HOH D . 
KA 5 HOH   287 687  1209 HOH   HOH D . 
KA 5 HOH   288 688  915  HOH   HOH D . 
KA 5 HOH   289 689  1044 HOH   HOH D . 
KA 5 HOH   290 690  1169 HOH   HOH D . 
KA 5 HOH   291 691  1180 HOH   HOH D . 
KA 5 HOH   292 692  1383 HOH   HOH D . 
KA 5 HOH   293 693  974  HOH   HOH D . 
KA 5 HOH   294 694  1270 HOH   HOH D . 
KA 5 HOH   295 695  1282 HOH   HOH D . 
KA 5 HOH   296 696  514  HOH   HOH D . 
KA 5 HOH   297 697  1541 HOH   HOH D . 
KA 5 HOH   298 698  1568 HOH   HOH D . 
KA 5 HOH   299 699  1464 HOH   HOH D . 
KA 5 HOH   300 700  409  HOH   HOH D . 
KA 5 HOH   301 701  173  HOH   HOH D . 
KA 5 HOH   302 702  1351 HOH   HOH D . 
KA 5 HOH   303 703  667  HOH   HOH D . 
KA 5 HOH   304 704  1662 HOH   HOH D . 
KA 5 HOH   305 705  1132 HOH   HOH D . 
KA 5 HOH   306 706  1115 HOH   HOH D . 
KA 5 HOH   307 707  1163 HOH   HOH D . 
KA 5 HOH   308 708  1300 HOH   HOH D . 
KA 5 HOH   309 709  621  HOH   HOH D . 
KA 5 HOH   310 710  1112 HOH   HOH D . 
KA 5 HOH   311 711  1261 HOH   HOH D . 
KA 5 HOH   312 712  1140 HOH   HOH D . 
KA 5 HOH   313 713  1176 HOH   HOH D . 
KA 5 HOH   314 714  1287 HOH   HOH D . 
KA 5 HOH   315 715  631  HOH   HOH D . 
KA 5 HOH   316 716  1350 HOH   HOH D . 
KA 5 HOH   317 717  773  HOH   HOH D . 
KA 5 HOH   318 718  1385 HOH   HOH D . 
KA 5 HOH   319 719  1598 HOH   HOH D . 
KA 5 HOH   320 720  1671 HOH   HOH D . 
KA 5 HOH   321 721  1413 HOH   HOH D . 
KA 5 HOH   322 722  1624 HOH   HOH D . 
KA 5 HOH   323 723  44   HOH   HOH D . 
KA 5 HOH   324 724  1011 HOH   HOH D . 
KA 5 HOH   325 725  1462 HOH   HOH D . 
KA 5 HOH   326 726  1606 HOH   HOH D . 
KA 5 HOH   327 727  837  HOH   HOH D . 
KA 5 HOH   328 728  1399 HOH   HOH D . 
KA 5 HOH   329 729  1610 HOH   HOH D . 
KA 5 HOH   330 730  1046 HOH   HOH D . 
KA 5 HOH   331 731  923  HOH   HOH D . 
KA 5 HOH   332 732  1365 HOH   HOH D . 
KA 5 HOH   333 733  1630 HOH   HOH D . 
KA 5 HOH   334 734  1252 HOH   HOH D . 
KA 5 HOH   335 735  1186 HOH   HOH D . 
KA 5 HOH   336 736  1443 HOH   HOH D . 
KA 5 HOH   337 737  1693 HOH   HOH D . 
KA 5 HOH   338 738  1534 HOH   HOH D . 
KA 5 HOH   339 739  726  HOH   HOH D . 
KA 5 HOH   340 740  1485 HOH   HOH D . 
KA 5 HOH   341 741  1376 HOH   HOH D . 
KA 5 HOH   342 742  888  HOH   HOH D . 
KA 5 HOH   343 743  843  HOH   HOH D . 
KA 5 HOH   344 744  1349 HOH   HOH D . 
KA 5 HOH   345 745  1481 HOH   HOH D . 
KA 5 HOH   346 746  595  HOH   HOH D . 
KA 5 HOH   347 747  1433 HOH   HOH D . 
KA 5 HOH   348 748  879  HOH   HOH D . 
KA 5 HOH   349 749  1679 HOH   HOH D . 
KA 5 HOH   350 750  1374 HOH   HOH D . 
KA 5 HOH   351 751  208  HOH   HOH D . 
KA 5 HOH   352 752  1360 HOH   HOH D . 
KA 5 HOH   353 753  1691 HOH   HOH D . 
KA 5 HOH   354 754  669  HOH   HOH D . 
KA 5 HOH   355 755  760  HOH   HOH D . 
KA 5 HOH   356 756  358  HOH   HOH D . 
KA 5 HOH   357 757  1454 HOH   HOH D . 
KA 5 HOH   358 758  1184 HOH   HOH D . 
KA 5 HOH   359 759  1638 HOH   HOH D . 
KA 5 HOH   360 760  1003 HOH   HOH D . 
KA 5 HOH   361 761  1057 HOH   HOH D . 
KA 5 HOH   362 762  885  HOH   HOH D . 
KA 5 HOH   363 763  822  HOH   HOH D . 
KA 5 HOH   364 764  756  HOH   HOH D . 
KA 5 HOH   365 765  1600 HOH   HOH D . 
KA 5 HOH   366 766  1095 HOH   HOH D . 
KA 5 HOH   367 767  1159 HOH   HOH D . 
KA 5 HOH   368 768  920  HOH   HOH D . 
KA 5 HOH   369 769  1268 HOH   HOH D . 
KA 5 HOH   370 770  1218 HOH   HOH D . 
KA 5 HOH   371 771  1263 HOH   HOH D . 
KA 5 HOH   372 772  1139 HOH   HOH D . 
KA 5 HOH   373 773  1034 HOH   HOH D . 
KA 5 HOH   374 774  925  HOH   HOH D . 
KA 5 HOH   375 775  784  HOH   HOH D . 
KA 5 HOH   376 776  638  HOH   HOH D . 
KA 5 HOH   377 777  819  HOH   HOH D . 
KA 5 HOH   378 778  1672 HOH   HOH D . 
KA 5 HOH   379 779  1168 HOH   HOH D . 
KA 5 HOH   380 780  1265 HOH   HOH D . 
KA 5 HOH   381 781  1243 HOH   HOH D . 
KA 5 HOH   382 782  1526 HOH   HOH D . 
KA 5 HOH   383 783  1035 HOH   HOH D . 
KA 5 HOH   384 784  618  HOH   HOH D . 
KA 5 HOH   385 785  1205 HOH   HOH D . 
KA 5 HOH   386 786  1246 HOH   HOH D . 
KA 5 HOH   387 787  775  HOH   HOH D . 
KA 5 HOH   388 788  1055 HOH   HOH D . 
KA 5 HOH   389 789  599  HOH   HOH D . 
KA 5 HOH   390 790  1673 HOH   HOH D . 
KA 5 HOH   391 791  360  HOH   HOH D . 
KA 5 HOH   392 792  1248 HOH   HOH D . 
KA 5 HOH   393 793  668  HOH   HOH D . 
KA 5 HOH   394 794  558  HOH   HOH D . 
KA 5 HOH   395 795  1379 HOH   HOH D . 
KA 5 HOH   396 796  1348 HOH   HOH D . 
KA 5 HOH   397 797  417  HOH   HOH D . 
KA 5 HOH   398 798  1536 HOH   HOH D . 
# 
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  ? ? ? '(1.12rc1_2801: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                     2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                     3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                     4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F2F 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     179.167 
_cell.length_a_esd                 ? 
_cell.length_b                     179.167 
_cell.length_b_esd                 ? 
_cell.length_c                     109.705 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        36 
_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                         9F2F 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3' 
_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                   9F2F 
_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             2.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.48 
_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              ? 
_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    '0.1M Magnesium acetate tetrahydrate, 0.1M MOPS pH 7.5, 12% w/v PEG 8000' 
_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 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-14 
_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   1.00003 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00003 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F2F 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.52 
_reflns.d_resolution_low                               44.792 
_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                                     202072 
_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 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                21.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.0 
_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                                0.042 
_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                              0.132 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.52 
_reflns_shell.d_res_low                                     1.55 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             20121 
_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                               20.4 
_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                               0.66 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.717 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.01 
_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                               ? 
_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                                 9F2F 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.520 
_refine.ls_d_res_low                             44.792 
_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                     201826 
_refine.ls_number_reflns_R_free                  10204 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.88 
_refine.ls_percent_reflns_R_free                 5.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1476 
_refine.ls_R_factor_R_free                       0.1670 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1465 
_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                          1.96 
_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       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 17.26 
_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                            0.14 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.520 
_refine_hist.d_res_low                        44.792 
_refine_hist.number_atoms_solvent             1640 
_refine_hist.number_atoms_total               10130 
_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        8264 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         226 
_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' ? 0.016  ? 8919  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.483  ? 12184 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.412 ? 5231  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.084  ? 1242  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 1566  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.5200 1.5373 . . 287 6332 100.00 . . . . 0.2411 . . . . . . . . . . . 0.2823 
'X-RAY DIFFRACTION' 1.5373 1.5554 . . 369 6344 99.00  . . . . 0.2253 . . . . . . . . . . . 0.2640 
'X-RAY DIFFRACTION' 1.5554 1.5743 . . 320 6389 100.00 . . . . 0.2126 . . . . . . . . . . . 0.2352 
'X-RAY DIFFRACTION' 1.5743 1.5943 . . 389 6329 100.00 . . . . 0.2127 . . . . . . . . . . . 0.2291 
'X-RAY DIFFRACTION' 1.5943 1.6152 . . 245 6590 100.00 . . . . 0.2237 . . . . . . . . . . . 0.2896 
'X-RAY DIFFRACTION' 1.6152 1.6374 . . 340 6370 100.00 . . . . 0.1788 . . . . . . . . . . . 0.2070 
'X-RAY DIFFRACTION' 1.6374 1.6608 . . 292 6315 100.00 . . . . 0.1891 . . . . . . . . . . . 0.2170 
'X-RAY DIFFRACTION' 1.6608 1.6856 . . 400 6415 100.00 . . . . 0.1846 . . . . . . . . . . . 0.2344 
'X-RAY DIFFRACTION' 1.6856 1.7119 . . 348 6338 100.00 . . . . 0.1721 . . . . . . . . . . . 0.1908 
'X-RAY DIFFRACTION' 1.7119 1.7400 . . 312 6440 100.00 . . . . 0.1641 . . . . . . . . . . . 0.1699 
'X-RAY DIFFRACTION' 1.7400 1.7700 . . 282 6529 100.00 . . . . 0.1592 . . . . . . . . . . . 0.2011 
'X-RAY DIFFRACTION' 1.7700 1.8021 . . 319 6309 100.00 . . . . 0.1517 . . . . . . . . . . . 0.1716 
'X-RAY DIFFRACTION' 1.8021 1.8368 . . 295 6450 100.00 . . . . 0.1513 . . . . . . . . . . . 0.2062 
'X-RAY DIFFRACTION' 1.8368 1.8743 . . 336 6341 100.00 . . . . 0.1469 . . . . . . . . . . . 0.1733 
'X-RAY DIFFRACTION' 1.8743 1.9151 . . 367 6352 100.00 . . . . 0.1523 . . . . . . . . . . . 0.1642 
'X-RAY DIFFRACTION' 1.9151 1.9596 . . 408 6398 100.00 . . . . 0.1499 . . . . . . . . . . . 0.1772 
'X-RAY DIFFRACTION' 1.9596 2.0086 . . 244 6437 100.00 . . . . 0.1557 . . . . . . . . . . . 0.1642 
'X-RAY DIFFRACTION' 2.0086 2.0629 . . 424 6289 100.00 . . . . 0.1525 . . . . . . . . . . . 0.1832 
'X-RAY DIFFRACTION' 2.0629 2.1236 . . 278 6513 100.00 . . . . 0.1494 . . . . . . . . . . . 0.1818 
'X-RAY DIFFRACTION' 2.1236 2.1922 . . 448 6314 100.00 . . . . 0.1474 . . . . . . . . . . . 0.1698 
'X-RAY DIFFRACTION' 2.1922 2.2705 . . 320 6387 100.00 . . . . 0.1417 . . . . . . . . . . . 0.1648 
'X-RAY DIFFRACTION' 2.2705 2.3614 . . 380 6375 100.00 . . . . 0.1469 . . . . . . . . . . . 0.1828 
'X-RAY DIFFRACTION' 2.3614 2.4689 . . 392 6322 100.00 . . . . 0.1450 . . . . . . . . . . . 0.1532 
'X-RAY DIFFRACTION' 2.4689 2.5990 . . 292 6487 100.00 . . . . 0.1473 . . . . . . . . . . . 0.1869 
'X-RAY DIFFRACTION' 2.5990 2.7619 . . 409 6312 100.00 . . . . 0.1412 . . . . . . . . . . . 0.1611 
'X-RAY DIFFRACTION' 2.7619 2.9751 . . 444 6299 100.00 . . . . 0.1436 . . . . . . . . . . . 0.1901 
'X-RAY DIFFRACTION' 2.9751 3.2744 . . 237 6413 100.00 . . . . 0.1403 . . . . . . . . . . . 0.1678 
'X-RAY DIFFRACTION' 3.2744 3.7480 . . 260 6533 100.00 . . . . 0.1377 . . . . . . . . . . . 0.1498 
'X-RAY DIFFRACTION' 3.7480 4.7212 . . 384 6357 100.00 . . . . 0.1116 . . . . . . . . . . . 0.1177 
'X-RAY DIFFRACTION' 4.7212 44.792 . . 383 6343 100.00 . . . . 0.1386 . . . . . . . . . . . 0.1480 
# 
_struct.entry_id                     9F2F 
_struct.title                        'Carbonic anhydrase II variant with bound iron complex in space group R3 (ArPase)' 
_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        9F2F 
_struct_keywords.text            'artificial enzyme, metalloenzyme, peroxidase, human carbonic anhydrase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 4 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 2 ? 
M  N N 3 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 4 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 3 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 3 ? 
BA N N 2 ? 
CA N N 3 ? 
DA N N 4 ? 
EA N N 3 ? 
FA N N 3 ? 
GA N N 3 ? 
HA N N 5 ? 
IA N N 5 ? 
JA N N 5 ? 
KA N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_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 9F2F A 1 ? 260 ? P00918 1 ? 260 ? 1 260 
2 1 9F2F B 1 ? 260 ? P00918 1 ? 260 ? 1 260 
3 1 9F2F C 1 ? 260 ? P00918 1 ? 260 ? 1 260 
4 1 9F2F D 1 ? 260 ? P00918 1 ? 260 ? 1 260 
# 
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 9F2F ALA A 2   ? UNP P00918 SER 2   conflict 2   1  
1 9F2F THR A 65  ? UNP P00918 ALA 65  conflict 65  2  
1 9F2F HIS A 100 ? UNP P00918 LEU 100 conflict 100 3  
1 9F2F LEU A 153 ? UNP P00918 LYS 153 conflict 153 4  
1 9F2F SER A 205 ? UNP P00918 CYS 205 conflict 205 5  
1 9F2F SER A 223 ? UNP P00918 LEU 223 conflict 223 6  
1 9F2F PRO A 239 ? UNP P00918 LEU 239 conflict 239 7  
1 9F2F THR A 247 ? UNP P00918 ALA 247 conflict 247 8  
2 9F2F ALA B 2   ? UNP P00918 SER 2   conflict 2   9  
2 9F2F THR B 65  ? UNP P00918 ALA 65  conflict 65  10 
2 9F2F HIS B 100 ? UNP P00918 LEU 100 conflict 100 11 
2 9F2F LEU B 153 ? UNP P00918 LYS 153 conflict 153 12 
2 9F2F SER B 205 ? UNP P00918 CYS 205 conflict 205 13 
2 9F2F SER B 223 ? UNP P00918 LEU 223 conflict 223 14 
2 9F2F PRO B 239 ? UNP P00918 LEU 239 conflict 239 15 
2 9F2F THR B 247 ? UNP P00918 ALA 247 conflict 247 16 
3 9F2F ALA C 2   ? UNP P00918 SER 2   conflict 2   17 
3 9F2F THR C 65  ? UNP P00918 ALA 65  conflict 65  18 
3 9F2F HIS C 100 ? UNP P00918 LEU 100 conflict 100 19 
3 9F2F LEU C 153 ? UNP P00918 LYS 153 conflict 153 20 
3 9F2F SER C 205 ? UNP P00918 CYS 205 conflict 205 21 
3 9F2F SER C 223 ? UNP P00918 LEU 223 conflict 223 22 
3 9F2F PRO C 239 ? UNP P00918 LEU 239 conflict 239 23 
3 9F2F THR C 247 ? UNP P00918 ALA 247 conflict 247 24 
4 9F2F ALA D 2   ? UNP P00918 SER 2   conflict 2   25 
4 9F2F THR D 65  ? UNP P00918 ALA 65  conflict 65  26 
4 9F2F HIS D 100 ? UNP P00918 LEU 100 conflict 100 27 
4 9F2F LEU D 153 ? UNP P00918 LYS 153 conflict 153 28 
4 9F2F SER D 205 ? UNP P00918 CYS 205 conflict 205 29 
4 9F2F SER D 223 ? UNP P00918 LEU 223 conflict 223 30 
4 9F2F PRO D 239 ? UNP P00918 LEU 239 conflict 239 31 
4 9F2F THR D 247 ? UNP P00918 ALA 247 conflict 247 32 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
4 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,F,G,H,I,J,K,HA     
2 1 B,L,M,N,O,P,Q,R,S,IA   
3 1 C,T,U,V,W,X,Y,Z,AA,JA  
4 1 D,BA,CA,DA,EA,FA,GA,KA 
# 
_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 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2  AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3  AA3 ASP A 129 ? VAL A 134 ? ASP A 129 VAL A 134 1 ? 6 
HELX_P HELX_P4  AA4 LEU A 153 ? GLY A 155 ? LEU A 153 GLY A 155 5 ? 3 
HELX_P HELX_P5  AA5 LEU A 156 ? LEU A 163 ? LEU A 156 LEU A 163 1 ? 8 
HELX_P HELX_P6  AA6 ASP A 164 ? ILE A 166 ? ASP A 164 ILE A 166 5 ? 3 
HELX_P HELX_P7  AA7 ASP A 179 ? LEU A 184 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P8  AA8 SER A 218 ? ARG A 226 ? SER A 218 ARG A 226 1 ? 9 
HELX_P HELX_P9  AA9 GLY B 12  ? ASP B 19  ? GLY B 12  ASP B 19  5 ? 8 
HELX_P HELX_P10 AB1 PHE B 20  ? GLY B 25  ? PHE B 20  GLY B 25  5 ? 6 
HELX_P HELX_P11 AB2 ASP B 129 ? VAL B 134 ? ASP B 129 VAL B 134 1 ? 6 
HELX_P HELX_P12 AB3 LEU B 153 ? GLY B 155 ? LEU B 153 GLY B 155 5 ? 3 
HELX_P HELX_P13 AB4 LEU B 156 ? LEU B 163 ? LEU B 156 LEU B 163 1 ? 8 
HELX_P HELX_P14 AB5 ASP B 164 ? LYS B 167 ? ASP B 164 LYS B 167 5 ? 4 
HELX_P HELX_P15 AB6 ASP B 179 ? LEU B 184 ? ASP B 179 LEU B 184 5 ? 6 
HELX_P HELX_P16 AB7 SER B 218 ? ARG B 226 ? SER B 218 ARG B 226 1 ? 9 
HELX_P HELX_P17 AB8 GLY C 12  ? ASP C 19  ? GLY C 12  ASP C 19  5 ? 8 
HELX_P HELX_P18 AB9 PHE C 20  ? GLY C 25  ? PHE C 20  GLY C 25  5 ? 6 
HELX_P HELX_P19 AC1 ASP C 129 ? VAL C 134 ? ASP C 129 VAL C 134 1 ? 6 
HELX_P HELX_P20 AC2 LEU C 153 ? GLY C 155 ? LEU C 153 GLY C 155 5 ? 3 
HELX_P HELX_P21 AC3 LEU C 156 ? LEU C 163 ? LEU C 156 LEU C 163 1 ? 8 
HELX_P HELX_P22 AC4 ASP C 164 ? LYS C 167 ? ASP C 164 LYS C 167 5 ? 4 
HELX_P HELX_P23 AC5 ASP C 179 ? LEU C 184 ? ASP C 179 LEU C 184 5 ? 6 
HELX_P HELX_P24 AC6 SER C 218 ? ARG C 226 ? SER C 218 ARG C 226 1 ? 9 
HELX_P HELX_P25 AC7 GLY D 12  ? ASP D 19  ? GLY D 12  ASP D 19  5 ? 8 
HELX_P HELX_P26 AC8 PHE D 20  ? GLY D 25  ? PHE D 20  GLY D 25  5 ? 6 
HELX_P HELX_P27 AC9 ASP D 129 ? VAL D 134 ? ASP D 129 VAL D 134 1 ? 6 
HELX_P HELX_P28 AD1 LEU D 153 ? GLY D 155 ? LEU D 153 GLY D 155 5 ? 3 
HELX_P HELX_P29 AD2 LEU D 156 ? LEU D 163 ? LEU D 156 LEU D 163 1 ? 8 
HELX_P HELX_P30 AD3 ASP D 164 ? ILE D 166 ? ASP D 164 ILE D 166 5 ? 3 
HELX_P HELX_P31 AD4 ASP D 179 ? LEU D 184 ? ASP D 179 LEU D 184 5 ? 6 
HELX_P HELX_P32 AD5 SER D 218 ? ARG D 226 ? SER D 218 ARG D 226 1 ? 9 
# 
_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  ALA   2   N   ? ? ? 1_555 AA ZN    .  ZN  ? ? A ALA   2   C ZN    308  6_554 ? ? ? ? ? ? ? 2.105 ? ? 
metalc2  metalc ? ? A  ALA   2   O   ? ? ? 1_555 AA ZN    .  ZN  ? ? A ALA   2   C ZN    308  6_554 ? ? ? ? ? ? ? 2.344 ? ? 
metalc3  metalc ? ? A  HIS   3   NE2 ? ? ? 1_555 T  A1H9O .  FE1 ? ? A HIS   3   C A1H9O 301  6_554 ? ? ? ? ? ? ? 2.267 ? ? 
metalc4  metalc ? ? A  HIS   4   NE2 ? ? ? 1_555 I  ZN    .  ZN  ? ? A HIS   4   A ZN    305  1_555 ? ? ? ? ? ? ? 2.011 ? ? 
metalc5  metalc ? ? A  HIS   4   ND1 ? ? ? 1_555 K  ZN    .  ZN  ? ? A HIS   4   A ZN    307  1_555 ? ? ? ? ? ? ? 2.071 ? ? 
metalc6  metalc ? ? A  HIS   10  NE2 ? ? ? 1_555 J  ZN    .  ZN  ? ? A HIS   10  A ZN    306  8_544 ? ? ? ? ? ? ? 2.068 ? ? 
metalc7  metalc ? ? A  ASP   34  OD1 ? ? ? 1_555 J  ZN    .  ZN  ? ? A ASP   34  A ZN    306  1_555 ? ? ? ? ? ? ? 2.442 ? ? 
metalc8  metalc ? ? A  ASP   34  OD2 ? ? ? 1_555 J  ZN    .  ZN  ? ? A ASP   34  A ZN    306  1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc9  metalc ? ? A  HIS   36  ND1 ? ? ? 1_555 J  ZN    .  ZN  ? ? A HIS   36  A ZN    306  1_555 ? ? ? ? ? ? ? 1.858 ? ? 
metalc10 metalc ? ? A  HIS   64  NE2 ? ? ? 1_555 I  ZN    .  ZN  ? ? A HIS   64  A ZN    305  1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc11 metalc ? ? A  HIS   94  NE2 ? ? ? 1_555 F  ZN    .  ZN  ? ? A HIS   94  A ZN    302  1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc12 metalc ? ? A  HIS   96  NE2 ? ? ? 1_555 F  ZN    .  ZN  ? ? A HIS   96  A ZN    302  1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc13 metalc ? ? A  HIS   119 ND1 ? ? ? 1_555 F  ZN    .  ZN  ? ? A HIS   119 A ZN    302  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc14 metalc ? ? E  A1H9O .   N1  ? ? ? 1_555 F  ZN    .  ZN  ? ? A A1H9O 301 A ZN    302  1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc15 metalc ? ? E  A1H9O .   FE1 ? ? ? 8_545 C  HIS   3  NE2 ? ? A A1H9O 301 C HIS   3    1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc16 metalc ? ? I  ZN    .   ZN  ? ? ? 1_555 HA HOH   .  O   ? ? A ZN    305 A HOH   1749 1_555 ? ? ? ? ? ? ? 2.080 ? ? 
metalc17 metalc ? ? I  ZN    .   ZN  ? ? ? 8_545 C  ALA   2  N   ? ? A ZN    305 C ALA   2    1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc18 metalc ? ? I  ZN    .   ZN  ? ? ? 8_545 C  ALA   2  O   ? ? A ZN    305 C ALA   2    1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc19 metalc ? ? J  ZN    .   ZN  ? ? ? 1_555 HA HOH   .  O   ? ? A ZN    306 A HOH   1895 1_555 ? ? ? ? ? ? ? 2.196 ? ? 
metalc20 metalc ? ? K  ZN    .   ZN  ? ? ? 1_555 HA HOH   .  O   ? ? A ZN    307 A HOH   1988 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc21 metalc ? ? K  ZN    .   ZN  ? ? ? 8_545 C  HIS   4  ND1 ? ? A ZN    307 C HIS   4    1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc22 metalc ? ? K  ZN    .   ZN  ? ? ? 1_555 JA HOH   .  O   ? ? A ZN    307 C HOH   679  6_554 ? ? ? ? ? ? ? 2.058 ? ? 
metalc23 metalc ? ? B  ALA   2   N   ? ? ? 1_555 S  ZN    .  ZN  ? ? B ALA   2   B ZN    308  1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc24 metalc ? ? B  ALA   2   O   ? ? ? 1_555 S  ZN    .  ZN  ? ? B ALA   2   B ZN    308  1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc25 metalc ? ? B  HIS   3   NE2 ? ? ? 1_555 BA A1H9O .  FE1 ? ? B HIS   3   D A1H9O 301  9_544 ? ? ? ? ? ? ? 2.287 ? ? 
metalc26 metalc ? ? B  HIS   4   ND1 ? ? ? 1_555 FA ZN    .  ZN  ? ? B HIS   4   D ZN    305  9_544 ? ? ? ? ? ? ? 2.064 ? ? 
metalc27 metalc ? ? B  HIS   4   NE2 ? ? ? 1_555 GA ZN    .  ZN  ? ? B HIS   4   D ZN    306  9_544 ? ? ? ? ? ? ? 2.004 ? ? 
metalc28 metalc ? ? B  HIS   10  NE2 ? ? ? 1_555 Q  ZN    .  ZN  ? ? B HIS   10  B ZN    306  1_555 ? ? ? ? ? ? ? 2.067 ? ? 
metalc29 metalc ? ? B  ASP   34  OD1 ? ? ? 1_555 R  ZN    .  ZN  ? ? B ASP   34  B ZN    307  1_555 ? ? ? ? ? ? ? 2.463 ? ? 
metalc30 metalc ? ? B  ASP   34  OD2 ? ? ? 1_555 R  ZN    .  ZN  ? ? B ASP   34  B ZN    307  1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc31 metalc ? ? B  HIS   36  ND1 ? ? ? 1_555 R  ZN    .  ZN  ? ? B HIS   36  B ZN    307  1_555 ? ? ? ? ? ? ? 1.892 ? ? 
metalc32 metalc ? ? B  HIS   64  NE2 ? ? ? 1_555 GA ZN    .  ZN  ? ? B HIS   64  D ZN    306  9_544 ? ? ? ? ? ? ? 2.096 ? ? 
metalc33 metalc ? ? B  HIS   94  NE2 ? ? ? 1_555 M  ZN    .  ZN  ? ? B HIS   94  B ZN    302  1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc34 metalc ? ? B  HIS   96  NE2 ? ? ? 1_555 M  ZN    .  ZN  ? ? B HIS   96  B ZN    302  1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc35 metalc ? ? B  HIS   119 ND1 ? ? ? 1_555 M  ZN    .  ZN  ? ? B HIS   119 B ZN    302  1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc36 metalc ? ? L  A1H9O .   N1  ? ? ? 1_555 M  ZN    .  ZN  ? ? B A1H9O 301 B ZN    302  1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc37 metalc ? ? L  A1H9O .   FE1 ? ? ? 5_445 D  HIS   3  NE2 ? ? B A1H9O 301 D HIS   3    1_555 ? ? ? ? ? ? ? 2.231 ? ? 
metalc38 metalc ? ? Q  ZN    .   ZN  ? ? ? 1_555 IA HOH   .  O   ? ? B ZN    306 B HOH   613  1_555 ? ? ? ? ? ? ? 2.517 ? ? 
metalc39 metalc ? ? Q  ZN    .   ZN  ? ? ? 5_445 C  ASP   34 OD1 ? ? B ZN    306 C ASP   34   1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc40 metalc ? ? Q  ZN    .   ZN  ? ? ? 5_445 C  ASP   34 OD2 ? ? B ZN    306 C ASP   34   1_555 ? ? ? ? ? ? ? 2.094 ? ? 
metalc41 metalc ? ? Q  ZN    .   ZN  ? ? ? 5_445 C  HIS   36 ND1 ? ? B ZN    306 C HIS   36   1_555 ? ? ? ? ? ? ? 1.777 ? ? 
metalc42 metalc ? ? R  ZN    .   ZN  ? ? ? 1_555 IA HOH   .  O   ? ? B ZN    307 B HOH   481  1_555 ? ? ? ? ? ? ? 2.495 ? ? 
metalc43 metalc ? ? R  ZN    .   ZN  ? ? ? 9_545 D  HIS   10 NE2 ? ? B ZN    307 D HIS   10   1_555 ? ? ? ? ? ? ? 2.078 ? ? 
metalc44 metalc ? ? S  ZN    .   ZN  ? ? ? 5_445 D  HIS   4  NE2 ? ? B ZN    308 D HIS   4    1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc45 metalc ? ? S  ZN    .   ZN  ? ? ? 5_445 D  HIS   64 NE2 ? ? B ZN    308 D HIS   64   1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc46 metalc ? ? S  ZN    .   ZN  ? ? ? 1_555 KA HOH   .  O   ? ? B ZN    308 D HOH   455  9_544 ? ? ? ? ? ? ? 2.066 ? ? 
metalc47 metalc ? ? IA HOH   .   O   ? ? ? 5_445 GA ZN    .  ZN  ? ? B HOH   458 D ZN    306  1_555 ? ? ? ? ? ? ? 2.093 ? ? 
metalc48 metalc ? ? IA HOH   .   O   ? ? ? 5_445 FA ZN    .  ZN  ? ? B HOH   684 D ZN    305  1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc49 metalc ? ? C  HIS   4   NE2 ? ? ? 1_555 AA ZN    .  ZN  ? ? C HIS   4   C ZN    308  1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc50 metalc ? ? C  HIS   10  NE2 ? ? ? 1_555 EA ZN    .  ZN  ? ? C HIS   10  D ZN    304  3_655 ? ? ? ? ? ? ? 2.588 ? ? 
metalc51 metalc ? ? C  HIS   64  NE2 ? ? ? 1_555 AA ZN    .  ZN  ? ? C HIS   64  C ZN    308  1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc52 metalc ? ? C  HIS   94  NE2 ? ? ? 1_555 U  ZN    .  ZN  ? ? C HIS   94  C ZN    302  1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc53 metalc ? ? C  HIS   96  NE2 ? ? ? 1_555 U  ZN    .  ZN  ? ? C HIS   96  C ZN    302  1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc54 metalc ? ? C  HIS   119 ND1 ? ? ? 1_555 U  ZN    .  ZN  ? ? C HIS   119 C ZN    302  1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc55 metalc ? ? T  A1H9O .   N1  ? ? ? 1_555 U  ZN    .  ZN  ? ? C A1H9O 301 C ZN    302  1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc56 metalc ? ? AA ZN    .   ZN  ? ? ? 1_555 JA HOH   .  O   ? ? C ZN    308 C HOH   444  1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc57 metalc ? ? D  ALA   2   N   ? ? ? 1_555 GA ZN    .  ZN  ? ? D ALA   2   D ZN    306  1_555 ? ? ? ? ? ? ? 2.142 ? ? 
metalc58 metalc ? ? D  ALA   2   O   ? ? ? 1_555 GA ZN    .  ZN  ? ? D ALA   2   D ZN    306  1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc59 metalc ? ? D  HIS   4   ND1 ? ? ? 1_555 FA ZN    .  ZN  ? ? D HIS   4   D ZN    305  1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc60 metalc ? ? D  ASP   34  OD1 ? ? ? 1_555 EA ZN    .  ZN  ? ? D ASP   34  D ZN    304  1_555 ? ? ? ? ? ? ? 2.634 ? ? 
metalc61 metalc ? ? D  ASP   34  OD2 ? ? ? 1_555 EA ZN    .  ZN  ? ? D ASP   34  D ZN    304  1_555 ? ? ? ? ? ? ? 1.974 ? ? 
metalc62 metalc ? ? D  HIS   36  ND1 ? ? ? 1_555 EA ZN    .  ZN  ? ? D HIS   36  D ZN    304  1_555 ? ? ? ? ? ? ? 1.912 ? ? 
metalc63 metalc ? ? D  HIS   94  NE2 ? ? ? 1_555 CA ZN    .  ZN  ? ? D HIS   94  D ZN    302  1_555 ? ? ? ? ? ? ? 1.998 ? ? 
metalc64 metalc ? ? D  HIS   96  NE2 ? ? ? 1_555 CA ZN    .  ZN  ? ? D HIS   96  D ZN    302  1_555 ? ? ? ? ? ? ? 2.042 ? ? 
metalc65 metalc ? ? D  HIS   119 ND1 ? ? ? 1_555 CA ZN    .  ZN  ? ? D HIS   119 D ZN    302  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc66 metalc ? ? BA A1H9O .   N1  ? ? ? 1_555 CA ZN    .  ZN  ? ? D A1H9O 301 D ZN    302  1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc67 metalc ? ? FA ZN    .   ZN  ? ? ? 1_555 KA HOH   .  O   ? ? D ZN    305 D HOH   672  1_555 ? ? ? ? ? ? ? 2.058 ? ? 
# 
_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   N   ? A  ALA   2   ? A ALA   2    ? 1_555 ZN  ? AA ZN    . ? C ZN    308 ? 6_554 O   ? A  ALA   2   ? A ALA   2    ? 1_555 
74.6  ? 
2   N   ? A  ALA   2   ? A ALA   2    ? 1_555 ZN  ? AA ZN    . ? C ZN    308 ? 6_554 NE2 ? C  HIS   4   ? C HIS   4    ? 1_555 
77.1  ? 
3   O   ? A  ALA   2   ? A ALA   2    ? 1_555 ZN  ? AA ZN    . ? C ZN    308 ? 6_554 NE2 ? C  HIS   4   ? C HIS   4    ? 1_555 
42.9  ? 
4   N   ? A  ALA   2   ? A ALA   2    ? 1_555 ZN  ? AA ZN    . ? C ZN    308 ? 6_554 NE2 ? C  HIS   64  ? C HIS   64   ? 1_555 
78.3  ? 
5   O   ? A  ALA   2   ? A ALA   2    ? 1_555 ZN  ? AA ZN    . ? C ZN    308 ? 6_554 NE2 ? C  HIS   64  ? C HIS   64   ? 1_555 
42.7  ? 
6   NE2 ? C  HIS   4   ? C HIS   4    ? 1_555 ZN  ? AA ZN    . ? C ZN    308 ? 6_554 NE2 ? C  HIS   64  ? C HIS   64   ? 1_555 1.2 
? 
7   N   ? A  ALA   2   ? A ALA   2    ? 1_555 ZN  ? AA ZN    . ? C ZN    308 ? 6_554 O   ? JA HOH   .   ? C HOH   444  ? 1_555 
76.2  ? 
8   O   ? A  ALA   2   ? A ALA   2    ? 1_555 ZN  ? AA ZN    . ? C ZN    308 ? 6_554 O   ? JA HOH   .   ? C HOH   444  ? 1_555 
43.1  ? 
9   NE2 ? C  HIS   4   ? C HIS   4    ? 1_555 ZN  ? AA ZN    . ? C ZN    308 ? 6_554 O   ? JA HOH   .   ? C HOH   444  ? 1_555 1.0 
? 
10  NE2 ? C  HIS   64  ? C HIS   64   ? 1_555 ZN  ? AA ZN    . ? C ZN    308 ? 6_554 O   ? JA HOH   .   ? C HOH   444  ? 1_555 2.2 
? 
11  NE2 ? A  HIS   3   ? A HIS   3    ? 1_555 FE1 ? T  A1H9O . ? C A1H9O 301 ? 6_554 N4  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 
104.1 ? 
12  NE2 ? A  HIS   3   ? A HIS   3    ? 1_555 FE1 ? T  A1H9O . ? C A1H9O 301 ? 6_554 N5  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 
106.5 ? 
13  N4  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 FE1 ? T  A1H9O . ? C A1H9O 301 ? 6_554 N5  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 
95.6  ? 
14  NE2 ? A  HIS   3   ? A HIS   3    ? 1_555 FE1 ? T  A1H9O . ? C A1H9O 301 ? 6_554 N7  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 
100.2 ? 
15  N4  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 FE1 ? T  A1H9O . ? C A1H9O 301 ? 6_554 N7  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 
84.2  ? 
16  N5  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 FE1 ? T  A1H9O . ? C A1H9O 301 ? 6_554 N7  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 
152.4 ? 
17  NE2 ? A  HIS   3   ? A HIS   3    ? 1_555 FE1 ? T  A1H9O . ? C A1H9O 301 ? 6_554 N6  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 
100.0 ? 
18  N4  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 FE1 ? T  A1H9O . ? C A1H9O 301 ? 6_554 N6  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 
154.5 ? 
19  N5  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 FE1 ? T  A1H9O . ? C A1H9O 301 ? 6_554 N6  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 
85.4  ? 
20  N7  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 FE1 ? T  A1H9O . ? C A1H9O 301 ? 6_554 N6  ? T  A1H9O .   ? C A1H9O 301  ? 6_554 
83.4  ? 
21  NE2 ? A  HIS   4   ? A HIS   4    ? 1_555 ZN  ? I  ZN    . ? A ZN    305 ? 1_555 NE2 ? A  HIS   64  ? A HIS   64   ? 1_555 
106.2 ? 
22  NE2 ? A  HIS   4   ? A HIS   4    ? 1_555 ZN  ? I  ZN    . ? A ZN    305 ? 1_555 O   ? HA HOH   .   ? A HOH   1749 ? 1_555 
120.3 ? 
23  NE2 ? A  HIS   64  ? A HIS   64   ? 1_555 ZN  ? I  ZN    . ? A ZN    305 ? 1_555 O   ? HA HOH   .   ? A HOH   1749 ? 1_555 
91.5  ? 
24  NE2 ? A  HIS   4   ? A HIS   4    ? 1_555 ZN  ? I  ZN    . ? A ZN    305 ? 1_555 N   ? C  ALA   2   ? C ALA   2    ? 1_555 
113.7 ? 
25  NE2 ? A  HIS   64  ? A HIS   64   ? 1_555 ZN  ? I  ZN    . ? A ZN    305 ? 1_555 N   ? C  ALA   2   ? C ALA   2    ? 1_555 
30.7  ? 
26  O   ? HA HOH   .   ? A HOH   1749 ? 1_555 ZN  ? I  ZN    . ? A ZN    305 ? 1_555 N   ? C  ALA   2   ? C ALA   2    ? 1_555 
109.9 ? 
27  NE2 ? A  HIS   4   ? A HIS   4    ? 1_555 ZN  ? I  ZN    . ? A ZN    305 ? 1_555 O   ? C  ALA   2   ? C ALA   2    ? 1_555 
113.2 ? 
28  NE2 ? A  HIS   64  ? A HIS   64   ? 1_555 ZN  ? I  ZN    . ? A ZN    305 ? 1_555 O   ? C  ALA   2   ? C ALA   2    ? 1_555 
29.8  ? 
29  O   ? HA HOH   .   ? A HOH   1749 ? 1_555 ZN  ? I  ZN    . ? A ZN    305 ? 1_555 O   ? C  ALA   2   ? C ALA   2    ? 1_555 
109.7 ? 
30  N   ? C  ALA   2   ? C ALA   2    ? 1_555 ZN  ? I  ZN    . ? A ZN    305 ? 1_555 O   ? C  ALA   2   ? C ALA   2    ? 1_555 1.0 
? 
31  ND1 ? A  HIS   4   ? A HIS   4    ? 1_555 ZN  ? K  ZN    . ? A ZN    307 ? 1_555 O   ? HA HOH   .   ? A HOH   1988 ? 1_555 
103.8 ? 
32  ND1 ? A  HIS   4   ? A HIS   4    ? 1_555 ZN  ? K  ZN    . ? A ZN    307 ? 1_555 ND1 ? C  HIS   4   ? C HIS   4    ? 1_555 
63.9  ? 
33  O   ? HA HOH   .   ? A HOH   1988 ? 1_555 ZN  ? K  ZN    . ? A ZN    307 ? 1_555 ND1 ? C  HIS   4   ? C HIS   4    ? 1_555 
52.7  ? 
34  ND1 ? A  HIS   4   ? A HIS   4    ? 1_555 ZN  ? K  ZN    . ? A ZN    307 ? 1_555 O   ? JA HOH   .   ? C HOH   679  ? 6_554 
118.5 ? 
35  O   ? HA HOH   .   ? A HOH   1988 ? 1_555 ZN  ? K  ZN    . ? A ZN    307 ? 1_555 O   ? JA HOH   .   ? C HOH   679  ? 6_554 
108.0 ? 
36  ND1 ? C  HIS   4   ? C HIS   4    ? 1_555 ZN  ? K  ZN    . ? A ZN    307 ? 1_555 O   ? JA HOH   .   ? C HOH   679  ? 6_554 
97.6  ? 
37  NE2 ? A  HIS   10  ? A HIS   10   ? 1_555 ZN  ? J  ZN    . ? A ZN    306 ? 8_544 OD1 ? A  ASP   34  ? A ASP   34   ? 1_555 
58.6  ? 
38  NE2 ? A  HIS   10  ? A HIS   10   ? 1_555 ZN  ? J  ZN    . ? A ZN    306 ? 8_544 OD2 ? A  ASP   34  ? A ASP   34   ? 1_555 
60.5  ? 
39  OD1 ? A  ASP   34  ? A ASP   34   ? 1_555 ZN  ? J  ZN    . ? A ZN    306 ? 8_544 OD2 ? A  ASP   34  ? A ASP   34   ? 1_555 2.0 
? 
40  NE2 ? A  HIS   10  ? A HIS   10   ? 1_555 ZN  ? J  ZN    . ? A ZN    306 ? 8_544 ND1 ? A  HIS   36  ? A HIS   36   ? 1_555 
62.2  ? 
41  OD1 ? A  ASP   34  ? A ASP   34   ? 1_555 ZN  ? J  ZN    . ? A ZN    306 ? 8_544 ND1 ? A  HIS   36  ? A HIS   36   ? 1_555 4.7 
? 
42  OD2 ? A  ASP   34  ? A ASP   34   ? 1_555 ZN  ? J  ZN    . ? A ZN    306 ? 8_544 ND1 ? A  HIS   36  ? A HIS   36   ? 1_555 2.9 
? 
43  NE2 ? A  HIS   10  ? A HIS   10   ? 1_555 ZN  ? J  ZN    . ? A ZN    306 ? 8_544 O   ? HA HOH   .   ? A HOH   1895 ? 1_555 
64.7  ? 
44  OD1 ? A  ASP   34  ? A ASP   34   ? 1_555 ZN  ? J  ZN    . ? A ZN    306 ? 8_544 O   ? HA HOH   .   ? A HOH   1895 ? 1_555 6.6 
? 
45  OD2 ? A  ASP   34  ? A ASP   34   ? 1_555 ZN  ? J  ZN    . ? A ZN    306 ? 8_544 O   ? HA HOH   .   ? A HOH   1895 ? 1_555 4.5 
? 
46  ND1 ? A  HIS   36  ? A HIS   36   ? 1_555 ZN  ? J  ZN    . ? A ZN    306 ? 8_544 O   ? HA HOH   .   ? A HOH   1895 ? 1_555 2.5 
? 
47  NE2 ? A  HIS   94  ? A HIS   94   ? 1_555 ZN  ? F  ZN    . ? A ZN    302 ? 1_555 NE2 ? A  HIS   96  ? A HIS   96   ? 1_555 
103.0 ? 
48  NE2 ? A  HIS   94  ? A HIS   94   ? 1_555 ZN  ? F  ZN    . ? A ZN    302 ? 1_555 ND1 ? A  HIS   119 ? A HIS   119  ? 1_555 
111.0 ? 
49  NE2 ? A  HIS   96  ? A HIS   96   ? 1_555 ZN  ? F  ZN    . ? A ZN    302 ? 1_555 ND1 ? A  HIS   119 ? A HIS   119  ? 1_555 
97.0  ? 
50  NE2 ? A  HIS   94  ? A HIS   94   ? 1_555 ZN  ? F  ZN    . ? A ZN    302 ? 1_555 N1  ? E  A1H9O .   ? A A1H9O 301  ? 1_555 
111.4 ? 
51  NE2 ? A  HIS   96  ? A HIS   96   ? 1_555 ZN  ? F  ZN    . ? A ZN    302 ? 1_555 N1  ? E  A1H9O .   ? A A1H9O 301  ? 1_555 
113.8 ? 
52  ND1 ? A  HIS   119 ? A HIS   119  ? 1_555 ZN  ? F  ZN    . ? A ZN    302 ? 1_555 N1  ? E  A1H9O .   ? A A1H9O 301  ? 1_555 
118.8 ? 
53  NE2 ? C  HIS   3   ? C HIS   3    ? 1_555 FE1 ? E  A1H9O . ? A A1H9O 301 ? 8_545 N4  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 
103.9 ? 
54  NE2 ? C  HIS   3   ? C HIS   3    ? 1_555 FE1 ? E  A1H9O . ? A A1H9O 301 ? 8_545 N5  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 
107.3 ? 
55  N4  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 FE1 ? E  A1H9O . ? A A1H9O 301 ? 8_545 N5  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 
95.6  ? 
56  NE2 ? C  HIS   3   ? C HIS   3    ? 1_555 FE1 ? E  A1H9O . ? A A1H9O 301 ? 8_545 N7  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 
99.7  ? 
57  N4  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 FE1 ? E  A1H9O . ? A A1H9O 301 ? 8_545 N7  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 
84.2  ? 
58  N5  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 FE1 ? E  A1H9O . ? A A1H9O 301 ? 8_545 N7  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 
152.1 ? 
59  NE2 ? C  HIS   3   ? C HIS   3    ? 1_555 FE1 ? E  A1H9O . ? A A1H9O 301 ? 8_545 N6  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 
99.9  ? 
60  N4  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 FE1 ? E  A1H9O . ? A A1H9O 301 ? 8_545 N6  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 
154.7 ? 
61  N5  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 FE1 ? E  A1H9O . ? A A1H9O 301 ? 8_545 N6  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 
85.4  ? 
62  N7  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 FE1 ? E  A1H9O . ? A A1H9O 301 ? 8_545 N6  ? E  A1H9O .   ? A A1H9O 301  ? 8_545 
83.3  ? 
63  N   ? B  ALA   2   ? B ALA   2    ? 1_555 ZN  ? S  ZN    . ? B ZN    308 ? 1_555 O   ? B  ALA   2   ? B ALA   2    ? 1_555 
73.5  ? 
64  N   ? B  ALA   2   ? B ALA   2    ? 1_555 ZN  ? S  ZN    . ? B ZN    308 ? 1_555 NE2 ? D  HIS   4   ? D HIS   4    ? 1_555 
156.1 ? 
65  O   ? B  ALA   2   ? B ALA   2    ? 1_555 ZN  ? S  ZN    . ? B ZN    308 ? 1_555 NE2 ? D  HIS   4   ? D HIS   4    ? 1_555 
84.7  ? 
66  N   ? B  ALA   2   ? B ALA   2    ? 1_555 ZN  ? S  ZN    . ? B ZN    308 ? 1_555 NE2 ? D  HIS   64  ? D HIS   64   ? 1_555 
154.5 ? 
67  O   ? B  ALA   2   ? B ALA   2    ? 1_555 ZN  ? S  ZN    . ? B ZN    308 ? 1_555 NE2 ? D  HIS   64  ? D HIS   64   ? 1_555 
82.4  ? 
68  NE2 ? D  HIS   4   ? D HIS   4    ? 1_555 ZN  ? S  ZN    . ? B ZN    308 ? 1_555 NE2 ? D  HIS   64  ? D HIS   64   ? 1_555 2.7 
? 
69  N   ? B  ALA   2   ? B ALA   2    ? 1_555 ZN  ? S  ZN    . ? B ZN    308 ? 1_555 O   ? KA HOH   .   ? D HOH   455  ? 9_544 
109.3 ? 
70  O   ? B  ALA   2   ? B ALA   2    ? 1_555 ZN  ? S  ZN    . ? B ZN    308 ? 1_555 O   ? KA HOH   .   ? D HOH   455  ? 9_544 
78.9  ? 
71  NE2 ? D  HIS   4   ? D HIS   4    ? 1_555 ZN  ? S  ZN    . ? B ZN    308 ? 1_555 O   ? KA HOH   .   ? D HOH   455  ? 9_544 
75.1  ? 
72  NE2 ? D  HIS   64  ? D HIS   64   ? 1_555 ZN  ? S  ZN    . ? B ZN    308 ? 1_555 O   ? KA HOH   .   ? D HOH   455  ? 9_544 
73.3  ? 
73  NE2 ? B  HIS   3   ? B HIS   3    ? 1_555 FE1 ? BA A1H9O . ? D A1H9O 301 ? 9_544 N4  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 
104.8 ? 
74  NE2 ? B  HIS   3   ? B HIS   3    ? 1_555 FE1 ? BA A1H9O . ? D A1H9O 301 ? 9_544 N5  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 
106.6 ? 
75  N4  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 FE1 ? BA A1H9O . ? D A1H9O 301 ? 9_544 N5  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 
95.6  ? 
76  NE2 ? B  HIS   3   ? B HIS   3    ? 1_555 FE1 ? BA A1H9O . ? D A1H9O 301 ? 9_544 N7  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 
100.5 ? 
77  N4  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 FE1 ? BA A1H9O . ? D A1H9O 301 ? 9_544 N7  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 
84.2  ? 
78  N5  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 FE1 ? BA A1H9O . ? D A1H9O 301 ? 9_544 N7  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 
152.0 ? 
79  NE2 ? B  HIS   3   ? B HIS   3    ? 1_555 FE1 ? BA A1H9O . ? D A1H9O 301 ? 9_544 N6  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 
99.4  ? 
80  N4  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 FE1 ? BA A1H9O . ? D A1H9O 301 ? 9_544 N6  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 
154.4 ? 
81  N5  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 FE1 ? BA A1H9O . ? D A1H9O 301 ? 9_544 N6  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 
85.4  ? 
82  N7  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 FE1 ? BA A1H9O . ? D A1H9O 301 ? 9_544 N6  ? BA A1H9O .   ? D A1H9O 301  ? 9_544 
83.2  ? 
83  ND1 ? B  HIS   4   ? B HIS   4    ? 1_555 ZN  ? FA ZN    . ? D ZN    305 ? 9_544 O   ? IA HOH   .   ? B HOH   684  ? 5_445 
32.5  ? 
84  ND1 ? B  HIS   4   ? B HIS   4    ? 1_555 ZN  ? FA ZN    . ? D ZN    305 ? 9_544 ND1 ? D  HIS   4   ? D HIS   4    ? 1_555 
32.2  ? 
85  O   ? IA HOH   .   ? B HOH   684  ? 5_445 ZN  ? FA ZN    . ? D ZN    305 ? 9_544 ND1 ? D  HIS   4   ? D HIS   4    ? 1_555 0.3 
? 
86  ND1 ? B  HIS   4   ? B HIS   4    ? 1_555 ZN  ? FA ZN    . ? D ZN    305 ? 9_544 O   ? KA HOH   .   ? D HOH   672  ? 1_555 
34.9  ? 
87  O   ? IA HOH   .   ? B HOH   684  ? 5_445 ZN  ? FA ZN    . ? D ZN    305 ? 9_544 O   ? KA HOH   .   ? D HOH   672  ? 1_555 3.5 
? 
88  ND1 ? D  HIS   4   ? D HIS   4    ? 1_555 ZN  ? FA ZN    . ? D ZN    305 ? 9_544 O   ? KA HOH   .   ? D HOH   672  ? 1_555 3.6 
? 
89  NE2 ? B  HIS   4   ? B HIS   4    ? 1_555 ZN  ? GA ZN    . ? D ZN    306 ? 9_544 NE2 ? B  HIS   64  ? B HIS   64   ? 1_555 
106.3 ? 
90  NE2 ? B  HIS   4   ? B HIS   4    ? 1_555 ZN  ? GA ZN    . ? D ZN    306 ? 9_544 O   ? IA HOH   .   ? B HOH   458  ? 5_445 
140.0 ? 
91  NE2 ? B  HIS   64  ? B HIS   64   ? 1_555 ZN  ? GA ZN    . ? D ZN    306 ? 9_544 O   ? IA HOH   .   ? B HOH   458  ? 5_445 
96.1  ? 
92  NE2 ? B  HIS   4   ? B HIS   4    ? 1_555 ZN  ? GA ZN    . ? D ZN    306 ? 9_544 N   ? D  ALA   2   ? D ALA   2    ? 1_555 
136.1 ? 
93  NE2 ? B  HIS   64  ? B HIS   64   ? 1_555 ZN  ? GA ZN    . ? D ZN    306 ? 9_544 N   ? D  ALA   2   ? D ALA   2    ? 1_555 
97.6  ? 
94  O   ? IA HOH   .   ? B HOH   458  ? 5_445 ZN  ? GA ZN    . ? D ZN    306 ? 9_544 N   ? D  ALA   2   ? D ALA   2    ? 1_555 3.9 
? 
95  NE2 ? B  HIS   4   ? B HIS   4    ? 1_555 ZN  ? GA ZN    . ? D ZN    306 ? 9_544 O   ? D  ALA   2   ? D ALA   2    ? 1_555 
137.4 ? 
96  NE2 ? B  HIS   64  ? B HIS   64   ? 1_555 ZN  ? GA ZN    . ? D ZN    306 ? 9_544 O   ? D  ALA   2   ? D ALA   2    ? 1_555 
95.2  ? 
97  O   ? IA HOH   .   ? B HOH   458  ? 5_445 ZN  ? GA ZN    . ? D ZN    306 ? 9_544 O   ? D  ALA   2   ? D ALA   2    ? 1_555 3.8 
? 
98  N   ? D  ALA   2   ? D ALA   2    ? 1_555 ZN  ? GA ZN    . ? D ZN    306 ? 9_544 O   ? D  ALA   2   ? D ALA   2    ? 1_555 2.4 
? 
99  NE2 ? B  HIS   10  ? B HIS   10   ? 1_555 ZN  ? Q  ZN    . ? B ZN    306 ? 1_555 O   ? IA HOH   .   ? B HOH   613  ? 1_555 
78.3  ? 
100 NE2 ? B  HIS   10  ? B HIS   10   ? 1_555 ZN  ? Q  ZN    . ? B ZN    306 ? 1_555 OD1 ? C  ASP   34  ? C ASP   34   ? 1_555 
36.5  ? 
101 O   ? IA HOH   .   ? B HOH   613  ? 1_555 ZN  ? Q  ZN    . ? B ZN    306 ? 1_555 OD1 ? C  ASP   34  ? C ASP   34   ? 1_555 
114.5 ? 
102 NE2 ? B  HIS   10  ? B HIS   10   ? 1_555 ZN  ? Q  ZN    . ? B ZN    306 ? 1_555 OD2 ? C  ASP   34  ? C ASP   34   ? 1_555 
38.9  ? 
103 O   ? IA HOH   .   ? B HOH   613  ? 1_555 ZN  ? Q  ZN    . ? B ZN    306 ? 1_555 OD2 ? C  ASP   34  ? C ASP   34   ? 1_555 
116.6 ? 
104 OD1 ? C  ASP   34  ? C ASP   34   ? 1_555 ZN  ? Q  ZN    . ? B ZN    306 ? 1_555 OD2 ? C  ASP   34  ? C ASP   34   ? 1_555 2.5 
? 
105 NE2 ? B  HIS   10  ? B HIS   10   ? 1_555 ZN  ? Q  ZN    . ? B ZN    306 ? 1_555 ND1 ? C  HIS   36  ? C HIS   36   ? 1_555 
36.9  ? 
106 O   ? IA HOH   .   ? B HOH   613  ? 1_555 ZN  ? Q  ZN    . ? B ZN    306 ? 1_555 ND1 ? C  HIS   36  ? C HIS   36   ? 1_555 
114.8 ? 
107 OD1 ? C  ASP   34  ? C ASP   34   ? 1_555 ZN  ? Q  ZN    . ? B ZN    306 ? 1_555 ND1 ? C  HIS   36  ? C HIS   36   ? 1_555 0.6 
? 
108 OD2 ? C  ASP   34  ? C ASP   34   ? 1_555 ZN  ? Q  ZN    . ? B ZN    306 ? 1_555 ND1 ? C  HIS   36  ? C HIS   36   ? 1_555 2.0 
? 
109 OD1 ? B  ASP   34  ? B ASP   34   ? 1_555 ZN  ? R  ZN    . ? B ZN    307 ? 1_555 OD2 ? B  ASP   34  ? B ASP   34   ? 1_555 
57.5  ? 
110 OD1 ? B  ASP   34  ? B ASP   34   ? 1_555 ZN  ? R  ZN    . ? B ZN    307 ? 1_555 ND1 ? B  HIS   36  ? B HIS   36   ? 1_555 
107.2 ? 
111 OD2 ? B  ASP   34  ? B ASP   34   ? 1_555 ZN  ? R  ZN    . ? B ZN    307 ? 1_555 ND1 ? B  HIS   36  ? B HIS   36   ? 1_555 
146.1 ? 
112 OD1 ? B  ASP   34  ? B ASP   34   ? 1_555 ZN  ? R  ZN    . ? B ZN    307 ? 1_555 O   ? IA HOH   .   ? B HOH   481  ? 1_555 
118.1 ? 
113 OD2 ? B  ASP   34  ? B ASP   34   ? 1_555 ZN  ? R  ZN    . ? B ZN    307 ? 1_555 O   ? IA HOH   .   ? B HOH   481  ? 1_555 
72.8  ? 
114 ND1 ? B  HIS   36  ? B HIS   36   ? 1_555 ZN  ? R  ZN    . ? B ZN    307 ? 1_555 O   ? IA HOH   .   ? B HOH   481  ? 1_555 
93.7  ? 
115 OD1 ? B  ASP   34  ? B ASP   34   ? 1_555 ZN  ? R  ZN    . ? B ZN    307 ? 1_555 NE2 ? D  HIS   10  ? D HIS   10   ? 1_555 
64.6  ? 
116 OD2 ? B  ASP   34  ? B ASP   34   ? 1_555 ZN  ? R  ZN    . ? B ZN    307 ? 1_555 NE2 ? D  HIS   10  ? D HIS   10   ? 1_555 
48.7  ? 
117 ND1 ? B  HIS   36  ? B HIS   36   ? 1_555 ZN  ? R  ZN    . ? B ZN    307 ? 1_555 NE2 ? D  HIS   10  ? D HIS   10   ? 1_555 
98.0  ? 
118 O   ? IA HOH   .   ? B HOH   481  ? 1_555 ZN  ? R  ZN    . ? B ZN    307 ? 1_555 NE2 ? D  HIS   10  ? D HIS   10   ? 1_555 
55.0  ? 
119 NE2 ? B  HIS   94  ? B HIS   94   ? 1_555 ZN  ? M  ZN    . ? B ZN    302 ? 1_555 NE2 ? B  HIS   96  ? B HIS   96   ? 1_555 
103.0 ? 
120 NE2 ? B  HIS   94  ? B HIS   94   ? 1_555 ZN  ? M  ZN    . ? B ZN    302 ? 1_555 ND1 ? B  HIS   119 ? B HIS   119  ? 1_555 
111.0 ? 
121 NE2 ? B  HIS   96  ? B HIS   96   ? 1_555 ZN  ? M  ZN    . ? B ZN    302 ? 1_555 ND1 ? B  HIS   119 ? B HIS   119  ? 1_555 
97.8  ? 
122 NE2 ? B  HIS   94  ? B HIS   94   ? 1_555 ZN  ? M  ZN    . ? B ZN    302 ? 1_555 N1  ? L  A1H9O .   ? B A1H9O 301  ? 1_555 
111.0 ? 
123 NE2 ? B  HIS   96  ? B HIS   96   ? 1_555 ZN  ? M  ZN    . ? B ZN    302 ? 1_555 N1  ? L  A1H9O .   ? B A1H9O 301  ? 1_555 
114.0 ? 
124 ND1 ? B  HIS   119 ? B HIS   119  ? 1_555 ZN  ? M  ZN    . ? B ZN    302 ? 1_555 N1  ? L  A1H9O .   ? B A1H9O 301  ? 1_555 
118.4 ? 
125 NE2 ? D  HIS   3   ? D HIS   3    ? 1_555 FE1 ? L  A1H9O . ? B A1H9O 301 ? 5_445 N4  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 
103.7 ? 
126 NE2 ? D  HIS   3   ? D HIS   3    ? 1_555 FE1 ? L  A1H9O . ? B A1H9O 301 ? 5_445 N5  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 
106.3 ? 
127 N4  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 FE1 ? L  A1H9O . ? B A1H9O 301 ? 5_445 N5  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 
95.6  ? 
128 NE2 ? D  HIS   3   ? D HIS   3    ? 1_555 FE1 ? L  A1H9O . ? B A1H9O 301 ? 5_445 N7  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 
101.0 ? 
129 N4  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 FE1 ? L  A1H9O . ? B A1H9O 301 ? 5_445 N7  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 
84.1  ? 
130 N5  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 FE1 ? L  A1H9O . ? B A1H9O 301 ? 5_445 N7  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 
151.9 ? 
131 NE2 ? D  HIS   3   ? D HIS   3    ? 1_555 FE1 ? L  A1H9O . ? B A1H9O 301 ? 5_445 N6  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 
100.8 ? 
132 N4  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 FE1 ? L  A1H9O . ? B A1H9O 301 ? 5_445 N6  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 
154.2 ? 
133 N5  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 FE1 ? L  A1H9O . ? B A1H9O 301 ? 5_445 N6  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 
85.3  ? 
134 N7  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 FE1 ? L  A1H9O . ? B A1H9O 301 ? 5_445 N6  ? L  A1H9O .   ? B A1H9O 301  ? 5_445 
83.2  ? 
135 NE2 ? C  HIS   10  ? C HIS   10   ? 1_555 ZN  ? EA ZN    . ? D ZN    304 ? 3_655 OD1 ? D  ASP   34  ? D ASP   34   ? 1_555 
139.6 ? 
136 NE2 ? C  HIS   10  ? C HIS   10   ? 1_555 ZN  ? EA ZN    . ? D ZN    304 ? 3_655 OD2 ? D  ASP   34  ? D ASP   34   ? 1_555 
140.7 ? 
137 OD1 ? D  ASP   34  ? D ASP   34   ? 1_555 ZN  ? EA ZN    . ? D ZN    304 ? 3_655 OD2 ? D  ASP   34  ? D ASP   34   ? 1_555 2.8 
? 
138 NE2 ? C  HIS   10  ? C HIS   10   ? 1_555 ZN  ? EA ZN    . ? D ZN    304 ? 3_655 ND1 ? D  HIS   36  ? D HIS   36   ? 1_555 
143.9 ? 
139 OD1 ? D  ASP   34  ? D ASP   34   ? 1_555 ZN  ? EA ZN    . ? D ZN    304 ? 3_655 ND1 ? D  HIS   36  ? D HIS   36   ? 1_555 4.4 
? 
140 OD2 ? D  ASP   34  ? D ASP   34   ? 1_555 ZN  ? EA ZN    . ? D ZN    304 ? 3_655 ND1 ? D  HIS   36  ? D HIS   36   ? 1_555 4.5 
? 
141 NE2 ? C  HIS   94  ? C HIS   94   ? 1_555 ZN  ? U  ZN    . ? C ZN    302 ? 1_555 NE2 ? C  HIS   96  ? C HIS   96   ? 1_555 
103.8 ? 
142 NE2 ? C  HIS   94  ? C HIS   94   ? 1_555 ZN  ? U  ZN    . ? C ZN    302 ? 1_555 ND1 ? C  HIS   119 ? C HIS   119  ? 1_555 
111.5 ? 
143 NE2 ? C  HIS   96  ? C HIS   96   ? 1_555 ZN  ? U  ZN    . ? C ZN    302 ? 1_555 ND1 ? C  HIS   119 ? C HIS   119  ? 1_555 
98.4  ? 
144 NE2 ? C  HIS   94  ? C HIS   94   ? 1_555 ZN  ? U  ZN    . ? C ZN    302 ? 1_555 N1  ? T  A1H9O .   ? C A1H9O 301  ? 1_555 
110.4 ? 
145 NE2 ? C  HIS   96  ? C HIS   96   ? 1_555 ZN  ? U  ZN    . ? C ZN    302 ? 1_555 N1  ? T  A1H9O .   ? C A1H9O 301  ? 1_555 
113.3 ? 
146 ND1 ? C  HIS   119 ? C HIS   119  ? 1_555 ZN  ? U  ZN    . ? C ZN    302 ? 1_555 N1  ? T  A1H9O .   ? C A1H9O 301  ? 1_555 
117.9 ? 
147 NE2 ? D  HIS   94  ? D HIS   94   ? 1_555 ZN  ? CA ZN    . ? D ZN    302 ? 1_555 NE2 ? D  HIS   96  ? D HIS   96   ? 1_555 
102.1 ? 
148 NE2 ? D  HIS   94  ? D HIS   94   ? 1_555 ZN  ? CA ZN    . ? D ZN    302 ? 1_555 ND1 ? D  HIS   119 ? D HIS   119  ? 1_555 
111.0 ? 
149 NE2 ? D  HIS   96  ? D HIS   96   ? 1_555 ZN  ? CA ZN    . ? D ZN    302 ? 1_555 ND1 ? D  HIS   119 ? D HIS   119  ? 1_555 
98.9  ? 
150 NE2 ? D  HIS   94  ? D HIS   94   ? 1_555 ZN  ? CA ZN    . ? D ZN    302 ? 1_555 N1  ? BA A1H9O .   ? D A1H9O 301  ? 1_555 
111.5 ? 
151 NE2 ? D  HIS   96  ? D HIS   96   ? 1_555 ZN  ? CA ZN    . ? D ZN    302 ? 1_555 N1  ? BA A1H9O .   ? D A1H9O 301  ? 1_555 
113.0 ? 
152 ND1 ? D  HIS   119 ? D HIS   119  ? 1_555 ZN  ? CA ZN    . ? D ZN    302 ? 1_555 N1  ? BA A1H9O .   ? D A1H9O 301  ? 1_555 
118.4 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 0.14  
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 6.59  
3 SER 29  B . ? SER 29  B PRO 30  B ? PRO 30  B 1 -0.24 
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 7.87  
5 SER 29  C . ? SER 29  C PRO 30  C ? PRO 30  C 1 -0.32 
6 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 7.57  
7 SER 29  D . ? SER 29  D PRO 30  D ? PRO 30  D 1 0.53  
8 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 6.97  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
AA7 ? 2  ? 
AA8 ? 10 ? 
AA9 ? 6  ? 
AB1 ? 2  ? 
AB2 ? 10 ? 
AB3 ? 6  ? 
# 
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      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? parallel      
AA7 1 2  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA8 3 4  ? anti-parallel 
AA8 4 5  ? parallel      
AA8 5 6  ? anti-parallel 
AA8 6 7  ? anti-parallel 
AA8 7 8  ? anti-parallel 
AA8 8 9  ? anti-parallel 
AA8 9 10 ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AA9 4 5  ? anti-parallel 
AA9 5 6  ? parallel      
AB1 1 2  ? parallel      
AB2 1 2  ? parallel      
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB2 4 5  ? parallel      
AB2 5 6  ? anti-parallel 
AB2 6 7  ? anti-parallel 
AB2 7 8  ? anti-parallel 
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? anti-parallel 
AB3 5 6  ? 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  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 256 ALA A 257 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 206 LEU A 211 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 172 ASP A 174 
AA3 1  LYS A 45  ? SER A 50  ? LYS A 45  SER A 50  
AA3 2  VAL A 78  ? GLY A 82  ? VAL A 78  GLY A 82  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 215 VAL A 217 
AA4 1  ASP B 32  ? ILE B 33  ? ASP B 32  ILE B 33  
AA4 2  THR B 108 ? VAL B 109 ? THR B 108 VAL B 109 
AA5 1  LYS B 39  ? TYR B 40  ? LYS B 39  TYR B 40  
AA5 2  LYS B 256 ? ALA B 257 ? LYS B 256 ALA B 257 
AA5 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
AA5 4  VAL B 206 ? LEU B 211 ? VAL B 206 LEU B 211 
AA5 5  LEU B 140 ? VAL B 149 ? LEU B 140 VAL B 149 
AA5 6  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
AA5 7  TYR B 88  ? TRP B 97  ? TYR B 88  TRP B 97  
AA5 8  PHE B 66  ? PHE B 70  ? PHE B 66  PHE B 70  
AA5 9  SER B 56  ? ASN B 61  ? SER B 56  ASN B 61  
AA5 10 SER B 172 ? ASP B 174 ? SER B 172 ASP B 174 
AA6 1  LYS B 45  ? SER B 50  ? LYS B 45  SER B 50  
AA6 2  VAL B 78  ? GLY B 82  ? VAL B 78  GLY B 82  
AA6 3  TYR B 88  ? TRP B 97  ? TYR B 88  TRP B 97  
AA6 4  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
AA6 5  LEU B 140 ? VAL B 149 ? LEU B 140 VAL B 149 
AA6 6  ILE B 215 ? VAL B 217 ? ILE B 215 VAL B 217 
AA7 1  ASP C 32  ? ILE C 33  ? ASP C 32  ILE C 33  
AA7 2  THR C 108 ? VAL C 109 ? THR C 108 VAL C 109 
AA8 1  LYS C 39  ? TYR C 40  ? LYS C 39  TYR C 40  
AA8 2  LYS C 256 ? ALA C 257 ? LYS C 256 ALA C 257 
AA8 3  TYR C 190 ? GLY C 195 ? TYR C 190 GLY C 195 
AA8 4  VAL C 206 ? LEU C 211 ? VAL C 206 LEU C 211 
AA8 5  LEU C 140 ? VAL C 149 ? LEU C 140 VAL C 149 
AA8 6  ALA C 116 ? ASN C 124 ? ALA C 116 ASN C 124 
AA8 7  TYR C 88  ? TRP C 97  ? TYR C 88  TRP C 97  
AA8 8  PHE C 66  ? PHE C 70  ? PHE C 66  PHE C 70  
AA8 9  SER C 56  ? ASN C 61  ? SER C 56  ASN C 61  
AA8 10 SER C 172 ? ASP C 174 ? SER C 172 ASP C 174 
AA9 1  LYS C 45  ? SER C 50  ? LYS C 45  SER C 50  
AA9 2  VAL C 78  ? GLY C 82  ? VAL C 78  GLY C 82  
AA9 3  TYR C 88  ? TRP C 97  ? TYR C 88  TRP C 97  
AA9 4  ALA C 116 ? ASN C 124 ? ALA C 116 ASN C 124 
AA9 5  LEU C 140 ? VAL C 149 ? LEU C 140 VAL C 149 
AA9 6  ILE C 215 ? VAL C 217 ? ILE C 215 VAL C 217 
AB1 1  ASP D 32  ? ILE D 33  ? ASP D 32  ILE D 33  
AB1 2  THR D 108 ? VAL D 109 ? THR D 108 VAL D 109 
AB2 1  LYS D 39  ? TYR D 40  ? LYS D 39  TYR D 40  
AB2 2  LYS D 256 ? ALA D 257 ? LYS D 256 ALA D 257 
AB2 3  TYR D 190 ? GLY D 195 ? TYR D 190 GLY D 195 
AB2 4  VAL D 206 ? LEU D 211 ? VAL D 206 LEU D 211 
AB2 5  LEU D 140 ? VAL D 149 ? LEU D 140 VAL D 149 
AB2 6  ALA D 116 ? ASN D 124 ? ALA D 116 ASN D 124 
AB2 7  TYR D 88  ? TRP D 97  ? TYR D 88  TRP D 97  
AB2 8  PHE D 66  ? PHE D 70  ? PHE D 66  PHE D 70  
AB2 9  SER D 56  ? ASN D 61  ? SER D 56  ASN D 61  
AB2 10 SER D 172 ? ASP D 174 ? SER D 172 ASP D 174 
AB3 1  LYS D 45  ? SER D 50  ? LYS D 45  SER D 50  
AB3 2  VAL D 78  ? GLY D 82  ? VAL D 78  GLY D 82  
AB3 3  TYR D 88  ? TRP D 97  ? TYR D 88  TRP D 97  
AB3 4  ALA D 116 ? ASN D 124 ? ALA D 116 ASN D 124 
AB3 5  LEU D 140 ? VAL D 149 ? LEU D 140 VAL D 149 
AB3 6  ILE D 215 ? VAL D 217 ? ILE D 215 VAL D 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 257 
AA2 2 3  O LYS A 256 ? O LYS A 256 N THR A 192 ? N THR A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O LEU A 211 ? O LEU A 211 N GLY A 144 ? N GLY A 144 
AA2 5 6  O ILE A 145 ? O ILE A 145 N LEU A 118 ? N LEU A 118 
AA2 6 7  O VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 173 
AA3 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 145 
AA3 5 6  N LYS A 148 ? N LYS A 148 O ILE A 215 ? O ILE A 215 
AA4 1 2  N ILE B 33  ? N ILE B 33  O THR B 108 ? O THR B 108 
AA5 1 2  N LYS B 39  ? N LYS B 39  O ALA B 257 ? O ALA B 257 
AA5 2 3  O LYS B 256 ? O LYS B 256 N THR B 192 ? N THR B 192 
AA5 3 4  N GLY B 195 ? N GLY B 195 O VAL B 206 ? O VAL B 206 
AA5 4 5  O LEU B 211 ? O LEU B 211 N GLY B 144 ? N GLY B 144 
AA5 5 6  O ILE B 145 ? O ILE B 145 N LEU B 118 ? N LEU B 118 
AA5 6 7  O VAL B 121 ? O VAL B 121 N GLN B 92  ? N GLN B 92  
AA5 7 8  O PHE B 93  ? O PHE B 93  N VAL B 68  ? N VAL B 68  
AA5 8 9  O GLU B 69  ? O GLU B 69  N LEU B 57  ? N LEU B 57  
AA5 9 10 N ILE B 59  ? N ILE B 59  O ALA B 173 ? O ALA B 173 
AA6 1 2  N SER B 48  ? N SER B 48  O LYS B 80  ? O LYS B 80  
AA6 2 3  N LEU B 79  ? N LEU B 79  O TYR B 88  ? O TYR B 88  
AA6 3 4  N GLN B 92  ? N GLN B 92  O VAL B 121 ? O VAL B 121 
AA6 4 5  N LEU B 118 ? N LEU B 118 O ILE B 145 ? O ILE B 145 
AA6 5 6  N LYS B 148 ? N LYS B 148 O ILE B 215 ? O ILE B 215 
AA7 1 2  N ILE C 33  ? N ILE C 33  O THR C 108 ? O THR C 108 
AA8 1 2  N LYS C 39  ? N LYS C 39  O ALA C 257 ? O ALA C 257 
AA8 2 3  O LYS C 256 ? O LYS C 256 N THR C 192 ? N THR C 192 
AA8 3 4  N GLY C 195 ? N GLY C 195 O VAL C 206 ? O VAL C 206 
AA8 4 5  O LEU C 211 ? O LEU C 211 N GLY C 144 ? N GLY C 144 
AA8 5 6  O ILE C 145 ? O ILE C 145 N LEU C 118 ? N LEU C 118 
AA8 6 7  O VAL C 121 ? O VAL C 121 N GLN C 92  ? N GLN C 92  
AA8 7 8  O PHE C 93  ? O PHE C 93  N VAL C 68  ? N VAL C 68  
AA8 8 9  O GLU C 69  ? O GLU C 69  N LEU C 57  ? N LEU C 57  
AA8 9 10 N ILE C 59  ? N ILE C 59  O ALA C 173 ? O ALA C 173 
AA9 1 2  N SER C 48  ? N SER C 48  O LYS C 80  ? O LYS C 80  
AA9 2 3  N LEU C 79  ? N LEU C 79  O TYR C 88  ? O TYR C 88  
AA9 3 4  N GLN C 92  ? N GLN C 92  O VAL C 121 ? O VAL C 121 
AA9 4 5  N LEU C 118 ? N LEU C 118 O ILE C 145 ? O ILE C 145 
AA9 5 6  N LYS C 148 ? N LYS C 148 O ILE C 215 ? O ILE C 215 
AB1 1 2  N ILE D 33  ? N ILE D 33  O THR D 108 ? O THR D 108 
AB2 1 2  N LYS D 39  ? N LYS D 39  O ALA D 257 ? O ALA D 257 
AB2 2 3  O LYS D 256 ? O LYS D 256 N THR D 192 ? N THR D 192 
AB2 3 4  N GLY D 195 ? N GLY D 195 O VAL D 206 ? O VAL D 206 
AB2 4 5  O LEU D 211 ? O LEU D 211 N GLY D 144 ? N GLY D 144 
AB2 5 6  O ILE D 145 ? O ILE D 145 N LEU D 118 ? N LEU D 118 
AB2 6 7  O VAL D 121 ? O VAL D 121 N GLN D 92  ? N GLN D 92  
AB2 7 8  O PHE D 93  ? O PHE D 93  N VAL D 68  ? N VAL D 68  
AB2 8 9  O GLU D 69  ? O GLU D 69  N LEU D 57  ? N LEU D 57  
AB2 9 10 N ILE D 59  ? N ILE D 59  O ALA D 173 ? O ALA D 173 
AB3 1 2  N SER D 48  ? N SER D 48  O LYS D 80  ? O LYS D 80  
AB3 2 3  N LEU D 79  ? N LEU D 79  O TYR D 88  ? O TYR D 88  
AB3 3 4  N GLN D 92  ? N GLN D 92  O VAL D 121 ? O VAL D 121 
AB3 4 5  N LEU D 118 ? N LEU D 118 O ILE D 145 ? O ILE D 145 
AB3 5 6  N LYS D 148 ? N LYS D 148 O ILE D 215 ? O ILE D 215 
# 
_pdbx_entry_details.entry_id                   9F2F 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O A HOH 1711 ? ? O A HOH 2008 ? ? 1.42 
2  1 O A HOH 1701 ? ? O A HOH 1722 ? ? 1.48 
3  1 O A THR 198  ? ? O A HOH 1701 ? ? 1.61 
4  1 O A HOH 1702 ? ? O A HOH 1846 ? ? 1.78 
5  1 O D HOH 411  ? ? O D HOH 706  ? ? 1.86 
6  1 O A HOH 2008 ? ? O A HOH 2094 ? ? 1.88 
7  1 O B HOH 679  ? ? O B HOH 687  ? ? 1.91 
8  1 O C HOH 551  ? ? O C HOH 749  ? ? 1.95 
9  1 O A HOH 1969 ? ? O A HOH 1982 ? ? 1.97 
10 1 O D HOH 403  ? ? O D HOH 583  ? ? 1.99 
11 1 O D HOH 681  ? ? O D HOH 690  ? ? 2.01 
12 1 O B HOH 438  ? ? O B HOH 772  ? ? 2.06 
13 1 O C HOH 598  ? ? O C HOH 770  ? ? 2.07 
14 1 O B HOH 406  ? ? O B HOH 557  ? ? 2.08 
15 1 O A HOH 1988 ? ? O A HOH 2012 ? ? 2.08 
16 1 O B HOH 459  ? ? O B HOH 711  ? ? 2.08 
17 1 O A HOH 1997 ? ? O A HOH 2002 ? ? 2.08 
18 1 O A HOH 1999 ? ? O A HOH 2097 ? ? 2.12 
19 1 O D HOH 675  ? ? O D HOH 755  ? ? 2.13 
20 1 O A HOH 1944 ? ? O A HOH 1980 ? ? 2.13 
21 1 O C HOH 635  ? ? O C HOH 674  ? ? 2.13 
22 1 O D HOH 689  ? ? O D HOH 788  ? ? 2.14 
23 1 O A HOH 1748 ? ? O A HOH 2060 ? ? 2.14 
24 1 O C HOH 725  ? ? O C HOH 762  ? ? 2.16 
25 1 O D HOH 576  ? ? O D HOH 744  ? ? 2.16 
26 1 O D HOH 672  ? ? O D HOH 700  ? ? 2.17 
27 1 O C HOH 552  ? ? O C HOH 569  ? ? 2.17 
28 1 O D HOH 533  ? ? O D HOH 628  ? ? 2.17 
29 1 O C HOH 679  ? ? O C HOH 710  ? ? 2.17 
30 1 O B HOH 586  ? ? O B HOH 782  ? ? 2.18 
31 1 O D HOH 660  ? ? O D HOH 728  ? ? 2.18 
32 1 O C HOH 519  ? ? O C HOH 657  ? ? 2.19 
33 1 O A HOH 1816 ? ? O A HOH 2048 ? ? 2.19 
34 1 O B HOH 726  ? ? O B HOH 761  ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1  1 O A HOH 1864 ? ? 1_555 O C HOH 692 ? ? 8_544 1.77 
2  1 O A HOH 2010 ? ? 1_555 O C HOH 679 ? ? 6_554 1.82 
3  1 O B HOH 710  ? ? 1_555 O D HOH 672 ? ? 9_544 1.86 
4  1 O A HOH 1990 ? ? 1_555 O D HOH 555 ? ? 5_444 1.87 
5  1 O A HOH 1988 ? ? 1_555 O C HOH 700 ? ? 6_554 1.90 
6  1 O B HOH 684  ? ? 1_555 O D HOH 694 ? ? 9_544 1.92 
7  1 O B HOH 663  ? ? 1_555 O B HOH 678 ? ? 9_544 2.04 
8  1 O A HOH 1969 ? ? 1_555 O C HOH 662 ? ? 8_544 2.05 
9  1 O A HOH 2084 ? ? 1_555 O D HOH 736 ? ? 5_444 2.08 
10 1 O B HOH 659  ? ? 1_555 O B HOH 687 ? ? 5_445 2.12 
11 1 O A HOH 2012 ? ? 1_555 O C HOH 700 ? ? 6_554 2.14 
12 1 O A HOH 2010 ? ? 1_555 O C HOH 710 ? ? 6_554 2.15 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              245 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              245 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              245 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.22 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.08 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                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 LEU A 57  ? ? -120.38 -50.70  
2  1 LYS A 76  ? ? -104.42 -71.95  
3  1 LYS A 111 ? ? 75.35   -0.06   
4  1 PHE A 175 ? ? -151.88 88.94   
5  1 ASN A 243 ? ? -94.34  51.93   
6  1 LYS A 251 ? ? 53.60   -136.15 
7  1 LYS B 76  ? ? -103.90 -73.30  
8  1 PHE B 175 ? ? -153.37 87.88   
9  1 ASN B 243 ? ? -94.52  51.51   
10 1 LYS B 251 ? ? 53.33   -136.79 
11 1 LYS C 76  ? ? -104.00 -73.55  
12 1 LYS C 111 ? ? 75.17   -0.41   
13 1 PHE C 175 ? ? -153.65 88.99   
14 1 ASN C 243 ? ? -94.37  51.80   
15 1 LYS C 251 ? ? 54.03   -138.00 
16 1 LEU D 57  ? ? -120.73 -50.27  
17 1 LYS D 76  ? ? -102.97 -72.25  
18 1 LYS D 111 ? ? 73.72   -0.41   
19 1 PHE D 175 ? ? -153.18 88.56   
20 1 ASN D 243 ? ? -94.52  52.40   
21 1 LYS D 251 ? ? 53.29   -137.17 
# 
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 50.4832 1.7150   -1.8025 0.0954 ? -0.0120 ? 0.0018  ? 0.1181 ? -0.0011 ? 0.1182 ? 0.6489 ? 0.1459 
? 0.2608  ? 1.2795 ? 0.0855  ? 1.6006 ? 0.0758  ? -0.0132 ? 0.0690  ? 0.0298  ? -0.0322 ? -0.1614 ? 0.0416  ? 0.1591  ? -0.0477 ? 
2  'X-RAY DIFFRACTION' ? refined 36.6368 -2.1031  21.8176 0.4459 ? -0.1407 ? 0.0384  ? 0.3612 ? -0.0350 ? 0.1566 ? 1.2018 ? 0.4928 
? 0.3654  ? 1.3090 ? 0.4003  ? 1.0285 ? 0.2357  ? -0.5505 ? 0.2619  ? 0.5237  ? -0.2048 ? 0.2027  ? 0.0905  ? -0.5102 ? -0.0533 ? 
3  'X-RAY DIFFRACTION' ? refined 33.5622 -14.3663 -1.6728 0.2088 ? -0.0638 ? -0.0069 ? 0.2061 ? 0.0173  ? 0.1960 ? 1.5030 ? 0.4841 
? -0.4649 ? 1.4712 ? 0.0842  ? 1.4123 ? 0.2453  ? -0.0311 ? 0.0706  ? 0.1629  ? -0.0967 ? 0.2651  ? 0.0252  ? -0.2868 ? -0.1230 ? 
4  'X-RAY DIFFRACTION' ? refined 39.2311 -8.7362  7.4033  0.2085 ? -0.0709 ? -0.0042 ? 0.1922 ? 0.0141  ? 0.1312 ? 0.8746 ? 0.3346 
? 0.5544  ? 1.4656 ? 0.4991  ? 1.0477 ? 0.1267  ? -0.2545 ? -0.0763 ? 0.2147  ? -0.1142 ? 0.0485  ? 0.1969  ? -0.1659 ? -0.0214 ? 
5  'X-RAY DIFFRACTION' ? refined 35.8281 -5.4657  5.6787  0.1771 ? -0.0604 ? 0.0179  ? 0.2068 ? -0.0025 ? 0.1431 ? 0.9959 ? 0.6386 
? 0.0908  ? 1.3754 ? 0.4556  ? 1.0756 ? 0.1126  ? -0.1532 ? 0.0068  ? 0.1366  ? -0.0712 ? 0.1223  ? 0.1091  ? -0.1532 ? -0.0507 ? 
6  'X-RAY DIFFRACTION' ? refined 39.8704 -25.0546 -0.1230 0.4417 ? -0.0572 ? -0.0569 ? 0.1979 ? 0.0301  ? 0.2286 ? 1.3020 ? 1.3948 
? -0.0669 ? 2.1073 ? -2.2036 ? 7.3497 ? -0.0204 ? -0.0062 ? -0.3494 ? -0.3792 ? -0.0925 ? -0.1808 ? 1.5278  ? -0.0427 ? 0.0925  ? 
7  'X-RAY DIFFRACTION' ? refined 35.6376 -18.2716 2.5742  0.2809 ? -0.1011 ? -0.0211 ? 0.2070 ? 0.0137  ? 0.1706 ? 0.4870 ? 0.2277 
? 0.3746  ? 0.9923 ? 0.3699  ? 0.7966 ? 0.1385  ? -0.1825 ? -0.1430 ? 0.1680  ? -0.1356 ? 0.0362  ? 0.2724  ? -0.1047 ? -0.0241 ? 
8  'X-RAY DIFFRACTION' ? refined 41.9590 -4.3667  9.7319  0.1922 ? -0.0558 ? -0.0125 ? 0.2014 ? 0.0070  ? 0.1405 ? 0.7623 ? 0.1997 
? 0.2238  ? 1.0759 ? 0.3192  ? 0.9635 ? 0.1457  ? -0.1881 ? -0.0806 ? 0.2370  ? -0.1225 ? -0.0152 ? 0.1535  ? -0.0883 ? -0.0449 ? 
9  'X-RAY DIFFRACTION' ? refined 49.6190 -19.9835 -6.1400 0.3127 ? -0.0024 ? -0.0236 ? 0.2008 ? -0.0305 ? 0.2406 ? 1.9474 ? 0.3249 
? -0.3922 ? 2.4127 ? -1.0785 ? 4.2236 ? 0.0343  ? 0.2576  ? -0.2509 ? -0.3283 ? 0.0448  ? -0.2237 ? 0.5843  ? 0.2163  ? -0.0989 ? 
10 'X-RAY DIFFRACTION' ? refined 48.8444 -2.2574  8.0570  0.1792 ? -0.0284 ? -0.0456 ? 0.1932 ? 0.0006  ? 0.1490 ? 1.0507 ? 0.6497 
? -0.2195 ? 1.3398 ? -0.6120 ? 0.2925 ? 0.2019  ? -0.1620 ? 0.0274  ? 0.2058  ? -0.0621 ? -0.1747 ? -0.0635 ? -0.0002 ? -0.0519 ? 
11 'X-RAY DIFFRACTION' ? refined 23.6759 -56.1032 14.5007 0.1249 ? 0.0040  ? 0.0023  ? 0.1171 ? -0.0068 ? 0.0946 ? 0.8431 ? 0.1484 
? 0.2710  ? 1.4436 ? -0.4975 ? 1.2101 ? -0.0083 ? 0.1681  ? -0.0764 ? -0.1190 ? -0.0606 ? -0.0767 ? -0.0292 ? 0.0652  ? 0.0623  ? 
12 'X-RAY DIFFRACTION' ? refined 20.0098 -29.0077 18.9086 0.4875 ? 0.0144  ? -0.1035 ? 0.1795 ? 0.0194  ? 0.3057 ? 0.9150 ? 
-0.1214 ? 0.1775  ? 0.7122 ? -0.2733 ? 2.3459 ? -0.1001 ? 0.0883  ? 0.2460  ? 0.2597  ? -0.0803 ? 0.2111  ? -0.8789 ? -0.3809 ? 
0.2102  ? 
13 'X-RAY DIFFRACTION' ? refined 25.8955 -44.1180 28.2875 0.2417 ? -0.0197 ? -0.0258 ? 0.1288 ? -0.0105 ? 0.1352 ? 1.1472 ? 
-0.1928 ? 0.4605  ? 0.6999 ? -0.1821 ? 1.5191 ? -0.0448 ? -0.0691 ? 0.1066  ? 0.1275  ? -0.0345 ? -0.0251 ? -0.3232 ? 0.0238  ? 
0.0548  ? 
14 'X-RAY DIFFRACTION' ? refined 41.3390 -47.7390 35.2257 0.3012 ? -0.0878 ? -0.1142 ? 0.2517 ? 0.0599  ? 0.2826 ? 1.2517 ? 2.5251 
? 0.3575  ? 5.0891 ? 0.6072  ? 1.1488 ? 0.0752  ? -0.0340 ? -0.2459 ? 0.6133  ? -0.1815 ? -1.1928 ? -0.2246 ? 0.3619  ? 0.0421  ? 
15 'X-RAY DIFFRACTION' ? refined 33.4623 -43.8507 34.5635 0.3196 ? -0.0419 ? -0.0625 ? 0.1787 ? 0.0064  ? 0.1669 ? 0.8180 ? 
-0.0770 ? 0.4950  ? 0.5702 ? -0.3486 ? 0.9887 ? -0.0579 ? -0.0874 ? 0.1158  ? 0.1420  ? -0.0383 ? -0.1547 ? -0.3508 ? 0.1028  ? 
0.0941  ? 
16 'X-RAY DIFFRACTION' ? refined 24.7569 -41.7645 20.4938 0.2459 ? -0.0211 ? -0.0169 ? 0.1363 ? 0.0071  ? 0.1297 ? 0.8648 ? 
-0.0462 ? 0.3209  ? 0.7318 ? -0.2384 ? 1.2019 ? -0.0797 ? 0.0264  ? 0.1248  ? 0.0266  ? -0.0101 ? -0.0089 ? -0.3481 ? 0.0986  ? 
0.0743  ? 
17 'X-RAY DIFFRACTION' ? refined 41.9990 -56.5928 26.9891 0.2306 ? 0.0034  ? -0.0516 ? 0.2605 ? 0.0386  ? 0.2428 ? 1.8634 ? 0.8179 
? -0.0071 ? 4.4540 ? 0.0039  ? 1.9771 ? 0.0270  ? 0.0208  ? -0.2770 ? 0.1577  ? -0.0821 ? -0.5365 ? 0.2191  ? 0.4361  ? 0.0795  ? 
18 'X-RAY DIFFRACTION' ? refined 26.3843 -45.6838 14.4298 0.2066 ? -0.0236 ? 0.0021  ? 0.1635 ? 0.0331  ? 0.1259 ? 0.9220 ? 0.4148 
? 0.2209  ? 0.7731 ? 0.8744  ? 1.0984 ? -0.0022 ? 0.2101  ? 0.0145  ? -0.1427 ? -0.0742 ? 0.1558  ? -0.2701 ? 0.1393  ? 0.0425  ? 
19 'X-RAY DIFFRACTION' ? refined 60.4277 -23.3690 58.2171 0.1166 ? 0.0072  ? -0.0075 ? 0.0968 ? 0.0090  ? 0.1208 ? 1.2640 ? 0.5568 
? 0.1072  ? 1.1187 ? -0.0831 ? 1.1860 ? -0.0687 ? -0.0198 ? -0.1513 ? -0.0293 ? 0.0983  ? -0.0378 ? 0.1437  ? 0.0807  ? -0.0161 ? 
20 'X-RAY DIFFRACTION' ? refined 35.1275 -22.6877 46.9741 0.2427 ? -0.1119 ? -0.1004 ? 0.3620 ? 0.0980  ? 0.3635 ? 0.9735 ? 0.3288 
? -0.3779 ? 1.8017 ? -0.6004 ? 1.0819 ? -0.1863 ? 0.0048  ? 0.1406  ? -0.1840 ? 0.3345  ? 0.8978  ? 0.1178  ? -0.4208 ? -0.1127 ? 
21 'X-RAY DIFFRACTION' ? refined 51.1511 -12.9999 46.1532 0.1711 ? -0.0228 ? -0.0530 ? 0.1561 ? 0.0400  ? 0.1700 ? 0.9057 ? 0.2811 
? -0.3183 ? 1.2946 ? -0.4949 ? 1.0689 ? -0.0600 ? 0.1078  ? 0.0869  ? -0.1986 ? 0.1271  ? 0.2248  ? -0.0210 ? -0.1406 ? -0.0603 ? 
22 'X-RAY DIFFRACTION' ? refined 61.5231 -10.5185 32.3538 0.3462 ? -0.1216 ? -0.0287 ? 0.3185 ? 0.0274  ? 0.1793 ? 3.6566 ? 2.1439 
? 2.8797  ? 2.7100 ? 0.4607  ? 3.2955 ? -0.3840 ? 0.9498  ? 0.0731  ? -0.5461 ? 0.4336  ? -0.0518 ? -0.1703 ? 0.7574  ? -0.0306 ? 
23 'X-RAY DIFFRACTION' ? refined 55.2506 -9.2530  37.8542 0.2475 ? -0.0668 ? -0.0643 ? 0.1948 ? 0.0645  ? 0.1970 ? 0.7171 ? 0.4409 
? -0.3280 ? 0.9686 ? -0.3653 ? 0.9519 ? -0.0731 ? 0.2133  ? 0.0654  ? -0.3027 ? 0.1659  ? 0.1758  ? 0.0140  ? -0.0514 ? -0.0677 ? 
24 'X-RAY DIFFRACTION' ? refined 48.5458 -20.4168 48.5785 0.1896 ? -0.0344 ? -0.0464 ? 0.1501 ? 0.0275  ? 0.1894 ? 0.9779 ? 0.2905 
? -0.1770 ? 1.0693 ? -0.3567 ? 0.9492 ? -0.0497 ? 0.0882  ? 0.0033  ? -0.2479 ? 0.1339  ? 0.1864  ? 0.1392  ? -0.1782 ? -0.0775 ? 
25 'X-RAY DIFFRACTION' ? refined 70.0119 -16.8024 39.3190 0.2490 ? -0.0496 ? 0.0381  ? 0.2651 ? 0.0209  ? 0.2253 ? 3.4578 ? 0.4351 
? 1.6897  ? 2.3637 ? 0.2821  ? 3.8958 ? -0.1552 ? 0.3324  ? -0.0499 ? -0.3363 ? 0.0930  ? -0.4083 ? -0.0255 ? 0.5019  ? 0.0759  ? 
26 'X-RAY DIFFRACTION' ? refined 52.7519 -25.9470 51.1178 0.2011 ? -0.0402 ? -0.0171 ? 0.1291 ? -0.0024 ? 0.1826 ? 0.5459 ? 
-0.6464 ? 0.3841  ? 0.8126 ? -0.5946 ? 1.6640 ? -0.0731 ? -0.1702 ? -0.1463 ? -0.1804 ? 0.0930  ? 0.1100  ? 0.2364  ? -0.1108 ? 
-0.0418 ? 
27 'X-RAY DIFFRACTION' ? refined 52.8365 -61.4163 60.3056 0.1326 ? -0.0024 ? 0.0059  ? 0.1168 ? 0.0125  ? 0.1244 ? 1.3358 ? 
-0.2118 ? -0.0646 ? 1.4496 ? 0.2317  ? 0.6223 ? -0.0293 ? -0.1414 ? -0.0752 ? 0.0879  ? 0.0338  ? -0.0866 ? 0.1485  ? -0.0431 ? 
0.0081  ? 
28 'X-RAY DIFFRACTION' ? refined 74.4176 -62.8112 43.1047 0.2584 ? 0.0109  ? 0.1458  ? 0.2664 ? -0.0471 ? 0.4598 ? 0.6976 ? 0.1516 
? 0.0761  ? 2.7638 ? -0.1707 ? 1.1594 ? 0.0214  ? 0.3648  ? 0.0142  ? -0.6608 ? 0.0801  ? -0.6355 ? 0.2840  ? 0.0155  ? 0.0249  ? 
29 'X-RAY DIFFRACTION' ? refined 62.2628 -40.9537 54.1021 0.1729 ? -0.0202 ? 0.0282  ? 0.1501 ? 0.0243  ? 0.2621 ? 1.3330 ? 0.2008 
? -0.2855 ? 1.6058 ? 0.2087  ? 1.5464 ? -0.0837 ? 0.2661  ? 0.1872  ? -0.2512 ? 0.0737  ? -0.2684 ? -0.1235 ? -0.0822 ? 0.0376  ? 
30 'X-RAY DIFFRACTION' ? refined 64.4356 -47.4576 45.7840 0.2265 ? -0.0072 ? 0.0737  ? 0.1553 ? 0.0313  ? 0.2591 ? 0.6774 ? 
-0.0118 ? 0.2132  ? 2.1214 ? 0.0235  ? 1.3339 ? -0.0024 ? 0.1323  ? 0.1253  ? -0.4351 ? -0.0514 ? -0.3355 ? -0.0988 ? 0.1404  ? 
0.0228  ? 
31 'X-RAY DIFFRACTION' ? refined 69.6307 -60.0440 64.7884 0.1830 ? 0.0218  ? -0.0528 ? 0.1663 ? 0.0005  ? 0.3007 ? 0.1053 ? 0.5265 
? 0.1181  ? 2.7962 ? 0.7210  ? 0.3075 ? 0.0532  ? -0.1059 ? -0.0925 ? 0.2960  ? 0.0178  ? -0.5603 ? 0.1004  ? 0.0628  ? -0.0224 ? 
32 'X-RAY DIFFRACTION' ? refined 62.9141 -51.7318 49.1380 0.1548 ? -0.0044 ? 0.0613  ? 0.1269 ? 0.0155  ? 0.1998 ? 1.1129 ? 0.2213 
? -0.0922 ? 2.1233 ? 0.2058  ? 0.9190 ? -0.0280 ? 0.0960  ? 0.0732  ? -0.1931 ? 0.0141  ? -0.2470 ? 0.0078  ? 0.0370  ? -0.0032 ? 
33 'X-RAY DIFFRACTION' ? refined 68.9054 -38.1801 63.8793 0.1867 ? -0.0146 ? -0.0277 ? 0.2090 ? -0.0775 ? 0.4414 ? 7.9893 ? 
-0.4712 ? -1.1603 ? 1.7746 ? -0.5436 ? 0.3798 ? 0.1793  ? -0.8669 ? 0.9388  ? 0.1741  ? 0.0591  ? -0.5122 ? -0.1725 ? 0.2977  ? 
-0.0901 ? 
34 'X-RAY DIFFRACTION' ? refined 68.3343 -41.7082 55.8324 0.1710 ? -0.0102 ? 0.0454  ? 0.1376 ? 0.0037  ? 0.3519 ? 0.6519 ? 0.0346 
? 0.0235  ? 1.1862 ? 0.3293  ? 0.5820 ? -0.0066 ? -0.0179 ? 0.1161  ? -0.0876 ? 0.0047  ? -0.3772 ? -0.0831 ? 0.1043  ? 0.0125  ? 
35 'X-RAY DIFFRACTION' ? refined 65.6061 -57.9417 52.3047 0.1532 ? 0.0122  ? 0.0353  ? 0.1359 ? 0.0168  ? 0.2375 ? 0.8085 ? 
-0.1341 ? 0.0448  ? 1.3010 ? 0.1442  ? 0.8799 ? -0.0165 ? 0.0394  ? -0.0174 ? -0.0774 ? -0.0014 ? -0.3730 ? 0.0136  ? 0.1132  ? 
0.0146  ? 
36 'X-RAY DIFFRACTION' ? refined 61.5291 -44.1876 71.3136 0.2447 ? 0.0004  ? -0.0140 ? 0.1976 ? -0.0613 ? 0.2783 ? 4.0100 ? 
-0.3021 ? -0.6947 ? 1.8305 ? -0.1950 ? 1.8270 ? 0.0108  ? -0.4280 ? 0.5230  ? 0.4748  ? 0.0496  ? -0.0796 ? -0.1774 ? -0.0406 ? 
-0.0261 ? 
37 'X-RAY DIFFRACTION' ? refined 63.2122 -62.4396 57.6253 0.1560 ? 0.0316  ? -0.0058 ? 0.1295 ? 0.0172  ? 0.2224 ? 1.2722 ? 0.9607 
? -0.0689 ? 0.9708 ? -0.4486 ? 0.6490 ? -0.0344 ? 0.0725  ? -0.1898 ? 0.0587  ? -0.0593 ? -0.2733 ? 0.2100  ? -0.0765 ? 0.0972  ? 
# 
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 2 through 34 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 35 through 50 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 51 through 70 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 71 through 115 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 116 through 153 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 154 through 165 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 166 through 189 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 190 through 218 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 219 through 237 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 238 through 260 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 34 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 35 through 50 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 51 through 153 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 154 through 166 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 167 through 189 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 190 through 218 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 219 through 237 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 238 through 260 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 2 through 34 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 35 through 50 )
;
21 'X-RAY DIFFRACTION' 21 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 51 through 153 )
;
22 'X-RAY DIFFRACTION' 22 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 154 through 165 )
;
23 'X-RAY DIFFRACTION' 23 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 166 through 189 )
;
24 'X-RAY DIFFRACTION' 24 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 190 through 218 )
;
25 'X-RAY DIFFRACTION' 25 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 219 through 237 )
;
26 'X-RAY DIFFRACTION' 26 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 238 through 260 )
;
27 'X-RAY DIFFRACTION' 27 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 2 through 34 )
;
28 'X-RAY DIFFRACTION' 28 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 35 through 50 )
;
29 'X-RAY DIFFRACTION' 29 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 51 through 70 )
;
30 'X-RAY DIFFRACTION' 30 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 71 through 97 )
;
31 'X-RAY DIFFRACTION' 31 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 98 through 115 )
;
32 'X-RAY DIFFRACTION' 32 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 116 through 153 )
;
33 'X-RAY DIFFRACTION' 33 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 154 through 166 )
;
34 'X-RAY DIFFRACTION' 34 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 167 through 189 )
;
35 'X-RAY DIFFRACTION' 35 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 190 through 218 )
;
36 'X-RAY DIFFRACTION' 36 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 219 through 237 )
;
37 'X-RAY DIFFRACTION' 37 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 238 through 260 )
;
# 
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 MET 1 ? A MET 1 
2 1 Y 1 B MET 1 ? B MET 1 
3 1 Y 1 C MET 1 ? C MET 1 
4 1 Y 1 D MET 1 ? D MET 1 
# 
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 
A1H9O C1   C  Y N 1   
A1H9O C2   C  Y N 2   
A1H9O C3   C  Y N 3   
A1H9O C4   C  Y N 4   
A1H9O C5   C  Y N 5   
A1H9O C6   C  Y N 6   
A1H9O C7   C  N N 7   
A1H9O C8   C  N N 8   
A1H9O C9   C  Y N 9   
A1H9O C10  C  Y N 10  
A1H9O C11  C  Y N 11  
A1H9O C12  C  Y N 12  
A1H9O C13  C  Y N 13  
A1H9O C14  C  Y N 14  
A1H9O C15  C  N N 15  
A1H9O C16  C  N N 16  
A1H9O C17  C  N N 17  
A1H9O C18  C  N N 18  
A1H9O C19  C  N N 19  
A1H9O C20  C  N N 20  
A1H9O C21  C  N N 21  
A1H9O C22  C  N N 22  
A1H9O C23  C  N N 23  
A1H9O C24  C  N N 24  
A1H9O C25  C  N N 25  
A1H9O C26  C  N N 26  
A1H9O N1   N  N N 27  
A1H9O N2   N  N N 28  
A1H9O N3   N  N N 29  
A1H9O N4   N  N N 30  
A1H9O N5   N  N N 31  
A1H9O N6   N  N N 32  
A1H9O N7   N  N N 33  
A1H9O O1   O  N N 34  
A1H9O O2   O  N N 35  
A1H9O O3   O  N N 36  
A1H9O O4   O  N N 37  
A1H9O O5   O  N N 38  
A1H9O O6   O  N N 39  
A1H9O O7   O  N N 40  
A1H9O S1   S  N N 41  
A1H9O FE1  FE N N 42  
A1H9O H1   H  N N 43  
A1H9O H2   H  N N 44  
A1H9O H3   H  N N 45  
A1H9O H4   H  N N 46  
A1H9O H5   H  N N 47  
A1H9O H6   H  N N 48  
A1H9O H7   H  N N 49  
A1H9O H8   H  N N 50  
A1H9O H9   H  N N 51  
A1H9O H10  H  N N 52  
A1H9O H11  H  N N 53  
A1H9O H12  H  N N 54  
A1H9O H13  H  N N 55  
A1H9O H14  H  N N 56  
A1H9O H15  H  N N 57  
A1H9O H16  H  N N 58  
A1H9O H17  H  N N 59  
A1H9O H18  H  N N 60  
A1H9O H19  H  N N 61  
A1H9O H20  H  N N 62  
A1H9O H21  H  N N 63  
A1H9O H22  H  N N 64  
A1H9O H23  H  N N 65  
A1H9O H24  H  N N 66  
A1H9O H25  H  N N 67  
A1H9O H26  H  N N 68  
A1H9O H27  H  N N 69  
A1H9O H28  H  N N 70  
A1H9O H29  H  N N 71  
ALA   N    N  N N 72  
ALA   CA   C  N S 73  
ALA   C    C  N N 74  
ALA   O    O  N N 75  
ALA   CB   C  N N 76  
ALA   OXT  O  N N 77  
ALA   H    H  N N 78  
ALA   H2   H  N N 79  
ALA   HA   H  N N 80  
ALA   HB1  H  N N 81  
ALA   HB2  H  N N 82  
ALA   HB3  H  N N 83  
ALA   HXT  H  N N 84  
ARG   N    N  N N 85  
ARG   CA   C  N S 86  
ARG   C    C  N N 87  
ARG   O    O  N N 88  
ARG   CB   C  N N 89  
ARG   CG   C  N N 90  
ARG   CD   C  N N 91  
ARG   NE   N  N N 92  
ARG   CZ   C  N N 93  
ARG   NH1  N  N N 94  
ARG   NH2  N  N N 95  
ARG   OXT  O  N N 96  
ARG   H    H  N N 97  
ARG   H2   H  N N 98  
ARG   HA   H  N N 99  
ARG   HB2  H  N N 100 
ARG   HB3  H  N N 101 
ARG   HG2  H  N N 102 
ARG   HG3  H  N N 103 
ARG   HD2  H  N N 104 
ARG   HD3  H  N N 105 
ARG   HE   H  N N 106 
ARG   HH11 H  N N 107 
ARG   HH12 H  N N 108 
ARG   HH21 H  N N 109 
ARG   HH22 H  N N 110 
ARG   HXT  H  N N 111 
ASN   N    N  N N 112 
ASN   CA   C  N S 113 
ASN   C    C  N N 114 
ASN   O    O  N N 115 
ASN   CB   C  N N 116 
ASN   CG   C  N N 117 
ASN   OD1  O  N N 118 
ASN   ND2  N  N N 119 
ASN   OXT  O  N N 120 
ASN   H    H  N N 121 
ASN   H2   H  N N 122 
ASN   HA   H  N N 123 
ASN   HB2  H  N N 124 
ASN   HB3  H  N N 125 
ASN   HD21 H  N N 126 
ASN   HD22 H  N N 127 
ASN   HXT  H  N N 128 
ASP   N    N  N N 129 
ASP   CA   C  N S 130 
ASP   C    C  N N 131 
ASP   O    O  N N 132 
ASP   CB   C  N N 133 
ASP   CG   C  N N 134 
ASP   OD1  O  N N 135 
ASP   OD2  O  N N 136 
ASP   OXT  O  N N 137 
ASP   H    H  N N 138 
ASP   H2   H  N N 139 
ASP   HA   H  N N 140 
ASP   HB2  H  N N 141 
ASP   HB3  H  N N 142 
ASP   HD2  H  N N 143 
ASP   HXT  H  N N 144 
CYS   N    N  N N 145 
CYS   CA   C  N R 146 
CYS   C    C  N N 147 
CYS   O    O  N N 148 
CYS   CB   C  N N 149 
CYS   SG   S  N N 150 
CYS   OXT  O  N N 151 
CYS   H    H  N N 152 
CYS   H2   H  N N 153 
CYS   HA   H  N N 154 
CYS   HB2  H  N N 155 
CYS   HB3  H  N N 156 
CYS   HG   H  N N 157 
CYS   HXT  H  N N 158 
EDO   C1   C  N N 159 
EDO   O1   O  N N 160 
EDO   C2   C  N N 161 
EDO   O2   O  N N 162 
EDO   H11  H  N N 163 
EDO   H12  H  N N 164 
EDO   HO1  H  N N 165 
EDO   H21  H  N N 166 
EDO   H22  H  N N 167 
EDO   HO2  H  N N 168 
GLN   N    N  N N 169 
GLN   CA   C  N S 170 
GLN   C    C  N N 171 
GLN   O    O  N N 172 
GLN   CB   C  N N 173 
GLN   CG   C  N N 174 
GLN   CD   C  N N 175 
GLN   OE1  O  N N 176 
GLN   NE2  N  N N 177 
GLN   OXT  O  N N 178 
GLN   H    H  N N 179 
GLN   H2   H  N N 180 
GLN   HA   H  N N 181 
GLN   HB2  H  N N 182 
GLN   HB3  H  N N 183 
GLN   HG2  H  N N 184 
GLN   HG3  H  N N 185 
GLN   HE21 H  N N 186 
GLN   HE22 H  N N 187 
GLN   HXT  H  N N 188 
GLU   N    N  N N 189 
GLU   CA   C  N S 190 
GLU   C    C  N N 191 
GLU   O    O  N N 192 
GLU   CB   C  N N 193 
GLU   CG   C  N N 194 
GLU   CD   C  N N 195 
GLU   OE1  O  N N 196 
GLU   OE2  O  N N 197 
GLU   OXT  O  N N 198 
GLU   H    H  N N 199 
GLU   H2   H  N N 200 
GLU   HA   H  N N 201 
GLU   HB2  H  N N 202 
GLU   HB3  H  N N 203 
GLU   HG2  H  N N 204 
GLU   HG3  H  N N 205 
GLU   HE2  H  N N 206 
GLU   HXT  H  N N 207 
GLY   N    N  N N 208 
GLY   CA   C  N N 209 
GLY   C    C  N N 210 
GLY   O    O  N N 211 
GLY   OXT  O  N N 212 
GLY   H    H  N N 213 
GLY   H2   H  N N 214 
GLY   HA2  H  N N 215 
GLY   HA3  H  N N 216 
GLY   HXT  H  N N 217 
HIS   N    N  N N 218 
HIS   CA   C  N S 219 
HIS   C    C  N N 220 
HIS   O    O  N N 221 
HIS   CB   C  N N 222 
HIS   CG   C  Y N 223 
HIS   ND1  N  Y N 224 
HIS   CD2  C  Y N 225 
HIS   CE1  C  Y N 226 
HIS   NE2  N  Y N 227 
HIS   OXT  O  N N 228 
HIS   H    H  N N 229 
HIS   H2   H  N N 230 
HIS   HA   H  N N 231 
HIS   HB2  H  N N 232 
HIS   HB3  H  N N 233 
HIS   HD1  H  N N 234 
HIS   HD2  H  N N 235 
HIS   HE1  H  N N 236 
HIS   HE2  H  N N 237 
HIS   HXT  H  N N 238 
HOH   O    O  N N 239 
HOH   H1   H  N N 240 
HOH   H2   H  N N 241 
ILE   N    N  N N 242 
ILE   CA   C  N S 243 
ILE   C    C  N N 244 
ILE   O    O  N N 245 
ILE   CB   C  N S 246 
ILE   CG1  C  N N 247 
ILE   CG2  C  N N 248 
ILE   CD1  C  N N 249 
ILE   OXT  O  N N 250 
ILE   H    H  N N 251 
ILE   H2   H  N N 252 
ILE   HA   H  N N 253 
ILE   HB   H  N N 254 
ILE   HG12 H  N N 255 
ILE   HG13 H  N N 256 
ILE   HG21 H  N N 257 
ILE   HG22 H  N N 258 
ILE   HG23 H  N N 259 
ILE   HD11 H  N N 260 
ILE   HD12 H  N N 261 
ILE   HD13 H  N N 262 
ILE   HXT  H  N N 263 
LEU   N    N  N N 264 
LEU   CA   C  N S 265 
LEU   C    C  N N 266 
LEU   O    O  N N 267 
LEU   CB   C  N N 268 
LEU   CG   C  N N 269 
LEU   CD1  C  N N 270 
LEU   CD2  C  N N 271 
LEU   OXT  O  N N 272 
LEU   H    H  N N 273 
LEU   H2   H  N N 274 
LEU   HA   H  N N 275 
LEU   HB2  H  N N 276 
LEU   HB3  H  N N 277 
LEU   HG   H  N N 278 
LEU   HD11 H  N N 279 
LEU   HD12 H  N N 280 
LEU   HD13 H  N N 281 
LEU   HD21 H  N N 282 
LEU   HD22 H  N N 283 
LEU   HD23 H  N N 284 
LEU   HXT  H  N N 285 
LYS   N    N  N N 286 
LYS   CA   C  N S 287 
LYS   C    C  N N 288 
LYS   O    O  N N 289 
LYS   CB   C  N N 290 
LYS   CG   C  N N 291 
LYS   CD   C  N N 292 
LYS   CE   C  N N 293 
LYS   NZ   N  N N 294 
LYS   OXT  O  N N 295 
LYS   H    H  N N 296 
LYS   H2   H  N N 297 
LYS   HA   H  N N 298 
LYS   HB2  H  N N 299 
LYS   HB3  H  N N 300 
LYS   HG2  H  N N 301 
LYS   HG3  H  N N 302 
LYS   HD2  H  N N 303 
LYS   HD3  H  N N 304 
LYS   HE2  H  N N 305 
LYS   HE3  H  N N 306 
LYS   HZ1  H  N N 307 
LYS   HZ2  H  N N 308 
LYS   HZ3  H  N N 309 
LYS   HXT  H  N N 310 
MET   N    N  N N 311 
MET   CA   C  N S 312 
MET   C    C  N N 313 
MET   O    O  N N 314 
MET   CB   C  N N 315 
MET   CG   C  N N 316 
MET   SD   S  N N 317 
MET   CE   C  N N 318 
MET   OXT  O  N N 319 
MET   H    H  N N 320 
MET   H2   H  N N 321 
MET   HA   H  N N 322 
MET   HB2  H  N N 323 
MET   HB3  H  N N 324 
MET   HG2  H  N N 325 
MET   HG3  H  N N 326 
MET   HE1  H  N N 327 
MET   HE2  H  N N 328 
MET   HE3  H  N N 329 
MET   HXT  H  N N 330 
PHE   N    N  N N 331 
PHE   CA   C  N S 332 
PHE   C    C  N N 333 
PHE   O    O  N N 334 
PHE   CB   C  N N 335 
PHE   CG   C  Y N 336 
PHE   CD1  C  Y N 337 
PHE   CD2  C  Y N 338 
PHE   CE1  C  Y N 339 
PHE   CE2  C  Y N 340 
PHE   CZ   C  Y N 341 
PHE   OXT  O  N N 342 
PHE   H    H  N N 343 
PHE   H2   H  N N 344 
PHE   HA   H  N N 345 
PHE   HB2  H  N N 346 
PHE   HB3  H  N N 347 
PHE   HD1  H  N N 348 
PHE   HD2  H  N N 349 
PHE   HE1  H  N N 350 
PHE   HE2  H  N N 351 
PHE   HZ   H  N N 352 
PHE   HXT  H  N N 353 
PRO   N    N  N N 354 
PRO   CA   C  N S 355 
PRO   C    C  N N 356 
PRO   O    O  N N 357 
PRO   CB   C  N N 358 
PRO   CG   C  N N 359 
PRO   CD   C  N N 360 
PRO   OXT  O  N N 361 
PRO   H    H  N N 362 
PRO   HA   H  N N 363 
PRO   HB2  H  N N 364 
PRO   HB3  H  N N 365 
PRO   HG2  H  N N 366 
PRO   HG3  H  N N 367 
PRO   HD2  H  N N 368 
PRO   HD3  H  N N 369 
PRO   HXT  H  N N 370 
SER   N    N  N N 371 
SER   CA   C  N S 372 
SER   C    C  N N 373 
SER   O    O  N N 374 
SER   CB   C  N N 375 
SER   OG   O  N N 376 
SER   OXT  O  N N 377 
SER   H    H  N N 378 
SER   H2   H  N N 379 
SER   HA   H  N N 380 
SER   HB2  H  N N 381 
SER   HB3  H  N N 382 
SER   HG   H  N N 383 
SER   HXT  H  N N 384 
THR   N    N  N N 385 
THR   CA   C  N S 386 
THR   C    C  N N 387 
THR   O    O  N N 388 
THR   CB   C  N R 389 
THR   OG1  O  N N 390 
THR   CG2  C  N N 391 
THR   OXT  O  N N 392 
THR   H    H  N N 393 
THR   H2   H  N N 394 
THR   HA   H  N N 395 
THR   HB   H  N N 396 
THR   HG1  H  N N 397 
THR   HG21 H  N N 398 
THR   HG22 H  N N 399 
THR   HG23 H  N N 400 
THR   HXT  H  N N 401 
TRP   N    N  N N 402 
TRP   CA   C  N S 403 
TRP   C    C  N N 404 
TRP   O    O  N N 405 
TRP   CB   C  N N 406 
TRP   CG   C  Y N 407 
TRP   CD1  C  Y N 408 
TRP   CD2  C  Y N 409 
TRP   NE1  N  Y N 410 
TRP   CE2  C  Y N 411 
TRP   CE3  C  Y N 412 
TRP   CZ2  C  Y N 413 
TRP   CZ3  C  Y N 414 
TRP   CH2  C  Y N 415 
TRP   OXT  O  N N 416 
TRP   H    H  N N 417 
TRP   H2   H  N N 418 
TRP   HA   H  N N 419 
TRP   HB2  H  N N 420 
TRP   HB3  H  N N 421 
TRP   HD1  H  N N 422 
TRP   HE1  H  N N 423 
TRP   HE3  H  N N 424 
TRP   HZ2  H  N N 425 
TRP   HZ3  H  N N 426 
TRP   HH2  H  N N 427 
TRP   HXT  H  N N 428 
TYR   N    N  N N 429 
TYR   CA   C  N S 430 
TYR   C    C  N N 431 
TYR   O    O  N N 432 
TYR   CB   C  N N 433 
TYR   CG   C  Y N 434 
TYR   CD1  C  Y N 435 
TYR   CD2  C  Y N 436 
TYR   CE1  C  Y N 437 
TYR   CE2  C  Y N 438 
TYR   CZ   C  Y N 439 
TYR   OH   O  N N 440 
TYR   OXT  O  N N 441 
TYR   H    H  N N 442 
TYR   H2   H  N N 443 
TYR   HA   H  N N 444 
TYR   HB2  H  N N 445 
TYR   HB3  H  N N 446 
TYR   HD1  H  N N 447 
TYR   HD2  H  N N 448 
TYR   HE1  H  N N 449 
TYR   HE2  H  N N 450 
TYR   HH   H  N N 451 
TYR   HXT  H  N N 452 
VAL   N    N  N N 453 
VAL   CA   C  N S 454 
VAL   C    C  N N 455 
VAL   O    O  N N 456 
VAL   CB   C  N N 457 
VAL   CG1  C  N N 458 
VAL   CG2  C  N N 459 
VAL   OXT  O  N N 460 
VAL   H    H  N N 461 
VAL   H2   H  N N 462 
VAL   HA   H  N N 463 
VAL   HB   H  N N 464 
VAL   HG11 H  N N 465 
VAL   HG12 H  N N 466 
VAL   HG13 H  N N 467 
VAL   HG21 H  N N 468 
VAL   HG22 H  N N 469 
VAL   HG23 H  N N 470 
VAL   HXT  H  N N 471 
ZN    ZN   ZN N N 472 
# 
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 
A1H9O C23 N3   sing N N 1   
A1H9O O6  C24  doub N N 2   
A1H9O N3  C24  sing N N 3   
A1H9O N3  C25  sing N N 4   
A1H9O O7  C25  doub N N 5   
A1H9O C24 N4   sing N N 6   
A1H9O C25 N5   sing N N 7   
A1H9O C19 C18  sing N N 8   
A1H9O N4  C18  sing N N 9   
A1H9O N4  FE1  sing N N 10  
A1H9O C21 C17  sing N N 11  
A1H9O N5  C17  sing N N 12  
A1H9O N5  FE1  sing N N 13  
A1H9O C18 C20  sing N N 14  
A1H9O C18 C15  sing N N 15  
A1H9O C17 C22  sing N N 16  
A1H9O C17 C16  sing N N 17  
A1H9O FE1 N7   sing N N 18  
A1H9O FE1 N6   sing N N 19  
A1H9O C15 N7   sing N N 20  
A1H9O C15 O4   doub N N 21  
A1H9O N7  C13  sing N N 22  
A1H9O C16 N6   sing N N 23  
A1H9O C16 O5   doub N N 24  
A1H9O N6  C14  sing N N 25  
A1H9O C13 C14  doub Y N 26  
A1H9O C13 C11  sing Y N 27  
A1H9O C14 C12  sing Y N 28  
A1H9O C11 C9   doub Y N 29  
A1H9O C12 C10  doub Y N 30  
A1H9O C9  C10  sing Y N 31  
A1H9O C9  C8   sing N N 32  
A1H9O O3  C8   doub N N 33  
A1H9O C8  N2   sing N N 34  
A1H9O N2  C26  sing N N 35  
A1H9O C26 C7   sing N N 36  
A1H9O C7  C6   sing N N 37  
A1H9O C5  C6   doub Y N 38  
A1H9O C5  C4   sing Y N 39  
A1H9O C6  C3   sing Y N 40  
A1H9O C4  C1   doub Y N 41  
A1H9O C3  C2   doub Y N 42  
A1H9O C1  C2   sing Y N 43  
A1H9O C1  S1   sing N N 44  
A1H9O N1  S1   sing N N 45  
A1H9O S1  O2   doub N N 46  
A1H9O S1  O1   doub N N 47  
A1H9O C2  H1   sing N N 48  
A1H9O C3  H2   sing N N 49  
A1H9O C4  H3   sing N N 50  
A1H9O C5  H4   sing N N 51  
A1H9O C7  H5   sing N N 52  
A1H9O C7  H6   sing N N 53  
A1H9O C10 H7   sing N N 54  
A1H9O C11 H8   sing N N 55  
A1H9O C12 H9   sing N N 56  
A1H9O C19 H10  sing N N 57  
A1H9O C19 H11  sing N N 58  
A1H9O C19 H12  sing N N 59  
A1H9O C20 H13  sing N N 60  
A1H9O C20 H14  sing N N 61  
A1H9O C20 H15  sing N N 62  
A1H9O C21 H16  sing N N 63  
A1H9O C21 H17  sing N N 64  
A1H9O C21 H18  sing N N 65  
A1H9O C22 H19  sing N N 66  
A1H9O C22 H20  sing N N 67  
A1H9O C22 H21  sing N N 68  
A1H9O C23 H22  sing N N 69  
A1H9O C23 H23  sing N N 70  
A1H9O C23 H24  sing N N 71  
A1H9O C26 H25  sing N N 72  
A1H9O C26 H26  sing N N 73  
A1H9O N1  H27  sing N N 74  
A1H9O N1  H28  sing N N 75  
A1H9O N2  H29  sing N N 76  
ALA   N   CA   sing N N 77  
ALA   N   H    sing N N 78  
ALA   N   H2   sing N N 79  
ALA   CA  C    sing N N 80  
ALA   CA  CB   sing N N 81  
ALA   CA  HA   sing N N 82  
ALA   C   O    doub N N 83  
ALA   C   OXT  sing N N 84  
ALA   CB  HB1  sing N N 85  
ALA   CB  HB2  sing N N 86  
ALA   CB  HB3  sing N N 87  
ALA   OXT HXT  sing N N 88  
ARG   N   CA   sing N N 89  
ARG   N   H    sing N N 90  
ARG   N   H2   sing N N 91  
ARG   CA  C    sing N N 92  
ARG   CA  CB   sing N N 93  
ARG   CA  HA   sing N N 94  
ARG   C   O    doub N N 95  
ARG   C   OXT  sing N N 96  
ARG   CB  CG   sing N N 97  
ARG   CB  HB2  sing N N 98  
ARG   CB  HB3  sing N N 99  
ARG   CG  CD   sing N N 100 
ARG   CG  HG2  sing N N 101 
ARG   CG  HG3  sing N N 102 
ARG   CD  NE   sing N N 103 
ARG   CD  HD2  sing N N 104 
ARG   CD  HD3  sing N N 105 
ARG   NE  CZ   sing N N 106 
ARG   NE  HE   sing N N 107 
ARG   CZ  NH1  sing N N 108 
ARG   CZ  NH2  doub N N 109 
ARG   NH1 HH11 sing N N 110 
ARG   NH1 HH12 sing N N 111 
ARG   NH2 HH21 sing N N 112 
ARG   NH2 HH22 sing N N 113 
ARG   OXT HXT  sing N N 114 
ASN   N   CA   sing N N 115 
ASN   N   H    sing N N 116 
ASN   N   H2   sing N N 117 
ASN   CA  C    sing N N 118 
ASN   CA  CB   sing N N 119 
ASN   CA  HA   sing N N 120 
ASN   C   O    doub N N 121 
ASN   C   OXT  sing N N 122 
ASN   CB  CG   sing N N 123 
ASN   CB  HB2  sing N N 124 
ASN   CB  HB3  sing N N 125 
ASN   CG  OD1  doub N N 126 
ASN   CG  ND2  sing N N 127 
ASN   ND2 HD21 sing N N 128 
ASN   ND2 HD22 sing N N 129 
ASN   OXT HXT  sing N N 130 
ASP   N   CA   sing N N 131 
ASP   N   H    sing N N 132 
ASP   N   H2   sing N N 133 
ASP   CA  C    sing N N 134 
ASP   CA  CB   sing N N 135 
ASP   CA  HA   sing N N 136 
ASP   C   O    doub N N 137 
ASP   C   OXT  sing N N 138 
ASP   CB  CG   sing N N 139 
ASP   CB  HB2  sing N N 140 
ASP   CB  HB3  sing N N 141 
ASP   CG  OD1  doub N N 142 
ASP   CG  OD2  sing N N 143 
ASP   OD2 HD2  sing N N 144 
ASP   OXT HXT  sing N N 145 
CYS   N   CA   sing N N 146 
CYS   N   H    sing N N 147 
CYS   N   H2   sing N N 148 
CYS   CA  C    sing N N 149 
CYS   CA  CB   sing N N 150 
CYS   CA  HA   sing N N 151 
CYS   C   O    doub N N 152 
CYS   C   OXT  sing N N 153 
CYS   CB  SG   sing N N 154 
CYS   CB  HB2  sing N N 155 
CYS   CB  HB3  sing N N 156 
CYS   SG  HG   sing N N 157 
CYS   OXT HXT  sing N N 158 
EDO   C1  O1   sing N N 159 
EDO   C1  C2   sing N N 160 
EDO   C1  H11  sing N N 161 
EDO   C1  H12  sing N N 162 
EDO   O1  HO1  sing N N 163 
EDO   C2  O2   sing N N 164 
EDO   C2  H21  sing N N 165 
EDO   C2  H22  sing N N 166 
EDO   O2  HO2  sing N N 167 
GLN   N   CA   sing N N 168 
GLN   N   H    sing N N 169 
GLN   N   H2   sing N N 170 
GLN   CA  C    sing N N 171 
GLN   CA  CB   sing N N 172 
GLN   CA  HA   sing N N 173 
GLN   C   O    doub N N 174 
GLN   C   OXT  sing N N 175 
GLN   CB  CG   sing N N 176 
GLN   CB  HB2  sing N N 177 
GLN   CB  HB3  sing N N 178 
GLN   CG  CD   sing N N 179 
GLN   CG  HG2  sing N N 180 
GLN   CG  HG3  sing N N 181 
GLN   CD  OE1  doub N N 182 
GLN   CD  NE2  sing N N 183 
GLN   NE2 HE21 sing N N 184 
GLN   NE2 HE22 sing N N 185 
GLN   OXT HXT  sing N N 186 
GLU   N   CA   sing N N 187 
GLU   N   H    sing N N 188 
GLU   N   H2   sing N N 189 
GLU   CA  C    sing N N 190 
GLU   CA  CB   sing N N 191 
GLU   CA  HA   sing N N 192 
GLU   C   O    doub N N 193 
GLU   C   OXT  sing N N 194 
GLU   CB  CG   sing N N 195 
GLU   CB  HB2  sing N N 196 
GLU   CB  HB3  sing N N 197 
GLU   CG  CD   sing N N 198 
GLU   CG  HG2  sing N N 199 
GLU   CG  HG3  sing N N 200 
GLU   CD  OE1  doub N N 201 
GLU   CD  OE2  sing N N 202 
GLU   OE2 HE2  sing N N 203 
GLU   OXT HXT  sing N N 204 
GLY   N   CA   sing N N 205 
GLY   N   H    sing N N 206 
GLY   N   H2   sing N N 207 
GLY   CA  C    sing N N 208 
GLY   CA  HA2  sing N N 209 
GLY   CA  HA3  sing N N 210 
GLY   C   O    doub N N 211 
GLY   C   OXT  sing N N 212 
GLY   OXT HXT  sing N N 213 
HIS   N   CA   sing N N 214 
HIS   N   H    sing N N 215 
HIS   N   H2   sing N N 216 
HIS   CA  C    sing N N 217 
HIS   CA  CB   sing N N 218 
HIS   CA  HA   sing N N 219 
HIS   C   O    doub N N 220 
HIS   C   OXT  sing N N 221 
HIS   CB  CG   sing N N 222 
HIS   CB  HB2  sing N N 223 
HIS   CB  HB3  sing N N 224 
HIS   CG  ND1  sing Y N 225 
HIS   CG  CD2  doub Y N 226 
HIS   ND1 CE1  doub Y N 227 
HIS   ND1 HD1  sing N N 228 
HIS   CD2 NE2  sing Y N 229 
HIS   CD2 HD2  sing N N 230 
HIS   CE1 NE2  sing Y N 231 
HIS   CE1 HE1  sing N N 232 
HIS   NE2 HE2  sing N N 233 
HIS   OXT HXT  sing N N 234 
HOH   O   H1   sing N N 235 
HOH   O   H2   sing N N 236 
ILE   N   CA   sing N N 237 
ILE   N   H    sing N N 238 
ILE   N   H2   sing N N 239 
ILE   CA  C    sing N N 240 
ILE   CA  CB   sing N N 241 
ILE   CA  HA   sing N N 242 
ILE   C   O    doub N N 243 
ILE   C   OXT  sing N N 244 
ILE   CB  CG1  sing N N 245 
ILE   CB  CG2  sing N N 246 
ILE   CB  HB   sing N N 247 
ILE   CG1 CD1  sing N N 248 
ILE   CG1 HG12 sing N N 249 
ILE   CG1 HG13 sing N N 250 
ILE   CG2 HG21 sing N N 251 
ILE   CG2 HG22 sing N N 252 
ILE   CG2 HG23 sing N N 253 
ILE   CD1 HD11 sing N N 254 
ILE   CD1 HD12 sing N N 255 
ILE   CD1 HD13 sing N N 256 
ILE   OXT HXT  sing N N 257 
LEU   N   CA   sing N N 258 
LEU   N   H    sing N N 259 
LEU   N   H2   sing N N 260 
LEU   CA  C    sing N N 261 
LEU   CA  CB   sing N N 262 
LEU   CA  HA   sing N N 263 
LEU   C   O    doub N N 264 
LEU   C   OXT  sing N N 265 
LEU   CB  CG   sing N N 266 
LEU   CB  HB2  sing N N 267 
LEU   CB  HB3  sing N N 268 
LEU   CG  CD1  sing N N 269 
LEU   CG  CD2  sing N N 270 
LEU   CG  HG   sing N N 271 
LEU   CD1 HD11 sing N N 272 
LEU   CD1 HD12 sing N N 273 
LEU   CD1 HD13 sing N N 274 
LEU   CD2 HD21 sing N N 275 
LEU   CD2 HD22 sing N N 276 
LEU   CD2 HD23 sing N N 277 
LEU   OXT HXT  sing N N 278 
LYS   N   CA   sing N N 279 
LYS   N   H    sing N N 280 
LYS   N   H2   sing N N 281 
LYS   CA  C    sing N N 282 
LYS   CA  CB   sing N N 283 
LYS   CA  HA   sing N N 284 
LYS   C   O    doub N N 285 
LYS   C   OXT  sing N N 286 
LYS   CB  CG   sing N N 287 
LYS   CB  HB2  sing N N 288 
LYS   CB  HB3  sing N N 289 
LYS   CG  CD   sing N N 290 
LYS   CG  HG2  sing N N 291 
LYS   CG  HG3  sing N N 292 
LYS   CD  CE   sing N N 293 
LYS   CD  HD2  sing N N 294 
LYS   CD  HD3  sing N N 295 
LYS   CE  NZ   sing N N 296 
LYS   CE  HE2  sing N N 297 
LYS   CE  HE3  sing N N 298 
LYS   NZ  HZ1  sing N N 299 
LYS   NZ  HZ2  sing N N 300 
LYS   NZ  HZ3  sing N N 301 
LYS   OXT HXT  sing N N 302 
MET   N   CA   sing N N 303 
MET   N   H    sing N N 304 
MET   N   H2   sing N N 305 
MET   CA  C    sing N N 306 
MET   CA  CB   sing N N 307 
MET   CA  HA   sing N N 308 
MET   C   O    doub N N 309 
MET   C   OXT  sing N N 310 
MET   CB  CG   sing N N 311 
MET   CB  HB2  sing N N 312 
MET   CB  HB3  sing N N 313 
MET   CG  SD   sing N N 314 
MET   CG  HG2  sing N N 315 
MET   CG  HG3  sing N N 316 
MET   SD  CE   sing N N 317 
MET   CE  HE1  sing N N 318 
MET   CE  HE2  sing N N 319 
MET   CE  HE3  sing N N 320 
MET   OXT HXT  sing N N 321 
PHE   N   CA   sing N N 322 
PHE   N   H    sing N N 323 
PHE   N   H2   sing N N 324 
PHE   CA  C    sing N N 325 
PHE   CA  CB   sing N N 326 
PHE   CA  HA   sing N N 327 
PHE   C   O    doub N N 328 
PHE   C   OXT  sing N N 329 
PHE   CB  CG   sing N N 330 
PHE   CB  HB2  sing N N 331 
PHE   CB  HB3  sing N N 332 
PHE   CG  CD1  doub Y N 333 
PHE   CG  CD2  sing Y N 334 
PHE   CD1 CE1  sing Y N 335 
PHE   CD1 HD1  sing N N 336 
PHE   CD2 CE2  doub Y N 337 
PHE   CD2 HD2  sing N N 338 
PHE   CE1 CZ   doub Y N 339 
PHE   CE1 HE1  sing N N 340 
PHE   CE2 CZ   sing Y N 341 
PHE   CE2 HE2  sing N N 342 
PHE   CZ  HZ   sing N N 343 
PHE   OXT HXT  sing N N 344 
PRO   N   CA   sing N N 345 
PRO   N   CD   sing N N 346 
PRO   N   H    sing N N 347 
PRO   CA  C    sing N N 348 
PRO   CA  CB   sing N N 349 
PRO   CA  HA   sing N N 350 
PRO   C   O    doub N N 351 
PRO   C   OXT  sing N N 352 
PRO   CB  CG   sing N N 353 
PRO   CB  HB2  sing N N 354 
PRO   CB  HB3  sing N N 355 
PRO   CG  CD   sing N N 356 
PRO   CG  HG2  sing N N 357 
PRO   CG  HG3  sing N N 358 
PRO   CD  HD2  sing N N 359 
PRO   CD  HD3  sing N N 360 
PRO   OXT HXT  sing N N 361 
SER   N   CA   sing N N 362 
SER   N   H    sing N N 363 
SER   N   H2   sing N N 364 
SER   CA  C    sing N N 365 
SER   CA  CB   sing N N 366 
SER   CA  HA   sing N N 367 
SER   C   O    doub N N 368 
SER   C   OXT  sing N N 369 
SER   CB  OG   sing N N 370 
SER   CB  HB2  sing N N 371 
SER   CB  HB3  sing N N 372 
SER   OG  HG   sing N N 373 
SER   OXT HXT  sing N N 374 
THR   N   CA   sing N N 375 
THR   N   H    sing N N 376 
THR   N   H2   sing N N 377 
THR   CA  C    sing N N 378 
THR   CA  CB   sing N N 379 
THR   CA  HA   sing N N 380 
THR   C   O    doub N N 381 
THR   C   OXT  sing N N 382 
THR   CB  OG1  sing N N 383 
THR   CB  CG2  sing N N 384 
THR   CB  HB   sing N N 385 
THR   OG1 HG1  sing N N 386 
THR   CG2 HG21 sing N N 387 
THR   CG2 HG22 sing N N 388 
THR   CG2 HG23 sing N N 389 
THR   OXT HXT  sing N N 390 
TRP   N   CA   sing N N 391 
TRP   N   H    sing N N 392 
TRP   N   H2   sing N N 393 
TRP   CA  C    sing N N 394 
TRP   CA  CB   sing N N 395 
TRP   CA  HA   sing N N 396 
TRP   C   O    doub N N 397 
TRP   C   OXT  sing N N 398 
TRP   CB  CG   sing N N 399 
TRP   CB  HB2  sing N N 400 
TRP   CB  HB3  sing N N 401 
TRP   CG  CD1  doub Y N 402 
TRP   CG  CD2  sing Y N 403 
TRP   CD1 NE1  sing Y N 404 
TRP   CD1 HD1  sing N N 405 
TRP   CD2 CE2  doub Y N 406 
TRP   CD2 CE3  sing Y N 407 
TRP   NE1 CE2  sing Y N 408 
TRP   NE1 HE1  sing N N 409 
TRP   CE2 CZ2  sing Y N 410 
TRP   CE3 CZ3  doub Y N 411 
TRP   CE3 HE3  sing N N 412 
TRP   CZ2 CH2  doub Y N 413 
TRP   CZ2 HZ2  sing N N 414 
TRP   CZ3 CH2  sing Y N 415 
TRP   CZ3 HZ3  sing N N 416 
TRP   CH2 HH2  sing N N 417 
TRP   OXT HXT  sing N N 418 
TYR   N   CA   sing N N 419 
TYR   N   H    sing N N 420 
TYR   N   H2   sing N N 421 
TYR   CA  C    sing N N 422 
TYR   CA  CB   sing N N 423 
TYR   CA  HA   sing N N 424 
TYR   C   O    doub N N 425 
TYR   C   OXT  sing N N 426 
TYR   CB  CG   sing N N 427 
TYR   CB  HB2  sing N N 428 
TYR   CB  HB3  sing N N 429 
TYR   CG  CD1  doub Y N 430 
TYR   CG  CD2  sing Y N 431 
TYR   CD1 CE1  sing Y N 432 
TYR   CD1 HD1  sing N N 433 
TYR   CD2 CE2  doub Y N 434 
TYR   CD2 HD2  sing N N 435 
TYR   CE1 CZ   doub Y N 436 
TYR   CE1 HE1  sing N N 437 
TYR   CE2 CZ   sing Y N 438 
TYR   CE2 HE2  sing N N 439 
TYR   CZ  OH   sing N N 440 
TYR   OH  HH   sing N N 441 
TYR   OXT HXT  sing N N 442 
VAL   N   CA   sing N N 443 
VAL   N   H    sing N N 444 
VAL   N   H2   sing N N 445 
VAL   CA  C    sing N N 446 
VAL   CA  CB   sing N N 447 
VAL   CA  HA   sing N N 448 
VAL   C   O    doub N N 449 
VAL   C   OXT  sing N N 450 
VAL   CB  CG1  sing N N 451 
VAL   CB  CG2  sing N N 452 
VAL   CB  HB   sing N N 453 
VAL   CG1 HG11 sing N N 454 
VAL   CG1 HG12 sing N N 455 
VAL   CG1 HG13 sing N N 456 
VAL   CG2 HG21 sing N N 457 
VAL   CG2 HG22 sing N N 458 
VAL   CG2 HG23 sing N N 459 
VAL   OXT HXT  sing N N 460 
# 
_pdbx_audit_support.funding_organization   'Swiss National Science Foundation' 
_pdbx_audit_support.country                Switzerland 
_pdbx_audit_support.grant_number           180544 
_pdbx_audit_support.ordinal                1 
# 
_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   7ONM 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F2F 
_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]   0.005581 
_atom_sites.fract_transf_matrix[1][2]   0.003222 
_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]   0.006445 
_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]   0.009115 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
S  
ZN 
# 
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   . ALA   A  1 2   ? 47.872 2.425   -18.298 1.00 16.87 ? 2    ALA   A N   1 
ATOM   2     C  CA  . ALA   A  1 2   ? 49.231 1.841   -18.392 1.00 17.29 ? 2    ALA   A CA  1 
ATOM   3     C  C   . ALA   A  1 2   ? 49.264 0.560   -17.591 1.00 17.51 ? 2    ALA   A C   1 
ATOM   4     O  O   . ALA   A  1 2   ? 48.244 -0.145  -17.548 1.00 17.37 ? 2    ALA   A O   1 
ATOM   5     C  CB  . ALA   A  1 2   ? 50.281 2.886   -17.895 1.00 16.19 ? 2    ALA   A CB  1 
ATOM   6     N  N   . HIS   A  1 3   ? 50.381 0.218   -16.932 1.00 16.93 ? 3    HIS   A N   1 
ATOM   7     C  CA  . HIS   A  1 3   ? 50.397 -1.054  -16.197 1.00 17.40 ? 3    HIS   A CA  1 
ATOM   8     C  C   . HIS   A  1 3   ? 49.533 -1.001  -14.950 1.00 16.40 ? 3    HIS   A C   1 
ATOM   9     O  O   . HIS   A  1 3   ? 49.599 -0.051  -14.178 1.00 17.63 ? 3    HIS   A O   1 
ATOM   10    C  CB  . HIS   A  1 3   ? 51.842 -1.445  -15.847 1.00 17.45 ? 3    HIS   A CB  1 
ATOM   11    C  CG  . HIS   A  1 3   ? 52.621 -1.868  -17.054 1.00 21.33 ? 3    HIS   A CG  1 
ATOM   12    N  ND1 . HIS   A  1 3   ? 53.218 -3.099  -17.167 1.00 27.58 ? 3    HIS   A ND1 1 
ATOM   13    C  CD2 . HIS   A  1 3   ? 52.785 -1.256  -18.251 1.00 23.40 ? 3    HIS   A CD2 1 
ATOM   14    C  CE1 . HIS   A  1 3   ? 53.780 -3.205  -18.361 1.00 27.36 ? 3    HIS   A CE1 1 
ATOM   15    N  NE2 . HIS   A  1 3   ? 53.536 -2.093  -19.034 1.00 24.40 ? 3    HIS   A NE2 1 
ATOM   16    N  N   . HIS   A  1 4   ? 48.701 -2.038  -14.750 1.00 15.72 ? 4    HIS   A N   1 
ATOM   17    C  CA  . HIS   A  1 4   ? 47.856 -2.078  -13.568 1.00 16.05 ? 4    HIS   A CA  1 
ATOM   18    C  C   . HIS   A  1 4   ? 48.708 -2.389  -12.346 1.00 15.35 ? 4    HIS   A C   1 
ATOM   19    O  O   . HIS   A  1 4   ? 49.724 -3.109  -12.421 1.00 16.25 ? 4    HIS   A O   1 
ATOM   20    C  CB  . HIS   A  1 4   ? 46.769 -3.133  -13.834 1.00 16.11 ? 4    HIS   A CB  1 
ATOM   21    C  CG  . HIS   A  1 4   ? 45.706 -3.280  -12.802 1.00 15.18 ? 4    HIS   A CG  1 
ATOM   22    N  ND1 . HIS   A  1 4   ? 44.792 -2.274  -12.494 1.00 12.96 ? 4    HIS   A ND1 1 
ATOM   23    C  CD2 . HIS   A  1 4   ? 45.344 -4.363  -12.080 1.00 15.82 ? 4    HIS   A CD2 1 
ATOM   24    C  CE1 . HIS   A  1 4   ? 43.930 -2.753  -11.597 1.00 14.42 ? 4    HIS   A CE1 1 
ATOM   25    N  NE2 . HIS   A  1 4   ? 44.248 -4.013  -11.336 1.00 14.63 ? 4    HIS   A NE2 1 
ATOM   26    N  N   . TRP   A  1 5   ? 48.262 -1.872  -11.202 1.00 14.80 ? 5    TRP   A N   1 
ATOM   27    C  CA  . TRP   A  1 5   ? 48.999 -2.107  -9.951  1.00 14.25 ? 5    TRP   A CA  1 
ATOM   28    C  C   . TRP   A  1 5   ? 49.018 -3.581  -9.553  1.00 16.61 ? 5    TRP   A C   1 
ATOM   29    O  O   . TRP   A  1 5   ? 48.226 -4.403  -10.026 1.00 16.08 ? 5    TRP   A O   1 
ATOM   30    C  CB  . TRP   A  1 5   ? 48.384 -1.289  -8.800  1.00 14.35 ? 5    TRP   A CB  1 
ATOM   31    C  CG  . TRP   A  1 5   ? 46.982 -1.725  -8.371  1.00 13.44 ? 5    TRP   A CG  1 
ATOM   32    C  CD1 . TRP   A  1 5   ? 45.799 -1.272  -8.884  1.00 15.39 ? 5    TRP   A CD1 1 
ATOM   33    C  CD2 . TRP   A  1 5   ? 46.676 -2.718  -7.397  1.00 13.59 ? 5    TRP   A CD2 1 
ATOM   34    N  NE1 . TRP   A  1 5   ? 44.735 -1.924  -8.262  1.00 14.67 ? 5    TRP   A NE1 1 
ATOM   35    C  CE2 . TRP   A  1 5   ? 45.247 -2.816  -7.347  1.00 13.59 ? 5    TRP   A CE2 1 
ATOM   36    C  CE3 . TRP   A  1 5   ? 47.450 -3.546  -6.581  1.00 14.36 ? 5    TRP   A CE3 1 
ATOM   37    C  CZ2 . TRP   A  1 5   ? 44.611 -3.673  -6.465  1.00 13.54 ? 5    TRP   A CZ2 1 
ATOM   38    C  CZ3 . TRP   A  1 5   ? 46.814 -4.405  -5.681  1.00 15.65 ? 5    TRP   A CZ3 1 
ATOM   39    C  CH2 . TRP   A  1 5   ? 45.399 -4.485  -5.655  1.00 14.51 ? 5    TRP   A CH2 1 
ATOM   40    N  N   . GLY   A  1 6   ? 49.989 -3.934  -8.720  1.00 14.76 ? 6    GLY   A N   1 
ATOM   41    C  CA  . GLY   A  1 6   ? 50.102 -5.308  -8.259  1.00 15.33 ? 6    GLY   A CA  1 
ATOM   42    C  C   . GLY   A  1 6   ? 50.988 -5.369  -6.998  1.00 12.99 ? 6    GLY   A C   1 
ATOM   43    O  O   . GLY   A  1 6   ? 51.009 -4.451  -6.172  1.00 15.12 ? 6    GLY   A O   1 
ATOM   44    N  N   . TYR   A  1 7   ? 51.703 -6.495  -6.881  1.00 15.78 ? 7    TYR   A N   1 
ATOM   45    C  CA  . TYR   A  1 7   ? 52.623 -6.741  -5.776  1.00 15.27 ? 7    TYR   A CA  1 
ATOM   46    C  C   . TYR   A  1 7   ? 53.996 -7.111  -6.275  1.00 17.38 ? 7    TYR   A C   1 
ATOM   47    O  O   . TYR   A  1 7   ? 54.818 -7.641  -5.502  1.00 19.66 ? 7    TYR   A O   1 
ATOM   48    C  CB  . TYR   A  1 7   ? 52.086 -7.855  -4.855  1.00 16.44 ? 7    TYR   A CB  1 
ATOM   49    C  CG  . TYR   A  1 7   ? 50.831 -7.464  -4.099  1.00 15.66 ? 7    TYR   A CG  1 
ATOM   50    C  CD1 . TYR   A  1 7   ? 50.907 -6.725  -2.908  1.00 15.41 ? 7    TYR   A CD1 1 
ATOM   51    C  CD2 . TYR   A  1 7   ? 49.559 -7.845  -4.557  1.00 16.74 ? 7    TYR   A CD2 1 
ATOM   52    C  CE1 . TYR   A  1 7   ? 49.757 -6.382  -2.194  1.00 15.35 ? 7    TYR   A CE1 1 
ATOM   53    C  CE2 . TYR   A  1 7   ? 48.412 -7.524  -3.849  1.00 17.41 ? 7    TYR   A CE2 1 
ATOM   54    C  CZ  . TYR   A  1 7   ? 48.523 -6.807  -2.688  1.00 15.07 ? 7    TYR   A CZ  1 
ATOM   55    O  OH  . TYR   A  1 7   ? 47.416 -6.479  -1.962  1.00 17.06 ? 7    TYR   A OH  1 
ATOM   56    N  N   . GLY   A  1 8   ? 54.276 -6.855  -7.548  1.00 17.69 ? 8    GLY   A N   1 
ATOM   57    C  CA  . GLY   A  1 8   ? 55.549 -7.203  -8.127  1.00 19.15 ? 8    GLY   A CA  1 
ATOM   58    C  C   . GLY   A  1 8   ? 56.581 -6.104  -7.933  1.00 18.74 ? 8    GLY   A C   1 
ATOM   59    O  O   . GLY   A  1 8   ? 56.357 -5.108  -7.233  1.00 17.73 ? 8    GLY   A O   1 
ATOM   60    N  N   . LYS   A  1 9   ? 57.719 -6.318  -8.580  1.00 19.85 ? 9    LYS   A N   1 
ATOM   61    C  CA  . LYS   A  1 9   ? 58.873 -5.435  -8.402  1.00 20.20 ? 9    LYS   A CA  1 
ATOM   62    C  C   . LYS   A  1 9   ? 58.618 -4.053  -8.956  1.00 20.28 ? 9    LYS   A C   1 
ATOM   63    O  O   . LYS   A  1 9   ? 59.165 -3.080  -8.438  1.00 20.83 ? 9    LYS   A O   1 
ATOM   64    C  CB  . LYS   A  1 9   ? 60.089 -6.021  -9.109  1.00 22.14 ? 9    LYS   A CB  1 
ATOM   65    C  CG  . LYS   A  1 9   ? 60.406 -7.423  -8.695  1.00 27.08 ? 9    LYS   A CG  1 
ATOM   66    C  CD  . LYS   A  1 9   ? 60.792 -7.389  -7.243  1.00 26.82 ? 9    LYS   A CD  1 
ATOM   67    C  CE  . LYS   A  1 9   ? 61.449 -8.758  -6.803  1.00 35.95 ? 9    LYS   A CE  1 
ATOM   68    N  NZ  . LYS   A  1 9   ? 62.835 -8.923  -7.351  1.00 42.02 ? 9    LYS   A NZ  1 
ATOM   69    N  N   . HIS   A  1 10  ? 57.840 -3.929  -10.036 1.00 20.27 ? 10   HIS   A N   1 
ATOM   70    C  CA  . HIS   A  1 10  ? 57.625 -2.628  -10.628 1.00 18.58 ? 10   HIS   A CA  1 
ATOM   71    C  C   . HIS   A  1 10  ? 56.301 -2.027  -10.275 1.00 18.26 ? 10   HIS   A C   1 
ATOM   72    O  O   . HIS   A  1 10  ? 56.181 -0.794  -10.275 1.00 20.49 ? 10   HIS   A O   1 
ATOM   73    C  CB  . HIS   A  1 10  ? 57.692 -2.705  -12.160 1.00 21.45 ? 10   HIS   A CB  1 
ATOM   74    C  CG  . HIS   A  1 10  ? 59.017 -3.122  -12.688 1.00 25.38 ? 10   HIS   A CG  1 
ATOM   75    N  ND1 . HIS   A  1 10  ? 59.183 -4.231  -13.482 1.00 29.90 ? 10   HIS   A ND1 1 
ATOM   76    C  CD2 . HIS   A  1 10  ? 60.228 -2.552  -12.554 1.00 28.01 ? 10   HIS   A CD2 1 
ATOM   77    C  CE1 . HIS   A  1 10  ? 60.469 -4.336  -13.805 1.00 31.78 ? 10   HIS   A CE1 1 
ATOM   78    N  NE2 . HIS   A  1 10  ? 61.128 -3.351  -13.218 1.00 28.31 ? 10   HIS   A NE2 1 
ATOM   79    N  N   . ASN   A  1 11  ? 55.311 -2.856  -9.926  1.00 16.43 ? 11   ASN   A N   1 
ATOM   80    C  CA  . ASN   A  1 11  ? 53.967 -2.329  -9.693  1.00 15.34 ? 11   ASN   A CA  1 
ATOM   81    C  C   . ASN   A  1 11  ? 53.493 -2.490  -8.255  1.00 15.68 ? 11   ASN   A C   1 
ATOM   82    O  O   . ASN   A  1 11  ? 52.314 -2.251  -7.980  1.00 14.36 ? 11   ASN   A O   1 
ATOM   83    C  CB  . ASN   A  1 11  ? 52.980 -2.990  -10.672 1.00 16.65 ? 11   ASN   A CB  1 
ATOM   84    C  CG  . ASN   A  1 11  ? 52.821 -4.488  -10.436 1.00 18.76 ? 11   ASN   A CG  1 
ATOM   85    O  OD1 . ASN   A  1 11  ? 53.329 -5.036  -9.463  1.00 18.99 ? 11   ASN   A OD1 1 
ATOM   86    N  ND2 . ASN   A  1 11  ? 52.078 -5.156  -11.331 1.00 20.00 ? 11   ASN   A ND2 1 
ATOM   87    N  N   . GLY   A  1 12  ? 54.371 -2.887  -7.336  1.00 14.98 ? 12   GLY   A N   1 
ATOM   88    C  CA  . GLY   A  1 12  ? 53.932 -3.245  -5.996  1.00 15.84 ? 12   GLY   A CA  1 
ATOM   89    C  C   . GLY   A  1 12  ? 53.871 -2.090  -4.993  1.00 15.54 ? 12   GLY   A C   1 
ATOM   90    O  O   . GLY   A  1 12  ? 54.031 -0.919  -5.339  1.00 15.69 ? 12   GLY   A O   1 
ATOM   91    N  N   . PRO   A  1 13  ? 53.647 -2.437  -3.720  1.00 14.48 ? 13   PRO   A N   1 
ATOM   92    C  CA  . PRO   A  1 13  ? 53.335 -1.444  -2.684  1.00 15.57 ? 13   PRO   A CA  1 
ATOM   93    C  C   . PRO   A  1 13  ? 54.244 -0.237  -2.626  1.00 14.00 ? 13   PRO   A C   1 
ATOM   94    O  O   . PRO   A  1 13  ? 53.719 0.891   -2.477  1.00 15.55 ? 13   PRO   A O   1 
ATOM   95    C  CB  . PRO   A  1 13  ? 53.429 -2.290  -1.405  1.00 16.99 ? 13   PRO   A CB  1 
ATOM   96    C  CG  . PRO   A  1 13  ? 52.879 -3.617  -1.859  1.00 15.82 ? 13   PRO   A CG  1 
ATOM   97    C  CD  . PRO   A  1 13  ? 53.358 -3.812  -3.279  1.00 15.74 ? 13   PRO   A CD  1 
ATOM   98    N  N   . GLU   A  1 14  ? 55.579 -0.398  -2.745  1.00 14.62 ? 14   GLU   A N   1 
ATOM   99    C  CA  . GLU   A  1 14  ? 56.459 0.782   -2.583  1.00 15.02 ? 14   GLU   A CA  1 
ATOM   100   C  C   . GLU   A  1 14  ? 56.258 1.781   -3.710  1.00 16.87 ? 14   GLU   A C   1 
ATOM   101   O  O   . GLU   A  1 14  ? 56.697 2.927   -3.591  1.00 17.91 ? 14   GLU   A O   1 
ATOM   102   C  CB  . GLU   A  1 14  ? 57.939 0.377   -2.495  1.00 15.59 ? 14   GLU   A CB  1 
ATOM   103   C  CG  . GLU   A  1 14  ? 58.512 -0.127  -3.811  1.00 16.21 ? 14   GLU   A CG  1 
ATOM   104   C  CD  . GLU   A  1 14  ? 60.014 -0.217  -3.747  1.00 21.99 ? 14   GLU   A CD  1 
ATOM   105   O  OE1 . GLU   A  1 14  ? 60.665 0.335   -2.787  1.00 22.03 ? 14   GLU   A OE1 1 
ATOM   106   O  OE2 . GLU   A  1 14  ? 60.580 -0.799  -4.696  1.00 24.08 ? 14   GLU   A OE2 1 
ATOM   107   N  N   . HIS   A  1 15  ? 55.635 1.365   -4.803  1.00 16.40 ? 15   HIS   A N   1 
ATOM   108   C  CA  . HIS   A  1 15  ? 55.408 2.216   -5.975  1.00 17.21 ? 15   HIS   A CA  1 
ATOM   109   C  C   . HIS   A  1 15  ? 53.984 2.713   -6.096  1.00 14.56 ? 15   HIS   A C   1 
ATOM   110   O  O   . HIS   A  1 15  ? 53.712 3.533   -6.986  1.00 15.77 ? 15   HIS   A O   1 
ATOM   111   C  CB  . HIS   A  1 15  ? 55.757 1.449   -7.272  1.00 17.32 ? 15   HIS   A CB  1 
ATOM   112   C  CG  . HIS   A  1 15  ? 57.186 1.002   -7.331  1.00 20.71 ? 15   HIS   A CG  1 
ATOM   113   N  ND1 . HIS   A  1 15  ? 58.236 1.883   -7.129  1.00 24.41 ? 15   HIS   A ND1 1 
ATOM   114   C  CD2 . HIS   A  1 15  ? 57.753 -0.231  -7.474  1.00 22.70 ? 15   HIS   A CD2 1 
ATOM   115   C  CE1 . HIS   A  1 15  ? 59.384 1.216   -7.181  1.00 26.44 ? 15   HIS   A CE1 1 
ATOM   116   N  NE2 . HIS   A  1 15  ? 59.112 -0.056  -7.419  1.00 24.37 ? 15   HIS   A NE2 1 
ATOM   117   N  N   . TRP   A  1 16  ? 53.034 2.242   -5.258  1.00 13.96 ? 16   TRP   A N   1 
ATOM   118   C  CA  . TRP   A  1 16  ? 51.650 2.607   -5.478  1.00 13.31 ? 16   TRP   A CA  1 
ATOM   119   C  C   . TRP   A  1 16  ? 51.429 4.100   -5.436  1.00 14.96 ? 16   TRP   A C   1 
ATOM   120   O  O   . TRP   A  1 16  ? 50.562 4.588   -6.167  1.00 16.08 ? 16   TRP   A O   1 
ATOM   121   C  CB  . TRP   A  1 16  ? 50.759 1.943   -4.429  1.00 13.77 ? 16   TRP   A CB  1 
ATOM   122   C  CG  . TRP   A  1 16  ? 50.605 0.465   -4.622  1.00 14.65 ? 16   TRP   A CG  1 
ATOM   123   C  CD1 . TRP   A  1 16  ? 50.934 -0.283  -5.718  1.00 13.51 ? 16   TRP   A CD1 1 
ATOM   124   C  CD2 . TRP   A  1 16  ? 50.081 -0.468  -3.641  1.00 14.13 ? 16   TRP   A CD2 1 
ATOM   125   N  NE1 . TRP   A  1 16  ? 50.620 -1.613  -5.487  1.00 14.01 ? 16   TRP   A NE1 1 
ATOM   126   C  CE2 . TRP   A  1 16  ? 50.139 -1.762  -4.219  1.00 13.16 ? 16   TRP   A CE2 1 
ATOM   127   C  CE3 . TRP   A  1 16  ? 49.608 -0.329  -2.336  1.00 14.37 ? 16   TRP   A CE3 1 
ATOM   128   C  CZ2 . TRP   A  1 16  ? 49.660 -2.907  -3.557  1.00 14.52 ? 16   TRP   A CZ2 1 
ATOM   129   C  CZ3 . TRP   A  1 16  ? 49.177 -1.460  -1.643  1.00 13.72 ? 16   TRP   A CZ3 1 
ATOM   130   C  CH2 . TRP   A  1 16  ? 49.186 -2.747  -2.267  1.00 14.50 ? 16   TRP   A CH2 1 
ATOM   131   N  N   . HIS   A  1 17  ? 52.167 4.828   -4.585  1.00 14.14 ? 17   HIS   A N   1 
ATOM   132   C  CA  . HIS   A  1 17  ? 52.005 6.296   -4.507  1.00 14.17 ? 17   HIS   A CA  1 
ATOM   133   C  C   . HIS   A  1 17  ? 52.162 6.988   -5.853  1.00 15.34 ? 17   HIS   A C   1 
ATOM   134   O  O   . HIS   A  1 17  ? 51.664 8.133   -5.992  1.00 16.91 ? 17   HIS   A O   1 
ATOM   135   C  CB  . HIS   A  1 17  ? 53.014 6.911   -3.509  1.00 17.66 ? 17   HIS   A CB  1 
ATOM   136   C  CG  . HIS   A  1 17  ? 54.425 6.767   -3.955  1.00 17.27 ? 17   HIS   A CG  1 
ATOM   137   N  ND1 . HIS   A  1 17  ? 55.094 7.767   -4.632  1.00 21.48 ? 17   HIS   A ND1 1 
ATOM   138   C  CD2 . HIS   A  1 17  ? 55.253 5.689   -3.933  1.00 15.01 ? 17   HIS   A CD2 1 
ATOM   139   C  CE1 . HIS   A  1 17  ? 56.304 7.320   -4.948  1.00 20.17 ? 17   HIS   A CE1 1 
ATOM   140   N  NE2 . HIS   A  1 17  ? 56.415 6.069   -4.531  1.00 19.12 ? 17   HIS   A NE2 1 
ATOM   141   N  N   . LYS   A  1 18  ? 52.860 6.363   -6.828  1.00 14.67 ? 18   LYS   A N   1 
ATOM   142   C  CA  . LYS   A  1 18  ? 53.110 7.030   -8.106  1.00 13.45 ? 18   LYS   A CA  1 
ATOM   143   C  C   . LYS   A  1 18  ? 51.815 7.241   -8.874  1.00 15.55 ? 18   LYS   A C   1 
ATOM   144   O  O   . LYS   A  1 18  ? 51.731 8.177   -9.679  1.00 15.06 ? 18   LYS   A O   1 
ATOM   145   C  CB  . LYS   A  1 18  ? 54.080 6.199   -8.946  1.00 16.62 ? 18   LYS   A CB  1 
ATOM   146   C  CG  . LYS   A  1 18  ? 55.442 6.184   -8.305  1.00 23.85 ? 18   LYS   A CG  1 
ATOM   147   C  CD  . LYS   A  1 18  ? 56.359 5.229   -9.110  1.00 25.43 ? 18   LYS   A CD  1 
ATOM   148   C  CE  . LYS   A  1 18  ? 57.711 5.052   -8.397  1.00 27.63 ? 18   LYS   A CE  1 
ATOM   149   N  NZ  . LYS   A  1 18  ? 58.552 4.097   -9.298  1.00 32.97 ? 18   LYS   A NZ  1 
ATOM   150   N  N   . ASP   A  1 19  ? 50.836 6.382   -8.649  1.00 14.75 ? 19   ASP   A N   1 
ATOM   151   C  CA  . ASP   A  1 19  ? 49.516 6.536   -9.274  1.00 15.22 ? 19   ASP   A CA  1 
ATOM   152   C  C   . ASP   A  1 19  ? 48.408 6.870   -8.290  1.00 15.96 ? 19   ASP   A C   1 
ATOM   153   O  O   . ASP   A  1 19  ? 47.384 7.435   -8.709  1.00 14.83 ? 19   ASP   A O   1 
ATOM   154   C  CB  . ASP   A  1 19  ? 49.127 5.244   -10.029 1.00 13.86 ? 19   ASP   A CB  1 
ATOM   155   C  CG  . ASP   A  1 19  ? 50.082 4.919   -11.107 1.00 16.42 ? 19   ASP   A CG  1 
ATOM   156   O  OD1 . ASP   A  1 19  ? 50.120 5.653   -12.095 1.00 19.55 ? 19   ASP   A OD1 1 
ATOM   157   O  OD2 . ASP   A  1 19  ? 50.835 3.912   -10.946 1.00 18.52 ? 19   ASP   A OD2 1 
ATOM   158   N  N   . PHE   A  1 20  ? 48.588 6.559   -7.006  1.00 13.94 ? 20   PHE   A N   1 
ATOM   159   C  CA  . PHE   A  1 20  ? 47.569 6.732   -5.977  1.00 15.22 ? 20   PHE   A CA  1 
ATOM   160   C  C   . PHE   A  1 20  ? 48.199 7.540   -4.863  1.00 15.41 ? 20   PHE   A C   1 
ATOM   161   O  O   . PHE   A  1 20  ? 48.685 6.977   -3.868  1.00 17.43 ? 20   PHE   A O   1 
ATOM   162   C  CB  . PHE   A  1 20  ? 47.067 5.382   -5.482  1.00 14.55 ? 20   PHE   A CB  1 
ATOM   163   C  CG  . PHE   A  1 20  ? 46.561 4.478   -6.608  1.00 13.26 ? 20   PHE   A CG  1 
ATOM   164   C  CD1 . PHE   A  1 20  ? 45.274 4.631   -7.070  1.00 15.18 ? 20   PHE   A CD1 1 
ATOM   165   C  CD2 . PHE   A  1 20  ? 47.379 3.514   -7.166  1.00 14.74 ? 20   PHE   A CD2 1 
ATOM   166   C  CE1 . PHE   A  1 20  ? 44.823 3.837   -8.113  1.00 13.77 ? 20   PHE   A CE1 1 
ATOM   167   C  CE2 . PHE   A  1 20  ? 46.930 2.678   -8.210  1.00 14.24 ? 20   PHE   A CE2 1 
ATOM   168   C  CZ  . PHE   A  1 20  ? 45.624 2.864   -8.714  1.00 15.07 ? 20   PHE   A CZ  1 
ATOM   169   N  N   . PRO   A  1 21  ? 48.251 8.857   -4.999  1.00 13.62 ? 21   PRO   A N   1 
ATOM   170   C  CA  . PRO   A  1 21  ? 49.044 9.647   -4.036  1.00 16.06 ? 21   PRO   A CA  1 
ATOM   171   C  C   . PRO   A  1 21  ? 48.506 9.566   -2.604  1.00 15.29 ? 21   PRO   A C   1 
ATOM   172   O  O   . PRO   A  1 21  ? 49.272 9.878   -1.671  1.00 16.85 ? 21   PRO   A O   1 
ATOM   173   C  CB  . PRO   A  1 21  ? 49.006 11.079  -4.597  1.00 19.13 ? 21   PRO   A CB  1 
ATOM   174   C  CG  . PRO   A  1 21  ? 48.037 11.029  -5.717  1.00 19.82 ? 21   PRO   A CG  1 
ATOM   175   C  CD  . PRO   A  1 21  ? 47.853 9.621   -6.189  1.00 14.22 ? 21   PRO   A CD  1 
ATOM   176   N  N   . ILE   A  1 22  ? 47.248 9.160   -2.408  1.00 13.99 ? 22   ILE   A N   1 
ATOM   177   C  CA  A ILE   A  1 22  ? 46.715 8.974   -1.060  0.53 14.23 ? 22   ILE   A CA  1 
ATOM   178   C  CA  B ILE   A  1 22  ? 46.730 8.997   -1.055  0.47 14.34 ? 22   ILE   A CA  1 
ATOM   179   C  C   . ILE   A  1 22  ? 47.485 7.908   -0.316  1.00 15.62 ? 22   ILE   A C   1 
ATOM   180   O  O   . ILE   A  1 22  ? 47.351 7.799   0.920   1.00 15.90 ? 22   ILE   A O   1 
ATOM   181   C  CB  A ILE   A  1 22  ? 45.200 8.665   -1.129  0.53 14.46 ? 22   ILE   A CB  1 
ATOM   182   C  CB  B ILE   A  1 22  ? 45.197 8.772   -1.123  0.47 14.48 ? 22   ILE   A CB  1 
ATOM   183   C  CG1 A ILE   A  1 22  ? 44.569 8.788   0.270   0.53 14.08 ? 22   ILE   A CG1 1 
ATOM   184   C  CG1 B ILE   A  1 22  ? 44.528 9.046   0.230   0.47 14.27 ? 22   ILE   A CG1 1 
ATOM   185   C  CG2 A ILE   A  1 22  ? 44.975 7.303   -1.702  0.53 15.16 ? 22   ILE   A CG2 1 
ATOM   186   C  CG2 B ILE   A  1 22  ? 44.862 7.375   -1.567  0.47 14.75 ? 22   ILE   A CG2 1 
ATOM   187   C  CD1 A ILE   A  1 22  ? 44.641 10.199  0.800   0.53 14.57 ? 22   ILE   A CD1 1 
ATOM   188   C  CD1 B ILE   A  1 22  ? 43.050 8.730   0.203   0.47 14.18 ? 22   ILE   A CD1 1 
ATOM   189   N  N   . ALA   A  1 23  ? 48.304 7.111   -1.023  1.00 14.86 ? 23   ALA   A N   1 
ATOM   190   C  CA  . ALA   A  1 23  ? 49.179 6.170   -0.322  1.00 15.13 ? 23   ALA   A CA  1 
ATOM   191   C  C   . ALA   A  1 23  ? 49.996 6.824   0.784   1.00 14.69 ? 23   ALA   A C   1 
ATOM   192   O  O   . ALA   A  1 23  ? 50.384 6.111   1.731   1.00 16.32 ? 23   ALA   A O   1 
ATOM   193   C  CB  . ALA   A  1 23  ? 50.180 5.534   -1.315  1.00 15.44 ? 23   ALA   A CB  1 
ATOM   194   N  N   . LYS   A  1 24  ? 50.297 8.128   0.678   1.00 16.00 ? 24   LYS   A N   1 
ATOM   195   C  CA  . LYS   A  1 24  ? 51.077 8.876   1.672   1.00 15.74 ? 24   LYS   A CA  1 
ATOM   196   C  C   . LYS   A  1 24  ? 50.177 9.720   2.575   1.00 16.54 ? 24   LYS   A C   1 
ATOM   197   O  O   . LYS   A  1 24  ? 50.655 10.677  3.206   1.00 18.86 ? 24   LYS   A O   1 
ATOM   198   C  CB  . LYS   A  1 24  ? 52.119 9.732   0.959   1.00 18.99 ? 24   LYS   A CB  1 
ATOM   199   C  CG  . LYS   A  1 24  ? 53.165 8.850   0.232   1.00 22.52 ? 24   LYS   A CG  1 
ATOM   200   C  CD  . LYS   A  1 24  ? 54.304 9.686   -0.321  1.00 30.60 ? 24   LYS   A CD  1 
ATOM   201   C  CE  . LYS   A  1 24  ? 55.290 8.817   -1.108  1.00 34.69 ? 24   LYS   A CE  1 
ATOM   202   N  NZ  . LYS   A  1 24  ? 56.132 7.859   -0.263  1.00 38.32 ? 24   LYS   A NZ  1 
ATOM   203   N  N   . GLY   A  1 25  ? 48.894 9.365   2.673   1.00 17.49 ? 25   GLY   A N   1 
ATOM   204   C  CA  . GLY   A  1 25  ? 47.868 10.112  3.402   1.00 17.99 ? 25   GLY   A CA  1 
ATOM   205   C  C   . GLY   A  1 25  ? 47.992 9.977   4.917   1.00 19.15 ? 25   GLY   A C   1 
ATOM   206   O  O   . GLY   A  1 25  ? 48.911 9.363   5.477   1.00 18.63 ? 25   GLY   A O   1 
ATOM   207   N  N   . GLU   A  1 26  ? 47.002 10.561  5.570   1.00 16.65 ? 26   GLU   A N   1 
ATOM   208   C  CA  . GLU   A  1 26  ? 46.987 10.700  7.017   1.00 19.96 ? 26   GLU   A CA  1 
ATOM   209   C  C   . GLU   A  1 26  ? 46.301 9.534   7.711   1.00 19.02 ? 26   GLU   A C   1 
ATOM   210   O  O   . GLU   A  1 26  ? 46.382 9.427   8.954   1.00 22.73 ? 26   GLU   A O   1 
ATOM   211   C  CB  . GLU   A  1 26  ? 46.285 12.018  7.379   1.00 19.88 ? 26   GLU   A CB  1 
ATOM   212   C  CG  . GLU   A  1 26  ? 46.978 13.284  6.853   1.00 23.18 ? 26   GLU   A CG  1 
ATOM   213   C  CD  . GLU   A  1 26  ? 48.367 13.378  7.458   1.00 32.56 ? 26   GLU   A CD  1 
ATOM   214   O  OE1 . GLU   A  1 26  ? 48.488 13.299  8.700   1.00 35.64 ? 26   GLU   A OE1 1 
ATOM   215   O  OE2 . GLU   A  1 26  ? 49.325 13.471  6.682   1.00 35.73 ? 26   GLU   A OE2 1 
ATOM   216   N  N   . ARG   A  1 27  ? 45.596 8.670   6.976   1.00 17.17 ? 27   ARG   A N   1 
ATOM   217   C  CA  A ARG   A  1 27  ? 44.781 7.611   7.555   0.53 16.77 ? 27   ARG   A CA  1 
ATOM   218   C  CA  B ARG   A  1 27  ? 44.865 7.572   7.629   0.47 16.71 ? 27   ARG   A CA  1 
ATOM   219   C  C   . ARG   A  1 27  ? 45.023 6.288   6.821   1.00 16.10 ? 27   ARG   A C   1 
ATOM   220   O  O   . ARG   A  1 27  ? 44.073 5.601   6.431   1.00 17.37 ? 27   ARG   A O   1 
ATOM   221   C  CB  A ARG   A  1 27  ? 43.307 8.040   7.486   0.53 17.83 ? 27   ARG   A CB  1 
ATOM   222   C  CB  B ARG   A  1 27  ? 43.393 7.892   7.840   0.47 17.26 ? 27   ARG   A CB  1 
ATOM   223   C  CG  A ARG   A  1 27  ? 42.290 7.220   8.265   0.53 19.02 ? 27   ARG   A CG  1 
ATOM   224   C  CG  B ARG   A  1 27  ? 43.102 9.237   8.441   0.47 16.61 ? 27   ARG   A CG  1 
ATOM   225   C  CD  A ARG   A  1 27  ? 40.837 7.733   8.003   0.53 17.78 ? 27   ARG   A CD  1 
ATOM   226   C  CD  B ARG   A  1 27  ? 41.601 9.293   8.885   0.47 16.83 ? 27   ARG   A CD  1 
ATOM   227   N  NE  A ARG   A  1 27  ? 39.856 6.632   7.881   0.53 11.17 ? 27   ARG   A NE  1 
ATOM   228   N  NE  B ARG   A  1 27  ? 40.580 9.074   7.830   0.47 15.95 ? 27   ARG   A NE  1 
ATOM   229   C  CZ  A ARG   A  1 27  ? 38.576 6.759   8.138   0.53 19.77 ? 27   ARG   A CZ  1 
ATOM   230   C  CZ  B ARG   A  1 27  ? 40.244 9.947   6.866   0.47 18.39 ? 27   ARG   A CZ  1 
ATOM   231   N  NH1 A ARG   A  1 27  ? 38.045 7.928   8.538   0.53 24.24 ? 27   ARG   A NH1 1 
ATOM   232   N  NH1 B ARG   A  1 27  ? 39.256 9.695   5.966   0.47 15.40 ? 27   ARG   A NH1 1 
ATOM   233   N  NH2 A ARG   A  1 27  ? 37.802 5.715   8.004   0.53 22.76 ? 27   ARG   A NH2 1 
ATOM   234   N  NH2 B ARG   A  1 27  ? 40.934 11.096  6.754   0.47 21.31 ? 27   ARG   A NH2 1 
ATOM   235   N  N   . GLN   A  1 28  ? 46.276 5.925   6.583   1.00 16.59 ? 28   GLN   A N   1 
ATOM   236   C  CA  . GLN   A  1 28  ? 46.574 4.732   5.778   1.00 15.70 ? 28   GLN   A CA  1 
ATOM   237   C  C   . GLN   A  1 28  ? 46.705 3.458   6.616   1.00 15.44 ? 28   GLN   A C   1 
ATOM   238   O  O   . GLN   A  1 28  ? 47.059 3.474   7.799   1.00 17.44 ? 28   GLN   A O   1 
ATOM   239   C  CB  . GLN   A  1 28  ? 47.885 4.941   5.007   1.00 16.08 ? 28   GLN   A CB  1 
ATOM   240   C  CG  . GLN   A  1 28  ? 47.681 6.010   3.920   1.00 15.24 ? 28   GLN   A CG  1 
ATOM   241   C  CD  . GLN   A  1 28  ? 46.784 5.453   2.811   1.00 14.40 ? 28   GLN   A CD  1 
ATOM   242   O  OE1 . GLN   A  1 28  ? 47.183 4.521   2.082   1.00 14.81 ? 28   GLN   A OE1 1 
ATOM   243   N  NE2 . GLN   A  1 28  ? 45.568 5.991   2.674   1.00 15.36 ? 28   GLN   A NE2 1 
ATOM   244   N  N   . SER   A  1 29  ? 46.466 2.336   5.956   1.00 14.47 ? 29   SER   A N   1 
ATOM   245   C  CA  . SER   A  1 29  ? 46.490 1.011   6.563   1.00 13.94 ? 29   SER   A CA  1 
ATOM   246   C  C   . SER   A  1 29  ? 47.351 0.096   5.705   1.00 16.08 ? 29   SER   A C   1 
ATOM   247   O  O   . SER   A  1 29  ? 47.479 0.316   4.489   1.00 15.66 ? 29   SER   A O   1 
ATOM   248   C  CB  . SER   A  1 29  ? 45.066 0.418   6.639   1.00 15.58 ? 29   SER   A CB  1 
ATOM   249   O  OG  . SER   A  1 29  ? 44.274 1.183   7.513   1.00 15.43 ? 29   SER   A OG  1 
ATOM   250   N  N   . PRO   A  1 30  ? 47.914 -0.973  6.290   1.00 15.73 ? 30   PRO   A N   1 
ATOM   251   C  CA  . PRO   A  1 30  ? 47.808 -1.397  7.690   1.00 14.98 ? 30   PRO   A CA  1 
ATOM   252   C  C   . PRO   A  1 30  ? 48.782 -0.649  8.558   1.00 16.63 ? 30   PRO   A C   1 
ATOM   253   O  O   . PRO   A  1 30  ? 49.504 0.194   8.036   1.00 16.21 ? 30   PRO   A O   1 
ATOM   254   C  CB  . PRO   A  1 30  ? 48.187 -2.881  7.610   1.00 16.27 ? 30   PRO   A CB  1 
ATOM   255   C  CG  . PRO   A  1 30  ? 49.323 -2.879  6.516   1.00 16.29 ? 30   PRO   A CG  1 
ATOM   256   C  CD  . PRO   A  1 30  ? 48.762 -1.895  5.493   1.00 16.86 ? 30   PRO   A CD  1 
ATOM   257   N  N   . VAL   A  1 31  ? 48.738 -0.892  9.862   1.00 16.30 ? 31   VAL   A N   1 
ATOM   258   C  CA  . VAL   A  1 31  ? 49.648 -0.265  10.821  1.00 16.06 ? 31   VAL   A CA  1 
ATOM   259   C  C   . VAL   A  1 31  ? 50.146 -1.336  11.771  1.00 17.59 ? 31   VAL   A C   1 
ATOM   260   O  O   . VAL   A  1 31  ? 49.565 -2.436  11.892  1.00 18.38 ? 31   VAL   A O   1 
ATOM   261   C  CB  . VAL   A  1 31  ? 48.960 0.864   11.620  1.00 16.39 ? 31   VAL   A CB  1 
ATOM   262   C  CG1 . VAL   A  1 31  ? 48.433 1.963   10.685  1.00 19.19 ? 31   VAL   A CG1 1 
ATOM   263   C  CG2 . VAL   A  1 31  ? 47.737 0.272   12.474  1.00 18.91 ? 31   VAL   A CG2 1 
ATOM   264   N  N   . ASP   A  1 32  ? 51.224 -0.995  12.477  1.00 17.04 ? 32   ASP   A N   1 
ATOM   265   C  CA  . ASP   A  1 32  ? 51.639 -1.774  13.620  1.00 17.27 ? 32   ASP   A CA  1 
ATOM   266   C  C   . ASP   A  1 32  ? 50.723 -1.456  14.794  1.00 19.91 ? 32   ASP   A C   1 
ATOM   267   O  O   . ASP   A  1 32  ? 50.426 -0.281  15.085  1.00 21.67 ? 32   ASP   A O   1 
ATOM   268   C  CB  . ASP   A  1 32  ? 53.099 -1.466  13.989  1.00 17.42 ? 32   ASP   A CB  1 
ATOM   269   C  CG  . ASP   A  1 32  ? 53.558 -2.265  15.207  1.00 21.39 ? 32   ASP   A CG  1 
ATOM   270   O  OD1 . ASP   A  1 32  ? 53.431 -3.512  15.164  1.00 21.90 ? 32   ASP   A OD1 1 
ATOM   271   O  OD2 . ASP   A  1 32  ? 54.039 -1.642  16.180  1.00 23.92 ? 32   ASP   A OD2 1 
ATOM   272   N  N   . ILE   A  1 33  ? 50.271 -2.501  15.474  1.00 19.09 ? 33   ILE   A N   1 
ATOM   273   C  CA  . ILE   A  1 33  ? 49.493 -2.358  16.701  1.00 19.45 ? 33   ILE   A CA  1 
ATOM   274   C  C   . ILE   A  1 33  ? 50.436 -2.586  17.871  1.00 20.49 ? 33   ILE   A C   1 
ATOM   275   O  O   . ILE   A  1 33  ? 50.908 -3.710  18.111  1.00 22.01 ? 33   ILE   A O   1 
ATOM   276   C  CB  . ILE   A  1 33  ? 48.339 -3.371  16.726  1.00 18.22 ? 33   ILE   A CB  1 
ATOM   277   C  CG1 . ILE   A  1 33  ? 47.447 -3.118  15.538  1.00 21.02 ? 33   ILE   A CG1 1 
ATOM   278   C  CG2 . ILE   A  1 33  ? 47.594 -3.253  18.048  1.00 21.37 ? 33   ILE   A CG2 1 
ATOM   279   C  CD1 . ILE   A  1 33  ? 46.511 -4.284  15.167  1.00 22.31 ? 33   ILE   A CD1 1 
ATOM   280   N  N   . ASP   A  1 34  ? 50.782 -1.512  18.587  1.00 22.65 ? 34   ASP   A N   1 
ATOM   281   C  CA  . ASP   A  1 34  ? 51.638 -1.648  19.742  1.00 22.47 ? 34   ASP   A CA  1 
ATOM   282   C  C   . ASP   A  1 34  ? 50.789 -1.826  20.987  1.00 26.54 ? 34   ASP   A C   1 
ATOM   283   O  O   . ASP   A  1 34  ? 49.987 -0.952  21.322  1.00 29.02 ? 34   ASP   A O   1 
ATOM   284   C  CB  . ASP   A  1 34  ? 52.561 -0.435  19.908  1.00 23.23 ? 34   ASP   A CB  1 
ATOM   285   C  CG  . ASP   A  1 34  ? 53.424 -0.614  21.112  1.00 26.10 ? 34   ASP   A CG  1 
ATOM   286   O  OD1 . ASP   A  1 34  ? 52.907 -0.456  22.231  1.00 28.65 ? 34   ASP   A OD1 1 
ATOM   287   O  OD2 . ASP   A  1 34  ? 54.546 -1.006  20.870  1.00 28.33 ? 34   ASP   A OD2 1 
ATOM   288   N  N   . THR   A  1 35  ? 50.930 -2.985  21.641  1.00 27.76 ? 35   THR   A N   1 
ATOM   289   C  CA  . THR   A  1 35  ? 50.007 -3.364  22.709  1.00 29.66 ? 35   THR   A CA  1 
ATOM   290   C  C   . THR   A  1 35  ? 50.223 -2.565  23.979  1.00 36.03 ? 35   THR   A C   1 
ATOM   291   O  O   . THR   A  1 35  ? 49.354 -2.597  24.869  1.00 39.68 ? 35   THR   A O   1 
ATOM   292   C  CB  . THR   A  1 35  ? 50.133 -4.856  23.013  1.00 29.17 ? 35   THR   A CB  1 
ATOM   293   O  OG1 . THR   A  1 35  ? 51.442 -5.163  23.508  1.00 29.83 ? 35   THR   A OG1 1 
ATOM   294   C  CG2 . THR   A  1 35  ? 49.868 -5.663  21.723  1.00 27.45 ? 35   THR   A CG2 1 
ATOM   295   N  N   . HIS   A  1 36  ? 51.361 -1.883  24.086  1.00 31.43 ? 36   HIS   A N   1 
ATOM   296   C  CA  . HIS   A  1 36  ? 51.645 -1.076  25.266  1.00 34.24 ? 36   HIS   A CA  1 
ATOM   297   C  C   . HIS   A  1 36  ? 50.959 0.273   25.203  1.00 34.27 ? 36   HIS   A C   1 
ATOM   298   O  O   . HIS   A  1 36  ? 50.745 0.895   26.254  1.00 36.45 ? 36   HIS   A O   1 
ATOM   299   C  CB  . HIS   A  1 36  ? 53.150 -0.903  25.392  1.00 38.43 ? 36   HIS   A CB  1 
ATOM   300   C  CG  . HIS   A  1 36  ? 53.877 -2.186  25.167  1.00 49.11 ? 36   HIS   A CG  1 
ATOM   301   N  ND1 . HIS   A  1 36  ? 54.969 -2.296  24.332  1.00 50.67 ? 36   HIS   A ND1 1 
ATOM   302   C  CD2 . HIS   A  1 36  ? 53.657 -3.428  25.672  1.00 52.46 ? 36   HIS   A CD2 1 
ATOM   303   C  CE1 . HIS   A  1 36  ? 55.369 -3.557  24.304  1.00 52.13 ? 36   HIS   A CE1 1 
ATOM   304   N  NE2 . HIS   A  1 36  ? 54.599 -4.260  25.121  1.00 51.94 ? 36   HIS   A NE2 1 
ATOM   305   N  N   . THR   A  1 37  ? 50.678 0.763   24.000  1.00 30.05 ? 37   THR   A N   1 
ATOM   306   C  CA  . THR   A  1 37  ? 50.095 2.084   23.838  1.00 27.84 ? 37   THR   A CA  1 
ATOM   307   C  C   . THR   A  1 37  ? 48.622 2.065   23.417  1.00 25.90 ? 37   THR   A C   1 
ATOM   308   O  O   . THR   A  1 37  ? 47.921 3.055   23.673  1.00 31.47 ? 37   THR   A O   1 
ATOM   309   C  CB  . THR   A  1 37  ? 50.923 2.902   22.830  1.00 29.98 ? 37   THR   A CB  1 
ATOM   310   O  OG1 . THR   A  1 37  ? 51.062 2.198   21.612  1.00 33.47 ? 37   THR   A OG1 1 
ATOM   311   C  CG2 . THR   A  1 37  ? 52.318 3.184   23.417  1.00 30.63 ? 37   THR   A CG2 1 
ATOM   312   N  N   . ALA   A  1 38  ? 48.142 0.977   22.807  1.00 26.37 ? 38   ALA   A N   1 
ATOM   313   C  CA  . ALA   A  1 38  ? 46.719 0.870   22.502  1.00 28.16 ? 38   ALA   A CA  1 
ATOM   314   C  C   . ALA   A  1 38  ? 45.929 1.010   23.810  1.00 33.35 ? 38   ALA   A C   1 
ATOM   315   O  O   . ALA   A  1 38  ? 46.320 0.435   24.823  1.00 39.08 ? 38   ALA   A O   1 
ATOM   316   C  CB  . ALA   A  1 38  ? 46.457 -0.463  21.802  1.00 27.96 ? 38   ALA   A CB  1 
ATOM   317   N  N   . LYS   A  1 39  ? 44.852 1.816   23.811  1.00 29.67 ? 39   LYS   A N   1 
ATOM   318   C  CA  . LYS   A  1 39  ? 44.109 2.154   25.028  1.00 30.43 ? 39   LYS   A CA  1 
ATOM   319   C  C   . LYS   A  1 39  ? 42.656 1.674   25.003  1.00 32.03 ? 39   LYS   A C   1 
ATOM   320   O  O   . LYS   A  1 39  ? 41.942 1.889   24.023  1.00 29.43 ? 39   LYS   A O   1 
ATOM   321   C  CB  . LYS   A  1 39  ? 44.102 3.668   25.268  1.00 35.67 ? 39   LYS   A CB  1 
ATOM   322   C  CG  . LYS   A  1 39  ? 45.410 4.244   25.808  1.00 43.90 ? 39   LYS   A CG  1 
ATOM   323   C  CD  . LYS   A  1 39  ? 45.215 5.696   26.222  1.00 49.07 ? 39   LYS   A CD  1 
ATOM   324   C  CE  . LYS   A  1 39  ? 44.058 5.794   27.222  1.00 55.11 ? 39   LYS   A CE  1 
ATOM   325   N  NZ  . LYS   A  1 39  ? 43.874 7.165   27.808  1.00 58.67 ? 39   LYS   A NZ  1 
ATOM   326   N  N   . TYR   A  1 40  ? 42.195 1.107   26.124  1.00 32.91 ? 40   TYR   A N   1 
ATOM   327   C  CA  . TYR   A  1 40  ? 40.788 0.744   26.256  1.00 31.65 ? 40   TYR   A CA  1 
ATOM   328   C  C   . TYR   A  1 40  ? 39.880 1.962   26.088  1.00 31.72 ? 40   TYR   A C   1 
ATOM   329   O  O   . TYR   A  1 40  ? 40.144 3.042   26.633  1.00 32.76 ? 40   TYR   A O   1 
ATOM   330   C  CB  . TYR   A  1 40  ? 40.555 0.087   27.616  1.00 32.99 ? 40   TYR   A CB  1 
ATOM   331   C  CG  . TYR   A  1 40  ? 39.107 -0.037  27.974  1.00 35.32 ? 40   TYR   A CG  1 
ATOM   332   C  CD1 . TYR   A  1 40  ? 38.277 -0.940  27.308  1.00 34.40 ? 40   TYR   A CD1 1 
ATOM   333   C  CD2 . TYR   A  1 40  ? 38.560 0.752   28.969  1.00 37.52 ? 40   TYR   A CD2 1 
ATOM   334   C  CE1 . TYR   A  1 40  ? 36.928 -1.048  27.652  1.00 37.25 ? 40   TYR   A CE1 1 
ATOM   335   C  CE2 . TYR   A  1 40  ? 37.231 0.643   29.334  1.00 41.57 ? 40   TYR   A CE2 1 
ATOM   336   C  CZ  . TYR   A  1 40  ? 36.418 -0.240  28.656  1.00 39.81 ? 40   TYR   A CZ  1 
ATOM   337   O  OH  . TYR   A  1 40  ? 35.081 -0.352  29.032  1.00 42.98 ? 40   TYR   A OH  1 
ATOM   338   N  N   . ASP   A  1 41  ? 38.825 1.797   25.295  1.00 31.20 ? 41   ASP   A N   1 
ATOM   339   C  CA  . ASP   A  1 41  ? 37.863 2.866   25.028  1.00 32.56 ? 41   ASP   A CA  1 
ATOM   340   C  C   . ASP   A  1 41  ? 36.510 2.458   25.607  1.00 34.02 ? 41   ASP   A C   1 
ATOM   341   O  O   . ASP   A  1 41  ? 35.777 1.650   25.001  1.00 32.98 ? 41   ASP   A O   1 
ATOM   342   C  CB  . ASP   A  1 41  ? 37.764 3.119   23.520  1.00 31.37 ? 41   ASP   A CB  1 
ATOM   343   C  CG  . ASP   A  1 41  ? 36.874 4.285   23.175  1.00 35.78 ? 41   ASP   A CG  1 
ATOM   344   O  OD1 . ASP   A  1 41  ? 36.170 4.833   24.072  1.00 38.93 ? 41   ASP   A OD1 1 
ATOM   345   O  OD2 . ASP   A  1 41  ? 36.870 4.641   21.970  1.00 37.87 ? 41   ASP   A OD2 1 
ATOM   346   N  N   . PRO   A  1 42  ? 36.119 3.009   26.748  1.00 36.36 ? 42   PRO   A N   1 
ATOM   347   C  CA  . PRO   A  1 42  ? 34.828 2.630   27.340  1.00 35.35 ? 42   PRO   A CA  1 
ATOM   348   C  C   . PRO   A  1 42  ? 33.616 3.009   26.497  1.00 35.06 ? 42   PRO   A C   1 
ATOM   349   O  O   . PRO   A  1 42  ? 32.505 2.526   26.799  1.00 38.55 ? 42   PRO   A O   1 
ATOM   350   C  CB  . PRO   A  1 42  ? 34.823 3.385   28.679  1.00 38.64 ? 42   PRO   A CB  1 
ATOM   351   C  CG  . PRO   A  1 42  ? 35.810 4.531   28.470  1.00 40.24 ? 42   PRO   A CG  1 
ATOM   352   C  CD  . PRO   A  1 42  ? 36.821 4.074   27.487  1.00 36.45 ? 42   PRO   A CD  1 
ATOM   353   N  N   . SER   A  1 43  ? 33.773 3.866   25.493  1.00 33.74 ? 43   SER   A N   1 
ATOM   354   C  CA  . SER   A  1 43  ? 32.666 4.264   24.631  1.00 38.23 ? 43   SER   A CA  1 
ATOM   355   C  C   . SER   A  1 43  ? 32.301 3.203   23.594  1.00 38.70 ? 43   SER   A C   1 
ATOM   356   O  O   . SER   A  1 43  ? 31.234 3.313   22.986  1.00 41.32 ? 43   SER   A O   1 
ATOM   357   C  CB  . SER   A  1 43  ? 32.990 5.593   23.913  1.00 39.15 ? 43   SER   A CB  1 
ATOM   358   O  OG  . SER   A  1 43  ? 33.841 5.417   22.780  1.00 39.02 ? 43   SER   A OG  1 
ATOM   359   N  N   . LEU   A  1 44  ? 33.148 2.202   23.368  1.00 34.31 ? 44   LEU   A N   1 
ATOM   360   C  CA  . LEU   A  1 44  ? 32.816 1.132   22.432  1.00 33.24 ? 44   LEU   A CA  1 
ATOM   361   C  C   . LEU   A  1 44  ? 31.636 0.303   22.939  1.00 37.47 ? 44   LEU   A C   1 
ATOM   362   O  O   . LEU   A  1 44  ? 31.586 -0.088  24.106  1.00 37.42 ? 44   LEU   A O   1 
ATOM   363   C  CB  . LEU   A  1 44  ? 34.023 0.211   22.219  1.00 30.96 ? 44   LEU   A CB  1 
ATOM   364   C  CG  . LEU   A  1 44  ? 35.180 0.924   21.516  1.00 29.26 ? 44   LEU   A CG  1 
ATOM   365   C  CD1 . LEU   A  1 44  ? 36.502 0.136   21.600  1.00 30.29 ? 44   LEU   A CD1 1 
ATOM   366   C  CD2 . LEU   A  1 44  ? 34.817 1.199   20.047  1.00 28.82 ? 44   LEU   A CD2 1 
ATOM   367   N  N   . LYS   A  1 45  ? 30.695 0.013   22.041  1.00 36.73 ? 45   LYS   A N   1 
ATOM   368   C  CA  . LYS   A  1 45  ? 29.585 -0.856  22.419  1.00 35.62 ? 45   LYS   A CA  1 
ATOM   369   C  C   . LYS   A  1 45  ? 29.948 -2.299  22.119  1.00 33.27 ? 45   LYS   A C   1 
ATOM   370   O  O   . LYS   A  1 45  ? 30.890 -2.567  21.353  1.00 31.04 ? 45   LYS   A O   1 
ATOM   371   C  CB  . LYS   A  1 45  ? 28.328 -0.464  21.648  1.00 37.19 ? 45   LYS   A CB  1 
ATOM   372   C  CG  . LYS   A  1 45  ? 27.965 1.018   21.730  1.00 42.17 ? 45   LYS   A CG  1 
ATOM   373   C  CD  . LYS   A  1 45  ? 27.684 1.447   23.147  1.00 50.03 ? 45   LYS   A CD  1 
ATOM   374   C  CE  . LYS   A  1 45  ? 27.476 2.977   23.259  1.00 55.87 ? 45   LYS   A CE  1 
ATOM   375   N  NZ  . LYS   A  1 45  ? 27.087 3.428   24.643  1.00 61.11 ? 45   LYS   A NZ  1 
ATOM   376   N  N   . PRO   A  1 46  ? 29.202 -3.268  22.664  1.00 32.02 ? 46   PRO   A N   1 
ATOM   377   C  CA  . PRO   A  1 46  ? 29.483 -4.668  22.330  1.00 32.03 ? 46   PRO   A CA  1 
ATOM   378   C  C   . PRO   A  1 46  ? 29.449 -4.868  20.819  1.00 31.38 ? 46   PRO   A C   1 
ATOM   379   O  O   . PRO   A  1 46  ? 28.590 -4.315  20.130  1.00 32.81 ? 46   PRO   A O   1 
ATOM   380   C  CB  . PRO   A  1 46  ? 28.350 -5.437  23.012  1.00 32.91 ? 46   PRO   A CB  1 
ATOM   381   C  CG  . PRO   A  1 46  ? 27.940 -4.498  24.170  1.00 35.67 ? 46   PRO   A CG  1 
ATOM   382   C  CD  . PRO   A  1 46  ? 28.051 -3.135  23.583  1.00 35.92 ? 46   PRO   A CD  1 
ATOM   383   N  N   . LEU   A  1 47  ? 30.401 -5.653  20.312  1.00 28.33 ? 47   LEU   A N   1 
ATOM   384   C  CA  . LEU   A  1 47  ? 30.496 -5.975  18.890  1.00 27.12 ? 47   LEU   A CA  1 
ATOM   385   C  C   . LEU   A  1 47  ? 29.603 -7.172  18.568  1.00 29.39 ? 47   LEU   A C   1 
ATOM   386   O  O   . LEU   A  1 47  ? 29.575 -8.165  19.323  1.00 33.57 ? 47   LEU   A O   1 
ATOM   387   C  CB  . LEU   A  1 47  ? 31.931 -6.287  18.495  1.00 29.58 ? 47   LEU   A CB  1 
ATOM   388   C  CG  . LEU   A  1 47  ? 32.142 -6.520  17.002  1.00 28.46 ? 47   LEU   A CG  1 
ATOM   389   C  CD1 . LEU   A  1 47  ? 32.049 -5.225  16.214  1.00 28.08 ? 47   LEU   A CD1 1 
ATOM   390   C  CD2 . LEU   A  1 47  ? 33.504 -7.186  16.769  1.00 31.19 ? 47   LEU   A CD2 1 
ATOM   391   N  N   . SER   A  1 48  ? 28.829 -7.035  17.496  1.00 27.52 ? 48   SER   A N   1 
ATOM   392   C  CA  A SER   A  1 48  ? 27.909 -8.071  17.049  0.55 30.52 ? 48   SER   A CA  1 
ATOM   393   C  CA  B SER   A  1 48  ? 27.885 -8.050  17.026  0.45 30.48 ? 48   SER   A CA  1 
ATOM   394   C  C   . SER   A  1 48  ? 28.351 -8.553  15.673  1.00 28.29 ? 48   SER   A C   1 
ATOM   395   O  O   . SER   A  1 48  ? 28.335 -7.792  14.702  1.00 28.57 ? 48   SER   A O   1 
ATOM   396   C  CB  A SER   A  1 48  ? 26.473 -7.543  17.022  0.55 32.66 ? 48   SER   A CB  1 
ATOM   397   C  CB  B SER   A  1 48  ? 26.476 -7.473  16.867  0.45 32.59 ? 48   SER   A CB  1 
ATOM   398   O  OG  A SER   A  1 48  ? 25.632 -8.481  16.392  0.55 33.78 ? 48   SER   A OG  1 
ATOM   399   O  OG  B SER   A  1 48  ? 25.840 -7.265  18.095  0.45 36.02 ? 48   SER   A OG  1 
ATOM   400   N  N   . VAL   A  1 49  ? 28.723 -9.831  15.593  1.00 30.19 ? 49   VAL   A N   1 
ATOM   401   C  CA  . VAL   A  1 49  ? 29.109 -10.454 14.329  1.00 29.81 ? 49   VAL   A CA  1 
ATOM   402   C  C   . VAL   A  1 49  ? 27.996 -11.446 14.013  1.00 29.51 ? 49   VAL   A C   1 
ATOM   403   O  O   . VAL   A  1 49  ? 27.908 -12.509 14.636  1.00 35.71 ? 49   VAL   A O   1 
ATOM   404   C  CB  . VAL   A  1 49  ? 30.460 -11.178 14.419  1.00 31.14 ? 49   VAL   A CB  1 
ATOM   405   C  CG1 . VAL   A  1 49  ? 30.809 -11.807 13.035  1.00 33.08 ? 49   VAL   A CG1 1 
ATOM   406   C  CG2 . VAL   A  1 49  ? 31.543 -10.238 14.897  1.00 31.70 ? 49   VAL   A CG2 1 
ATOM   407   N  N   A SER   A  1 50  ? 27.113 -11.105 13.071  0.51 31.48 ? 50   SER   A N   1 
ATOM   408   N  N   B SER   A  1 50  ? 27.151 -11.120 13.041  0.49 31.36 ? 50   SER   A N   1 
ATOM   409   C  CA  A SER   A  1 50  ? 25.883 -11.873 12.834  0.51 33.08 ? 50   SER   A CA  1 
ATOM   410   C  CA  B SER   A  1 50  ? 25.908 -11.859 12.833  0.49 33.06 ? 50   SER   A CA  1 
ATOM   411   C  C   A SER   A  1 50  ? 26.002 -12.532 11.466  0.51 31.23 ? 50   SER   A C   1 
ATOM   412   C  C   B SER   A  1 50  ? 25.990 -12.534 11.469  0.49 31.26 ? 50   SER   A C   1 
ATOM   413   O  O   A SER   A  1 50  ? 25.634 -11.951 10.444  0.51 31.68 ? 50   SER   A O   1 
ATOM   414   O  O   B SER   A  1 50  ? 25.597 -11.958 10.452  0.49 31.68 ? 50   SER   A O   1 
ATOM   415   C  CB  A SER   A  1 50  ? 24.631 -10.995 12.906  0.51 35.46 ? 50   SER   A CB  1 
ATOM   416   C  CB  B SER   A  1 50  ? 24.712 -10.931 12.941  0.49 35.41 ? 50   SER   A CB  1 
ATOM   417   O  OG  A SER   A  1 50  ? 24.517 -10.341 14.153  0.51 38.30 ? 50   SER   A OG  1 
ATOM   418   O  OG  B SER   A  1 50  ? 23.510 -11.658 12.905  0.49 38.42 ? 50   SER   A OG  1 
ATOM   419   N  N   . TYR   A  1 51  ? 26.501 -13.766 11.455  1.00 31.25 ? 51   TYR   A N   1 
ATOM   420   C  CA  . TYR   A  1 51  ? 26.795 -14.470 10.223  1.00 30.26 ? 51   TYR   A CA  1 
ATOM   421   C  C   . TYR   A  1 51  ? 25.978 -15.745 10.063  1.00 33.73 ? 51   TYR   A C   1 
ATOM   422   O  O   . TYR   A  1 51  ? 26.315 -16.562 9.205   1.00 33.32 ? 51   TYR   A O   1 
ATOM   423   C  CB  . TYR   A  1 51  ? 28.277 -14.841 10.162  1.00 29.94 ? 51   TYR   A CB  1 
ATOM   424   C  CG  . TYR   A  1 51  ? 29.268 -13.727 9.892   1.00 26.08 ? 51   TYR   A CG  1 
ATOM   425   C  CD1 . TYR   A  1 51  ? 28.865 -12.424 9.584   1.00 26.98 ? 51   TYR   A CD1 1 
ATOM   426   C  CD2 . TYR   A  1 51  ? 30.624 -13.994 9.948   1.00 24.28 ? 51   TYR   A CD2 1 
ATOM   427   C  CE1 . TYR   A  1 51  ? 29.811 -11.410 9.317   1.00 25.77 ? 51   TYR   A CE1 1 
ATOM   428   C  CE2 . TYR   A  1 51  ? 31.566 -13.016 9.693   1.00 23.26 ? 51   TYR   A CE2 1 
ATOM   429   C  CZ  . TYR   A  1 51  ? 31.178 -11.718 9.360   1.00 22.56 ? 51   TYR   A CZ  1 
ATOM   430   O  OH  . TYR   A  1 51  ? 32.154 -10.796 9.099   1.00 23.14 ? 51   TYR   A OH  1 
ATOM   431   N  N   . ASP   A  1 52  ? 24.941 -15.931 10.872  1.00 35.35 ? 52   ASP   A N   1 
ATOM   432   C  CA  . ASP   A  1 52  ? 24.167 -17.174 10.823  1.00 37.21 ? 52   ASP   A CA  1 
ATOM   433   C  C   . ASP   A  1 52  ? 23.495 -17.390 9.469   1.00 36.12 ? 52   ASP   A C   1 
ATOM   434   O  O   . ASP   A  1 52  ? 23.248 -18.539 9.089   1.00 39.85 ? 52   ASP   A O   1 
ATOM   435   C  CB  . ASP   A  1 52  ? 23.108 -17.184 11.945  1.00 39.61 ? 52   ASP   A CB  1 
ATOM   436   C  CG  . ASP   A  1 52  ? 23.710 -17.291 13.341  1.00 45.62 ? 52   ASP   A CG  1 
ATOM   437   O  OD1 . ASP   A  1 52  ? 24.939 -17.475 13.504  1.00 45.33 ? 52   ASP   A OD1 1 
ATOM   438   O  OD2 . ASP   A  1 52  ? 22.927 -17.194 14.316  1.00 48.13 ? 52   ASP   A OD2 1 
ATOM   439   N  N   . GLN   A  1 53  ? 23.165 -16.326 8.736   1.00 32.42 ? 53   GLN   A N   1 
ATOM   440   C  CA  . GLN   A  1 53  ? 22.398 -16.446 7.492   1.00 33.05 ? 53   GLN   A CA  1 
ATOM   441   C  C   . GLN   A  1 53  ? 23.205 -16.016 6.273   1.00 33.41 ? 53   GLN   A C   1 
ATOM   442   O  O   . GLN   A  1 53  ? 22.650 -15.514 5.284   1.00 34.30 ? 53   GLN   A O   1 
ATOM   443   C  CB  . GLN   A  1 53  ? 21.103 -15.636 7.563   1.00 35.82 ? 53   GLN   A CB  1 
ATOM   444   C  CG  . GLN   A  1 53  ? 20.146 -16.110 8.643   1.00 38.94 ? 53   GLN   A CG  1 
ATOM   445   C  CD  . GLN   A  1 53  ? 18.763 -15.486 8.501   1.00 45.64 ? 53   GLN   A CD  1 
ATOM   446   O  OE1 . GLN   A  1 53  ? 18.588 -14.287 8.671   1.00 46.75 ? 53   GLN   A OE1 1 
ATOM   447   N  NE2 . GLN   A  1 53  ? 17.770 -16.315 8.182   1.00 51.09 ? 53   GLN   A NE2 1 
ATOM   448   N  N   . ALA   A  1 54  ? 24.509 -16.179 6.339   1.00 30.28 ? 54   ALA   A N   1 
ATOM   449   C  CA  . ALA   A  1 54  ? 25.352 -15.704 5.246   1.00 29.96 ? 54   ALA   A CA  1 
ATOM   450   C  C   . ALA   A  1 54  ? 25.200 -16.599 4.023   1.00 29.39 ? 54   ALA   A C   1 
ATOM   451   O  O   . ALA   A  1 54  ? 25.117 -17.823 4.154   1.00 29.02 ? 54   ALA   A O   1 
ATOM   452   C  CB  . ALA   A  1 54  ? 26.812 -15.667 5.696   1.00 31.35 ? 54   ALA   A CB  1 
ATOM   453   N  N   . THR   A  1 55  ? 25.148 -15.995 2.828   1.00 25.87 ? 55   THR   A N   1 
ATOM   454   C  CA  . THR   A  1 55  ? 24.937 -16.751 1.589   1.00 25.16 ? 55   THR   A CA  1 
ATOM   455   C  C   . THR   A  1 55  ? 26.159 -16.499 0.709   1.00 23.56 ? 55   THR   A C   1 
ATOM   456   O  O   . THR   A  1 55  ? 26.219 -15.486 0.015   1.00 23.62 ? 55   THR   A O   1 
ATOM   457   C  CB  . THR   A  1 55  ? 23.642 -16.327 0.856   1.00 28.36 ? 55   THR   A CB  1 
ATOM   458   O  OG1 . THR   A  1 55  ? 22.526 -16.526 1.717   1.00 30.49 ? 55   THR   A OG1 1 
ATOM   459   C  CG2 . THR   A  1 55  ? 23.429 -17.085 -0.473  1.00 27.68 ? 55   THR   A CG2 1 
ATOM   460   N  N   . SER   A  1 56  ? 27.128 -17.412 0.713   1.00 20.78 ? 56   SER   A N   1 
ATOM   461   C  CA  . SER   A  1 56  ? 28.228 -17.274 -0.233  1.00 19.74 ? 56   SER   A CA  1 
ATOM   462   C  C   . SER   A  1 56  ? 27.810 -17.687 -1.641  1.00 20.58 ? 56   SER   A C   1 
ATOM   463   O  O   . SER   A  1 56  ? 26.900 -18.519 -1.846  1.00 22.92 ? 56   SER   A O   1 
ATOM   464   C  CB  . SER   A  1 56  ? 29.444 -18.097 0.221   1.00 19.07 ? 56   SER   A CB  1 
ATOM   465   O  OG  . SER   A  1 56  ? 29.172 -19.505 0.100   1.00 21.83 ? 56   SER   A OG  1 
ATOM   466   N  N   . LEU   A  1 57  ? 28.454 -17.058 -2.637  1.00 20.19 ? 57   LEU   A N   1 
ATOM   467   C  CA  . LEU   A  1 57  ? 28.108 -17.305 -4.026  1.00 19.38 ? 57   LEU   A CA  1 
ATOM   468   C  C   . LEU   A  1 57  ? 29.264 -17.842 -4.853  1.00 20.88 ? 57   LEU   A C   1 
ATOM   469   O  O   . LEU   A  1 57  ? 29.056 -18.789 -5.633  1.00 20.72 ? 57   LEU   A O   1 
ATOM   470   C  CB  . LEU   A  1 57  ? 27.591 -16.009 -4.684  1.00 25.27 ? 57   LEU   A CB  1 
ATOM   471   C  CG  . LEU   A  1 57  ? 26.265 -15.530 -4.125  1.00 29.68 ? 57   LEU   A CG  1 
ATOM   472   C  CD1 . LEU   A  1 57  ? 25.989 -14.140 -4.754  1.00 30.87 ? 57   LEU   A CD1 1 
ATOM   473   C  CD2 . LEU   A  1 57  ? 25.148 -16.557 -4.383  1.00 30.52 ? 57   LEU   A CD2 1 
ATOM   474   N  N   . ARG   A  1 58  ? 30.424 -17.198 -4.812  1.00 18.46 ? 58   ARG   A N   1 
ATOM   475   C  CA  . ARG   A  1 58  ? 31.460 -17.504 -5.788  1.00 19.11 ? 58   ARG   A CA  1 
ATOM   476   C  C   . ARG   A  1 58  ? 32.813 -17.078 -5.241  1.00 19.04 ? 58   ARG   A C   1 
ATOM   477   O  O   . ARG   A  1 58  ? 32.918 -16.300 -4.265  1.00 19.48 ? 58   ARG   A O   1 
ATOM   478   C  CB  . ARG   A  1 58  ? 31.160 -16.869 -7.155  1.00 25.34 ? 58   ARG   A CB  1 
ATOM   479   C  CG  . ARG   A  1 58  ? 31.031 -15.423 -7.138  1.00 27.80 ? 58   ARG   A CG  1 
ATOM   480   C  CD  . ARG   A  1 58  ? 30.591 -14.912 -8.529  1.00 31.71 ? 58   ARG   A CD  1 
ATOM   481   N  NE  . ARG   A  1 58  ? 29.394 -15.614 -8.977  1.00 35.60 ? 58   ARG   A NE  1 
ATOM   482   C  CZ  . ARG   A  1 58  ? 28.141 -15.182 -8.808  1.00 37.39 ? 58   ARG   A CZ  1 
ATOM   483   N  NH1 . ARG   A  1 58  ? 27.150 -15.944 -9.256  1.00 35.09 ? 58   ARG   A NH1 1 
ATOM   484   N  NH2 . ARG   A  1 58  ? 27.874 -14.019 -8.176  1.00 33.00 ? 58   ARG   A NH2 1 
ATOM   485   N  N   . ILE   A  1 59  ? 33.856 -17.626 -5.845  1.00 17.12 ? 59   ILE   A N   1 
ATOM   486   C  CA  . ILE   A  1 59  ? 35.228 -17.295 -5.474  1.00 16.95 ? 59   ILE   A CA  1 
ATOM   487   C  C   . ILE   A  1 59  ? 35.972 -16.883 -6.741  1.00 17.59 ? 59   ILE   A C   1 
ATOM   488   O  O   . ILE   A  1 59  ? 35.821 -17.504 -7.794  1.00 19.32 ? 59   ILE   A O   1 
ATOM   489   C  CB  . ILE   A  1 59  ? 35.885 -18.488 -4.763  1.00 16.84 ? 59   ILE   A CB  1 
ATOM   490   C  CG1 . ILE   A  1 59  ? 37.253 -18.046 -4.186  1.00 18.32 ? 59   ILE   A CG1 1 
ATOM   491   C  CG2 . ILE   A  1 59  ? 35.954 -19.742 -5.711  1.00 18.13 ? 59   ILE   A CG2 1 
ATOM   492   C  CD1 . ILE   A  1 59  ? 37.938 -19.186 -3.381  1.00 20.21 ? 59   ILE   A CD1 1 
ATOM   493   N  N   . LEU   A  1 60  ? 36.736 -15.803 -6.662  1.00 18.24 ? 60   LEU   A N   1 
ATOM   494   C  CA  . LEU   A  1 60  ? 37.328 -15.177 -7.837  1.00 19.07 ? 60   LEU   A CA  1 
ATOM   495   C  C   . LEU   A  1 60  ? 38.794 -14.927 -7.589  1.00 17.66 ? 60   LEU   A C   1 
ATOM   496   O  O   . LEU   A  1 60  ? 39.154 -14.335 -6.561  1.00 18.14 ? 60   LEU   A O   1 
ATOM   497   C  CB  . LEU   A  1 60  ? 36.653 -13.831 -8.125  1.00 18.67 ? 60   LEU   A CB  1 
ATOM   498   C  CG  . LEU   A  1 60  ? 37.322 -12.931 -9.159  1.00 18.73 ? 60   LEU   A CG  1 
ATOM   499   C  CD1 . LEU   A  1 60  ? 37.164 -13.448 -10.615 1.00 18.72 ? 60   LEU   A CD1 1 
ATOM   500   C  CD2 . LEU   A  1 60  ? 36.683 -11.550 -9.097  1.00 20.98 ? 60   LEU   A CD2 1 
ATOM   501   N  N   . ASN   A  1 61  ? 39.648 -15.316 -8.522  1.00 17.01 ? 61   ASN   A N   1 
ATOM   502   C  CA  . ASN   A  1 61  ? 41.043 -14.862 -8.498  1.00 15.40 ? 61   ASN   A CA  1 
ATOM   503   C  C   . ASN   A  1 61  ? 41.076 -13.506 -9.221  1.00 15.69 ? 61   ASN   A C   1 
ATOM   504   O  O   . ASN   A  1 61  ? 40.814 -13.439 -10.440 1.00 16.53 ? 61   ASN   A O   1 
ATOM   505   C  CB  . ASN   A  1 61  ? 41.919 -15.902 -9.222  1.00 17.21 ? 61   ASN   A CB  1 
ATOM   506   C  CG  . ASN   A  1 61  ? 43.382 -15.484 -9.317  1.00 17.02 ? 61   ASN   A CG  1 
ATOM   507   O  OD1 . ASN   A  1 61  ? 43.708 -14.291 -9.261  1.00 17.42 ? 61   ASN   A OD1 1 
ATOM   508   N  ND2 . ASN   A  1 61  ? 44.289 -16.468 -9.382  1.00 18.64 ? 61   ASN   A ND2 1 
ATOM   509   N  N   . ASN   A  1 62  ? 41.300 -12.413 -8.497  1.00 15.98 ? 62   ASN   A N   1 
ATOM   510   C  CA  . ASN   A  1 62  ? 41.270 -11.078 -9.113  1.00 16.76 ? 62   ASN   A CA  1 
ATOM   511   C  C   . ASN   A  1 62  ? 42.652 -10.600 -9.533  1.00 14.23 ? 62   ASN   A C   1 
ATOM   512   O  O   . ASN   A  1 62  ? 42.821 -9.422  -9.863  1.00 17.03 ? 62   ASN   A O   1 
ATOM   513   C  CB  . ASN   A  1 62  ? 40.600 -10.025 -8.199  1.00 14.77 ? 62   ASN   A CB  1 
ATOM   514   C  CG  . ASN   A  1 62  ? 41.462 -9.650  -6.989  1.00 16.68 ? 62   ASN   A CG  1 
ATOM   515   O  OD1 . ASN   A  1 62  ? 42.483 -10.273 -6.739  1.00 15.42 ? 62   ASN   A OD1 1 
ATOM   516   N  ND2 . ASN   A  1 62  ? 41.013 -8.668  -6.216  1.00 15.50 ? 62   ASN   A ND2 1 
ATOM   517   N  N   . GLY   A  1 63  ? 43.610 -11.514 -9.584  1.00 15.46 ? 63   GLY   A N   1 
ATOM   518   C  CA  . GLY   A  1 63  ? 44.973 -11.163 -9.963  1.00 15.46 ? 63   GLY   A CA  1 
ATOM   519   C  C   . GLY   A  1 63  ? 45.779 -10.531 -8.849  1.00 16.73 ? 63   GLY   A C   1 
ATOM   520   O  O   . GLY   A  1 63  ? 46.930 -10.136 -9.098  1.00 18.95 ? 63   GLY   A O   1 
ATOM   521   N  N   . HIS   A  1 64  ? 45.204 -10.419 -7.645  1.00 16.32 ? 64   HIS   A N   1 
ATOM   522   C  CA  . HIS   A  1 64  ? 45.840 -9.818  -6.474  1.00 14.58 ? 64   HIS   A CA  1 
ATOM   523   C  C   . HIS   A  1 64  ? 45.737 -10.795 -5.323  1.00 17.26 ? 64   HIS   A C   1 
ATOM   524   O  O   . HIS   A  1 64  ? 46.716 -11.034 -4.599  1.00 18.34 ? 64   HIS   A O   1 
ATOM   525   C  CB  . HIS   A  1 64  ? 45.222 -8.472  -6.101  1.00 14.90 ? 64   HIS   A CB  1 
ATOM   526   C  CG  . HIS   A  1 64  ? 45.099 -7.504  -7.243  1.00 13.69 ? 64   HIS   A CG  1 
ATOM   527   N  ND1 . HIS   A  1 64  ? 46.193 -6.937  -7.885  1.00 14.65 ? 64   HIS   A ND1 1 
ATOM   528   C  CD2 . HIS   A  1 64  ? 43.999 -7.012  -7.862  1.00 15.53 ? 64   HIS   A CD2 1 
ATOM   529   C  CE1 . HIS   A  1 64  ? 45.749 -6.090  -8.821  1.00 17.16 ? 64   HIS   A CE1 1 
ATOM   530   N  NE2 . HIS   A  1 64  ? 44.422 -6.115  -8.816  1.00 15.90 ? 64   HIS   A NE2 1 
ATOM   531   N  N   . THR   A  1 65  ? 44.561 -11.369 -5.141  1.00 14.86 ? 65   THR   A N   1 
ATOM   532   C  CA  . THR   A  1 65  ? 44.231 -12.328 -4.101  1.00 14.18 ? 65   THR   A CA  1 
ATOM   533   C  C   . THR   A  1 65  ? 43.040 -13.148 -4.623  1.00 15.02 ? 65   THR   A C   1 
ATOM   534   O  O   . THR   A  1 65  ? 42.772 -13.157 -5.832  1.00 15.28 ? 65   THR   A O   1 
ATOM   535   C  CB  . THR   A  1 65  ? 43.931 -11.598 -2.792  1.00 15.53 ? 65   THR   A CB  1 
ATOM   536   O  OG1 . THR   A  1 65  ? 43.708 -12.607 -1.789  1.00 17.86 ? 65   THR   A OG1 1 
ATOM   537   C  CG2 . THR   A  1 65  ? 42.667 -10.719 -2.892  1.00 16.88 ? 65   THR   A CG2 1 
ATOM   538   N  N   . PHE   A  1 66  ? 42.370 -13.923 -3.752  1.00 15.36 ? 66   PHE   A N   1 
ATOM   539   C  CA  . PHE   A  1 66  ? 41.090 -14.507 -4.126  1.00 14.43 ? 66   PHE   A CA  1 
ATOM   540   C  C   . PHE   A  1 66  ? 40.027 -13.946 -3.189  1.00 15.81 ? 66   PHE   A C   1 
ATOM   541   O  O   . PHE   A  1 66  ? 40.268 -13.771 -1.997  1.00 16.32 ? 66   PHE   A O   1 
ATOM   542   C  CB  . PHE   A  1 66  ? 41.091 -16.085 -4.132  1.00 17.69 ? 66   PHE   A CB  1 
ATOM   543   C  CG  . PHE   A  1 66  ? 41.385 -16.714 -2.788  1.00 16.54 ? 66   PHE   A CG  1 
ATOM   544   C  CD1 . PHE   A  1 66  ? 40.343 -16.981 -1.911  1.00 19.07 ? 66   PHE   A CD1 1 
ATOM   545   C  CD2 . PHE   A  1 66  ? 42.691 -17.040 -2.406  1.00 17.68 ? 66   PHE   A CD2 1 
ATOM   546   C  CE1 . PHE   A  1 66  ? 40.605 -17.542 -0.672  1.00 19.55 ? 66   PHE   A CE1 1 
ATOM   547   C  CE2 . PHE   A  1 66  ? 42.963 -17.579 -1.152  1.00 19.61 ? 66   PHE   A CE2 1 
ATOM   548   C  CZ  . PHE   A  1 66  ? 41.897 -17.873 -0.313  1.00 19.13 ? 66   PHE   A CZ  1 
ATOM   549   N  N   . ASN   A  1 67  ? 38.878 -13.586 -3.766  1.00 16.45 ? 67   ASN   A N   1 
ATOM   550   C  CA  . ASN   A  1 67  ? 37.750 -13.024 -3.027  1.00 16.23 ? 67   ASN   A CA  1 
ATOM   551   C  C   . ASN   A  1 67  ? 36.627 -14.043 -3.018  1.00 18.25 ? 67   ASN   A C   1 
ATOM   552   O  O   . ASN   A  1 67  ? 36.233 -14.534 -4.097  1.00 18.22 ? 67   ASN   A O   1 
ATOM   553   C  CB  . ASN   A  1 67  ? 37.202 -11.759 -3.691  1.00 16.94 ? 67   ASN   A CB  1 
ATOM   554   C  CG  . ASN   A  1 67  ? 38.169 -10.628 -3.720  1.00 18.22 ? 67   ASN   A CG  1 
ATOM   555   O  OD1 . ASN   A  1 67  ? 39.155 -10.599 -2.935  1.00 17.16 ? 67   ASN   A OD1 1 
ATOM   556   N  ND2 . ASN   A  1 67  ? 37.937 -9.664  -4.619  1.00 19.24 ? 67   ASN   A ND2 1 
ATOM   557   N  N   . VAL   A  1 68  ? 36.052 -14.308 -1.841  1.00 17.05 ? 68   VAL   A N   1 
ATOM   558   C  CA  . VAL   A  1 68  ? 34.824 -15.081 -1.738  1.00 17.92 ? 68   VAL   A CA  1 
ATOM   559   C  C   . VAL   A  1 68  ? 33.697 -14.086 -1.568  1.00 19.73 ? 68   VAL   A C   1 
ATOM   560   O  O   . VAL   A  1 68  ? 33.680 -13.334 -0.577  1.00 18.69 ? 68   VAL   A O   1 
ATOM   561   C  CB  . VAL   A  1 68  ? 34.889 -16.060 -0.560  1.00 18.70 ? 68   VAL   A CB  1 
ATOM   562   C  CG1 . VAL   A  1 68  ? 33.497 -16.661 -0.284  1.00 20.25 ? 68   VAL   A CG1 1 
ATOM   563   C  CG2 . VAL   A  1 68  ? 35.964 -17.160 -0.800  1.00 18.55 ? 68   VAL   A CG2 1 
ATOM   564   N  N   . GLU   A  1 69  ? 32.755 -14.062 -2.516  1.00 18.81 ? 69   GLU   A N   1 
ATOM   565   C  CA  . GLU   A  1 69  ? 31.720 -13.047 -2.597  1.00 19.68 ? 69   GLU   A CA  1 
ATOM   566   C  C   . GLU   A  1 69  ? 30.436 -13.593 -1.976  1.00 19.61 ? 69   GLU   A C   1 
ATOM   567   O  O   . GLU   A  1 69  ? 30.113 -14.790 -2.140  1.00 22.37 ? 69   GLU   A O   1 
ATOM   568   C  CB  . GLU   A  1 69  ? 31.466 -12.669 -4.066  1.00 26.29 ? 69   GLU   A CB  1 
ATOM   569   C  CG  . GLU   A  1 69  ? 30.461 -11.557 -4.304  1.00 39.83 ? 69   GLU   A CG  1 
ATOM   570   C  CD  . GLU   A  1 69  ? 29.863 -11.574 -5.746  1.00 49.15 ? 69   GLU   A CD  1 
ATOM   571   O  OE1 . GLU   A  1 69  ? 28.915 -10.791 -6.013  1.00 52.28 ? 69   GLU   A OE1 1 
ATOM   572   O  OE2 . GLU   A  1 69  ? 30.303 -12.393 -6.594  1.00 50.42 ? 69   GLU   A OE2 1 
ATOM   573   N  N   . PHE   A  1 70  ? 29.699 -12.726 -1.286  1.00 18.98 ? 70   PHE   A N   1 
ATOM   574   C  CA  . PHE   A  1 70  ? 28.415 -13.034 -0.656  1.00 19.70 ? 70   PHE   A CA  1 
ATOM   575   C  C   . PHE   A  1 70  ? 27.264 -12.238 -1.254  1.00 24.46 ? 70   PHE   A C   1 
ATOM   576   O  O   . PHE   A  1 70  ? 27.448 -11.166 -1.809  1.00 22.78 ? 70   PHE   A O   1 
ATOM   577   C  CB  . PHE   A  1 70  ? 28.473 -12.743 0.845   1.00 20.23 ? 70   PHE   A CB  1 
ATOM   578   C  CG  . PHE   A  1 70  ? 29.361 -13.694 1.576   1.00 20.73 ? 70   PHE   A CG  1 
ATOM   579   C  CD1 . PHE   A  1 70  ? 30.758 -13.576 1.499   1.00 21.06 ? 70   PHE   A CD1 1 
ATOM   580   C  CD2 . PHE   A  1 70  ? 28.823 -14.732 2.298   1.00 21.09 ? 70   PHE   A CD2 1 
ATOM   581   C  CE1 . PHE   A  1 70  ? 31.559 -14.501 2.169   1.00 19.92 ? 70   PHE   A CE1 1 
ATOM   582   C  CE2 . PHE   A  1 70  ? 29.608 -15.650 2.965   1.00 21.75 ? 70   PHE   A CE2 1 
ATOM   583   C  CZ  . PHE   A  1 70  ? 30.997 -15.529 2.874   1.00 21.87 ? 70   PHE   A CZ  1 
ATOM   584   N  N   . ASP   A  1 71  ? 26.050 -12.779 -1.119  1.00 23.73 ? 71   ASP   A N   1 
ATOM   585   C  CA  . ASP   A  1 71  ? 24.865 -12.006 -1.458  1.00 22.93 ? 71   ASP   A CA  1 
ATOM   586   C  C   . ASP   A  1 71  ? 24.693 -10.932 -0.387  1.00 23.56 ? 71   ASP   A C   1 
ATOM   587   O  O   . ASP   A  1 71  ? 24.487 -11.256 0.779   1.00 26.99 ? 71   ASP   A O   1 
ATOM   588   C  CB  . ASP   A  1 71  ? 23.665 -12.946 -1.513  1.00 25.19 ? 71   ASP   A CB  1 
ATOM   589   C  CG  . ASP   A  1 71  ? 22.391 -12.239 -1.960  1.00 25.71 ? 71   ASP   A CG  1 
ATOM   590   O  OD1 . ASP   A  1 71  ? 22.197 -11.085 -1.571  1.00 26.11 ? 71   ASP   A OD1 1 
ATOM   591   O  OD2 . ASP   A  1 71  ? 21.551 -12.860 -2.677  1.00 29.03 ? 71   ASP   A OD2 1 
ATOM   592   N  N   . ASP   A  1 72  ? 24.885 -9.654  -0.734  1.00 21.46 ? 72   ASP   A N   1 
ATOM   593   C  CA  . ASP   A  1 72  ? 24.747 -8.569  0.231   1.00 19.34 ? 72   ASP   A CA  1 
ATOM   594   C  C   . ASP   A  1 72  ? 23.486 -7.745  0.001   1.00 22.71 ? 72   ASP   A C   1 
ATOM   595   O  O   . ASP   A  1 72  ? 23.472 -6.533  0.281   1.00 22.39 ? 72   ASP   A O   1 
ATOM   596   C  CB  . ASP   A  1 72  ? 25.981 -7.662  0.167   1.00 19.73 ? 72   ASP   A CB  1 
ATOM   597   C  CG  . ASP   A  1 72  ? 26.134 -6.988  -1.220  1.00 21.30 ? 72   ASP   A CG  1 
ATOM   598   O  OD1 . ASP   A  1 72  ? 25.420 -7.339  -2.204  1.00 24.22 ? 72   ASP   A OD1 1 
ATOM   599   O  OD2 . ASP   A  1 72  ? 27.004 -6.083  -1.329  1.00 21.89 ? 72   ASP   A OD2 1 
ATOM   600   N  N   . SER   A  1 73  ? 22.406 -8.385  -0.458  1.00 22.70 ? 73   SER   A N   1 
ATOM   601   C  CA  . SER   A  1 73  ? 21.187 -7.650  -0.755  1.00 22.58 ? 73   SER   A CA  1 
ATOM   602   C  C   . SER   A  1 73  ? 20.305 -7.438  0.465   1.00 27.21 ? 73   SER   A C   1 
ATOM   603   O  O   . SER   A  1 73  ? 19.296 -6.718  0.364   1.00 28.42 ? 73   SER   A O   1 
ATOM   604   C  CB  . SER   A  1 73  ? 20.395 -8.389  -1.843  1.00 25.75 ? 73   SER   A CB  1 
ATOM   605   O  OG  . SER   A  1 73  ? 19.884 -9.630  -1.360  1.00 26.60 ? 73   SER   A OG  1 
ATOM   606   N  N   . GLN   A  1 74  ? 20.609 -8.096  1.585   1.00 24.23 ? 74   GLN   A N   1 
ATOM   607   C  CA  . GLN   A  1 74  ? 19.765 -8.025  2.770   1.00 25.26 ? 74   GLN   A CA  1 
ATOM   608   C  C   . GLN   A  1 74  ? 20.625 -7.884  4.010   1.00 24.31 ? 74   GLN   A C   1 
ATOM   609   O  O   . GLN   A  1 74  ? 21.801 -8.266  4.034   1.00 26.30 ? 74   GLN   A O   1 
ATOM   610   C  CB  . GLN   A  1 74  ? 18.876 -9.253  2.927   1.00 27.79 ? 74   GLN   A CB  1 
ATOM   611   C  CG  . GLN   A  1 74  ? 17.926 -9.386  1.784   1.00 26.42 ? 74   GLN   A CG  1 
ATOM   612   C  CD  . GLN   A  1 74  ? 16.991 -10.586 1.949   1.00 30.40 ? 74   GLN   A CD  1 
ATOM   613   O  OE1 . GLN   A  1 74  ? 17.453 -11.720 2.166   1.00 32.71 ? 74   GLN   A OE1 1 
ATOM   614   N  NE2 . GLN   A  1 74  ? 15.669 -10.341 1.870   1.00 33.89 ? 74   GLN   A NE2 1 
ATOM   615   N  N   . ASP   A  1 75  ? 19.979 -7.357  5.061   1.00 28.72 ? 75   ASP   A N   1 
ATOM   616   C  CA  . ASP   A  1 75  ? 20.616 -7.122  6.359   1.00 31.09 ? 75   ASP   A CA  1 
ATOM   617   C  C   . ASP   A  1 75  ? 20.715 -8.440  7.128   1.00 34.46 ? 75   ASP   A C   1 
ATOM   618   O  O   . ASP   A  1 75  ? 20.161 -8.605  8.213   1.00 39.11 ? 75   ASP   A O   1 
ATOM   619   C  CB  . ASP   A  1 75  ? 19.829 -6.103  7.180   1.00 33.28 ? 75   ASP   A CB  1 
ATOM   620   C  CG  . ASP   A  1 75  ? 20.052 -4.669  6.762   1.00 35.73 ? 75   ASP   A CG  1 
ATOM   621   O  OD1 . ASP   A  1 75  ? 20.916 -4.404  5.925   1.00 32.99 ? 75   ASP   A OD1 1 
ATOM   622   O  OD2 . ASP   A  1 75  ? 19.390 -3.767  7.344   1.00 39.48 ? 75   ASP   A OD2 1 
ATOM   623   N  N   . LYS   A  1 76  ? 21.361 -9.417  6.516   1.00 31.53 ? 76   LYS   A N   1 
ATOM   624   C  CA  . LYS   A  1 76  ? 21.475 -10.720 7.153   1.00 31.38 ? 76   LYS   A CA  1 
ATOM   625   C  C   . LYS   A  1 76  ? 22.885 -10.888 7.701   1.00 32.74 ? 76   LYS   A C   1 
ATOM   626   O  O   . LYS   A  1 76  ? 23.077 -10.768 8.920   1.00 34.83 ? 76   LYS   A O   1 
ATOM   627   C  CB  . LYS   A  1 76  ? 21.065 -11.834 6.183   1.00 32.58 ? 76   LYS   A CB  1 
ATOM   628   C  CG  . LYS   A  1 76  ? 19.513 -11.863 5.984   1.00 35.77 ? 76   LYS   A CG  1 
ATOM   629   C  CD  . LYS   A  1 76  ? 19.012 -13.005 5.045   1.00 37.16 ? 76   LYS   A CD  1 
ATOM   630   C  CE  . LYS   A  1 76  ? 17.483 -13.112 5.120   1.00 38.65 ? 76   LYS   A CE  1 
ATOM   631   N  NZ  . LYS   A  1 76  ? 16.916 -13.920 4.012   1.00 39.54 ? 76   LYS   A NZ  1 
ATOM   632   N  N   . ALA   A  1 77  ? 23.889 -11.074 6.831   1.00 27.27 ? 77   ALA   A N   1 
ATOM   633   C  CA  . ALA   A  1 77  ? 25.260 -11.214 7.308   1.00 24.82 ? 77   ALA   A CA  1 
ATOM   634   C  C   . ALA   A  1 77  ? 25.789 -9.807  7.557   1.00 25.91 ? 77   ALA   A C   1 
ATOM   635   O  O   . ALA   A  1 77  ? 26.145 -9.091  6.610   1.00 24.46 ? 77   ALA   A O   1 
ATOM   636   C  CB  . ALA   A  1 77  ? 26.120 -11.965 6.302   1.00 27.92 ? 77   ALA   A CB  1 
ATOM   637   N  N   . VAL   A  1 78  ? 25.838 -9.395  8.827   1.00 25.56 ? 78   VAL   A N   1 
ATOM   638   C  CA  . VAL   A  1 78  ? 26.164 -8.013  9.152   1.00 25.83 ? 78   VAL   A CA  1 
ATOM   639   C  C   . VAL   A  1 78  ? 27.101 -7.944  10.334  1.00 26.01 ? 78   VAL   A C   1 
ATOM   640   O  O   . VAL   A  1 78  ? 27.168 -8.848  11.166  1.00 28.30 ? 78   VAL   A O   1 
ATOM   641   C  CB  . VAL   A  1 78  ? 24.923 -7.160  9.486   1.00 25.26 ? 78   VAL   A CB  1 
ATOM   642   C  CG1 . VAL   A  1 78  ? 23.958 -7.156  8.287   1.00 26.33 ? 78   VAL   A CG1 1 
ATOM   643   C  CG2 . VAL   A  1 78  ? 24.231 -7.662  10.707  1.00 28.83 ? 78   VAL   A CG2 1 
ATOM   644   N  N   . LEU   A  1 79  ? 27.764 -6.791  10.419  1.00 24.73 ? 79   LEU   A N   1 
ATOM   645   C  CA  . LEU   A  1 79  ? 28.547 -6.392  11.567  1.00 23.74 ? 79   LEU   A CA  1 
ATOM   646   C  C   . LEU   A  1 79  ? 27.900 -5.138  12.144  1.00 26.61 ? 79   LEU   A C   1 
ATOM   647   O  O   . LEU   A  1 79  ? 27.562 -4.220  11.380  1.00 29.64 ? 79   LEU   A O   1 
ATOM   648   C  CB  . LEU   A  1 79  ? 29.971 -6.145  11.071  1.00 25.64 ? 79   LEU   A CB  1 
ATOM   649   C  CG  . LEU   A  1 79  ? 31.095 -5.884  12.004  1.00 30.32 ? 79   LEU   A CG  1 
ATOM   650   C  CD1 . LEU   A  1 79  ? 31.235 -7.128  12.854  1.00 33.11 ? 79   LEU   A CD1 1 
ATOM   651   C  CD2 . LEU   A  1 79  ? 32.290 -5.670  11.125  1.00 23.89 ? 79   LEU   A CD2 1 
ATOM   652   N  N   . LYS   A  1 80  ? 27.720 -5.090  13.474  1.00 26.51 ? 80   LYS   A N   1 
ATOM   653   C  CA  . LYS   A  1 80  ? 27.131 -3.946  14.170  1.00 28.66 ? 80   LYS   A CA  1 
ATOM   654   C  C   . LYS   A  1 80  ? 27.838 -3.780  15.514  1.00 29.00 ? 80   LYS   A C   1 
ATOM   655   O  O   . LYS   A  1 80  ? 28.592 -4.655  15.944  1.00 30.04 ? 80   LYS   A O   1 
ATOM   656   C  CB  . LYS   A  1 80  ? 25.616 -4.069  14.408  1.00 35.40 ? 80   LYS   A CB  1 
ATOM   657   C  CG  . LYS   A  1 80  ? 24.796 -4.151  13.115  1.00 38.24 ? 80   LYS   A CG  1 
ATOM   658   C  CD  . LYS   A  1 80  ? 23.305 -3.951  13.389  1.00 40.63 ? 80   LYS   A CD  1 
ATOM   659   C  CE  . LYS   A  1 80  ? 22.782 -4.906  14.400  1.00 48.62 ? 80   LYS   A CE  1 
ATOM   660   N  NZ  . LYS   A  1 80  ? 23.336 -6.252  14.129  1.00 51.63 ? 80   LYS   A NZ  1 
ATOM   661   N  N   . GLY   A  1 81  ? 27.610 -2.616  16.168  1.00 27.71 ? 81   GLY   A N   1 
ATOM   662   C  CA  . GLY   A  1 81  ? 28.189 -2.363  17.480  1.00 28.60 ? 81   GLY   A CA  1 
ATOM   663   C  C   . GLY   A  1 81  ? 29.676 -2.043  17.372  1.00 27.51 ? 81   GLY   A C   1 
ATOM   664   O  O   . GLY   A  1 81  ? 30.192 -1.602  16.341  1.00 26.41 ? 81   GLY   A O   1 
ATOM   665   N  N   . GLY   A  1 82  ? 30.366 -2.255  18.487  1.00 29.38 ? 82   GLY   A N   1 
ATOM   666   C  CA  . GLY   A  1 82  ? 31.751 -1.859  18.588  1.00 28.24 ? 82   GLY   A CA  1 
ATOM   667   C  C   . GLY   A  1 82  ? 31.909 -0.377  18.302  1.00 27.13 ? 82   GLY   A C   1 
ATOM   668   O  O   . GLY   A  1 82  ? 31.229 0.458   18.893  1.00 30.12 ? 82   GLY   A O   1 
ATOM   669   N  N   . PRO   A  1 83  ? 32.826 -0.027  17.385  1.00 25.77 ? 83   PRO   A N   1 
ATOM   670   C  CA  . PRO   A  1 83  ? 32.990 1.376   16.985  1.00 25.32 ? 83   PRO   A CA  1 
ATOM   671   C  C   . PRO   A  1 83  ? 31.995 1.852   15.943  1.00 29.32 ? 83   PRO   A C   1 
ATOM   672   O  O   . PRO   A  1 83  ? 32.076 3.027   15.553  1.00 31.82 ? 83   PRO   A O   1 
ATOM   673   C  CB  . PRO   A  1 83  ? 34.411 1.389   16.378  1.00 22.09 ? 83   PRO   A CB  1 
ATOM   674   C  CG  . PRO   A  1 83  ? 34.477 0.030   15.670  1.00 22.79 ? 83   PRO   A CG  1 
ATOM   675   C  CD  . PRO   A  1 83  ? 33.744 -0.919  16.660  1.00 24.92 ? 83   PRO   A CD  1 
ATOM   676   N  N   . LEU   A  1 84  ? 31.101 0.971   15.453  1.00 25.37 ? 84   LEU   A N   1 
ATOM   677   C  CA  . LEU   A  1 84  ? 30.293 1.258   14.277  1.00 24.56 ? 84   LEU   A CA  1 
ATOM   678   C  C   . LEU   A  1 84  ? 28.983 1.912   14.671  1.00 24.78 ? 84   LEU   A C   1 
ATOM   679   O  O   . LEU   A  1 84  ? 28.321 1.490   15.633  1.00 26.89 ? 84   LEU   A O   1 
ATOM   680   C  CB  . LEU   A  1 84  ? 29.983 -0.029  13.517  1.00 22.65 ? 84   LEU   A CB  1 
ATOM   681   C  CG  . LEU   A  1 84  ? 31.257 -0.825  13.194  1.00 23.07 ? 84   LEU   A CG  1 
ATOM   682   C  CD1 . LEU   A  1 84  ? 30.867 -2.191  12.570  1.00 26.15 ? 84   LEU   A CD1 1 
ATOM   683   C  CD2 . LEU   A  1 84  ? 32.170 -0.034  12.198  1.00 21.53 ? 84   LEU   A CD2 1 
ATOM   684   N  N   . ASP   A  1 85  ? 28.579 2.891   13.875  1.00 27.50 ? 85   ASP   A N   1 
ATOM   685   C  CA  . ASP   A  1 85  ? 27.213 3.394   13.884  1.00 29.25 ? 85   ASP   A CA  1 
ATOM   686   C  C   . ASP   A  1 85  ? 26.465 2.753   12.731  1.00 27.79 ? 85   ASP   A C   1 
ATOM   687   O  O   . ASP   A  1 85  ? 26.940 2.798   11.588  1.00 28.35 ? 85   ASP   A O   1 
ATOM   688   C  CB  . ASP   A  1 85  ? 27.202 4.909   13.747  1.00 31.60 ? 85   ASP   A CB  1 
ATOM   689   C  CG  . ASP   A  1 85  ? 27.853 5.576   14.932  1.00 39.96 ? 85   ASP   A CG  1 
ATOM   690   O  OD1 . ASP   A  1 85  ? 27.491 5.212   16.081  1.00 42.08 ? 85   ASP   A OD1 1 
ATOM   691   O  OD2 . ASP   A  1 85  ? 28.756 6.422   14.727  1.00 43.01 ? 85   ASP   A OD2 1 
ATOM   692   N  N   . GLY   A  1 86  ? 25.313 2.146   13.021  1.00 30.74 ? 86   GLY   A N   1 
ATOM   693   C  CA  . GLY   A  1 86  ? 24.525 1.545   11.952  1.00 31.12 ? 86   GLY   A CA  1 
ATOM   694   C  C   . GLY   A  1 86  ? 24.921 0.105   11.654  1.00 31.35 ? 86   GLY   A C   1 
ATOM   695   O  O   . GLY   A  1 86  ? 25.530 -0.607  12.464  1.00 31.47 ? 86   GLY   A O   1 
ATOM   696   N  N   . THR   A  1 87  ? 24.581 -0.319  10.437  1.00 25.99 ? 87   THR   A N   1 
ATOM   697   C  CA  . THR   A  1 87  ? 24.668 -1.721  10.058  1.00 25.31 ? 87   THR   A CA  1 
ATOM   698   C  C   . THR   A  1 87  ? 25.597 -1.854  8.871   1.00 25.42 ? 87   THR   A C   1 
ATOM   699   O  O   . THR   A  1 87  ? 25.447 -1.116  7.883   1.00 26.40 ? 87   THR   A O   1 
ATOM   700   C  CB  . THR   A  1 87  ? 23.289 -2.259  9.700   1.00 27.00 ? 87   THR   A CB  1 
ATOM   701   O  OG1 . THR   A  1 87  ? 22.442 -2.232  10.867  1.00 28.82 ? 87   THR   A OG1 1 
ATOM   702   C  CG2 . THR   A  1 87  ? 23.377 -3.694  9.115   1.00 27.43 ? 87   THR   A CG2 1 
ATOM   703   N  N   . TYR   A  1 88  ? 26.540 -2.809  8.932   1.00 23.89 ? 88   TYR   A N   1 
ATOM   704   C  CA  . TYR   A  1 88  ? 27.492 -3.020  7.825   1.00 21.51 ? 88   TYR   A CA  1 
ATOM   705   C  C   . TYR   A  1 88  ? 27.341 -4.434  7.264   1.00 22.23 ? 88   TYR   A C   1 
ATOM   706   O  O   . TYR   A  1 88  ? 27.546 -5.414  7.986   1.00 22.53 ? 88   TYR   A O   1 
ATOM   707   C  CB  . TYR   A  1 88  ? 28.923 -2.797  8.313   1.00 20.71 ? 88   TYR   A CB  1 
ATOM   708   C  CG  . TYR   A  1 88  ? 29.281 -1.349  8.580   1.00 18.06 ? 88   TYR   A CG  1 
ATOM   709   C  CD1 . TYR   A  1 88  ? 28.720 -0.658  9.665   1.00 20.45 ? 88   TYR   A CD1 1 
ATOM   710   C  CD2 . TYR   A  1 88  ? 30.235 -0.694  7.765   1.00 18.17 ? 88   TYR   A CD2 1 
ATOM   711   C  CE1 . TYR   A  1 88  ? 29.077 0.685   9.947   1.00 21.06 ? 88   TYR   A CE1 1 
ATOM   712   C  CE2 . TYR   A  1 88  ? 30.571 0.625   8.014   1.00 17.92 ? 88   TYR   A CE2 1 
ATOM   713   C  CZ  . TYR   A  1 88  ? 30.008 1.325   9.110   1.00 20.34 ? 88   TYR   A CZ  1 
ATOM   714   O  OH  . TYR   A  1 88  ? 30.384 2.660   9.397   1.00 22.66 ? 88   TYR   A OH  1 
ATOM   715   N  N   . ARG   A  1 89  ? 27.032 -4.538  5.965   1.00 21.48 ? 89   ARG   A N   1 
ATOM   716   C  CA  . ARG   A  1 89  ? 26.774 -5.833  5.322   1.00 20.91 ? 89   ARG   A CA  1 
ATOM   717   C  C   . ARG   A  1 89  ? 28.065 -6.463  4.821   1.00 19.90 ? 89   ARG   A C   1 
ATOM   718   O  O   . ARG   A  1 89  ? 28.861 -5.801  4.152   1.00 19.32 ? 89   ARG   A O   1 
ATOM   719   C  CB  . ARG   A  1 89  ? 25.825 -5.681  4.139   1.00 20.93 ? 89   ARG   A CB  1 
ATOM   720   C  CG  . ARG   A  1 89  ? 24.372 -5.409  4.519   1.00 24.01 ? 89   ARG   A CG  1 
ATOM   721   C  CD  . ARG   A  1 89  ? 23.521 -5.448  3.248   1.00 22.40 ? 89   ARG   A CD  1 
ATOM   722   N  NE  . ARG   A  1 89  ? 22.195 -4.865  3.505   1.00 24.69 ? 89   ARG   A NE  1 
ATOM   723   C  CZ  . ARG   A  1 89  ? 21.358 -4.452  2.563   1.00 23.48 ? 89   ARG   A CZ  1 
ATOM   724   N  NH1 . ARG   A  1 89  ? 21.652 -4.569  1.282   1.00 24.60 ? 89   ARG   A NH1 1 
ATOM   725   N  NH2 . ARG   A  1 89  ? 20.208 -3.893  2.927   1.00 28.30 ? 89   ARG   A NH2 1 
ATOM   726   N  N   . LEU   A  1 90  ? 28.259 -7.751  5.124   1.00 20.18 ? 90   LEU   A N   1 
ATOM   727   C  CA  . LEU   A  1 90  ? 29.367 -8.532  4.554   1.00 18.59 ? 90   LEU   A CA  1 
ATOM   728   C  C   . LEU   A  1 90  ? 29.216 -8.641  3.031   1.00 18.61 ? 90   LEU   A C   1 
ATOM   729   O  O   . LEU   A  1 90  ? 28.165 -9.106  2.549   1.00 20.49 ? 90   LEU   A O   1 
ATOM   730   C  CB  . LEU   A  1 90  ? 29.335 -9.948  5.163   1.00 20.90 ? 90   LEU   A CB  1 
ATOM   731   C  CG  . LEU   A  1 90  ? 30.396 -10.897 4.579   1.00 21.05 ? 90   LEU   A CG  1 
ATOM   732   C  CD1 . LEU   A  1 90  ? 31.792 -10.406 4.943   1.00 21.10 ? 90   LEU   A CD1 1 
ATOM   733   C  CD2 . LEU   A  1 90  ? 30.157 -12.328 5.100   1.00 23.34 ? 90   LEU   A CD2 1 
ATOM   734   N  N   . ILE   A  1 91  ? 30.248 -8.220  2.276   1.00 17.81 ? 91   ILE   A N   1 
ATOM   735   C  CA  . ILE   A  1 91  ? 30.238 -8.401  0.830   1.00 18.25 ? 91   ILE   A CA  1 
ATOM   736   C  C   . ILE   A  1 91  ? 31.220 -9.479  0.374   1.00 17.92 ? 91   ILE   A C   1 
ATOM   737   O  O   . ILE   A  1 91  ? 30.927 -10.224 -0.564  1.00 17.96 ? 91   ILE   A O   1 
ATOM   738   C  CB  . ILE   A  1 91  ? 30.459 -7.068  0.070   1.00 17.83 ? 91   ILE   A CB  1 
ATOM   739   C  CG1 . ILE   A  1 91  ? 30.473 -7.349  -1.442  1.00 19.66 ? 91   ILE   A CG1 1 
ATOM   740   C  CG2 . ILE   A  1 91  ? 31.770 -6.336  0.441   1.00 19.34 ? 91   ILE   A CG2 1 
ATOM   741   C  CD1 . ILE   A  1 91  ? 30.308 -6.064  -2.231  1.00 20.05 ? 91   ILE   A CD1 1 
ATOM   742   N  N   . GLN   A  1 92  ? 32.381 -9.596  1.004   1.00 17.45 ? 92   GLN   A N   1 
ATOM   743   C  CA  . GLN   A  1 92  ? 33.385 -10.566 0.563   1.00 17.36 ? 92   GLN   A CA  1 
ATOM   744   C  C   . GLN   A  1 92  ? 34.423 -10.749 1.668   1.00 17.33 ? 92   GLN   A C   1 
ATOM   745   O  O   . GLN   A  1 92  ? 34.554 -9.906  2.570   1.00 17.34 ? 92   GLN   A O   1 
ATOM   746   C  CB  . GLN   A  1 92  ? 34.097 -10.144 -0.743  1.00 16.19 ? 92   GLN   A CB  1 
ATOM   747   C  CG  . GLN   A  1 92  ? 34.796 -8.754  -0.661  1.00 16.45 ? 92   GLN   A CG  1 
ATOM   748   C  CD  . GLN   A  1 92  ? 36.295 -8.871  -0.697  1.00 17.46 ? 92   GLN   A CD  1 
ATOM   749   O  OE1 . GLN   A  1 92  ? 36.886 -9.629  0.060   1.00 17.82 ? 92   GLN   A OE1 1 
ATOM   750   N  NE2 . GLN   A  1 92  ? 36.932 -8.082  -1.574  1.00 20.66 ? 92   GLN   A NE2 1 
ATOM   751   N  N   . PHE   A  1 93  ? 35.148 -11.873 1.595   1.00 17.20 ? 93   PHE   A N   1 
ATOM   752   C  CA  . PHE   A  1 93  ? 36.412 -11.955 2.332   1.00 16.94 ? 93   PHE   A CA  1 
ATOM   753   C  C   . PHE   A  1 93  ? 37.536 -12.402 1.410   1.00 17.11 ? 93   PHE   A C   1 
ATOM   754   O  O   . PHE   A  1 93  ? 37.317 -13.009 0.375   1.00 16.82 ? 93   PHE   A O   1 
ATOM   755   C  CB  . PHE   A  1 93  ? 36.319 -12.887 3.574   1.00 18.76 ? 93   PHE   A CB  1 
ATOM   756   C  CG  . PHE   A  1 93  ? 36.174 -14.350 3.279   1.00 17.74 ? 93   PHE   A CG  1 
ATOM   757   C  CD1 . PHE   A  1 93  ? 37.275 -15.155 2.893   1.00 18.41 ? 93   PHE   A CD1 1 
ATOM   758   C  CD2 . PHE   A  1 93  ? 34.927 -14.944 3.462   1.00 19.08 ? 93   PHE   A CD2 1 
ATOM   759   C  CE1 . PHE   A  1 93  ? 37.095 -16.503 2.656   1.00 19.06 ? 93   PHE   A CE1 1 
ATOM   760   C  CE2 . PHE   A  1 93  ? 34.746 -16.300 3.221   1.00 19.23 ? 93   PHE   A CE2 1 
ATOM   761   C  CZ  . PHE   A  1 93  ? 35.826 -17.087 2.823   1.00 20.29 ? 93   PHE   A CZ  1 
ATOM   762   N  N   . HIS   A  1 94  ? 38.766 -12.127 1.835   1.00 15.77 ? 94   HIS   A N   1 
ATOM   763   C  CA  . HIS   A  1 94  ? 39.966 -12.523 1.106   1.00 16.49 ? 94   HIS   A CA  1 
ATOM   764   C  C   . HIS   A  1 94  ? 41.096 -12.574 2.128   1.00 16.76 ? 94   HIS   A C   1 
ATOM   765   O  O   . HIS   A  1 94  ? 40.917 -12.184 3.277   1.00 16.57 ? 94   HIS   A O   1 
ATOM   766   C  CB  . HIS   A  1 94  ? 40.320 -11.499 0.005   1.00 15.30 ? 94   HIS   A CB  1 
ATOM   767   C  CG  . HIS   A  1 94  ? 40.559 -10.126 0.583   1.00 13.50 ? 94   HIS   A CG  1 
ATOM   768   N  ND1 . HIS   A  1 94  ? 39.546 -9.221  0.831   1.00 15.27 ? 94   HIS   A ND1 1 
ATOM   769   C  CD2 . HIS   A  1 94  ? 41.701 -9.554  1.023   1.00 14.92 ? 94   HIS   A CD2 1 
ATOM   770   C  CE1 . HIS   A  1 94  ? 40.054 -8.122  1.376   1.00 15.27 ? 94   HIS   A CE1 1 
ATOM   771   N  NE2 . HIS   A  1 94  ? 41.358 -8.308  1.538   1.00 13.35 ? 94   HIS   A NE2 1 
ATOM   772   N  N   . PHE   A  1 95  ? 42.278 -13.002 1.685   1.00 16.85 ? 95   PHE   A N   1 
ATOM   773   C  CA  . PHE   A  1 95  ? 43.453 -13.111 2.542   1.00 15.10 ? 95   PHE   A CA  1 
ATOM   774   C  C   . PHE   A  1 95  ? 44.637 -12.379 1.922   1.00 17.02 ? 95   PHE   A C   1 
ATOM   775   O  O   . PHE   A  1 95  ? 44.689 -12.081 0.713   1.00 17.09 ? 95   PHE   A O   1 
ATOM   776   C  CB  . PHE   A  1 95  ? 43.883 -14.592 2.773   1.00 16.80 ? 95   PHE   A CB  1 
ATOM   777   C  CG  . PHE   A  1 95  ? 42.826 -15.479 3.383   1.00 17.71 ? 95   PHE   A CG  1 
ATOM   778   C  CD1 . PHE   A  1 95  ? 41.777 -15.965 2.578   1.00 18.59 ? 95   PHE   A CD1 1 
ATOM   779   C  CD2 . PHE   A  1 95  ? 42.892 -15.846 4.737   1.00 18.85 ? 95   PHE   A CD2 1 
ATOM   780   C  CE1 . PHE   A  1 95  ? 40.844 -16.809 3.123   1.00 17.72 ? 95   PHE   A CE1 1 
ATOM   781   C  CE2 . PHE   A  1 95  ? 41.926 -16.716 5.286   1.00 20.16 ? 95   PHE   A CE2 1 
ATOM   782   C  CZ  . PHE   A  1 95  ? 40.897 -17.176 4.480   1.00 21.08 ? 95   PHE   A CZ  1 
ATOM   783   N  N   . HIS   A  1 96  ? 45.619 -12.127 2.789   1.00 15.71 ? 96   HIS   A N   1 
ATOM   784   C  CA  . HIS   A  1 96  ? 46.947 -11.683 2.406   1.00 15.30 ? 96   HIS   A CA  1 
ATOM   785   C  C   . HIS   A  1 96  ? 47.915 -12.689 3.014   1.00 16.23 ? 96   HIS   A C   1 
ATOM   786   O  O   . HIS   A  1 96  ? 47.725 -13.116 4.165   1.00 17.24 ? 96   HIS   A O   1 
ATOM   787   C  CB  . HIS   A  1 96  ? 47.219 -10.267 2.958   1.00 15.70 ? 96   HIS   A CB  1 
ATOM   788   C  CG  . HIS   A  1 96  ? 46.209 -9.244  2.497   1.00 14.98 ? 96   HIS   A CG  1 
ATOM   789   N  ND1 . HIS   A  1 96  ? 46.432 -8.371  1.444   1.00 17.63 ? 96   HIS   A ND1 1 
ATOM   790   C  CD2 . HIS   A  1 96  ? 44.928 -9.023  2.911   1.00 14.60 ? 96   HIS   A CD2 1 
ATOM   791   C  CE1 . HIS   A  1 96  ? 45.342 -7.625  1.262   1.00 15.69 ? 96   HIS   A CE1 1 
ATOM   792   N  NE2 . HIS   A  1 96  ? 44.421 -7.976  2.159   1.00 15.44 ? 96   HIS   A NE2 1 
ATOM   793   N  N   . TRP   A  1 97  ? 48.946 -13.083 2.268   1.00 16.56 ? 97   TRP   A N   1 
ATOM   794   C  CA  . TRP   A  1 97  ? 49.894 -14.090 2.779   1.00 15.82 ? 97   TRP   A CA  1 
ATOM   795   C  C   . TRP   A  1 97  ? 51.273 -13.906 2.178   1.00 18.69 ? 97   TRP   A C   1 
ATOM   796   O  O   . TRP   A  1 97  ? 51.474 -13.093 1.272   1.00 17.40 ? 97   TRP   A O   1 
ATOM   797   C  CB  . TRP   A  1 97  ? 49.422 -15.523 2.513   1.00 16.30 ? 97   TRP   A CB  1 
ATOM   798   C  CG  . TRP   A  1 97  ? 49.271 -15.863 1.029   1.00 17.25 ? 97   TRP   A CG  1 
ATOM   799   C  CD1 . TRP   A  1 97  ? 50.202 -16.403 0.195   1.00 18.07 ? 97   TRP   A CD1 1 
ATOM   800   C  CD2 . TRP   A  1 97  ? 48.080 -15.650 0.225   1.00 17.05 ? 97   TRP   A CD2 1 
ATOM   801   N  NE1 . TRP   A  1 97  ? 49.679 -16.542 -1.085  1.00 18.50 ? 97   TRP   A NE1 1 
ATOM   802   C  CE2 . TRP   A  1 97  ? 48.385 -16.096 -1.088  1.00 18.47 ? 97   TRP   A CE2 1 
ATOM   803   C  CE3 . TRP   A  1 97  ? 46.804 -15.114 0.495   1.00 15.78 ? 97   TRP   A CE3 1 
ATOM   804   C  CZ2 . TRP   A  1 97  ? 47.433 -16.062 -2.145  1.00 17.33 ? 97   TRP   A CZ2 1 
ATOM   805   C  CZ3 . TRP   A  1 97  ? 45.882 -15.078 -0.534  1.00 16.61 ? 97   TRP   A CZ3 1 
ATOM   806   C  CH2 . TRP   A  1 97  ? 46.194 -15.572 -1.835  1.00 16.80 ? 97   TRP   A CH2 1 
ATOM   807   N  N   . GLY   A  1 98  ? 52.236 -14.687 2.680   1.00 18.79 ? 98   GLY   A N   1 
ATOM   808   C  CA  . GLY   A  1 98  ? 53.630 -14.508 2.351   1.00 18.84 ? 98   GLY   A CA  1 
ATOM   809   C  C   . GLY   A  1 98  ? 54.170 -15.590 1.420   1.00 20.46 ? 98   GLY   A C   1 
ATOM   810   O  O   . GLY   A  1 98  ? 53.498 -16.556 1.036   1.00 20.26 ? 98   GLY   A O   1 
ATOM   811   N  N   . SER   A  1 99  ? 55.445 -15.383 1.026   1.00 20.10 ? 99   SER   A N   1 
ATOM   812   C  CA  . SER   A  1 99  ? 56.181 -16.429 0.316   1.00 21.46 ? 99   SER   A CA  1 
ATOM   813   C  C   . SER   A  1 99  ? 56.721 -17.512 1.248   1.00 21.89 ? 99   SER   A C   1 
ATOM   814   O  O   . SER   A  1 99  ? 57.185 -18.544 0.751   1.00 24.45 ? 99   SER   A O   1 
ATOM   815   C  CB  . SER   A  1 99  ? 57.331 -15.840 -0.507  1.00 24.20 ? 99   SER   A CB  1 
ATOM   816   O  OG  . SER   A  1 99  ? 58.140 -14.987 0.290   1.00 25.69 ? 99   SER   A OG  1 
ATOM   817   N  N   . HIS   A  1 100 ? 56.663 -17.309 2.561   1.00 23.63 ? 100  HIS   A N   1 
ATOM   818   C  CA  . HIS   A  1 100 ? 57.009 -18.324 3.540   1.00 24.38 ? 100  HIS   A CA  1 
ATOM   819   C  C   . HIS   A  1 100 ? 56.231 -17.984 4.795   1.00 23.37 ? 100  HIS   A C   1 
ATOM   820   O  O   . HIS   A  1 100 ? 55.639 -16.910 4.890   1.00 24.52 ? 100  HIS   A O   1 
ATOM   821   C  CB  . HIS   A  1 100 ? 58.528 -18.369 3.788   1.00 24.42 ? 100  HIS   A CB  1 
ATOM   822   C  CG  . HIS   A  1 100 ? 59.093 -17.082 4.271   1.00 24.72 ? 100  HIS   A CG  1 
ATOM   823   N  ND1 . HIS   A  1 100 ? 59.125 -16.753 5.610   1.00 26.60 ? 100  HIS   A ND1 1 
ATOM   824   C  CD2 . HIS   A  1 100 ? 59.598 -16.014 3.603   1.00 26.40 ? 100  HIS   A CD2 1 
ATOM   825   C  CE1 . HIS   A  1 100 ? 59.643 -15.543 5.750   1.00 27.32 ? 100  HIS   A CE1 1 
ATOM   826   N  NE2 . HIS   A  1 100 ? 59.930 -15.066 4.547   1.00 24.63 ? 100  HIS   A NE2 1 
ATOM   827   N  N   . ASP   A  1 101 ? 56.225 -18.910 5.763   1.00 24.13 ? 101  ASP   A N   1 
ATOM   828   C  CA  . ASP   A  1 101 ? 55.336 -18.750 6.910   1.00 23.50 ? 101  ASP   A CA  1 
ATOM   829   C  C   . ASP   A  1 101 ? 55.730 -17.593 7.828   1.00 24.59 ? 101  ASP   A C   1 
ATOM   830   O  O   . ASP   A  1 101 ? 54.946 -17.234 8.716   1.00 26.05 ? 101  ASP   A O   1 
ATOM   831   C  CB  . ASP   A  1 101 ? 55.340 -20.021 7.756   1.00 26.59 ? 101  ASP   A CB  1 
ATOM   832   C  CG  . ASP   A  1 101 ? 54.648 -21.209 7.082   1.00 26.25 ? 101  ASP   A CG  1 
ATOM   833   O  OD1 . ASP   A  1 101 ? 54.016 -21.045 6.001   1.00 27.67 ? 101  ASP   A OD1 1 
ATOM   834   O  OD2 . ASP   A  1 101 ? 54.721 -22.305 7.689   1.00 29.42 ? 101  ASP   A OD2 1 
ATOM   835   N  N   . GLY   A  1 102 ? 56.924 -17.051 7.672   1.00 24.14 ? 102  GLY   A N   1 
ATOM   836   C  CA  . GLY   A  1 102 ? 57.409 -16.000 8.556   1.00 24.28 ? 102  GLY   A CA  1 
ATOM   837   C  C   . GLY   A  1 102 ? 56.951 -14.596 8.229   1.00 24.27 ? 102  GLY   A C   1 
ATOM   838   O  O   . GLY   A  1 102 ? 57.299 -13.641 8.942   1.00 25.27 ? 102  GLY   A O   1 
ATOM   839   N  N   . GLN   A  1 103 ? 56.183 -14.428 7.163   1.00 21.65 ? 103  GLN   A N   1 
ATOM   840   C  CA  . GLN   A  1 103 ? 55.589 -13.130 6.844   1.00 21.44 ? 103  GLN   A CA  1 
ATOM   841   C  C   . GLN   A  1 103 ? 54.284 -13.394 6.121   1.00 21.17 ? 103  GLN   A C   1 
ATOM   842   O  O   . GLN   A  1 103 ? 53.985 -14.533 5.729   1.00 21.42 ? 103  GLN   A O   1 
ATOM   843   C  CB  . GLN   A  1 103 ? 56.532 -12.236 6.003   1.00 21.40 ? 103  GLN   A CB  1 
ATOM   844   C  CG  . GLN   A  1 103 ? 56.882 -12.782 4.620   1.00 22.95 ? 103  GLN   A CG  1 
ATOM   845   C  CD  . GLN   A  1 103 ? 58.027 -12.023 3.952   1.00 24.15 ? 103  GLN   A CD  1 
ATOM   846   O  OE1 . GLN   A  1 103 ? 58.889 -11.492 4.648   1.00 26.67 ? 103  GLN   A OE1 1 
ATOM   847   N  NE2 . GLN   A  1 103 ? 58.056 -11.972 2.613   1.00 22.56 ? 103  GLN   A NE2 1 
ATOM   848   N  N   . GLY   A  1 104 ? 53.507 -12.322 5.927   1.00 20.20 ? 104  GLY   A N   1 
ATOM   849   C  CA  . GLY   A  1 104 ? 52.241 -12.472 5.232   1.00 18.22 ? 104  GLY   A CA  1 
ATOM   850   C  C   . GLY   A  1 104 ? 51.154 -11.564 5.736   1.00 18.06 ? 104  GLY   A C   1 
ATOM   851   O  O   . GLY   A  1 104 ? 50.375 -11.027 4.938   1.00 18.43 ? 104  GLY   A O   1 
ATOM   852   N  N   . SER   A  1 105 ? 51.074 -11.391 7.057   1.00 17.36 ? 105  SER   A N   1 
ATOM   853   C  CA  . SER   A  1 105 ? 50.033 -10.490 7.543   1.00 17.18 ? 105  SER   A CA  1 
ATOM   854   C  C   . SER   A  1 105 ? 50.326 -9.040  7.141   1.00 17.26 ? 105  SER   A C   1 
ATOM   855   O  O   . SER   A  1 105 ? 51.477 -8.648  6.843   1.00 17.45 ? 105  SER   A O   1 
ATOM   856   C  CB  . SER   A  1 105 ? 49.853 -10.618 9.059   1.00 18.42 ? 105  SER   A CB  1 
ATOM   857   O  OG  . SER   A  1 105 ? 50.991 -10.120 9.804   1.00 19.28 ? 105  SER   A OG  1 
ATOM   858   N  N   . GLU   A  1 106 ? 49.269 -8.223  7.175   1.00 17.51 ? 106  GLU   A N   1 
ATOM   859   C  CA  . GLU   A  1 106 ? 49.356 -6.802  6.864   1.00 14.91 ? 106  GLU   A CA  1 
ATOM   860   C  C   . GLU   A  1 106 ? 49.559 -5.996  8.150   1.00 15.93 ? 106  GLU   A C   1 
ATOM   861   O  O   . GLU   A  1 106 ? 50.580 -5.333  8.332   1.00 16.90 ? 106  GLU   A O   1 
ATOM   862   C  CB  . GLU   A  1 106 ? 48.098 -6.358  6.079   1.00 17.04 ? 106  GLU   A CB  1 
ATOM   863   C  CG  . GLU   A  1 106 ? 48.026 -7.104  4.745   1.00 17.06 ? 106  GLU   A CG  1 
ATOM   864   C  CD  . GLU   A  1 106 ? 47.379 -6.246  3.680   1.00 15.73 ? 106  GLU   A CD  1 
ATOM   865   O  OE1 . GLU   A  1 106 ? 46.202 -5.865  3.901   1.00 15.84 ? 106  GLU   A OE1 1 
ATOM   866   O  OE2 . GLU   A  1 106 ? 48.052 -5.934  2.685   1.00 18.55 ? 106  GLU   A OE2 1 
ATOM   867   N  N   . HIS   A  1 107 ? 48.611 -6.102  9.068   1.00 16.59 ? 107  HIS   A N   1 
ATOM   868   C  CA  . HIS   A  1 107 ? 48.859 -5.573  10.389  1.00 18.44 ? 107  HIS   A CA  1 
ATOM   869   C  C   . HIS   A  1 107 ? 49.953 -6.381  11.083  1.00 18.45 ? 107  HIS   A C   1 
ATOM   870   O  O   . HIS   A  1 107 ? 50.189 -7.558  10.769  1.00 18.50 ? 107  HIS   A O   1 
ATOM   871   C  CB  . HIS   A  1 107 ? 47.564 -5.581  11.216  1.00 16.31 ? 107  HIS   A CB  1 
ATOM   872   C  CG  . HIS   A  1 107 ? 46.557 -4.608  10.683  1.00 16.83 ? 107  HIS   A CG  1 
ATOM   873   N  ND1 . HIS   A  1 107 ? 45.678 -4.954  9.691   1.00 17.58 ? 107  HIS   A ND1 1 
ATOM   874   C  CD2 . HIS   A  1 107 ? 46.376 -3.278  10.910  1.00 17.35 ? 107  HIS   A CD2 1 
ATOM   875   C  CE1 . HIS   A  1 107 ? 44.943 -3.895  9.370   1.00 16.97 ? 107  HIS   A CE1 1 
ATOM   876   N  NE2 . HIS   A  1 107 ? 45.348 -2.864  10.087  1.00 17.40 ? 107  HIS   A NE2 1 
ATOM   877   N  N   . THR   A  1 108 ? 50.670 -5.722  11.999  1.00 17.58 ? 108  THR   A N   1 
ATOM   878   C  CA  . THR   A  1 108 ? 51.603 -6.402  12.905  1.00 17.93 ? 108  THR   A CA  1 
ATOM   879   C  C   . THR   A  1 108 ? 51.207 -6.099  14.338  1.00 19.09 ? 108  THR   A C   1 
ATOM   880   O  O   . THR   A  1 108 ? 50.481 -5.140  14.589  1.00 20.45 ? 108  THR   A O   1 
ATOM   881   C  CB  . THR   A  1 108 ? 53.078 -5.961  12.659  1.00 17.43 ? 108  THR   A CB  1 
ATOM   882   O  OG1 . THR   A  1 108 ? 53.166 -4.541  12.768  1.00 19.21 ? 108  THR   A OG1 1 
ATOM   883   C  CG2 . THR   A  1 108 ? 53.530 -6.334  11.261  1.00 18.87 ? 108  THR   A CG2 1 
ATOM   884   N  N   . VAL   A  1 109 ? 51.649 -6.946  15.275  1.00 18.50 ? 109  VAL   A N   1 
ATOM   885   C  CA  . VAL   A  1 109 ? 51.392 -6.761  16.704  1.00 20.08 ? 109  VAL   A CA  1 
ATOM   886   C  C   . VAL   A  1 109 ? 52.749 -6.692  17.357  1.00 21.24 ? 109  VAL   A C   1 
ATOM   887   O  O   . VAL   A  1 109 ? 53.507 -7.668  17.360  1.00 21.77 ? 109  VAL   A O   1 
ATOM   888   C  CB  . VAL   A  1 109 ? 50.488 -7.865  17.291  1.00 22.25 ? 109  VAL   A CB  1 
ATOM   889   C  CG1 . VAL   A  1 109 ? 50.195 -7.600  18.775  1.00 24.30 ? 109  VAL   A CG1 1 
ATOM   890   C  CG2 . VAL   A  1 109 ? 49.165 -7.875  16.556  1.00 22.94 ? 109  VAL   A CG2 1 
ATOM   891   N  N   . ASP   A  1 110 ? 53.079 -5.525  17.922  1.00 21.45 ? 110  ASP   A N   1 
ATOM   892   C  CA  . ASP   A  1 110 ? 54.410 -5.310  18.508  1.00 21.93 ? 110  ASP   A CA  1 
ATOM   893   C  C   . ASP   A  1 110 ? 55.489 -5.749  17.511  1.00 22.99 ? 110  ASP   A C   1 
ATOM   894   O  O   . ASP   A  1 110 ? 56.493 -6.393  17.864  1.00 25.31 ? 110  ASP   A O   1 
ATOM   895   C  CB  . ASP   A  1 110 ? 54.558 -6.025  19.876  1.00 25.02 ? 110  ASP   A CB  1 
ATOM   896   C  CG  . ASP   A  1 110 ? 53.547 -5.515  20.890  1.00 30.24 ? 110  ASP   A CG  1 
ATOM   897   O  OD1 . ASP   A  1 110 ? 53.145 -4.318  20.825  1.00 26.79 ? 110  ASP   A OD1 1 
ATOM   898   O  OD2 . ASP   A  1 110 ? 53.205 -6.296  21.812  1.00 32.30 ? 110  ASP   A OD2 1 
ATOM   899   N  N   . LYS   A  1 111 ? 55.278 -5.385  16.246  1.00 22.49 ? 111  LYS   A N   1 
ATOM   900   C  CA  . LYS   A  1 111 ? 56.157 -5.562  15.085  1.00 22.87 ? 111  LYS   A CA  1 
ATOM   901   C  C   . LYS   A  1 111 ? 56.179 -6.994  14.573  1.00 25.54 ? 111  LYS   A C   1 
ATOM   902   O  O   . LYS   A  1 111 ? 56.846 -7.268  13.549  1.00 28.16 ? 111  LYS   A O   1 
ATOM   903   C  CB  . LYS   A  1 111 ? 57.604 -5.101  15.356  1.00 26.21 ? 111  LYS   A CB  1 
ATOM   904   C  CG  . LYS   A  1 111 ? 57.726 -3.669  15.855  1.00 33.20 ? 111  LYS   A CG  1 
ATOM   905   C  CD  . LYS   A  1 111 ? 57.102 -2.732  14.834  1.00 40.12 ? 111  LYS   A CD  1 
ATOM   906   C  CE  . LYS   A  1 111 ? 57.808 -2.914  13.472  1.00 43.83 ? 111  LYS   A CE  1 
ATOM   907   N  NZ  . LYS   A  1 111 ? 57.268 -2.072  12.396  1.00 39.49 ? 111  LYS   A NZ  1 
ATOM   908   N  N   . LYS   A  1 112 ? 55.441 -7.903  15.192  1.00 22.37 ? 112  LYS   A N   1 
ATOM   909   C  CA  . LYS   A  1 112 ? 55.447 -9.310  14.801  1.00 24.94 ? 112  LYS   A CA  1 
ATOM   910   C  C   . LYS   A  1 112 ? 54.468 -9.535  13.673  1.00 22.84 ? 112  LYS   A C   1 
ATOM   911   O  O   . LYS   A  1 112 ? 53.347 -9.006  13.696  1.00 22.42 ? 112  LYS   A O   1 
ATOM   912   C  CB  . LYS   A  1 112 ? 55.047 -10.198 15.977  1.00 29.76 ? 112  LYS   A CB  1 
ATOM   913   C  CG  . LYS   A  1 112 ? 54.885 -11.713 15.689  1.00 41.66 ? 112  LYS   A CG  1 
ATOM   914   C  CD  . LYS   A  1 112 ? 53.383 -12.114 15.642  1.00 45.73 ? 112  LYS   A CD  1 
ATOM   915   C  CE  . LYS   A  1 112 ? 53.158 -13.611 15.865  1.00 48.11 ? 112  LYS   A CE  1 
ATOM   916   N  NZ  . LYS   A  1 112 ? 53.946 -14.466 14.952  1.00 50.07 ? 112  LYS   A NZ  1 
ATOM   917   N  N   . LYS   A  1 113 ? 54.898 -10.335 12.697  1.00 22.16 ? 113  LYS   A N   1 
ATOM   918   C  CA  . LYS   A  1 113 ? 54.032 -10.748 11.602  1.00 21.12 ? 113  LYS   A CA  1 
ATOM   919   C  C   . LYS   A  1 113 ? 53.496 -12.167 11.777  1.00 21.84 ? 113  LYS   A C   1 
ATOM   920   O  O   . LYS   A  1 113 ? 54.135 -13.038 12.387  1.00 25.43 ? 113  LYS   A O   1 
ATOM   921   C  CB  . LYS   A  1 113 ? 54.794 -10.682 10.267  1.00 19.49 ? 113  LYS   A CB  1 
ATOM   922   C  CG  . LYS   A  1 113 ? 55.124 -9.285  9.868   1.00 21.32 ? 113  LYS   A CG  1 
ATOM   923   C  CD  . LYS   A  1 113 ? 55.831 -9.257  8.523   1.00 24.32 ? 113  LYS   A CD  1 
ATOM   924   C  CE  . LYS   A  1 113 ? 55.888 -7.813  8.036   1.00 24.07 ? 113  LYS   A CE  1 
ATOM   925   N  NZ  . LYS   A  1 113 ? 56.091 -7.745  6.516   1.00 25.95 ? 113  LYS   A NZ  1 
ATOM   926   N  N   . TYR   A  1 114 ? 52.287 -12.373 11.271  1.00 20.49 ? 114  TYR   A N   1 
ATOM   927   C  CA  . TYR   A  1 114 ? 51.706 -13.700 11.159  1.00 21.65 ? 114  TYR   A CA  1 
ATOM   928   C  C   . TYR   A  1 114 ? 51.860 -14.207 9.729   1.00 20.60 ? 114  TYR   A C   1 
ATOM   929   O  O   . TYR   A  1 114 ? 52.181 -13.448 8.824   1.00 20.47 ? 114  TYR   A O   1 
ATOM   930   C  CB  . TYR   A  1 114 ? 50.220 -13.667 11.548  1.00 23.12 ? 114  TYR   A CB  1 
ATOM   931   C  CG  . TYR   A  1 114 ? 49.997 -13.363 13.015  1.00 22.68 ? 114  TYR   A CG  1 
ATOM   932   C  CD1 . TYR   A  1 114 ? 49.897 -12.049 13.456  1.00 24.11 ? 114  TYR   A CD1 1 
ATOM   933   C  CD2 . TYR   A  1 114 ? 49.841 -14.399 13.960  1.00 27.94 ? 114  TYR   A CD2 1 
ATOM   934   C  CE1 . TYR   A  1 114 ? 49.673 -11.780 14.797  1.00 28.39 ? 114  TYR   A CE1 1 
ATOM   935   C  CE2 . TYR   A  1 114 ? 49.650 -14.108 15.320  1.00 27.81 ? 114  TYR   A CE2 1 
ATOM   936   C  CZ  . TYR   A  1 114 ? 49.575 -12.790 15.702  1.00 29.92 ? 114  TYR   A CZ  1 
ATOM   937   O  OH  . TYR   A  1 114 ? 49.340 -12.464 17.034  1.00 34.84 ? 114  TYR   A OH  1 
ATOM   938   N  N   . ALA   A  1 115 ? 51.569 -15.501 9.527   1.00 21.67 ? 115  ALA   A N   1 
ATOM   939   C  CA  . ALA   A  1 115 ? 51.700 -16.103 8.207   1.00 20.46 ? 115  ALA   A CA  1 
ATOM   940   C  C   . ALA   A  1 115 ? 50.656 -15.589 7.229   1.00 18.87 ? 115  ALA   A C   1 
ATOM   941   O  O   . ALA   A  1 115 ? 50.878 -15.619 5.996   1.00 20.84 ? 115  ALA   A O   1 
ATOM   942   C  CB  . ALA   A  1 115 ? 51.583 -17.644 8.333   1.00 22.41 ? 115  ALA   A CB  1 
ATOM   943   N  N   . ALA   A  1 116 ? 49.511 -15.111 7.712   1.00 18.90 ? 116  ALA   A N   1 
ATOM   944   C  CA  . ALA   A  1 116 ? 48.520 -14.581 6.792   1.00 17.70 ? 116  ALA   A CA  1 
ATOM   945   C  C   . ALA   A  1 116 ? 47.536 -13.741 7.598   1.00 18.53 ? 116  ALA   A C   1 
ATOM   946   O  O   . ALA   A  1 116 ? 47.570 -13.705 8.834   1.00 18.44 ? 116  ALA   A O   1 
ATOM   947   C  CB  . ALA   A  1 116 ? 47.802 -15.701 5.986   1.00 18.71 ? 116  ALA   A CB  1 
ATOM   948   N  N   . GLU   A  1 117 ? 46.680 -13.046 6.877   1.00 17.95 ? 117  GLU   A N   1 
ATOM   949   C  CA  . GLU   A  1 117 ? 45.646 -12.223 7.482   1.00 19.10 ? 117  GLU   A CA  1 
ATOM   950   C  C   . GLU   A  1 117 ? 44.402 -12.326 6.619   1.00 17.64 ? 117  GLU   A C   1 
ATOM   951   O  O   . GLU   A  1 117 ? 44.455 -12.213 5.389   1.00 17.64 ? 117  GLU   A O   1 
ATOM   952   C  CB  . GLU   A  1 117 ? 46.117 -10.758 7.630   1.00 17.93 ? 117  GLU   A CB  1 
ATOM   953   C  CG  . GLU   A  1 117 ? 45.183 -9.883  8.410   1.00 17.71 ? 117  GLU   A CG  1 
ATOM   954   C  CD  . GLU   A  1 117 ? 45.780 -8.499  8.664   1.00 17.56 ? 117  GLU   A CD  1 
ATOM   955   O  OE1 . GLU   A  1 117 ? 47.002 -8.394  8.883   1.00 17.50 ? 117  GLU   A OE1 1 
ATOM   956   O  OE2 . GLU   A  1 117 ? 45.031 -7.508  8.693   1.00 18.16 ? 117  GLU   A OE2 1 
ATOM   957   N  N   . LEU   A  1 118 ? 43.282 -12.544 7.290   1.00 17.14 ? 118  LEU   A N   1 
ATOM   958   C  CA  . LEU   A  1 118 ? 41.957 -12.628 6.703   1.00 17.47 ? 118  LEU   A CA  1 
ATOM   959   C  C   . LEU   A  1 118 ? 41.228 -11.306 6.874   1.00 16.46 ? 118  LEU   A C   1 
ATOM   960   O  O   . LEU   A  1 118 ? 41.235 -10.718 7.968   1.00 17.62 ? 118  LEU   A O   1 
ATOM   961   C  CB  . LEU   A  1 118 ? 41.203 -13.747 7.435   1.00 17.61 ? 118  LEU   A CB  1 
ATOM   962   C  CG  . LEU   A  1 118 ? 39.682 -13.776 7.228   1.00 16.85 ? 118  LEU   A CG  1 
ATOM   963   C  CD1 . LEU   A  1 118 ? 39.273 -14.029 5.756   1.00 17.25 ? 118  LEU   A CD1 1 
ATOM   964   C  CD2 . LEU   A  1 118 ? 39.088 -14.904 8.103   1.00 18.91 ? 118  LEU   A CD2 1 
ATOM   965   N  N   . HIS   A  1 119 ? 40.616 -10.811 5.784   1.00 15.80 ? 119  HIS   A N   1 
ATOM   966   C  CA  . HIS   A  1 119 ? 39.805 -9.588  5.806   1.00 17.02 ? 119  HIS   A CA  1 
ATOM   967   C  C   . HIS   A  1 119 ? 38.383 -9.905  5.408   1.00 16.22 ? 119  HIS   A C   1 
ATOM   968   O  O   . HIS   A  1 119 ? 38.128 -10.291 4.252   1.00 16.64 ? 119  HIS   A O   1 
ATOM   969   C  CB  . HIS   A  1 119 ? 40.376 -8.549  4.829   1.00 15.91 ? 119  HIS   A CB  1 
ATOM   970   C  CG  . HIS   A  1 119 ? 41.670 -7.996  5.303   1.00 14.69 ? 119  HIS   A CG  1 
ATOM   971   N  ND1 . HIS   A  1 119 ? 42.559 -7.346  4.475   1.00 14.31 ? 119  HIS   A ND1 1 
ATOM   972   C  CD2 . HIS   A  1 119 ? 42.222 -8.003  6.542   1.00 15.81 ? 119  HIS   A CD2 1 
ATOM   973   C  CE1 . HIS   A  1 119 ? 43.615 -6.971  5.196   1.00 16.47 ? 119  HIS   A CE1 1 
ATOM   974   N  NE2 . HIS   A  1 119 ? 43.448 -7.405  6.432   1.00 16.08 ? 119  HIS   A NE2 1 
ATOM   975   N  N   . LEU   A  1 120 ? 37.458 -9.668  6.329   1.00 17.26 ? 120  LEU   A N   1 
ATOM   976   C  CA  . LEU   A  1 120 ? 36.014 -9.761  6.064   1.00 16.79 ? 120  LEU   A CA  1 
ATOM   977   C  C   . LEU   A  1 120 ? 35.535 -8.328  5.839   1.00 17.66 ? 120  LEU   A C   1 
ATOM   978   O  O   . LEU   A  1 120 ? 35.638 -7.479  6.730   1.00 16.99 ? 120  LEU   A O   1 
ATOM   979   C  CB  . LEU   A  1 120 ? 35.308 -10.452 7.231   1.00 18.41 ? 120  LEU   A CB  1 
ATOM   980   C  CG  . LEU   A  1 120 ? 35.671 -11.931 7.319   1.00 18.69 ? 120  LEU   A CG  1 
ATOM   981   C  CD1 . LEU   A  1 120 ? 36.152 -12.236 8.786   1.00 23.24 ? 120  LEU   A CD1 1 
ATOM   982   C  CD2 . LEU   A  1 120 ? 34.505 -12.843 6.919   1.00 21.40 ? 120  LEU   A CD2 1 
ATOM   983   N  N   . VAL   A  1 121 ? 35.056 -8.037  4.629   1.00 18.21 ? 121  VAL   A N   1 
ATOM   984   C  CA  . VAL   A  1 121 ? 34.802 -6.676  4.159   1.00 16.87 ? 121  VAL   A CA  1 
ATOM   985   C  C   . VAL   A  1 121 ? 33.316 -6.372  4.234   1.00 18.60 ? 121  VAL   A C   1 
ATOM   986   O  O   . VAL   A  1 121 ? 32.497 -7.129  3.679   1.00 18.41 ? 121  VAL   A O   1 
ATOM   987   C  CB  . VAL   A  1 121 ? 35.295 -6.530  2.713   1.00 16.68 ? 121  VAL   A CB  1 
ATOM   988   C  CG1 . VAL   A  1 121 ? 35.083 -5.088  2.191   1.00 17.18 ? 121  VAL   A CG1 1 
ATOM   989   C  CG2 . VAL   A  1 121 ? 36.802 -6.928  2.615   1.00 18.24 ? 121  VAL   A CG2 1 
ATOM   990   N  N   . HIS   A  1 122 ? 32.959 -5.259  4.866   1.00 17.41 ? 122  HIS   A N   1 
ATOM   991   C  CA  . HIS   A  1 122 ? 31.555 -4.883  5.057   1.00 17.69 ? 122  HIS   A CA  1 
ATOM   992   C  C   . HIS   A  1 122 ? 31.325 -3.423  4.676   1.00 18.78 ? 122  HIS   A C   1 
ATOM   993   O  O   . HIS   A  1 122 ? 32.215 -2.574  4.868   1.00 18.38 ? 122  HIS   A O   1 
ATOM   994   C  CB  . HIS   A  1 122 ? 31.089 -5.063  6.524   1.00 17.96 ? 122  HIS   A CB  1 
ATOM   995   C  CG  . HIS   A  1 122 ? 31.502 -6.360  7.161   1.00 17.76 ? 122  HIS   A CG  1 
ATOM   996   N  ND1 . HIS   A  1 122 ? 32.810 -6.612  7.548   1.00 17.98 ? 122  HIS   A ND1 1 
ATOM   997   C  CD2 . HIS   A  1 122 ? 30.772 -7.457  7.524   1.00 19.73 ? 122  HIS   A CD2 1 
ATOM   998   C  CE1 . HIS   A  1 122 ? 32.860 -7.822  8.107   1.00 18.83 ? 122  HIS   A CE1 1 
ATOM   999   N  NE2 . HIS   A  1 122 ? 31.643 -8.345  8.117   1.00 20.31 ? 122  HIS   A NE2 1 
ATOM   1000  N  N   . TRP   A  1 123 ? 30.088 -3.122  4.195   1.00 18.38 ? 123  TRP   A N   1 
ATOM   1001  C  CA  . TRP   A  1 123 ? 29.755 -1.748  3.824   1.00 19.29 ? 123  TRP   A CA  1 
ATOM   1002  C  C   . TRP   A  1 123 ? 28.506 -1.245  4.528   1.00 18.22 ? 123  TRP   A C   1 
ATOM   1003  O  O   . TRP   A  1 123 ? 27.566 -1.987  4.854   1.00 20.64 ? 123  TRP   A O   1 
ATOM   1004  C  CB  . TRP   A  1 123 ? 29.630 -1.561  2.287   1.00 17.33 ? 123  TRP   A CB  1 
ATOM   1005  C  CG  . TRP   A  1 123 ? 28.609 -2.489  1.646   1.00 18.84 ? 123  TRP   A CG  1 
ATOM   1006  C  CD1 . TRP   A  1 123 ? 28.808 -3.781  1.199   1.00 18.58 ? 123  TRP   A CD1 1 
ATOM   1007  C  CD2 . TRP   A  1 123 ? 27.210 -2.187  1.389   1.00 19.55 ? 123  TRP   A CD2 1 
ATOM   1008  N  NE1 . TRP   A  1 123 ? 27.622 -4.280  0.651   1.00 19.19 ? 123  TRP   A NE1 1 
ATOM   1009  C  CE2 . TRP   A  1 123 ? 26.629 -3.331  0.804   1.00 20.24 ? 123  TRP   A CE2 1 
ATOM   1010  C  CE3 . TRP   A  1 123 ? 26.401 -1.061  1.623   1.00 19.79 ? 123  TRP   A CE3 1 
ATOM   1011  C  CZ2 . TRP   A  1 123 ? 25.276 -3.367  0.416   1.00 19.70 ? 123  TRP   A CZ2 1 
ATOM   1012  C  CZ3 . TRP   A  1 123 ? 25.039 -1.107  1.276   1.00 20.51 ? 123  TRP   A CZ3 1 
ATOM   1013  C  CH2 . TRP   A  1 123 ? 24.505 -2.250  0.660   1.00 23.79 ? 123  TRP   A CH2 1 
ATOM   1014  N  N   . ASN   A  1 124 ? 28.529 0.066   4.782   1.00 20.54 ? 124  ASN   A N   1 
ATOM   1015  C  CA  . ASN   A  1 124 ? 27.506 0.742   5.575   1.00 19.97 ? 124  ASN   A CA  1 
ATOM   1016  C  C   . ASN   A  1 124 ? 26.206 0.888   4.796   1.00 22.08 ? 124  ASN   A C   1 
ATOM   1017  O  O   . ASN   A  1 124 ? 26.194 1.555   3.756   1.00 21.50 ? 124  ASN   A O   1 
ATOM   1018  C  CB  . ASN   A  1 124 ? 28.071 2.114   5.956   1.00 20.41 ? 124  ASN   A CB  1 
ATOM   1019  C  CG  . ASN   A  1 124 ? 27.210 2.862   6.947   1.00 23.87 ? 124  ASN   A CG  1 
ATOM   1020  O  OD1 . ASN   A  1 124 ? 26.031 2.549   7.156   1.00 24.16 ? 124  ASN   A OD1 1 
ATOM   1021  N  ND2 . ASN   A  1 124 ? 27.828 3.850   7.608   1.00 22.50 ? 124  ASN   A ND2 1 
ATOM   1022  N  N   . THR   A  1 125 ? 25.102 0.311   5.321   1.00 20.06 ? 125  THR   A N   1 
ATOM   1023  C  CA  . THR   A  1 125 ? 23.841 0.403   4.574   1.00 21.73 ? 125  THR   A CA  1 
ATOM   1024  C  C   . THR   A  1 125 ? 23.263 1.813   4.556   1.00 24.69 ? 125  THR   A C   1 
ATOM   1025  O  O   . THR   A  1 125 ? 22.206 2.044   3.947   1.00 28.40 ? 125  THR   A O   1 
ATOM   1026  C  CB  . THR   A  1 125 ? 22.800 -0.548  5.145   1.00 23.43 ? 125  THR   A CB  1 
ATOM   1027  O  OG1 . THR   A  1 125 ? 22.486 -0.150  6.504   1.00 27.28 ? 125  THR   A OG1 1 
ATOM   1028  C  CG2 . THR   A  1 125 ? 23.319 -1.955  5.135   1.00 24.17 ? 125  THR   A CG2 1 
ATOM   1029  N  N   . LYS   A  1 126 ? 23.889 2.747   5.257   1.00 23.94 ? 126  LYS   A N   1 
ATOM   1030  C  CA  . LYS   A  1 126 ? 23.613 4.161   5.051   1.00 27.07 ? 126  LYS   A CA  1 
ATOM   1031  C  C   . LYS   A  1 126 ? 23.726 4.539   3.573   1.00 25.49 ? 126  LYS   A C   1 
ATOM   1032  O  O   . LYS   A  1 126 ? 23.036 5.451   3.102   1.00 28.00 ? 126  LYS   A O   1 
ATOM   1033  C  CB  . LYS   A  1 126 ? 24.606 4.948   5.934   1.00 30.30 ? 126  LYS   A CB  1 
ATOM   1034  C  CG  . LYS   A  1 126 ? 24.701 6.441   5.740   1.00 31.02 ? 126  LYS   A CG  1 
ATOM   1035  C  CD  . LYS   A  1 126 ? 25.728 7.072   6.729   1.00 31.11 ? 126  LYS   A CD  1 
ATOM   1036  C  CE  . LYS   A  1 126 ? 25.767 8.597   6.522   1.00 34.42 ? 126  LYS   A CE  1 
ATOM   1037  N  NZ  . LYS   A  1 126 ? 26.831 9.306   7.292   1.00 34.09 ? 126  LYS   A NZ  1 
ATOM   1038  N  N   . TYR   A  1 127 ? 24.604 3.866   2.832   1.00 23.05 ? 127  TYR   A N   1 
ATOM   1039  C  CA  . TYR   A  1 127 ? 24.877 4.159   1.432   1.00 23.89 ? 127  TYR   A CA  1 
ATOM   1040  C  C   . TYR   A  1 127 ? 24.249 3.045   0.601   1.00 27.59 ? 127  TYR   A C   1 
ATOM   1041  O  O   . TYR   A  1 127 ? 23.801 2.028   1.134   1.00 29.45 ? 127  TYR   A O   1 
ATOM   1042  C  CB  . TYR   A  1 127 ? 26.407 4.297   1.228   1.00 22.52 ? 127  TYR   A CB  1 
ATOM   1043  C  CG  . TYR   A  1 127 ? 26.980 5.326   2.189   1.00 22.16 ? 127  TYR   A CG  1 
ATOM   1044  C  CD1 . TYR   A  1 127 ? 26.606 6.655   2.080   1.00 23.52 ? 127  TYR   A CD1 1 
ATOM   1045  C  CD2 . TYR   A  1 127 ? 27.882 4.973   3.220   1.00 21.28 ? 127  TYR   A CD2 1 
ATOM   1046  C  CE1 . TYR   A  1 127 ? 27.078 7.612   2.939   1.00 23.37 ? 127  TYR   A CE1 1 
ATOM   1047  C  CE2 . TYR   A  1 127 ? 28.386 5.942   4.110   1.00 21.54 ? 127  TYR   A CE2 1 
ATOM   1048  C  CZ  . TYR   A  1 127 ? 27.985 7.271   3.959   1.00 24.17 ? 127  TYR   A CZ  1 
ATOM   1049  O  OH  . TYR   A  1 127 ? 28.418 8.267   4.802   1.00 25.30 ? 127  TYR   A OH  1 
ATOM   1050  N  N   . GLY   A  1 128 ? 24.170 3.228   -0.714  1.00 29.64 ? 128  GLY   A N   1 
ATOM   1051  C  CA  . GLY   A  1 128 ? 23.327 2.306   -1.468  1.00 29.83 ? 128  GLY   A CA  1 
ATOM   1052  C  C   . GLY   A  1 128 ? 23.952 0.940   -1.681  1.00 25.85 ? 128  GLY   A C   1 
ATOM   1053  O  O   . GLY   A  1 128 ? 23.244 -0.069  -1.860  1.00 29.28 ? 128  GLY   A O   1 
ATOM   1054  N  N   . ASP   A  1 129 ? 25.268 0.891   -1.717  1.00 22.39 ? 129  ASP   A N   1 
ATOM   1055  C  CA  . ASP   A  1 129 ? 25.977 -0.322  -2.105  1.00 21.93 ? 129  ASP   A CA  1 
ATOM   1056  C  C   . ASP   A  1 129 ? 27.452 -0.073  -1.784  1.00 20.00 ? 129  ASP   A C   1 
ATOM   1057  O  O   . ASP   A  1 129 ? 27.859 1.036   -1.379  1.00 20.71 ? 129  ASP   A O   1 
ATOM   1058  C  CB  . ASP   A  1 129 ? 25.777 -0.669  -3.592  1.00 24.94 ? 129  ASP   A CB  1 
ATOM   1059  C  CG  . ASP   A  1 129 ? 26.048 0.525   -4.515  1.00 28.63 ? 129  ASP   A CG  1 
ATOM   1060  O  OD1 . ASP   A  1 129 ? 27.050 1.216   -4.324  1.00 26.03 ? 129  ASP   A OD1 1 
ATOM   1061  O  OD2 . ASP   A  1 129 ? 25.240 0.780   -5.438  1.00 32.17 ? 129  ASP   A OD2 1 
ATOM   1062  N  N   . PHE   A  1 130 ? 28.265 -1.094  -2.047  1.00 18.79 ? 130  PHE   A N   1 
ATOM   1063  C  CA  . PHE   A  1 130 ? 29.678 -1.016  -1.720  1.00 19.41 ? 130  PHE   A CA  1 
ATOM   1064  C  C   . PHE   A  1 130 ? 30.342 0.153   -2.453  1.00 19.21 ? 130  PHE   A C   1 
ATOM   1065  O  O   . PHE   A  1 130 ? 31.141 0.889   -1.862  1.00 19.18 ? 130  PHE   A O   1 
ATOM   1066  C  CB  . PHE   A  1 130 ? 30.394 -2.329  -2.070  1.00 20.06 ? 130  PHE   A CB  1 
ATOM   1067  C  CG  . PHE   A  1 130 ? 31.871 -2.259  -1.841  1.00 17.58 ? 130  PHE   A CG  1 
ATOM   1068  C  CD1 . PHE   A  1 130 ? 32.733 -1.778  -2.806  1.00 18.23 ? 130  PHE   A CD1 1 
ATOM   1069  C  CD2 . PHE   A  1 130 ? 32.439 -2.629  -0.615  1.00 18.59 ? 130  PHE   A CD2 1 
ATOM   1070  C  CE1 . PHE   A  1 130 ? 34.110 -1.670  -2.582  1.00 19.22 ? 130  PHE   A CE1 1 
ATOM   1071  C  CE2 . PHE   A  1 130 ? 33.827 -2.558  -0.396  1.00 18.89 ? 130  PHE   A CE2 1 
ATOM   1072  C  CZ  . PHE   A  1 130 ? 34.687 -2.060  -1.354  1.00 18.65 ? 130  PHE   A CZ  1 
ATOM   1073  N  N   . GLY   A  1 131 ? 30.017 0.324   -3.744  1.00 19.71 ? 131  GLY   A N   1 
ATOM   1074  C  CA  . GLY   A  1 131 ? 30.677 1.375   -4.514  1.00 18.75 ? 131  GLY   A CA  1 
ATOM   1075  C  C   . GLY   A  1 131 ? 30.418 2.771   -3.989  1.00 19.90 ? 131  GLY   A C   1 
ATOM   1076  O  O   . GLY   A  1 131 ? 31.300 3.640   -4.056  1.00 19.69 ? 131  GLY   A O   1 
ATOM   1077  N  N   . LYS   A  1 132 ? 29.210 3.023   -3.493  1.00 18.92 ? 132  LYS   A N   1 
ATOM   1078  C  CA  . LYS   A  1 132 ? 28.961 4.320   -2.871  1.00 19.03 ? 132  LYS   A CA  1 
ATOM   1079  C  C   . LYS   A  1 132 ? 29.651 4.412   -1.511  1.00 22.33 ? 132  LYS   A C   1 
ATOM   1080  O  O   . LYS   A  1 132 ? 30.219 5.464   -1.152  1.00 19.67 ? 132  LYS   A O   1 
ATOM   1081  C  CB  . LYS   A  1 132 ? 27.449 4.514   -2.753  1.00 19.69 ? 132  LYS   A CB  1 
ATOM   1082  C  CG  . LYS   A  1 132 ? 26.817 4.690   -4.127  1.00 22.83 ? 132  LYS   A CG  1 
ATOM   1083  C  CD  . LYS   A  1 132 ? 25.274 4.647   -4.031  1.00 26.95 ? 132  LYS   A CD  1 
ATOM   1084  C  CE  . LYS   A  1 132 ? 24.658 4.918   -5.374  1.00 32.63 ? 132  LYS   A CE  1 
ATOM   1085  N  NZ  . LYS   A  1 132 ? 24.922 3.774   -6.305  1.00 39.57 ? 132  LYS   A NZ  1 
ATOM   1086  N  N   . ALA   A  1 133 ? 29.618 3.330   -0.730  1.00 19.84 ? 133  ALA   A N   1 
ATOM   1087  C  CA  . ALA   A  1 133 ? 30.165 3.373   0.624   1.00 18.27 ? 133  ALA   A CA  1 
ATOM   1088  C  C   . ALA   A  1 133 ? 31.670 3.610   0.622   1.00 19.80 ? 133  ALA   A C   1 
ATOM   1089  O  O   . ALA   A  1 133 ? 32.187 4.282   1.517   1.00 18.56 ? 133  ALA   A O   1 
ATOM   1090  C  CB  . ALA   A  1 133 ? 29.861 2.054   1.374   1.00 18.03 ? 133  ALA   A CB  1 
ATOM   1091  N  N   . VAL   A  1 134 ? 32.396 3.027   -0.337  1.00 17.31 ? 134  VAL   A N   1 
ATOM   1092  C  CA  . VAL   A  1 134 ? 33.857 3.080   -0.266  1.00 18.72 ? 134  VAL   A CA  1 
ATOM   1093  C  C   . VAL   A  1 134 ? 34.362 4.491   -0.488  1.00 19.39 ? 134  VAL   A C   1 
ATOM   1094  O  O   . VAL   A  1 134 ? 35.531 4.758   -0.248  1.00 17.62 ? 134  VAL   A O   1 
ATOM   1095  C  CB  . VAL   A  1 134 ? 34.468 2.086   -1.267  1.00 18.42 ? 134  VAL   A CB  1 
ATOM   1096  C  CG1 . VAL   A  1 134 ? 34.173 2.544   -2.672  1.00 16.73 ? 134  VAL   A CG1 1 
ATOM   1097  C  CG2 . VAL   A  1 134 ? 36.024 1.957   -1.080  1.00 17.07 ? 134  VAL   A CG2 1 
ATOM   1098  N  N   . GLN   A  1 135 ? 33.499 5.385   -0.933  1.00 18.23 ? 135  GLN   A N   1 
ATOM   1099  C  CA  . GLN   A  1 135 ? 33.866 6.782   -1.130  1.00 18.23 ? 135  GLN   A CA  1 
ATOM   1100  C  C   . GLN   A  1 135 ? 33.645 7.617   0.121   1.00 20.37 ? 135  GLN   A C   1 
ATOM   1101  O  O   . GLN   A  1 135 ? 33.894 8.834   0.070   1.00 25.24 ? 135  GLN   A O   1 
ATOM   1102  C  CB  . GLN   A  1 135 ? 33.077 7.385   -2.288  1.00 19.22 ? 135  GLN   A CB  1 
ATOM   1103  C  CG  . GLN   A  1 135 ? 33.335 6.656   -3.624  1.00 18.79 ? 135  GLN   A CG  1 
ATOM   1104  C  CD  . GLN   A  1 135 ? 34.806 6.739   -4.083  1.00 17.90 ? 135  GLN   A CD  1 
ATOM   1105  O  OE1 . GLN   A  1 135 ? 35.516 7.731   -3.774  1.00 22.42 ? 135  GLN   A OE1 1 
ATOM   1106  N  NE2 . GLN   A  1 135 ? 35.250 5.711   -4.830  1.00 16.91 ? 135  GLN   A NE2 1 
ATOM   1107  N  N   . GLN   A  1 136 ? 33.229 7.009   1.234   1.00 19.33 ? 136  GLN   A N   1 
ATOM   1108  C  CA  . GLN   A  1 136 ? 32.863 7.777   2.415   1.00 20.53 ? 136  GLN   A CA  1 
ATOM   1109  C  C   . GLN   A  1 136 ? 33.711 7.393   3.613   1.00 19.93 ? 136  GLN   A C   1 
ATOM   1110  O  O   . GLN   A  1 136 ? 34.035 6.221   3.790   1.00 19.57 ? 136  GLN   A O   1 
ATOM   1111  C  CB  . GLN   A  1 136 ? 31.370 7.563   2.786   1.00 21.40 ? 136  GLN   A CB  1 
ATOM   1112  C  CG  . GLN   A  1 136 ? 30.411 7.933   1.658   1.00 24.09 ? 136  GLN   A CG  1 
ATOM   1113  C  CD  . GLN   A  1 136 ? 30.429 9.407   1.331   1.00 29.32 ? 136  GLN   A CD  1 
ATOM   1114  O  OE1 . GLN   A  1 136 ? 30.824 10.244  2.151   1.00 32.36 ? 136  GLN   A OE1 1 
ATOM   1115  N  NE2 . GLN   A  1 136 ? 30.040 9.740   0.091   1.00 30.67 ? 136  GLN   A NE2 1 
ATOM   1116  N  N   . PRO   A  1 137 ? 34.063 8.343   4.475   1.00 20.65 ? 137  PRO   A N   1 
ATOM   1117  C  CA  . PRO   A  1 137 ? 34.938 7.986   5.608   1.00 20.80 ? 137  PRO   A CA  1 
ATOM   1118  C  C   . PRO   A  1 137 ? 34.342 6.932   6.504   1.00 22.10 ? 137  PRO   A C   1 
ATOM   1119  O  O   . PRO   A  1 137 ? 35.086 6.127   7.087   1.00 23.25 ? 137  PRO   A O   1 
ATOM   1120  C  CB  . PRO   A  1 137 ? 35.122 9.329   6.351   1.00 23.34 ? 137  PRO   A CB  1 
ATOM   1121  C  CG  . PRO   A  1 137 ? 34.978 10.342  5.295   1.00 28.92 ? 137  PRO   A CG  1 
ATOM   1122  C  CD  . PRO   A  1 137 ? 33.878 9.808   4.352   1.00 25.14 ? 137  PRO   A CD  1 
ATOM   1123  N  N   . ASP   A  1 138 ? 33.010 6.930   6.689   1.00 19.48 ? 138  ASP   A N   1 
ATOM   1124  C  CA  . ASP   A  1 138 ? 32.328 5.928   7.487   1.00 20.07 ? 138  ASP   A CA  1 
ATOM   1125  C  C   . ASP   A  1 138 ? 31.750 4.807   6.634   1.00 19.32 ? 138  ASP   A C   1 
ATOM   1126  O  O   . ASP   A  1 138 ? 30.800 4.132   7.065   1.00 21.12 ? 138  ASP   A O   1 
ATOM   1127  C  CB  . ASP   A  1 138 ? 31.213 6.564   8.331   1.00 20.61 ? 138  ASP   A CB  1 
ATOM   1128  C  CG  . ASP   A  1 138 ? 30.155 7.257   7.495   1.00 25.50 ? 138  ASP   A CG  1 
ATOM   1129  O  OD1 . ASP   A  1 138 ? 30.338 7.411   6.298   1.00 24.57 ? 138  ASP   A OD1 1 
ATOM   1130  O  OD2 . ASP   A  1 138 ? 29.120 7.699   8.056   1.00 27.35 ? 138  ASP   A OD2 1 
ATOM   1131  N  N   . GLY   A  1 139 ? 32.289 4.614   5.437   1.00 19.04 ? 139  GLY   A N   1 
ATOM   1132  C  CA  . GLY   A  1 139 ? 31.654 3.705   4.492   1.00 18.82 ? 139  GLY   A CA  1 
ATOM   1133  C  C   . GLY   A  1 139 ? 31.874 2.217   4.747   1.00 18.27 ? 139  GLY   A C   1 
ATOM   1134  O  O   . GLY   A  1 139 ? 30.960 1.415   4.497   1.00 19.63 ? 139  GLY   A O   1 
ATOM   1135  N  N   . LEU   A  1 140 ? 33.079 1.819   5.188   1.00 18.56 ? 140  LEU   A N   1 
ATOM   1136  C  CA  . LEU   A  1 140 ? 33.428 0.402   5.248   1.00 17.28 ? 140  LEU   A CA  1 
ATOM   1137  C  C   . LEU   A  1 140 ? 33.886 0.027   6.645   1.00 18.49 ? 140  LEU   A C   1 
ATOM   1138  O  O   . LEU   A  1 140 ? 34.385 0.871   7.401   1.00 18.76 ? 140  LEU   A O   1 
ATOM   1139  C  CB  . LEU   A  1 140 ? 34.581 0.033   4.277   1.00 16.99 ? 140  LEU   A CB  1 
ATOM   1140  C  CG  . LEU   A  1 140 ? 34.320 0.396   2.811   1.00 18.14 ? 140  LEU   A CG  1 
ATOM   1141  C  CD1 . LEU   A  1 140 ? 35.530 -0.123  2.023   1.00 17.33 ? 140  LEU   A CD1 1 
ATOM   1142  C  CD2 . LEU   A  1 140 ? 33.024 -0.274  2.266   1.00 18.20 ? 140  LEU   A CD2 1 
ATOM   1143  N  N   . ALA   A  1 141 ? 33.740 -1.266  6.944   1.00 17.73 ? 141  ALA   A N   1 
ATOM   1144  C  CA  . ALA   A  1 141 ? 34.273 -1.868  8.167   1.00 17.77 ? 141  ALA   A CA  1 
ATOM   1145  C  C   . ALA   A  1 141 ? 34.929 -3.159  7.744   1.00 18.76 ? 141  ALA   A C   1 
ATOM   1146  O  O   . ALA   A  1 141 ? 34.277 -4.009  7.122   1.00 18.93 ? 141  ALA   A O   1 
ATOM   1147  C  CB  . ALA   A  1 141 ? 33.186 -2.138  9.221   1.00 20.37 ? 141  ALA   A CB  1 
ATOM   1148  N  N   . VAL   A  1 142 ? 36.207 -3.320  8.075   1.00 17.09 ? 142  VAL   A N   1 
ATOM   1149  C  CA  . VAL   A  1 142 ? 36.910 -4.541  7.725   1.00 17.50 ? 142  VAL   A CA  1 
ATOM   1150  C  C   . VAL   A  1 142 ? 37.300 -5.225  9.028   1.00 18.11 ? 142  VAL   A C   1 
ATOM   1151  O  O   . VAL   A  1 142 ? 37.946 -4.617  9.901   1.00 20.03 ? 142  VAL   A O   1 
ATOM   1152  C  CB  . VAL   A  1 142 ? 38.128 -4.322  6.813   1.00 16.40 ? 142  VAL   A CB  1 
ATOM   1153  C  CG1 . VAL   A  1 142 ? 38.734 -5.712  6.441   1.00 18.33 ? 142  VAL   A CG1 1 
ATOM   1154  C  CG2 . VAL   A  1 142 ? 37.702 -3.677  5.494   1.00 17.79 ? 142  VAL   A CG2 1 
ATOM   1155  N  N   . LEU   A  1 143 ? 36.880 -6.476  9.153   1.00 18.25 ? 143  LEU   A N   1 
ATOM   1156  C  CA  . LEU   A  1 143 ? 37.212 -7.323  10.288  1.00 19.44 ? 143  LEU   A CA  1 
ATOM   1157  C  C   . LEU   A  1 143 ? 38.459 -8.105  9.903   1.00 20.01 ? 143  LEU   A C   1 
ATOM   1158  O  O   . LEU   A  1 143 ? 38.437 -8.891  8.935   1.00 19.72 ? 143  LEU   A O   1 
ATOM   1159  C  CB  . LEU   A  1 143 ? 36.030 -8.237  10.611  1.00 19.53 ? 143  LEU   A CB  1 
ATOM   1160  C  CG  . LEU   A  1 143 ? 36.182 -9.174  11.796  1.00 22.23 ? 143  LEU   A CG  1 
ATOM   1161  C  CD1 . LEU   A  1 143 ? 36.384 -8.399  13.099  1.00 24.05 ? 143  LEU   A CD1 1 
ATOM   1162  C  CD2 . LEU   A  1 143 ? 34.882 -10.004 11.948  1.00 22.53 ? 143  LEU   A CD2 1 
ATOM   1163  N  N   . GLY   A  1 144 ? 39.567 -7.813  10.579  1.00 17.83 ? 144  GLY   A N   1 
ATOM   1164  C  CA  . GLY   A  1 144 ? 40.836 -8.433  10.259  1.00 19.81 ? 144  GLY   A CA  1 
ATOM   1165  C  C   . GLY   A  1 144 ? 41.169 -9.485  11.293  1.00 19.31 ? 144  GLY   A C   1 
ATOM   1166  O  O   . GLY   A  1 144 ? 40.983 -9.264  12.490  1.00 19.39 ? 144  GLY   A O   1 
ATOM   1167  N  N   . ILE   A  1 145 ? 41.585 -10.657 10.803  1.00 17.83 ? 145  ILE   A N   1 
ATOM   1168  C  CA  . ILE   A  1 145 ? 41.877 -11.821 11.639  1.00 19.89 ? 145  ILE   A CA  1 
ATOM   1169  C  C   . ILE   A  1 145 ? 43.224 -12.407 11.234  1.00 19.84 ? 145  ILE   A C   1 
ATOM   1170  O  O   . ILE   A  1 145 ? 43.451 -12.679 10.047  1.00 20.58 ? 145  ILE   A O   1 
ATOM   1171  C  CB  . ILE   A  1 145 ? 40.780 -12.891 11.506  1.00 20.55 ? 145  ILE   A CB  1 
ATOM   1172  C  CG1 . ILE   A  1 145 ? 39.430 -12.257 11.878  1.00 21.86 ? 145  ILE   A CG1 1 
ATOM   1173  C  CG2 . ILE   A  1 145 ? 41.134 -14.137 12.385  1.00 20.65 ? 145  ILE   A CG2 1 
ATOM   1174  C  CD1 . ILE   A  1 145 ? 38.180 -13.170 11.766  1.00 23.63 ? 145  ILE   A CD1 1 
ATOM   1175  N  N   . PHE   A  1 146 ? 44.107 -12.593 12.207  1.00 20.16 ? 146  PHE   A N   1 
ATOM   1176  C  CA  . PHE   A  1 146 ? 45.427 -13.156 11.947  1.00 19.83 ? 146  PHE   A CA  1 
ATOM   1177  C  C   . PHE   A  1 146 ? 45.372 -14.678 11.844  1.00 22.38 ? 146  PHE   A C   1 
ATOM   1178  O  O   . PHE   A  1 146 ? 44.613 -15.333 12.561  1.00 21.77 ? 146  PHE   A O   1 
ATOM   1179  C  CB  . PHE   A  1 146 ? 46.391 -12.780 13.068  1.00 19.41 ? 146  PHE   A CB  1 
ATOM   1180  C  CG  . PHE   A  1 146 ? 46.638 -11.312 13.193  1.00 18.93 ? 146  PHE   A CG  1 
ATOM   1181  C  CD1 . PHE   A  1 146 ? 47.249 -10.625 12.147  1.00 19.55 ? 146  PHE   A CD1 1 
ATOM   1182  C  CD2 . PHE   A  1 146 ? 46.259 -10.628 14.335  1.00 20.04 ? 146  PHE   A CD2 1 
ATOM   1183  C  CE1 . PHE   A  1 146 ? 47.503 -9.275  12.243  1.00 21.40 ? 146  PHE   A CE1 1 
ATOM   1184  C  CE2 . PHE   A  1 146 ? 46.501 -9.255  14.475  1.00 20.20 ? 146  PHE   A CE2 1 
ATOM   1185  C  CZ  . PHE   A  1 146 ? 47.146 -8.565  13.410  1.00 20.70 ? 146  PHE   A CZ  1 
ATOM   1186  N  N   . LEU   A  1 147 ? 46.214 -15.242 10.964  1.00 20.92 ? 147  LEU   A N   1 
ATOM   1187  C  CA  . LEU   A  1 147 ? 46.385 -16.693 10.821  1.00 21.68 ? 147  LEU   A CA  1 
ATOM   1188  C  C   . LEU   A  1 147 ? 47.759 -17.073 11.343  1.00 21.95 ? 147  LEU   A C   1 
ATOM   1189  O  O   . LEU   A  1 147 ? 48.789 -16.618 10.810  1.00 23.40 ? 147  LEU   A O   1 
ATOM   1190  C  CB  . LEU   A  1 147 ? 46.254 -17.158 9.368   1.00 21.88 ? 147  LEU   A CB  1 
ATOM   1191  C  CG  . LEU   A  1 147 ? 44.824 -17.297 8.819   1.00 20.72 ? 147  LEU   A CG  1 
ATOM   1192  C  CD1 . LEU   A  1 147 ? 44.113 -15.940 8.742   1.00 22.16 ? 147  LEU   A CD1 1 
ATOM   1193  C  CD2 . LEU   A  1 147 ? 44.817 -17.978 7.412   1.00 21.81 ? 147  LEU   A CD2 1 
ATOM   1194  N  N   . LYS   A  1 148 ? 47.778 -17.942 12.344  1.00 23.54 ? 148  LYS   A N   1 
ATOM   1195  C  CA  . LYS   A  1 148 ? 49.008 -18.442 12.913  1.00 25.79 ? 148  LYS   A CA  1 
ATOM   1196  C  C   . LYS   A  1 148 ? 49.180 -19.899 12.528  1.00 28.53 ? 148  LYS   A C   1 
ATOM   1197  O  O   . LYS   A  1 148 ? 48.214 -20.659 12.557  1.00 32.03 ? 148  LYS   A O   1 
ATOM   1198  C  CB  . LYS   A  1 148 ? 48.948 -18.298 14.438  1.00 30.68 ? 148  LYS   A CB  1 
ATOM   1199  C  CG  . LYS   A  1 148 ? 50.127 -18.813 15.198  1.00 39.32 ? 148  LYS   A CG  1 
ATOM   1200  C  CD  . LYS   A  1 148 ? 49.780 -18.706 16.687  1.00 44.78 ? 148  LYS   A CD  1 
ATOM   1201  C  CE  . LYS   A  1 148 ? 48.438 -19.378 16.944  1.00 50.62 ? 148  LYS   A CE  1 
ATOM   1202  N  NZ  . LYS   A  1 148 ? 48.396 -20.797 16.411  1.00 56.01 ? 148  LYS   A NZ  1 
ATOM   1203  N  N   . VAL   A  1 149 ? 50.408 -20.292 12.194  1.00 26.50 ? 149  VAL   A N   1 
ATOM   1204  C  CA  . VAL   A  1 149 ? 50.691 -21.673 11.805  1.00 30.64 ? 149  VAL   A CA  1 
ATOM   1205  C  C   . VAL   A  1 149 ? 50.615 -22.601 13.015  1.00 30.90 ? 149  VAL   A C   1 
ATOM   1206  O  O   . VAL   A  1 149 ? 51.238 -22.359 14.062  1.00 34.26 ? 149  VAL   A O   1 
ATOM   1207  C  CB  . VAL   A  1 149 ? 52.065 -21.764 11.128  1.00 34.32 ? 149  VAL   A CB  1 
ATOM   1208  C  CG1 . VAL   A  1 149 ? 52.455 -23.217 10.908  1.00 36.07 ? 149  VAL   A CG1 1 
ATOM   1209  C  CG2 . VAL   A  1 149 ? 52.042 -21.030 9.818   1.00 33.44 ? 149  VAL   A CG2 1 
ATOM   1210  N  N   . GLY   A  1 150 ? 49.865 -23.683 12.863  1.00 30.03 ? 150  GLY   A N   1 
ATOM   1211  C  CA  . GLY   A  1 150 ? 49.675 -24.670 13.904  1.00 32.14 ? 150  GLY   A CA  1 
ATOM   1212  C  C   . GLY   A  1 150 ? 48.813 -25.781 13.356  1.00 31.72 ? 150  GLY   A C   1 
ATOM   1213  O  O   . GLY   A  1 150 ? 49.111 -26.296 12.273  1.00 32.06 ? 150  GLY   A O   1 
ATOM   1214  N  N   . SER   A  1 151 ? 47.763 -26.164 14.087  1.00 33.56 ? 151  SER   A N   1 
ATOM   1215  C  CA  A SER   A  1 151 ? 46.860 -27.216 13.640  0.42 32.68 ? 151  SER   A CA  1 
ATOM   1216  C  CA  B SER   A  1 151 ? 46.879 -27.224 13.622  0.58 32.51 ? 151  SER   A CA  1 
ATOM   1217  C  C   . SER   A  1 151 ? 46.033 -26.724 12.452  1.00 31.23 ? 151  SER   A C   1 
ATOM   1218  O  O   . SER   A  1 151 ? 45.768 -25.534 12.313  1.00 32.23 ? 151  SER   A O   1 
ATOM   1219  C  CB  A SER   A  1 151 ? 45.936 -27.632 14.783  0.42 34.55 ? 151  SER   A CB  1 
ATOM   1220  C  CB  B SER   A  1 151 ? 45.972 -27.701 14.748  0.58 34.68 ? 151  SER   A CB  1 
ATOM   1221  O  OG  A SER   A  1 151 ? 45.078 -26.558 15.149  0.42 34.89 ? 151  SER   A OG  1 
ATOM   1222  O  OG  B SER   A  1 151 ? 46.730 -28.260 15.791  0.58 36.84 ? 151  SER   A OG  1 
ATOM   1223  N  N   . ALA   A  1 152 ? 45.620 -27.665 11.609  1.00 33.52 ? 152  ALA   A N   1 
ATOM   1224  C  CA  . ALA   A  1 152 ? 44.773 -27.346 10.463  1.00 31.46 ? 152  ALA   A CA  1 
ATOM   1225  C  C   . ALA   A  1 152 ? 43.410 -26.848 10.941  1.00 33.14 ? 152  ALA   A C   1 
ATOM   1226  O  O   . ALA   A  1 152 ? 42.880 -27.324 11.951  1.00 35.78 ? 152  ALA   A O   1 
ATOM   1227  C  CB  . ALA   A  1 152 ? 44.612 -28.587 9.573   1.00 31.93 ? 152  ALA   A CB  1 
ATOM   1228  N  N   . LEU   A  1 153 ? 42.844 -25.879 10.213  1.00 29.66 ? 153  LEU   A N   1 
ATOM   1229  C  CA  . LEU   A  1 153 ? 41.551 -25.305 10.540  1.00 27.49 ? 153  LEU   A CA  1 
ATOM   1230  C  C   . LEU   A  1 153 ? 40.487 -25.957 9.676   1.00 26.03 ? 153  LEU   A C   1 
ATOM   1231  O  O   . LEU   A  1 153 ? 40.487 -25.740 8.448   1.00 26.02 ? 153  LEU   A O   1 
ATOM   1232  C  CB  . LEU   A  1 153 ? 41.551 -23.794 10.315  1.00 27.56 ? 153  LEU   A CB  1 
ATOM   1233  C  CG  . LEU   A  1 153 ? 40.313 -23.029 10.811  1.00 28.76 ? 153  LEU   A CG  1 
ATOM   1234  C  CD1 . LEU   A  1 153 ? 40.152 -23.127 12.354  1.00 31.57 ? 153  LEU   A CD1 1 
ATOM   1235  C  CD2 . LEU   A  1 153 ? 40.369 -21.584 10.389  1.00 27.75 ? 153  LEU   A CD2 1 
ATOM   1236  N  N   . PRO   A  1 154 ? 39.542 -26.677 10.243  1.00 27.11 ? 154  PRO   A N   1 
ATOM   1237  C  CA  . PRO   A  1 154 ? 38.559 -27.364 9.390   1.00 27.93 ? 154  PRO   A CA  1 
ATOM   1238  C  C   . PRO   A  1 154 ? 37.709 -26.378 8.628   1.00 28.87 ? 154  PRO   A C   1 
ATOM   1239  O  O   . PRO   A  1 154 ? 37.362 -26.648 7.474   1.00 30.31 ? 154  PRO   A O   1 
ATOM   1240  C  CB  . PRO   A  1 154 ? 37.745 -28.211 10.398  1.00 32.48 ? 154  PRO   A CB  1 
ATOM   1241  C  CG  . PRO   A  1 154 ? 38.666 -28.368 11.585  1.00 34.61 ? 154  PRO   A CG  1 
ATOM   1242  C  CD  . PRO   A  1 154 ? 39.403 -27.058 11.668  1.00 30.60 ? 154  PRO   A CD  1 
ATOM   1243  N  N   . GLY   A  1 155 ? 37.446 -25.200 9.214   1.00 28.81 ? 155  GLY   A N   1 
ATOM   1244  C  CA  . GLY   A  1 155 ? 36.635 -24.186 8.570   1.00 29.22 ? 155  GLY   A CA  1 
ATOM   1245  C  C   . GLY   A  1 155 ? 37.270 -23.583 7.343   1.00 25.55 ? 155  GLY   A C   1 
ATOM   1246  O  O   . GLY   A  1 155 ? 36.574 -22.944 6.549   1.00 27.35 ? 155  GLY   A O   1 
ATOM   1247  N  N   . LEU   A  1 156 ? 38.572 -23.777 7.169   1.00 23.60 ? 156  LEU   A N   1 
ATOM   1248  C  CA  . LEU   A  1 156 ? 39.260 -23.291 5.986   1.00 23.29 ? 156  LEU   A CA  1 
ATOM   1249  C  C   . LEU   A  1 156 ? 39.306 -24.329 4.860   1.00 25.51 ? 156  LEU   A C   1 
ATOM   1250  O  O   . LEU   A  1 156 ? 39.636 -23.974 3.723   1.00 23.75 ? 156  LEU   A O   1 
ATOM   1251  C  CB  . LEU   A  1 156 ? 40.691 -22.872 6.392   1.00 23.87 ? 156  LEU   A CB  1 
ATOM   1252  C  CG  . LEU   A  1 156 ? 41.579 -22.188 5.347   1.00 24.86 ? 156  LEU   A CG  1 
ATOM   1253  C  CD1 . LEU   A  1 156 ? 40.941 -20.900 4.858   1.00 22.69 ? 156  LEU   A CD1 1 
ATOM   1254  C  CD2 . LEU   A  1 156 ? 42.956 -21.924 5.955   1.00 23.93 ? 156  LEU   A CD2 1 
ATOM   1255  N  N   . GLN   A  1 157 ? 38.971 -25.592 5.126   1.00 26.85 ? 157  GLN   A N   1 
ATOM   1256  C  CA  . GLN   A  1 157 ? 39.314 -26.629 4.159   1.00 26.79 ? 157  GLN   A CA  1 
ATOM   1257  C  C   . GLN   A  1 157 ? 38.534 -26.448 2.851   1.00 27.45 ? 157  GLN   A C   1 
ATOM   1258  O  O   . GLN   A  1 157 ? 39.079 -26.663 1.765   1.00 25.79 ? 157  GLN   A O   1 
ATOM   1259  C  CB  . GLN   A  1 157 ? 39.096 -28.029 4.762   1.00 31.46 ? 157  GLN   A CB  1 
ATOM   1260  C  CG  . GLN   A  1 157 ? 39.875 -29.105 3.988   1.00 36.72 ? 157  GLN   A CG  1 
ATOM   1261  C  CD  . GLN   A  1 157 ? 41.397 -28.801 3.850   1.00 39.02 ? 157  GLN   A CD  1 
ATOM   1262  O  OE1 . GLN   A  1 157 ? 42.063 -28.372 4.803   1.00 38.48 ? 157  GLN   A OE1 1 
ATOM   1263  N  NE2 . GLN   A  1 157 ? 41.950 -29.091 2.683   1.00 35.71 ? 157  GLN   A NE2 1 
ATOM   1264  N  N   . LYS   A  1 158 ? 37.285 -25.990 2.918   1.00 25.40 ? 158  LYS   A N   1 
ATOM   1265  C  CA  . LYS   A  1 158 ? 36.521 -25.827 1.682   1.00 27.13 ? 158  LYS   A CA  1 
ATOM   1266  C  C   . LYS   A  1 158 ? 37.151 -24.769 0.780   1.00 23.69 ? 158  LYS   A C   1 
ATOM   1267  O  O   . LYS   A  1 158 ? 37.117 -24.863 -0.457  1.00 25.63 ? 158  LYS   A O   1 
ATOM   1268  C  CB  . LYS   A  1 158 ? 35.074 -25.450 2.001   1.00 28.55 ? 158  LYS   A CB  1 
ATOM   1269  C  CG  . LYS   A  1 158 ? 34.158 -25.461 0.744   1.00 31.36 ? 158  LYS   A CG  1 
ATOM   1270  C  CD  . LYS   A  1 158 ? 32.851 -24.744 1.031   1.00 34.14 ? 158  LYS   A CD  1 
ATOM   1271  C  CE  . LYS   A  1 158 ? 31.968 -24.593 -0.244  1.00 33.84 ? 158  LYS   A CE  1 
ATOM   1272  N  NZ  . LYS   A  1 158 ? 31.135 -25.790 -0.322  1.00 33.88 ? 158  LYS   A NZ  1 
ATOM   1273  N  N   . VAL   A  1 159 ? 37.716 -23.725 1.381   1.00 21.09 ? 159  VAL   A N   1 
ATOM   1274  C  CA  . VAL   A  1 159 ? 38.407 -22.724 0.590   1.00 19.28 ? 159  VAL   A CA  1 
ATOM   1275  C  C   . VAL   A  1 159 ? 39.629 -23.335 -0.076  1.00 22.43 ? 159  VAL   A C   1 
ATOM   1276  O  O   . VAL   A  1 159 ? 39.820 -23.228 -1.292  1.00 23.51 ? 159  VAL   A O   1 
ATOM   1277  C  CB  . VAL   A  1 159 ? 38.815 -21.550 1.491   1.00 20.31 ? 159  VAL   A CB  1 
ATOM   1278  C  CG1 . VAL   A  1 159 ? 39.727 -20.569 0.711   1.00 21.71 ? 159  VAL   A CG1 1 
ATOM   1279  C  CG2 . VAL   A  1 159 ? 37.592 -20.788 2.108   1.00 24.35 ? 159  VAL   A CG2 1 
ATOM   1280  N  N   . VAL   A  1 160 ? 40.503 -23.956 0.710   1.00 24.86 ? 160  VAL   A N   1 
ATOM   1281  C  CA  A VAL   A  1 160 ? 41.750 -24.511 0.178   0.44 27.58 ? 160  VAL   A CA  1 
ATOM   1282  C  CA  B VAL   A  1 160 ? 41.735 -24.396 0.077   0.56 27.25 ? 160  VAL   A CA  1 
ATOM   1283  C  C   . VAL   A  1 160 ? 41.466 -25.467 -0.967  1.00 29.43 ? 160  VAL   A C   1 
ATOM   1284  O  O   . VAL   A  1 160 ? 42.192 -25.526 -1.969  1.00 30.43 ? 160  VAL   A O   1 
ATOM   1285  C  CB  A VAL   A  1 160 ? 42.526 -25.207 1.316   0.44 31.54 ? 160  VAL   A CB  1 
ATOM   1286  C  CB  B VAL   A  1 160 ? 42.774 -24.831 1.129   0.56 31.21 ? 160  VAL   A CB  1 
ATOM   1287  C  CG1 A VAL   A  1 160 ? 43.476 -26.258 0.759   0.44 34.19 ? 160  VAL   A CG1 1 
ATOM   1288  C  CG1 B VAL   A  1 160 ? 43.223 -23.603 1.909   0.56 30.27 ? 160  VAL   A CG1 1 
ATOM   1289  C  CG2 A VAL   A  1 160 ? 43.273 -24.183 2.127   0.44 31.61 ? 160  VAL   A CG2 1 
ATOM   1290  C  CG2 B VAL   A  1 160 ? 42.205 -25.879 2.034   0.56 32.25 ? 160  VAL   A CG2 1 
ATOM   1291  N  N   . ASP   A  1 161 ? 40.397 -26.245 -0.828  1.00 28.20 ? 161  ASP   A N   1 
ATOM   1292  C  CA  . ASP   A  1 161 ? 40.113 -27.317 -1.769  1.00 31.49 ? 161  ASP   A CA  1 
ATOM   1293  C  C   . ASP   A  1 161 ? 39.733 -26.810 -3.154  1.00 31.38 ? 161  ASP   A C   1 
ATOM   1294  O  O   . ASP   A  1 161 ? 39.891 -27.561 -4.129  1.00 38.82 ? 161  ASP   A O   1 
ATOM   1295  C  CB  . ASP   A  1 161 ? 38.988 -28.209 -1.249  1.00 34.01 ? 161  ASP   A CB  1 
ATOM   1296  C  CG  . ASP   A  1 161 ? 39.446 -29.150 -0.124  1.00 35.98 ? 161  ASP   A CG  1 
ATOM   1297  O  OD1 . ASP   A  1 161 ? 40.679 -29.277 0.093   1.00 37.10 ? 161  ASP   A OD1 1 
ATOM   1298  O  OD2 . ASP   A  1 161 ? 38.560 -29.757 0.513   1.00 39.70 ? 161  ASP   A OD2 1 
ATOM   1299  N  N   . VAL   A  1 162 ? 39.221 -25.570 -3.270  1.00 25.55 ? 162  VAL   A N   1 
ATOM   1300  C  CA  . VAL   A  1 162 ? 38.748 -25.019 -4.543  1.00 26.54 ? 162  VAL   A CA  1 
ATOM   1301  C  C   . VAL   A  1 162 ? 39.824 -24.192 -5.253  1.00 23.82 ? 162  VAL   A C   1 
ATOM   1302  O  O   . VAL   A  1 162 ? 39.663 -23.855 -6.430  1.00 25.53 ? 162  VAL   A O   1 
ATOM   1303  C  CB  . VAL   A  1 162 ? 37.492 -24.135 -4.327  1.00 24.82 ? 162  VAL   A CB  1 
ATOM   1304  C  CG1 . VAL   A  1 162 ? 37.851 -22.755 -3.811  1.00 25.45 ? 162  VAL   A CG1 1 
ATOM   1305  C  CG2 . VAL   A  1 162 ? 36.628 -24.049 -5.593  1.00 28.67 ? 162  VAL   A CG2 1 
ATOM   1306  N  N   . LEU   A  1 163 ? 40.948 -23.920 -4.594  1.00 23.49 ? 163  LEU   A N   1 
ATOM   1307  C  CA  . LEU   A  1 163 ? 41.882 -22.960 -5.169  1.00 24.87 ? 163  LEU   A CA  1 
ATOM   1308  C  C   . LEU   A  1 163 ? 42.518 -23.464 -6.466  1.00 27.44 ? 163  LEU   A C   1 
ATOM   1309  O  O   . LEU   A  1 163 ? 42.852 -22.654 -7.348  1.00 24.17 ? 163  LEU   A O   1 
ATOM   1310  C  CB  . LEU   A  1 163 ? 42.960 -22.606 -4.161  1.00 24.07 ? 163  LEU   A CB  1 
ATOM   1311  C  CG  . LEU   A  1 163 ? 42.417 -21.903 -2.893  1.00 22.70 ? 163  LEU   A CG  1 
ATOM   1312  C  CD1 . LEU   A  1 163 ? 43.637 -21.549 -1.985  1.00 23.88 ? 163  LEU   A CD1 1 
ATOM   1313  C  CD2 . LEU   A  1 163 ? 41.638 -20.653 -3.249  1.00 22.51 ? 163  LEU   A CD2 1 
ATOM   1314  N  N   . ASP   A  1 164 ? 42.732 -24.784 -6.610  1.00 30.96 ? 164  ASP   A N   1 
ATOM   1315  C  CA  . ASP   A  1 164 ? 43.353 -25.251 -7.849  1.00 32.16 ? 164  ASP   A CA  1 
ATOM   1316  C  C   . ASP   A  1 164 ? 42.471 -25.025 -9.072  1.00 29.77 ? 164  ASP   A C   1 
ATOM   1317  O  O   . ASP   A  1 164 ? 42.978 -25.096 -10.199 1.00 32.08 ? 164  ASP   A O   1 
ATOM   1318  C  CB  . ASP   A  1 164 ? 43.727 -26.744 -7.750  1.00 43.70 ? 164  ASP   A CB  1 
ATOM   1319  C  CG  . ASP   A  1 164 ? 45.103 -26.972 -7.075  1.00 54.36 ? 164  ASP   A CG  1 
ATOM   1320  O  OD1 . ASP   A  1 164 ? 45.939 -26.031 -7.027  1.00 56.15 ? 164  ASP   A OD1 1 
ATOM   1321  O  OD2 . ASP   A  1 164 ? 45.349 -28.087 -6.559  1.00 59.32 ? 164  ASP   A OD2 1 
ATOM   1322  N  N   . SER   A  1 165 ? 41.188 -24.717 -8.882  1.00 28.04 ? 165  SER   A N   1 
ATOM   1323  C  CA  . SER   A  1 165 ? 40.307 -24.415 -9.991  1.00 28.24 ? 165  SER   A CA  1 
ATOM   1324  C  C   . SER   A  1 165 ? 40.302 -22.936 -10.384 1.00 25.26 ? 165  SER   A C   1 
ATOM   1325  O  O   . SER   A  1 165 ? 39.652 -22.581 -11.391 1.00 28.30 ? 165  SER   A O   1 
ATOM   1326  C  CB  . SER   A  1 165 ? 38.874 -24.876 -9.692  1.00 34.22 ? 165  SER   A CB  1 
ATOM   1327  O  OG  . SER   A  1 165 ? 38.241 -24.000 -8.786  1.00 34.08 ? 165  SER   A OG  1 
ATOM   1328  N  N   . ILE   A  1 166 ? 41.004 -22.074 -9.634  1.00 21.39 ? 166  ILE   A N   1 
ATOM   1329  C  CA  . ILE   A  1 166 ? 41.041 -20.650 -9.966  1.00 20.40 ? 166  ILE   A CA  1 
ATOM   1330  C  C   . ILE   A  1 166 ? 42.484 -20.153 -9.969  1.00 20.13 ? 166  ILE   A C   1 
ATOM   1331  O  O   . ILE   A  1 166 ? 42.790 -19.119 -9.373  1.00 18.04 ? 166  ILE   A O   1 
ATOM   1332  C  CB  . ILE   A  1 166 ? 40.155 -19.829 -9.009  1.00 19.07 ? 166  ILE   A CB  1 
ATOM   1333  C  CG1 . ILE   A  1 166 ? 40.515 -20.034 -7.525  1.00 17.92 ? 166  ILE   A CG1 1 
ATOM   1334  C  CG2 . ILE   A  1 166 ? 38.646 -20.211 -9.253  1.00 19.93 ? 166  ILE   A CG2 1 
ATOM   1335  C  CD1 . ILE   A  1 166 ? 40.084 -18.779 -6.662  1.00 18.19 ? 166  ILE   A CD1 1 
ATOM   1336  N  N   . LYS   A  1 167 ? 43.371 -20.862 -10.678 1.00 21.87 ? 167  LYS   A N   1 
ATOM   1337  C  CA  . LYS   A  1 167 ? 44.799 -20.640 -10.496 1.00 21.67 ? 167  LYS   A CA  1 
ATOM   1338  C  C   . LYS   A  1 167 ? 45.228 -19.279 -11.028 1.00 20.60 ? 167  LYS   A C   1 
ATOM   1339  O  O   . LYS   A  1 167 ? 46.149 -18.680 -10.487 1.00 21.07 ? 167  LYS   A O   1 
ATOM   1340  C  CB  . LYS   A  1 167 ? 45.603 -21.766 -11.196 1.00 22.88 ? 167  LYS   A CB  1 
ATOM   1341  C  CG  . LYS   A  1 167 ? 47.139 -21.603 -11.023 1.00 29.85 ? 167  LYS   A CG  1 
ATOM   1342  C  CD  . LYS   A  1 167 ? 47.902 -22.787 -11.721 1.00 35.16 ? 167  LYS   A CD  1 
ATOM   1343  C  CE  . LYS   A  1 167 ? 49.409 -22.648 -11.542 1.00 42.10 ? 167  LYS   A CE  1 
ATOM   1344  N  NZ  . LYS   A  1 167 ? 50.127 -23.679 -12.333 1.00 49.05 ? 167  LYS   A NZ  1 
ATOM   1345  N  N   . THR   A  1 168 ? 44.627 -18.810 -12.131 1.00 19.37 ? 168  THR   A N   1 
ATOM   1346  C  CA  . THR   A  1 168 ? 45.088 -17.578 -12.770 1.00 18.84 ? 168  THR   A CA  1 
ATOM   1347  C  C   . THR   A  1 168 ? 44.048 -16.467 -12.731 1.00 19.68 ? 168  THR   A C   1 
ATOM   1348  O  O   . THR   A  1 168 ? 42.849 -16.684 -12.491 1.00 17.87 ? 168  THR   A O   1 
ATOM   1349  C  CB  . THR   A  1 168 ? 45.493 -17.892 -14.238 1.00 20.88 ? 168  THR   A CB  1 
ATOM   1350  O  OG1 . THR   A  1 168 ? 44.425 -18.600 -14.858 1.00 22.65 ? 168  THR   A OG1 1 
ATOM   1351  C  CG2 . THR   A  1 168 ? 46.727 -18.799 -14.255 1.00 23.04 ? 168  THR   A CG2 1 
ATOM   1352  N  N   . LYS   A  1 169 ? 44.539 -15.245 -12.985 1.00 20.45 ? 169  LYS   A N   1 
ATOM   1353  C  CA  . LYS   A  1 169 ? 43.697 -14.065 -12.911 1.00 20.06 ? 169  LYS   A CA  1 
ATOM   1354  C  C   . LYS   A  1 169 ? 42.433 -14.199 -13.753 1.00 19.62 ? 169  LYS   A C   1 
ATOM   1355  O  O   . LYS   A  1 169 ? 42.482 -14.558 -14.946 1.00 19.43 ? 169  LYS   A O   1 
ATOM   1356  C  CB  . LYS   A  1 169 ? 44.469 -12.815 -13.378 1.00 19.20 ? 169  LYS   A CB  1 
ATOM   1357  C  CG  . LYS   A  1 169 ? 43.626 -11.573 -13.283 1.00 18.27 ? 169  LYS   A CG  1 
ATOM   1358  C  CD  . LYS   A  1 169 ? 44.436 -10.299 -13.673 1.00 19.58 ? 169  LYS   A CD  1 
ATOM   1359  C  CE  . LYS   A  1 169 ? 43.518 -9.054  -13.578 1.00 22.13 ? 169  LYS   A CE  1 
ATOM   1360  N  NZ  . LYS   A  1 169 ? 44.313 -7.764  -13.802 1.00 26.81 ? 169  LYS   A NZ  1 
ATOM   1361  N  N   . GLY   A  1 170 ? 41.305 -13.832 -13.137 1.00 19.19 ? 170  GLY   A N   1 
ATOM   1362  C  CA  . GLY   A  1 170 ? 40.026 -13.809 -13.813 1.00 19.50 ? 170  GLY   A CA  1 
ATOM   1363  C  C   . GLY   A  1 170 ? 39.223 -15.091 -13.654 1.00 19.74 ? 170  GLY   A C   1 
ATOM   1364  O  O   . GLY   A  1 170 ? 38.020 -15.097 -13.970 1.00 21.93 ? 170  GLY   A O   1 
ATOM   1365  N  N   . LYS   A  1 171 ? 39.856 -16.185 -13.207 1.00 18.21 ? 171  LYS   A N   1 
ATOM   1366  C  CA  . LYS   A  1 171 ? 39.124 -17.432 -13.065 1.00 18.50 ? 171  LYS   A CA  1 
ATOM   1367  C  C   . LYS   A  1 171 ? 38.235 -17.337 -11.840 1.00 18.83 ? 171  LYS   A C   1 
ATOM   1368  O  O   . LYS   A  1 171 ? 38.612 -16.731 -10.828 1.00 19.33 ? 171  LYS   A O   1 
ATOM   1369  C  CB  . LYS   A  1 171 ? 40.044 -18.645 -12.927 1.00 20.62 ? 171  LYS   A CB  1 
ATOM   1370  C  CG  . LYS   A  1 171 ? 40.863 -18.921 -14.173 1.00 21.49 ? 171  LYS   A CG  1 
ATOM   1371  C  CD  . LYS   A  1 171 ? 41.448 -20.337 -14.152 1.00 27.80 ? 171  LYS   A CD  1 
ATOM   1372  C  CE  . LYS   A  1 171 ? 40.391 -21.417 -14.382 1.00 28.95 ? 171  LYS   A CE  1 
ATOM   1373  N  NZ  . LYS   A  1 171 ? 40.972 -22.812 -14.446 1.00 33.77 ? 171  LYS   A NZ  1 
ATOM   1374  N  N   . SER   A  1 172 ? 37.048 -17.933 -11.947 1.00 19.76 ? 172  SER   A N   1 
ATOM   1375  C  CA  A SER   A  1 172 ? 36.114 -17.946 -10.837 0.53 17.89 ? 172  SER   A CA  1 
ATOM   1376  C  CA  B SER   A  1 172 ? 36.017 -17.898 -10.913 0.47 17.69 ? 172  SER   A CA  1 
ATOM   1377  C  C   . SER   A  1 172 ? 35.416 -19.295 -10.787 1.00 22.08 ? 172  SER   A C   1 
ATOM   1378  O  O   . SER   A  1 172 ? 35.487 -20.105 -11.728 1.00 27.24 ? 172  SER   A O   1 
ATOM   1379  C  CB  A SER   A  1 172 ? 35.096 -16.821 -10.948 0.53 19.53 ? 172  SER   A CB  1 
ATOM   1380  C  CB  B SER   A  1 172 ? 34.933 -16.845 -11.249 0.47 19.54 ? 172  SER   A CB  1 
ATOM   1381  O  OG  A SER   A  1 172 ? 34.334 -17.029 -12.121 0.53 20.50 ? 172  SER   A OG  1 
ATOM   1382  O  OG  B SER   A  1 172 ? 33.909 -16.740 -10.267 0.47 17.67 ? 172  SER   A OG  1 
ATOM   1383  N  N   . ALA   A  1 173 ? 34.798 -19.566 -9.645  1.00 19.56 ? 173  ALA   A N   1 
ATOM   1384  C  CA  . ALA   A  1 173 ? 34.066 -20.822 -9.474  1.00 19.94 ? 173  ALA   A CA  1 
ATOM   1385  C  C   . ALA   A  1 173 ? 32.892 -20.576 -8.542  1.00 17.40 ? 173  ALA   A C   1 
ATOM   1386  O  O   . ALA   A  1 173 ? 32.981 -19.748 -7.631  1.00 19.29 ? 173  ALA   A O   1 
ATOM   1387  C  CB  . ALA   A  1 173 ? 34.960 -21.941 -8.901  1.00 22.43 ? 173  ALA   A CB  1 
ATOM   1388  N  N   . ASP   A  1 174 ? 31.800 -21.350 -8.729  1.00 19.15 ? 174  ASP   A N   1 
ATOM   1389  C  CA  . ASP   A  1 174 ? 30.740 -21.323 -7.729  1.00 19.65 ? 174  ASP   A CA  1 
ATOM   1390  C  C   . ASP   A  1 174 ? 31.303 -21.715 -6.362  1.00 21.61 ? 174  ASP   A C   1 
ATOM   1391  O  O   . ASP   A  1 174 ? 32.150 -22.606 -6.261  1.00 21.34 ? 174  ASP   A O   1 
ATOM   1392  C  CB  . ASP   A  1 174 ? 29.641 -22.328 -8.063  1.00 20.73 ? 174  ASP   A CB  1 
ATOM   1393  C  CG  . ASP   A  1 174 ? 28.997 -22.105 -9.420  1.00 25.24 ? 174  ASP   A CG  1 
ATOM   1394  O  OD1 . ASP   A  1 174 ? 28.962 -20.981 -9.868  1.00 24.73 ? 174  ASP   A OD1 1 
ATOM   1395  O  OD2 . ASP   A  1 174 ? 28.459 -23.106 -9.954  1.00 31.13 ? 174  ASP   A OD2 1 
ATOM   1396  N  N   . PHE   A  1 175 ? 30.784 -21.088 -5.319  1.00 18.87 ? 175  PHE   A N   1 
ATOM   1397  C  CA  . PHE   A  1 175 ? 31.322 -21.339 -3.978  1.00 18.91 ? 175  PHE   A CA  1 
ATOM   1398  C  C   . PHE   A  1 175 ? 30.162 -21.092 -3.016  1.00 18.09 ? 175  PHE   A C   1 
ATOM   1399  O  O   . PHE   A  1 175 ? 29.997 -19.988 -2.463  1.00 20.96 ? 175  PHE   A O   1 
ATOM   1400  C  CB  . PHE   A  1 175 ? 32.516 -20.449 -3.684  1.00 19.12 ? 175  PHE   A CB  1 
ATOM   1401  C  CG  . PHE   A  1 175 ? 33.313 -20.899 -2.480  1.00 20.15 ? 175  PHE   A CG  1 
ATOM   1402  C  CD1 . PHE   A  1 175 ? 34.123 -22.022 -2.584  1.00 22.74 ? 175  PHE   A CD1 1 
ATOM   1403  C  CD2 . PHE   A  1 175 ? 33.195 -20.247 -1.264  1.00 19.46 ? 175  PHE   A CD2 1 
ATOM   1404  C  CE1 . PHE   A  1 175 ? 34.894 -22.455 -1.471  1.00 24.67 ? 175  PHE   A CE1 1 
ATOM   1405  C  CE2 . PHE   A  1 175 ? 33.960 -20.691 -0.148  1.00 20.26 ? 175  PHE   A CE2 1 
ATOM   1406  C  CZ  . PHE   A  1 175 ? 34.778 -21.772 -0.255  1.00 23.00 ? 175  PHE   A CZ  1 
ATOM   1407  N  N   . THR   A  1 176 ? 29.409 -22.145 -2.770  1.00 19.11 ? 176  THR   A N   1 
ATOM   1408  C  CA  . THR   A  1 176 ? 28.128 -22.034 -2.094  1.00 19.65 ? 176  THR   A CA  1 
ATOM   1409  C  C   . THR   A  1 176 ? 28.154 -22.722 -0.731  1.00 23.91 ? 176  THR   A C   1 
ATOM   1410  O  O   . THR   A  1 176 ? 29.021 -23.543 -0.428  1.00 24.46 ? 176  THR   A O   1 
ATOM   1411  C  CB  . THR   A  1 176 ? 27.005 -22.618 -2.950  1.00 20.48 ? 176  THR   A CB  1 
ATOM   1412  O  OG1 . THR   A  1 176 ? 27.320 -23.963 -3.271  1.00 23.14 ? 176  THR   A OG1 1 
ATOM   1413  C  CG2 . THR   A  1 176 ? 26.908 -21.827 -4.263  1.00 22.79 ? 176  THR   A CG2 1 
ATOM   1414  N  N   . ASN   A  1 177 ? 27.233 -22.294 0.117   1.00 24.06 ? 177  ASN   A N   1 
ATOM   1415  C  CA  . ASN   A  1 177 ? 27.033 -22.911 1.429   1.00 25.90 ? 177  ASN   A CA  1 
ATOM   1416  C  C   . ASN   A  1 177 ? 28.273 -22.806 2.328   1.00 26.99 ? 177  ASN   A C   1 
ATOM   1417  O  O   . ASN   A  1 177 ? 28.468 -23.652 3.219   1.00 30.29 ? 177  ASN   A O   1 
ATOM   1418  C  CB  . ASN   A  1 177 ? 26.602 -24.383 1.257   1.00 29.05 ? 177  ASN   A CB  1 
ATOM   1419  C  CG  . ASN   A  1 177 ? 25.386 -24.536 0.292   1.00 31.16 ? 177  ASN   A CG  1 
ATOM   1420  O  OD1 . ASN   A  1 177 ? 25.396 -25.279 -0.739  1.00 32.91 ? 177  ASN   A OD1 1 
ATOM   1421  N  ND2 . ASN   A  1 177 ? 24.326 -23.835 0.641   1.00 28.85 ? 177  ASN   A ND2 1 
ATOM   1422  N  N   . PHE   A  1 178 ? 29.085 -21.766 2.177   1.00 24.03 ? 178  PHE   A N   1 
ATOM   1423  C  CA  . PHE   A  1 178 ? 30.258 -21.597 3.024   1.00 22.48 ? 178  PHE   A CA  1 
ATOM   1424  C  C   . PHE   A  1 178 ? 29.880 -20.794 4.265   1.00 25.67 ? 178  PHE   A C   1 
ATOM   1425  O  O   . PHE   A  1 178 ? 29.285 -19.718 4.165   1.00 26.33 ? 178  PHE   A O   1 
ATOM   1426  C  CB  . PHE   A  1 178 ? 31.399 -20.884 2.295   1.00 22.61 ? 178  PHE   A CB  1 
ATOM   1427  C  CG  . PHE   A  1 178 ? 32.625 -20.770 3.155   1.00 22.04 ? 178  PHE   A CG  1 
ATOM   1428  C  CD1 . PHE   A  1 178 ? 33.366 -21.906 3.451   1.00 26.07 ? 178  PHE   A CD1 1 
ATOM   1429  C  CD2 . PHE   A  1 178 ? 32.959 -19.579 3.735   1.00 20.62 ? 178  PHE   A CD2 1 
ATOM   1430  C  CE1 . PHE   A  1 178 ? 34.493 -21.794 4.313   1.00 26.30 ? 178  PHE   A CE1 1 
ATOM   1431  C  CE2 . PHE   A  1 178 ? 34.061 -19.471 4.571   1.00 22.50 ? 178  PHE   A CE2 1 
ATOM   1432  C  CZ  . PHE   A  1 178 ? 34.817 -20.582 4.846   1.00 22.12 ? 178  PHE   A CZ  1 
ATOM   1433  N  N   . ASP   A  1 179 ? 30.280 -21.300 5.437   1.00 26.06 ? 179  ASP   A N   1 
ATOM   1434  C  CA  . ASP   A  1 179 ? 29.998 -20.662 6.714   1.00 24.75 ? 179  ASP   A CA  1 
ATOM   1435  C  C   . ASP   A  1 179 ? 31.192 -19.820 7.163   1.00 25.52 ? 179  ASP   A C   1 
ATOM   1436  O  O   . ASP   A  1 179 ? 32.180 -20.383 7.661   1.00 25.13 ? 179  ASP   A O   1 
ATOM   1437  C  CB  . ASP   A  1 179 ? 29.709 -21.768 7.740   1.00 23.60 ? 179  ASP   A CB  1 
ATOM   1438  C  CG  . ASP   A  1 179 ? 29.399 -21.238 9.106   1.00 27.82 ? 179  ASP   A CG  1 
ATOM   1439  O  OD1 . ASP   A  1 179 ? 29.325 -19.980 9.241   1.00 26.19 ? 179  ASP   A OD1 1 
ATOM   1440  O  OD2 . ASP   A  1 179 ? 29.242 -22.096 10.023  1.00 33.67 ? 179  ASP   A OD2 1 
ATOM   1441  N  N   . PRO   A  1 180 ? 31.167 -18.484 7.041   1.00 22.81 ? 180  PRO   A N   1 
ATOM   1442  C  CA  . PRO   A  1 180 ? 32.343 -17.701 7.487   1.00 23.78 ? 180  PRO   A CA  1 
ATOM   1443  C  C   . PRO   A  1 180 ? 32.535 -17.715 8.997   1.00 23.43 ? 180  PRO   A C   1 
ATOM   1444  O  O   . PRO   A  1 180 ? 33.615 -17.318 9.455   1.00 23.61 ? 180  PRO   A O   1 
ATOM   1445  C  CB  . PRO   A  1 180 ? 32.068 -16.282 6.961   1.00 22.61 ? 180  PRO   A CB  1 
ATOM   1446  C  CG  . PRO   A  1 180 ? 30.536 -16.239 6.900   1.00 25.50 ? 180  PRO   A CG  1 
ATOM   1447  C  CD  . PRO   A  1 180 ? 30.088 -17.637 6.496   1.00 24.33 ? 180  PRO   A CD  1 
ATOM   1448  N  N   . ARG   A  1 181 ? 31.560 -18.199 9.784   1.00 24.49 ? 181  ARG   A N   1 
ATOM   1449  C  CA  . ARG   A  1 181 ? 31.812 -18.310 11.220  1.00 26.12 ? 181  ARG   A CA  1 
ATOM   1450  C  C   . ARG   A  1 181 ? 32.946 -19.273 11.516  1.00 23.84 ? 181  ARG   A C   1 
ATOM   1451  O  O   . ARG   A  1 181 ? 33.581 -19.176 12.589  1.00 25.70 ? 181  ARG   A O   1 
ATOM   1452  C  CB  . ARG   A  1 181 ? 30.540 -18.740 11.938  1.00 29.51 ? 181  ARG   A CB  1 
ATOM   1453  C  CG  . ARG   A  1 181 ? 29.434 -17.727 11.845  1.00 28.82 ? 181  ARG   A CG  1 
ATOM   1454  C  CD  . ARG   A  1 181 ? 28.148 -18.302 12.364  1.00 29.42 ? 181  ARG   A CD  1 
ATOM   1455  N  NE  . ARG   A  1 181 ? 27.850 -19.520 11.634  1.00 33.08 ? 181  ARG   A NE  1 
ATOM   1456  C  CZ  . ARG   A  1 181 ? 26.894 -20.359 11.987  1.00 37.88 ? 181  ARG   A CZ  1 
ATOM   1457  N  NH1 . ARG   A  1 181 ? 26.155 -20.069 13.051  1.00 43.04 ? 181  ARG   A NH1 1 
ATOM   1458  N  NH2 . ARG   A  1 181 ? 26.685 -21.468 11.292  1.00 38.10 ? 181  ARG   A NH2 1 
ATOM   1459  N  N   . GLY   A  1 182 ? 33.195 -20.223 10.619  1.00 27.00 ? 182  GLY   A N   1 
ATOM   1460  C  CA  . GLY   A  1 182 ? 34.279 -21.152 10.859  1.00 26.62 ? 182  GLY   A CA  1 
ATOM   1461  C  C   . GLY   A  1 182 ? 35.664 -20.539 10.747  1.00 26.02 ? 182  GLY   A C   1 
ATOM   1462  O  O   . GLY   A  1 182 ? 36.653 -21.220 11.072  1.00 27.84 ? 182  GLY   A O   1 
ATOM   1463  N  N   . LEU   A  1 183 ? 35.761 -19.271 10.324  1.00 25.54 ? 183  LEU   A N   1 
ATOM   1464  C  CA  . LEU   A  1 183 ? 37.032 -18.556 10.235  1.00 21.85 ? 183  LEU   A CA  1 
ATOM   1465  C  C   . LEU   A  1 183 ? 37.231 -17.569 11.378  1.00 23.43 ? 183  LEU   A C   1 
ATOM   1466  O  O   . LEU   A  1 183 ? 38.197 -16.804 11.352  1.00 23.91 ? 183  LEU   A O   1 
ATOM   1467  C  CB  . LEU   A  1 183 ? 37.135 -17.810 8.896   1.00 21.32 ? 183  LEU   A CB  1 
ATOM   1468  C  CG  . LEU   A  1 183 ? 37.054 -18.728 7.657   1.00 22.33 ? 183  LEU   A CG  1 
ATOM   1469  C  CD1 . LEU   A  1 183 ? 37.084 -17.885 6.405   1.00 22.07 ? 183  LEU   A CD1 1 
ATOM   1470  C  CD2 . LEU   A  1 183 ? 38.176 -19.778 7.657   1.00 24.20 ? 183  LEU   A CD2 1 
ATOM   1471  N  N   . LEU   A  1 184 ? 36.352 -17.580 12.389  1.00 24.37 ? 184  LEU   A N   1 
ATOM   1472  C  CA  . LEU   A  1 184 ? 36.419 -16.674 13.540  1.00 24.84 ? 184  LEU   A CA  1 
ATOM   1473  C  C   . LEU   A  1 184 ? 37.050 -17.374 14.735  1.00 24.47 ? 184  LEU   A C   1 
ATOM   1474  O  O   . LEU   A  1 184 ? 36.760 -18.552 14.998  1.00 27.13 ? 184  LEU   A O   1 
ATOM   1475  C  CB  . LEU   A  1 184 ? 35.028 -16.183 13.960  1.00 26.17 ? 184  LEU   A CB  1 
ATOM   1476  C  CG  . LEU   A  1 184 ? 34.186 -15.502 12.865  1.00 28.86 ? 184  LEU   A CG  1 
ATOM   1477  C  CD1 . LEU   A  1 184 ? 32.808 -15.179 13.465  1.00 29.01 ? 184  LEU   A CD1 1 
ATOM   1478  C  CD2 . LEU   A  1 184 ? 34.891 -14.249 12.406  1.00 28.03 ? 184  LEU   A CD2 1 
ATOM   1479  N  N   . PRO   A  1 185 ? 37.854 -16.655 15.510  1.00 24.72 ? 185  PRO   A N   1 
ATOM   1480  C  CA  . PRO   A  1 185 ? 38.338 -17.192 16.786  1.00 26.51 ? 185  PRO   A CA  1 
ATOM   1481  C  C   . PRO   A  1 185 ? 37.239 -17.160 17.844  1.00 27.75 ? 185  PRO   A C   1 
ATOM   1482  O  O   . PRO   A  1 185 ? 36.178 -16.562 17.665  1.00 29.53 ? 185  PRO   A O   1 
ATOM   1483  C  CB  . PRO   A  1 185 ? 39.471 -16.220 17.176  1.00 24.65 ? 185  PRO   A CB  1 
ATOM   1484  C  CG  . PRO   A  1 185 ? 38.995 -14.864 16.633  1.00 24.89 ? 185  PRO   A CG  1 
ATOM   1485  C  CD  . PRO   A  1 185 ? 38.234 -15.229 15.299  1.00 23.52 ? 185  PRO   A CD  1 
ATOM   1486  N  N   . GLU   A  1 186 ? 37.521 -17.791 18.987  1.00 27.88 ? 186  GLU   A N   1 
ATOM   1487  C  CA  . GLU   A  1 186 ? 36.514 -17.817 20.037  1.00 32.55 ? 186  GLU   A CA  1 
ATOM   1488  C  C   . GLU   A  1 186 ? 36.306 -16.438 20.663  1.00 32.79 ? 186  GLU   A C   1 
ATOM   1489  O  O   . GLU   A  1 186 ? 35.172 -16.074 20.996  1.00 33.30 ? 186  GLU   A O   1 
ATOM   1490  C  CB  . GLU   A  1 186 ? 36.906 -18.845 21.091  1.00 38.44 ? 186  GLU   A CB  1 
ATOM   1491  C  CG  . GLU   A  1 186 ? 35.914 -18.957 22.245  1.00 50.12 ? 186  GLU   A CG  1 
ATOM   1492  C  CD  . GLU   A  1 186 ? 36.144 -20.188 23.143  1.00 60.06 ? 186  GLU   A CD  1 
ATOM   1493  O  OE1 . GLU   A  1 186 ? 35.202 -20.547 23.887  1.00 64.00 ? 186  GLU   A OE1 1 
ATOM   1494  O  OE2 . GLU   A  1 186 ? 37.243 -20.802 23.103  1.00 62.59 ? 186  GLU   A OE2 1 
ATOM   1495  N  N   . SER   A  1 187 ? 37.384 -15.681 20.889  1.00 28.07 ? 187  SER   A N   1 
ATOM   1496  C  CA  . SER   A  1 187 ? 37.276 -14.356 21.493  1.00 29.69 ? 187  SER   A CA  1 
ATOM   1497  C  C   . SER   A  1 187 ? 37.129 -13.293 20.420  1.00 29.00 ? 187  SER   A C   1 
ATOM   1498  O  O   . SER   A  1 187 ? 37.856 -13.310 19.433  1.00 26.59 ? 187  SER   A O   1 
ATOM   1499  C  CB  . SER   A  1 187 ? 38.517 -14.026 22.304  1.00 29.24 ? 187  SER   A CB  1 
ATOM   1500  O  OG  . SER   A  1 187 ? 38.418 -12.689 22.827  1.00 31.53 ? 187  SER   A OG  1 
ATOM   1501  N  N   . LEU   A  1 188 ? 36.244 -12.327 20.664  1.00 29.96 ? 188  LEU   A N   1 
ATOM   1502  C  CA  . LEU   A  1 188 ? 36.097 -11.202 19.750  1.00 28.26 ? 188  LEU   A CA  1 
ATOM   1503  C  C   . LEU   A  1 188 ? 36.703 -9.918  20.314  1.00 28.03 ? 188  LEU   A C   1 
ATOM   1504  O  O   . LEU   A  1 188 ? 36.419 -8.836  19.794  1.00 30.46 ? 188  LEU   A O   1 
ATOM   1505  C  CB  . LEU   A  1 188 ? 34.627 -10.990 19.367  1.00 29.63 ? 188  LEU   A CB  1 
ATOM   1506  C  CG  . LEU   A  1 188 ? 33.928 -12.150 18.658  1.00 31.50 ? 188  LEU   A CG  1 
ATOM   1507  C  CD1 . LEU   A  1 188 ? 32.493 -11.781 18.301  1.00 33.23 ? 188  LEU   A CD1 1 
ATOM   1508  C  CD2 . LEU   A  1 188 ? 34.680 -12.540 17.388  1.00 28.35 ? 188  LEU   A CD2 1 
ATOM   1509  N  N   . ASP   A  1 189 ? 37.580 -10.026 21.316  1.00 25.20 ? 189  ASP   A N   1 
ATOM   1510  C  CA  . ASP   A  1 189 ? 38.413 -8.892  21.732  1.00 26.05 ? 189  ASP   A CA  1 
ATOM   1511  C  C   . ASP   A  1 189 ? 39.129 -8.306  20.523  1.00 24.22 ? 189  ASP   A C   1 
ATOM   1512  O  O   . ASP   A  1 189 ? 39.610 -9.043  19.653  1.00 23.40 ? 189  ASP   A O   1 
ATOM   1513  C  CB  . ASP   A  1 189 ? 39.461 -9.356  22.743  1.00 26.40 ? 189  ASP   A CB  1 
ATOM   1514  C  CG  . ASP   A  1 189 ? 38.877 -9.646  24.125  1.00 31.10 ? 189  ASP   A CG  1 
ATOM   1515  O  OD1 . ASP   A  1 189 ? 37.669 -9.437  24.343  1.00 34.88 ? 189  ASP   A OD1 1 
ATOM   1516  O  OD2 . ASP   A  1 189 ? 39.626 -10.112 25.004  1.00 33.37 ? 189  ASP   A OD2 1 
ATOM   1517  N  N   . TYR   A  1 190 ? 39.196 -6.973  20.439  1.00 21.32 ? 190  TYR   A N   1 
ATOM   1518  C  CA  . TYR   A  1 190 ? 39.741 -6.388  19.211  1.00 20.54 ? 190  TYR   A CA  1 
ATOM   1519  C  C   . TYR   A  1 190 ? 40.396 -5.037  19.480  1.00 22.12 ? 190  TYR   A C   1 
ATOM   1520  O  O   . TYR   A  1 190 ? 40.226 -4.425  20.542  1.00 23.29 ? 190  TYR   A O   1 
ATOM   1521  C  CB  . TYR   A  1 190 ? 38.657 -6.220  18.124  1.00 20.37 ? 190  TYR   A CB  1 
ATOM   1522  C  CG  . TYR   A  1 190 ? 37.559 -5.242  18.531  1.00 21.96 ? 190  TYR   A CG  1 
ATOM   1523  C  CD1 . TYR   A  1 190 ? 37.722 -3.866  18.324  1.00 23.49 ? 190  TYR   A CD1 1 
ATOM   1524  C  CD2 . TYR   A  1 190 ? 36.380 -5.676  19.140  1.00 21.84 ? 190  TYR   A CD2 1 
ATOM   1525  C  CE1 . TYR   A  1 190 ? 36.713 -2.938  18.721  1.00 24.87 ? 190  TYR   A CE1 1 
ATOM   1526  C  CE2 . TYR   A  1 190 ? 35.366 -4.753  19.528  1.00 23.84 ? 190  TYR   A CE2 1 
ATOM   1527  C  CZ  . TYR   A  1 190 ? 35.535 -3.386  19.305  1.00 23.51 ? 190  TYR   A CZ  1 
ATOM   1528  O  OH  . TYR   A  1 190 ? 34.551 -2.471  19.784  1.00 26.22 ? 190  TYR   A OH  1 
ATOM   1529  N  N   . TRP   A  1 191 ? 41.207 -4.615  18.504  1.00 22.01 ? 191  TRP   A N   1 
ATOM   1530  C  CA  . TRP   A  1 191 ? 41.703 -3.251  18.383  1.00 20.66 ? 191  TRP   A CA  1 
ATOM   1531  C  C   . TRP   A  1 191 ? 40.986 -2.561  17.228  1.00 20.97 ? 191  TRP   A C   1 
ATOM   1532  O  O   . TRP   A  1 191 ? 40.637 -3.212  16.226  1.00 19.79 ? 191  TRP   A O   1 
ATOM   1533  C  CB  . TRP   A  1 191 ? 43.212 -3.243  18.130  1.00 21.92 ? 191  TRP   A CB  1 
ATOM   1534  C  CG  . TRP   A  1 191 ? 44.027 -3.856  19.192  1.00 21.09 ? 191  TRP   A CG  1 
ATOM   1535  C  CD1 . TRP   A  1 191 ? 44.348 -3.296  20.393  1.00 22.13 ? 191  TRP   A CD1 1 
ATOM   1536  C  CD2 . TRP   A  1 191 ? 44.719 -5.125  19.152  1.00 21.82 ? 191  TRP   A CD2 1 
ATOM   1537  N  NE1 . TRP   A  1 191 ? 45.157 -4.143  21.126  1.00 26.60 ? 191  TRP   A NE1 1 
ATOM   1538  C  CE2 . TRP   A  1 191 ? 45.437 -5.249  20.369  1.00 24.27 ? 191  TRP   A CE2 1 
ATOM   1539  C  CE3 . TRP   A  1 191 ? 44.828 -6.142  18.195  1.00 25.07 ? 191  TRP   A CE3 1 
ATOM   1540  C  CZ2 . TRP   A  1 191 ? 46.204 -6.404  20.697  1.00 23.79 ? 191  TRP   A CZ2 1 
ATOM   1541  C  CZ3 . TRP   A  1 191 ? 45.598 -7.275  18.502  1.00 25.01 ? 191  TRP   A CZ3 1 
ATOM   1542  C  CH2 . TRP   A  1 191 ? 46.278 -7.391  19.732  1.00 25.04 ? 191  TRP   A CH2 1 
ATOM   1543  N  N   . THR   A  1 192 ? 40.779 -1.242  17.321  1.00 20.05 ? 192  THR   A N   1 
ATOM   1544  C  CA  . THR   A  1 192 ? 40.120 -0.527  16.230  1.00 18.31 ? 192  THR   A CA  1 
ATOM   1545  C  C   . THR   A  1 192 ? 40.782 0.810   15.996  1.00 19.35 ? 192  THR   A C   1 
ATOM   1546  O  O   . THR   A  1 192 ? 41.260 1.469   16.931  1.00 22.32 ? 192  THR   A O   1 
ATOM   1547  C  CB  . THR   A  1 192 ? 38.601 -0.356  16.493  1.00 18.59 ? 192  THR   A CB  1 
ATOM   1548  O  OG1 . THR   A  1 192 ? 37.959 0.250   15.334  1.00 19.53 ? 192  THR   A OG1 1 
ATOM   1549  C  CG2 . THR   A  1 192 ? 38.338 0.469   17.733  1.00 21.24 ? 192  THR   A CG2 1 
ATOM   1550  N  N   . TYR   A  1 193 ? 40.792 1.223   14.737  1.00 18.72 ? 193  TYR   A N   1 
ATOM   1551  C  CA  . TYR   A  1 193 ? 41.337 2.528   14.380  1.00 19.13 ? 193  TYR   A CA  1 
ATOM   1552  C  C   . TYR   A  1 193 ? 40.783 2.914   13.009  1.00 18.21 ? 193  TYR   A C   1 
ATOM   1553  O  O   . TYR   A  1 193 ? 40.355 2.044   12.245  1.00 18.62 ? 193  TYR   A O   1 
ATOM   1554  C  CB  . TYR   A  1 193 ? 42.896 2.529   14.371  1.00 18.58 ? 193  TYR   A CB  1 
ATOM   1555  C  CG  . TYR   A  1 193 ? 43.457 1.791   13.172  1.00 17.86 ? 193  TYR   A CG  1 
ATOM   1556  C  CD1 . TYR   A  1 193 ? 43.558 0.410   13.200  1.00 18.44 ? 193  TYR   A CD1 1 
ATOM   1557  C  CD2 . TYR   A  1 193 ? 43.906 2.481   12.043  1.00 16.33 ? 193  TYR   A CD2 1 
ATOM   1558  C  CE1 . TYR   A  1 193 ? 44.056 -0.296  12.109  1.00 18.64 ? 193  TYR   A CE1 1 
ATOM   1559  C  CE2 . TYR   A  1 193 ? 44.406 1.803   10.924  1.00 16.12 ? 193  TYR   A CE2 1 
ATOM   1560  C  CZ  . TYR   A  1 193 ? 44.484 0.396   10.990  1.00 16.35 ? 193  TYR   A CZ  1 
ATOM   1561  O  OH  . TYR   A  1 193 ? 44.926 -0.293  9.865   1.00 16.96 ? 193  TYR   A OH  1 
ATOM   1562  N  N   . PRO   A  1 194 ? 40.741 4.205   12.688  1.00 16.74 ? 194  PRO   A N   1 
ATOM   1563  C  CA  . PRO   A  1 194 ? 40.288 4.651   11.355  1.00 18.26 ? 194  PRO   A CA  1 
ATOM   1564  C  C   . PRO   A  1 194 ? 41.419 4.521   10.352  1.00 17.02 ? 194  PRO   A C   1 
ATOM   1565  O  O   . PRO   A  1 194 ? 42.523 5.043   10.565  1.00 17.18 ? 194  PRO   A O   1 
ATOM   1566  C  CB  . PRO   A  1 194 ? 39.947 6.137   11.575  1.00 17.69 ? 194  PRO   A CB  1 
ATOM   1567  C  CG  . PRO   A  1 194 ? 40.774 6.524   12.768  1.00 22.00 ? 194  PRO   A CG  1 
ATOM   1568  C  CD  . PRO   A  1 194 ? 40.974 5.329   13.621  1.00 18.23 ? 194  PRO   A CD  1 
ATOM   1569  N  N   . GLY   A  1 195 ? 41.146 3.882   9.234   1.00 15.71 ? 195  GLY   A N   1 
ATOM   1570  C  CA  . GLY   A  1 195 ? 42.177 3.677   8.217   1.00 14.39 ? 195  GLY   A CA  1 
ATOM   1571  C  C   . GLY   A  1 195 ? 41.643 3.620   6.812   1.00 14.31 ? 195  GLY   A C   1 
ATOM   1572  O  O   . GLY   A  1 195 ? 40.671 4.316   6.467   1.00 16.27 ? 195  GLY   A O   1 
ATOM   1573  N  N   . SER   A  1 196 ? 42.269 2.770   6.001   1.00 14.57 ? 196  SER   A N   1 
ATOM   1574  C  CA  . SER   A  1 196 ? 42.061 2.801   4.554   1.00 14.83 ? 196  SER   A CA  1 
ATOM   1575  C  C   . SER   A  1 196 ? 41.977 1.386   4.002   1.00 15.16 ? 196  SER   A C   1 
ATOM   1576  O  O   . SER   A  1 196 ? 42.313 0.402   4.668   1.00 15.45 ? 196  SER   A O   1 
ATOM   1577  C  CB  . SER   A  1 196 ? 43.241 3.531   3.862   1.00 14.98 ? 196  SER   A CB  1 
ATOM   1578  O  OG  . SER   A  1 196 ? 44.425 2.689   3.890   1.00 16.26 ? 196  SER   A OG  1 
ATOM   1579  N  N   . LEU   A  1 197 ? 41.588 1.305   2.716   1.00 14.71 ? 197  LEU   A N   1 
ATOM   1580  C  CA  . LEU   A  1 197 ? 41.870 0.078   1.974   1.00 13.73 ? 197  LEU   A CA  1 
ATOM   1581  C  C   . LEU   A  1 197 ? 43.381 -0.174  1.989   1.00 14.58 ? 197  LEU   A C   1 
ATOM   1582  O  O   . LEU   A  1 197 ? 44.173 0.765   1.894   1.00 14.74 ? 197  LEU   A O   1 
ATOM   1583  C  CB  . LEU   A  1 197 ? 41.397 0.219   0.518   1.00 14.19 ? 197  LEU   A CB  1 
ATOM   1584  C  CG  . LEU   A  1 197 ? 39.900 0.526   0.312   1.00 14.11 ? 197  LEU   A CG  1 
ATOM   1585  C  CD1 . LEU   A  1 197 ? 39.715 0.711   -1.199  1.00 14.75 ? 197  LEU   A CD1 1 
ATOM   1586  C  CD2 . LEU   A  1 197 ? 39.015 -0.639  0.819   1.00 15.57 ? 197  LEU   A CD2 1 
ATOM   1587  N  N   . THR   A  1 198 ? 43.769 -1.455  2.050   1.00 14.29 ? 198  THR   A N   1 
ATOM   1588  C  CA  . THR   A  1 198 ? 45.210 -1.736  1.999   1.00 14.04 ? 198  THR   A CA  1 
ATOM   1589  C  C   . THR   A  1 198 ? 45.681 -2.038  0.586   1.00 13.52 ? 198  THR   A C   1 
ATOM   1590  O  O   . THR   A  1 198 ? 46.862 -2.374  0.424   1.00 14.45 ? 198  THR   A O   1 
ATOM   1591  C  CB  . THR   A  1 198 ? 45.635 -2.899  2.917   1.00 14.43 ? 198  THR   A CB  1 
ATOM   1592  O  OG1 . THR   A  1 198 ? 45.006 -4.080  2.379   1.00 14.06 ? 198  THR   A OG1 1 
ATOM   1593  C  CG2 . THR   A  1 198 ? 45.178 -2.675  4.344   1.00 15.25 ? 198  THR   A CG2 1 
ATOM   1594  N  N   . THR   A  1 199 ? 44.836 -1.841  -0.418  1.00 14.63 ? 199  THR   A N   1 
ATOM   1595  C  CA  . THR   A  1 199 ? 45.239 -1.920  -1.814  1.00 12.88 ? 199  THR   A CA  1 
ATOM   1596  C  C   . THR   A  1 199 ? 44.769 -0.633  -2.477  1.00 13.55 ? 199  THR   A C   1 
ATOM   1597  O  O   . THR   A  1 199 ? 43.855 0.042   -1.973  1.00 14.18 ? 199  THR   A O   1 
ATOM   1598  C  CB  . THR   A  1 199 ? 44.596 -3.108  -2.578  1.00 14.46 ? 199  THR   A CB  1 
ATOM   1599  O  OG1 . THR   A  1 199 ? 43.177 -2.892  -2.644  1.00 15.74 ? 199  THR   A OG1 1 
ATOM   1600  C  CG2 . THR   A  1 199 ? 44.847 -4.408  -1.883  1.00 15.31 ? 199  THR   A CG2 1 
ATOM   1601  N  N   . PRO   A  1 200 ? 45.366 -0.277  -3.614  1.00 14.39 ? 200  PRO   A N   1 
ATOM   1602  C  CA  . PRO   A  1 200 ? 44.769 0.762   -4.458  1.00 12.40 ? 200  PRO   A CA  1 
ATOM   1603  C  C   . PRO   A  1 200 ? 43.281 0.503   -4.588  1.00 13.13 ? 200  PRO   A C   1 
ATOM   1604  O  O   . PRO   A  1 200 ? 42.843 -0.655  -4.770  1.00 14.17 ? 200  PRO   A O   1 
ATOM   1605  C  CB  . PRO   A  1 200 ? 45.525 0.624   -5.820  1.00 14.61 ? 200  PRO   A CB  1 
ATOM   1606  C  CG  . PRO   A  1 200 ? 46.941 0.158   -5.343  1.00 15.75 ? 200  PRO   A CG  1 
ATOM   1607  C  CD  . PRO   A  1 200 ? 46.537 -0.918  -4.264  1.00 14.16 ? 200  PRO   A CD  1 
ATOM   1608  N  N   . PRO   A  1 201 ? 42.449 1.555   -4.563  1.00 13.54 ? 201  PRO   A N   1 
ATOM   1609  C  CA  . PRO   A  1 201 ? 42.859 2.965   -4.556  1.00 14.00 ? 201  PRO   A CA  1 
ATOM   1610  C  C   . PRO   A  1 201 ? 43.197 3.544   -3.182  1.00 13.23 ? 201  PRO   A C   1 
ATOM   1611  O  O   . PRO   A  1 201 ? 43.355 4.770   -3.092  1.00 14.46 ? 201  PRO   A O   1 
ATOM   1612  C  CB  . PRO   A  1 201 ? 41.637 3.686   -5.163  1.00 13.64 ? 201  PRO   A CB  1 
ATOM   1613  C  CG  . PRO   A  1 201 ? 40.456 2.843   -4.670  1.00 13.52 ? 201  PRO   A CG  1 
ATOM   1614  C  CD  . PRO   A  1 201 ? 40.980 1.395   -4.741  1.00 13.99 ? 201  PRO   A CD  1 
ATOM   1615  N  N   . LEU   A  1 202 ? 43.315 2.714   -2.138  1.00 13.90 ? 202  LEU   A N   1 
ATOM   1616  C  CA  . LEU   A  1 202 ? 43.846 3.160   -0.826  1.00 12.92 ? 202  LEU   A CA  1 
ATOM   1617  C  C   . LEU   A  1 202 ? 42.956 4.230   -0.178  1.00 13.84 ? 202  LEU   A C   1 
ATOM   1618  O  O   . LEU   A  1 202 ? 43.452 5.046   0.647   1.00 14.97 ? 202  LEU   A O   1 
ATOM   1619  C  CB  . LEU   A  1 202 ? 45.306 3.671   -0.938  1.00 14.59 ? 202  LEU   A CB  1 
ATOM   1620  C  CG  . LEU   A  1 202 ? 46.268 2.598   -1.454  1.00 14.04 ? 202  LEU   A CG  1 
ATOM   1621  C  CD1 . LEU   A  1 202 ? 47.657 3.166   -1.842  1.00 14.75 ? 202  LEU   A CD1 1 
ATOM   1622  C  CD2 . LEU   A  1 202 ? 46.449 1.423   -0.439  1.00 14.08 ? 202  LEU   A CD2 1 
ATOM   1623  N  N   . LEU   A  1 203 ? 41.665 4.233   -0.523  1.00 14.31 ? 203  LEU   A N   1 
ATOM   1624  C  CA  . LEU   A  1 203 ? 40.769 5.259   0.024   1.00 14.54 ? 203  LEU   A CA  1 
ATOM   1625  C  C   . LEU   A  1 203 ? 40.620 5.131   1.540   1.00 14.63 ? 203  LEU   A C   1 
ATOM   1626  O  O   . LEU   A  1 203 ? 40.551 4.033   2.094   1.00 14.46 ? 203  LEU   A O   1 
ATOM   1627  C  CB  . LEU   A  1 203 ? 39.410 5.160   -0.662  1.00 15.08 ? 203  LEU   A CB  1 
ATOM   1628  C  CG  . LEU   A  1 203 ? 39.530 5.477   -2.172  1.00 15.25 ? 203  LEU   A CG  1 
ATOM   1629  C  CD1 . LEU   A  1 203 ? 38.157 5.121   -2.839  1.00 17.36 ? 203  LEU   A CD1 1 
ATOM   1630  C  CD2 . LEU   A  1 203 ? 39.888 6.974   -2.374  1.00 17.30 ? 203  LEU   A CD2 1 
ATOM   1631  N  N   . GLU   A  1 204 ? 40.495 6.272   2.217   1.00 15.47 ? 204  GLU   A N   1 
ATOM   1632  C  CA  . GLU   A  1 204 ? 40.484 6.312   3.691   1.00 14.72 ? 204  GLU   A CA  1 
ATOM   1633  C  C   . GLU   A  1 204 ? 39.041 6.228   4.196   1.00 16.78 ? 204  GLU   A C   1 
ATOM   1634  O  O   . GLU   A  1 204 ? 38.479 7.138   4.823   1.00 18.25 ? 204  GLU   A O   1 
ATOM   1635  C  CB  . GLU   A  1 204 ? 41.221 7.562   4.142   1.00 17.04 ? 204  GLU   A CB  1 
ATOM   1636  C  CG  . GLU   A  1 204 ? 42.715 7.450   3.728   1.00 15.52 ? 204  GLU   A CG  1 
ATOM   1637  C  CD  . GLU   A  1 204 ? 43.571 8.652   4.115   1.00 16.29 ? 204  GLU   A CD  1 
ATOM   1638  O  OE1 . GLU   A  1 204 ? 43.010 9.766   4.243   1.00 18.23 ? 204  GLU   A OE1 1 
ATOM   1639  O  OE2 . GLU   A  1 204 ? 44.799 8.443   4.224   1.00 16.93 ? 204  GLU   A OE2 1 
ATOM   1640  N  N   . SER   A  1 205 ? 38.453 5.073   3.884   1.00 16.02 ? 205  SER   A N   1 
ATOM   1641  C  CA  A SER   A  1 205 ? 37.033 4.831   4.131   0.61 16.06 ? 205  SER   A CA  1 
ATOM   1642  C  CA  B SER   A  1 205 ? 37.038 4.822   4.115   0.39 15.97 ? 205  SER   A CA  1 
ATOM   1643  C  C   . SER   A  1 205 ? 36.770 3.656   5.054   1.00 15.31 ? 205  SER   A C   1 
ATOM   1644  O  O   . SER   A  1 205 ? 35.616 3.210   5.150   1.00 17.70 ? 205  SER   A O   1 
ATOM   1645  C  CB  A SER   A  1 205 ? 36.311 4.599   2.811   0.61 17.02 ? 205  SER   A CB  1 
ATOM   1646  C  CB  B SER   A  1 205 ? 36.370 4.599   2.763   0.39 16.69 ? 205  SER   A CB  1 
ATOM   1647  O  OG  A SER   A  1 205 ? 36.986 3.593   2.123   0.61 17.64 ? 205  SER   A OG  1 
ATOM   1648  O  OG  B SER   A  1 205 ? 36.793 5.645   1.904   0.39 16.21 ? 205  SER   A OG  1 
ATOM   1649  N  N   . VAL   A  1 206 ? 37.780 3.141   5.766   1.00 16.24 ? 206  VAL   A N   1 
ATOM   1650  C  CA  . VAL   A  1 206 ? 37.625 1.885   6.502   1.00 16.52 ? 206  VAL   A CA  1 
ATOM   1651  C  C   . VAL   A  1 206 ? 37.728 2.127   7.996   1.00 17.39 ? 206  VAL   A C   1 
ATOM   1652  O  O   . VAL   A  1 206 ? 38.709 2.712   8.470   1.00 18.14 ? 206  VAL   A O   1 
ATOM   1653  C  CB  . VAL   A  1 206 ? 38.685 0.853   6.071   1.00 15.15 ? 206  VAL   A CB  1 
ATOM   1654  C  CG1 . VAL   A  1 206 ? 38.538 -0.464  6.942   1.00 16.06 ? 206  VAL   A CG1 1 
ATOM   1655  C  CG2 . VAL   A  1 206 ? 38.609 0.508   4.562   1.00 15.15 ? 206  VAL   A CG2 1 
ATOM   1656  N  N   . THR   A  1 207 ? 36.760 1.611   8.752   1.00 17.16 ? 207  THR   A N   1 
ATOM   1657  C  CA  . THR   A  1 207 ? 36.948 1.397   10.195  1.00 17.91 ? 207  THR   A CA  1 
ATOM   1658  C  C   . THR   A  1 207 ? 37.494 -0.009  10.382  1.00 18.20 ? 207  THR   A C   1 
ATOM   1659  O  O   . THR   A  1 207 ? 36.835 -0.970  10.010  1.00 18.37 ? 207  THR   A O   1 
ATOM   1660  C  CB  . THR   A  1 207 ? 35.621 1.561   10.939  1.00 17.40 ? 207  THR   A CB  1 
ATOM   1661  O  OG1 . THR   A  1 207 ? 35.143 2.900   10.768  1.00 20.70 ? 207  THR   A OG1 1 
ATOM   1662  C  CG2 . THR   A  1 207 ? 35.838 1.296   12.427  1.00 19.38 ? 207  THR   A CG2 1 
ATOM   1663  N  N   . TRP   A  1 208 ? 38.752 -0.113  10.810  1.00 17.53 ? 208  TRP   A N   1 
ATOM   1664  C  CA  . TRP   A  1 208 ? 39.404 -1.411  11.031  1.00 18.29 ? 208  TRP   A CA  1 
ATOM   1665  C  C   . TRP   A  1 208 ? 39.055 -1.969  12.397  1.00 19.23 ? 208  TRP   A C   1 
ATOM   1666  O  O   . TRP   A  1 208 ? 39.158 -1.258  13.412  1.00 19.26 ? 208  TRP   A O   1 
ATOM   1667  C  CB  . TRP   A  1 208 ? 40.942 -1.257  10.925  1.00 17.34 ? 208  TRP   A CB  1 
ATOM   1668  C  CG  . TRP   A  1 208 ? 41.326 -1.269  9.467   1.00 17.39 ? 208  TRP   A CG  1 
ATOM   1669  C  CD1 . TRP   A  1 208 ? 41.542 -0.189  8.650   1.00 16.17 ? 208  TRP   A CD1 1 
ATOM   1670  C  CD2 . TRP   A  1 208 ? 41.451 -2.431  8.655   1.00 16.13 ? 208  TRP   A CD2 1 
ATOM   1671  N  NE1 . TRP   A  1 208 ? 41.769 -0.628  7.335   1.00 15.69 ? 208  TRP   A NE1 1 
ATOM   1672  C  CE2 . TRP   A  1 208 ? 41.735 -2.000  7.337   1.00 15.35 ? 208  TRP   A CE2 1 
ATOM   1673  C  CE3 . TRP   A  1 208 ? 41.387 -3.814  8.931   1.00 17.12 ? 208  TRP   A CE3 1 
ATOM   1674  C  CZ2 . TRP   A  1 208 ? 41.926 -2.897  6.267   1.00 15.92 ? 208  TRP   A CZ2 1 
ATOM   1675  C  CZ3 . TRP   A  1 208 ? 41.549 -4.721  7.835   1.00 17.72 ? 208  TRP   A CZ3 1 
ATOM   1676  C  CH2 . TRP   A  1 208 ? 41.836 -4.253  6.552   1.00 17.27 ? 208  TRP   A CH2 1 
ATOM   1677  N  N   . ILE   A  1 209 ? 38.710 -3.258  12.425  1.00 18.12 ? 209  ILE   A N   1 
ATOM   1678  C  CA  . ILE   A  1 209 ? 38.450 -3.989  13.637  1.00 17.98 ? 209  ILE   A CA  1 
ATOM   1679  C  C   . ILE   A  1 209 ? 39.325 -5.220  13.529  1.00 19.33 ? 209  ILE   A C   1 
ATOM   1680  O  O   . ILE   A  1 209 ? 39.018 -6.135  12.734  1.00 19.91 ? 209  ILE   A O   1 
ATOM   1681  C  CB  . ILE   A  1 209 ? 36.967 -4.365  13.745  1.00 20.13 ? 209  ILE   A CB  1 
ATOM   1682  C  CG1 . ILE   A  1 209 ? 36.104 -3.082  13.819  1.00 22.03 ? 209  ILE   A CG1 1 
ATOM   1683  C  CG2 . ILE   A  1 209 ? 36.742 -5.256  14.964  1.00 20.58 ? 209  ILE   A CG2 1 
ATOM   1684  C  CD1 . ILE   A  1 209 ? 34.598 -3.346  13.667  1.00 21.87 ? 209  ILE   A CD1 1 
ATOM   1685  N  N   . VAL   A  1 210 ? 40.442 -5.240  14.257  1.00 18.98 ? 210  VAL   A N   1 
ATOM   1686  C  CA  . VAL   A  1 210 ? 41.428 -6.315  14.157  1.00 19.02 ? 210  VAL   A CA  1 
ATOM   1687  C  C   . VAL   A  1 210 ? 41.347 -7.177  15.399  1.00 21.42 ? 210  VAL   A C   1 
ATOM   1688  O  O   . VAL   A  1 210 ? 41.584 -6.693  16.524  1.00 20.23 ? 210  VAL   A O   1 
ATOM   1689  C  CB  . VAL   A  1 210 ? 42.841 -5.751  13.983  1.00 19.05 ? 210  VAL   A CB  1 
ATOM   1690  C  CG1 . VAL   A  1 210 ? 43.870 -6.902  13.885  1.00 19.59 ? 210  VAL   A CG1 1 
ATOM   1691  C  CG2 . VAL   A  1 210 ? 42.888 -4.864  12.726  1.00 17.57 ? 210  VAL   A CG2 1 
ATOM   1692  N  N   . LEU   A  1 211 ? 40.963 -8.455  15.218  1.00 20.82 ? 211  LEU   A N   1 
ATOM   1693  C  CA  . LEU   A  1 211 ? 40.810 -9.305  16.395  1.00 20.04 ? 211  LEU   A CA  1 
ATOM   1694  C  C   . LEU   A  1 211 ? 42.163 -9.664  17.008  1.00 21.08 ? 211  LEU   A C   1 
ATOM   1695  O  O   . LEU   A  1 211 ? 43.156 -9.913  16.312  1.00 22.94 ? 211  LEU   A O   1 
ATOM   1696  C  CB  . LEU   A  1 211 ? 40.080 -10.572 16.016  1.00 20.32 ? 211  LEU   A CB  1 
ATOM   1697  C  CG  . LEU   A  1 211 ? 38.665 -10.374 15.458  1.00 21.98 ? 211  LEU   A CG  1 
ATOM   1698  C  CD1 . LEU   A  1 211 ? 38.046 -11.771 15.304  1.00 21.91 ? 211  LEU   A CD1 1 
ATOM   1699  C  CD2 . LEU   A  1 211 ? 37.829 -9.570  16.449  1.00 24.28 ? 211  LEU   A CD2 1 
ATOM   1700  N  N   . LYS   A  1 212 ? 42.205 -9.679  18.337  1.00 22.86 ? 212  LYS   A N   1 
ATOM   1701  C  CA  . LYS   A  1 212 ? 43.440 -10.016 19.032  1.00 22.56 ? 212  LYS   A CA  1 
ATOM   1702  C  C   . LYS   A  1 212 ? 43.800 -11.503 18.932  1.00 24.71 ? 212  LYS   A C   1 
ATOM   1703  O  O   . LYS   A  1 212 ? 44.978 -11.859 18.817  1.00 26.07 ? 212  LYS   A O   1 
ATOM   1704  C  CB  . LYS   A  1 212 ? 43.307 -9.615  20.495  1.00 26.21 ? 212  LYS   A CB  1 
ATOM   1705  C  CG  . LYS   A  1 212 ? 44.466 -10.103 21.325  1.00 29.17 ? 212  LYS   A CG  1 
ATOM   1706  C  CD  . LYS   A  1 212 ? 44.504 -9.393  22.642  1.00 35.77 ? 212  LYS   A CD  1 
ATOM   1707  C  CE  . LYS   A  1 212 ? 45.641 -9.981  23.477  1.00 40.50 ? 212  LYS   A CE  1 
ATOM   1708  N  NZ  . LYS   A  1 212 ? 45.626 -9.421  24.833  1.00 43.89 ? 212  LYS   A NZ  1 
ATOM   1709  N  N   . GLU   A  1 213 ? 42.815 -12.388 18.966  1.00 22.82 ? 213  GLU   A N   1 
ATOM   1710  C  CA  . GLU   A  1 213 ? 43.101 -13.826 18.956  1.00 23.76 ? 213  GLU   A CA  1 
ATOM   1711  C  C   . GLU   A  1 213 ? 43.250 -14.319 17.521  1.00 23.41 ? 213  GLU   A C   1 
ATOM   1712  O  O   . GLU   A  1 213 ? 42.327 -14.147 16.724  1.00 23.86 ? 213  GLU   A O   1 
ATOM   1713  C  CB  . GLU   A  1 213 ? 41.986 -14.630 19.648  1.00 25.18 ? 213  GLU   A CB  1 
ATOM   1714  C  CG  . GLU   A  1 213 ? 42.268 -16.127 19.715  1.00 29.35 ? 213  GLU   A CG  1 
ATOM   1715  C  CD  . GLU   A  1 213 ? 41.249 -16.928 20.534  1.00 34.22 ? 213  GLU   A CD  1 
ATOM   1716  O  OE1 . GLU   A  1 213 ? 40.118 -16.462 20.810  1.00 35.77 ? 213  GLU   A OE1 1 
ATOM   1717  O  OE2 . GLU   A  1 213 ? 41.624 -18.048 20.940  1.00 40.00 ? 213  GLU   A OE2 1 
ATOM   1718  N  N   . PRO   A  1 214 ? 44.356 -14.958 17.159  1.00 23.14 ? 214  PRO   A N   1 
ATOM   1719  C  CA  . PRO   A  1 214 ? 44.459 -15.528 15.803  1.00 24.12 ? 214  PRO   A CA  1 
ATOM   1720  C  C   . PRO   A  1 214 ? 43.660 -16.810 15.702  1.00 24.16 ? 214  PRO   A C   1 
ATOM   1721  O  O   . PRO   A  1 214 ? 43.348 -17.475 16.707  1.00 28.07 ? 214  PRO   A O   1 
ATOM   1722  C  CB  . PRO   A  1 214 ? 45.953 -15.838 15.638  1.00 24.58 ? 214  PRO   A CB  1 
ATOM   1723  C  CG  . PRO   A  1 214 ? 46.623 -15.299 16.948  1.00 32.26 ? 214  PRO   A CG  1 
ATOM   1724  C  CD  . PRO   A  1 214 ? 45.548 -15.280 17.974  1.00 27.42 ? 214  PRO   A CD  1 
ATOM   1725  N  N   . ILE   A  1 215 ? 43.385 -17.189 14.442  1.00 23.98 ? 215  ILE   A N   1 
ATOM   1726  C  CA  . ILE   A  1 215 ? 42.954 -18.542 14.137  1.00 24.28 ? 215  ILE   A CA  1 
ATOM   1727  C  C   . ILE   A  1 215 ? 44.174 -19.357 13.723  1.00 24.62 ? 215  ILE   A C   1 
ATOM   1728  O  O   . ILE   A  1 215 ? 45.163 -18.817 13.184  1.00 26.52 ? 215  ILE   A O   1 
ATOM   1729  C  CB  . ILE   A  1 215 ? 41.836 -18.547 13.076  1.00 24.43 ? 215  ILE   A CB  1 
ATOM   1730  C  CG1 . ILE   A  1 215 ? 42.344 -17.965 11.742  1.00 23.43 ? 215  ILE   A CG1 1 
ATOM   1731  C  CG2 . ILE   A  1 215 ? 40.608 -17.784 13.601  1.00 25.02 ? 215  ILE   A CG2 1 
ATOM   1732  C  CD1 . ILE   A  1 215 ? 41.287 -18.015 10.564  1.00 23.98 ? 215  ILE   A CD1 1 
ATOM   1733  N  N   . SER   A  1 216 ? 44.122 -20.664 13.977  1.00 26.77 ? 216  SER   A N   1 
ATOM   1734  C  CA  A SER   A  1 216 ? 45.246 -21.537 13.694  0.55 29.05 ? 216  SER   A CA  1 
ATOM   1735  C  CA  B SER   A  1 216 ? 45.229 -21.566 13.709  0.45 29.19 ? 216  SER   A CA  1 
ATOM   1736  C  C   . SER   A  1 216 ? 44.973 -22.294 12.403  1.00 31.20 ? 216  SER   A C   1 
ATOM   1737  O  O   . SER   A  1 216 ? 43.919 -22.938 12.266  1.00 34.61 ? 216  SER   A O   1 
ATOM   1738  C  CB  A SER   A  1 216 ? 45.510 -22.519 14.840  0.55 32.30 ? 216  SER   A CB  1 
ATOM   1739  C  CB  B SER   A  1 216 ? 45.377 -22.592 14.829  0.45 31.99 ? 216  SER   A CB  1 
ATOM   1740  O  OG  A SER   A  1 216 ? 46.089 -21.860 15.974  0.55 31.99 ? 216  SER   A OG  1 
ATOM   1741  O  OG  B SER   A  1 216 ? 46.225 -23.651 14.440  0.45 32.35 ? 216  SER   A OG  1 
ATOM   1742  N  N   . VAL   A  1 217 ? 45.937 -22.229 11.472  1.00 28.11 ? 217  VAL   A N   1 
ATOM   1743  C  CA  . VAL   A  1 217 ? 45.894 -22.989 10.221  1.00 29.57 ? 217  VAL   A CA  1 
ATOM   1744  C  C   . VAL   A  1 217 ? 47.166 -23.809 10.071  1.00 28.36 ? 217  VAL   A C   1 
ATOM   1745  O  O   . VAL   A  1 217 ? 48.202 -23.506 10.676  1.00 29.24 ? 217  VAL   A O   1 
ATOM   1746  C  CB  . VAL   A  1 217 ? 45.727 -22.069 9.012   1.00 30.83 ? 217  VAL   A CB  1 
ATOM   1747  C  CG1 . VAL   A  1 217 ? 44.418 -21.326 9.141   1.00 32.59 ? 217  VAL   A CG1 1 
ATOM   1748  C  CG2 . VAL   A  1 217 ? 46.950 -21.141 8.913   1.00 27.25 ? 217  VAL   A CG2 1 
ATOM   1749  N  N   . SER   A  1 218 ? 47.098 -24.862 9.241   1.00 28.79 ? 218  SER   A N   1 
ATOM   1750  C  CA  . SER   A  1 218 ? 48.317 -25.635 9.069   1.00 29.30 ? 218  SER   A CA  1 
ATOM   1751  C  C   . SER   A  1 218 ? 49.234 -25.005 8.009   1.00 27.91 ? 218  SER   A C   1 
ATOM   1752  O  O   . SER   A  1 218 ? 48.789 -24.307 7.103   1.00 24.65 ? 218  SER   A O   1 
ATOM   1753  C  CB  . SER   A  1 218 ? 47.991 -27.076 8.690   1.00 31.77 ? 218  SER   A CB  1 
ATOM   1754  O  OG  . SER   A  1 218 ? 47.516 -27.131 7.351   1.00 29.44 ? 218  SER   A OG  1 
ATOM   1755  N  N   . SER   A  1 219 ? 50.528 -25.331 8.097   1.00 30.31 ? 219  SER   A N   1 
ATOM   1756  C  CA  A SER   A  1 219 ? 51.469 -24.945 7.052   0.42 29.28 ? 219  SER   A CA  1 
ATOM   1757  C  CA  B SER   A  1 219 ? 51.468 -24.945 7.048   0.58 29.22 ? 219  SER   A CA  1 
ATOM   1758  C  C   . SER   A  1 219 ? 51.015 -25.462 5.687   1.00 27.21 ? 219  SER   A C   1 
ATOM   1759  O  O   . SER   A  1 219 ? 51.127 -24.763 4.680   1.00 26.67 ? 219  SER   A O   1 
ATOM   1760  C  CB  A SER   A  1 219 ? 52.860 -25.470 7.397   0.42 32.25 ? 219  SER   A CB  1 
ATOM   1761  C  CB  B SER   A  1 219 ? 52.862 -25.473 7.358   0.58 32.35 ? 219  SER   A CB  1 
ATOM   1762  O  OG  A SER   A  1 219 ? 53.830 -25.058 6.453   0.42 33.17 ? 219  SER   A OG  1 
ATOM   1763  O  OG  B SER   A  1 219 ? 53.474 -24.734 8.391   0.58 32.80 ? 219  SER   A OG  1 
ATOM   1764  N  N   . GLU   A  1 220 ? 50.487 -26.677 5.645   1.00 28.96 ? 220  GLU   A N   1 
ATOM   1765  C  CA  . GLU   A  1 220 ? 50.013 -27.241 4.389   1.00 30.55 ? 220  GLU   A CA  1 
ATOM   1766  C  C   . GLU   A  1 220 ? 48.867 -26.434 3.815   1.00 29.58 ? 220  GLU   A C   1 
ATOM   1767  O  O   . GLU   A  1 220 ? 48.822 -26.196 2.598   1.00 28.78 ? 220  GLU   A O   1 
ATOM   1768  C  CB  . GLU   A  1 220 ? 49.602 -28.697 4.608   1.00 34.57 ? 220  GLU   A CB  1 
ATOM   1769  C  CG  . GLU   A  1 220 ? 50.797 -29.600 4.978   1.00 45.65 ? 220  GLU   A CG  1 
ATOM   1770  C  CD  . GLU   A  1 220 ? 51.101 -29.725 6.503   1.00 49.60 ? 220  GLU   A CD  1 
ATOM   1771  O  OE1 . GLU   A  1 220 ? 50.785 -28.821 7.317   1.00 45.73 ? 220  GLU   A OE1 1 
ATOM   1772  O  OE2 . GLU   A  1 220 ? 51.672 -30.772 6.884   1.00 52.98 ? 220  GLU   A OE2 1 
ATOM   1773  N  N   . GLN   A  1 221 ? 47.945 -25.965 4.664   1.00 26.77 ? 221  GLN   A N   1 
ATOM   1774  C  CA  . GLN   A  1 221 ? 46.843 -25.151 4.155   1.00 24.86 ? 221  GLN   A CA  1 
ATOM   1775  C  C   . GLN   A  1 221 ? 47.359 -23.850 3.545   1.00 24.90 ? 221  GLN   A C   1 
ATOM   1776  O  O   . GLN   A  1 221 ? 46.942 -23.457 2.448   1.00 23.41 ? 221  GLN   A O   1 
ATOM   1777  C  CB  . GLN   A  1 221 ? 45.831 -24.862 5.263   1.00 25.67 ? 221  GLN   A CB  1 
ATOM   1778  C  CG  . GLN   A  1 221 ? 44.938 -26.070 5.599   1.00 27.32 ? 221  GLN   A CG  1 
ATOM   1779  C  CD  . GLN   A  1 221 ? 43.982 -25.795 6.744   1.00 26.95 ? 221  GLN   A CD  1 
ATOM   1780  O  OE1 . GLN   A  1 221 ? 44.367 -25.187 7.753   1.00 26.81 ? 221  GLN   A OE1 1 
ATOM   1781  N  NE2 . GLN   A  1 221 ? 42.728 -26.232 6.603   1.00 26.29 ? 221  GLN   A NE2 1 
ATOM   1782  N  N   . VAL   A  1 222 ? 48.269 -23.143 4.235   1.00 23.04 ? 222  VAL   A N   1 
ATOM   1783  C  CA  . VAL   A  1 222 ? 48.777 -21.898 3.684   1.00 22.50 ? 222  VAL   A CA  1 
ATOM   1784  C  C   . VAL   A  1 222 ? 49.542 -22.144 2.391   1.00 24.08 ? 222  VAL   A C   1 
ATOM   1785  O  O   . VAL   A  1 222 ? 49.533 -21.300 1.478   1.00 22.68 ? 222  VAL   A O   1 
ATOM   1786  C  CB  . VAL   A  1 222 ? 49.670 -21.152 4.706   1.00 26.01 ? 222  VAL   A CB  1 
ATOM   1787  C  CG1 . VAL   A  1 222 ? 50.047 -19.748 4.160   1.00 24.90 ? 222  VAL   A CG1 1 
ATOM   1788  C  CG2 . VAL   A  1 222 ? 48.967 -21.028 6.008   1.00 31.13 ? 222  VAL   A CG2 1 
ATOM   1789  N  N   . SER   A  1 223 ? 50.263 -23.270 2.301   1.00 24.18 ? 223  SER   A N   1 
ATOM   1790  C  CA  . SER   A  1 223 ? 51.026 -23.530 1.087   1.00 25.68 ? 223  SER   A CA  1 
ATOM   1791  C  C   . SER   A  1 223 ? 50.100 -23.614 -0.126  1.00 25.15 ? 223  SER   A C   1 
ATOM   1792  O  O   . SER   A  1 223 ? 50.521 -23.326 -1.258  1.00 24.52 ? 223  SER   A O   1 
ATOM   1793  C  CB  . SER   A  1 223 ? 51.839 -24.825 1.218   1.00 28.96 ? 223  SER   A CB  1 
ATOM   1794  O  OG  . SER   A  1 223 ? 50.993 -25.961 1.050   1.00 33.99 ? 223  SER   A OG  1 
ATOM   1795  N  N   . LYS   A  1 224 ? 48.862 -24.052 0.083   1.00 23.14 ? 224  LYS   A N   1 
ATOM   1796  C  CA  . LYS   A  1 224 ? 47.914 -24.098 -1.024  1.00 23.54 ? 224  LYS   A CA  1 
ATOM   1797  C  C   . LYS   A  1 224 ? 47.587 -22.704 -1.549  1.00 21.10 ? 224  LYS   A C   1 
ATOM   1798  O  O   . LYS   A  1 224 ? 47.340 -22.546 -2.755  1.00 22.10 ? 224  LYS   A O   1 
ATOM   1799  C  CB  . LYS   A  1 224 ? 46.622 -24.801 -0.608  1.00 23.81 ? 224  LYS   A CB  1 
ATOM   1800  C  CG  . LYS   A  1 224 ? 46.805 -26.274 -0.163  1.00 27.96 ? 224  LYS   A CG  1 
ATOM   1801  C  CD  . LYS   A  1 224 ? 47.396 -27.094 -1.262  1.00 34.28 ? 224  LYS   A CD  1 
ATOM   1802  C  CE  . LYS   A  1 224 ? 47.586 -28.565 -0.780  1.00 43.79 ? 224  LYS   A CE  1 
ATOM   1803  N  NZ  . LYS   A  1 224 ? 48.470 -29.364 -1.691  1.00 49.54 ? 224  LYS   A NZ  1 
ATOM   1804  N  N   . PHE   A  1 225 ? 47.576 -21.692 -0.681  1.00 19.48 ? 225  PHE   A N   1 
ATOM   1805  C  CA  . PHE   A  1 225 ? 47.414 -20.323 -1.158  1.00 21.36 ? 225  PHE   A CA  1 
ATOM   1806  C  C   . PHE   A  1 225 ? 48.496 -19.978 -2.180  1.00 19.37 ? 225  PHE   A C   1 
ATOM   1807  O  O   . PHE   A  1 225 ? 48.250 -19.255 -3.146  1.00 20.08 ? 225  PHE   A O   1 
ATOM   1808  C  CB  . PHE   A  1 225 ? 47.532 -19.311 -0.011  1.00 21.76 ? 225  PHE   A CB  1 
ATOM   1809  C  CG  . PHE   A  1 225 ? 46.403 -19.306 1.001   1.00 21.27 ? 225  PHE   A CG  1 
ATOM   1810  C  CD1 . PHE   A  1 225 ? 45.299 -20.131 0.891   1.00 24.83 ? 225  PHE   A CD1 1 
ATOM   1811  C  CD2 . PHE   A  1 225 ? 46.520 -18.471 2.109   1.00 23.69 ? 225  PHE   A CD2 1 
ATOM   1812  C  CE1 . PHE   A  1 225 ? 44.297 -20.119 1.882   1.00 25.14 ? 225  PHE   A CE1 1 
ATOM   1813  C  CE2 . PHE   A  1 225 ? 45.518 -18.415 3.095   1.00 26.82 ? 225  PHE   A CE2 1 
ATOM   1814  C  CZ  . PHE   A  1 225 ? 44.391 -19.241 2.957   1.00 23.67 ? 225  PHE   A CZ  1 
ATOM   1815  N  N   . ARG   A  1 226 ? 49.717 -20.449 -1.939  1.00 20.19 ? 226  ARG   A N   1 
ATOM   1816  C  CA  . ARG   A  1 226 ? 50.861 -20.035 -2.740  1.00 19.15 ? 226  ARG   A CA  1 
ATOM   1817  C  C   . ARG   A  1 226 ? 50.890 -20.711 -4.093  1.00 20.66 ? 226  ARG   A C   1 
ATOM   1818  O  O   . ARG   A  1 226 ? 51.709 -20.311 -4.945  1.00 22.69 ? 226  ARG   A O   1 
ATOM   1819  C  CB  . ARG   A  1 226 ? 52.170 -20.331 -1.989  1.00 20.00 ? 226  ARG   A CB  1 
ATOM   1820  C  CG  . ARG   A  1 226 ? 52.242 -19.727 -0.583  1.00 22.15 ? 226  ARG   A CG  1 
ATOM   1821  C  CD  . ARG   A  1 226 ? 53.689 -19.785 -0.041  1.00 21.92 ? 226  ARG   A CD  1 
ATOM   1822  N  NE  . ARG   A  1 226 ? 53.693 -19.321 1.358   1.00 23.49 ? 226  ARG   A NE  1 
ATOM   1823  C  CZ  . ARG   A  1 226 ? 53.682 -20.100 2.437   1.00 23.69 ? 226  ARG   A CZ  1 
ATOM   1824  N  NH1 . ARG   A  1 226 ? 53.741 -21.446 2.334   1.00 26.42 ? 226  ARG   A NH1 1 
ATOM   1825  N  NH2 . ARG   A  1 226 ? 53.624 -19.568 3.648   1.00 23.98 ? 226  ARG   A NH2 1 
ATOM   1826  N  N   . LYS   A  1 227 ? 49.969 -21.670 -4.360  1.00 20.62 ? 227  LYS   A N   1 
ATOM   1827  C  CA  . LYS   A  1 227 ? 49.908 -22.273 -5.679  1.00 22.11 ? 227  LYS   A CA  1 
ATOM   1828  C  C   . LYS   A  1 227 ? 49.058 -21.475 -6.647  1.00 21.27 ? 227  LYS   A C   1 
ATOM   1829  O  O   . LYS   A  1 227 ? 49.034 -21.810 -7.846  1.00 23.42 ? 227  LYS   A O   1 
ATOM   1830  C  CB  . LYS   A  1 227 ? 49.359 -23.698 -5.587  1.00 23.26 ? 227  LYS   A CB  1 
ATOM   1831  C  CG  . LYS   A  1 227 ? 50.272 -24.622 -4.785  1.00 26.13 ? 227  LYS   A CG  1 
ATOM   1832  C  CD  . LYS   A  1 227 ? 49.576 -25.981 -4.601  1.00 37.24 ? 227  LYS   A CD  1 
ATOM   1833  C  CE  . LYS   A  1 227 ? 49.446 -26.712 -5.923  1.00 45.19 ? 227  LYS   A CE  1 
ATOM   1834  N  NZ  . LYS   A  1 227 ? 48.794 -28.065 -5.776  1.00 49.66 ? 227  LYS   A NZ  1 
ATOM   1835  N  N   . LEU   A  1 228 ? 48.321 -20.476 -6.152  1.00 19.89 ? 228  LEU   A N   1 
ATOM   1836  C  CA  . LEU   A  1 228 ? 47.681 -19.524 -7.050  1.00 19.53 ? 228  LEU   A CA  1 
ATOM   1837  C  C   . LEU   A  1 228 ? 48.729 -18.680 -7.758  1.00 19.68 ? 228  LEU   A C   1 
ATOM   1838  O  O   . LEU   A  1 228 ? 49.873 -18.568 -7.294  1.00 19.69 ? 228  LEU   A O   1 
ATOM   1839  C  CB  . LEU   A  1 228 ? 46.761 -18.586 -6.277  1.00 20.20 ? 228  LEU   A CB  1 
ATOM   1840  C  CG  . LEU   A  1 228 ? 45.622 -19.325 -5.580  1.00 20.85 ? 228  LEU   A CG  1 
ATOM   1841  C  CD1 . LEU   A  1 228 ? 44.974 -18.414 -4.501  1.00 22.69 ? 228  LEU   A CD1 1 
ATOM   1842  C  CD2 . LEU   A  1 228 ? 44.609 -19.700 -6.591  1.00 23.65 ? 228  LEU   A CD2 1 
ATOM   1843  N  N   . ASN   A  1 229 ? 48.297 -18.031 -8.846  1.00 19.84 ? 229  ASN   A N   1 
ATOM   1844  C  CA  . ASN   A  1 229 ? 49.156 -17.172 -9.662  1.00 20.33 ? 229  ASN   A CA  1 
ATOM   1845  C  C   . ASN   A  1 229 ? 48.532 -15.777 -9.818  1.00 19.76 ? 229  ASN   A C   1 
ATOM   1846  O  O   . ASN   A  1 229 ? 47.306 -15.638 -9.950  1.00 19.63 ? 229  ASN   A O   1 
ATOM   1847  C  CB  . ASN   A  1 229 ? 49.360 -17.786 -11.068 1.00 22.22 ? 229  ASN   A CB  1 
ATOM   1848  C  CG  . ASN   A  1 229 ? 50.319 -18.977 -11.091 1.00 27.71 ? 229  ASN   A CG  1 
ATOM   1849  O  OD1 . ASN   A  1 229 ? 50.951 -19.303 -10.118 1.00 27.50 ? 229  ASN   A OD1 1 
ATOM   1850  N  ND2 . ASN   A  1 229 ? 50.439 -19.608 -12.256 1.00 33.22 ? 229  ASN   A ND2 1 
ATOM   1851  N  N   . PHE   A  1 230 ? 49.394 -14.746 -9.838  1.00 19.33 ? 230  PHE   A N   1 
ATOM   1852  C  CA  . PHE   A  1 230 ? 48.919 -13.394 -10.138 1.00 19.06 ? 230  PHE   A CA  1 
ATOM   1853  C  C   . PHE   A  1 230 ? 48.563 -13.239 -11.590 1.00 20.51 ? 230  PHE   A C   1 
ATOM   1854  O  O   . PHE   A  1 230 ? 47.680 -12.449 -11.928 1.00 20.27 ? 230  PHE   A O   1 
ATOM   1855  C  CB  . PHE   A  1 230 ? 49.995 -12.345 -9.851  1.00 19.38 ? 230  PHE   A CB  1 
ATOM   1856  C  CG  . PHE   A  1 230 ? 50.335 -12.142 -8.419  1.00 18.33 ? 230  PHE   A CG  1 
ATOM   1857  C  CD1 . PHE   A  1 230 ? 49.383 -11.655 -7.492  1.00 17.49 ? 230  PHE   A CD1 1 
ATOM   1858  C  CD2 . PHE   A  1 230 ? 51.648 -12.298 -8.024  1.00 18.78 ? 230  PHE   A CD2 1 
ATOM   1859  C  CE1 . PHE   A  1 230 ? 49.759 -11.349 -6.190  1.00 17.78 ? 230  PHE   A CE1 1 
ATOM   1860  C  CE2 . PHE   A  1 230 ? 52.039 -11.998 -6.702  1.00 18.38 ? 230  PHE   A CE2 1 
ATOM   1861  C  CZ  . PHE   A  1 230 ? 51.098 -11.529 -5.786  1.00 18.45 ? 230  PHE   A CZ  1 
ATOM   1862  N  N   . ASN   A  1 231 ? 49.294 -13.919 -12.476 1.00 21.15 ? 231  ASN   A N   1 
ATOM   1863  C  CA  . ASN   A  1 231 ? 49.164 -13.690 -13.904 1.00 22.37 ? 231  ASN   A CA  1 
ATOM   1864  C  C   . ASN   A  1 231 ? 47.916 -14.342 -14.500 1.00 22.91 ? 231  ASN   A C   1 
ATOM   1865  O  O   . ASN   A  1 231 ? 47.285 -15.223 -13.913 1.00 22.58 ? 231  ASN   A O   1 
ATOM   1866  C  CB  . ASN   A  1 231 ? 50.393 -14.249 -14.614 1.00 25.05 ? 231  ASN   A CB  1 
ATOM   1867  C  CG  . ASN   A  1 231 ? 50.607 -15.745 -14.296 1.00 24.07 ? 231  ASN   A CG  1 
ATOM   1868  O  OD1 . ASN   A  1 231 ? 51.065 -16.084 -13.234 1.00 23.39 ? 231  ASN   A OD1 1 
ATOM   1869  N  ND2 . ASN   A  1 231 ? 50.265 -16.629 -15.249 1.00 25.90 ? 231  ASN   A ND2 1 
ATOM   1870  N  N   . GLY   A  1 232 ? 47.554 -13.856 -15.685 1.00 24.23 ? 232  GLY   A N   1 
ATOM   1871  C  CA  . GLY   A  1 232 ? 46.584 -14.561 -16.491 1.00 26.42 ? 232  GLY   A CA  1 
ATOM   1872  C  C   . GLY   A  1 232 ? 47.206 -15.704 -17.269 1.00 27.86 ? 232  GLY   A C   1 
ATOM   1873  O  O   . GLY   A  1 232 ? 48.417 -15.778 -17.492 1.00 28.50 ? 232  GLY   A O   1 
ATOM   1874  N  N   . GLU   A  1 233 ? 46.350 -16.605 -17.717 1.00 30.07 ? 233  GLU   A N   1 
ATOM   1875  C  CA  . GLU   A  1 233 ? 46.804 -17.726 -18.543 1.00 37.37 ? 233  GLU   A CA  1 
ATOM   1876  C  C   . GLU   A  1 233 ? 47.537 -17.229 -19.794 1.00 35.10 ? 233  GLU   A C   1 
ATOM   1877  O  O   . GLU   A  1 233 ? 47.095 -16.291 -20.462 1.00 37.44 ? 233  GLU   A O   1 
ATOM   1878  C  CB  . GLU   A  1 233 ? 45.584 -18.573 -18.905 1.00 44.10 ? 233  GLU   A CB  1 
ATOM   1879  C  CG  . GLU   A  1 233 ? 45.840 -20.015 -19.208 1.00 53.22 ? 233  GLU   A CG  1 
ATOM   1880  C  CD  . GLU   A  1 233 ? 44.525 -20.780 -19.359 1.00 62.81 ? 233  GLU   A CD  1 
ATOM   1881  O  OE1 . GLU   A  1 233 ? 44.046 -21.389 -18.365 1.00 63.72 ? 233  GLU   A OE1 1 
ATOM   1882  O  OE2 . GLU   A  1 233 ? 43.950 -20.740 -20.470 1.00 67.72 ? 233  GLU   A OE2 1 
ATOM   1883  N  N   . GLY   A  1 234 ? 48.686 -17.843 -20.118 1.00 34.19 ? 234  GLY   A N   1 
ATOM   1884  C  CA  . GLY   A  1 234 ? 49.463 -17.422 -21.275 1.00 35.35 ? 234  GLY   A CA  1 
ATOM   1885  C  C   . GLY   A  1 234 ? 50.468 -16.308 -21.028 1.00 36.55 ? 234  GLY   A C   1 
ATOM   1886  O  O   . GLY   A  1 234 ? 51.192 -15.915 -21.962 1.00 37.43 ? 234  GLY   A O   1 
ATOM   1887  N  N   . GLU   A  1 235 ? 50.562 -15.811 -19.805 1.00 36.61 ? 235  GLU   A N   1 
ATOM   1888  C  CA  . GLU   A  1 235 ? 51.579 -14.862 -19.392 1.00 34.60 ? 235  GLU   A CA  1 
ATOM   1889  C  C   . GLU   A  1 235 ? 52.601 -15.552 -18.510 1.00 35.36 ? 235  GLU   A C   1 
ATOM   1890  O  O   . GLU   A  1 235 ? 52.328 -16.632 -17.980 1.00 32.71 ? 235  GLU   A O   1 
ATOM   1891  C  CB  . GLU   A  1 235 ? 50.939 -13.712 -18.634 1.00 34.45 ? 235  GLU   A CB  1 
ATOM   1892  C  CG  . GLU   A  1 235 ? 49.765 -13.108 -19.371 1.00 36.64 ? 235  GLU   A CG  1 
ATOM   1893  C  CD  . GLU   A  1 235 ? 49.160 -11.955 -18.577 1.00 40.08 ? 235  GLU   A CD  1 
ATOM   1894  O  OE1 . GLU   A  1 235 ? 48.790 -10.926 -19.197 1.00 43.25 ? 235  GLU   A OE1 1 
ATOM   1895  O  OE2 . GLU   A  1 235 ? 49.076 -12.081 -17.342 1.00 34.37 ? 235  GLU   A OE2 1 
ATOM   1896  N  N   . PRO   A  1 236 ? 53.808 -14.990 -18.352 1.00 37.23 ? 236  PRO   A N   1 
ATOM   1897  C  CA  . PRO   A  1 236 ? 54.821 -15.687 -17.545 1.00 38.83 ? 236  PRO   A CA  1 
ATOM   1898  C  C   . PRO   A  1 236 ? 54.321 -15.900 -16.127 1.00 32.12 ? 236  PRO   A C   1 
ATOM   1899  O  O   . PRO   A  1 236 ? 53.659 -15.033 -15.555 1.00 30.56 ? 236  PRO   A O   1 
ATOM   1900  C  CB  . PRO   A  1 236 ? 56.038 -14.758 -17.602 1.00 42.64 ? 236  PRO   A CB  1 
ATOM   1901  C  CG  . PRO   A  1 236 ? 55.863 -14.025 -18.943 1.00 42.77 ? 236  PRO   A CG  1 
ATOM   1902  C  CD  . PRO   A  1 236 ? 54.356 -13.806 -19.043 1.00 39.66 ? 236  PRO   A CD  1 
ATOM   1903  N  N   . GLU   A  1 237 ? 54.642 -17.070 -15.577 1.00 35.47 ? 237  GLU   A N   1 
ATOM   1904  C  CA  . GLU   A  1 237 ? 54.089 -17.461 -14.285 1.00 36.09 ? 237  GLU   A CA  1 
ATOM   1905  C  C   . GLU   A  1 237 ? 54.625 -16.572 -13.174 1.00 33.61 ? 237  GLU   A C   1 
ATOM   1906  O  O   . GLU   A  1 237 ? 55.834 -16.381 -13.033 1.00 33.69 ? 237  GLU   A O   1 
ATOM   1907  C  CB  . GLU   A  1 237 ? 54.413 -18.921 -13.972 1.00 42.55 ? 237  GLU   A CB  1 
ATOM   1908  C  CG  . GLU   A  1 237 ? 54.150 -19.269 -12.509 1.00 49.82 ? 237  GLU   A CG  1 
ATOM   1909  C  CD  . GLU   A  1 237 ? 53.992 -20.764 -12.239 1.00 58.28 ? 237  GLU   A CD  1 
ATOM   1910  O  OE1 . GLU   A  1 237 ? 53.135 -21.421 -12.881 1.00 61.16 ? 237  GLU   A OE1 1 
ATOM   1911  O  OE2 . GLU   A  1 237 ? 54.740 -21.280 -11.371 1.00 60.07 ? 237  GLU   A OE2 1 
ATOM   1912  N  N   . GLU   A  1 238 ? 53.720 -16.034 -12.369 1.00 26.25 ? 238  GLU   A N   1 
ATOM   1913  C  CA  . GLU   A  1 238 ? 54.081 -15.240 -11.194 1.00 24.80 ? 238  GLU   A CA  1 
ATOM   1914  C  C   . GLU   A  1 238 ? 53.295 -15.809 -10.027 1.00 24.41 ? 238  GLU   A C   1 
ATOM   1915  O  O   . GLU   A  1 238 ? 52.107 -15.479 -9.873  1.00 24.62 ? 238  GLU   A O   1 
ATOM   1916  C  CB  . GLU   A  1 238 ? 53.757 -13.768 -11.356 1.00 27.83 ? 238  GLU   A CB  1 
ATOM   1917  C  CG  . GLU   A  1 238 ? 54.358 -13.139 -12.621 1.00 36.57 ? 238  GLU   A CG  1 
ATOM   1918  C  CD  . GLU   A  1 238 ? 53.737 -11.777 -12.927 1.00 45.11 ? 238  GLU   A CD  1 
ATOM   1919  O  OE1 . GLU   A  1 238 ? 52.853 -11.333 -12.152 1.00 46.46 ? 238  GLU   A OE1 1 
ATOM   1920  O  OE2 . GLU   A  1 238 ? 54.106 -11.157 -13.956 1.00 48.30 ? 238  GLU   A OE2 1 
ATOM   1921  N  N   . PRO   A  1 239 ? 53.927 -16.602 -9.176  1.00 22.93 ? 239  PRO   A N   1 
ATOM   1922  C  CA  . PRO   A  1 239 ? 53.227 -17.146 -8.005  1.00 22.45 ? 239  PRO   A CA  1 
ATOM   1923  C  C   . PRO   A  1 239 ? 52.598 -16.043 -7.164  1.00 20.14 ? 239  PRO   A C   1 
ATOM   1924  O  O   . PRO   A  1 239 ? 53.204 -15.005 -6.900  1.00 21.51 ? 239  PRO   A O   1 
ATOM   1925  C  CB  . PRO   A  1 239 ? 54.340 -17.877 -7.240  1.00 24.12 ? 239  PRO   A CB  1 
ATOM   1926  C  CG  . PRO   A  1 239 ? 55.349 -18.273 -8.334  1.00 28.78 ? 239  PRO   A CG  1 
ATOM   1927  C  CD  . PRO   A  1 239 ? 55.289 -17.160 -9.334  1.00 26.60 ? 239  PRO   A CD  1 
ATOM   1928  N  N   . MET   A  1 240 ? 51.370 -16.312 -6.713  1.00 18.58 ? 240  MET   A N   1 
ATOM   1929  C  CA  . MET   A  1 240 ? 50.635 -15.348 -5.891  1.00 17.73 ? 240  MET   A CA  1 
ATOM   1930  C  C   . MET   A  1 240 ? 51.140 -15.516 -4.456  1.00 19.31 ? 240  MET   A C   1 
ATOM   1931  O  O   . MET   A  1 240 ? 50.635 -16.361 -3.702  1.00 17.57 ? 240  MET   A O   1 
ATOM   1932  C  CB  . MET   A  1 240 ? 49.136 -15.611 -5.972  1.00 17.48 ? 240  MET   A CB  1 
ATOM   1933  C  CG  . MET   A  1 240 ? 48.337 -14.486 -5.217  1.00 17.72 ? 240  MET   A CG  1 
ATOM   1934  S  SD  . MET   A  1 240 ? 46.561 -14.774 -5.330  1.00 17.74 ? 240  MET   A SD  1 
ATOM   1935  C  CE  . MET   A  1 240 ? 46.271 -14.076 -6.936  1.00 18.88 ? 240  MET   A CE  1 
ATOM   1936  N  N   . VAL   A  1 241 ? 52.155 -14.719 -4.091  1.00 18.21 ? 241  VAL   A N   1 
ATOM   1937  C  CA  . VAL   A  1 241 ? 52.766 -14.746 -2.759  1.00 17.70 ? 241  VAL   A CA  1 
ATOM   1938  C  C   . VAL   A  1 241 ? 53.124 -13.296 -2.428  1.00 18.33 ? 241  VAL   A C   1 
ATOM   1939  O  O   . VAL   A  1 241 ? 53.337 -12.476 -3.326  1.00 18.70 ? 241  VAL   A O   1 
ATOM   1940  C  CB  . VAL   A  1 241 ? 54.014 -15.656 -2.655  1.00 21.47 ? 241  VAL   A CB  1 
ATOM   1941  C  CG1 . VAL   A  1 241 ? 53.623 -17.127 -2.935  1.00 19.79 ? 241  VAL   A CG1 1 
ATOM   1942  C  CG2 . VAL   A  1 241 ? 55.124 -15.201 -3.578  1.00 20.52 ? 241  VAL   A CG2 1 
ATOM   1943  N  N   . ASP   A  1 242 ? 53.210 -12.991 -1.120  1.00 18.18 ? 242  ASP   A N   1 
ATOM   1944  C  CA  . ASP   A  1 242 ? 53.614 -11.649 -0.673  1.00 17.88 ? 242  ASP   A CA  1 
ATOM   1945  C  C   . ASP   A  1 242 ? 52.685 -10.582 -1.250  1.00 17.68 ? 242  ASP   A C   1 
ATOM   1946  O  O   . ASP   A  1 242 ? 53.107 -9.494  -1.691  1.00 18.17 ? 242  ASP   A O   1 
ATOM   1947  C  CB  . ASP   A  1 242 ? 55.090 -11.381 -1.010  1.00 18.45 ? 242  ASP   A CB  1 
ATOM   1948  C  CG  . ASP   A  1 242 ? 56.034 -12.232 -0.157  1.00 21.24 ? 242  ASP   A CG  1 
ATOM   1949  O  OD1 . ASP   A  1 242 ? 55.732 -12.457 1.045   1.00 18.79 ? 242  ASP   A OD1 1 
ATOM   1950  O  OD2 . ASP   A  1 242 ? 57.069 -12.657 -0.707  1.00 23.61 ? 242  ASP   A OD2 1 
ATOM   1951  N  N   . ASN   A  1 243 ? 51.392 -10.868 -1.164  1.00 15.03 ? 243  ASN   A N   1 
ATOM   1952  C  CA  . ASN   A  1 243 ? 50.335 -9.910  -1.550  1.00 14.76 ? 243  ASN   A CA  1 
ATOM   1953  C  C   . ASN   A  1 243 ? 49.855 -9.127  -0.325  1.00 15.25 ? 243  ASN   A C   1 
ATOM   1954  O  O   . ASN   A  1 243 ? 48.655 -9.013  -0.057  1.00 16.78 ? 243  ASN   A O   1 
ATOM   1955  C  CB  . ASN   A  1 243 ? 49.168 -10.601 -2.267  1.00 15.71 ? 243  ASN   A CB  1 
ATOM   1956  C  CG  . ASN   A  1 243 ? 48.553 -11.772 -1.477  1.00 15.04 ? 243  ASN   A CG  1 
ATOM   1957  O  OD1 . ASN   A  1 243 ? 49.004 -12.112 -0.385  1.00 17.61 ? 243  ASN   A OD1 1 
ATOM   1958  N  ND2 . ASN   A  1 243 ? 47.490 -12.376 -2.045  1.00 17.41 ? 243  ASN   A ND2 1 
ATOM   1959  N  N   . TRP   A  1 244 ? 50.826 -8.559  0.374   1.00 15.81 ? 244  TRP   A N   1 
ATOM   1960  C  CA  . TRP   A  1 244 ? 50.601 -7.724  1.549   1.00 16.32 ? 244  TRP   A CA  1 
ATOM   1961  C  C   . TRP   A  1 244 ? 51.272 -6.376  1.370   1.00 17.98 ? 244  TRP   A C   1 
ATOM   1962  O  O   . TRP   A  1 244 ? 52.295 -6.245  0.694   1.00 19.07 ? 244  TRP   A O   1 
ATOM   1963  C  CB  . TRP   A  1 244 ? 51.156 -8.400  2.838   1.00 17.91 ? 244  TRP   A CB  1 
ATOM   1964  C  CG  . TRP   A  1 244 ? 52.566 -8.909  2.756   1.00 19.72 ? 244  TRP   A CG  1 
ATOM   1965  C  CD1 . TRP   A  1 244 ? 52.936 -10.170 2.383   1.00 19.45 ? 244  TRP   A CD1 1 
ATOM   1966  C  CD2 . TRP   A  1 244 ? 53.803 -8.187  3.027   1.00 21.73 ? 244  TRP   A CD2 1 
ATOM   1967  N  NE1 . TRP   A  1 244 ? 54.322 -10.291 2.444   1.00 18.98 ? 244  TRP   A NE1 1 
ATOM   1968  C  CE2 . TRP   A  1 244 ? 54.876 -9.088  2.812   1.00 22.48 ? 244  TRP   A CE2 1 
ATOM   1969  C  CE3 . TRP   A  1 244 ? 54.107 -6.856  3.412   1.00 22.70 ? 244  TRP   A CE3 1 
ATOM   1970  C  CZ2 . TRP   A  1 244 ? 56.248 -8.719  2.951   1.00 27.29 ? 244  TRP   A CZ2 1 
ATOM   1971  C  CZ3 . TRP   A  1 244 ? 55.455 -6.482  3.548   1.00 24.56 ? 244  TRP   A CZ3 1 
ATOM   1972  C  CH2 . TRP   A  1 244 ? 56.520 -7.423  3.353   1.00 25.87 ? 244  TRP   A CH2 1 
ATOM   1973  N  N   . ARG   A  1 245 ? 50.651 -5.361  1.982   1.00 15.60 ? 245  ARG   A N   1 
ATOM   1974  C  CA  . ARG   A  1 245 ? 51.235 -4.007  2.051   1.00 15.37 ? 245  ARG   A CA  1 
ATOM   1975  C  C   . ARG   A  1 245 ? 52.031 -3.849  3.349   1.00 16.05 ? 245  ARG   A C   1 
ATOM   1976  O  O   . ARG   A  1 245 ? 51.533 -4.262  4.395   1.00 18.62 ? 245  ARG   A O   1 
ATOM   1977  C  CB  . ARG   A  1 245 ? 50.097 -2.974  1.996   1.00 14.94 ? 245  ARG   A CB  1 
ATOM   1978  C  CG  . ARG   A  1 245 ? 50.665 -1.559  1.834   1.00 13.43 ? 245  ARG   A CG  1 
ATOM   1979  C  CD  . ARG   A  1 245 ? 49.600 -0.475  1.955   1.00 15.99 ? 245  ARG   A CD  1 
ATOM   1980  N  NE  . ARG   A  1 245 ? 50.196 0.807   1.583   1.00 14.75 ? 245  ARG   A NE  1 
ATOM   1981  C  CZ  . ARG   A  1 245 ? 49.639 1.998   1.811   1.00 14.96 ? 245  ARG   A CZ  1 
ATOM   1982  N  NH1 . ARG   A  1 245 ? 48.472 2.136   2.500   1.00 14.45 ? 245  ARG   A NH1 1 
ATOM   1983  N  NH2 . ARG   A  1 245 ? 50.287 3.092   1.324   1.00 15.75 ? 245  ARG   A NH2 1 
ATOM   1984  N  N   . PRO   A  1 246 ? 53.229 -3.226  3.299   1.00 16.63 ? 246  PRO   A N   1 
ATOM   1985  C  CA  . PRO   A  1 246 ? 53.979 -2.909  4.552   1.00 17.87 ? 246  PRO   A CA  1 
ATOM   1986  C  C   . PRO   A  1 246 ? 53.139 -2.017  5.473   1.00 17.31 ? 246  PRO   A C   1 
ATOM   1987  O  O   . PRO   A  1 246 ? 52.270 -1.259  5.014   1.00 17.36 ? 246  PRO   A O   1 
ATOM   1988  C  CB  . PRO   A  1 246 ? 55.244 -2.159  4.070   1.00 22.23 ? 246  PRO   A CB  1 
ATOM   1989  C  CG  . PRO   A  1 246 ? 55.447 -2.589  2.626   1.00 19.82 ? 246  PRO   A CG  1 
ATOM   1990  C  CD  . PRO   A  1 246 ? 53.987 -2.846  2.091   1.00 19.28 ? 246  PRO   A CD  1 
ATOM   1991  N  N   . THR   A  1 247 ? 53.394 -2.113  6.772   1.00 18.34 ? 247  THR   A N   1 
ATOM   1992  C  CA  . THR   A  1 247 ? 52.701 -1.207  7.687   1.00 17.59 ? 247  THR   A CA  1 
ATOM   1993  C  C   . THR   A  1 247 ? 53.116 0.253   7.445   1.00 17.05 ? 247  THR   A C   1 
ATOM   1994  O  O   . THR   A  1 247 ? 54.246 0.576   7.043   1.00 19.09 ? 247  THR   A O   1 
ATOM   1995  C  CB  . THR   A  1 247 ? 52.957 -1.555  9.162   1.00 18.51 ? 247  THR   A CB  1 
ATOM   1996  O  OG1 . THR   A  1 247 ? 54.364 -1.628  9.411   1.00 19.89 ? 247  THR   A OG1 1 
ATOM   1997  C  CG2 . THR   A  1 247 ? 52.351 -2.916  9.498   1.00 18.51 ? 247  THR   A CG2 1 
ATOM   1998  N  N   . GLN   A  1 248 ? 52.160 1.145   7.663   1.00 15.50 ? 248  GLN   A N   1 
ATOM   1999  C  CA  . GLN   A  1 248 ? 52.265 2.557   7.386   1.00 14.73 ? 248  GLN   A CA  1 
ATOM   2000  C  C   . GLN   A  1 248 ? 52.234 3.369   8.677   1.00 16.06 ? 248  GLN   A C   1 
ATOM   2001  O  O   . GLN   A  1 248 ? 51.785 2.881   9.719   1.00 17.71 ? 248  GLN   A O   1 
ATOM   2002  C  CB  . GLN   A  1 248 ? 51.103 2.992   6.467   1.00 15.72 ? 248  GLN   A CB  1 
ATOM   2003  C  CG  . GLN   A  1 248 ? 51.038 2.202   5.125   1.00 15.58 ? 248  GLN   A CG  1 
ATOM   2004  C  CD  . GLN   A  1 248 ? 52.323 2.432   4.334   1.00 15.39 ? 248  GLN   A CD  1 
ATOM   2005  O  OE1 . GLN   A  1 248 ? 52.772 3.578   4.151   1.00 18.18 ? 248  GLN   A OE1 1 
ATOM   2006  N  NE2 . GLN   A  1 248 ? 52.938 1.334   3.915   1.00 15.44 ? 248  GLN   A NE2 1 
ATOM   2007  N  N   . PRO   A  1 249 ? 52.691 4.612   8.638   1.00 16.53 ? 249  PRO   A N   1 
ATOM   2008  C  CA  . PRO   A  1 249 ? 52.780 5.424   9.858   1.00 18.33 ? 249  PRO   A CA  1 
ATOM   2009  C  C   . PRO   A  1 249 ? 51.390 5.656   10.436  1.00 17.86 ? 249  PRO   A C   1 
ATOM   2010  O  O   . PRO   A  1 249 ? 50.457 5.983   9.713   1.00 17.89 ? 249  PRO   A O   1 
ATOM   2011  C  CB  . PRO   A  1 249 ? 53.389 6.742   9.367   1.00 19.98 ? 249  PRO   A CB  1 
ATOM   2012  C  CG  . PRO   A  1 249 ? 54.184 6.358   8.126   1.00 19.46 ? 249  PRO   A CG  1 
ATOM   2013  C  CD  . PRO   A  1 249 ? 53.304 5.277   7.468   1.00 17.99 ? 249  PRO   A CD  1 
ATOM   2014  N  N   . LEU   A  1 250 ? 51.278 5.533   11.754  1.00 18.35 ? 250  LEU   A N   1 
ATOM   2015  C  CA  . LEU   A  1 250 ? 50.015 5.828   12.440  1.00 18.53 ? 250  LEU   A CA  1 
ATOM   2016  C  C   . LEU   A  1 250 ? 49.664 7.311   12.351  1.00 18.41 ? 250  LEU   A C   1 
ATOM   2017  O  O   . LEU   A  1 250 ? 48.472 7.666   12.322  1.00 20.43 ? 250  LEU   A O   1 
ATOM   2018  C  CB  . LEU   A  1 250 ? 50.128 5.370   13.919  1.00 22.41 ? 250  LEU   A CB  1 
ATOM   2019  C  CG  . LEU   A  1 250 ? 48.830 5.293   14.722  1.00 24.13 ? 250  LEU   A CG  1 
ATOM   2020  C  CD1 . LEU   A  1 250 ? 47.733 4.450   14.014  1.00 20.91 ? 250  LEU   A CD1 1 
ATOM   2021  C  CD2 . LEU   A  1 250 ? 49.134 4.748   16.146  1.00 27.11 ? 250  LEU   A CD2 1 
ATOM   2022  N  N   . LYS   A  1 251 ? 50.664 8.215   12.308  1.00 18.25 ? 251  LYS   A N   1 
ATOM   2023  C  CA  . LYS   A  1 251 ? 50.415 9.647   12.283  1.00 19.77 ? 251  LYS   A CA  1 
ATOM   2024  C  C   . LYS   A  1 251 ? 49.518 10.020  13.451  1.00 22.59 ? 251  LYS   A C   1 
ATOM   2025  O  O   . LYS   A  1 251 ? 49.770 9.583   14.588  1.00 23.98 ? 251  LYS   A O   1 
ATOM   2026  C  CB  . LYS   A  1 251 ? 49.888 10.074  10.914  1.00 21.81 ? 251  LYS   A CB  1 
ATOM   2027  C  CG  . LYS   A  1 251 ? 50.948 9.699   9.814   1.00 25.95 ? 251  LYS   A CG  1 
ATOM   2028  C  CD  . LYS   A  1 251 ? 50.708 10.341  8.443   1.00 26.07 ? 251  LYS   A CD  1 
ATOM   2029  C  CE  . LYS   A  1 251 ? 51.780 9.891   7.455   1.00 30.16 ? 251  LYS   A CE  1 
ATOM   2030  N  NZ  . LYS   A  1 251 ? 51.557 10.475  6.098   1.00 31.35 ? 251  LYS   A NZ  1 
ATOM   2031  N  N   . ASN   A  1 252 ? 48.520 10.863  13.203  1.00 21.60 ? 252  ASN   A N   1 
ATOM   2032  C  CA  . ASN   A  1 252 ? 47.755 11.464  14.286  1.00 24.16 ? 252  ASN   A CA  1 
ATOM   2033  C  C   . ASN   A  1 252 ? 46.476 10.666  14.495  1.00 27.04 ? 252  ASN   A C   1 
ATOM   2034  O  O   . ASN   A  1 252 ? 45.356 11.171  14.282  1.00 31.12 ? 252  ASN   A O   1 
ATOM   2035  C  CB  . ASN   A  1 252 ? 47.459 12.928  13.971  1.00 28.34 ? 252  ASN   A CB  1 
ATOM   2036  C  CG  . ASN   A  1 252 ? 46.933 13.649  15.151  1.00 34.48 ? 252  ASN   A CG  1 
ATOM   2037  O  OD1 . ASN   A  1 252 ? 46.927 13.112  16.271  1.00 34.07 ? 252  ASN   A OD1 1 
ATOM   2038  N  ND2 . ASN   A  1 252 ? 46.441 14.863  14.930  1.00 38.81 ? 252  ASN   A ND2 1 
ATOM   2039  N  N   . ARG   A  1 253 ? 46.679 9.393   14.876  1.00 21.66 ? 253  ARG   A N   1 
ATOM   2040  C  CA  . ARG   A  1 253 ? 45.601 8.444   15.165  1.00 22.05 ? 253  ARG   A CA  1 
ATOM   2041  C  C   . ARG   A  1 253 ? 45.897 7.682   16.455  1.00 24.18 ? 253  ARG   A C   1 
ATOM   2042  O  O   . ARG   A  1 253 ? 47.054 7.600   16.893  1.00 27.29 ? 253  ARG   A O   1 
ATOM   2043  C  CB  . ARG   A  1 253 ? 45.397 7.417   14.013  1.00 20.85 ? 253  ARG   A CB  1 
ATOM   2044  C  CG  . ARG   A  1 253 ? 44.878 8.077   12.748  1.00 19.85 ? 253  ARG   A CG  1 
ATOM   2045  C  CD  . ARG   A  1 253 ? 44.779 7.068   11.589  1.00 19.33 ? 253  ARG   A CD  1 
ATOM   2046  N  NE  . ARG   A  1 253 ? 46.101 6.641   11.149  1.00 18.34 ? 253  ARG   A NE  1 
ATOM   2047  C  CZ  . ARG   A  1 253 ? 46.320 5.686   10.248  1.00 16.70 ? 253  ARG   A CZ  1 
ATOM   2048  N  NH1 . ARG   A  1 253 ? 45.297 4.990   9.745   1.00 17.04 ? 253  ARG   A NH1 1 
ATOM   2049  N  NH2 . ARG   A  1 253 ? 47.557 5.415   9.840   1.00 16.36 ? 253  ARG   A NH2 1 
ATOM   2050  N  N   . GLN   A  1 254 ? 44.837 7.120   17.040  1.00 23.40 ? 254  GLN   A N   1 
ATOM   2051  C  CA  . GLN   A  1 254 ? 44.910 6.353   18.283  1.00 28.34 ? 254  GLN   A CA  1 
ATOM   2052  C  C   . GLN   A  1 254 ? 44.283 4.999   18.011  1.00 27.30 ? 254  GLN   A C   1 
ATOM   2053  O  O   . GLN   A  1 254 ? 43.196 4.924   17.419  1.00 30.04 ? 254  GLN   A O   1 
ATOM   2054  C  CB  . GLN   A  1 254 ? 44.164 7.055   19.436  1.00 34.45 ? 254  GLN   A CB  1 
ATOM   2055  C  CG  . GLN   A  1 254 ? 44.572 8.482   19.602  1.00 43.53 ? 254  GLN   A CG  1 
ATOM   2056  C  CD  . GLN   A  1 254 ? 43.686 9.240   20.568  1.00 51.72 ? 254  GLN   A CD  1 
ATOM   2057  O  OE1 . GLN   A  1 254 ? 44.181 9.849   21.517  1.00 56.87 ? 254  GLN   A OE1 1 
ATOM   2058  N  NE2 . GLN   A  1 254 ? 42.369 9.218   20.329  1.00 53.64 ? 254  GLN   A NE2 1 
ATOM   2059  N  N   . ILE   A  1 255 ? 44.983 3.933   18.400  1.00 23.95 ? 255  ILE   A N   1 
ATOM   2060  C  CA  . ILE   A  1 255 ? 44.422 2.594   18.311  1.00 23.14 ? 255  ILE   A CA  1 
ATOM   2061  C  C   . ILE   A  1 255 ? 43.722 2.335   19.635  1.00 24.08 ? 255  ILE   A C   1 
ATOM   2062  O  O   . ILE   A  1 255 ? 44.307 2.511   20.713  1.00 26.47 ? 255  ILE   A O   1 
ATOM   2063  C  CB  . ILE   A  1 255 ? 45.499 1.544   18.001  1.00 22.48 ? 255  ILE   A CB  1 
ATOM   2064  C  CG1 . ILE   A  1 255 ? 46.170 1.875   16.659  1.00 24.51 ? 255  ILE   A CG1 1 
ATOM   2065  C  CG2 . ILE   A  1 255 ? 44.859 0.139   17.880  1.00 23.15 ? 255  ILE   A CG2 1 
ATOM   2066  C  CD1 . ILE   A  1 255 ? 47.272 0.856   16.239  1.00 23.86 ? 255  ILE   A CD1 1 
ATOM   2067  N  N   . LYS   A  1 256 ? 42.439 1.996   19.564  1.00 23.42 ? 256  LYS   A N   1 
ATOM   2068  C  CA  . LYS   A  1 256 ? 41.662 1.735   20.770  1.00 23.51 ? 256  LYS   A CA  1 
ATOM   2069  C  C   . LYS   A  1 256 ? 41.475 0.232   20.957  1.00 23.60 ? 256  LYS   A C   1 
ATOM   2070  O  O   . LYS   A  1 256 ? 41.428 -0.524  19.992  1.00 24.52 ? 256  LYS   A O   1 
ATOM   2071  C  CB  . LYS   A  1 256 ? 40.282 2.410   20.712  1.00 24.79 ? 256  LYS   A CB  1 
ATOM   2072  C  CG  . LYS   A  1 256 ? 40.291 3.930   20.618  1.00 27.12 ? 256  LYS   A CG  1 
ATOM   2073  C  CD  . LYS   A  1 256 ? 41.115 4.531   21.776  1.00 32.48 ? 256  LYS   A CD  1 
ATOM   2074  C  CE  . LYS   A  1 256 ? 40.937 6.038   21.866  1.00 38.28 ? 256  LYS   A CE  1 
ATOM   2075  N  NZ  . LYS   A  1 256 ? 41.820 6.582   22.982  1.00 41.21 ? 256  LYS   A NZ  1 
ATOM   2076  N  N   . ALA   A  1 257 ? 41.388 -0.200  22.206  1.00 25.45 ? 257  ALA   A N   1 
ATOM   2077  C  CA  . ALA   A  1 257 ? 41.096 -1.593  22.540  1.00 26.11 ? 257  ALA   A CA  1 
ATOM   2078  C  C   . ALA   A  1 257 ? 39.681 -1.741  23.081  1.00 26.15 ? 257  ALA   A C   1 
ATOM   2079  O  O   . ALA   A  1 257 ? 39.185 -0.881  23.819  1.00 27.02 ? 257  ALA   A O   1 
ATOM   2080  C  CB  . ALA   A  1 257 ? 42.065 -2.142  23.590  1.00 26.67 ? 257  ALA   A CB  1 
ATOM   2081  N  N   . SER   A  1 258 ? 39.042 -2.862  22.734  1.00 25.06 ? 258  SER   A N   1 
ATOM   2082  C  CA  . SER   A  1 258 ? 37.674 -3.151  23.232  1.00 24.82 ? 258  SER   A CA  1 
ATOM   2083  C  C   . SER   A  1 258 ? 37.768 -3.738  24.640  1.00 29.03 ? 258  SER   A C   1 
ATOM   2084  O  O   . SER   A  1 258 ? 36.724 -3.819  25.317  1.00 31.62 ? 258  SER   A O   1 
ATOM   2085  C  CB  . SER   A  1 258 ? 36.993 -4.135  22.334  1.00 23.83 ? 258  SER   A CB  1 
ATOM   2086  O  OG  . SER   A  1 258 ? 37.655 -5.391  22.373  1.00 25.39 ? 258  SER   A OG  1 
ATOM   2087  N  N   . PHE   A  1 259 ? 38.970 -4.147  25.042  1.00 28.02 ? 259  PHE   A N   1 
ATOM   2088  C  CA  . PHE   A  1 259 ? 39.140 -4.823  26.353  1.00 30.80 ? 259  PHE   A CA  1 
ATOM   2089  C  C   . PHE   A  1 259 ? 39.939 -3.927  27.292  1.00 33.01 ? 259  PHE   A C   1 
ATOM   2090  O  O   . PHE   A  1 259 ? 40.819 -3.172  26.838  1.00 33.46 ? 259  PHE   A O   1 
ATOM   2091  C  CB  . PHE   A  1 259 ? 39.818 -6.168  26.075  1.00 31.01 ? 259  PHE   A CB  1 
ATOM   2092  C  CG  . PHE   A  1 259 ? 41.065 -6.086  25.204  1.00 30.24 ? 259  PHE   A CG  1 
ATOM   2093  C  CD1 . PHE   A  1 259 ? 40.977 -6.175  23.819  1.00 29.57 ? 259  PHE   A CD1 1 
ATOM   2094  C  CD2 . PHE   A  1 259 ? 42.323 -5.925  25.773  1.00 33.69 ? 259  PHE   A CD2 1 
ATOM   2095  C  CE1 . PHE   A  1 259 ? 42.113 -6.100  23.030  1.00 30.49 ? 259  PHE   A CE1 1 
ATOM   2096  C  CE2 . PHE   A  1 259 ? 43.455 -5.850  24.979  1.00 31.16 ? 259  PHE   A CE2 1 
ATOM   2097  C  CZ  . PHE   A  1 259 ? 43.348 -5.938  23.610  1.00 32.13 ? 259  PHE   A CZ  1 
ATOM   2098  N  N   . LYS   A  1 260 ? 39.622 -4.018  28.586  1.00 65.87 ? 260  LYS   A N   1 
ATOM   2099  C  CA  . LYS   A  1 260 ? 40.457 -3.414  29.654  1.00 62.65 ? 260  LYS   A CA  1 
ATOM   2100  C  C   . LYS   A  1 260 ? 41.760 -4.219  29.779  1.00 58.62 ? 260  LYS   A C   1 
ATOM   2101  O  O   . LYS   A  1 260 ? 41.745 -5.421  29.530  1.00 56.30 ? 260  LYS   A O   1 
ATOM   2102  C  CB  . LYS   A  1 260 ? 39.681 -3.400  30.974  1.00 63.23 ? 260  LYS   A CB  1 
ATOM   2103  C  CG  . LYS   A  1 260 ? 38.417 -2.553  30.965  1.00 64.93 ? 260  LYS   A CG  1 
ATOM   2104  C  CD  . LYS   A  1 260 ? 37.556 -2.763  32.204  1.00 67.77 ? 260  LYS   A CD  1 
ATOM   2105  C  CE  . LYS   A  1 260 ? 36.409 -1.808  32.281  1.00 70.67 ? 260  LYS   A CE  1 
ATOM   2106  N  NZ  . LYS   A  1 260 ? 36.868 -0.435  32.499  1.00 72.41 ? 260  LYS   A NZ  1 
ATOM   2107  O  OXT . LYS   A  1 260 ? 42.776 -3.603  30.125  1.00 57.58 ? 260  LYS   A OXT 1 
ATOM   2108  N  N   . ALA   B  1 2   ? 21.857 -71.044 21.815  1.00 17.25 ? 2    ALA   B N   1 
ATOM   2109  C  CA  . ALA   B  1 2   ? 23.025 -71.441 20.986  1.00 17.54 ? 2    ALA   B CA  1 
ATOM   2110  C  C   . ALA   B  1 2   ? 24.160 -70.473 21.291  1.00 18.09 ? 2    ALA   B C   1 
ATOM   2111  O  O   . ALA   B  1 2   ? 24.253 -70.015 22.431  1.00 16.37 ? 2    ALA   B O   1 
ATOM   2112  C  CB  . ALA   B  1 2   ? 22.604 -71.436 19.487  1.00 16.64 ? 2    ALA   B CB  1 
ATOM   2113  N  N   . HIS   B  1 3   ? 25.021 -70.109 20.333  1.00 16.79 ? 3    HIS   B N   1 
ATOM   2114  C  CA  . HIS   B  1 3   ? 26.125 -69.217 20.692  1.00 17.00 ? 3    HIS   B CA  1 
ATOM   2115  C  C   . HIS   B  1 3   ? 25.641 -67.802 20.960  1.00 16.36 ? 3    HIS   B C   1 
ATOM   2116  O  O   . HIS   B  1 3   ? 24.867 -67.245 20.189  1.00 17.42 ? 3    HIS   B O   1 
ATOM   2117  C  CB  . HIS   B  1 3   ? 27.181 -69.224 19.577  1.00 17.20 ? 3    HIS   B CB  1 
ATOM   2118  C  CG  . HIS   B  1 3   ? 27.930 -70.507 19.523  1.00 21.95 ? 3    HIS   B CG  1 
ATOM   2119  N  ND1 . HIS   B  1 3   ? 29.295 -70.571 19.613  1.00 26.14 ? 3    HIS   B ND1 1 
ATOM   2120  C  CD2 . HIS   B  1 3   ? 27.490 -71.786 19.520  1.00 23.24 ? 3    HIS   B CD2 1 
ATOM   2121  C  CE1 . HIS   B  1 3   ? 29.676 -71.839 19.579  1.00 26.74 ? 3    HIS   B CE1 1 
ATOM   2122  N  NE2 . HIS   B  1 3   ? 28.595 -72.593 19.527  1.00 24.26 ? 3    HIS   B NE2 1 
ATOM   2123  N  N   . HIS   B  1 4   ? 26.115 -67.191 22.051  1.00 14.92 ? 4    HIS   B N   1 
ATOM   2124  C  CA  . HIS   B  1 4   ? 25.712 -65.826 22.372  1.00 15.48 ? 4    HIS   B CA  1 
ATOM   2125  C  C   . HIS   B  1 4   ? 26.407 -64.863 21.416  1.00 15.08 ? 4    HIS   B C   1 
ATOM   2126  O  O   . HIS   B  1 4   ? 27.541 -65.104 20.948  1.00 15.67 ? 4    HIS   B O   1 
ATOM   2127  C  CB  . HIS   B  1 4   ? 26.078 -65.592 23.856  1.00 15.47 ? 4    HIS   B CB  1 
ATOM   2128  C  CG  . HIS   B  1 4   ? 25.672 -64.280 24.453  1.00 14.66 ? 4    HIS   B CG  1 
ATOM   2129  N  ND1 . HIS   B  1 4   ? 24.340 -63.873 24.617  1.00 13.10 ? 4    HIS   B ND1 1 
ATOM   2130  C  CD2 . HIS   B  1 4   ? 26.434 -63.322 25.014  1.00 15.70 ? 4    HIS   B CD2 1 
ATOM   2131  C  CE1 . HIS   B  1 4   ? 24.342 -62.694 25.243  1.00 14.72 ? 4    HIS   B CE1 1 
ATOM   2132  N  NE2 . HIS   B  1 4   ? 25.596 -62.347 25.497  1.00 14.42 ? 4    HIS   B NE2 1 
ATOM   2133  N  N   . TRP   B  1 5   ? 25.737 -63.725 21.169  1.00 14.91 ? 5    TRP   B N   1 
ATOM   2134  C  CA  . TRP   B  1 5   ? 26.316 -62.725 20.255  1.00 15.61 ? 5    TRP   B CA  1 
ATOM   2135  C  C   . TRP   B  1 5   ? 27.608 -62.104 20.795  1.00 15.71 ? 5    TRP   B C   1 
ATOM   2136  O  O   . TRP   B  1 5   ? 27.937 -62.190 21.983  1.00 15.36 ? 5    TRP   B O   1 
ATOM   2137  C  CB  . TRP   B  1 5   ? 25.296 -61.618 19.973  1.00 15.14 ? 5    TRP   B CB  1 
ATOM   2138  C  CG  . TRP   B  1 5   ? 24.965 -60.726 21.195  1.00 14.08 ? 5    TRP   B CG  1 
ATOM   2139  C  CD1 . TRP   B  1 5   ? 23.980 -60.947 22.133  1.00 14.84 ? 5    TRP   B CD1 1 
ATOM   2140  C  CD2 . TRP   B  1 5   ? 25.664 -59.564 21.581  1.00 14.36 ? 5    TRP   B CD2 1 
ATOM   2141  N  NE1 . TRP   B  1 5   ? 24.005 -59.937 23.086  1.00 15.19 ? 5    TRP   B NE1 1 
ATOM   2142  C  CE2 . TRP   B  1 5   ? 25.051 -59.094 22.792  1.00 13.97 ? 5    TRP   B CE2 1 
ATOM   2143  C  CE3 . TRP   B  1 5   ? 26.759 -58.879 21.060  1.00 13.63 ? 5    TRP   B CE3 1 
ATOM   2144  C  CZ2 . TRP   B  1 5   ? 25.463 -57.925 23.416  1.00 14.07 ? 5    TRP   B CZ2 1 
ATOM   2145  C  CZ3 . TRP   B  1 5   ? 27.195 -57.697 21.695  1.00 14.73 ? 5    TRP   B CZ3 1 
ATOM   2146  C  CH2 . TRP   B  1 5   ? 26.557 -57.245 22.874  1.00 14.89 ? 5    TRP   B CH2 1 
ATOM   2147  N  N   . GLY   B  1 6   ? 28.395 -61.551 19.890  1.00 15.46 ? 6    GLY   B N   1 
ATOM   2148  C  CA  . GLY   B  1 6   ? 29.645 -60.924 20.284  1.00 15.27 ? 6    GLY   B CA  1 
ATOM   2149  C  C   . GLY   B  1 6   ? 30.140 -59.995 19.176  1.00 13.43 ? 6    GLY   B C   1 
ATOM   2150  O  O   . GLY   B  1 6   ? 29.356 -59.363 18.457  1.00 14.55 ? 6    GLY   B O   1 
ATOM   2151  N  N   . TYR   B  1 7   ? 31.472 -59.898 19.084  1.00 15.38 ? 7    TYR   B N   1 
ATOM   2152  C  CA  . TYR   B  1 7   ? 32.153 -59.073 18.087  1.00 15.08 ? 7    TYR   B CA  1 
ATOM   2153  C  C   . TYR   B  1 7   ? 33.158 -59.873 17.299  1.00 17.01 ? 7    TYR   B C   1 
ATOM   2154  O  O   . TYR   B  1 7   ? 34.039 -59.281 16.637  1.00 19.92 ? 7    TYR   B O   1 
ATOM   2155  C  CB  . TYR   B  1 7   ? 32.856 -57.854 18.750  1.00 16.19 ? 7    TYR   B CB  1 
ATOM   2156  C  CG  . TYR   B  1 7   ? 31.886 -56.845 19.326  1.00 14.74 ? 7    TYR   B CG  1 
ATOM   2157  C  CD1 . TYR   B  1 7   ? 31.299 -55.873 18.494  1.00 15.81 ? 7    TYR   B CD1 1 
ATOM   2158  C  CD2 . TYR   B  1 7   ? 31.581 -56.833 20.697  1.00 16.32 ? 7    TYR   B CD2 1 
ATOM   2159  C  CE1 . TYR   B  1 7   ? 30.405 -54.921 19.003  1.00 15.46 ? 7    TYR   B CE1 1 
ATOM   2160  C  CE2 . TYR   B  1 7   ? 30.728 -55.867 21.239  1.00 16.66 ? 7    TYR   B CE2 1 
ATOM   2161  C  CZ  . TYR   B  1 7   ? 30.157 -54.931 20.399  1.00 14.85 ? 7    TYR   B CZ  1 
ATOM   2162  O  OH  . TYR   B  1 7   ? 29.331 -53.969 20.920  1.00 17.53 ? 7    TYR   B OH  1 
ATOM   2163  N  N   . GLY   B  1 8   ? 33.087 -61.203 17.378  1.00 17.30 ? 8    GLY   B N   1 
ATOM   2164  C  CA  . GLY   B  1 8   ? 34.030 -62.057 16.689  1.00 17.49 ? 8    GLY   B CA  1 
ATOM   2165  C  C   . GLY   B  1 8   ? 33.590 -62.355 15.267  1.00 19.82 ? 8    GLY   B C   1 
ATOM   2166  O  O   . GLY   B  1 8   ? 32.619 -61.793 14.746  1.00 17.97 ? 8    GLY   B O   1 
ATOM   2167  N  N   . LYS   B  1 9   ? 34.333 -63.260 14.658  1.00 19.78 ? 9    LYS   B N   1 
ATOM   2168  C  CA  . LYS   B  1 9   ? 34.140 -63.570 13.239  1.00 20.84 ? 9    LYS   B CA  1 
ATOM   2169  C  C   . LYS   B  1 9   ? 32.814 -64.249 12.973  1.00 20.49 ? 9    LYS   B C   1 
ATOM   2170  O  O   . LYS   B  1 9   ? 32.250 -64.068 11.892  1.00 20.37 ? 9    LYS   B O   1 
ATOM   2171  C  CB  . LYS   B  1 9   ? 35.259 -64.484 12.741  1.00 21.77 ? 9    LYS   B CB  1 
ATOM   2172  C  CG  . LYS   B  1 9   ? 36.667 -63.973 13.007  1.00 26.27 ? 9    LYS   B CG  1 
ATOM   2173  C  CD  . LYS   B  1 9   ? 36.793 -62.692 12.238  1.00 28.32 ? 9    LYS   B CD  1 
ATOM   2174  C  CE  . LYS   B  1 9   ? 38.298 -62.239 12.163  1.00 37.66 ? 9    LYS   B CE  1 
ATOM   2175  N  NZ  . LYS   B  1 9   ? 39.145 -63.069 11.222  1.00 42.80 ? 9    LYS   B NZ  1 
ATOM   2176  N  N   . HIS   B  1 10  ? 32.310 -65.077 13.905  1.00 20.26 ? 10   HIS   B N   1 
ATOM   2177  C  CA  . HIS   B  1 10  ? 31.079 -65.798 13.658  1.00 19.31 ? 10   HIS   B CA  1 
ATOM   2178  C  C   . HIS   B  1 10  ? 29.902 -65.167 14.346  1.00 18.29 ? 10   HIS   B C   1 
ATOM   2179  O  O   . HIS   B  1 10  ? 28.769 -65.313 13.871  1.00 20.59 ? 10   HIS   B O   1 
ATOM   2180  C  CB  . HIS   B  1 10  ? 31.188 -67.241 14.149  1.00 20.55 ? 10   HIS   B CB  1 
ATOM   2181  C  CG  . HIS   B  1 10  ? 32.233 -68.032 13.462  1.00 24.27 ? 10   HIS   B CG  1 
ATOM   2182  N  ND1 . HIS   B  1 10  ? 33.291 -68.610 14.123  1.00 28.79 ? 10   HIS   B ND1 1 
ATOM   2183  C  CD2 . HIS   B  1 10  ? 32.337 -68.389 12.170  1.00 26.67 ? 10   HIS   B CD2 1 
ATOM   2184  C  CE1 . HIS   B  1 10  ? 34.050 -69.246 13.237  1.00 30.64 ? 10   HIS   B CE1 1 
ATOM   2185  N  NE2 . HIS   B  1 10  ? 33.505 -69.094 12.039  1.00 27.04 ? 10   HIS   B NE2 1 
ATOM   2186  N  N   . ASN   B  1 11  ? 30.124 -64.409 15.428  1.00 16.73 ? 11   ASN   B N   1 
ATOM   2187  C  CA  . ASN   B  1 11  ? 29.000 -63.891 16.201  1.00 15.38 ? 11   ASN   B CA  1 
ATOM   2188  C  C   . ASN   B  1 11  ? 28.909 -62.372 16.193  1.00 15.80 ? 11   ASN   B C   1 
ATOM   2189  O  O   . ASN   B  1 11  ? 28.114 -61.800 16.947  1.00 14.17 ? 11   ASN   B O   1 
ATOM   2190  C  CB  . ASN   B  1 11  ? 29.081 -64.418 17.652  1.00 16.27 ? 11   ASN   B CB  1 
ATOM   2191  C  CG  . ASN   B  1 11  ? 30.282 -63.912 18.387  1.00 19.29 ? 11   ASN   B CG  1 
ATOM   2192  O  OD1 . ASN   B  1 11  ? 31.011 -63.047 17.897  1.00 18.92 ? 11   ASN   B OD1 1 
ATOM   2193  N  ND2 . ASN   B  1 11  ? 30.484 -64.409 19.593  1.00 20.71 ? 11   ASN   B ND2 1 
ATOM   2194  N  N   . GLY   B  1 12  ? 29.686 -61.690 15.354  1.00 15.17 ? 12   GLY   B N   1 
ATOM   2195  C  CA  . GLY   B  1 12  ? 29.796 -60.236 15.424  1.00 16.35 ? 12   GLY   B CA  1 
ATOM   2196  C  C   . GLY   B  1 12  ? 28.757 -59.471 14.614  1.00 16.03 ? 12   GLY   B C   1 
ATOM   2197  O  O   . GLY   B  1 12  ? 27.827 -60.044 14.042  1.00 15.62 ? 12   GLY   B O   1 
ATOM   2198  N  N   . PRO   B  1 13  ? 28.936 -58.150 14.538  1.00 14.60 ? 13   PRO   B N   1 
ATOM   2199  C  CA  . PRO   B  1 13  ? 27.914 -57.245 13.978  1.00 14.28 ? 13   PRO   B CA  1 
ATOM   2200  C  C   . PRO   B  1 13  ? 27.332 -57.664 12.638  1.00 14.08 ? 13   PRO   B C   1 
ATOM   2201  O  O   . PRO   B  1 13  ? 26.090 -57.554 12.496  1.00 15.20 ? 13   PRO   B O   1 
ATOM   2202  C  CB  . PRO   B  1 13  ? 28.699 -55.927 13.881  1.00 16.29 ? 13   PRO   B CB  1 
ATOM   2203  C  CG  . PRO   B  1 13  ? 29.577 -55.974 15.112  1.00 15.96 ? 13   PRO   B CG  1 
ATOM   2204  C  CD  . PRO   B  1 13  ? 29.973 -57.431 15.297  1.00 15.80 ? 13   PRO   B CD  1 
ATOM   2205  N  N   . GLU   B  1 14  ? 28.136 -58.133 11.660  1.00 13.96 ? 14   GLU   B N   1 
ATOM   2206  C  CA  . GLU   B  1 14  ? 27.560 -58.420 10.339  1.00 15.50 ? 14   GLU   B CA  1 
ATOM   2207  C  C   . GLU   B  1 14  ? 26.598 -59.598 10.400  1.00 16.52 ? 14   GLU   B C   1 
ATOM   2208  O  O   . GLU   B  1 14  ? 25.821 -59.805 9.466   1.00 18.10 ? 14   GLU   B O   1 
ATOM   2209  C  CB  . GLU   B  1 14  ? 28.663 -58.678 9.309   1.00 15.71 ? 14   GLU   B CB  1 
ATOM   2210  C  CG  . GLU   B  1 14  ? 29.381 -59.988 9.492   1.00 16.89 ? 14   GLU   B CG  1 
ATOM   2211  C  CD  . GLU   B  1 14  ? 30.191 -60.366 8.289   1.00 21.38 ? 14   GLU   B CD  1 
ATOM   2212  O  OE1 . GLU   B  1 14  ? 30.045 -59.757 7.175   1.00 21.64 ? 14   GLU   B OE1 1 
ATOM   2213  O  OE2 . GLU   B  1 14  ? 30.974 -61.328 8.418   1.00 23.64 ? 14   GLU   B OE2 1 
ATOM   2214  N  N   . HIS   B  1 15  ? 26.649 -60.389 11.473  1.00 15.41 ? 15   HIS   B N   1 
ATOM   2215  C  CA  . HIS   B  1 15  ? 25.777 -61.555 11.649  1.00 15.95 ? 15   HIS   B CA  1 
ATOM   2216  C  C   . HIS   B  1 15  ? 24.633 -61.336 12.616  1.00 15.49 ? 15   HIS   B C   1 
ATOM   2217  O  O   . HIS   B  1 15  ? 23.784 -62.231 12.744  1.00 16.47 ? 15   HIS   B O   1 
ATOM   2218  C  CB  . HIS   B  1 15  ? 26.614 -62.750 12.159  1.00 16.95 ? 15   HIS   B CB  1 
ATOM   2219  C  CG  . HIS   B  1 15  ? 27.698 -63.148 11.211  1.00 21.58 ? 15   HIS   B CG  1 
ATOM   2220  N  ND1 . HIS   B  1 15  ? 27.446 -63.412 9.876   1.00 25.19 ? 15   HIS   B ND1 1 
ATOM   2221  C  CD2 . HIS   B  1 15  ? 29.044 -63.256 11.373  1.00 23.13 ? 15   HIS   B CD2 1 
ATOM   2222  C  CE1 . HIS   B  1 15  ? 28.591 -63.690 9.266   1.00 26.55 ? 15   HIS   B CE1 1 
ATOM   2223  N  NE2 . HIS   B  1 15  ? 29.563 -63.629 10.161  1.00 23.88 ? 15   HIS   B NE2 1 
ATOM   2224  N  N   . TRP   B  1 16  ? 24.582 -60.193 13.323  1.00 14.15 ? 16   TRP   B N   1 
ATOM   2225  C  CA  . TRP   B  1 16  ? 23.572 -60.045 14.363  1.00 13.29 ? 16   TRP   B CA  1 
ATOM   2226  C  C   . TRP   B  1 16  ? 22.165 -60.199 13.829  1.00 14.83 ? 16   TRP   B C   1 
ATOM   2227  O  O   . TRP   B  1 16  ? 21.312 -60.717 14.555  1.00 15.39 ? 16   TRP   B O   1 
ATOM   2228  C  CB  . TRP   B  1 16  ? 23.697 -58.680 15.043  1.00 13.07 ? 16   TRP   B CB  1 
ATOM   2229  C  CG  . TRP   B  1 16  ? 24.921 -58.582 15.934  1.00 14.71 ? 16   TRP   B CG  1 
ATOM   2230  C  CD1 . TRP   B  1 16  ? 25.719 -59.602 16.394  1.00 14.57 ? 16   TRP   B CD1 1 
ATOM   2231  C  CD2 . TRP   B  1 16  ? 25.458 -57.364 16.500  1.00 14.19 ? 16   TRP   B CD2 1 
ATOM   2232  N  NE1 . TRP   B  1 16  ? 26.715 -59.075 17.226  1.00 13.73 ? 16   TRP   B NE1 1 
ATOM   2233  C  CE2 . TRP   B  1 16  ? 26.598 -57.722 17.261  1.00 13.81 ? 16   TRP   B CE2 1 
ATOM   2234  C  CE3 . TRP   B  1 16  ? 25.120 -56.015 16.370  1.00 14.01 ? 16   TRP   B CE3 1 
ATOM   2235  C  CZ2 . TRP   B  1 16  ? 27.364 -56.776 17.963  1.00 14.04 ? 16   TRP   B CZ2 1 
ATOM   2236  C  CZ3 . TRP   B  1 16  ? 25.858 -55.070 17.040  1.00 14.91 ? 16   TRP   B CZ3 1 
ATOM   2237  C  CH2 . TRP   B  1 16  ? 26.993 -55.454 17.830  1.00 14.90 ? 16   TRP   B CH2 1 
ATOM   2238  N  N   . HIS   B  1 17  ? 21.896 -59.754 12.586  1.00 14.40 ? 17   HIS   B N   1 
ATOM   2239  C  CA  . HIS   B  1 17  ? 20.540 -59.876 12.005  1.00 13.71 ? 17   HIS   B CA  1 
ATOM   2240  C  C   . HIS   B  1 17  ? 20.031 -61.303 11.996  1.00 14.86 ? 17   HIS   B C   1 
ATOM   2241  O  O   . HIS   B  1 17  ? 18.797 -61.487 11.912  1.00 16.75 ? 17   HIS   B O   1 
ATOM   2242  C  CB  . HIS   B  1 17  ? 20.499 -59.335 10.565  1.00 17.11 ? 17   HIS   B CB  1 
ATOM   2243  C  CG  . HIS   B  1 17  ? 21.350 -60.117 9.622   1.00 17.50 ? 17   HIS   B CG  1 
ATOM   2244  N  ND1 . HIS   B  1 17  ? 20.843 -61.114 8.814   1.00 21.75 ? 17   HIS   B ND1 1 
ATOM   2245  C  CD2 . HIS   B  1 17  ? 22.702 -60.147 9.467   1.00 15.47 ? 17   HIS   B CD2 1 
ATOM   2246  C  CE1 . HIS   B  1 17  ? 21.847 -61.670 8.147   1.00 20.84 ? 17   HIS   B CE1 1 
ATOM   2247  N  NE2 . HIS   B  1 17  ? 22.977 -61.107 8.537   1.00 19.83 ? 17   HIS   B NE2 1 
ATOM   2248  N  N   . LYS   B  1 18  ? 20.923 -62.319 12.038  1.00 14.84 ? 18   LYS   B N   1 
ATOM   2249  C  CA  . LYS   B  1 18  ? 20.455 -63.699 11.959  1.00 12.53 ? 18   LYS   B CA  1 
ATOM   2250  C  C   . LYS   B  1 18  ? 19.628 -64.076 13.168  1.00 15.48 ? 18   LYS   B C   1 
ATOM   2251  O  O   . LYS   B  1 18  ? 18.784 -64.982 13.061  1.00 15.73 ? 18   LYS   B O   1 
ATOM   2252  C  CB  . LYS   B  1 18  ? 21.660 -64.648 11.812  1.00 15.86 ? 18   LYS   B CB  1 
ATOM   2253  C  CG  . LYS   B  1 18  ? 22.366 -64.395 10.526  1.00 23.63 ? 18   LYS   B CG  1 
ATOM   2254  C  CD  . LYS   B  1 18  ? 23.640 -65.263 10.480  1.00 25.65 ? 18   LYS   B CD  1 
ATOM   2255  C  CE  . LYS   B  1 18  ? 24.465 -64.925 9.256   1.00 27.88 ? 18   LYS   B CE  1 
ATOM   2256  N  NZ  . LYS   B  1 18  ? 25.705 -65.843 9.282   1.00 33.08 ? 18   LYS   B NZ  1 
ATOM   2257  N  N   . ASP   B  1 19  ? 19.880 -63.427 14.295  1.00 13.84 ? 19   ASP   B N   1 
ATOM   2258  C  CA  . ASP   B  1 19  ? 19.100 -63.675 15.509  1.00 14.09 ? 19   ASP   B CA  1 
ATOM   2259  C  C   . ASP   B  1 19  ? 18.256 -62.493 15.928  1.00 16.16 ? 19   ASP   B C   1 
ATOM   2260  O  O   . ASP   B  1 19  ? 17.259 -62.687 16.640  1.00 15.35 ? 19   ASP   B O   1 
ATOM   2261  C  CB  . ASP   B  1 19  ? 20.018 -64.058 16.685  1.00 14.74 ? 19   ASP   B CB  1 
ATOM   2262  C  CG  . ASP   B  1 19  ? 20.787 -65.305 16.425  1.00 16.90 ? 19   ASP   B CG  1 
ATOM   2263  O  OD1 . ASP   B  1 19  ? 20.176 -66.383 16.342  1.00 19.40 ? 19   ASP   B OD1 1 
ATOM   2264  O  OD2 . ASP   B  1 19  ? 22.023 -65.203 16.242  1.00 18.67 ? 19   ASP   B OD2 1 
ATOM   2265  N  N   . PHE   B  1 20  ? 18.620 -61.274 15.511  1.00 14.11 ? 20   PHE   B N   1 
ATOM   2266  C  CA  . PHE   B  1 20  ? 17.950 -60.042 15.914  1.00 15.33 ? 20   PHE   B CA  1 
ATOM   2267  C  C   . PHE   B  1 20  ? 17.574 -59.313 14.643  1.00 16.09 ? 20   PHE   B C   1 
ATOM   2268  O  O   . PHE   B  1 20  ? 18.301 -58.416 14.191  1.00 17.14 ? 20   PHE   B O   1 
ATOM   2269  C  CB  . PHE   B  1 20  ? 18.867 -59.208 16.810  1.00 15.54 ? 20   PHE   B CB  1 
ATOM   2270  C  CG  . PHE   B  1 20  ? 19.386 -59.975 18.017  1.00 13.83 ? 20   PHE   B CG  1 
ATOM   2271  C  CD1 . PHE   B  1 20  ? 18.625 -60.075 19.153  1.00 15.93 ? 20   PHE   B CD1 1 
ATOM   2272  C  CD2 . PHE   B  1 20  ? 20.636 -60.566 17.966  1.00 14.08 ? 20   PHE   B CD2 1 
ATOM   2273  C  CE1 . PHE   B  1 20  ? 19.103 -60.810 20.248  1.00 13.00 ? 20   PHE   B CE1 1 
ATOM   2274  C  CE2 . PHE   B  1 20  ? 21.152 -61.280 19.066  1.00 13.53 ? 20   PHE   B CE2 1 
ATOM   2275  C  CZ  . PHE   B  1 20  ? 20.376 -61.418 20.242  1.00 14.46 ? 20   PHE   B CZ  1 
ATOM   2276  N  N   . PRO   B  1 21  ? 16.466 -59.674 14.021  1.00 13.76 ? 21   PRO   B N   1 
ATOM   2277  C  CA  . PRO   B  1 21  ? 16.191 -59.121 12.679  1.00 15.28 ? 21   PRO   B CA  1 
ATOM   2278  C  C   . PRO   B  1 21  ? 15.985 -57.610 12.677  1.00 15.56 ? 21   PRO   B C   1 
ATOM   2279  O  O   . PRO   B  1 21  ? 16.091 -57.012 11.584  1.00 16.26 ? 21   PRO   B O   1 
ATOM   2280  C  CB  . PRO   B  1 21  ? 14.941 -59.877 12.205  1.00 18.08 ? 21   PRO   B CB  1 
ATOM   2281  C  CG  . PRO   B  1 21  ? 14.471 -60.659 13.411  1.00 19.67 ? 21   PRO   B CG  1 
ATOM   2282  C  CD  . PRO   B  1 21  ? 15.604 -60.818 14.381  1.00 15.06 ? 21   PRO   B CD  1 
ATOM   2283  N  N   A ILE   B  1 22  ? 15.701 -56.991 13.830  0.51 14.23 ? 22   ILE   B N   1 
ATOM   2284  N  N   B ILE   B  1 22  ? 15.703 -56.993 13.830  0.49 14.22 ? 22   ILE   B N   1 
ATOM   2285  C  CA  A ILE   B  1 22  ? 15.569 -55.537 13.902  0.51 13.92 ? 22   ILE   B CA  1 
ATOM   2286  C  CA  B ILE   B  1 22  ? 15.565 -55.542 13.896  0.49 13.97 ? 22   ILE   B CA  1 
ATOM   2287  C  C   A ILE   B  1 22  ? 16.880 -54.871 13.549  0.51 15.04 ? 22   ILE   B C   1 
ATOM   2288  C  C   B ILE   B  1 22  ? 16.879 -54.871 13.559  0.49 15.03 ? 22   ILE   B C   1 
ATOM   2289  O  O   A ILE   B  1 22  ? 16.905 -53.668 13.305  0.51 15.75 ? 22   ILE   B O   1 
ATOM   2290  O  O   B ILE   B  1 22  ? 16.906 -53.665 13.330  0.49 15.71 ? 22   ILE   B O   1 
ATOM   2291  C  CB  A ILE   B  1 22  ? 15.060 -55.104 15.300  0.51 14.41 ? 22   ILE   B CB  1 
ATOM   2292  C  CB  B ILE   B  1 22  ? 15.021 -55.123 15.285  0.49 14.43 ? 22   ILE   B CB  1 
ATOM   2293  C  CG1 A ILE   B  1 22  ? 14.621 -53.629 15.291  0.51 14.86 ? 22   ILE   B CG1 1 
ATOM   2294  C  CG1 B ILE   B  1 22  ? 14.440 -53.702 15.245  0.49 14.89 ? 22   ILE   B CG1 1 
ATOM   2295  C  CG2 A ILE   B  1 22  ? 16.120 -55.364 16.346  0.51 14.41 ? 22   ILE   B CG2 1 
ATOM   2296  C  CG2 B ILE   B  1 22  ? 16.101 -55.256 16.352  0.49 14.48 ? 22   ILE   B CG2 1 
ATOM   2297  C  CD1 A ILE   B  1 22  ? 13.507 -53.353 14.302  0.51 16.08 ? 22   ILE   B CD1 1 
ATOM   2298  C  CD1 B ILE   B  1 22  ? 13.943 -53.244 16.585  0.49 14.85 ? 22   ILE   B CD1 1 
ATOM   2299  N  N   . ALA   B  1 23  ? 17.975 -55.643 13.499  1.00 14.23 ? 23   ALA   B N   1 
ATOM   2300  C  CA  . ALA   B  1 23  ? 19.237 -55.097 12.981  1.00 15.25 ? 23   ALA   B CA  1 
ATOM   2301  C  C   . ALA   B  1 23  ? 19.084 -54.393 11.638  1.00 15.19 ? 23   ALA   B C   1 
ATOM   2302  O  O   . ALA   B  1 23  ? 19.906 -53.503 11.337  1.00 15.81 ? 23   ALA   B O   1 
ATOM   2303  C  CB  . ALA   B  1 23  ? 20.295 -56.228 12.807  1.00 15.84 ? 23   ALA   B CB  1 
ATOM   2304  N  N   . LYS   B  1 24  ? 18.097 -54.785 10.824  1.00 15.30 ? 24   LYS   B N   1 
ATOM   2305  C  CA  . LYS   B  1 24  ? 17.856 -54.189 9.501   1.00 14.71 ? 24   LYS   B CA  1 
ATOM   2306  C  C   . LYS   B  1 24  ? 16.677 -53.212 9.525   1.00 15.17 ? 24   LYS   B C   1 
ATOM   2307  O  O   . LYS   B  1 24  ? 16.092 -52.927 8.471   1.00 18.19 ? 24   LYS   B O   1 
ATOM   2308  C  CB  . LYS   B  1 24  ? 17.637 -55.299 8.485   1.00 19.41 ? 24   LYS   B CB  1 
ATOM   2309  C  CG  . LYS   B  1 24  ? 18.934 -56.131 8.287   1.00 22.51 ? 24   LYS   B CG  1 
ATOM   2310  C  CD  . LYS   B  1 24  ? 18.811 -57.142 7.155   1.00 29.01 ? 24   LYS   B CD  1 
ATOM   2311  C  CE  . LYS   B  1 24  ? 20.070 -57.998 7.006   1.00 34.15 ? 24   LYS   B CE  1 
ATOM   2312  N  NZ  . LYS   B  1 24  ? 21.290 -57.280 6.416   1.00 36.93 ? 24   LYS   B NZ  1 
ATOM   2313  N  N   . GLY   B  1 25  ? 16.352 -52.683 10.710  1.00 16.90 ? 25   GLY   B N   1 
ATOM   2314  C  CA  . GLY   B  1 25  ? 15.183 -51.867 10.947  1.00 16.79 ? 25   GLY   B CA  1 
ATOM   2315  C  C   . GLY   B  1 25  ? 15.343 -50.454 10.402  1.00 19.11 ? 25   GLY   B C   1 
ATOM   2316  O  O   . GLY   B  1 25  ? 16.341 -50.090 9.768   1.00 18.27 ? 25   GLY   B O   1 
ATOM   2317  N  N   . GLU   B  1 26  ? 14.348 -49.655 10.718  1.00 15.94 ? 26   GLU   B N   1 
ATOM   2318  C  CA  . GLU   B  1 26  ? 14.232 -48.302 10.189  1.00 19.33 ? 26   GLU   B CA  1 
ATOM   2319  C  C   . GLU   B  1 26  ? 14.915 -47.249 11.070  1.00 19.17 ? 26   GLU   B C   1 
ATOM   2320  O  O   . GLU   B  1 26  ? 15.035 -46.078 10.639  1.00 22.77 ? 26   GLU   B O   1 
ATOM   2321  C  CB  . GLU   B  1 26  ? 12.744 -47.971 10.031  1.00 21.43 ? 26   GLU   B CB  1 
ATOM   2322  C  CG  . GLU   B  1 26  ? 12.000 -48.883 9.051   1.00 22.97 ? 26   GLU   B CG  1 
ATOM   2323  C  CD  . GLU   B  1 26  ? 12.617 -48.756 7.678   1.00 31.37 ? 26   GLU   B CD  1 
ATOM   2324  O  OE1 . GLU   B  1 26  ? 12.762 -47.612 7.183   1.00 33.72 ? 26   GLU   B OE1 1 
ATOM   2325  O  OE2 . GLU   B  1 26  ? 12.971 -49.805 7.124   1.00 35.74 ? 26   GLU   B OE2 1 
ATOM   2326  N  N   . ARG   B  1 27  ? 15.308 -47.592 12.298  1.00 17.09 ? 27   ARG   B N   1 
ATOM   2327  C  CA  A ARG   B  1 27  ? 15.796 -46.632 13.272  0.53 16.99 ? 27   ARG   B CA  1 
ATOM   2328  C  CA  B ARG   B  1 27  ? 15.875 -46.573 13.195  0.47 16.71 ? 27   ARG   B CA  1 
ATOM   2329  C  C   . ARG   B  1 27  ? 17.063 -47.165 13.946  1.00 15.08 ? 27   ARG   B C   1 
ATOM   2330  O  O   . ARG   B  1 27  ? 17.177 -47.131 15.184  1.00 17.54 ? 27   ARG   B O   1 
ATOM   2331  C  CB  A ARG   B  1 27  ? 14.678 -46.365 14.301  0.53 18.49 ? 27   ARG   B CB  1 
ATOM   2332  C  CB  B ARG   B  1 27  ? 14.850 -46.012 14.175  0.47 18.47 ? 27   ARG   B CB  1 
ATOM   2333  C  CG  A ARG   B  1 27  ? 14.875 -45.167 15.244  0.53 20.64 ? 27   ARG   B CG  1 
ATOM   2334  C  CG  B ARG   B  1 27  ? 13.568 -45.567 13.556  0.47 17.87 ? 27   ARG   B CG  1 
ATOM   2335  C  CD  A ARG   B  1 27  ? 13.686 -45.014 16.248  0.53 18.33 ? 27   ARG   B CD  1 
ATOM   2336  C  CD  B ARG   B  1 27  ? 12.734 -44.750 14.597  0.47 17.40 ? 27   ARG   B CD  1 
ATOM   2337  N  NE  A ARG   B  1 27  ? 14.158 -44.738 17.627  0.53 11.29 ? 27   ARG   B NE  1 
ATOM   2338  N  NE  B ARG   B  1 27  ? 12.446 -45.412 15.896  0.47 18.09 ? 27   ARG   B NE  1 
ATOM   2339  C  CZ  A ARG   B  1 27  ? 13.433 -44.184 18.563  0.53 18.37 ? 27   ARG   B CZ  1 
ATOM   2340  C  CZ  B ARG   B  1 27  ? 11.504 -46.348 16.103  0.47 19.65 ? 27   ARG   B CZ  1 
ATOM   2341  N  NH1 A ARG   B  1 27  ? 12.160 -43.832 18.350  0.53 21.70 ? 27   ARG   B NH1 1 
ATOM   2342  N  NH1 B ARG   B  1 27  ? 11.268 -46.880 17.329  0.47 17.02 ? 27   ARG   B NH1 1 
ATOM   2343  N  NH2 A ARG   B  1 27  ? 13.969 -43.987 19.739  0.53 20.91 ? 27   ARG   B NH2 1 
ATOM   2344  N  NH2 B ARG   B  1 27  ? 10.814 -46.820 15.053  0.47 21.28 ? 27   ARG   B NH2 1 
ATOM   2345  N  N   . GLN   B  1 28  ? 17.997 -47.712 13.168  1.00 15.72 ? 28   GLN   B N   1 
ATOM   2346  C  CA  . GLN   B  1 28  ? 19.186 -48.352 13.762  1.00 14.80 ? 28   GLN   B CA  1 
ATOM   2347  C  C   . GLN   B  1 28  ? 20.352 -47.371 13.966  1.00 16.14 ? 28   GLN   B C   1 
ATOM   2348  O  O   . GLN   B  1 28  ? 20.500 -46.362 13.276  1.00 17.07 ? 28   GLN   B O   1 
ATOM   2349  C  CB  . GLN   B  1 28  ? 19.660 -49.488 12.858  1.00 15.55 ? 28   GLN   B CB  1 
ATOM   2350  C  CG  . GLN   B  1 28  ? 18.616 -50.639 12.877  1.00 15.08 ? 28   GLN   B CG  1 
ATOM   2351  C  CD  . GLN   B  1 28  ? 18.660 -51.330 14.242  1.00 14.27 ? 28   GLN   B CD  1 
ATOM   2352  O  OE1 . GLN   B  1 28  ? 19.668 -51.973 14.580  1.00 14.17 ? 28   GLN   B OE1 1 
ATOM   2353  N  NE2 . GLN   B  1 28  ? 17.593 -51.204 15.029  1.00 14.84 ? 28   GLN   B NE2 1 
ATOM   2354  N  N   . SER   B  1 29  ? 21.206 -47.719 14.913  1.00 14.73 ? 29   SER   B N   1 
ATOM   2355  C  CA  . SER   B  1 29  ? 22.376 -46.946 15.311  1.00 13.59 ? 29   SER   B CA  1 
ATOM   2356  C  C   . SER   B  1 29  ? 23.600 -47.857 15.331  1.00 16.15 ? 29   SER   B C   1 
ATOM   2357  O  O   . SER   B  1 29  ? 23.478 -49.079 15.516  1.00 15.32 ? 29   SER   B O   1 
ATOM   2358  C  CB  . SER   B  1 29  ? 22.180 -46.360 16.722  1.00 15.72 ? 29   SER   B CB  1 
ATOM   2359  O  OG  . SER   B  1 29  ? 21.081 -45.447 16.728  1.00 15.98 ? 29   SER   B OG  1 
ATOM   2360  N  N   . PRO   B  1 30  ? 24.813 -47.285 15.195  1.00 14.62 ? 30   PRO   B N   1 
ATOM   2361  C  CA  . PRO   B  1 30  ? 25.135 -45.865 15.020  1.00 14.77 ? 30   PRO   B CA  1 
ATOM   2362  C  C   . PRO   B  1 30  ? 24.942 -45.464 13.566  1.00 15.69 ? 30   PRO   B C   1 
ATOM   2363  O  O   . PRO   B  1 30  ? 24.565 -46.321 12.746  1.00 16.78 ? 30   PRO   B O   1 
ATOM   2364  C  CB  . PRO   B  1 30  ? 26.612 -45.824 15.413  1.00 16.25 ? 30   PRO   B CB  1 
ATOM   2365  C  CG  . PRO   B  1 30  ? 27.149 -47.176 14.867  1.00 16.10 ? 30   PRO   B CG  1 
ATOM   2366  C  CD  . PRO   B  1 30  ? 26.028 -48.133 15.209  1.00 16.82 ? 30   PRO   B CD  1 
ATOM   2367  N  N   . VAL   B  1 31  ? 25.142 -44.181 13.274  1.00 14.91 ? 31   VAL   B N   1 
ATOM   2368  C  CA  . VAL   B  1 31  ? 25.044 -43.630 11.921  1.00 15.67 ? 31   VAL   B CA  1 
ATOM   2369  C  C   . VAL   B  1 31  ? 26.228 -42.705 11.694  1.00 18.13 ? 31   VAL   B C   1 
ATOM   2370  O  O   . VAL   B  1 31  ? 26.905 -42.237 12.642  1.00 19.09 ? 31   VAL   B O   1 
ATOM   2371  C  CB  . VAL   B  1 31  ? 23.728 -42.852 11.698  1.00 17.21 ? 31   VAL   B CB  1 
ATOM   2372  C  CG1 . VAL   B  1 31  ? 22.511 -43.759 11.911  1.00 18.54 ? 31   VAL   B CG1 1 
ATOM   2373  C  CG2 . VAL   B  1 31  ? 23.639 -41.637 12.694  1.00 18.78 ? 31   VAL   B CG2 1 
ATOM   2374  N  N   . ASP   B  1 32  ? 26.472 -42.403 10.416  1.00 17.87 ? 32   ASP   B N   1 
ATOM   2375  C  CA  . ASP   B  1 32  ? 27.358 -41.319 10.076  1.00 18.19 ? 32   ASP   B CA  1 
ATOM   2376  C  C   . ASP   B  1 32  ? 26.624 -39.996 10.280  1.00 19.99 ? 32   ASP   B C   1 
ATOM   2377  O  O   . ASP   B  1 32  ? 25.470 -39.825 9.854   1.00 21.87 ? 32   ASP   B O   1 
ATOM   2378  C  CB  . ASP   B  1 32  ? 27.821 -41.454 8.621   1.00 17.07 ? 32   ASP   B CB  1 
ATOM   2379  C  CG  . ASP   B  1 32  ? 28.738 -40.294 8.215   1.00 19.80 ? 32   ASP   B CG  1 
ATOM   2380  O  OD1 . ASP   B  1 32  ? 29.760 -40.093 8.914   1.00 20.72 ? 32   ASP   B OD1 1 
ATOM   2381  O  OD2 . ASP   B  1 32  ? 28.453 -39.610 7.204   1.00 23.65 ? 32   ASP   B OD2 1 
ATOM   2382  N  N   . ILE   B  1 33  ? 27.302 -39.045 10.915  1.00 18.83 ? 33   ILE   B N   1 
ATOM   2383  C  CA  . ILE   B  1 33  ? 26.782 -37.688 11.071  1.00 19.89 ? 33   ILE   B CA  1 
ATOM   2384  C  C   . ILE   B  1 33  ? 27.456 -36.825 10.024  1.00 20.48 ? 33   ILE   B C   1 
ATOM   2385  O  O   . ILE   B  1 33  ? 28.662 -36.556 10.087  1.00 22.28 ? 33   ILE   B O   1 
ATOM   2386  C  CB  . ILE   B  1 33  ? 27.063 -37.154 12.486  1.00 18.04 ? 33   ILE   B CB  1 
ATOM   2387  C  CG1 . ILE   B  1 33  ? 26.387 -38.084 13.478  1.00 21.10 ? 33   ILE   B CG1 1 
ATOM   2388  C  CG2 . ILE   B  1 33  ? 26.637 -35.692 12.580  1.00 21.69 ? 33   ILE   B CG2 1 
ATOM   2389  C  CD1 . ILE   B  1 33  ? 26.911 -38.014 14.932  1.00 23.24 ? 33   ILE   B CD1 1 
ATOM   2390  N  N   . ASP   B  1 34  ? 26.700 -36.440 8.998   1.00 22.37 ? 34   ASP   B N   1 
ATOM   2391  C  CA  . ASP   B  1 34  ? 27.242 -35.571 7.978   1.00 23.43 ? 34   ASP   B CA  1 
ATOM   2392  C  C   . ASP   B  1 34  ? 26.974 -34.124 8.348   1.00 27.42 ? 34   ASP   B C   1 
ATOM   2393  O  O   . ASP   B  1 34  ? 25.815 -33.727 8.508   1.00 28.57 ? 34   ASP   B O   1 
ATOM   2394  C  CB  . ASP   B  1 34  ? 26.646 -35.887 6.601   1.00 24.01 ? 34   ASP   B CB  1 
ATOM   2395  C  CG  . ASP   B  1 34  ? 27.228 -34.982 5.562   1.00 26.31 ? 34   ASP   B CG  1 
ATOM   2396  O  OD1 . ASP   B  1 34  ? 26.831 -33.809 5.521   1.00 28.00 ? 34   ASP   B OD1 1 
ATOM   2397  O  OD2 . ASP   B  1 34  ? 28.140 -35.479 4.933   1.00 28.62 ? 34   ASP   B OD2 1 
ATOM   2398  N  N   . THR   B  1 35  ? 28.050 -33.357 8.552   1.00 28.31 ? 35   THR   B N   1 
ATOM   2399  C  CA  . THR   B  1 35  ? 27.917 -32.020 9.110   1.00 30.11 ? 35   THR   B CA  1 
ATOM   2400  C  C   . THR   B  1 35  ? 27.342 -31.030 8.119   1.00 36.29 ? 35   THR   B C   1 
ATOM   2401  O  O   . THR   B  1 35  ? 26.947 -29.931 8.534   1.00 40.81 ? 35   THR   B O   1 
ATOM   2402  C  CB  . THR   B  1 35  ? 29.266 -31.514 9.617   1.00 28.99 ? 35   THR   B CB  1 
ATOM   2403  O  OG1 . THR   B  1 35  ? 30.203 -31.353 8.532   1.00 29.62 ? 35   THR   B OG1 1 
ATOM   2404  C  CG2 . THR   B  1 35  ? 29.804 -32.516 10.654  1.00 27.29 ? 35   THR   B CG2 1 
ATOM   2405  N  N   . HIS   B  1 36  ? 27.323 -31.382 6.836   1.00 31.25 ? 36   HIS   B N   1 
ATOM   2406  C  CA  . HIS   B  1 36  ? 26.769 -30.481 5.832   1.00 34.16 ? 36   HIS   B CA  1 
ATOM   2407  C  C   . HIS   B  1 36  ? 25.258 -30.561 5.785   1.00 34.71 ? 36   HIS   B C   1 
ATOM   2408  O  O   . HIS   B  1 36  ? 24.609 -29.601 5.347   1.00 36.46 ? 36   HIS   B O   1 
ATOM   2409  C  CB  . HIS   B  1 36  ? 27.380 -30.826 4.488   1.00 38.41 ? 36   HIS   B CB  1 
ATOM   2410  C  CG  . HIS   B  1 36  ? 28.855 -31.013 4.578   1.00 48.37 ? 36   HIS   B CG  1 
ATOM   2411  N  ND1 . HIS   B  1 36  ? 29.512 -32.087 4.019   1.00 49.87 ? 36   HIS   B ND1 1 
ATOM   2412  C  CD2 . HIS   B  1 36  ? 29.809 -30.248 5.169   1.00 51.72 ? 36   HIS   B CD2 1 
ATOM   2413  C  CE1 . HIS   B  1 36  ? 30.804 -31.997 4.294   1.00 51.83 ? 36   HIS   B CE1 1 
ATOM   2414  N  NE2 . HIS   B  1 36  ? 31.012 -30.883 4.979   1.00 51.21 ? 36   HIS   B NE2 1 
ATOM   2415  N  N   . THR   B  1 37  ? 24.690 -31.698 6.187   1.00 29.15 ? 37   THR   B N   1 
ATOM   2416  C  CA  . THR   B  1 37  ? 23.253 -31.881 6.113   1.00 26.93 ? 37   THR   B CA  1 
ATOM   2417  C  C   . THR   B  1 37  ? 22.536 -31.851 7.464   1.00 25.65 ? 37   THR   B C   1 
ATOM   2418  O  O   . THR   B  1 37  ? 21.328 -31.592 7.480   1.00 30.38 ? 37   THR   B O   1 
ATOM   2419  C  CB  . THR   B  1 37  ? 22.929 -33.185 5.372   1.00 28.80 ? 37   THR   B CB  1 
ATOM   2420  O  OG1 . THR   B  1 37  ? 23.591 -34.266 5.983   1.00 31.09 ? 37   THR   B OG1 1 
ATOM   2421  C  CG2 . THR   B  1 37  ? 23.403 -33.079 3.908   1.00 30.72 ? 37   THR   B CG2 1 
ATOM   2422  N  N   . ALA   B  1 38  ? 23.230 -32.111 8.577   1.00 26.70 ? 38   ALA   B N   1 
ATOM   2423  C  CA  . ALA   B  1 38  ? 22.608 -31.948 9.885   1.00 27.67 ? 38   ALA   B CA  1 
ATOM   2424  C  C   . ALA   B  1 38  ? 22.109 -30.509 10.032  1.00 33.02 ? 38   ALA   B C   1 
ATOM   2425  O  O   . ALA   B  1 38  ? 22.815 -29.572 9.655   1.00 39.21 ? 38   ALA   B O   1 
ATOM   2426  C  CB  . ALA   B  1 38  ? 23.620 -32.308 10.977  1.00 25.18 ? 38   ALA   B CB  1 
ATOM   2427  N  N   . LYS   B  1 39  ? 20.873 -30.327 10.531  1.00 28.81 ? 39   LYS   B N   1 
ATOM   2428  C  CA  . LYS   B  1 39  ? 20.213 -29.017 10.571  1.00 30.04 ? 39   LYS   B CA  1 
ATOM   2429  C  C   . LYS   B  1 39  ? 19.894 -28.561 11.997  1.00 30.95 ? 39   LYS   B C   1 
ATOM   2430  O  O   . LYS   B  1 39  ? 19.341 -29.324 12.789  1.00 27.78 ? 39   LYS   B O   1 
ATOM   2431  C  CB  . LYS   B  1 39  ? 18.913 -29.053 9.765   1.00 33.87 ? 39   LYS   B CB  1 
ATOM   2432  C  CG  . LYS   B  1 39  ? 19.112 -29.045 8.245   1.00 42.46 ? 39   LYS   B CG  1 
ATOM   2433  C  CD  . LYS   B  1 39  ? 17.796 -28.832 7.516   1.00 47.39 ? 39   LYS   B CD  1 
ATOM   2434  C  CE  . LYS   B  1 39  ? 17.134 -27.545 8.015   1.00 53.75 ? 39   LYS   B CE  1 
ATOM   2435  N  NZ  . LYS   B  1 39  ? 15.904 -27.175 7.241   1.00 57.81 ? 39   LYS   B NZ  1 
ATOM   2436  N  N   . TYR   B  1 40  ? 20.145 -27.277 12.283  1.00 31.20 ? 40   TYR   B N   1 
ATOM   2437  C  CA  . TYR   B  1 40  ? 19.737 -26.687 13.552  1.00 31.30 ? 40   TYR   B CA  1 
ATOM   2438  C  C   . TYR   B  1 40  ? 18.224 -26.809 13.773  1.00 29.83 ? 40   TYR   B C   1 
ATOM   2439  O  O   . TYR   B  1 40  ? 17.421 -26.565 12.863  1.00 32.21 ? 40   TYR   B O   1 
ATOM   2440  C  CB  . TYR   B  1 40  ? 20.159 -25.219 13.576  1.00 32.31 ? 40   TYR   B CB  1 
ATOM   2441  C  CG  . TYR   B  1 40  ? 19.553 -24.438 14.698  1.00 34.52 ? 40   TYR   B CG  1 
ATOM   2442  C  CD1 . TYR   B  1 40  ? 19.953 -24.654 16.016  1.00 34.31 ? 40   TYR   B CD1 1 
ATOM   2443  C  CD2 . TYR   B  1 40  ? 18.582 -23.482 14.449  1.00 37.40 ? 40   TYR   B CD2 1 
ATOM   2444  C  CE1 . TYR   B  1 40  ? 19.395 -23.902 17.058  1.00 37.78 ? 40   TYR   B CE1 1 
ATOM   2445  C  CE2 . TYR   B  1 40  ? 18.030 -22.727 15.477  1.00 41.55 ? 40   TYR   B CE2 1 
ATOM   2446  C  CZ  . TYR   B  1 40  ? 18.421 -22.963 16.771  1.00 40.29 ? 40   TYR   B CZ  1 
ATOM   2447  O  OH  . TYR   B  1 40  ? 17.855 -22.213 17.788  1.00 43.53 ? 40   TYR   B OH  1 
ATOM   2448  N  N   . ASP   B  1 41  ? 17.838 -27.213 14.981  1.00 29.60 ? 41   ASP   B N   1 
ATOM   2449  C  CA  . ASP   B  1 41  ? 16.430 -27.374 15.349  1.00 31.46 ? 41   ASP   B CA  1 
ATOM   2450  C  C   . ASP   B  1 41  ? 16.102 -26.370 16.446  1.00 33.77 ? 41   ASP   B C   1 
ATOM   2451  O  O   . ASP   B  1 41  ? 16.441 -26.591 17.626  1.00 32.24 ? 41   ASP   B O   1 
ATOM   2452  C  CB  . ASP   B  1 41  ? 16.162 -28.798 15.822  1.00 31.34 ? 41   ASP   B CB  1 
ATOM   2453  C  CG  . ASP   B  1 41  ? 14.700 -29.068 16.102  1.00 36.08 ? 41   ASP   B CG  1 
ATOM   2454  O  OD1 . ASP   B  1 41  ? 13.869 -28.124 16.122  1.00 37.23 ? 41   ASP   B OD1 1 
ATOM   2455  O  OD2 . ASP   B  1 41  ? 14.378 -30.277 16.276  1.00 36.64 ? 41   ASP   B OD2 1 
ATOM   2456  N  N   . PRO   B  1 42  ? 15.433 -25.270 16.122  1.00 35.00 ? 42   PRO   B N   1 
ATOM   2457  C  CA  . PRO   B  1 42  ? 15.127 -24.279 17.163  1.00 34.40 ? 42   PRO   B CA  1 
ATOM   2458  C  C   . PRO   B  1 42  ? 14.196 -24.785 18.253  1.00 35.85 ? 42   PRO   B C   1 
ATOM   2459  O  O   . PRO   B  1 42  ? 14.048 -24.093 19.276  1.00 40.10 ? 42   PRO   B O   1 
ATOM   2460  C  CB  . PRO   B  1 42  ? 14.484 -23.123 16.373  1.00 37.11 ? 42   PRO   B CB  1 
ATOM   2461  C  CG  . PRO   B  1 42  ? 13.979 -23.766 15.097  1.00 38.61 ? 42   PRO   B CG  1 
ATOM   2462  C  CD  . PRO   B  1 42  ? 14.867 -24.933 14.800  1.00 35.63 ? 42   PRO   B CD  1 
ATOM   2463  N  N   . SER   B  1 43  ? 13.527 -25.915 18.057  1.00 33.76 ? 43   SER   B N   1 
ATOM   2464  C  CA  . SER   B  1 43  ? 12.635 -26.470 19.070  1.00 38.71 ? 43   SER   B CA  1 
ATOM   2465  C  C   . SER   B  1 43  ? 13.380 -27.168 20.211  1.00 39.17 ? 43   SER   B C   1 
ATOM   2466  O  O   . SER   B  1 43  ? 12.768 -27.429 21.253  1.00 39.80 ? 43   SER   B O   1 
ATOM   2467  C  CB  . SER   B  1 43  ? 11.640 -27.452 18.416  1.00 39.54 ? 43   SER   B CB  1 
ATOM   2468  O  OG  . SER   B  1 43  ? 12.217 -28.731 18.162  1.00 39.77 ? 43   SER   B OG  1 
ATOM   2469  N  N   . LEU   B  1 44  ? 14.667 -27.461 20.051  1.00 35.81 ? 44   LEU   B N   1 
ATOM   2470  C  CA  . LEU   B  1 44  ? 15.436 -28.070 21.131  1.00 33.19 ? 44   LEU   B CA  1 
ATOM   2471  C  C   . LEU   B  1 44  ? 15.567 -27.113 22.319  1.00 36.53 ? 44   LEU   B C   1 
ATOM   2472  O  O   . LEU   B  1 44  ? 15.858 -25.921 22.150  1.00 36.30 ? 44   LEU   B O   1 
ATOM   2473  C  CB  . LEU   B  1 44  ? 16.830 -28.465 20.638  1.00 31.34 ? 44   LEU   B CB  1 
ATOM   2474  C  CG  . LEU   B  1 44  ? 16.825 -29.589 19.604  1.00 29.33 ? 44   LEU   B CG  1 
ATOM   2475  C  CD1 . LEU   B  1 44  ? 18.177 -29.754 18.891  1.00 28.81 ? 44   LEU   B CD1 1 
ATOM   2476  C  CD2 . LEU   B  1 44  ? 16.442 -30.914 20.305  1.00 28.22 ? 44   LEU   B CD2 1 
ATOM   2477  N  N   . LYS   B  1 45  ? 15.351 -27.626 23.528  1.00 37.15 ? 45   LYS   B N   1 
ATOM   2478  C  CA  . LYS   B  1 45  ? 15.552 -26.808 24.721  1.00 36.64 ? 45   LYS   B CA  1 
ATOM   2479  C  C   . LYS   B  1 45  ? 16.978 -26.975 25.196  1.00 33.33 ? 45   LYS   B C   1 
ATOM   2480  O  O   . LYS   B  1 45  ? 17.674 -27.923 24.782  1.00 30.23 ? 45   LYS   B O   1 
ATOM   2481  C  CB  . LYS   B  1 45  ? 14.569 -27.218 25.812  1.00 38.14 ? 45   LYS   B CB  1 
ATOM   2482  C  CG  . LYS   B  1 45  ? 13.123 -27.294 25.350  1.00 44.76 ? 45   LYS   B CG  1 
ATOM   2483  C  CD  . LYS   B  1 45  ? 12.661 -25.976 24.804  1.00 53.93 ? 45   LYS   B CD  1 
ATOM   2484  C  CE  . LYS   B  1 45  ? 11.268 -26.075 24.167  1.00 60.64 ? 45   LYS   B CE  1 
ATOM   2485  N  NZ  . LYS   B  1 45  ? 10.204 -26.094 25.213  1.00 65.37 ? 45   LYS   B NZ  1 
ATOM   2486  N  N   . PRO   B  1 46  ? 17.445 -26.093 26.088  1.00 33.25 ? 46   PRO   B N   1 
ATOM   2487  C  CA  . PRO   B  1 46  ? 18.801 -26.236 26.632  1.00 32.56 ? 46   PRO   B CA  1 
ATOM   2488  C  C   . PRO   B  1 46  ? 18.974 -27.615 27.252  1.00 31.56 ? 46   PRO   B C   1 
ATOM   2489  O  O   . PRO   B  1 46  ? 18.070 -28.112 27.921  1.00 31.14 ? 46   PRO   B O   1 
ATOM   2490  C  CB  . PRO   B  1 46  ? 18.877 -25.134 27.697  1.00 34.32 ? 46   PRO   B CB  1 
ATOM   2491  C  CG  . PRO   B  1 46  ? 17.832 -24.106 27.227  1.00 38.05 ? 46   PRO   B CG  1 
ATOM   2492  C  CD  . PRO   B  1 46  ? 16.727 -24.935 26.663  1.00 38.79 ? 46   PRO   B CD  1 
ATOM   2493  N  N   . LEU   B  1 47  ? 20.134 -28.223 27.011  1.00 28.60 ? 47   LEU   B N   1 
ATOM   2494  C  CA  . LEU   B  1 47  ? 20.447 -29.546 27.560  1.00 27.21 ? 47   LEU   B CA  1 
ATOM   2495  C  C   . LEU   B  1 47  ? 21.031 -29.392 28.962  1.00 29.66 ? 47   LEU   B C   1 
ATOM   2496  O  O   . LEU   B  1 47  ? 21.890 -28.519 29.196  1.00 33.00 ? 47   LEU   B O   1 
ATOM   2497  C  CB  . LEU   B  1 47  ? 21.432 -30.298 26.679  1.00 30.11 ? 47   LEU   B CB  1 
ATOM   2498  C  CG  . LEU   B  1 47  ? 21.689 -31.740 27.111  1.00 28.22 ? 47   LEU   B CG  1 
ATOM   2499  C  CD1 . LEU   B  1 47  ? 20.524 -32.702 26.827  1.00 27.94 ? 47   LEU   B CD1 1 
ATOM   2500  C  CD2 . LEU   B  1 47  ? 22.958 -32.215 26.410  1.00 31.03 ? 47   LEU   B CD2 1 
ATOM   2501  N  N   . SER   B  1 48  ? 20.520 -30.202 29.887  1.00 28.29 ? 48   SER   B N   1 
ATOM   2502  C  CA  A SER   B  1 48  ? 20.942 -30.192 31.279  0.54 29.98 ? 48   SER   B CA  1 
ATOM   2503  C  CA  B SER   B  1 48  ? 20.920 -30.205 31.292  0.46 29.98 ? 48   SER   B CA  1 
ATOM   2504  C  C   . SER   B  1 48  ? 21.580 -31.536 31.601  1.00 27.87 ? 48   SER   B C   1 
ATOM   2505  O  O   . SER   B  1 48  ? 20.914 -32.570 31.552  1.00 28.19 ? 48   SER   B O   1 
ATOM   2506  C  CB  A SER   B  1 48  ? 19.753 -29.910 32.197  0.54 32.00 ? 48   SER   B CB  1 
ATOM   2507  C  CB  B SER   B  1 48  ? 19.709 -30.023 32.209  0.46 32.02 ? 48   SER   B CB  1 
ATOM   2508  O  OG  A SER   B  1 48  ? 20.160 -30.054 33.536  0.54 33.68 ? 48   SER   B OG  1 
ATOM   2509  O  OG  B SER   B  1 48  ? 19.206 -28.718 32.152  0.46 36.47 ? 48   SER   B OG  1 
ATOM   2510  N  N   . VAL   B  1 49  ? 22.864 -31.508 31.941  1.00 30.49 ? 49   VAL   B N   1 
ATOM   2511  C  CA  . VAL   B  1 49  ? 23.594 -32.707 32.346  1.00 29.90 ? 49   VAL   B CA  1 
ATOM   2512  C  C   . VAL   B  1 49  ? 23.891 -32.527 33.826  1.00 31.18 ? 49   VAL   B C   1 
ATOM   2513  O  O   . VAL   B  1 49  ? 24.785 -31.758 34.188  1.00 34.93 ? 49   VAL   B O   1 
ATOM   2514  C  CB  . VAL   B  1 49  ? 24.893 -32.884 31.547  1.00 31.39 ? 49   VAL   B CB  1 
ATOM   2515  C  CG1 . VAL   B  1 49  ? 25.632 -34.168 32.021  1.00 32.95 ? 49   VAL   B CG1 1 
ATOM   2516  C  CG2 . VAL   B  1 49  ? 24.605 -32.897 30.044  1.00 30.87 ? 49   VAL   B CG2 1 
ATOM   2517  N  N   . SER   B  1 50  ? 23.157 -33.216 34.701  1.00 30.75 ? 50   SER   B N   1 
ATOM   2518  C  CA  . SER   B  1 50  ? 23.238 -32.950 36.148  1.00 32.39 ? 50   SER   B CA  1 
ATOM   2519  C  C   . SER   B  1 50  ? 23.867 -34.169 36.798  1.00 29.06 ? 50   SER   B C   1 
ATOM   2520  O  O   . SER   B  1 50  ? 23.178 -35.118 37.175  1.00 31.18 ? 50   SER   B O   1 
ATOM   2521  C  CB  . SER   B  1 50  ? 21.887 -32.652 36.788  1.00 37.96 ? 50   SER   B CB  1 
ATOM   2522  O  OG  . SER   B  1 50  ? 21.254 -31.601 36.103  1.00 44.69 ? 50   SER   B OG  1 
ATOM   2523  N  N   . TYR   B  1 51  ? 25.190 -34.123 36.954  1.00 29.45 ? 51   TYR   B N   1 
ATOM   2524  C  CA  . TYR   B  1 51  ? 25.955 -35.246 37.454  1.00 28.88 ? 51   TYR   B CA  1 
ATOM   2525  C  C   . TYR   B  1 51  ? 26.644 -34.944 38.785  1.00 33.97 ? 51   TYR   B C   1 
ATOM   2526  O  O   . TYR   B  1 51  ? 27.527 -35.708 39.185  1.00 34.33 ? 51   TYR   B O   1 
ATOM   2527  C  CB  . TYR   B  1 51  ? 27.016 -35.661 36.435  1.00 28.94 ? 51   TYR   B CB  1 
ATOM   2528  C  CG  . TYR   B  1 51  ? 26.531 -36.402 35.205  1.00 25.52 ? 51   TYR   B CG  1 
ATOM   2529  C  CD1 . TYR   B  1 51  ? 25.203 -36.795 35.063  1.00 26.05 ? 51   TYR   B CD1 1 
ATOM   2530  C  CD2 . TYR   B  1 51  ? 27.414 -36.678 34.178  1.00 22.98 ? 51   TYR   B CD2 1 
ATOM   2531  C  CE1 . TYR   B  1 51  ? 24.784 -37.492 33.919  1.00 23.39 ? 51   TYR   B CE1 1 
ATOM   2532  C  CE2 . TYR   B  1 51  ? 27.030 -37.352 33.056  1.00 21.81 ? 51   TYR   B CE2 1 
ATOM   2533  C  CZ  . TYR   B  1 51  ? 25.725 -37.773 32.902  1.00 21.23 ? 51   TYR   B CZ  1 
ATOM   2534  O  OH  . TYR   B  1 51  ? 25.419 -38.459 31.766  1.00 22.57 ? 51   TYR   B OH  1 
ATOM   2535  N  N   . ASP   B  1 52  ? 26.276 -33.850 39.456  1.00 34.67 ? 52   ASP   B N   1 
ATOM   2536  C  CA  . ASP   B  1 52  ? 26.956 -33.462 40.692  1.00 36.37 ? 52   ASP   B CA  1 
ATOM   2537  C  C   . ASP   B  1 52  ? 26.788 -34.504 41.801  1.00 34.38 ? 52   ASP   B C   1 
ATOM   2538  O  O   . ASP   B  1 52  ? 27.637 -34.590 42.697  1.00 38.31 ? 52   ASP   B O   1 
ATOM   2539  C  CB  . ASP   B  1 52  ? 26.445 -32.086 41.172  1.00 38.98 ? 52   ASP   B CB  1 
ATOM   2540  C  CG  . ASP   B  1 52  ? 26.845 -30.942 40.250  1.00 45.61 ? 52   ASP   B CG  1 
ATOM   2541  O  OD1 . ASP   B  1 52  ? 27.616 -31.149 39.276  1.00 45.03 ? 52   ASP   B OD1 1 
ATOM   2542  O  OD2 . ASP   B  1 52  ? 26.387 -29.794 40.508  1.00 47.44 ? 52   ASP   B OD2 1 
ATOM   2543  N  N   . GLN   B  1 53  ? 25.702 -35.272 41.804  1.00 30.92 ? 53   GLN   B N   1 
ATOM   2544  C  CA  . GLN   B  1 53  ? 25.438 -36.216 42.890  1.00 30.38 ? 53   GLN   B CA  1 
ATOM   2545  C  C   . GLN   B  1 53  ? 25.473 -37.671 42.427  1.00 31.95 ? 53   GLN   B C   1 
ATOM   2546  O  O   . GLN   B  1 53  ? 24.789 -38.527 43.000  1.00 34.52 ? 53   GLN   B O   1 
ATOM   2547  C  CB  . GLN   B  1 53  ? 24.091 -35.922 43.539  1.00 33.92 ? 53   GLN   B CB  1 
ATOM   2548  C  CG  . GLN   B  1 53  ? 24.058 -34.558 44.198  1.00 35.55 ? 53   GLN   B CG  1 
ATOM   2549  C  CD  . GLN   B  1 53  ? 22.835 -34.384 45.076  1.00 42.01 ? 53   GLN   B CD  1 
ATOM   2550  O  OE1 . GLN   B  1 53  ? 21.710 -34.333 44.591  1.00 44.84 ? 53   GLN   B OE1 1 
ATOM   2551  N  NE2 . GLN   B  1 53  ? 23.053 -34.310 46.389  1.00 47.12 ? 53   GLN   B NE2 1 
ATOM   2552  N  N   . ALA   B  1 54  ? 26.261 -37.964 41.408  1.00 29.83 ? 54   ALA   B N   1 
ATOM   2553  C  CA  . ALA   B  1 54  ? 26.269 -39.325 40.870  1.00 28.80 ? 54   ALA   B CA  1 
ATOM   2554  C  C   . ALA   B  1 54  ? 26.958 -40.290 41.825  1.00 27.82 ? 54   ALA   B C   1 
ATOM   2555  O  O   . ALA   B  1 54  ? 27.965 -39.949 42.448  1.00 29.73 ? 54   ALA   B O   1 
ATOM   2556  C  CB  . ALA   B  1 54  ? 26.982 -39.344 39.521  1.00 29.66 ? 54   ALA   B CB  1 
ATOM   2557  N  N   . THR   B  1 55  ? 26.408 -41.503 41.973  1.00 25.64 ? 55   THR   B N   1 
ATOM   2558  C  CA  . THR   B  1 55  ? 26.965 -42.470 42.929  1.00 24.19 ? 55   THR   B CA  1 
ATOM   2559  C  C   . THR   B  1 55  ? 27.371 -43.688 42.108  1.00 23.77 ? 55   THR   B C   1 
ATOM   2560  O  O   . THR   B  1 55  ? 26.525 -44.537 41.815  1.00 23.34 ? 55   THR   B O   1 
ATOM   2561  C  CB  . THR   B  1 55  ? 25.967 -42.875 44.032  1.00 27.77 ? 55   THR   B CB  1 
ATOM   2562  O  OG1 . THR   B  1 55  ? 25.581 -41.709 44.747  1.00 30.85 ? 55   THR   B OG1 1 
ATOM   2563  C  CG2 . THR   B  1 55  ? 26.558 -43.896 45.019  1.00 27.54 ? 55   THR   B CG2 1 
ATOM   2564  N  N   . SER   B  1 56  ? 28.656 -43.800 41.766  1.00 20.59 ? 56   SER   B N   1 
ATOM   2565  C  CA  . SER   B  1 56  ? 29.079 -45.028 41.097  1.00 20.61 ? 56   SER   B CA  1 
ATOM   2566  C  C   . SER   B  1 56  ? 29.226 -46.163 42.099  1.00 20.48 ? 56   SER   B C   1 
ATOM   2567  O  O   . SER   B  1 56  ? 29.489 -45.956 43.301  1.00 23.09 ? 56   SER   B O   1 
ATOM   2568  C  CB  . SER   B  1 56  ? 30.400 -44.816 40.351  1.00 18.82 ? 56   SER   B CB  1 
ATOM   2569  O  OG  . SER   B  1 56  ? 31.473 -44.649 41.277  1.00 22.20 ? 56   SER   B OG  1 
ATOM   2570  N  N   . LEU   B  1 57  ? 28.983 -47.392 41.601  1.00 21.49 ? 57   LEU   B N   1 
ATOM   2571  C  CA  . LEU   B  1 57  ? 29.035 -48.558 42.458  1.00 21.99 ? 57   LEU   B CA  1 
ATOM   2572  C  C   . LEU   B  1 57  ? 30.084 -49.588 42.055  1.00 20.77 ? 57   LEU   B C   1 
ATOM   2573  O  O   . LEU   B  1 57  ? 30.806 -50.075 42.939  1.00 20.67 ? 57   LEU   B O   1 
ATOM   2574  C  CB  . LEU   B  1 57  ? 27.656 -49.248 42.485  1.00 26.03 ? 57   LEU   B CB  1 
ATOM   2575  C  CG  . LEU   B  1 57  ? 26.595 -48.455 43.249  1.00 29.95 ? 57   LEU   B CG  1 
ATOM   2576  C  CD1 . LEU   B  1 57  ? 25.234 -49.173 43.049  1.00 31.03 ? 57   LEU   B CD1 1 
ATOM   2577  C  CD2 . LEU   B  1 57  ? 26.952 -48.253 44.756  1.00 31.34 ? 57   LEU   B CD2 1 
ATOM   2578  N  N   . ARG   B  1 58  ? 30.120 -49.998 40.786  1.00 18.14 ? 58   ARG   B N   1 
ATOM   2579  C  CA  . ARG   B  1 58  ? 30.903 -51.171 40.425  1.00 19.12 ? 58   ARG   B CA  1 
ATOM   2580  C  C   . ARG   B  1 58  ? 31.201 -51.116 38.936  1.00 18.55 ? 58   ARG   B C   1 
ATOM   2581  O  O   . ARG   B  1 58  ? 30.574 -50.359 38.172  1.00 20.01 ? 58   ARG   B O   1 
ATOM   2582  C  CB  . ARG   B  1 58  ? 30.190 -52.478 40.820  1.00 25.05 ? 58   ARG   B CB  1 
ATOM   2583  C  CG  . ARG   B  1 58  ? 28.874 -52.653 40.214  1.00 27.42 ? 58   ARG   B CG  1 
ATOM   2584  C  CD  . ARG   B  1 58  ? 28.226 -53.946 40.787  1.00 33.36 ? 58   ARG   B CD  1 
ATOM   2585  N  NE  . ARG   B  1 58  ? 28.246 -53.935 42.247  1.00 36.59 ? 58   ARG   B NE  1 
ATOM   2586  C  CZ  . ARG   B  1 58  ? 27.234 -53.506 43.010  1.00 35.77 ? 58   ARG   B CZ  1 
ATOM   2587  N  NH1 . ARG   B  1 58  ? 26.096 -53.028 42.443  1.00 33.00 ? 58   ARG   B NH1 1 
ATOM   2588  N  NH2 . ARG   B  1 58  ? 27.379 -53.549 44.335  1.00 33.19 ? 58   ARG   B NH2 1 
ATOM   2589  N  N   . ILE   B  1 59  ? 32.191 -51.909 38.546  1.00 17.38 ? 59   ILE   B N   1 
ATOM   2590  C  CA  . ILE   B  1 59  ? 32.584 -52.023 37.146  1.00 16.67 ? 59   ILE   B CA  1 
ATOM   2591  C  C   . ILE   B  1 59  ? 32.607 -53.502 36.767  1.00 16.30 ? 59   ILE   B C   1 
ATOM   2592  O  O   . ILE   B  1 59  ? 33.088 -54.337 37.546  1.00 18.13 ? 59   ILE   B O   1 
ATOM   2593  C  CB  . ILE   B  1 59  ? 33.932 -51.324 36.936  1.00 16.32 ? 59   ILE   B CB  1 
ATOM   2594  C  CG1 . ILE   B  1 59  ? 34.262 -51.270 35.431  1.00 18.89 ? 59   ILE   B CG1 1 
ATOM   2595  C  CG2 . ILE   B  1 59  ? 35.070 -51.979 37.770  1.00 18.10 ? 59   ILE   B CG2 1 
ATOM   2596  C  CD1 . ILE   B  1 59  ? 35.548 -50.481 35.160  1.00 20.32 ? 59   ILE   B CD1 1 
ATOM   2597  N  N   . LEU   B  1 60  ? 32.054 -53.822 35.614  1.00 17.42 ? 60   LEU   B N   1 
ATOM   2598  C  CA  . LEU   B  1 60  ? 31.803 -55.200 35.221  1.00 17.86 ? 60   LEU   B CA  1 
ATOM   2599  C  C   . LEU   B  1 60  ? 32.317 -55.413 33.816  1.00 17.65 ? 60   LEU   B C   1 
ATOM   2600  O  O   . LEU   B  1 60  ? 32.010 -54.620 32.920  1.00 18.05 ? 60   LEU   B O   1 
ATOM   2601  C  CB  . LEU   B  1 60  ? 30.294 -55.509 35.265  1.00 17.74 ? 60   LEU   B CB  1 
ATOM   2602  C  CG  . LEU   B  1 60  ? 29.844 -56.824 34.622  1.00 18.59 ? 60   LEU   B CG  1 
ATOM   2603  C  CD1 . LEU   B  1 60  ? 30.212 -58.052 35.465  1.00 18.66 ? 60   LEU   B CD1 1 
ATOM   2604  C  CD2 . LEU   B  1 60  ? 28.327 -56.807 34.467  1.00 20.13 ? 60   LEU   B CD2 1 
ATOM   2605  N  N   . ASN   B  1 61  ? 33.084 -56.473 33.614  1.00 17.00 ? 61   ASN   B N   1 
ATOM   2606  C  CA  . ASN   B  1 61  ? 33.386 -56.935 32.249  1.00 14.37 ? 61   ASN   B CA  1 
ATOM   2607  C  C   . ASN   B  1 61  ? 32.228 -57.849 31.828  1.00 15.03 ? 61   ASN   B C   1 
ATOM   2608  O  O   . ASN   B  1 61  ? 32.023 -58.931 32.426  1.00 17.12 ? 61   ASN   B O   1 
ATOM   2609  C  CB  . ASN   B  1 61  ? 34.730 -57.685 32.269  1.00 16.41 ? 61   ASN   B CB  1 
ATOM   2610  C  CG  . ASN   B  1 61  ? 35.094 -58.283 30.902  1.00 16.40 ? 61   ASN   B CG  1 
ATOM   2611  O  OD1 . ASN   B  1 61  ? 34.218 -58.549 30.070  1.00 16.82 ? 61   ASN   B OD1 1 
ATOM   2612  N  ND2 . ASN   B  1 61  ? 36.395 -58.462 30.657  1.00 17.67 ? 61   ASN   B ND2 1 
ATOM   2613  N  N   . ASN   B  1 62  ? 31.400 -57.388 30.885  1.00 16.23 ? 62   ASN   B N   1 
ATOM   2614  C  CA  . ASN   B  1 62  ? 30.235 -58.191 30.489  1.00 17.83 ? 62   ASN   B CA  1 
ATOM   2615  C  C   . ASN   B  1 62  ? 30.517 -59.073 29.283  1.00 15.81 ? 62   ASN   B C   1 
ATOM   2616  O  O   . ASN   B  1 62  ? 29.585 -59.648 28.711  1.00 17.54 ? 62   ASN   B O   1 
ATOM   2617  C  CB  . ASN   B  1 62  ? 28.999 -57.315 30.239  1.00 15.32 ? 62   ASN   B CB  1 
ATOM   2618  C  CG  . ASN   B  1 62  ? 29.102 -56.498 28.963  1.00 17.45 ? 62   ASN   B CG  1 
ATOM   2619  O  OD1 . ASN   B  1 62  ? 30.146 -56.463 28.342  1.00 16.05 ? 62   ASN   B OD1 1 
ATOM   2620  N  ND2 . ASN   B  1 62  ? 28.006 -55.817 28.596  1.00 15.91 ? 62   ASN   B ND2 1 
ATOM   2621  N  N   . GLY   B  1 63  ? 31.795 -59.268 28.944  1.00 15.85 ? 63   GLY   B N   1 
ATOM   2622  C  CA  . GLY   B  1 63  ? 32.157 -60.079 27.794  1.00 14.81 ? 63   GLY   B CA  1 
ATOM   2623  C  C   . GLY   B  1 63  ? 32.026 -59.365 26.474  1.00 16.09 ? 63   GLY   B C   1 
ATOM   2624  O  O   . GLY   B  1 63  ? 32.272 -60.002 25.426  1.00 18.22 ? 63   GLY   B O   1 
ATOM   2625  N  N   . HIS   B  1 64  ? 31.641 -58.097 26.490  1.00 16.40 ? 64   HIS   B N   1 
ATOM   2626  C  CA  . HIS   B  1 64  ? 31.447 -57.262 25.314  1.00 13.72 ? 64   HIS   B CA  1 
ATOM   2627  C  C   . HIS   B  1 64  ? 32.215 -55.967 25.470  1.00 17.09 ? 64   HIS   B C   1 
ATOM   2628  O  O   . HIS   B  1 64  ? 32.893 -55.527 24.529  1.00 18.57 ? 64   HIS   B O   1 
ATOM   2629  C  CB  . HIS   B  1 64  ? 29.952 -56.954 25.068  1.00 14.38 ? 64   HIS   B CB  1 
ATOM   2630  C  CG  . HIS   B  1 64  ? 29.051 -58.160 25.090  1.00 14.34 ? 64   HIS   B CG  1 
ATOM   2631  N  ND1 . HIS   B  1 64  ? 29.095 -59.147 24.115  1.00 15.01 ? 64   HIS   B ND1 1 
ATOM   2632  C  CD2 . HIS   B  1 64  ? 28.072 -58.518 25.955  1.00 15.27 ? 64   HIS   B CD2 1 
ATOM   2633  C  CE1 . HIS   B  1 64  ? 28.163 -60.061 24.383  1.00 17.42 ? 64   HIS   B CE1 1 
ATOM   2634  N  NE2 . HIS   B  1 64  ? 27.531 -59.697 25.496  1.00 15.68 ? 64   HIS   B NE2 1 
ATOM   2635  N  N   . THR   B  1 65  ? 32.141 -55.361 26.636  1.00 15.34 ? 65   THR   B N   1 
ATOM   2636  C  CA  . THR   B  1 65  ? 32.802 -54.126 26.995  1.00 15.08 ? 65   THR   B CA  1 
ATOM   2637  C  C   . THR   B  1 65  ? 32.923 -54.134 28.521  1.00 15.39 ? 65   THR   B C   1 
ATOM   2638  O  O   . THR   B  1 65  ? 32.777 -55.192 29.146  1.00 16.39 ? 65   THR   B O   1 
ATOM   2639  C  CB  . THR   B  1 65  ? 32.013 -52.935 26.460  1.00 15.08 ? 65   THR   B CB  1 
ATOM   2640  O  OG1 . THR   B  1 65  ? 32.771 -51.763 26.788  1.00 17.38 ? 65   THR   B OG1 1 
ATOM   2641  C  CG2 . THR   B  1 65  ? 30.633 -52.812 27.106  1.00 16.34 ? 65   THR   B CG2 1 
ATOM   2642  N  N   . PHE   B  1 66  ? 33.266 -52.995 29.140  1.00 16.15 ? 66   PHE   B N   1 
ATOM   2643  C  CA  . PHE   B  1 66  ? 33.116 -52.869 30.589  1.00 15.05 ? 66   PHE   B CA  1 
ATOM   2644  C  C   . PHE   B  1 66  ? 32.091 -51.780 30.890  1.00 15.32 ? 66   PHE   B C   1 
ATOM   2645  O  O   . PHE   B  1 66  ? 32.048 -50.746 30.219  1.00 16.10 ? 66   PHE   B O   1 
ATOM   2646  C  CB  . PHE   B  1 66  ? 34.468 -52.597 31.353  1.00 17.36 ? 66   PHE   B CB  1 
ATOM   2647  C  CG  . PHE   B  1 66  ? 35.162 -51.314 30.952  1.00 16.68 ? 66   PHE   B CG  1 
ATOM   2648  C  CD1 . PHE   B  1 66  ? 36.097 -51.288 29.901  1.00 18.63 ? 66   PHE   B CD1 1 
ATOM   2649  C  CD2 . PHE   B  1 66  ? 34.886 -50.139 31.628  1.00 17.69 ? 66   PHE   B CD2 1 
ATOM   2650  C  CE1 . PHE   B  1 66  ? 36.718 -50.108 29.527  1.00 18.34 ? 66   PHE   B CE1 1 
ATOM   2651  C  CE2 . PHE   B  1 66  ? 35.519 -48.949 31.282  1.00 18.50 ? 66   PHE   B CE2 1 
ATOM   2652  C  CZ  . PHE   B  1 66  ? 36.451 -48.923 30.246  1.00 19.54 ? 66   PHE   B CZ  1 
ATOM   2653  N  N   . ASN   B  1 67  ? 31.219 -52.067 31.851  1.00 15.85 ? 67   ASN   B N   1 
ATOM   2654  C  CA  . ASN   B  1 67  ? 30.170 -51.145 32.258  1.00 16.02 ? 67   ASN   B CA  1 
ATOM   2655  C  C   . ASN   B  1 67  ? 30.479 -50.644 33.657  1.00 18.07 ? 67   ASN   B C   1 
ATOM   2656  O  O   . ASN   B  1 67  ? 30.704 -51.461 34.575  1.00 18.63 ? 67   ASN   B O   1 
ATOM   2657  C  CB  . ASN   B  1 67  ? 28.797 -51.816 32.312  1.00 16.89 ? 67   ASN   B CB  1 
ATOM   2658  C  CG  . ASN   B  1 67  ? 28.305 -52.288 30.999  1.00 18.12 ? 67   ASN   B CG  1 
ATOM   2659  O  OD1 . ASN   B  1 67  ? 28.753 -51.834 29.941  1.00 17.00 ? 67   ASN   B OD1 1 
ATOM   2660  N  ND2 . ASN   B  1 67  ? 27.379 -53.236 31.042  1.00 19.81 ? 67   ASN   B ND2 1 
ATOM   2661  N  N   . VAL   B  1 68  ? 30.432 -49.321 33.848  1.00 16.89 ? 68   VAL   B N   1 
ATOM   2662  C  CA  . VAL   B  1 68  ? 30.494 -48.730 35.181  1.00 17.23 ? 68   VAL   B CA  1 
ATOM   2663  C  C   . VAL   B  1 68  ? 29.065 -48.400 35.575  1.00 18.82 ? 68   VAL   B C   1 
ATOM   2664  O  O   . VAL   B  1 68  ? 28.407 -47.588 34.907  1.00 18.66 ? 68   VAL   B O   1 
ATOM   2665  C  CB  . VAL   B  1 68  ? 31.384 -47.475 35.207  1.00 18.78 ? 68   VAL   B CB  1 
ATOM   2666  C  CG1 . VAL   B  1 68  ? 31.208 -46.734 36.544  1.00 21.08 ? 68   VAL   B CG1 1 
ATOM   2667  C  CG2 . VAL   B  1 68  ? 32.885 -47.823 34.940  1.00 18.92 ? 68   VAL   B CG2 1 
ATOM   2668  N  N   . GLU   B  1 69  ? 28.570 -49.025 36.641  1.00 18.42 ? 69   GLU   B N   1 
ATOM   2669  C  CA  . GLU   B  1 69  ? 27.173 -48.959 37.039  1.00 20.50 ? 69   GLU   B CA  1 
ATOM   2670  C  C   . GLU   B  1 69  ? 27.017 -47.926 38.162  1.00 19.71 ? 69   GLU   B C   1 
ATOM   2671  O  O   . GLU   B  1 69  ? 27.889 -47.812 39.049  1.00 22.53 ? 69   GLU   B O   1 
ATOM   2672  C  CB  . GLU   B  1 69  ? 26.715 -50.343 37.528  1.00 27.61 ? 69   GLU   B CB  1 
ATOM   2673  C  CG  . GLU   B  1 69  ? 25.246 -50.477 37.919  1.00 40.17 ? 69   GLU   B CG  1 
ATOM   2674  C  CD  . GLU   B  1 69  ? 24.980 -51.682 38.877  1.00 49.78 ? 69   GLU   B CD  1 
ATOM   2675  O  OE1 . GLU   B  1 69  ? 25.923 -52.470 39.171  1.00 51.23 ? 69   GLU   B OE1 1 
ATOM   2676  O  OE2 . GLU   B  1 69  ? 23.824 -51.817 39.359  1.00 52.61 ? 69   GLU   B OE2 1 
ATOM   2677  N  N   . PHE   B  1 70  ? 25.890 -47.218 38.137  1.00 18.83 ? 70   PHE   B N   1 
ATOM   2678  C  CA  . PHE   B  1 70  ? 25.507 -46.197 39.115  1.00 18.94 ? 70   PHE   B CA  1 
ATOM   2679  C  C   . PHE   B  1 70  ? 24.238 -46.574 39.861  1.00 23.53 ? 70   PHE   B C   1 
ATOM   2680  O  O   . PHE   B  1 70  ? 23.396 -47.312 39.351  1.00 23.00 ? 70   PHE   B O   1 
ATOM   2681  C  CB  . PHE   B  1 70  ? 25.292 -44.862 38.413  1.00 20.07 ? 70   PHE   B CB  1 
ATOM   2682  C  CG  . PHE   B  1 70  ? 26.546 -44.270 37.893  1.00 20.49 ? 70   PHE   B CG  1 
ATOM   2683  C  CD1 . PHE   B  1 70  ? 27.139 -44.747 36.714  1.00 21.53 ? 70   PHE   B CD1 1 
ATOM   2684  C  CD2 . PHE   B  1 70  ? 27.176 -43.253 38.605  1.00 21.10 ? 70   PHE   B CD2 1 
ATOM   2685  C  CE1 . PHE   B  1 70  ? 28.338 -44.187 36.271  1.00 20.66 ? 70   PHE   B CE1 1 
ATOM   2686  C  CE2 . PHE   B  1 70  ? 28.367 -42.689 38.174  1.00 22.23 ? 70   PHE   B CE2 1 
ATOM   2687  C  CZ  . PHE   B  1 70  ? 28.959 -43.183 37.001  1.00 22.03 ? 70   PHE   B CZ  1 
ATOM   2688  N  N   . ASP   B  1 71  ? 24.085 -46.010 41.066  1.00 22.94 ? 71   ASP   B N   1 
ATOM   2689  C  CA  . ASP   B  1 71  ? 22.826 -46.117 41.798  1.00 22.15 ? 71   ASP   B CA  1 
ATOM   2690  C  C   . ASP   B  1 71  ? 21.812 -45.229 41.083  1.00 24.16 ? 71   ASP   B C   1 
ATOM   2691  O  O   . ASP   B  1 71  ? 22.008 -44.019 41.003  1.00 26.36 ? 71   ASP   B O   1 
ATOM   2692  C  CB  . ASP   B  1 71  ? 23.052 -45.663 43.239  1.00 24.42 ? 71   ASP   B CB  1 
ATOM   2693  C  CG  . ASP   B  1 71  ? 21.806 -45.826 44.098  1.00 26.89 ? 71   ASP   B CG  1 
ATOM   2694  O  OD1 . ASP   B  1 71  ? 20.714 -45.603 43.563  1.00 26.27 ? 71   ASP   B OD1 1 
ATOM   2695  O  OD2 . ASP   B  1 71  ? 21.907 -46.133 45.318  1.00 28.72 ? 71   ASP   B OD2 1 
ATOM   2696  N  N   . ASP   B  1 72  ? 20.805 -45.827 40.441  1.00 22.65 ? 72   ASP   B N   1 
ATOM   2697  C  CA  . ASP   B  1 72  ? 19.797 -45.067 39.704  1.00 19.88 ? 72   ASP   B CA  1 
ATOM   2698  C  C   . ASP   B  1 72  ? 18.452 -45.060 40.420  1.00 22.50 ? 72   ASP   B C   1 
ATOM   2699  O  O   . ASP   B  1 72  ? 17.395 -44.987 39.774  1.00 23.07 ? 72   ASP   B O   1 
ATOM   2700  C  CB  . ASP   B  1 72  ? 19.636 -45.645 38.286  1.00 19.79 ? 72   ASP   B CB  1 
ATOM   2701  C  CG  . ASP   B  1 72  ? 19.138 -47.089 38.300  1.00 21.13 ? 72   ASP   B CG  1 
ATOM   2702  O  OD1 . ASP   B  1 72  ? 19.076 -47.733 39.397  1.00 23.96 ? 72   ASP   B OD1 1 
ATOM   2703  O  OD2 . ASP   B  1 72  ? 18.798 -47.605 37.205  1.00 21.79 ? 72   ASP   B OD2 1 
ATOM   2704  N  N   . SER   B  1 73  ? 18.474 -45.068 41.759  1.00 22.20 ? 73   SER   B N   1 
ATOM   2705  C  CA  . SER   B  1 73  ? 17.227 -45.115 42.510  1.00 23.56 ? 73   SER   B CA  1 
ATOM   2706  C  C   . SER   B  1 73  ? 16.594 -43.742 42.716  1.00 26.75 ? 73   SER   B C   1 
ATOM   2707  O  O   . SER   B  1 73  ? 15.453 -43.662 43.207  1.00 27.69 ? 73   SER   B O   1 
ATOM   2708  C  CB  . SER   B  1 73  ? 17.488 -45.788 43.866  1.00 25.63 ? 73   SER   B CB  1 
ATOM   2709  O  OG  . SER   B  1 73  ? 18.274 -44.968 44.731  1.00 26.23 ? 73   SER   B OG  1 
ATOM   2710  N  N   . GLN   B  1 74  ? 17.308 -42.662 42.400  1.00 23.55 ? 74   GLN   B N   1 
ATOM   2711  C  CA  . GLN   B  1 74  ? 16.829 -41.314 42.679  1.00 24.88 ? 74   GLN   B CA  1 
ATOM   2712  C  C   . GLN   B  1 74  ? 17.115 -40.411 41.493  1.00 26.04 ? 74   GLN   B C   1 
ATOM   2713  O  O   . GLN   B  1 74  ? 18.012 -40.681 40.681  1.00 26.86 ? 74   GLN   B O   1 
ATOM   2714  C  CB  . GLN   B  1 74  ? 17.469 -40.727 43.944  1.00 27.31 ? 74   GLN   B CB  1 
ATOM   2715  C  CG  . GLN   B  1 74  ? 17.118 -41.518 45.171  1.00 25.64 ? 74   GLN   B CG  1 
ATOM   2716  C  CD  . GLN   B  1 74  ? 17.697 -40.881 46.415  1.00 31.54 ? 74   GLN   B CD  1 
ATOM   2717  O  OE1 . GLN   B  1 74  ? 18.903 -40.615 46.499  1.00 33.13 ? 74   GLN   B OE1 1 
ATOM   2718  N  NE2 . GLN   B  1 74  ? 16.822 -40.584 47.379  1.00 34.88 ? 74   GLN   B NE2 1 
ATOM   2719  N  N   . ASP   B  1 75  ? 16.335 -39.312 41.424  1.00 28.82 ? 75   ASP   B N   1 
ATOM   2720  C  CA  . ASP   B  1 75  ? 16.453 -38.319 40.348  1.00 31.03 ? 75   ASP   B CA  1 
ATOM   2721  C  C   . ASP   B  1 75  ? 17.644 -37.406 40.635  1.00 33.63 ? 75   ASP   B C   1 
ATOM   2722  O  O   . ASP   B  1 75  ? 17.515 -36.193 40.805  1.00 37.94 ? 75   ASP   B O   1 
ATOM   2723  C  CB  . ASP   B  1 75  ? 15.179 -37.491 40.213  1.00 34.26 ? 75   ASP   B CB  1 
ATOM   2724  C  CG  . ASP   B  1 75  ? 14.065 -38.211 39.502  1.00 35.59 ? 75   ASP   B CG  1 
ATOM   2725  O  OD1 . ASP   B  1 75  ? 14.297 -39.297 38.966  1.00 31.48 ? 75   ASP   B OD1 1 
ATOM   2726  O  OD2 . ASP   B  1 75  ? 12.932 -37.663 39.455  1.00 39.38 ? 75   ASP   B OD2 1 
ATOM   2727  N  N   . LYS   B  1 76  ? 18.809 -38.017 40.773  1.00 30.74 ? 76   LYS   B N   1 
ATOM   2728  C  CA  . LYS   B  1 76  ? 19.998 -37.237 41.081  1.00 31.39 ? 76   LYS   B CA  1 
ATOM   2729  C  C   . LYS   B  1 76  ? 20.844 -37.095 39.821  1.00 33.54 ? 76   LYS   B C   1 
ATOM   2730  O  O   . LYS   B  1 76  ? 20.803 -36.020 39.209  1.00 35.36 ? 76   LYS   B O   1 
ATOM   2731  C  CB  . LYS   B  1 76  ? 20.760 -37.849 42.260  1.00 33.36 ? 76   LYS   B CB  1 
ATOM   2732  C  CG  . LYS   B  1 76  ? 19.996 -37.596 43.607  1.00 36.11 ? 76   LYS   B CG  1 
ATOM   2733  C  CD  . LYS   B  1 76  ? 20.714 -38.139 44.872  1.00 35.60 ? 76   LYS   B CD  1 
ATOM   2734  C  CE  . LYS   B  1 76  ? 19.982 -37.628 46.134  1.00 36.97 ? 76   LYS   B CE  1 
ATOM   2735  N  NZ  . LYS   B  1 76  ? 20.344 -38.350 47.393  1.00 39.17 ? 76   LYS   B NZ  1 
ATOM   2736  N  N   . ALA   B  1 77  ? 21.532 -38.156 39.369  1.00 27.75 ? 77   ALA   B N   1 
ATOM   2737  C  CA  . ALA   B  1 77  ? 22.345 -38.056 38.155  1.00 26.02 ? 77   ALA   B CA  1 
ATOM   2738  C  C   . ALA   B  1 77  ? 21.406 -38.232 36.974  1.00 25.48 ? 77   ALA   B C   1 
ATOM   2739  O  O   . ALA   B  1 77  ? 20.972 -39.354 36.667  1.00 23.86 ? 77   ALA   B O   1 
ATOM   2740  C  CB  . ALA   B  1 77  ? 23.457 -39.092 38.134  1.00 28.66 ? 77   ALA   B CB  1 
ATOM   2741  N  N   . VAL   B  1 78  ? 21.056 -37.121 36.319  1.00 25.86 ? 78   VAL   B N   1 
ATOM   2742  C  CA  . VAL   B  1 78  ? 20.026 -37.157 35.291  1.00 25.85 ? 78   VAL   B CA  1 
ATOM   2743  C  C   . VAL   B  1 78  ? 20.427 -36.306 34.107  1.00 24.62 ? 78   VAL   B C   1 
ATOM   2744  O  O   . VAL   B  1 78  ? 21.213 -35.364 34.221  1.00 27.07 ? 78   VAL   B O   1 
ATOM   2745  C  CB  . VAL   B  1 78  ? 18.654 -36.653 35.780  1.00 25.41 ? 78   VAL   B CB  1 
ATOM   2746  C  CG1 . VAL   B  1 78  ? 18.168 -37.473 36.982  1.00 26.77 ? 78   VAL   B CG1 1 
ATOM   2747  C  CG2 . VAL   B  1 78  ? 18.717 -35.232 36.120  1.00 28.42 ? 78   VAL   B CG2 1 
ATOM   2748  N  N   . LEU   B  1 79  ? 19.765 -36.606 32.995  1.00 24.52 ? 79   LEU   B N   1 
ATOM   2749  C  CA  . LEU   B  1 79  ? 19.799 -35.823 31.776  1.00 24.30 ? 79   LEU   B CA  1 
ATOM   2750  C  C   . LEU   B  1 79  ? 18.390 -35.293 31.530  1.00 26.50 ? 79   LEU   B C   1 
ATOM   2751  O  O   . LEU   B  1 79  ? 17.420 -36.050 31.638  1.00 27.57 ? 79   LEU   B O   1 
ATOM   2752  C  CB  . LEU   B  1 79  ? 20.285 -36.745 30.648  1.00 26.68 ? 79   LEU   B CB  1 
ATOM   2753  C  CG  . LEU   B  1 79  ? 20.623 -36.247 29.284  1.00 29.72 ? 79   LEU   B CG  1 
ATOM   2754  C  CD1 . LEU   B  1 79  ? 21.752 -35.268 29.492  1.00 33.57 ? 79   LEU   B CD1 1 
ATOM   2755  C  CD2 . LEU   B  1 79  ? 21.086 -37.445 28.472  1.00 23.25 ? 79   LEU   B CD2 1 
ATOM   2756  N  N   . LYS   B  1 80  ? 18.269 -33.999 31.201  1.00 25.28 ? 80   LYS   B N   1 
ATOM   2757  C  CA  . LYS   B  1 80  ? 16.981 -33.356 30.961  1.00 28.47 ? 80   LYS   B CA  1 
ATOM   2758  C  C   . LYS   B  1 80  ? 17.178 -32.343 29.840  1.00 30.25 ? 80   LYS   B C   1 
ATOM   2759  O  O   . LYS   B  1 80  ? 18.310 -31.988 29.514  1.00 30.61 ? 80   LYS   B O   1 
ATOM   2760  C  CB  . LYS   B  1 80  ? 16.467 -32.625 32.211  1.00 34.94 ? 80   LYS   B CB  1 
ATOM   2761  C  CG  . LYS   B  1 80  ? 16.208 -33.526 33.425  1.00 37.96 ? 80   LYS   B CG  1 
ATOM   2762  C  CD  . LYS   B  1 80  ? 15.636 -32.741 34.613  1.00 39.68 ? 80   LYS   B CD  1 
ATOM   2763  C  CE  . LYS   B  1 80  ? 14.319 -32.072 34.293  1.00 47.94 ? 80   LYS   B CE  1 
ATOM   2764  N  NZ  . LYS   B  1 80  ? 13.229 -33.081 33.981  1.00 51.50 ? 80   LYS   B NZ  1 
ATOM   2765  N  N   . GLY   B  1 81  ? 16.060 -31.882 29.248  1.00 28.03 ? 81   GLY   B N   1 
ATOM   2766  C  CA  . GLY   B  1 81  ? 16.139 -30.857 28.207  1.00 26.11 ? 81   GLY   B CA  1 
ATOM   2767  C  C   . GLY   B  1 81  ? 16.616 -31.433 26.880  1.00 26.80 ? 81   GLY   B C   1 
ATOM   2768  O  O   . GLY   B  1 81  ? 16.522 -32.622 26.600  1.00 26.25 ? 81   GLY   B O   1 
ATOM   2769  N  N   . GLY   B  1 82  ? 17.144 -30.532 26.045  1.00 27.55 ? 82   GLY   B N   1 
ATOM   2770  C  CA  . GLY   B  1 82  ? 17.488 -30.917 24.693  1.00 27.04 ? 82   GLY   B CA  1 
ATOM   2771  C  C   . GLY   B  1 82  ? 16.276 -31.468 23.969  1.00 27.26 ? 82   GLY   B C   1 
ATOM   2772  O  O   . GLY   B  1 82  ? 15.227 -30.832 23.928  1.00 29.21 ? 82   GLY   B O   1 
ATOM   2773  N  N   . PRO   B  1 83  ? 16.416 -32.655 23.358  1.00 25.91 ? 83   PRO   B N   1 
ATOM   2774  C  CA  . PRO   B  1 83  ? 15.284 -33.304 22.686  1.00 26.80 ? 83   PRO   B CA  1 
ATOM   2775  C  C   . PRO   B  1 83  ? 14.366 -34.069 23.621  1.00 28.64 ? 83   PRO   B C   1 
ATOM   2776  O  O   . PRO   B  1 83  ? 13.387 -34.661 23.135  1.00 31.14 ? 83   PRO   B O   1 
ATOM   2777  C  CB  . PRO   B  1 83  ? 15.988 -34.283 21.722  1.00 23.20 ? 83   PRO   B CB  1 
ATOM   2778  C  CG  . PRO   B  1 83  ? 17.196 -34.739 22.532  1.00 22.76 ? 83   PRO   B CG  1 
ATOM   2779  C  CD  . PRO   B  1 83  ? 17.647 -33.458 23.260  1.00 24.33 ? 83   PRO   B CD  1 
ATOM   2780  N  N   . LEU   B  1 84  ? 14.684 -34.109 24.930  1.00 24.90 ? 84   LEU   B N   1 
ATOM   2781  C  CA  . LEU   B  1 84  ? 14.043 -35.039 25.846  1.00 25.82 ? 84   LEU   B CA  1 
ATOM   2782  C  C   . LEU   B  1 84  ? 12.825 -34.408 26.486  1.00 24.60 ? 84   LEU   B C   1 
ATOM   2783  O  O   . LEU   B  1 84  ? 12.844 -33.241 26.886  1.00 27.17 ? 84   LEU   B O   1 
ATOM   2784  C  CB  . LEU   B  1 84  ? 15.014 -35.441 26.950  1.00 22.31 ? 84   LEU   B CB  1 
ATOM   2785  C  CG  . LEU   B  1 84  ? 16.355 -35.966 26.425  1.00 22.98 ? 84   LEU   B CG  1 
ATOM   2786  C  CD1 . LEU   B  1 84  ? 17.348 -36.227 27.627  1.00 25.63 ? 84   LEU   B CD1 1 
ATOM   2787  C  CD2 . LEU   B  1 84  ? 16.137 -37.254 25.606  1.00 23.43 ? 84   LEU   B CD2 1 
ATOM   2788  N  N   . ASP   B  1 85  ? 11.786 -35.210 26.620  1.00 27.73 ? 85   ASP   B N   1 
ATOM   2789  C  CA  . ASP   B  1 85  ? 10.671 -34.889 27.502  1.00 28.86 ? 85   ASP   B CA  1 
ATOM   2790  C  C   . ASP   B  1 85  ? 10.839 -35.656 28.801  1.00 28.10 ? 85   ASP   B C   1 
ATOM   2791  O  O   . ASP   B  1 85  ? 11.019 -36.878 28.766  1.00 28.28 ? 85   ASP   B O   1 
ATOM   2792  C  CB  . ASP   B  1 85  ? 9.358  -35.266 26.827  1.00 31.89 ? 85   ASP   B CB  1 
ATOM   2793  C  CG  . ASP   B  1 85  ? 9.111  -34.441 25.574  1.00 39.91 ? 85   ASP   B CG  1 
ATOM   2794  O  OD1 . ASP   B  1 85  ? 9.242  -33.193 25.655  1.00 41.62 ? 85   ASP   B OD1 1 
ATOM   2795  O  OD2 . ASP   B  1 85  ? 8.835  -35.045 24.515  1.00 42.10 ? 85   ASP   B OD2 1 
ATOM   2796  N  N   . GLY   B  1 86  ? 10.794 -34.961 29.935  1.00 30.89 ? 86   GLY   B N   1 
ATOM   2797  C  CA  . GLY   B  1 86  ? 10.922 -35.666 31.207  1.00 32.37 ? 86   GLY   B CA  1 
ATOM   2798  C  C   . GLY   B  1 86  ? 12.365 -35.818 31.665  1.00 32.01 ? 86   GLY   B C   1 
ATOM   2799  O  O   . GLY   B  1 86  ? 13.273 -35.103 31.233  1.00 31.93 ? 86   GLY   B O   1 
ATOM   2800  N  N   . THR   B  1 87  ? 12.579 -36.797 32.546  1.00 26.54 ? 87   THR   B N   1 
ATOM   2801  C  CA  . THR   B  1 87  ? 13.839 -36.923 33.259  1.00 23.64 ? 87   THR   B CA  1 
ATOM   2802  C  C   . THR   B  1 87  ? 14.414 -38.288 32.974  1.00 24.04 ? 87   THR   B C   1 
ATOM   2803  O  O   . THR   B  1 87  ? 13.689 -39.295 33.055  1.00 24.12 ? 87   THR   B O   1 
ATOM   2804  C  CB  . THR   B  1 87  ? 13.634 -36.762 34.775  1.00 25.02 ? 87   THR   B CB  1 
ATOM   2805  O  OG1 . THR   B  1 87  ? 13.168 -35.431 35.073  1.00 29.48 ? 87   THR   B OG1 1 
ATOM   2806  C  CG2 . THR   B  1 87  ? 14.944 -37.024 35.550  1.00 26.06 ? 87   THR   B CG2 1 
ATOM   2807  N  N   . TYR   B  1 88  ? 15.704 -38.340 32.639  1.00 23.92 ? 88   TYR   B N   1 
ATOM   2808  C  CA  . TYR   B  1 88  ? 16.362 -39.619 32.316  1.00 20.56 ? 88   TYR   B CA  1 
ATOM   2809  C  C   . TYR   B  1 88  ? 17.518 -39.873 33.284  1.00 22.44 ? 88   TYR   B C   1 
ATOM   2810  O  O   . TYR   B  1 88  ? 18.446 -39.065 33.372  1.00 22.57 ? 88   TYR   B O   1 
ATOM   2811  C  CB  . TYR   B  1 88  ? 16.869 -39.615 30.874  1.00 21.53 ? 88   TYR   B CB  1 
ATOM   2812  C  CG  . TYR   B  1 88  ? 15.788 -39.700 29.808  1.00 18.77 ? 88   TYR   B CG  1 
ATOM   2813  C  CD1 . TYR   B  1 88  ? 14.898 -38.627 29.588  1.00 20.93 ? 88   TYR   B CD1 1 
ATOM   2814  C  CD2 . TYR   B  1 88  ? 15.701 -40.842 29.005  1.00 18.71 ? 88   TYR   B CD2 1 
ATOM   2815  C  CE1 . TYR   B  1 88  ? 13.941 -38.683 28.563  1.00 20.72 ? 88   TYR   B CE1 1 
ATOM   2816  C  CE2 . TYR   B  1 88  ? 14.755 -40.916 28.001  1.00 17.77 ? 88   TYR   B CE2 1 
ATOM   2817  C  CZ  . TYR   B  1 88  ? 13.863 -39.848 27.791  1.00 20.46 ? 88   TYR   B CZ  1 
ATOM   2818  O  OH  . TYR   B  1 88  ? 12.926 -39.921 26.738  1.00 22.52 ? 88   TYR   B OH  1 
ATOM   2819  N  N   . ARG   B  1 89  ? 17.456 -40.994 34.007  1.00 21.13 ? 89   ARG   B N   1 
ATOM   2820  C  CA  . ARG   B  1 89  ? 18.444 -41.311 35.044  1.00 20.31 ? 89   ARG   B CA  1 
ATOM   2821  C  C   . ARG   B  1 89  ? 19.639 -42.047 34.461  1.00 18.94 ? 89   ARG   B C   1 
ATOM   2822  O  O   . ARG   B  1 89  ? 19.467 -43.008 33.716  1.00 19.85 ? 89   ARG   B O   1 
ATOM   2823  C  CB  . ARG   B  1 89  ? 17.832 -42.177 36.145  1.00 19.95 ? 89   ARG   B CB  1 
ATOM   2824  C  CG  . ARG   B  1 89  ? 16.881 -41.435 37.089  1.00 23.37 ? 89   ARG   B CG  1 
ATOM   2825  C  CD  . ARG   B  1 89  ? 16.494 -42.387 38.228  1.00 22.43 ? 89   ARG   B CD  1 
ATOM   2826  N  NE  . ARG   B  1 89  ? 15.332 -41.866 38.951  1.00 24.82 ? 89   ARG   B NE  1 
ATOM   2827  C  CZ  . ARG   B  1 89  ? 14.551 -42.588 39.746  1.00 23.19 ? 89   ARG   B CZ  1 
ATOM   2828  N  NH1 . ARG   B  1 89  ? 14.789 -43.881 39.980  1.00 23.34 ? 89   ARG   B NH1 1 
ATOM   2829  N  NH2 . ARG   B  1 89  ? 13.479 -41.992 40.257  1.00 28.42 ? 89   ARG   B NH2 1 
ATOM   2830  N  N   . LEU   B  1 90  ? 20.844 -41.611 34.833  1.00 20.63 ? 90   LEU   B N   1 
ATOM   2831  C  CA  . LEU   B  1 90  ? 22.065 -42.342 34.482  1.00 19.30 ? 90   LEU   B CA  1 
ATOM   2832  C  C   . LEU   B  1 90  ? 22.087 -43.718 35.149  1.00 19.10 ? 90   LEU   B C   1 
ATOM   2833  O  O   . LEU   B  1 90  ? 21.977 -43.793 36.396  1.00 20.56 ? 90   LEU   B O   1 
ATOM   2834  C  CB  . LEU   B  1 90  ? 23.263 -41.518 34.965  1.00 20.57 ? 90   LEU   B CB  1 
ATOM   2835  C  CG  . LEU   B  1 90  ? 24.630 -42.200 34.723  1.00 19.99 ? 90   LEU   B CG  1 
ATOM   2836  C  CD1 . LEU   B  1 90  ? 24.900 -42.357 33.211  1.00 20.71 ? 90   LEU   B CD1 1 
ATOM   2837  C  CD2 . LEU   B  1 90  ? 25.742 -41.361 35.414  1.00 21.62 ? 90   LEU   B CD2 1 
ATOM   2838  N  N   . ILE   B  1 91  ? 22.226 -44.798 34.354  1.00 18.11 ? 91   ILE   B N   1 
ATOM   2839  C  CA  . ILE   B  1 91  ? 22.392 -46.117 34.938  1.00 18.51 ? 91   ILE   B CA  1 
ATOM   2840  C  C   . ILE   B  1 91  ? 23.821 -46.634 34.796  1.00 16.26 ? 91   ILE   B C   1 
ATOM   2841  O  O   . ILE   B  1 91  ? 24.314 -47.327 35.693  1.00 17.64 ? 91   ILE   B O   1 
ATOM   2842  C  CB  . ILE   B  1 91  ? 21.357 -47.137 34.398  1.00 17.40 ? 91   ILE   B CB  1 
ATOM   2843  C  CG1 . ILE   B  1 91  ? 21.579 -48.543 35.007  1.00 19.34 ? 91   ILE   B CG1 1 
ATOM   2844  C  CG2 . ILE   B  1 91  ? 21.353 -47.245 32.846  1.00 19.01 ? 91   ILE   B CG2 1 
ATOM   2845  C  CD1 . ILE   B  1 91  ? 20.388 -49.443 34.776  1.00 20.69 ? 91   ILE   B CD1 1 
ATOM   2846  N  N   . GLN   B  1 92  ? 24.501 -46.358 33.685  1.00 15.96 ? 92   GLN   B N   1 
ATOM   2847  C  CA  . GLN   B  1 92  ? 25.846 -46.893 33.477  1.00 17.15 ? 92   GLN   B CA  1 
ATOM   2848  C  C   . GLN   B  1 92  ? 26.511 -46.123 32.344  1.00 17.85 ? 92   GLN   B C   1 
ATOM   2849  O  O   . GLN   B  1 92  ? 25.840 -45.445 31.541  1.00 18.03 ? 92   GLN   B O   1 
ATOM   2850  C  CB  . GLN   B  1 92  ? 25.847 -48.398 33.132  1.00 15.32 ? 92   GLN   B CB  1 
ATOM   2851  C  CG  . GLN   B  1 92  ? 24.998 -48.736 31.874  1.00 17.56 ? 92   GLN   B CG  1 
ATOM   2852  C  CD  . GLN   B  1 92  ? 25.846 -49.183 30.697  1.00 15.34 ? 92   GLN   B CD  1 
ATOM   2853  O  OE1 . GLN   B  1 92  ? 26.819 -48.525 30.313  1.00 16.94 ? 92   GLN   B OE1 1 
ATOM   2854  N  NE2 . GLN   B  1 92  ? 25.470 -50.322 30.100  1.00 18.88 ? 92   GLN   B NE2 1 
ATOM   2855  N  N   . PHE   B  1 93  ? 27.848 -46.202 32.308  1.00 16.91 ? 93   PHE   B N   1 
ATOM   2856  C  CA  . PHE   B  1 93  ? 28.558 -45.879 31.064  1.00 16.83 ? 93   PHE   B CA  1 
ATOM   2857  C  C   . PHE   B  1 93  ? 29.522 -47.001 30.674  1.00 17.67 ? 93   PHE   B C   1 
ATOM   2858  O  O   . PHE   B  1 93  ? 29.926 -47.832 31.477  1.00 16.39 ? 93   PHE   B O   1 
ATOM   2859  C  CB  . PHE   B  1 93  ? 29.324 -44.531 31.152  1.00 18.63 ? 93   PHE   B CB  1 
ATOM   2860  C  CG  . PHE   B  1 93  ? 30.512 -44.516 32.087  1.00 18.23 ? 93   PHE   B CG  1 
ATOM   2861  C  CD1 . PHE   B  1 93  ? 31.745 -45.081 31.707  1.00 17.74 ? 93   PHE   B CD1 1 
ATOM   2862  C  CD2 . PHE   B  1 93  ? 30.408 -43.858 33.319  1.00 19.51 ? 93   PHE   B CD2 1 
ATOM   2863  C  CE1 . PHE   B  1 93  ? 32.833 -45.003 32.550  1.00 17.22 ? 93   PHE   B CE1 1 
ATOM   2864  C  CE2 . PHE   B  1 93  ? 31.505 -43.787 34.184  1.00 20.43 ? 93   PHE   B CE2 1 
ATOM   2865  C  CZ  . PHE   B  1 93  ? 32.708 -44.361 33.820  1.00 19.77 ? 93   PHE   B CZ  1 
ATOM   2866  N  N   . HIS   B  1 94  ? 29.903 -47.001 29.406  1.00 16.21 ? 94   HIS   B N   1 
ATOM   2867  C  CA  . HIS   B  1 94  ? 30.826 -47.974 28.841  1.00 16.66 ? 94   HIS   B CA  1 
ATOM   2868  C  C   . HIS   B  1 94  ? 31.439 -47.322 27.608  1.00 16.07 ? 94   HIS   B C   1 
ATOM   2869  O  O   . HIS   B  1 94  ? 31.017 -46.248 27.190  1.00 16.33 ? 94   HIS   B O   1 
ATOM   2870  C  CB  . HIS   B  1 94  ? 30.107 -49.284 28.437  1.00 15.58 ? 94   HIS   B CB  1 
ATOM   2871  C  CG  . HIS   B  1 94  ? 29.047 -49.043 27.397  1.00 13.64 ? 94   HIS   B CG  1 
ATOM   2872  N  ND1 . HIS   B  1 94  ? 27.757 -48.665 27.732  1.00 15.25 ? 94   HIS   B ND1 1 
ATOM   2873  C  CD2 . HIS   B  1 94  ? 29.109 -49.030 26.045  1.00 15.91 ? 94   HIS   B CD2 1 
ATOM   2874  C  CE1 . HIS   B  1 94  ? 27.059 -48.452 26.618  1.00 14.74 ? 94   HIS   B CE1 1 
ATOM   2875  N  NE2 . HIS   B  1 94  ? 27.856 -48.650 25.575  1.00 14.07 ? 94   HIS   B NE2 1 
ATOM   2876  N  N   . PHE   B  1 95  ? 32.391 -48.020 26.989  1.00 16.47 ? 95   PHE   B N   1 
ATOM   2877  C  CA  . PHE   B  1 95  ? 33.088 -47.531 25.805  1.00 16.71 ? 95   PHE   B CA  1 
ATOM   2878  C  C   . PHE   B  1 95  ? 33.053 -48.573 24.694  1.00 17.85 ? 95   PHE   B C   1 
ATOM   2879  O  O   . PHE   B  1 95  ? 32.816 -49.776 24.913  1.00 17.53 ? 95   PHE   B O   1 
ATOM   2880  C  CB  . PHE   B  1 95  ? 34.583 -47.186 26.086  1.00 17.05 ? 95   PHE   B CB  1 
ATOM   2881  C  CG  . PHE   B  1 95  ? 34.818 -46.167 27.142  1.00 17.88 ? 95   PHE   B CG  1 
ATOM   2882  C  CD1 . PHE   B  1 95  ? 34.715 -46.539 28.492  1.00 18.09 ? 95   PHE   B CD1 1 
ATOM   2883  C  CD2 . PHE   B  1 95  ? 35.143 -44.850 26.811  1.00 18.61 ? 95   PHE   B CD2 1 
ATOM   2884  C  CE1 . PHE   B  1 95  ? 34.976 -45.608 29.484  1.00 18.54 ? 95   PHE   B CE1 1 
ATOM   2885  C  CE2 . PHE   B  1 95  ? 35.423 -43.901 27.819  1.00 19.35 ? 95   PHE   B CE2 1 
ATOM   2886  C  CZ  . PHE   B  1 95  ? 35.335 -44.287 29.159  1.00 20.76 ? 95   PHE   B CZ  1 
ATOM   2887  N  N   . HIS   B  1 96  ? 33.319 -48.083 23.474  1.00 15.79 ? 96   HIS   B N   1 
ATOM   2888  C  CA  . HIS   B  1 96  ? 33.597 -48.901 22.306  1.00 15.52 ? 96   HIS   B CA  1 
ATOM   2889  C  C   . HIS   B  1 96  ? 34.955 -48.442 21.777  1.00 16.28 ? 96   HIS   B C   1 
ATOM   2890  O  O   . HIS   B  1 96  ? 35.231 -47.242 21.766  1.00 17.31 ? 96   HIS   B O   1 
ATOM   2891  C  CB  . HIS   B  1 96  ? 32.515 -48.696 21.228  1.00 15.31 ? 96   HIS   B CB  1 
ATOM   2892  C  CG  . HIS   B  1 96  ? 31.120 -49.001 21.712  1.00 14.62 ? 96   HIS   B CG  1 
ATOM   2893  N  ND1 . HIS   B  1 96  ? 30.501 -50.222 21.495  1.00 17.54 ? 96   HIS   B ND1 1 
ATOM   2894  C  CD2 . HIS   B  1 96  ? 30.269 -48.276 22.497  1.00 16.52 ? 96   HIS   B CD2 1 
ATOM   2895  C  CE1 . HIS   B  1 96  ? 29.301 -50.202 22.082  1.00 15.10 ? 96   HIS   B CE1 1 
ATOM   2896  N  NE2 . HIS   B  1 96  ? 29.139 -49.042 22.704  1.00 16.22 ? 96   HIS   B NE2 1 
ATOM   2897  N  N   . TRP   B  1 97  ? 35.822 -49.377 21.368  1.00 15.82 ? 97   TRP   B N   1 
ATOM   2898  C  CA  . TRP   B  1 97  ? 37.166 -48.997 20.899  1.00 15.83 ? 97   TRP   B CA  1 
ATOM   2899  C  C   . TRP   B  1 97  ? 37.684 -49.993 19.880  1.00 18.27 ? 97   TRP   B C   1 
ATOM   2900  O  O   . TRP   B  1 97  ? 37.072 -51.035 19.641  1.00 16.76 ? 97   TRP   B O   1 
ATOM   2901  C  CB  . TRP   B  1 97  ? 38.145 -48.882 22.074  1.00 17.52 ? 97   TRP   B CB  1 
ATOM   2902  C  CG  . TRP   B  1 97  ? 38.344 -50.176 22.846  1.00 16.85 ? 97   TRP   B CG  1 
ATOM   2903  C  CD1 . TRP   B  1 97  ? 39.289 -51.137 22.609  1.00 18.21 ? 97   TRP   B CD1 1 
ATOM   2904  C  CD2 . TRP   B  1 97  ? 37.581 -50.626 23.983  1.00 16.40 ? 97   TRP   B CD2 1 
ATOM   2905  N  NE1 . TRP   B  1 97  ? 39.173 -52.178 23.525  1.00 17.37 ? 97   TRP   B NE1 1 
ATOM   2906  C  CE2 . TRP   B  1 97  ? 38.123 -51.889 24.377  1.00 17.11 ? 97   TRP   B CE2 1 
ATOM   2907  C  CE3 . TRP   B  1 97  ? 36.508 -50.078 24.713  1.00 15.32 ? 97   TRP   B CE3 1 
ATOM   2908  C  CZ2 . TRP   B  1 97  ? 37.627 -52.601 25.504  1.00 17.59 ? 97   TRP   B CZ2 1 
ATOM   2909  C  CZ3 . TRP   B  1 97  ? 35.994 -50.801 25.781  1.00 16.95 ? 97   TRP   B CZ3 1 
ATOM   2910  C  CH2 . TRP   B  1 97  ? 36.585 -52.020 26.186  1.00 16.43 ? 97   TRP   B CH2 1 
ATOM   2911  N  N   . GLY   B  1 98  ? 38.831 -49.668 19.276  1.00 18.37 ? 98   GLY   B N   1 
ATOM   2912  C  CA  . GLY   B  1 98  ? 39.377 -50.438 18.177  1.00 18.63 ? 98   GLY   B CA  1 
ATOM   2913  C  C   . GLY   B  1 98  ? 40.606 -51.262 18.576  1.00 19.73 ? 98   GLY   B C   1 
ATOM   2914  O  O   . GLY   B  1 98  ? 41.092 -51.264 19.712  1.00 20.25 ? 98   GLY   B O   1 
ATOM   2915  N  N   . SER   B  1 99  ? 41.073 -52.051 17.592  1.00 20.31 ? 99   SER   B N   1 
ATOM   2916  C  CA  . SER   B  1 99  ? 42.342 -52.748 17.730  1.00 21.16 ? 99   SER   B CA  1 
ATOM   2917  C  C   . SER   B  1 99  ? 43.549 -51.838 17.472  1.00 22.63 ? 99   SER   B C   1 
ATOM   2918  O  O   . SER   B  1 99  ? 44.687 -52.248 17.734  1.00 24.16 ? 99   SER   B O   1 
ATOM   2919  C  CB  . SER   B  1 99  ? 42.364 -53.958 16.789  1.00 23.07 ? 99   SER   B CB  1 
ATOM   2920  O  OG  . SER   B  1 99  ? 42.018 -53.582 15.462  1.00 25.40 ? 99   SER   B OG  1 
ATOM   2921  N  N   . HIS   B  1 100 ? 43.324 -50.628 16.974  1.00 23.77 ? 100  HIS   B N   1 
ATOM   2922  C  CA  . HIS   B  1 100 ? 44.376 -49.639 16.837  1.00 23.95 ? 100  HIS   B CA  1 
ATOM   2923  C  C   . HIS   B  1 100 ? 43.708 -48.280 16.891  1.00 23.88 ? 100  HIS   B C   1 
ATOM   2924  O  O   . HIS   B  1 100 ? 42.482 -48.192 16.834  1.00 23.68 ? 100  HIS   B O   1 
ATOM   2925  C  CB  . HIS   B  1 100 ? 45.146 -49.851 15.527  1.00 22.91 ? 100  HIS   B CB  1 
ATOM   2926  C  CG  . HIS   B  1 100 ? 44.305 -49.769 14.306  1.00 24.65 ? 100  HIS   B CG  1 
ATOM   2927  N  ND1 . HIS   B  1 100 ? 44.061 -48.576 13.663  1.00 27.32 ? 100  HIS   B ND1 1 
ATOM   2928  C  CD2 . HIS   B  1 100 ? 43.637 -50.721 13.613  1.00 25.47 ? 100  HIS   B CD2 1 
ATOM   2929  C  CE1 . HIS   B  1 100 ? 43.284 -48.794 12.614  1.00 27.89 ? 100  HIS   B CE1 1 
ATOM   2930  N  NE2 . HIS   B  1 100 ? 42.996 -50.086 12.569  1.00 25.73 ? 100  HIS   B NE2 1 
ATOM   2931  N  N   . ASP   B  1 101 ? 44.513 -47.215 17.009  1.00 22.93 ? 101  ASP   B N   1 
ATOM   2932  C  CA  . ASP   B  1 101 ? 43.930 -45.901 17.269  1.00 23.73 ? 101  ASP   B CA  1 
ATOM   2933  C  C   . ASP   B  1 101 ? 43.123 -45.352 16.092  1.00 24.37 ? 101  ASP   B C   1 
ATOM   2934  O  O   . ASP   B  1 101 ? 42.392 -44.377 16.274  1.00 26.01 ? 101  ASP   B O   1 
ATOM   2935  C  CB  . ASP   B  1 101 ? 45.020 -44.884 17.592  1.00 27.15 ? 101  ASP   B CB  1 
ATOM   2936  C  CG  . ASP   B  1 101 ? 45.678 -45.110 18.958  1.00 26.13 ? 101  ASP   B CG  1 
ATOM   2937  O  OD1 . ASP   B  1 101 ? 45.196 -45.947 19.764  1.00 27.13 ? 101  ASP   B OD1 1 
ATOM   2938  O  OD2 . ASP   B  1 101 ? 46.703 -44.405 19.197  1.00 28.32 ? 101  ASP   B OD2 1 
ATOM   2939  N  N   . GLY   B  1 102 ? 43.255 -45.921 14.907  1.00 24.76 ? 102  GLY   B N   1 
ATOM   2940  C  CA  . GLY   B  1 102 ? 42.554 -45.375 13.761  1.00 24.01 ? 102  GLY   B CA  1 
ATOM   2941  C  C   . GLY   B  1 102 ? 41.106 -45.801 13.583  1.00 25.06 ? 102  GLY   B C   1 
ATOM   2942  O  O   . GLY   B  1 102 ? 40.453 -45.419 12.598  1.00 26.39 ? 102  GLY   B O   1 
ATOM   2943  N  N   . GLN   B  1 103 ? 40.586 -46.622 14.480  1.00 21.65 ? 103  GLN   B N   1 
ATOM   2944  C  CA  . GLN   B  1 103 ? 39.166 -46.966 14.464  1.00 20.94 ? 103  GLN   B CA  1 
ATOM   2945  C  C   . GLN   B  1 103 ? 38.745 -47.224 15.892  1.00 22.19 ? 103  GLN   B C   1 
ATOM   2946  O  O   . GLN   B  1 103 ? 39.584 -47.327 16.802  1.00 21.48 ? 103  GLN   B O   1 
ATOM   2947  C  CB  . GLN   B  1 103 ? 38.847 -48.177 13.545  1.00 22.32 ? 103  GLN   B CB  1 
ATOM   2948  C  CG  . GLN   B  1 103 ? 39.514 -49.478 13.975  1.00 24.53 ? 103  GLN   B CG  1 
ATOM   2949  C  CD  . GLN   B  1 103 ? 39.436 -50.550 12.914  1.00 24.62 ? 103  GLN   B CD  1 
ATOM   2950  O  OE1 . GLN   B  1 103 ? 39.384 -50.230 11.725  1.00 25.73 ? 103  GLN   B OE1 1 
ATOM   2951  N  NE2 . GLN   B  1 103 ? 39.419 -51.825 13.309  1.00 21.44 ? 103  GLN   B NE2 1 
ATOM   2952  N  N   . GLY   B  1 104 ? 37.433 -47.361 16.090  1.00 19.94 ? 104  GLY   B N   1 
ATOM   2953  C  CA  . GLY   B  1 104 ? 36.921 -47.620 17.418  1.00 18.74 ? 104  GLY   B CA  1 
ATOM   2954  C  C   . GLY   B  1 104 ? 35.593 -46.976 17.714  1.00 18.09 ? 104  GLY   B C   1 
ATOM   2955  O  O   . GLY   B  1 104 ? 34.756 -47.577 18.391  1.00 18.87 ? 104  GLY   B O   1 
ATOM   2956  N  N   . SER   B  1 105 ? 35.391 -45.736 17.239  1.00 17.15 ? 105  SER   B N   1 
ATOM   2957  C  CA  . SER   B  1 105 ? 34.105 -45.117 17.518  1.00 17.56 ? 105  SER   B CA  1 
ATOM   2958  C  C   . SER   B  1 105 ? 32.996 -45.819 16.741  1.00 16.48 ? 105  SER   B C   1 
ATOM   2959  O  O   . SER   B  1 105 ? 33.235 -46.496 15.727  1.00 17.35 ? 105  SER   B O   1 
ATOM   2960  C  CB  . SER   B  1 105 ? 34.139 -43.606 17.211  1.00 18.06 ? 105  SER   B CB  1 
ATOM   2961  O  OG  . SER   B  1 105 ? 34.261 -43.328 15.804  1.00 19.18 ? 105  SER   B OG  1 
ATOM   2962  N  N   . GLU   B  1 106 ? 31.752 -45.619 17.215  1.00 16.82 ? 106  GLU   B N   1 
ATOM   2963  C  CA  . GLU   B  1 106 ? 30.572 -46.195 16.576  1.00 15.07 ? 106  GLU   B CA  1 
ATOM   2964  C  C   . GLU   B  1 106 ? 29.979 -45.184 15.598  1.00 16.88 ? 106  GLU   B C   1 
ATOM   2965  O  O   . GLU   B  1 106 ? 29.939 -45.410 14.394  1.00 16.74 ? 106  GLU   B O   1 
ATOM   2966  C  CB  . GLU   B  1 106 ? 29.548 -46.656 17.635  1.00 17.43 ? 106  GLU   B CB  1 
ATOM   2967  C  CG  . GLU   B  1 106 ? 30.136 -47.765 18.491  1.00 16.86 ? 106  GLU   B CG  1 
ATOM   2968  C  CD  . GLU   B  1 106 ? 29.068 -48.701 18.986  1.00 16.26 ? 106  GLU   B CD  1 
ATOM   2969  O  OE1 . GLU   B  1 106 ? 28.166 -48.209 19.708  1.00 17.00 ? 106  GLU   B OE1 1 
ATOM   2970  O  OE2 . GLU   B  1 106 ? 29.150 -49.884 18.614  1.00 17.31 ? 106  GLU   B OE2 1 
ATOM   2971  N  N   . HIS   B  1 107 ? 29.588 -44.027 16.107  1.00 16.20 ? 107  HIS   B N   1 
ATOM   2972  C  CA  . HIS   B  1 107 ? 29.262 -42.931 15.219  1.00 17.53 ? 107  HIS   B CA  1 
ATOM   2973  C  C   . HIS   B  1 107 ? 30.514 -42.449 14.485  1.00 18.09 ? 107  HIS   B C   1 
ATOM   2974  O  O   . HIS   B  1 107 ? 31.646 -42.601 14.960  1.00 18.80 ? 107  HIS   B O   1 
ATOM   2975  C  CB  . HIS   B  1 107 ? 28.618 -41.782 16.003  1.00 15.66 ? 107  HIS   B CB  1 
ATOM   2976  C  CG  . HIS   B  1 107 ? 27.273 -42.159 16.536  1.00 16.11 ? 107  HIS   B CG  1 
ATOM   2977  N  ND1 . HIS   B  1 107 ? 27.126 -42.777 17.753  1.00 16.55 ? 107  HIS   B ND1 1 
ATOM   2978  C  CD2 . HIS   B  1 107 ? 26.041 -42.114 15.970  1.00 17.64 ? 107  HIS   B CD2 1 
ATOM   2979  C  CE1 . HIS   B  1 107 ? 25.839 -43.043 17.951  1.00 17.75 ? 107  HIS   B CE1 1 
ATOM   2980  N  NE2 . HIS   B  1 107 ? 25.158 -42.660 16.886  1.00 17.31 ? 107  HIS   B NE2 1 
ATOM   2981  N  N   . THR   B  1 108 ? 30.289 -41.916 13.289  1.00 16.97 ? 108  THR   B N   1 
ATOM   2982  C  CA  . THR   B  1 108 ? 31.333 -41.220 12.532  1.00 17.37 ? 108  THR   B CA  1 
ATOM   2983  C  C   . THR   B  1 108 ? 30.864 -39.802 12.245  1.00 17.53 ? 108  THR   B C   1 
ATOM   2984  O  O   . THR   B  1 108 ? 29.667 -39.533 12.274  1.00 19.58 ? 108  THR   B O   1 
ATOM   2985  C  CB  . THR   B  1 108 ? 31.678 -41.951 11.203  1.00 17.51 ? 108  THR   B CB  1 
ATOM   2986  O  OG1 . THR   B  1 108 ? 30.506 -42.146 10.399  1.00 19.41 ? 108  THR   B OG1 1 
ATOM   2987  C  CG2 . THR   B  1 108 ? 32.279 -43.327 11.473  1.00 19.66 ? 108  THR   B CG2 1 
ATOM   2988  N  N   . VAL   B  1 109 ? 31.809 -38.900 11.958  1.00 18.55 ? 109  VAL   B N   1 
ATOM   2989  C  CA  . VAL   B  1 109 ? 31.531 -37.500 11.599  1.00 19.95 ? 109  VAL   B CA  1 
ATOM   2990  C  C   . VAL   B  1 109 ? 32.145 -37.286 10.234  1.00 22.10 ? 109  VAL   B C   1 
ATOM   2991  O  O   . VAL   B  1 109 ? 33.362 -37.362 10.058  1.00 21.88 ? 109  VAL   B O   1 
ATOM   2992  C  CB  . VAL   B  1 109 ? 32.047 -36.499 12.656  1.00 21.23 ? 109  VAL   B CB  1 
ATOM   2993  C  CG1 . VAL   B  1 109 ? 31.659 -35.053 12.274  1.00 24.12 ? 109  VAL   B CG1 1 
ATOM   2994  C  CG2 . VAL   B  1 109 ? 31.418 -36.833 14.012  1.00 21.53 ? 109  VAL   B CG2 1 
ATOM   2995  N  N   . ASP   B  1 110 ? 31.300 -37.058 9.234   1.00 20.93 ? 110  ASP   B N   1 
ATOM   2996  C  CA  . ASP   B  1 110 ? 31.780 -36.921 7.857   1.00 21.74 ? 110  ASP   B CA  1 
ATOM   2997  C  C   . ASP   B  1 110 ? 32.707 -38.096 7.527   1.00 24.27 ? 110  ASP   B C   1 
ATOM   2998  O  O   . ASP   B  1 110 ? 33.770 -37.940 6.917   1.00 27.39 ? 110  ASP   B O   1 
ATOM   2999  C  CB  . ASP   B  1 110 ? 32.471 -35.556 7.618   1.00 23.90 ? 110  ASP   B CB  1 
ATOM   3000  C  CG  . ASP   B  1 110 ? 31.523 -34.400 7.839   1.00 29.78 ? 110  ASP   B CG  1 
ATOM   3001  O  OD1 . ASP   B  1 110 ? 30.287 -34.560 7.608   1.00 26.25 ? 110  ASP   B OD1 1 
ATOM   3002  O  OD2 . ASP   B  1 110 ? 32.011 -33.306 8.207   1.00 31.88 ? 110  ASP   B OD2 1 
ATOM   3003  N  N   . LYS   B  1 111 ? 32.284 -39.295 7.946   1.00 22.59 ? 111  LYS   B N   1 
ATOM   3004  C  CA  . LYS   B  1 111 ? 32.909 -40.607 7.701   1.00 22.04 ? 111  LYS   B CA  1 
ATOM   3005  C  C   . LYS   B  1 111 ? 34.166 -40.841 8.521   1.00 25.91 ? 111  LYS   B C   1 
ATOM   3006  O  O   . LYS   B  1 111 ? 34.745 -41.930 8.449   1.00 30.23 ? 111  LYS   B O   1 
ATOM   3007  C  CB  . LYS   B  1 111 ? 33.229 -40.874 6.217   1.00 26.03 ? 111  LYS   B CB  1 
ATOM   3008  C  CG  . LYS   B  1 111 ? 32.063 -40.711 5.285   1.00 32.26 ? 111  LYS   B CG  1 
ATOM   3009  C  CD  . LYS   B  1 111 ? 30.910 -41.637 5.683   1.00 40.02 ? 111  LYS   B CD  1 
ATOM   3010  C  CE  . LYS   B  1 111 ? 31.381 -43.122 5.679   1.00 44.38 ? 111  LYS   B CE  1 
ATOM   3011  N  NZ  . LYS   B  1 111 ? 30.334 -44.083 6.061   1.00 41.52 ? 111  LYS   B NZ  1 
ATOM   3012  N  N   . LYS   B  1 112 ? 34.571 -39.897 9.347   1.00 23.80 ? 112  LYS   B N   1 
ATOM   3013  C  CA  . LYS   B  1 112 ? 35.793 -40.051 10.126  1.00 26.35 ? 112  LYS   B CA  1 
ATOM   3014  C  C   . LYS   B  1 112 ? 35.502 -40.790 11.409  1.00 22.66 ? 112  LYS   B C   1 
ATOM   3015  O  O   . LYS   B  1 112 ? 34.493 -40.534 12.072  1.00 21.21 ? 112  LYS   B O   1 
ATOM   3016  C  CB  . LYS   B  1 112 ? 36.388 -38.689 10.457  1.00 31.66 ? 112  LYS   B CB  1 
ATOM   3017  C  CG  . LYS   B  1 112 ? 37.635 -38.708 11.371  1.00 42.53 ? 112  LYS   B CG  1 
ATOM   3018  C  CD  . LYS   B  1 112 ? 37.322 -38.235 12.811  1.00 47.12 ? 112  LYS   B CD  1 
ATOM   3019  C  CE  . LYS   B  1 112 ? 38.587 -37.800 13.557  1.00 50.26 ? 112  LYS   B CE  1 
ATOM   3020  N  NZ  . LYS   B  1 112 ? 39.652 -38.840 13.540  1.00 53.67 ? 112  LYS   B NZ  1 
ATOM   3021  N  N   . LYS   B  1 113 ? 36.399 -41.700 11.759  1.00 21.42 ? 113  LYS   B N   1 
ATOM   3022  C  CA  . LYS   B  1 113 ? 36.324 -42.417 13.022  1.00 20.33 ? 113  LYS   B CA  1 
ATOM   3023  C  C   . LYS   B  1 113 ? 37.282 -41.859 14.070  1.00 21.62 ? 113  LYS   B C   1 
ATOM   3024  O  O   . LYS   B  1 113 ? 38.366 -41.338 13.761  1.00 26.67 ? 113  LYS   B O   1 
ATOM   3025  C  CB  . LYS   B  1 113 ? 36.665 -43.891 12.808  1.00 20.18 ? 113  LYS   B CB  1 
ATOM   3026  C  CG  . LYS   B  1 113 ? 35.590 -44.597 12.043  1.00 22.29 ? 113  LYS   B CG  1 
ATOM   3027  C  CD  . LYS   B  1 113 ? 35.911 -46.085 11.888  1.00 25.99 ? 113  LYS   B CD  1 
ATOM   3028  C  CE  . LYS   B  1 113 ? 34.690 -46.815 11.314  1.00 25.59 ? 113  LYS   B CE  1 
ATOM   3029  N  NZ  . LYS   B  1 113 ? 34.724 -48.322 11.583  1.00 26.75 ? 113  LYS   B NZ  1 
ATOM   3030  N  N   . TYR   B  1 114 ? 36.857 -41.976 15.323  1.00 21.64 ? 114  TYR   B N   1 
ATOM   3031  C  CA  . TYR   B  1 114 ? 37.717 -41.666 16.452  1.00 22.60 ? 114  TYR   B CA  1 
ATOM   3032  C  C   . TYR   B  1 114 ? 38.240 -42.961 17.047  1.00 20.01 ? 114  TYR   B C   1 
ATOM   3033  O  O   . TYR   B  1 114 ? 37.720 -44.037 16.749  1.00 19.58 ? 114  TYR   B O   1 
ATOM   3034  C  CB  . TYR   B  1 114 ? 36.950 -40.867 17.506  1.00 22.75 ? 114  TYR   B CB  1 
ATOM   3035  C  CG  . TYR   B  1 114 ? 36.580 -39.489 17.052  1.00 24.16 ? 114  TYR   B CG  1 
ATOM   3036  C  CD1 . TYR   B  1 114 ? 35.394 -39.257 16.369  1.00 24.29 ? 114  TYR   B CD1 1 
ATOM   3037  C  CD2 . TYR   B  1 114 ? 37.409 -38.398 17.364  1.00 27.51 ? 114  TYR   B CD2 1 
ATOM   3038  C  CE1 . TYR   B  1 114 ? 35.060 -37.963 15.967  1.00 28.27 ? 114  TYR   B CE1 1 
ATOM   3039  C  CE2 . TYR   B  1 114 ? 37.074 -37.101 16.949  1.00 27.41 ? 114  TYR   B CE2 1 
ATOM   3040  C  CZ  . TYR   B  1 114 ? 35.889 -36.922 16.267  1.00 29.39 ? 114  TYR   B CZ  1 
ATOM   3041  O  OH  . TYR   B  1 114 ? 35.520 -35.654 15.862  1.00 34.17 ? 114  TYR   B OH  1 
ATOM   3042  N  N   . ALA   B  1 115 ? 39.194 -42.853 17.977  1.00 20.85 ? 115  ALA   B N   1 
ATOM   3043  C  CA  . ALA   B  1 115 ? 39.778 -44.041 18.588  1.00 20.09 ? 115  ALA   B CA  1 
ATOM   3044  C  C   . ALA   B  1 115 ? 38.828 -44.756 19.522  1.00 20.59 ? 115  ALA   B C   1 
ATOM   3045  O  O   . ALA   B  1 115 ? 38.989 -45.967 19.755  1.00 20.16 ? 115  ALA   B O   1 
ATOM   3046  C  CB  . ALA   B  1 115 ? 41.056 -43.648 19.369  1.00 22.20 ? 115  ALA   B CB  1 
ATOM   3047  N  N   . ALA   B  1 116 ? 37.836 -44.057 20.068  1.00 18.79 ? 116  ALA   B N   1 
ATOM   3048  C  CA  . ALA   B  1 116 ? 36.885 -44.741 20.931  1.00 18.05 ? 116  ALA   B CA  1 
ATOM   3049  C  C   . ALA   B  1 116 ? 35.665 -43.843 21.069  1.00 19.08 ? 116  ALA   B C   1 
ATOM   3050  O  O   . ALA   B  1 116 ? 35.669 -42.700 20.608  1.00 18.95 ? 116  ALA   B O   1 
ATOM   3051  C  CB  . ALA   B  1 116 ? 37.517 -45.080 22.309  1.00 18.81 ? 116  ALA   B CB  1 
ATOM   3052  N  N   . GLU   B  1 117 ? 34.625 -44.384 21.692  1.00 17.57 ? 117  GLU   B N   1 
ATOM   3053  C  CA  . GLU   B  1 117 ? 33.401 -43.641 21.925  1.00 18.15 ? 117  GLU   B CA  1 
ATOM   3054  C  C   . GLU   B  1 117 ? 32.862 -44.064 23.284  1.00 17.89 ? 117  GLU   B C   1 
ATOM   3055  O  O   . GLU   B  1 117 ? 32.787 -45.254 23.586  1.00 17.74 ? 117  GLU   B O   1 
ATOM   3056  C  CB  . GLU   B  1 117 ? 32.381 -43.901 20.797  1.00 17.27 ? 117  GLU   B CB  1 
ATOM   3057  C  CG  . GLU   B  1 117 ? 31.124 -43.035 20.896  1.00 17.57 ? 117  GLU   B CG  1 
ATOM   3058  C  CD  . GLU   B  1 117 ? 30.235 -43.191 19.682  1.00 18.28 ? 117  GLU   B CD  1 
ATOM   3059  O  OE1 . GLU   B  1 117 ? 30.765 -43.357 18.554  1.00 17.63 ? 117  GLU   B OE1 1 
ATOM   3060  O  OE2 . GLU   B  1 117 ? 28.995 -43.125 19.822  1.00 18.61 ? 117  GLU   B OE2 1 
ATOM   3061  N  N   . LEU   B  1 118 ? 32.489 -43.061 24.085  1.00 17.48 ? 118  LEU   B N   1 
ATOM   3062  C  CA  . LEU   B  1 118 ? 31.919 -43.227 25.412  1.00 17.18 ? 118  LEU   B CA  1 
ATOM   3063  C  C   . LEU   B  1 118 ? 30.406 -43.079 25.326  1.00 16.43 ? 118  LEU   B C   1 
ATOM   3064  O  O   . LEU   B  1 118 ? 29.899 -42.152 24.671  1.00 18.36 ? 118  LEU   B O   1 
ATOM   3065  C  CB  . LEU   B  1 118 ? 32.510 -42.141 26.326  1.00 17.35 ? 118  LEU   B CB  1 
ATOM   3066  C  CG  . LEU   B  1 118 ? 31.764 -41.923 27.640  1.00 17.69 ? 118  LEU   B CG  1 
ATOM   3067  C  CD1 . LEU   B  1 118 ? 31.819 -43.154 28.552  1.00 17.42 ? 118  LEU   B CD1 1 
ATOM   3068  C  CD2 . LEU   B  1 118 ? 32.390 -40.710 28.353  1.00 20.33 ? 118  LEU   B CD2 1 
ATOM   3069  N  N   . HIS   B  1 119 ? 29.680 -44.015 25.942  1.00 15.72 ? 119  HIS   B N   1 
ATOM   3070  C  CA  . HIS   B  1 119 ? 28.215 -43.978 26.012  1.00 15.97 ? 119  HIS   B CA  1 
ATOM   3071  C  C   . HIS   B  1 119 ? 27.778 -43.896 27.462  1.00 16.57 ? 119  HIS   B C   1 
ATOM   3072  O  O   . HIS   B  1 119 ? 27.994 -44.855 28.224  1.00 16.96 ? 119  HIS   B O   1 
ATOM   3073  C  CB  . HIS   B  1 119 ? 27.602 -45.232 25.383  1.00 16.05 ? 119  HIS   B CB  1 
ATOM   3074  C  CG  . HIS   B  1 119 ? 27.763 -45.255 23.902  1.00 15.57 ? 119  HIS   B CG  1 
ATOM   3075  N  ND1 . HIS   B  1 119 ? 27.629 -46.390 23.147  1.00 15.20 ? 119  HIS   B ND1 1 
ATOM   3076  C  CD2 . HIS   B  1 119 ? 28.054 -44.244 23.038  1.00 15.00 ? 119  HIS   B CD2 1 
ATOM   3077  C  CE1 . HIS   B  1 119 ? 27.827 -46.080 21.868  1.00 14.95 ? 119  HIS   B CE1 1 
ATOM   3078  N  NE2 . HIS   B  1 119 ? 28.134 -44.793 21.788  1.00 16.22 ? 119  HIS   B NE2 1 
ATOM   3079  N  N   . LEU   B  1 120 ? 27.107 -42.794 27.808  1.00 18.25 ? 120  LEU   B N   1 
ATOM   3080  C  CA  . LEU   B  1 120 ? 26.465 -42.624 29.117  1.00 17.28 ? 120  LEU   B CA  1 
ATOM   3081  C  C   . LEU   B  1 120 ? 24.976 -42.933 28.917  1.00 18.64 ? 120  LEU   B C   1 
ATOM   3082  O  O   . LEU   B  1 120 ? 24.275 -42.238 28.150  1.00 16.89 ? 120  LEU   B O   1 
ATOM   3083  C  CB  . LEU   B  1 120 ? 26.704 -41.209 29.633  1.00 18.35 ? 120  LEU   B CB  1 
ATOM   3084  C  CG  . LEU   B  1 120 ? 28.157 -40.933 29.999  1.00 18.77 ? 120  LEU   B CG  1 
ATOM   3085  C  CD1 . LEU   B  1 120 ? 28.631 -39.608 29.327  1.00 23.61 ? 120  LEU   B CD1 1 
ATOM   3086  C  CD2 . LEU   B  1 120 ? 28.368 -40.894 31.512  1.00 22.00 ? 120  LEU   B CD2 1 
ATOM   3087  N  N   . VAL   B  1 121 ? 24.494 -43.989 29.563  1.00 18.00 ? 121  VAL   B N   1 
ATOM   3088  C  CA  . VAL   B  1 121 ? 23.185 -44.580 29.282  1.00 17.60 ? 121  VAL   B CA  1 
ATOM   3089  C  C   . VAL   B  1 121 ? 22.170 -44.143 30.334  1.00 18.13 ? 121  VAL   B C   1 
ATOM   3090  O  O   . VAL   B  1 121 ? 22.411 -44.301 31.545  1.00 17.82 ? 121  VAL   B O   1 
ATOM   3091  C  CB  . VAL   B  1 121 ? 23.297 -46.109 29.271  1.00 16.75 ? 121  VAL   B CB  1 
ATOM   3092  C  CG1 . VAL   B  1 121 ? 21.929 -46.767 28.977  1.00 16.96 ? 121  VAL   B CG1 1 
ATOM   3093  C  CG2 . VAL   B  1 121 ? 24.367 -46.596 28.274  1.00 18.79 ? 121  VAL   B CG2 1 
ATOM   3094  N  N   . HIS   B  1 122 ? 21.035 -43.609 29.895  1.00 17.30 ? 122  HIS   B N   1 
ATOM   3095  C  CA  . HIS   B  1 122 ? 20.018 -43.087 30.804  1.00 17.59 ? 122  HIS   B CA  1 
ATOM   3096  C  C   . HIS   B  1 122 ? 18.638 -43.628 30.433  1.00 18.12 ? 122  HIS   B C   1 
ATOM   3097  O  O   . HIS   B  1 122 ? 18.356 -43.864 29.244  1.00 18.14 ? 122  HIS   B O   1 
ATOM   3098  C  CB  . HIS   B  1 122 ? 19.945 -41.544 30.766  1.00 19.61 ? 122  HIS   B CB  1 
ATOM   3099  C  CG  . HIS   B  1 122 ? 21.264 -40.844 30.814  1.00 17.84 ? 122  HIS   B CG  1 
ATOM   3100  N  ND1 . HIS   B  1 122 ? 22.138 -40.810 29.739  1.00 17.91 ? 122  HIS   B ND1 1 
ATOM   3101  C  CD2 . HIS   B  1 122 ? 21.843 -40.103 31.804  1.00 19.05 ? 122  HIS   B CD2 1 
ATOM   3102  C  CE1 . HIS   B  1 122 ? 23.208 -40.092 30.084  1.00 17.08 ? 122  HIS   B CE1 1 
ATOM   3103  N  NE2 . HIS   B  1 122 ? 23.051 -39.653 31.324  1.00 20.48 ? 122  HIS   B NE2 1 
ATOM   3104  N  N   . TRP   B  1 123 ? 17.753 -43.764 31.451  1.00 19.11 ? 123  TRP   B N   1 
ATOM   3105  C  CA  . TRP   B  1 123 ? 16.400 -44.264 31.184  1.00 18.68 ? 123  TRP   B CA  1 
ATOM   3106  C  C   . TRP   B  1 123 ? 15.336 -43.326 31.740  1.00 19.13 ? 123  TRP   B C   1 
ATOM   3107  O  O   . TRP   B  1 123 ? 15.491 -42.651 32.772  1.00 20.76 ? 123  TRP   B O   1 
ATOM   3108  C  CB  . TRP   B  1 123 ? 16.184 -45.714 31.707  1.00 17.12 ? 123  TRP   B CB  1 
ATOM   3109  C  CG  . TRP   B  1 123 ? 16.470 -45.853 33.204  1.00 17.89 ? 123  TRP   B CG  1 
ATOM   3110  C  CD1 . TRP   B  1 123 ? 17.678 -46.102 33.802  1.00 17.62 ? 123  TRP   B CD1 1 
ATOM   3111  C  CD2 . TRP   B  1 123 ? 15.511 -45.730 34.279  1.00 19.04 ? 123  TRP   B CD2 1 
ATOM   3112  N  NE1 . TRP   B  1 123 ? 17.521 -46.194 35.180  1.00 18.65 ? 123  TRP   B NE1 1 
ATOM   3113  C  CE2 . TRP   B  1 123 ? 16.202 -45.945 35.486  1.00 18.82 ? 123  TRP   B CE2 1 
ATOM   3114  C  CE3 . TRP   B  1 123 ? 14.127 -45.483 34.322  1.00 19.19 ? 123  TRP   B CE3 1 
ATOM   3115  C  CZ2 . TRP   B  1 123 ? 15.553 -45.917 36.723  1.00 19.41 ? 123  TRP   B CZ2 1 
ATOM   3116  C  CZ3 . TRP   B  1 123 ? 13.489 -45.431 35.534  1.00 20.14 ? 123  TRP   B CZ3 1 
ATOM   3117  C  CH2 . TRP   B  1 123 ? 14.200 -45.660 36.732  1.00 21.42 ? 123  TRP   B CH2 1 
ATOM   3118  N  N   . ASN   B  1 124 ? 14.218 -43.304 31.028  1.00 19.56 ? 124  ASN   B N   1 
ATOM   3119  C  CA  . ASN   B  1 124 ? 13.121 -42.375 31.274  1.00 20.02 ? 124  ASN   B CA  1 
ATOM   3120  C  C   . ASN   B  1 124 ? 12.337 -42.759 32.524  1.00 21.53 ? 124  ASN   B C   1 
ATOM   3121  O  O   . ASN   B  1 124 ? 11.773 -43.857 32.574  1.00 21.85 ? 124  ASN   B O   1 
ATOM   3122  C  CB  . ASN   B  1 124 ? 12.234 -42.398 30.016  1.00 20.43 ? 124  ASN   B CB  1 
ATOM   3123  C  CG  . ASN   B  1 124 ? 11.137 -41.334 30.032  1.00 23.87 ? 124  ASN   B CG  1 
ATOM   3124  O  OD1 . ASN   B  1 124 ? 10.792 -40.759 31.078  1.00 24.27 ? 124  ASN   B OD1 1 
ATOM   3125  N  ND2 . ASN   B  1 124 ? 10.594 -41.046 28.834  1.00 23.67 ? 124  ASN   B ND2 1 
ATOM   3126  N  N   . THR   B  1 125 ? 12.262 -41.843 33.531  1.00 20.22 ? 125  THR   B N   1 
ATOM   3127  C  CA  . THR   B  1 125 ? 11.541 -42.189 34.769  1.00 20.40 ? 125  THR   B CA  1 
ATOM   3128  C  C   . THR   B  1 125 ? 10.028 -42.278 34.572  1.00 23.67 ? 125  THR   B C   1 
ATOM   3129  O  O   . THR   B  1 125 ? 9.297  -42.574 35.537  1.00 29.16 ? 125  THR   B O   1 
ATOM   3130  C  CB  . THR   B  1 125 ? 11.835 -41.182 35.873  1.00 23.92 ? 125  THR   B CB  1 
ATOM   3131  O  OG1 . THR   B  1 125 ? 11.363 -39.882 35.459  1.00 27.94 ? 125  THR   B OG1 1 
ATOM   3132  C  CG2 . THR   B  1 125 ? 13.313 -41.155 36.147  1.00 23.70 ? 125  THR   B CG2 1 
ATOM   3133  N  N   . LYS   B  1 126 ? 9.540  -41.968 33.375  1.00 25.40 ? 126  LYS   B N   1 
ATOM   3134  C  CA  . LYS   B  1 126 ? 8.176  -42.307 32.994  1.00 29.38 ? 126  LYS   B CA  1 
ATOM   3135  C  C   . LYS   B  1 126 ? 7.909  -43.795 33.211  1.00 26.31 ? 126  LYS   B C   1 
ATOM   3136  O  O   . LYS   B  1 126 ? 6.785  -44.197 33.531  1.00 29.28 ? 126  LYS   B O   1 
ATOM   3137  C  CB  . LYS   B  1 126 ? 7.992  -41.876 31.531  1.00 31.68 ? 126  LYS   B CB  1 
ATOM   3138  C  CG  . LYS   B  1 126 ? 6.754  -42.338 30.823  1.00 31.68 ? 126  LYS   B CG  1 
ATOM   3139  C  CD  . LYS   B  1 126 ? 6.715  -41.782 29.381  1.00 31.85 ? 126  LYS   B CD  1 
ATOM   3140  C  CE  . LYS   B  1 126 ? 5.423  -42.272 28.698  1.00 36.04 ? 126  LYS   B CE  1 
ATOM   3141  N  NZ  . LYS   B  1 126 ? 5.305  -41.928 27.258  1.00 34.62 ? 126  LYS   B NZ  1 
ATOM   3142  N  N   . TYR   B  1 127 ? 8.936  -44.619 33.069  1.00 24.06 ? 127  TYR   B N   1 
ATOM   3143  C  CA  . TYR   B  1 127 ? 8.834  -46.067 33.163  1.00 24.35 ? 127  TYR   B CA  1 
ATOM   3144  C  C   . TYR   B  1 127 ? 9.473  -46.501 34.482  1.00 27.82 ? 127  TYR   B C   1 
ATOM   3145  O  O   . TYR   B  1 127 ? 10.127 -45.714 35.167  1.00 28.37 ? 127  TYR   B O   1 
ATOM   3146  C  CB  . TYR   B  1 127 ? 9.488  -46.709 31.910  1.00 20.83 ? 127  TYR   B CB  1 
ATOM   3147  C  CG  . TYR   B  1 127 ? 8.884  -46.157 30.639  1.00 22.02 ? 127  TYR   B CG  1 
ATOM   3148  C  CD1 . TYR   B  1 127 ? 7.557  -46.380 30.359  1.00 22.80 ? 127  TYR   B CD1 1 
ATOM   3149  C  CD2 . TYR   B  1 127 ? 9.627  -45.393 29.723  1.00 20.43 ? 127  TYR   B CD2 1 
ATOM   3150  C  CE1 . TYR   B  1 127 ? 6.963  -45.864 29.251  1.00 22.97 ? 127  TYR   B CE1 1 
ATOM   3151  C  CE2 . TYR   B  1 127 ? 9.040  -44.860 28.589  1.00 20.81 ? 127  TYR   B CE2 1 
ATOM   3152  C  CZ  . TYR   B  1 127 ? 7.692  -45.100 28.346  1.00 25.70 ? 127  TYR   B CZ  1 
ATOM   3153  O  OH  . TYR   B  1 127 ? 7.066  -44.588 27.238  1.00 31.94 ? 127  TYR   B OH  1 
ATOM   3154  N  N   . GLY   B  1 128 ? 9.278  -47.752 34.884  1.00 28.85 ? 128  GLY   B N   1 
ATOM   3155  C  CA  . GLY   B  1 128 ? 9.620  -48.081 36.267  1.00 28.95 ? 128  GLY   B CA  1 
ATOM   3156  C  C   . GLY   B  1 128 ? 11.110 -48.234 36.494  1.00 25.92 ? 128  GLY   B C   1 
ATOM   3157  O  O   . GLY   B  1 128 ? 11.610 -48.039 37.621  1.00 29.93 ? 128  GLY   B O   1 
ATOM   3158  N  N   . ASP   B  1 129 ? 11.824 -48.622 35.459  1.00 22.78 ? 129  ASP   B N   1 
ATOM   3159  C  CA  . ASP   B  1 129 ? 13.235 -48.981 35.579  1.00 22.23 ? 129  ASP   B CA  1 
ATOM   3160  C  C   . ASP   B  1 129 ? 13.761 -49.144 34.155  1.00 20.92 ? 129  ASP   B C   1 
ATOM   3161  O  O   . ASP   B  1 129 ? 13.001 -49.053 33.171  1.00 20.83 ? 129  ASP   B O   1 
ATOM   3162  C  CB  . ASP   B  1 129 ? 13.438 -50.268 36.405  1.00 23.29 ? 129  ASP   B CB  1 
ATOM   3163  C  CG  . ASP   B  1 129 ? 12.553 -51.413 35.931  1.00 28.22 ? 129  ASP   B CG  1 
ATOM   3164  O  OD1 . ASP   B  1 129 ? 12.507 -51.636 34.716  1.00 24.78 ? 129  ASP   B OD1 1 
ATOM   3165  O  OD2 . ASP   B  1 129 ? 11.885 -52.072 36.763  1.00 31.92 ? 129  ASP   B OD2 1 
ATOM   3166  N  N   . PHE   B  1 130 ? 15.054 -49.459 34.065  1.00 19.80 ? 130  PHE   B N   1 
ATOM   3167  C  CA  . PHE   B  1 130 ? 15.710 -49.575 32.771  1.00 19.34 ? 130  PHE   B CA  1 
ATOM   3168  C  C   . PHE   B  1 130 ? 15.040 -50.656 31.920  1.00 18.99 ? 130  PHE   B C   1 
ATOM   3169  O  O   . PHE   B  1 130 ? 14.802 -50.454 30.726  1.00 17.95 ? 130  PHE   B O   1 
ATOM   3170  C  CB  . PHE   B  1 130 ? 17.205 -49.912 32.911  1.00 19.43 ? 130  PHE   B CB  1 
ATOM   3171  C  CG  . PHE   B  1 130 ? 17.888 -50.121 31.570  1.00 17.72 ? 130  PHE   B CG  1 
ATOM   3172  C  CD1 . PHE   B  1 130 ? 17.916 -51.365 30.950  1.00 18.03 ? 130  PHE   B CD1 1 
ATOM   3173  C  CD2 . PHE   B  1 130 ? 18.490 -49.070 30.892  1.00 17.77 ? 130  PHE   B CD2 1 
ATOM   3174  C  CE1 . PHE   B  1 130 ? 18.505 -51.545 29.700  1.00 18.45 ? 130  PHE   B CE1 1 
ATOM   3175  C  CE2 . PHE   B  1 130 ? 19.117 -49.248 29.660  1.00 18.50 ? 130  PHE   B CE2 1 
ATOM   3176  C  CZ  . PHE   B  1 130 ? 19.130 -50.496 29.048  1.00 18.40 ? 130  PHE   B CZ  1 
ATOM   3177  N  N   . GLY   B  1 131 ? 14.737 -51.802 32.532  1.00 19.37 ? 131  GLY   B N   1 
ATOM   3178  C  CA  . GLY   B  1 131 ? 14.164 -52.902 31.757  1.00 17.72 ? 131  GLY   B CA  1 
ATOM   3179  C  C   . GLY   B  1 131 ? 12.831 -52.561 31.129  1.00 19.81 ? 131  GLY   B C   1 
ATOM   3180  O  O   . GLY   B  1 131 ? 12.508 -53.020 30.021  1.00 19.46 ? 131  GLY   B O   1 
ATOM   3181  N  N   . LYS   B  1 132 ? 12.017 -51.773 31.816  1.00 19.00 ? 132  LYS   B N   1 
ATOM   3182  C  CA  . LYS   B  1 132 ? 10.767 -51.337 31.208  1.00 19.72 ? 132  LYS   B CA  1 
ATOM   3183  C  C   . LYS   B  1 132 ? 11.023 -50.277 30.145  1.00 20.95 ? 132  LYS   B C   1 
ATOM   3184  O  O   . LYS   B  1 132 ? 10.401 -50.281 29.067  1.00 19.94 ? 132  LYS   B O   1 
ATOM   3185  C  CB  . LYS   B  1 132 ? 9.830  -50.813 32.301  1.00 20.93 ? 132  LYS   B CB  1 
ATOM   3186  C  CG  . LYS   B  1 132 ? 9.347  -51.936 33.211  1.00 23.26 ? 132  LYS   B CG  1 
ATOM   3187  C  CD  . LYS   B  1 132 ? 8.579  -51.382 34.445  1.00 29.34 ? 132  LYS   B CD  1 
ATOM   3188  C  CE  . LYS   B  1 132 ? 8.088  -52.527 35.281  1.00 34.83 ? 132  LYS   B CE  1 
ATOM   3189  N  NZ  . LYS   B  1 132 ? 9.286  -53.193 35.896  1.00 42.00 ? 132  LYS   B NZ  1 
ATOM   3190  N  N   . ALA   B  1 133 ? 11.938 -49.353 30.426  1.00 19.06 ? 133  ALA   B N   1 
ATOM   3191  C  CA  . ALA   B  1 133 ? 12.165 -48.238 29.514  1.00 17.68 ? 133  ALA   B CA  1 
ATOM   3192  C  C   . ALA   B  1 133 ? 12.713 -48.711 28.169  1.00 19.95 ? 133  ALA   B C   1 
ATOM   3193  O  O   . ALA   B  1 133 ? 12.377 -48.124 27.132  1.00 17.88 ? 133  ALA   B O   1 
ATOM   3194  C  CB  . ALA   B  1 133 ? 13.158 -47.245 30.156  1.00 17.73 ? 133  ALA   B CB  1 
ATOM   3195  N  N   . VAL   B  1 134 ? 13.574 -49.732 28.173  1.00 17.38 ? 134  VAL   B N   1 
ATOM   3196  C  CA  . VAL   B  1 134 ? 14.275 -50.107 26.929  1.00 17.14 ? 134  VAL   B CA  1 
ATOM   3197  C  C   . VAL   B  1 134 ? 13.317 -50.715 25.918  1.00 18.53 ? 134  VAL   B C   1 
ATOM   3198  O  O   . VAL   B  1 134 ? 13.659 -50.842 24.748  1.00 17.88 ? 134  VAL   B O   1 
ATOM   3199  C  CB  . VAL   B  1 134 ? 15.448 -51.047 27.235  1.00 17.51 ? 134  VAL   B CB  1 
ATOM   3200  C  CG1 . VAL   B  1 134 ? 14.940 -52.388 27.728  1.00 17.55 ? 134  VAL   B CG1 1 
ATOM   3201  C  CG2 . VAL   B  1 134 ? 16.361 -51.256 25.992  1.00 16.62 ? 134  VAL   B CG2 1 
ATOM   3202  N  N   . GLN   B  1 135 ? 12.112 -51.038 26.351  1.00 18.87 ? 135  GLN   B N   1 
ATOM   3203  C  CA  . GLN   B  1 135 ? 11.066 -51.535 25.463  1.00 18.21 ? 135  GLN   B CA  1 
ATOM   3204  C  C   . GLN   B  1 135 ? 10.226 -50.428 24.838  1.00 21.33 ? 135  GLN   B C   1 
ATOM   3205  O  O   . GLN   B  1 135 ? 9.259  -50.743 24.122  1.00 25.31 ? 135  GLN   B O   1 
ATOM   3206  C  CB  . GLN   B  1 135 ? 10.158 -52.491 26.216  1.00 19.02 ? 135  GLN   B CB  1 
ATOM   3207  C  CG  . GLN   B  1 135 ? 10.902 -53.729 26.775  1.00 19.60 ? 135  GLN   B CG  1 
ATOM   3208  C  CD  . GLN   B  1 135 ? 11.552 -54.597 25.684  1.00 19.00 ? 135  GLN   B CD  1 
ATOM   3209  O  OE1 . GLN   B  1 135 ? 11.077 -54.644 24.529  1.00 22.64 ? 135  GLN   B OE1 1 
ATOM   3210  N  NE2 . GLN   B  1 135 ? 12.655 -55.259 26.045  1.00 16.96 ? 135  GLN   B NE2 1 
ATOM   3211  N  N   . GLN   B  1 136 ? 10.533 -49.153 25.094  1.00 20.24 ? 136  GLN   B N   1 
ATOM   3212  C  CA  . GLN   B  1 136 ? 9.683  -48.067 24.635  1.00 19.83 ? 136  GLN   B CA  1 
ATOM   3213  C  C   . GLN   B  1 136 ? 10.450 -47.119 23.733  1.00 19.92 ? 136  GLN   B C   1 
ATOM   3214  O  O   . GLN   B  1 136 ? 11.629 -46.859 23.973  1.00 19.61 ? 136  GLN   B O   1 
ATOM   3215  C  CB  . GLN   B  1 136 ? 9.139  -47.281 25.835  1.00 20.96 ? 136  GLN   B CB  1 
ATOM   3216  C  CG  . GLN   B  1 136 ? 8.379  -48.154 26.818  1.00 23.95 ? 136  GLN   B CG  1 
ATOM   3217  C  CD  . GLN   B  1 136 ? 7.085  -48.701 26.220  1.00 30.20 ? 136  GLN   B CD  1 
ATOM   3218  O  OE1 . GLN   B  1 136 ? 6.563  -48.166 25.235  1.00 37.69 ? 136  GLN   B OE1 1 
ATOM   3219  N  NE2 . GLN   B  1 136 ? 6.557  -49.775 26.819  1.00 30.92 ? 136  GLN   B NE2 1 
ATOM   3220  N  N   . PRO   B  1 137 ? 9.817  -46.572 22.697  1.00 20.16 ? 137  PRO   B N   1 
ATOM   3221  C  CA  . PRO   B  1 137 ? 10.559 -45.693 21.780  1.00 21.11 ? 137  PRO   B CA  1 
ATOM   3222  C  C   . PRO   B  1 137 ? 11.169 -44.495 22.461  1.00 22.50 ? 137  PRO   B C   1 
ATOM   3223  O  O   . PRO   B  1 137 ? 12.252 -44.045 22.056  1.00 24.05 ? 137  PRO   B O   1 
ATOM   3224  C  CB  . PRO   B  1 137 ? 9.490  -45.281 20.750  1.00 22.82 ? 137  PRO   B CB  1 
ATOM   3225  C  CG  . PRO   B  1 137 ? 8.534  -46.390 20.743  1.00 27.85 ? 137  PRO   B CG  1 
ATOM   3226  C  CD  . PRO   B  1 137 ? 8.448  -46.845 22.210  1.00 24.71 ? 137  PRO   B CD  1 
ATOM   3227  N  N   . ASP   B  1 138 ? 10.513 -43.955 23.496  1.00 19.72 ? 138  ASP   B N   1 
ATOM   3228  C  CA  . ASP   B  1 138 ? 11.030 -42.827 24.252  1.00 19.90 ? 138  ASP   B CA  1 
ATOM   3229  C  C   . ASP   B  1 138 ? 11.716 -43.270 25.544  1.00 18.64 ? 138  ASP   B C   1 
ATOM   3230  O  O   . ASP   B  1 138 ? 11.854 -42.479 26.489  1.00 20.75 ? 138  ASP   B O   1 
ATOM   3231  C  CB  . ASP   B  1 138 ? 9.908  -41.829 24.569  1.00 21.22 ? 138  ASP   B CB  1 
ATOM   3232  C  CG  . ASP   B  1 138 ? 8.789  -42.434 25.388  1.00 25.10 ? 138  ASP   B CG  1 
ATOM   3233  O  OD1 . ASP   B  1 138 ? 8.750  -43.653 25.581  1.00 25.16 ? 138  ASP   B OD1 1 
ATOM   3234  O  OD2 . ASP   B  1 138 ? 7.904  -41.659 25.850  1.00 27.87 ? 138  ASP   B OD2 1 
ATOM   3235  N  N   . GLY   B  1 139 ? 12.153 -44.520 25.599  1.00 19.53 ? 139  GLY   B N   1 
ATOM   3236  C  CA  . GLY   B  1 139 ? 12.611 -45.072 26.871  1.00 18.42 ? 139  GLY   B CA  1 
ATOM   3237  C  C   . GLY   B  1 139 ? 14.007 -44.653 27.300  1.00 18.75 ? 139  GLY   B C   1 
ATOM   3238  O  O   . GLY   B  1 139 ? 14.241 -44.528 28.506  1.00 18.45 ? 139  GLY   B O   1 
ATOM   3239  N  N   . LEU   B  1 140 ? 14.954 -44.533 26.361  1.00 18.57 ? 140  LEU   B N   1 
ATOM   3240  C  CA  . LEU   B  1 140 ? 16.357 -44.330 26.707  1.00 16.20 ? 140  LEU   B CA  1 
ATOM   3241  C  C   . LEU   B  1 140 ? 16.908 -43.076 26.052  1.00 18.04 ? 140  LEU   B C   1 
ATOM   3242  O  O   . LEU   B  1 140 ? 16.432 -42.638 24.999  1.00 18.72 ? 140  LEU   B O   1 
ATOM   3243  C  CB  . LEU   B  1 140 ? 17.232 -45.514 26.269  1.00 17.37 ? 140  LEU   B CB  1 
ATOM   3244  C  CG  . LEU   B  1 140 ? 16.814 -46.899 26.812  1.00 18.12 ? 140  LEU   B CG  1 
ATOM   3245  C  CD1 . LEU   B  1 140 ? 17.859 -47.906 26.305  1.00 18.34 ? 140  LEU   B CD1 1 
ATOM   3246  C  CD2 . LEU   B  1 140 ? 16.752 -46.942 28.371  1.00 19.00 ? 140  LEU   B CD2 1 
ATOM   3247  N  N   . ALA   B  1 141 ? 17.957 -42.526 26.682  1.00 17.51 ? 141  ALA   B N   1 
ATOM   3248  C  CA  . ALA   B  1 141 ? 18.750 -41.440 26.108  1.00 18.50 ? 141  ALA   B CA  1 
ATOM   3249  C  C   . ALA   B  1 141 ? 20.202 -41.805 26.328  1.00 18.66 ? 141  ALA   B C   1 
ATOM   3250  O  O   . ALA   B  1 141 ? 20.599 -42.072 27.462  1.00 19.39 ? 141  ALA   B O   1 
ATOM   3251  C  CB  . ALA   B  1 141 ? 18.428 -40.096 26.760  1.00 19.98 ? 141  ALA   B CB  1 
ATOM   3252  N  N   . VAL   B  1 142 ? 20.990 -41.848 25.260  1.00 17.46 ? 142  VAL   B N   1 
ATOM   3253  C  CA  . VAL   B  1 142 ? 22.402 -42.174 25.375  1.00 17.21 ? 142  VAL   B CA  1 
ATOM   3254  C  C   . VAL   B  1 142 ? 23.192 -40.947 24.934  1.00 17.80 ? 142  VAL   B C   1 
ATOM   3255  O  O   . VAL   B  1 142 ? 22.960 -40.393 23.838  1.00 18.90 ? 142  VAL   B O   1 
ATOM   3256  C  CB  . VAL   B  1 142 ? 22.825 -43.424 24.587  1.00 16.31 ? 142  VAL   B CB  1 
ATOM   3257  C  CG1 . VAL   B  1 142 ? 24.344 -43.673 24.834  1.00 17.76 ? 142  VAL   B CG1 1 
ATOM   3258  C  CG2 . VAL   B  1 142 ? 22.066 -44.666 25.059  1.00 17.35 ? 142  VAL   B CG2 1 
ATOM   3259  N  N   . LEU   B  1 143 ? 24.053 -40.482 25.828  1.00 19.60 ? 143  LEU   B N   1 
ATOM   3260  C  CA  . LEU   B  1 143 ? 24.948 -39.366 25.574  1.00 20.04 ? 143  LEU   B CA  1 
ATOM   3261  C  C   . LEU   B  1 143 ? 26.244 -39.969 25.054  1.00 19.89 ? 143  LEU   B C   1 
ATOM   3262  O  O   . LEU   B  1 143 ? 26.904 -40.749 25.778  1.00 19.06 ? 143  LEU   B O   1 
ATOM   3263  C  CB  . LEU   B  1 143 ? 25.141 -38.565 26.864  1.00 20.16 ? 143  LEU   B CB  1 
ATOM   3264  C  CG  . LEU   B  1 143 ? 26.022 -37.338 26.771  1.00 21.58 ? 143  LEU   B CG  1 
ATOM   3265  C  CD1 . LEU   B  1 143 ? 25.459 -36.284 25.796  1.00 22.84 ? 143  LEU   B CD1 1 
ATOM   3266  C  CD2 . LEU   B  1 143 ? 26.136 -36.736 28.193  1.00 22.06 ? 143  LEU   B CD2 1 
ATOM   3267  N  N   . GLY   B  1 144 ? 26.556 -39.703 23.786  1.00 18.33 ? 144  GLY   B N   1 
ATOM   3268  C  CA  . GLY   B  1 144 ? 27.729 -40.276 23.142  1.00 19.81 ? 144  GLY   B CA  1 
ATOM   3269  C  C   . GLY   B  1 144 ? 28.812 -39.221 23.015  1.00 20.20 ? 144  GLY   B C   1 
ATOM   3270  O  O   . GLY   B  1 144 ? 28.538 -38.082 22.653  1.00 20.37 ? 144  GLY   B O   1 
ATOM   3271  N  N   . ILE   B  1 145 ? 30.028 -39.607 23.388  1.00 18.13 ? 145  ILE   B N   1 
ATOM   3272  C  CA  . ILE   B  1 145 ? 31.174 -38.696 23.428  1.00 20.21 ? 145  ILE   B CA  1 
ATOM   3273  C  C   . ILE   B  1 145 ? 32.366 -39.361 22.747  1.00 20.09 ? 145  ILE   B C   1 
ATOM   3274  O  O   . ILE   B  1 145 ? 32.716 -40.501 23.074  1.00 20.80 ? 145  ILE   B O   1 
ATOM   3275  C  CB  . ILE   B  1 145 ? 31.529 -38.322 24.880  1.00 21.32 ? 145  ILE   B CB  1 
ATOM   3276  C  CG1 . ILE   B  1 145 ? 30.299 -37.691 25.553  1.00 23.19 ? 145  ILE   B CG1 1 
ATOM   3277  C  CG2 . ILE   B  1 145 ? 32.764 -37.398 24.897  1.00 21.69 ? 145  ILE   B CG2 1 
ATOM   3278  C  CD1 . ILE   B  1 145 ? 30.481 -37.292 27.022  1.00 24.54 ? 145  ILE   B CD1 1 
ATOM   3279  N  N   . PHE   B  1 146 ? 32.979 -38.661 21.793  1.00 19.24 ? 146  PHE   B N   1 
ATOM   3280  C  CA  . PHE   B  1 146 ? 34.129 -39.201 21.073  1.00 19.62 ? 146  PHE   B CA  1 
ATOM   3281  C  C   . PHE   B  1 146 ? 35.417 -39.034 21.868  1.00 22.57 ? 146  PHE   B C   1 
ATOM   3282  O  O   . PHE   B  1 146 ? 35.595 -38.032 22.566  1.00 22.44 ? 146  PHE   B O   1 
ATOM   3283  C  CB  . PHE   B  1 146 ? 34.297 -38.511 19.714  1.00 19.14 ? 146  PHE   B CB  1 
ATOM   3284  C  CG  . PHE   B  1 146 ? 33.140 -38.723 18.774  1.00 19.37 ? 146  PHE   B CG  1 
ATOM   3285  C  CD1 . PHE   B  1 146 ? 32.815 -39.990 18.308  1.00 19.40 ? 146  PHE   B CD1 1 
ATOM   3286  C  CD2 . PHE   B  1 146 ? 32.381 -37.652 18.375  1.00 20.24 ? 146  PHE   B CD2 1 
ATOM   3287  C  CE1 . PHE   B  1 146 ? 31.736 -40.196 17.430  1.00 20.86 ? 146  PHE   B CE1 1 
ATOM   3288  C  CE2 . PHE   B  1 146 ? 31.294 -37.801 17.506  1.00 21.02 ? 146  PHE   B CE2 1 
ATOM   3289  C  CZ  . PHE   B  1 146 ? 30.964 -39.101 16.998  1.00 21.45 ? 146  PHE   B CZ  1 
ATOM   3290  N  N   . LEU   B  1 147 ? 36.321 -40.019 21.748  1.00 20.94 ? 147  LEU   B N   1 
ATOM   3291  C  CA  . LEU   B  1 147 ? 37.659 -39.968 22.344  1.00 22.27 ? 147  LEU   B CA  1 
ATOM   3292  C  C   . LEU   B  1 147 ? 38.674 -39.805 21.224  1.00 22.07 ? 147  LEU   B C   1 
ATOM   3293  O  O   . LEU   B  1 147 ? 38.776 -40.677 20.339  1.00 23.73 ? 147  LEU   B O   1 
ATOM   3294  C  CB  . LEU   B  1 147 ? 37.984 -41.230 23.140  1.00 22.52 ? 147  LEU   B CB  1 
ATOM   3295  C  CG  . LEU   B  1 147 ? 37.413 -41.324 24.558  1.00 21.25 ? 147  LEU   B CG  1 
ATOM   3296  C  CD1 . LEU   B  1 147 ? 35.884 -41.373 24.600  1.00 21.29 ? 147  LEU   B CD1 1 
ATOM   3297  C  CD2 . LEU   B  1 147 ? 37.997 -42.520 25.355  1.00 21.55 ? 147  LEU   B CD2 1 
ATOM   3298  N  N   . LYS   B  1 148 ? 39.433 -38.725 21.286  1.00 23.53 ? 148  LYS   B N   1 
ATOM   3299  C  CA  . LYS   B  1 148 ? 40.474 -38.431 20.325  1.00 26.83 ? 148  LYS   B CA  1 
ATOM   3300  C  C   . LYS   B  1 148 ? 41.823 -38.610 20.997  1.00 29.88 ? 148  LYS   B C   1 
ATOM   3301  O  O   . LYS   B  1 148 ? 42.015 -38.170 22.134  1.00 33.09 ? 148  LYS   B O   1 
ATOM   3302  C  CB  . LYS   B  1 148 ? 40.309 -36.989 19.833  1.00 32.42 ? 148  LYS   B CB  1 
ATOM   3303  C  CG  . LYS   B  1 148 ? 41.318 -36.527 18.856  1.00 39.29 ? 148  LYS   B CG  1 
ATOM   3304  C  CD  . LYS   B  1 148 ? 41.078 -35.039 18.559  1.00 44.36 ? 148  LYS   B CD  1 
ATOM   3305  C  CE  . LYS   B  1 148 ? 42.024 -34.545 17.462  1.00 48.72 ? 148  LYS   B CE  1 
ATOM   3306  N  NZ  . LYS   B  1 148 ? 41.666 -33.167 17.018  1.00 52.95 ? 148  LYS   B NZ  1 
ATOM   3307  N  N   . VAL   B  1 149 ? 42.771 -39.214 20.285  1.00 28.44 ? 149  VAL   B N   1 
ATOM   3308  C  CA  . VAL   B  1 149 ? 44.108 -39.441 20.837  1.00 32.13 ? 149  VAL   B CA  1 
ATOM   3309  C  C   . VAL   B  1 149 ? 44.871 -38.123 20.947  1.00 31.58 ? 149  VAL   B C   1 
ATOM   3310  O  O   . VAL   B  1 149 ? 44.941 -37.330 19.993  1.00 34.68 ? 149  VAL   B O   1 
ATOM   3311  C  CB  . VAL   B  1 149 ? 44.886 -40.455 19.986  1.00 36.28 ? 149  VAL   B CB  1 
ATOM   3312  C  CG1 . VAL   B  1 149 ? 46.347 -40.489 20.424  1.00 36.53 ? 149  VAL   B CG1 1 
ATOM   3313  C  CG2 . VAL   B  1 149 ? 44.284 -41.832 20.132  1.00 35.95 ? 149  VAL   B CG2 1 
ATOM   3314  N  N   . GLY   B  1 150 ? 45.447 -37.884 22.117  1.00 31.07 ? 150  GLY   B N   1 
ATOM   3315  C  CA  . GLY   B  1 150 ? 46.187 -36.675 22.386  1.00 31.90 ? 150  GLY   B CA  1 
ATOM   3316  C  C   . GLY   B  1 150 ? 46.733 -36.754 23.788  1.00 31.93 ? 150  GLY   B C   1 
ATOM   3317  O  O   . GLY   B  1 150 ? 47.321 -37.779 24.143  1.00 32.31 ? 150  GLY   B O   1 
ATOM   3318  N  N   . SER   B  1 151 ? 46.565 -35.690 24.582  1.00 32.95 ? 151  SER   B N   1 
ATOM   3319  C  CA  . SER   B  1 151 ? 47.007 -35.695 25.969  1.00 31.45 ? 151  SER   B CA  1 
ATOM   3320  C  C   . SER   B  1 151 ? 46.162 -36.646 26.816  1.00 30.31 ? 151  SER   B C   1 
ATOM   3321  O  O   . SER   B  1 151 ? 44.999 -36.907 26.512  1.00 32.84 ? 151  SER   B O   1 
ATOM   3322  C  CB  . SER   B  1 151 ? 46.910 -34.300 26.548  1.00 35.51 ? 151  SER   B CB  1 
ATOM   3323  O  OG  . SER   B  1 151 ? 47.848 -33.448 25.923  1.00 43.50 ? 151  SER   B OG  1 
ATOM   3324  N  N   . ALA   B  1 152 ? 46.773 -37.174 27.876  1.00 33.75 ? 152  ALA   B N   1 
ATOM   3325  C  CA  . ALA   B  1 152 ? 46.064 -38.060 28.796  1.00 33.16 ? 152  ALA   B CA  1 
ATOM   3326  C  C   . ALA   B  1 152 ? 44.945 -37.296 29.497  1.00 34.18 ? 152  ALA   B C   1 
ATOM   3327  O  O   . ALA   B  1 152 ? 45.087 -36.105 29.803  1.00 35.64 ? 152  ALA   B O   1 
ATOM   3328  C  CB  . ALA   B  1 152 ? 47.046 -38.636 29.829  1.00 31.66 ? 152  ALA   B CB  1 
ATOM   3329  N  N   . LEU   B  1 153 ? 43.821 -37.987 29.743  1.00 30.31 ? 153  LEU   B N   1 
ATOM   3330  C  CA  . LEU   B  1 153 ? 42.684 -37.392 30.420  1.00 27.83 ? 153  LEU   B CA  1 
ATOM   3331  C  C   . LEU   B  1 153 ? 42.722 -37.783 31.884  1.00 26.27 ? 153  LEU   B C   1 
ATOM   3332  O  O   . LEU   B  1 153 ? 42.568 -38.978 32.196  1.00 26.49 ? 153  LEU   B O   1 
ATOM   3333  C  CB  . LEU   B  1 153 ? 41.374 -37.862 29.783  1.00 28.09 ? 153  LEU   B CB  1 
ATOM   3334  C  CG  . LEU   B  1 153 ? 40.094 -37.160 30.264  1.00 30.24 ? 153  LEU   B CG  1 
ATOM   3335  C  CD1 . LEU   B  1 153 ? 40.105 -35.646 29.937  1.00 31.40 ? 153  LEU   B CD1 1 
ATOM   3336  C  CD2 . LEU   B  1 153 ? 38.848 -37.802 29.692  1.00 28.27 ? 153  LEU   B CD2 1 
ATOM   3337  N  N   . PRO   B  1 154 ? 42.885 -36.851 32.806  1.00 28.02 ? 154  PRO   B N   1 
ATOM   3338  C  CA  . PRO   B  1 154 ? 42.984 -37.260 34.218  1.00 29.50 ? 154  PRO   B CA  1 
ATOM   3339  C  C   . PRO   B  1 154 ? 41.713 -37.908 34.712  1.00 28.62 ? 154  PRO   B C   1 
ATOM   3340  O  O   . PRO   B  1 154 ? 41.783 -38.804 35.563  1.00 31.32 ? 154  PRO   B O   1 
ATOM   3341  C  CB  . PRO   B  1 154 ? 43.297 -35.934 34.948  1.00 32.03 ? 154  PRO   B CB  1 
ATOM   3342  C  CG  . PRO   B  1 154 ? 43.923 -35.050 33.861  1.00 34.06 ? 154  PRO   B CG  1 
ATOM   3343  C  CD  . PRO   B  1 154 ? 43.162 -35.415 32.605  1.00 31.58 ? 154  PRO   B CD  1 
ATOM   3344  N  N   . GLY   B  1 155 ? 40.553 -37.495 34.187  1.00 28.35 ? 155  GLY   B N   1 
ATOM   3345  C  CA  . GLY   B  1 155 ? 39.275 -38.044 34.596  1.00 28.07 ? 155  GLY   B CA  1 
ATOM   3346  C  C   . GLY   B  1 155 ? 39.054 -39.480 34.197  1.00 26.51 ? 155  GLY   B C   1 
ATOM   3347  O  O   . GLY   B  1 155 ? 38.115 -40.108 34.697  1.00 27.99 ? 155  GLY   B O   1 
ATOM   3348  N  N   . LEU   B  1 156 ? 39.873 -39.998 33.291  1.00 24.89 ? 156  LEU   B N   1 
ATOM   3349  C  CA  . LEU   B  1 156 ? 39.795 -41.385 32.865  1.00 23.94 ? 156  LEU   B CA  1 
ATOM   3350  C  C   . LEU   B  1 156 ? 40.726 -42.287 33.674  1.00 24.61 ? 156  LEU   B C   1 
ATOM   3351  O  O   . LEU   B  1 156 ? 40.597 -43.519 33.630  1.00 23.78 ? 156  LEU   B O   1 
ATOM   3352  C  CB  . LEU   B  1 156 ? 40.132 -41.458 31.359  1.00 24.10 ? 156  LEU   B CB  1 
ATOM   3353  C  CG  . LEU   B  1 156 ? 39.992 -42.814 30.650  1.00 24.97 ? 156  LEU   B CG  1 
ATOM   3354  C  CD1 . LEU   B  1 156 ? 38.564 -43.351 30.715  1.00 22.57 ? 156  LEU   B CD1 1 
ATOM   3355  C  CD2 . LEU   B  1 156 ? 40.482 -42.693 29.212  1.00 25.99 ? 156  LEU   B CD2 1 
ATOM   3356  N  N   . GLN   B  1 157 ? 41.642 -41.717 34.454  1.00 24.62 ? 157  GLN   B N   1 
ATOM   3357  C  CA  . GLN   B  1 157 ? 42.712 -42.540 35.001  1.00 24.87 ? 157  GLN   B CA  1 
ATOM   3358  C  C   . GLN   B  1 157 ? 42.176 -43.565 36.006  1.00 26.57 ? 157  GLN   B C   1 
ATOM   3359  O  O   . GLN   B  1 157 ? 42.639 -44.703 36.018  1.00 25.56 ? 157  GLN   B O   1 
ATOM   3360  C  CB  . GLN   B  1 157 ? 43.814 -41.663 35.625  1.00 29.03 ? 157  GLN   B CB  1 
ATOM   3361  C  CG  . GLN   B  1 157 ? 45.150 -42.430 35.774  1.00 33.16 ? 157  GLN   B CG  1 
ATOM   3362  C  CD  . GLN   B  1 157 ? 45.653 -43.082 34.447  1.00 37.19 ? 157  GLN   B CD  1 
ATOM   3363  O  OE1 . GLN   B  1 157 ? 45.623 -42.478 33.365  1.00 36.70 ? 157  GLN   B OE1 1 
ATOM   3364  N  NE2 . GLN   B  1 157 ? 46.172 -44.287 34.553  1.00 35.47 ? 157  GLN   B NE2 1 
ATOM   3365  N  N   . LYS   B  1 158 ? 41.144 -43.227 36.784  1.00 25.90 ? 158  LYS   B N   1 
ATOM   3366  C  CA  . LYS   B  1 158 ? 40.613 -44.208 37.733  1.00 26.89 ? 158  LYS   B CA  1 
ATOM   3367  C  C   . LYS   B  1 158 ? 40.018 -45.411 37.019  1.00 24.05 ? 158  LYS   B C   1 
ATOM   3368  O  O   . LYS   B  1 158 ? 40.107 -46.547 37.501  1.00 26.21 ? 158  LYS   B O   1 
ATOM   3369  C  CB  . LYS   B  1 158 ? 39.559 -43.563 38.629  1.00 29.47 ? 158  LYS   B CB  1 
ATOM   3370  C  CG  . LYS   B  1 158 ? 39.103 -44.467 39.777  1.00 32.13 ? 158  LYS   B CG  1 
ATOM   3371  C  CD  . LYS   B  1 158 ? 37.856 -43.918 40.446  1.00 33.00 ? 158  LYS   B CD  1 
ATOM   3372  C  CE  . LYS   B  1 158 ? 37.303 -44.908 41.524  1.00 32.56 ? 158  LYS   B CE  1 
ATOM   3373  N  NZ  . LYS   B  1 158 ? 37.986 -44.586 42.770  1.00 34.49 ? 158  LYS   B NZ  1 
ATOM   3374  N  N   . VAL   B  1 159 ? 39.396 -45.180 35.857  1.00 21.55 ? 159  VAL   B N   1 
ATOM   3375  C  CA  . VAL   B  1 159 ? 38.875 -46.291 35.075  1.00 20.14 ? 159  VAL   B CA  1 
ATOM   3376  C  C   . VAL   B  1 159 ? 40.012 -47.177 34.605  1.00 23.44 ? 159  VAL   B C   1 
ATOM   3377  O  O   . VAL   B  1 159 ? 40.014 -48.401 34.810  1.00 24.28 ? 159  VAL   B O   1 
ATOM   3378  C  CB  . VAL   B  1 159 ? 38.086 -45.752 33.880  1.00 20.91 ? 159  VAL   B CB  1 
ATOM   3379  C  CG1 . VAL   B  1 159 ? 37.702 -46.913 32.951  1.00 21.18 ? 159  VAL   B CG1 1 
ATOM   3380  C  CG2 . VAL   B  1 159 ? 36.799 -44.974 34.307  1.00 22.85 ? 159  VAL   B CG2 1 
ATOM   3381  N  N   . VAL   B  1 160 ? 40.994 -46.573 33.920  1.00 24.67 ? 160  VAL   B N   1 
ATOM   3382  C  CA  A VAL   B  1 160 ? 42.103 -47.334 33.339  0.43 27.01 ? 160  VAL   B CA  1 
ATOM   3383  C  CA  B VAL   B  1 160 ? 41.992 -47.450 33.333  0.57 26.92 ? 160  VAL   B CA  1 
ATOM   3384  C  C   . VAL   B  1 160 ? 42.787 -48.184 34.399  1.00 28.10 ? 160  VAL   B C   1 
ATOM   3385  O  O   . VAL   B  1 160 ? 43.187 -49.332 34.162  1.00 30.23 ? 160  VAL   B O   1 
ATOM   3386  C  CB  A VAL   B  1 160 ? 43.094 -46.367 32.659  0.43 30.67 ? 160  VAL   B CB  1 
ATOM   3387  C  CB  B VAL   B  1 160 ? 42.886 -46.693 32.344  0.57 30.35 ? 160  VAL   B CB  1 
ATOM   3388  C  CG1 A VAL   B  1 160 ? 44.483 -46.971 32.618  0.43 31.87 ? 160  VAL   B CG1 1 
ATOM   3389  C  CG1 B VAL   B  1 160 ? 42.062 -46.350 31.109  0.57 30.57 ? 160  VAL   B CG1 1 
ATOM   3390  C  CG2 A VAL   B  1 160 ? 42.616 -46.027 31.264  0.43 31.41 ? 160  VAL   B CG2 1 
ATOM   3391  C  CG2 B VAL   B  1 160 ? 43.464 -45.475 32.998  0.57 30.61 ? 160  VAL   B CG2 1 
ATOM   3392  N  N   . ASP   B  1 161 ? 42.934 -47.625 35.598  1.00 27.61 ? 161  ASP   B N   1 
ATOM   3393  C  CA  . ASP   B  1 161 ? 43.708 -48.257 36.660  1.00 31.26 ? 161  ASP   B CA  1 
ATOM   3394  C  C   . ASP   B  1 161 ? 43.067 -49.536 37.185  1.00 30.25 ? 161  ASP   B C   1 
ATOM   3395  O  O   . ASP   B  1 161 ? 43.783 -50.369 37.764  1.00 38.83 ? 161  ASP   B O   1 
ATOM   3396  C  CB  . ASP   B  1 161 ? 43.896 -47.298 37.843  1.00 33.37 ? 161  ASP   B CB  1 
ATOM   3397  C  CG  . ASP   B  1 161 ? 44.933 -46.188 37.567  1.00 35.21 ? 161  ASP   B CG  1 
ATOM   3398  O  OD1 . ASP   B  1 161 ? 45.685 -46.292 36.565  1.00 36.77 ? 161  ASP   B OD1 1 
ATOM   3399  O  OD2 . ASP   B  1 161 ? 44.996 -45.227 38.377  1.00 38.29 ? 161  ASP   B OD2 1 
ATOM   3400  N  N   . VAL   B  1 162 ? 41.740 -49.700 37.038  1.00 25.63 ? 162  VAL   B N   1 
ATOM   3401  C  CA  . VAL   B  1 162 ? 41.034 -50.860 37.597  1.00 26.16 ? 162  VAL   B CA  1 
ATOM   3402  C  C   . VAL   B  1 162 ? 40.871 -51.980 36.573  1.00 24.85 ? 162  VAL   B C   1 
ATOM   3403  O  O   . VAL   B  1 162 ? 40.539 -53.107 36.953  1.00 26.06 ? 162  VAL   B O   1 
ATOM   3404  C  CB  . VAL   B  1 162 ? 39.638 -50.443 38.127  1.00 25.42 ? 162  VAL   B CB  1 
ATOM   3405  C  CG1 . VAL   B  1 162 ? 38.637 -50.326 37.025  1.00 26.06 ? 162  VAL   B CG1 1 
ATOM   3406  C  CG2 . VAL   B  1 162 ? 39.143 -51.375 39.260  1.00 28.85 ? 162  VAL   B CG2 1 
ATOM   3407  N  N   . LEU   B  1 163 ? 41.188 -51.726 35.302  1.00 23.55 ? 163  LEU   B N   1 
ATOM   3408  C  CA  . LEU   B  1 163 ? 40.823 -52.714 34.286  1.00 22.83 ? 163  LEU   B CA  1 
ATOM   3409  C  C   . LEU   B  1 163 ? 41.595 -54.027 34.444  1.00 27.25 ? 163  LEU   B C   1 
ATOM   3410  O  O   . LEU   B  1 163 ? 41.066 -55.095 34.081  1.00 24.90 ? 163  LEU   B O   1 
ATOM   3411  C  CB  . LEU   B  1 163 ? 41.027 -52.115 32.900  1.00 22.55 ? 163  LEU   B CB  1 
ATOM   3412  C  CG  . LEU   B  1 163 ? 40.092 -50.909 32.717  1.00 24.65 ? 163  LEU   B CG  1 
ATOM   3413  C  CD1 . LEU   B  1 163 ? 40.304 -50.367 31.350  1.00 31.51 ? 163  LEU   B CD1 1 
ATOM   3414  C  CD2 . LEU   B  1 163 ? 38.651 -51.305 32.778  1.00 21.09 ? 163  LEU   B CD2 1 
ATOM   3415  N  N   . ASP   B  1 164 ? 42.843 -53.991 34.943  1.00 30.51 ? 164  ASP   B N   1 
ATOM   3416  C  CA  . ASP   B  1 164 ? 43.574 -55.249 35.084  1.00 32.05 ? 164  ASP   B CA  1 
ATOM   3417  C  C   . ASP   B  1 164 ? 42.922 -56.180 36.095  1.00 31.11 ? 164  ASP   B C   1 
ATOM   3418  O  O   . ASP   B  1 164 ? 43.219 -57.381 36.100  1.00 32.96 ? 164  ASP   B O   1 
ATOM   3419  C  CB  . ASP   B  1 164 ? 45.036 -54.995 35.490  1.00 44.14 ? 164  ASP   B CB  1 
ATOM   3420  C  CG  . ASP   B  1 164 ? 45.939 -54.701 34.283  1.00 54.84 ? 164  ASP   B CG  1 
ATOM   3421  O  OD1 . ASP   B  1 164 ? 45.565 -55.057 33.133  1.00 56.13 ? 164  ASP   B OD1 1 
ATOM   3422  O  OD2 . ASP   B  1 164 ? 47.013 -54.083 34.474  1.00 59.56 ? 164  ASP   B OD2 1 
ATOM   3423  N  N   . SER   B  1 165 ? 42.014 -55.666 36.920  1.00 27.68 ? 165  SER   B N   1 
ATOM   3424  C  CA  . SER   B  1 165 ? 41.302 -56.499 37.864  1.00 26.57 ? 165  SER   B CA  1 
ATOM   3425  C  C   . SER   B  1 165 ? 40.026 -57.119 37.290  1.00 24.08 ? 165  SER   B C   1 
ATOM   3426  O  O   . SER   B  1 165 ? 39.408 -57.960 37.976  1.00 27.96 ? 165  SER   B O   1 
ATOM   3427  C  CB  . SER   B  1 165 ? 40.981 -55.716 39.146  1.00 33.50 ? 165  SER   B CB  1 
ATOM   3428  O  OG  . SER   B  1 165 ? 39.914 -54.814 38.946  1.00 34.13 ? 165  SER   B OG  1 
ATOM   3429  N  N   . ILE   B  1 166 ? 39.618 -56.762 36.061  1.00 22.15 ? 166  ILE   B N   1 
ATOM   3430  C  CA  . ILE   B  1 166 ? 38.402 -57.349 35.489  1.00 20.53 ? 166  ILE   B CA  1 
ATOM   3431  C  C   . ILE   B  1 166 ? 38.682 -57.870 34.078  1.00 20.43 ? 166  ILE   B C   1 
ATOM   3432  O  O   . ILE   B  1 166 ? 37.932 -57.574 33.142  1.00 18.22 ? 166  ILE   B O   1 
ATOM   3433  C  CB  . ILE   B  1 166 ? 37.239 -56.340 35.500  1.00 17.93 ? 166  ILE   B CB  1 
ATOM   3434  C  CG1 . ILE   B  1 166 ? 37.618 -55.016 34.812  1.00 17.31 ? 166  ILE   B CG1 1 
ATOM   3435  C  CG2 . ILE   B  1 166 ? 36.830 -56.060 36.962  1.00 21.23 ? 166  ILE   B CG2 1 
ATOM   3436  C  CD1 . ILE   B  1 166 ? 36.372 -54.300 34.293  1.00 18.44 ? 166  ILE   B CD1 1 
ATOM   3437  N  N   . LYS   B  1 167 ? 39.749 -58.662 33.918  1.00 21.08 ? 167  LYS   B N   1 
ATOM   3438  C  CA  . LYS   B  1 167 ? 40.269 -58.932 32.585  1.00 21.31 ? 167  LYS   B CA  1 
ATOM   3439  C  C   . LYS   B  1 167 ? 39.302 -59.781 31.766  1.00 21.41 ? 167  LYS   B C   1 
ATOM   3440  O  O   . LYS   B  1 167 ? 39.250 -59.635 30.553  1.00 21.62 ? 167  LYS   B O   1 
ATOM   3441  C  CB  . LYS   B  1 167 ? 41.648 -59.639 32.680  1.00 22.96 ? 167  LYS   B CB  1 
ATOM   3442  C  CG  . LYS   B  1 167 ? 42.291 -60.018 31.328  1.00 29.12 ? 167  LYS   B CG  1 
ATOM   3443  C  CD  . LYS   B  1 167 ? 43.648 -60.740 31.579  1.00 32.85 ? 167  LYS   B CD  1 
ATOM   3444  C  CE  . LYS   B  1 167 ? 44.291 -61.235 30.295  1.00 41.61 ? 167  LYS   B CE  1 
ATOM   3445  N  NZ  . LYS   B  1 167 ? 44.656 -60.159 29.363  1.00 51.24 ? 167  LYS   B NZ  1 
ATOM   3446  N  N   . THR   B  1 168 ? 38.587 -60.723 32.400  1.00 20.61 ? 168  THR   B N   1 
ATOM   3447  C  CA  . THR   B  1 168 ? 37.773 -61.683 31.661  1.00 18.98 ? 168  THR   B CA  1 
ATOM   3448  C  C   . THR   B  1 168 ? 36.285 -61.537 31.962  1.00 19.73 ? 168  THR   B C   1 
ATOM   3449  O  O   . THR   B  1 168 ? 35.863 -60.915 32.955  1.00 19.38 ? 168  THR   B O   1 
ATOM   3450  C  CB  . THR   B  1 168 ? 38.245 -63.132 31.965  1.00 20.99 ? 168  THR   B CB  1 
ATOM   3451  O  OG1 . THR   B  1 168 ? 38.304 -63.314 33.378  1.00 22.97 ? 168  THR   B OG1 1 
ATOM   3452  C  CG2 . THR   B  1 168 ? 39.629 -63.348 31.395  1.00 24.21 ? 168  THR   B CG2 1 
ATOM   3453  N  N   . LYS   B  1 169 ? 35.481 -62.131 31.071  1.00 19.37 ? 169  LYS   B N   1 
ATOM   3454  C  CA  . LYS   B  1 169 ? 34.034 -61.996 31.171  1.00 19.52 ? 169  LYS   B CA  1 
ATOM   3455  C  C   . LYS   B  1 169 ? 33.519 -62.385 32.560  1.00 19.72 ? 169  LYS   B C   1 
ATOM   3456  O  O   . LYS   B  1 169 ? 33.837 -63.467 33.087  1.00 20.75 ? 169  LYS   B O   1 
ATOM   3457  C  CB  . LYS   B  1 169 ? 33.335 -62.889 30.122  1.00 18.68 ? 169  LYS   B CB  1 
ATOM   3458  C  CG  . LYS   B  1 169 ? 31.824 -62.745 30.176  1.00 18.12 ? 169  LYS   B CG  1 
ATOM   3459  C  CD  . LYS   B  1 169 ? 31.161 -63.583 29.065  1.00 18.25 ? 169  LYS   B CD  1 
ATOM   3460  C  CE  . LYS   B  1 169 ? 29.634 -63.436 29.171  1.00 21.72 ? 169  LYS   B CE  1 
ATOM   3461  N  NZ  . LYS   B  1 169 ? 28.953 -64.119 27.983  1.00 25.51 ? 169  LYS   B NZ  1 
ATOM   3462  N  N   . GLY   B  1 170 ? 32.644 -61.545 33.093  1.00 19.07 ? 170  GLY   B N   1 
ATOM   3463  C  CA  . GLY   B  1 170 ? 31.983 -61.827 34.338  1.00 19.71 ? 170  GLY   B CA  1 
ATOM   3464  C  C   . GLY   B  1 170 ? 32.687 -61.247 35.554  1.00 20.63 ? 170  GLY   B C   1 
ATOM   3465  O  O   . GLY   B  1 170 ? 32.084 -61.206 36.645  1.00 22.29 ? 170  GLY   B O   1 
ATOM   3466  N  N   . LYS   B  1 171 ? 33.949 -60.829 35.415  1.00 18.35 ? 171  LYS   B N   1 
ATOM   3467  C  CA  . LYS   B  1 171 ? 34.664 -60.272 36.555  1.00 18.99 ? 171  LYS   B CA  1 
ATOM   3468  C  C   . LYS   B  1 171 ? 34.136 -58.877 36.831  1.00 18.82 ? 171  LYS   B C   1 
ATOM   3469  O  O   . LYS   B  1 171 ? 33.812 -58.131 35.905  1.00 19.32 ? 171  LYS   B O   1 
ATOM   3470  C  CB  . LYS   B  1 171 ? 36.178 -60.211 36.318  1.00 21.67 ? 171  LYS   B CB  1 
ATOM   3471  C  CG  . LYS   B  1 171 ? 36.831 -61.582 36.218  1.00 23.41 ? 171  LYS   B CG  1 
ATOM   3472  C  CD  . LYS   B  1 171 ? 38.346 -61.500 36.410  1.00 28.13 ? 171  LYS   B CD  1 
ATOM   3473  C  CE  . LYS   B  1 171 ? 38.762 -61.208 37.876  1.00 29.35 ? 171  LYS   B CE  1 
ATOM   3474  N  NZ  . LYS   B  1 171 ? 40.278 -61.215 38.084  1.00 33.53 ? 171  LYS   B NZ  1 
ATOM   3475  N  N   . SER   B  1 172 ? 34.039 -58.535 38.113  1.00 20.10 ? 172  SER   B N   1 
ATOM   3476  C  CA  A SER   B  1 172 ? 33.587 -57.217 38.501  0.52 19.40 ? 172  SER   B CA  1 
ATOM   3477  C  CA  B SER   B  1 172 ? 33.495 -57.263 38.580  0.48 19.17 ? 172  SER   B CA  1 
ATOM   3478  C  C   . SER   B  1 172 ? 34.403 -56.743 39.691  1.00 21.08 ? 172  SER   B C   1 
ATOM   3479  O  O   . SER   B  1 172 ? 35.162 -57.512 40.313  1.00 23.09 ? 172  SER   B O   1 
ATOM   3480  C  CB  A SER   B  1 172 ? 32.115 -57.228 38.848  0.52 20.34 ? 172  SER   B CB  1 
ATOM   3481  C  CB  B SER   B  1 172 ? 32.035 -57.424 39.076  0.48 20.62 ? 172  SER   B CB  1 
ATOM   3482  O  OG  A SER   B  1 172 ? 31.945 -58.054 39.982  0.52 19.79 ? 172  SER   B OG  1 
ATOM   3483  O  OG  B SER   B  1 172 ? 31.448 -56.231 39.617  0.48 19.04 ? 172  SER   B OG  1 
ATOM   3484  N  N   . ALA   B  1 173 ? 34.318 -55.445 39.961  1.00 18.93 ? 173  ALA   B N   1 
ATOM   3485  C  CA  . ALA   B  1 173 ? 35.051 -54.859 41.087  1.00 19.48 ? 173  ALA   B CA  1 
ATOM   3486  C  C   . ALA   B  1 173 ? 34.264 -53.664 41.612  1.00 17.32 ? 173  ALA   B C   1 
ATOM   3487  O  O   . ALA   B  1 173 ? 33.588 -52.961 40.846  1.00 19.03 ? 173  ALA   B O   1 
ATOM   3488  C  CB  . ALA   B  1 173 ? 36.478 -54.403 40.685  1.00 21.47 ? 173  ALA   B CB  1 
ATOM   3489  N  N   . ASP   B  1 174 ? 34.395 -53.402 42.927  1.00 17.82 ? 174  ASP   B N   1 
ATOM   3490  C  CA  . ASP   B  1 174 ? 33.850 -52.160 43.453  1.00 20.16 ? 174  ASP   B CA  1 
ATOM   3491  C  C   . ASP   B  1 174 ? 34.477 -50.969 42.734  1.00 21.67 ? 174  ASP   B C   1 
ATOM   3492  O  O   . ASP   B  1 174 ? 35.667 -50.978 42.419  1.00 21.48 ? 174  ASP   B O   1 
ATOM   3493  C  CB  . ASP   B  1 174 ? 34.156 -52.014 44.940  1.00 19.98 ? 174  ASP   B CB  1 
ATOM   3494  C  CG  . ASP   B  1 174 ? 33.619 -53.152 45.807  1.00 23.54 ? 174  ASP   B CG  1 
ATOM   3495  O  OD1 . ASP   B  1 174 ? 32.620 -53.749 45.455  1.00 25.11 ? 174  ASP   B OD1 1 
ATOM   3496  O  OD2 . ASP   B  1 174 ? 34.203 -53.323 46.902  1.00 30.98 ? 174  ASP   B OD2 1 
ATOM   3497  N  N   . PHE   B  1 175 ? 33.681 -49.937 42.529  1.00 18.44 ? 175  PHE   B N   1 
ATOM   3498  C  CA  . PHE   B  1 175 ? 34.156 -48.790 41.750  1.00 19.06 ? 175  PHE   B CA  1 
ATOM   3499  C  C   . PHE   B  1 175 ? 33.353 -47.590 42.249  1.00 18.50 ? 175  PHE   B C   1 
ATOM   3500  O  O   . PHE   B  1 175 ? 32.308 -47.219 41.671  1.00 21.23 ? 175  PHE   B O   1 
ATOM   3501  C  CB  . PHE   B  1 175 ? 33.971 -49.018 40.266  1.00 18.55 ? 175  PHE   B CB  1 
ATOM   3502  C  CG  . PHE   B  1 175 ? 34.751 -48.049 39.417  1.00 20.64 ? 175  PHE   B CG  1 
ATOM   3503  C  CD1 . PHE   B  1 175 ? 36.138 -48.180 39.311  1.00 23.17 ? 175  PHE   B CD1 1 
ATOM   3504  C  CD2 . PHE   B  1 175 ? 34.118 -46.972 38.814  1.00 19.04 ? 175  PHE   B CD2 1 
ATOM   3505  C  CE1 . PHE   B  1 175 ? 36.898 -47.275 38.516  1.00 25.35 ? 175  PHE   B CE1 1 
ATOM   3506  C  CE2 . PHE   B  1 175 ? 34.869 -46.076 38.007  1.00 21.23 ? 175  PHE   B CE2 1 
ATOM   3507  C  CZ  . PHE   B  1 175 ? 36.230 -46.210 37.886  1.00 22.92 ? 175  PHE   B CZ  1 
ATOM   3508  N  N   . THR   B  1 176 ? 33.874 -46.963 43.286  1.00 19.62 ? 176  THR   B N   1 
ATOM   3509  C  CA  . THR   B  1 176 ? 33.137 -45.978 44.052  1.00 20.56 ? 176  THR   B CA  1 
ATOM   3510  C  C   . THR   B  1 176 ? 33.736 -44.588 43.883  1.00 25.16 ? 176  THR   B C   1 
ATOM   3511  O  O   . THR   B  1 176 ? 34.891 -44.410 43.484  1.00 25.59 ? 176  THR   B O   1 
ATOM   3512  C  CB  . THR   B  1 176 ? 33.111 -46.369 45.527  1.00 20.98 ? 176  THR   B CB  1 
ATOM   3513  O  OG1 . THR   B  1 176 ? 34.445 -46.510 46.003  1.00 23.36 ? 176  THR   B OG1 1 
ATOM   3514  C  CG2 . THR   B  1 176 ? 32.401 -47.742 45.662  1.00 24.10 ? 176  THR   B CG2 1 
ATOM   3515  N  N   . ASN   B  1 177 ? 32.902 -43.594 44.157  1.00 23.79 ? 177  ASN   B N   1 
ATOM   3516  C  CA  . ASN   B  1 177 ? 33.349 -42.201 44.191  1.00 25.47 ? 177  ASN   B CA  1 
ATOM   3517  C  C   . ASN   B  1 177 ? 33.883 -41.729 42.834  1.00 26.68 ? 177  ASN   B C   1 
ATOM   3518  O  O   . ASN   B  1 177 ? 34.693 -40.786 42.774  1.00 30.49 ? 177  ASN   B O   1 
ATOM   3519  C  CB  . ASN   B  1 177 ? 34.415 -42.002 45.292  1.00 29.39 ? 177  ASN   B CB  1 
ATOM   3520  C  CG  . ASN   B  1 177 ? 33.938 -42.516 46.655  1.00 29.76 ? 177  ASN   B CG  1 
ATOM   3521  O  OD1 . ASN   B  1 177 ? 34.566 -43.381 47.340  1.00 32.44 ? 177  ASN   B OD1 1 
ATOM   3522  N  ND2 . ASN   B  1 177 ? 32.813 -41.978 47.062  1.00 27.96 ? 177  ASN   B ND2 1 
ATOM   3523  N  N   . PHE   B  1 178 ? 33.397 -42.278 41.733  1.00 24.69 ? 178  PHE   B N   1 
ATOM   3524  C  CA  . PHE   B  1 178 ? 33.832 -41.831 40.414  1.00 23.99 ? 178  PHE   B CA  1 
ATOM   3525  C  C   . PHE   B  1 178 ? 32.940 -40.698 39.916  1.00 26.54 ? 178  PHE   B C   1 
ATOM   3526  O  O   . PHE   B  1 178 ? 31.710 -40.805 39.931  1.00 26.65 ? 178  PHE   B O   1 
ATOM   3527  C  CB  . PHE   B  1 178 ? 33.814 -42.971 39.399  1.00 23.17 ? 178  PHE   B CB  1 
ATOM   3528  C  CG  . PHE   B  1 178 ? 34.331 -42.536 38.059  1.00 22.80 ? 178  PHE   B CG  1 
ATOM   3529  C  CD1 . PHE   B  1 178 ? 35.676 -42.271 37.890  1.00 24.27 ? 178  PHE   B CD1 1 
ATOM   3530  C  CD2 . PHE   B  1 178 ? 33.473 -42.308 37.026  1.00 19.62 ? 178  PHE   B CD2 1 
ATOM   3531  C  CE1 . PHE   B  1 178 ? 36.141 -41.792 36.610  1.00 26.12 ? 178  PHE   B CE1 1 
ATOM   3532  C  CE2 . PHE   B  1 178 ? 33.918 -41.851 35.774  1.00 23.30 ? 178  PHE   B CE2 1 
ATOM   3533  C  CZ  . PHE   B  1 178 ? 35.251 -41.608 35.573  1.00 23.14 ? 178  PHE   B CZ  1 
ATOM   3534  N  N   . ASP   B  1 179 ? 33.577 -39.617 39.440  1.00 25.05 ? 179  ASP   B N   1 
ATOM   3535  C  CA  . ASP   B  1 179 ? 32.876 -38.445 38.942  1.00 24.82 ? 179  ASP   B CA  1 
ATOM   3536  C  C   . ASP   B  1 179 ? 32.763 -38.496 37.418  1.00 24.97 ? 179  ASP   B C   1 
ATOM   3537  O  O   . ASP   B  1 179 ? 33.752 -38.213 36.714  1.00 24.03 ? 179  ASP   B O   1 
ATOM   3538  C  CB  . ASP   B  1 179 ? 33.670 -37.214 39.388  1.00 25.50 ? 179  ASP   B CB  1 
ATOM   3539  C  CG  . ASP   B  1 179 ? 33.060 -35.926 38.928  1.00 29.18 ? 179  ASP   B CG  1 
ATOM   3540  O  OD1 . ASP   B  1 179 ? 31.957 -35.978 38.331  1.00 25.79 ? 179  ASP   B OD1 1 
ATOM   3541  O  OD2 . ASP   B  1 179 ? 33.714 -34.877 39.164  1.00 33.69 ? 179  ASP   B OD2 1 
ATOM   3542  N  N   . PRO   B  1 180 ? 31.604 -38.832 36.843  1.00 22.44 ? 180  PRO   B N   1 
ATOM   3543  C  CA  . PRO   B  1 180 ? 31.539 -38.891 35.366  1.00 23.22 ? 180  PRO   B CA  1 
ATOM   3544  C  C   . PRO   B  1 180 ? 31.641 -37.516 34.712  1.00 23.55 ? 180  PRO   B C   1 
ATOM   3545  O  O   . PRO   B  1 180 ? 31.820 -37.447 33.489  1.00 22.61 ? 180  PRO   B O   1 
ATOM   3546  C  CB  . PRO   B  1 180 ? 30.187 -39.577 35.086  1.00 22.38 ? 180  PRO   B CB  1 
ATOM   3547  C  CG  . PRO   B  1 180 ? 29.346 -39.186 36.311  1.00 24.75 ? 180  PRO   B CG  1 
ATOM   3548  C  CD  . PRO   B  1 180 ? 30.317 -39.161 37.490  1.00 24.44 ? 180  PRO   B CD  1 
ATOM   3549  N  N   . ARG   B  1 181 ? 31.545 -36.420 35.473  1.00 24.69 ? 181  ARG   B N   1 
ATOM   3550  C  CA  . ARG   B  1 181 ? 31.760 -35.120 34.842  1.00 25.95 ? 181  ARG   B CA  1 
ATOM   3551  C  C   . ARG   B  1 181 ? 33.165 -35.003 34.283  1.00 24.08 ? 181  ARG   B C   1 
ATOM   3552  O  O   . ARG   B  1 181 ? 33.404 -34.181 33.375  1.00 26.44 ? 181  ARG   B O   1 
ATOM   3553  C  CB  . ARG   B  1 181 ? 31.493 -34.006 35.838  1.00 28.13 ? 181  ARG   B CB  1 
ATOM   3554  C  CG  . ARG   B  1 181 ? 30.068 -33.933 36.327  1.00 28.62 ? 181  ARG   B CG  1 
ATOM   3555  C  CD  . ARG   B  1 181 ? 29.946 -32.985 37.485  1.00 30.06 ? 181  ARG   B CD  1 
ATOM   3556  N  NE  . ARG   B  1 181 ? 30.852 -33.395 38.551  1.00 33.52 ? 181  ARG   B NE  1 
ATOM   3557  C  CZ  . ARG   B  1 181 ? 31.110 -32.632 39.602  1.00 36.75 ? 181  ARG   B CZ  1 
ATOM   3558  N  NH1 . ARG   B  1 181 ? 30.502 -31.454 39.686  1.00 42.23 ? 181  ARG   B NH1 1 
ATOM   3559  N  NH2 . ARG   B  1 181 ? 31.960 -33.022 40.553  1.00 37.24 ? 181  ARG   B NH2 1 
ATOM   3560  N  N   . GLY   B  1 182 ? 34.102 -35.777 34.820  1.00 26.94 ? 182  GLY   B N   1 
ATOM   3561  C  CA  . GLY   B  1 182 ? 35.455 -35.699 34.297  1.00 24.40 ? 182  GLY   B CA  1 
ATOM   3562  C  C   . GLY   B  1 182 ? 35.623 -36.298 32.923  1.00 24.44 ? 182  GLY   B C   1 
ATOM   3563  O  O   . GLY   B  1 182 ? 36.697 -36.138 32.321  1.00 26.13 ? 182  GLY   B O   1 
ATOM   3564  N  N   . LEU   B  1 183 ? 34.573 -36.939 32.400  1.00 23.77 ? 183  LEU   B N   1 
ATOM   3565  C  CA  . LEU   B  1 183 ? 34.572 -37.503 31.054  1.00 21.36 ? 183  LEU   B CA  1 
ATOM   3566  C  C   . LEU   B  1 183 ? 33.809 -36.646 30.043  1.00 24.14 ? 183  LEU   B C   1 
ATOM   3567  O  O   . LEU   B  1 183 ? 33.622 -37.078 28.903  1.00 23.68 ? 183  LEU   B O   1 
ATOM   3568  C  CB  . LEU   B  1 183 ? 33.967 -38.917 31.067  1.00 21.54 ? 183  LEU   B CB  1 
ATOM   3569  C  CG  . LEU   B  1 183 ? 34.762 -39.895 31.944  1.00 22.04 ? 183  LEU   B CG  1 
ATOM   3570  C  CD1 . LEU   B  1 183 ? 34.068 -41.257 31.960  1.00 22.66 ? 183  LEU   B CD1 1 
ATOM   3571  C  CD2 . LEU   B  1 183 ? 36.192 -40.061 31.448  1.00 24.14 ? 183  LEU   B CD2 1 
ATOM   3572  N  N   . LEU   B  1 184 ? 33.390 -35.442 30.428  1.00 24.48 ? 184  LEU   B N   1 
ATOM   3573  C  CA  . LEU   B  1 184 ? 32.645 -34.528 29.552  1.00 23.89 ? 184  LEU   B CA  1 
ATOM   3574  C  C   . LEU   B  1 184 ? 33.572 -33.481 28.967  1.00 24.09 ? 184  LEU   B C   1 
ATOM   3575  O  O   . LEU   B  1 184 ? 34.449 -32.963 29.652  1.00 26.50 ? 184  LEU   B O   1 
ATOM   3576  C  CB  . LEU   B  1 184 ? 31.533 -33.807 30.318  1.00 26.46 ? 184  LEU   B CB  1 
ATOM   3577  C  CG  . LEU   B  1 184 ? 30.514 -34.695 31.061  1.00 29.68 ? 184  LEU   B CG  1 
ATOM   3578  C  CD1 . LEU   B  1 184 ? 29.574 -33.826 31.886  1.00 30.47 ? 184  LEU   B CD1 1 
ATOM   3579  C  CD2 . LEU   B  1 184 ? 29.741 -35.507 30.046  1.00 26.86 ? 184  LEU   B CD2 1 
ATOM   3580  N  N   . PRO   B  1 185 ? 33.345 -33.084 27.727  1.00 24.46 ? 185  PRO   B N   1 
ATOM   3581  C  CA  . PRO   B  1 185 ? 34.062 -31.945 27.153  1.00 27.11 ? 185  PRO   B CA  1 
ATOM   3582  C  C   . PRO   B  1 185 ? 33.487 -30.628 27.670  1.00 25.83 ? 185  PRO   B C   1 
ATOM   3583  O  O   . PRO   B  1 185 ? 32.429 -30.593 28.295  1.00 30.04 ? 185  PRO   B O   1 
ATOM   3584  C  CB  . PRO   B  1 185 ? 33.805 -32.088 25.641  1.00 26.37 ? 185  PRO   B CB  1 
ATOM   3585  C  CG  . PRO   B  1 185 ? 32.395 -32.711 25.583  1.00 25.49 ? 185  PRO   B CG  1 
ATOM   3586  C  CD  . PRO   B  1 185 ? 32.310 -33.654 26.834  1.00 22.83 ? 185  PRO   B CD  1 
ATOM   3587  N  N   . GLU   B  1 186 ? 34.178 -29.518 27.358  1.00 26.81 ? 186  GLU   B N   1 
ATOM   3588  C  CA  . GLU   B  1 186 ? 33.710 -28.225 27.827  1.00 31.82 ? 186  GLU   B CA  1 
ATOM   3589  C  C   . GLU   B  1 186 ? 32.402 -27.810 27.149  1.00 33.33 ? 186  GLU   B C   1 
ATOM   3590  O  O   . GLU   B  1 186 ? 31.510 -27.261 27.805  1.00 34.69 ? 186  GLU   B O   1 
ATOM   3591  C  CB  . GLU   B  1 186 ? 34.810 -27.188 27.589  1.00 37.96 ? 186  GLU   B CB  1 
ATOM   3592  C  CG  . GLU   B  1 186 ? 34.483 -25.761 27.999  1.00 50.62 ? 186  GLU   B CG  1 
ATOM   3593  C  CD  . GLU   B  1 186 ? 35.714 -24.829 27.950  1.00 61.27 ? 186  GLU   B CD  1 
ATOM   3594  O  OE1 . GLU   B  1 186 ? 36.738 -25.199 27.315  1.00 64.09 ? 186  GLU   B OE1 1 
ATOM   3595  O  OE2 . GLU   B  1 186 ? 35.646 -23.717 28.527  1.00 64.78 ? 186  GLU   B OE2 1 
ATOM   3596  N  N   . SER   B  1 187 ? 32.275 -28.044 25.840  1.00 28.00 ? 187  SER   B N   1 
ATOM   3597  C  CA  . SER   B  1 187 ? 31.078 -27.656 25.097  1.00 28.55 ? 187  SER   B CA  1 
ATOM   3598  C  C   . SER   B  1 187 ? 30.075 -28.796 25.082  1.00 27.35 ? 187  SER   B C   1 
ATOM   3599  O  O   . SER   B  1 187 ? 30.445 -29.944 24.851  1.00 26.19 ? 187  SER   B O   1 
ATOM   3600  C  CB  . SER   B  1 187 ? 31.416 -27.313 23.656  1.00 29.66 ? 187  SER   B CB  1 
ATOM   3601  O  OG  . SER   B  1 187 ? 30.211 -26.993 22.967  1.00 32.86 ? 187  SER   B OG  1 
ATOM   3602  N  N   . LEU   B  1 188 ? 28.798 -28.467 25.259  1.00 29.09 ? 188  LEU   B N   1 
ATOM   3603  C  CA  . LEU   B  1 188 ? 27.758 -29.486 25.157  1.00 27.12 ? 188  LEU   B CA  1 
ATOM   3604  C  C   . LEU   B  1 188 ? 26.943 -29.348 23.873  1.00 28.39 ? 188  LEU   B C   1 
ATOM   3605  O  O   . LEU   B  1 188 ? 25.837 -29.892 23.787  1.00 29.57 ? 188  LEU   B O   1 
ATOM   3606  C  CB  . LEU   B  1 188 ? 26.834 -29.474 26.374  1.00 30.33 ? 188  LEU   B CB  1 
ATOM   3607  C  CG  . LEU   B  1 188 ? 27.481 -29.702 27.732  1.00 32.15 ? 188  LEU   B CG  1 
ATOM   3608  C  CD1 . LEU   B  1 188 ? 26.396 -29.735 28.795  1.00 34.75 ? 188  LEU   B CD1 1 
ATOM   3609  C  CD2 . LEU   B  1 188 ? 28.272 -30.992 27.750  1.00 30.56 ? 188  LEU   B CD2 1 
ATOM   3610  N  N   . ASP   B  1 189 ? 27.487 -28.661 22.872  1.00 25.54 ? 189  ASP   B N   1 
ATOM   3611  C  CA  . ASP   B  1 189 ? 26.927 -28.688 21.524  1.00 24.91 ? 189  ASP   B CA  1 
ATOM   3612  C  C   . ASP   B  1 189 ? 26.768 -30.134 21.066  1.00 22.77 ? 189  ASP   B C   1 
ATOM   3613  O  O   . ASP   B  1 189 ? 27.641 -30.975 21.300  1.00 23.11 ? 189  ASP   B O   1 
ATOM   3614  C  CB  . ASP   B  1 189 ? 27.863 -27.951 20.558  1.00 24.89 ? 189  ASP   B CB  1 
ATOM   3615  C  CG  . ASP   B  1 189 ? 27.815 -26.443 20.708  1.00 30.28 ? 189  ASP   B CG  1 
ATOM   3616  O  OD1 . ASP   B  1 189 ? 27.036 -25.927 21.530  1.00 34.57 ? 189  ASP   B OD1 1 
ATOM   3617  O  OD2 . ASP   B  1 189 ? 28.577 -25.763 20.007  1.00 33.30 ? 189  ASP   B OD2 1 
ATOM   3618  N  N   . TYR   B  1 190 ? 25.652 -30.432 20.400  1.00 21.44 ? 190  TYR   B N   1 
ATOM   3619  C  CA  . TYR   B  1 190 ? 25.402 -31.846 20.105  1.00 19.68 ? 190  TYR   B CA  1 
ATOM   3620  C  C   . TYR   B  1 190 ? 24.561 -32.003 18.839  1.00 22.26 ? 190  TYR   B C   1 
ATOM   3621  O  O   . TYR   B  1 190 ? 23.921 -31.056 18.356  1.00 23.43 ? 190  TYR   B O   1 
ATOM   3622  C  CB  . TYR   B  1 190 ? 24.700 -32.584 21.271  1.00 20.15 ? 190  TYR   B CB  1 
ATOM   3623  C  CG  . TYR   B  1 190 ? 23.305 -32.058 21.566  1.00 20.98 ? 190  TYR   B CG  1 
ATOM   3624  C  CD1 . TYR   B  1 190 ? 22.197 -32.539 20.846  1.00 23.60 ? 190  TYR   B CD1 1 
ATOM   3625  C  CD2 . TYR   B  1 190 ? 23.084 -31.057 22.534  1.00 21.72 ? 190  TYR   B CD2 1 
ATOM   3626  C  CE1 . TYR   B  1 190 ? 20.886 -32.025 21.098  1.00 24.68 ? 190  TYR   B CE1 1 
ATOM   3627  C  CE2 . TYR   B  1 190 ? 21.763 -30.547 22.788  1.00 23.28 ? 190  TYR   B CE2 1 
ATOM   3628  C  CZ  . TYR   B  1 190 ? 20.679 -31.045 22.078  1.00 22.80 ? 190  TYR   B CZ  1 
ATOM   3629  O  OH  . TYR   B  1 190 ? 19.388 -30.503 22.298  1.00 26.25 ? 190  TYR   B OH  1 
ATOM   3630  N  N   . TRP   B  1 191 ? 24.587 -33.233 18.313  1.00 21.11 ? 191  TRP   B N   1 
ATOM   3631  C  CA  . TRP   B  1 191 ? 23.675 -33.729 17.285  1.00 20.26 ? 191  TRP   B CA  1 
ATOM   3632  C  C   . TRP   B  1 191 ? 22.725 -34.725 17.936  1.00 21.01 ? 191  TRP   B C   1 
ATOM   3633  O  O   . TRP   B  1 191 ? 23.114 -35.464 18.862  1.00 20.10 ? 191  TRP   B O   1 
ATOM   3634  C  CB  . TRP   B  1 191 ? 24.422 -34.399 16.131  1.00 21.34 ? 191  TRP   B CB  1 
ATOM   3635  C  CG  . TRP   B  1 191 ? 25.351 -33.528 15.418  1.00 21.31 ? 191  TRP   B CG  1 
ATOM   3636  C  CD1 . TRP   B  1 191 ? 25.024 -32.570 14.506  1.00 23.32 ? 191  TRP   B CD1 1 
ATOM   3637  C  CD2 . TRP   B  1 191 ? 26.789 -33.551 15.479  1.00 22.02 ? 191  TRP   B CD2 1 
ATOM   3638  N  NE1 . TRP   B  1 191 ? 26.152 -31.982 14.008  1.00 26.46 ? 191  TRP   B NE1 1 
ATOM   3639  C  CE2 . TRP   B  1 191 ? 27.253 -32.593 14.539  1.00 24.78 ? 191  TRP   B CE2 1 
ATOM   3640  C  CE3 . TRP   B  1 191 ? 27.723 -34.324 16.187  1.00 24.70 ? 191  TRP   B CE3 1 
ATOM   3641  C  CZ2 . TRP   B  1 191 ? 28.631 -32.307 14.350  1.00 24.58 ? 191  TRP   B CZ2 1 
ATOM   3642  C  CZ3 . TRP   B  1 191 ? 29.093 -34.074 15.982  1.00 25.19 ? 191  TRP   B CZ3 1 
ATOM   3643  C  CH2 . TRP   B  1 191 ? 29.527 -33.079 15.070  1.00 25.40 ? 191  TRP   B CH2 1 
ATOM   3644  N  N   . THR   B  1 192 ? 21.483 -34.788 17.452  1.00 20.46 ? 192  THR   B N   1 
ATOM   3645  C  CA  . THR   B  1 192 ? 20.527 -35.736 18.024  1.00 19.87 ? 192  THR   B CA  1 
ATOM   3646  C  C   . THR   B  1 192 ? 19.692 -36.381 16.930  1.00 18.62 ? 192  THR   B C   1 
ATOM   3647  O  O   . THR   B  1 192 ? 19.350 -35.753 15.908  1.00 21.43 ? 192  THR   B O   1 
ATOM   3648  C  CB  . THR   B  1 192 ? 19.608 -35.069 19.091  1.00 18.89 ? 192  THR   B CB  1 
ATOM   3649  O  OG1 . THR   B  1 192 ? 18.758 -36.070 19.719  1.00 19.61 ? 192  THR   B OG1 1 
ATOM   3650  C  CG2 . THR   B  1 192 ? 18.779 -33.915 18.503  1.00 21.16 ? 192  THR   B CG2 1 
ATOM   3651  N  N   . TYR   B  1 193 ? 19.346 -37.636 17.148  1.00 18.81 ? 193  TYR   B N   1 
ATOM   3652  C  CA  . TYR   B  1 193 ? 18.482 -38.347 16.215  1.00 18.47 ? 193  TYR   B CA  1 
ATOM   3653  C  C   . TYR   B  1 193 ? 17.875 -39.548 16.943  1.00 19.30 ? 193  TYR   B C   1 
ATOM   3654  O  O   . TYR   B  1 193 ? 18.419 -40.009 17.963  1.00 18.81 ? 193  TYR   B O   1 
ATOM   3655  C  CB  . TYR   B  1 193 ? 19.259 -38.811 14.944  1.00 17.84 ? 193  TYR   B CB  1 
ATOM   3656  C  CG  . TYR   B  1 193 ? 20.173 -39.982 15.221  1.00 17.19 ? 193  TYR   B CG  1 
ATOM   3657  C  CD1 . TYR   B  1 193 ? 21.420 -39.758 15.787  1.00 17.94 ? 193  TYR   B CD1 1 
ATOM   3658  C  CD2 . TYR   B  1 193 ? 19.781 -41.282 14.911  1.00 17.41 ? 193  TYR   B CD2 1 
ATOM   3659  C  CE1 . TYR   B  1 193 ? 22.286 -40.825 16.087  1.00 17.72 ? 193  TYR   B CE1 1 
ATOM   3660  C  CE2 . TYR   B  1 193 ? 20.620 -42.376 15.192  1.00 16.24 ? 193  TYR   B CE2 1 
ATOM   3661  C  CZ  . TYR   B  1 193 ? 21.881 -42.116 15.786  1.00 16.18 ? 193  TYR   B CZ  1 
ATOM   3662  O  OH  . TYR   B  1 193 ? 22.697 -43.206 16.118  1.00 17.26 ? 193  TYR   B OH  1 
ATOM   3663  N  N   . PRO   B  1 194 ? 16.732 -40.048 16.470  1.00 16.71 ? 194  PRO   B N   1 
ATOM   3664  C  CA  . PRO   B  1 194 ? 16.121 -41.245 17.079  1.00 18.24 ? 194  PRO   B CA  1 
ATOM   3665  C  C   . PRO   B  1 194 ? 16.784 -42.507 16.547  1.00 16.63 ? 194  PRO   B C   1 
ATOM   3666  O  O   . PRO   B  1 194 ? 16.884 -42.690 15.325  1.00 16.39 ? 194  PRO   B O   1 
ATOM   3667  C  CB  . PRO   B  1 194 ? 14.670 -41.190 16.596  1.00 17.14 ? 194  PRO   B CB  1 
ATOM   3668  C  CG  . PRO   B  1 194 ? 14.760 -40.367 15.304  1.00 20.57 ? 194  PRO   B CG  1 
ATOM   3669  C  CD  . PRO   B  1 194 ? 15.887 -39.431 15.423  1.00 17.95 ? 194  PRO   B CD  1 
ATOM   3670  N  N   . GLY   B  1 195 ? 17.230 -43.369 17.430  1.00 15.57 ? 195  GLY   B N   1 
ATOM   3671  C  CA  . GLY   B  1 195 ? 17.895 -44.607 17.019  1.00 14.99 ? 195  GLY   B CA  1 
ATOM   3672  C  C   . GLY   B  1 195 ? 17.694 -45.755 17.966  1.00 14.63 ? 195  GLY   B C   1 
ATOM   3673  O  O   . GLY   B  1 195 ? 16.613 -45.922 18.551  1.00 15.84 ? 195  GLY   B O   1 
ATOM   3674  N  N   . SER   B  1 196 ? 18.750 -46.559 18.130  1.00 14.81 ? 196  SER   B N   1 
ATOM   3675  C  CA  . SER   B  1 196 ? 18.615 -47.867 18.759  1.00 14.84 ? 196  SER   B CA  1 
ATOM   3676  C  C   . SER   B  1 196 ? 19.792 -48.137 19.684  1.00 15.55 ? 196  SER   B C   1 
ATOM   3677  O  O   . SER   B  1 196 ? 20.815 -47.435 19.648  1.00 14.54 ? 196  SER   B O   1 
ATOM   3678  C  CB  . SER   B  1 196 ? 18.556 -48.993 17.684  1.00 15.56 ? 196  SER   B CB  1 
ATOM   3679  O  OG  . SER   B  1 196 ? 19.870 -49.174 17.107  1.00 15.77 ? 196  SER   B OG  1 
ATOM   3680  N  N   . LEU   B  1 197 ? 19.658 -49.221 20.474  1.00 14.38 ? 197  LEU   B N   1 
ATOM   3681  C  CA  . LEU   B  1 197 ? 20.860 -49.787 21.060  1.00 13.80 ? 197  LEU   B CA  1 
ATOM   3682  C  C   . LEU   B  1 197 ? 21.829 -50.169 19.946  1.00 15.32 ? 197  LEU   B C   1 
ATOM   3683  O  O   . LEU   B  1 197 ? 21.410 -50.646 18.879  1.00 14.22 ? 197  LEU   B O   1 
ATOM   3684  C  CB  . LEU   B  1 197 ? 20.519 -51.054 21.835  1.00 14.03 ? 197  LEU   B CB  1 
ATOM   3685  C  CG  . LEU   B  1 197 ? 19.524 -50.887 22.981  1.00 13.78 ? 197  LEU   B CG  1 
ATOM   3686  C  CD1 . LEU   B  1 197 ? 19.260 -52.285 23.557  1.00 15.89 ? 197  LEU   B CD1 1 
ATOM   3687  C  CD2 . LEU   B  1 197 ? 20.046 -49.939 24.088  1.00 15.58 ? 197  LEU   B CD2 1 
ATOM   3688  N  N   . THR   B  1 198 ? 23.127 -50.020 20.209  1.00 14.54 ? 198  THR   B N   1 
ATOM   3689  C  CA  . THR   B  1 198 ? 24.084 -50.435 19.160  1.00 13.96 ? 198  THR   B CA  1 
ATOM   3690  C  C   . THR   B  1 198 ? 24.593 -51.863 19.378  1.00 14.71 ? 198  THR   B C   1 
ATOM   3691  O  O   . THR   B  1 198 ? 25.494 -52.303 18.651  1.00 12.85 ? 198  THR   B O   1 
ATOM   3692  C  CB  . THR   B  1 198 ? 25.304 -49.505 19.064  1.00 13.74 ? 198  THR   B CB  1 
ATOM   3693  O  OG1 . THR   B  1 198 ? 26.034 -49.624 20.318  1.00 14.69 ? 198  THR   B OG1 1 
ATOM   3694  C  CG2 . THR   B  1 198 ? 24.892 -48.042 18.831  1.00 15.21 ? 198  THR   B CG2 1 
ATOM   3695  N  N   . THR   B  1 199 ? 24.004 -52.575 20.328  1.00 14.39 ? 199  THR   B N   1 
ATOM   3696  C  CA  . THR   B  1 199 ? 24.283 -53.993 20.502  1.00 12.66 ? 199  THR   B CA  1 
ATOM   3697  C  C   . THR   B  1 199 ? 22.939 -54.704 20.508  1.00 13.38 ? 199  THR   B C   1 
ATOM   3698  O  O   . THR   B  1 199 ? 21.898 -54.076 20.770  1.00 15.06 ? 199  THR   B O   1 
ATOM   3699  C  CB  . THR   B  1 199 ? 24.991 -54.321 21.842  1.00 13.83 ? 199  THR   B CB  1 
ATOM   3700  O  OG1 . THR   B  1 199 ? 24.110 -54.029 22.947  1.00 16.05 ? 199  THR   B OG1 1 
ATOM   3701  C  CG2 . THR   B  1 199 ? 26.268 -53.534 21.996  1.00 15.66 ? 199  THR   B CG2 1 
ATOM   3702  N  N   . PRO   B  1 200 ? 22.923 -55.998 20.225  1.00 14.46 ? 200  PRO   B N   1 
ATOM   3703  C  CA  . PRO   B  1 200 ? 21.715 -56.799 20.523  1.00 12.37 ? 200  PRO   B CA  1 
ATOM   3704  C  C   . PRO   B  1 200 ? 21.203 -56.467 21.915  1.00 13.63 ? 200  PRO   B C   1 
ATOM   3705  O  O   . PRO   B  1 200 ? 21.998 -56.298 22.864  1.00 14.40 ? 200  PRO   B O   1 
ATOM   3706  C  CB  . PRO   B  1 200 ? 22.222 -58.271 20.420  1.00 14.47 ? 200  PRO   B CB  1 
ATOM   3707  C  CG  . PRO   B  1 200 ? 23.320 -58.148 19.299  1.00 14.55 ? 200  PRO   B CG  1 
ATOM   3708  C  CD  . PRO   B  1 200 ? 24.067 -56.847 19.787  1.00 13.35 ? 200  PRO   B CD  1 
ATOM   3709  N  N   . PRO   B  1 201 ? 19.878 -56.370 22.086  1.00 14.10 ? 201  PRO   B N   1 
ATOM   3710  C  CA  . PRO   B  1 201 ? 18.852 -56.715 21.084  1.00 14.25 ? 201  PRO   B CA  1 
ATOM   3711  C  C   . PRO   B  1 201 ? 18.506 -55.621 20.061  1.00 13.10 ? 201  PRO   B C   1 
ATOM   3712  O  O   . PRO   B  1 201 ? 17.551 -55.788 19.310  1.00 14.36 ? 201  PRO   B O   1 
ATOM   3713  C  CB  . PRO   B  1 201 ? 17.612 -57.031 21.964  1.00 13.66 ? 201  PRO   B CB  1 
ATOM   3714  C  CG  . PRO   B  1 201 ? 17.773 -56.105 23.168  1.00 13.75 ? 201  PRO   B CG  1 
ATOM   3715  C  CD  . PRO   B  1 201 ? 19.283 -56.109 23.414  1.00 14.68 ? 201  PRO   B CD  1 
ATOM   3716  N  N   . LEU   B  1 202 ? 19.286 -54.522 20.007  1.00 13.50 ? 202  LEU   B N   1 
ATOM   3717  C  CA  . LEU   B  1 202 ? 19.189 -53.508 18.927  1.00 12.49 ? 202  LEU   B CA  1 
ATOM   3718  C  C   . LEU   B  1 202 ? 17.822 -52.808 18.922  1.00 13.36 ? 202  LEU   B C   1 
ATOM   3719  O  O   . LEU   B  1 202 ? 17.367 -52.311 17.860  1.00 14.73 ? 202  LEU   B O   1 
ATOM   3720  C  CB  . LEU   B  1 202 ? 19.483 -54.122 17.537  1.00 13.04 ? 202  LEU   B CB  1 
ATOM   3721  C  CG  . LEU   B  1 202 ? 20.893 -54.737 17.435  1.00 13.32 ? 202  LEU   B CG  1 
ATOM   3722  C  CD1 . LEU   B  1 202 ? 21.055 -55.561 16.142  1.00 14.79 ? 202  LEU   B CD1 1 
ATOM   3723  C  CD2 . LEU   B  1 202 ? 21.966 -53.647 17.470  1.00 14.30 ? 202  LEU   B CD2 1 
ATOM   3724  N  N   . LEU   B  1 203 ? 17.150 -52.777 20.072  1.00 14.48 ? 203  LEU   B N   1 
ATOM   3725  C  CA  . LEU   B  1 203 ? 15.820 -52.168 20.145  1.00 14.30 ? 203  LEU   B CA  1 
ATOM   3726  C  C   . LEU   B  1 203 ? 15.871 -50.685 19.823  1.00 14.27 ? 203  LEU   B C   1 
ATOM   3727  O  O   . LEU   B  1 203 ? 16.786 -49.960 20.227  1.00 13.70 ? 203  LEU   B O   1 
ATOM   3728  C  CB  . LEU   B  1 203 ? 15.237 -52.404 21.539  1.00 13.82 ? 203  LEU   B CB  1 
ATOM   3729  C  CG  . LEU   B  1 203 ? 15.016 -53.905 21.822  1.00 14.49 ? 203  LEU   B CG  1 
ATOM   3730  C  CD1 . LEU   B  1 203 ? 14.634 -54.097 23.326  1.00 17.73 ? 203  LEU   B CD1 1 
ATOM   3731  C  CD2 . LEU   B  1 203 ? 13.944 -54.485 20.848  1.00 18.28 ? 203  LEU   B CD2 1 
ATOM   3732  N  N   . GLU   B  1 204 ? 14.805 -50.209 19.187  1.00 14.55 ? 204  GLU   B N   1 
ATOM   3733  C  CA  . GLU   B  1 204 ? 14.754 -48.821 18.685  1.00 13.99 ? 204  GLU   B CA  1 
ATOM   3734  C  C   . GLU   B  1 204 ? 14.110 -47.909 19.736  1.00 16.05 ? 204  GLU   B C   1 
ATOM   3735  O  O   . GLU   B  1 204 ? 13.050 -47.281 19.538  1.00 18.14 ? 204  GLU   B O   1 
ATOM   3736  C  CB  . GLU   B  1 204 ? 14.042 -48.807 17.340  1.00 15.67 ? 204  GLU   B CB  1 
ATOM   3737  C  CG  . GLU   B  1 204 ? 14.895 -49.609 16.312  1.00 14.94 ? 204  GLU   B CG  1 
ATOM   3738  C  CD  . GLU   B  1 204 ? 14.295 -49.697 14.904  1.00 16.26 ? 204  GLU   B CD  1 
ATOM   3739  O  OE1 . GLU   B  1 204 ? 13.041 -49.616 14.793  1.00 18.86 ? 204  GLU   B OE1 1 
ATOM   3740  O  OE2 . GLU   B  1 204 ? 15.094 -49.877 13.953  1.00 17.19 ? 204  GLU   B OE2 1 
ATOM   3741  N  N   . SER   B  1 205 ? 14.830 -47.830 20.867  1.00 15.30 ? 205  SER   B N   1 
ATOM   3742  C  CA  A SER   B  1 205 ? 14.319 -47.144 22.053  0.61 14.84 ? 205  SER   B CA  1 
ATOM   3743  C  CA  B SER   B  1 205 ? 14.342 -47.164 22.067  0.39 14.89 ? 205  SER   B CA  1 
ATOM   3744  C  C   . SER   B  1 205 ? 15.222 -46.010 22.510  1.00 15.15 ? 205  SER   B C   1 
ATOM   3745  O  O   . SER   B  1 205 ? 15.051 -45.511 23.637  1.00 17.49 ? 205  SER   B O   1 
ATOM   3746  C  CB  A SER   B  1 205 ? 14.129 -48.136 23.184  0.61 16.15 ? 205  SER   B CB  1 
ATOM   3747  C  CB  B SER   B  1 205 ? 14.222 -48.192 23.178  0.39 15.82 ? 205  SER   B CB  1 
ATOM   3748  O  OG  A SER   B  1 205 ? 15.311 -48.861 23.313  0.61 16.55 ? 205  SER   B OG  1 
ATOM   3749  O  OG  B SER   B  1 205 ? 13.596 -49.330 22.630  0.39 15.88 ? 205  SER   B OG  1 
ATOM   3750  N  N   . VAL   B  1 206 ? 16.157 -45.555 21.684  1.00 15.99 ? 206  VAL   B N   1 
ATOM   3751  C  CA  . VAL   B  1 206 ? 17.180 -44.612 22.157  1.00 16.03 ? 206  VAL   B CA  1 
ATOM   3752  C  C   . VAL   B  1 206 ? 17.032 -43.276 21.449  1.00 17.97 ? 206  VAL   B C   1 
ATOM   3753  O  O   . VAL   B  1 206 ? 17.030 -43.209 20.208  1.00 18.14 ? 206  VAL   B O   1 
ATOM   3754  C  CB  . VAL   B  1 206 ? 18.605 -45.146 21.917  1.00 15.36 ? 206  VAL   B CB  1 
ATOM   3755  C  CG1 . VAL   B  1 206 ? 19.668 -44.092 22.390  1.00 16.84 ? 206  VAL   B CG1 1 
ATOM   3756  C  CG2 . VAL   B  1 206 ? 18.863 -46.507 22.606  1.00 14.67 ? 206  VAL   B CG2 1 
ATOM   3757  N  N   . THR   B  1 207 ? 16.997 -42.191 22.224  1.00 17.33 ? 207  THR   B N   1 
ATOM   3758  C  CA  . THR   B  1 207 ? 17.263 -40.849 21.706  1.00 18.54 ? 207  THR   B CA  1 
ATOM   3759  C  C   . THR   B  1 207 ? 18.754 -40.609 21.869  1.00 18.01 ? 207  THR   B C   1 
ATOM   3760  O  O   . THR   B  1 207 ? 19.256 -40.595 23.001  1.00 17.66 ? 207  THR   B O   1 
ATOM   3761  C  CB  . THR   B  1 207 ? 16.467 -39.797 22.477  1.00 18.41 ? 207  THR   B CB  1 
ATOM   3762  O  OG1 . THR   B  1 207 ? 15.078 -40.040 22.288  1.00 20.34 ? 207  THR   B OG1 1 
ATOM   3763  C  CG2 . THR   B  1 207 ? 16.769 -38.410 21.900  1.00 19.77 ? 207  THR   B CG2 1 
ATOM   3764  N  N   . TRP   B  1 208 ? 19.467 -40.528 20.750  1.00 17.18 ? 208  TRP   B N   1 
ATOM   3765  C  CA  . TRP   B  1 208 ? 20.915 -40.293 20.745  1.00 17.12 ? 208  TRP   B CA  1 
ATOM   3766  C  C   . TRP   B  1 208 ? 21.229 -38.813 20.843  1.00 18.79 ? 208  TRP   B C   1 
ATOM   3767  O  O   . TRP   B  1 208 ? 20.651 -38.007 20.100  1.00 18.84 ? 208  TRP   B O   1 
ATOM   3768  C  CB  . TRP   B  1 208 ? 21.549 -40.853 19.448  1.00 16.52 ? 208  TRP   B CB  1 
ATOM   3769  C  CG  . TRP   B  1 208 ? 21.753 -42.344 19.644  1.00 16.01 ? 208  TRP   B CG  1 
ATOM   3770  C  CD1 . TRP   B  1 208 ? 20.930 -43.353 19.218  1.00 16.14 ? 208  TRP   B CD1 1 
ATOM   3771  C  CD2 . TRP   B  1 208 ? 22.844 -42.960 20.338  1.00 16.24 ? 208  TRP   B CD2 1 
ATOM   3772  N  NE1 . TRP   B  1 208 ? 21.430 -44.583 19.671  1.00 16.60 ? 208  TRP   B NE1 1 
ATOM   3773  C  CE2 . TRP   B  1 208 ? 22.591 -44.336 20.356  1.00 16.19 ? 208  TRP   B CE2 1 
ATOM   3774  C  CE3 . TRP   B  1 208 ? 23.994 -42.452 20.972  1.00 17.03 ? 208  TRP   B CE3 1 
ATOM   3775  C  CZ2 . TRP   B  1 208 ? 23.461 -45.257 20.966  1.00 15.30 ? 208  TRP   B CZ2 1 
ATOM   3776  C  CZ3 . TRP   B  1 208 ? 24.866 -43.374 21.610  1.00 16.86 ? 208  TRP   B CZ3 1 
ATOM   3777  C  CH2 . TRP   B  1 208 ? 24.596 -44.755 21.577  1.00 16.60 ? 208  TRP   B CH2 1 
ATOM   3778  N  N   . ILE   B  1 209 ? 22.169 -38.475 21.723  1.00 17.84 ? 209  ILE   B N   1 
ATOM   3779  C  CA  . ILE   B  1 209 ? 22.676 -37.135 21.868  1.00 17.80 ? 209  ILE   B CA  1 
ATOM   3780  C  C   . ILE   B  1 209 ? 24.187 -37.292 21.754  1.00 19.31 ? 209  ILE   B C   1 
ATOM   3781  O  O   . ILE   B  1 209 ? 24.826 -37.797 22.690  1.00 20.04 ? 209  ILE   B O   1 
ATOM   3782  C  CB  . ILE   B  1 209 ? 22.265 -36.542 23.225  1.00 19.56 ? 209  ILE   B CB  1 
ATOM   3783  C  CG1 . ILE   B  1 209 ? 20.725 -36.461 23.312  1.00 21.87 ? 209  ILE   B CG1 1 
ATOM   3784  C  CG2 . ILE   B  1 209 ? 22.912 -35.171 23.442  1.00 20.22 ? 209  ILE   B CG2 1 
ATOM   3785  C  CD1 . ILE   B  1 209 ? 20.179 -36.144 24.722  1.00 23.03 ? 209  ILE   B CD1 1 
ATOM   3786  N  N   . VAL   B  1 210 ? 24.762 -36.911 20.615  1.00 18.58 ? 210  VAL   B N   1 
ATOM   3787  C  CA  . VAL   B  1 210 ? 26.191 -37.122 20.342  1.00 18.69 ? 210  VAL   B CA  1 
ATOM   3788  C  C   . VAL   B  1 210 ? 26.903 -35.784 20.403  1.00 21.47 ? 210  VAL   B C   1 
ATOM   3789  O  O   . VAL   B  1 210 ? 26.589 -34.863 19.639  1.00 20.36 ? 210  VAL   B O   1 
ATOM   3790  C  CB  . VAL   B  1 210 ? 26.407 -37.784 18.985  1.00 19.36 ? 210  VAL   B CB  1 
ATOM   3791  C  CG1 . VAL   B  1 210 ? 27.922 -37.975 18.743  1.00 18.70 ? 210  VAL   B CG1 1 
ATOM   3792  C  CG2 . VAL   B  1 210 ? 25.694 -39.151 18.958  1.00 19.01 ? 210  VAL   B CG2 1 
ATOM   3793  N  N   . LEU   B  1 211 ? 27.817 -35.639 21.370  1.00 20.63 ? 211  LEU   B N   1 
ATOM   3794  C  CA  . LEU   B  1 211 ? 28.467 -34.345 21.529  1.00 21.04 ? 211  LEU   B CA  1 
ATOM   3795  C  C   . LEU   B  1 211 ? 29.455 -34.077 20.396  1.00 22.24 ? 211  LEU   B C   1 
ATOM   3796  O  O   . LEU   B  1 211 ? 30.185 -34.965 19.944  1.00 23.39 ? 211  LEU   B O   1 
ATOM   3797  C  CB  . LEU   B  1 211 ? 29.182 -34.286 22.863  1.00 20.86 ? 211  LEU   B CB  1 
ATOM   3798  C  CG  . LEU   B  1 211 ? 28.338 -34.419 24.138  1.00 22.41 ? 211  LEU   B CG  1 
ATOM   3799  C  CD1 . LEU   B  1 211 ? 29.300 -34.150 25.337  1.00 23.33 ? 211  LEU   B CD1 1 
ATOM   3800  C  CD2 . LEU   B  1 211 ? 27.247 -33.327 24.069  1.00 25.30 ? 211  LEU   B CD2 1 
ATOM   3801  N  N   . LYS   B  1 212 ? 29.494 -32.825 19.930  1.00 22.88 ? 212  LYS   B N   1 
ATOM   3802  C  CA  . LYS   B  1 212 ? 30.399 -32.474 18.849  1.00 23.41 ? 212  LYS   B CA  1 
ATOM   3803  C  C   . LYS   B  1 212 ? 31.860 -32.426 19.299  1.00 25.23 ? 212  LYS   B C   1 
ATOM   3804  O  O   . LYS   B  1 212 ? 32.763 -32.795 18.536  1.00 26.69 ? 212  LYS   B O   1 
ATOM   3805  C  CB  . LYS   B  1 212 ? 29.967 -31.138 18.266  1.00 25.47 ? 212  LYS   B CB  1 
ATOM   3806  C  CG  . LYS   B  1 212 ? 30.965 -30.568 17.267  1.00 27.44 ? 212  LYS   B CG  1 
ATOM   3807  C  CD  . LYS   B  1 212 ? 30.340 -29.441 16.468  1.00 34.71 ? 212  LYS   B CD  1 
ATOM   3808  C  CE  . LYS   B  1 212 ? 31.383 -28.844 15.531  1.00 42.01 ? 212  LYS   B CE  1 
ATOM   3809  N  NZ  . LYS   B  1 212 ? 30.813 -27.666 14.864  1.00 45.40 ? 212  LYS   B NZ  1 
ATOM   3810  N  N   . GLU   B  1 213 ? 32.128 -31.962 20.516  1.00 23.12 ? 213  GLU   B N   1 
ATOM   3811  C  CA  . GLU   B  1 213 ? 33.514 -31.813 20.957  1.00 23.77 ? 213  GLU   B CA  1 
ATOM   3812  C  C   . GLU   B  1 213 ? 34.023 -33.123 21.544  1.00 23.34 ? 213  GLU   B C   1 
ATOM   3813  O  O   . GLU   B  1 213 ? 33.424 -33.624 22.498  1.00 23.07 ? 213  GLU   B O   1 
ATOM   3814  C  CB  . GLU   B  1 213 ? 33.639 -30.705 22.000  1.00 24.35 ? 213  GLU   B CB  1 
ATOM   3815  C  CG  . GLU   B  1 213 ? 35.090 -30.468 22.453  1.00 27.15 ? 213  GLU   B CG  1 
ATOM   3816  C  CD  . GLU   B  1 213 ? 35.275 -29.282 23.390  1.00 33.01 ? 213  GLU   B CD  1 
ATOM   3817  O  OE1 . GLU   B  1 213 ? 34.303 -28.792 23.997  1.00 34.35 ? 213  GLU   B OE1 1 
ATOM   3818  O  OE2 . GLU   B  1 213 ? 36.429 -28.811 23.479  1.00 38.21 ? 213  GLU   B OE2 1 
ATOM   3819  N  N   . PRO   B  1 214 ? 35.124 -33.684 21.057  1.00 23.82 ? 214  PRO   B N   1 
ATOM   3820  C  CA  . PRO   B  1 214 ? 35.664 -34.899 21.690  1.00 23.48 ? 214  PRO   B CA  1 
ATOM   3821  C  C   . PRO   B  1 214 ? 36.378 -34.549 22.973  1.00 23.99 ? 214  PRO   B C   1 
ATOM   3822  O  O   . PRO   B  1 214 ? 36.791 -33.395 23.213  1.00 27.31 ? 214  PRO   B O   1 
ATOM   3823  C  CB  . PRO   B  1 214 ? 36.681 -35.431 20.668  1.00 25.05 ? 214  PRO   B CB  1 
ATOM   3824  C  CG  . PRO   B  1 214 ? 36.566 -34.496 19.456  1.00 33.05 ? 214  PRO   B CG  1 
ATOM   3825  C  CD  . PRO   B  1 214 ? 36.001 -33.215 19.971  1.00 27.25 ? 214  PRO   B CD  1 
ATOM   3826  N  N   . ILE   B  1 215 ? 36.569 -35.595 23.790  1.00 23.54 ? 215  ILE   B N   1 
ATOM   3827  C  CA  . ILE   B  1 215 ? 37.526 -35.556 24.882  1.00 23.00 ? 215  ILE   B CA  1 
ATOM   3828  C  C   . ILE   B  1 215 ? 38.833 -36.166 24.405  1.00 25.24 ? 215  ILE   B C   1 
ATOM   3829  O  O   . ILE   B  1 215 ? 38.863 -37.031 23.509  1.00 25.99 ? 215  ILE   B O   1 
ATOM   3830  C  CB  . ILE   B  1 215 ? 36.985 -36.226 26.164  1.00 23.79 ? 215  ILE   B CB  1 
ATOM   3831  C  CG1 . ILE   B  1 215 ? 36.685 -37.712 25.937  1.00 22.48 ? 215  ILE   B CG1 1 
ATOM   3832  C  CG2 . ILE   B  1 215 ? 35.744 -35.472 26.644  1.00 24.68 ? 215  ILE   B CG2 1 
ATOM   3833  C  CD1 . ILE   B  1 215 ? 36.206 -38.467 27.225  1.00 23.87 ? 215  ILE   B CD1 1 
ATOM   3834  N  N   . SER   B  1 216 ? 39.932 -35.678 24.971  1.00 27.08 ? 216  SER   B N   1 
ATOM   3835  C  CA  A SER   B  1 216 ? 41.268 -36.109 24.606  0.50 27.98 ? 216  SER   B CA  1 
ATOM   3836  C  CA  B SER   B  1 216 ? 41.260 -36.124 24.589  0.50 27.93 ? 216  SER   B CA  1 
ATOM   3837  C  C   . SER   B  1 216 ? 41.761 -37.134 25.605  1.00 30.88 ? 216  SER   B C   1 
ATOM   3838  O  O   . SER   B  1 216 ? 41.778 -36.845 26.813  1.00 35.07 ? 216  SER   B O   1 
ATOM   3839  C  CB  A SER   B  1 216 ? 42.237 -34.931 24.605  0.50 30.56 ? 216  SER   B CB  1 
ATOM   3840  C  CB  B SER   B  1 216 ? 42.242 -34.952 24.491  0.50 30.76 ? 216  SER   B CB  1 
ATOM   3841  O  OG  A SER   B  1 216 ? 43.561 -35.405 24.634  0.50 30.67 ? 216  SER   B OG  1 
ATOM   3842  O  OG  B SER   B  1 216 ? 42.019 -34.177 23.311  0.50 30.14 ? 216  SER   B OG  1 
ATOM   3843  N  N   . VAL   B  1 217 ? 42.196 -38.295 25.105  1.00 27.02 ? 217  VAL   B N   1 
ATOM   3844  C  CA  . VAL   B  1 217 ? 42.841 -39.337 25.907  1.00 28.73 ? 217  VAL   B CA  1 
ATOM   3845  C  C   . VAL   B  1 217 ? 44.186 -39.717 25.288  1.00 28.03 ? 217  VAL   B C   1 
ATOM   3846  O  O   . VAL   B  1 217 ? 44.428 -39.497 24.100  1.00 30.34 ? 217  VAL   B O   1 
ATOM   3847  C  CB  . VAL   B  1 217 ? 41.946 -40.574 26.008  1.00 29.60 ? 217  VAL   B CB  1 
ATOM   3848  C  CG1 . VAL   B  1 217 ? 40.643 -40.188 26.676  1.00 32.86 ? 217  VAL   B CG1 1 
ATOM   3849  C  CG2 . VAL   B  1 217 ? 41.745 -41.175 24.604  1.00 27.67 ? 217  VAL   B CG2 1 
ATOM   3850  N  N   . SER   B  1 218 ? 45.069 -40.321 26.098  1.00 29.05 ? 218  SER   B N   1 
ATOM   3851  C  CA  . SER   B  1 218 ? 46.350 -40.715 25.518  1.00 28.82 ? 218  SER   B CA  1 
ATOM   3852  C  C   . SER   B  1 218 ? 46.265 -42.090 24.831  1.00 27.06 ? 218  SER   B C   1 
ATOM   3853  O  O   . SER   B  1 218 ? 45.450 -42.940 25.192  1.00 25.01 ? 218  SER   B O   1 
ATOM   3854  C  CB  . SER   B  1 218 ? 47.444 -40.732 26.586  1.00 30.54 ? 218  SER   B CB  1 
ATOM   3855  O  OG  . SER   B  1 218 ? 47.284 -41.813 27.503  1.00 28.55 ? 218  SER   B OG  1 
ATOM   3856  N  N   . SER   B  1 219 ? 47.201 -42.337 23.896  1.00 30.20 ? 219  SER   B N   1 
ATOM   3857  C  CA  . SER   B  1 219 ? 47.339 -43.676 23.316  1.00 28.45 ? 219  SER   B CA  1 
ATOM   3858  C  C   . SER   B  1 219 ? 47.584 -44.726 24.396  1.00 25.45 ? 219  SER   B C   1 
ATOM   3859  O  O   . SER   B  1 219 ? 47.011 -45.820 24.346  1.00 27.10 ? 219  SER   B O   1 
ATOM   3860  C  CB  . SER   B  1 219 ? 48.478 -43.724 22.306  1.00 33.48 ? 219  SER   B CB  1 
ATOM   3861  O  OG  . SER   B  1 219 ? 48.135 -43.007 21.140  1.00 39.45 ? 219  SER   B OG  1 
ATOM   3862  N  N   . GLU   B  1 220 ? 48.389 -44.394 25.407  1.00 28.96 ? 220  GLU   B N   1 
ATOM   3863  C  CA  . GLU   B  1 220 ? 48.614 -45.341 26.498  1.00 29.41 ? 220  GLU   B CA  1 
ATOM   3864  C  C   . GLU   B  1 220 ? 47.332 -45.664 27.231  1.00 28.14 ? 220  GLU   B C   1 
ATOM   3865  O  O   . GLU   B  1 220 ? 47.103 -46.822 27.574  1.00 27.75 ? 220  GLU   B O   1 
ATOM   3866  C  CB  . GLU   B  1 220 ? 49.652 -44.821 27.505  1.00 36.21 ? 220  GLU   B CB  1 
ATOM   3867  C  CG  . GLU   B  1 220 ? 51.066 -44.691 26.958  1.00 52.34 ? 220  GLU   B CG  1 
ATOM   3868  C  CD  . GLU   B  1 220 ? 51.376 -43.308 26.393  1.00 63.94 ? 220  GLU   B CD  1 
ATOM   3869  O  OE1 . GLU   B  1 220 ? 50.460 -42.452 26.373  1.00 67.68 ? 220  GLU   B OE1 1 
ATOM   3870  O  OE2 . GLU   B  1 220 ? 52.512 -43.083 25.917  1.00 68.85 ? 220  GLU   B OE2 1 
ATOM   3871  N  N   . GLN   B  1 221 ? 46.471 -44.671 27.466  1.00 26.39 ? 221  GLN   B N   1 
ATOM   3872  C  CA  . GLN   B  1 221 ? 45.214 -44.961 28.150  1.00 24.93 ? 221  GLN   B CA  1 
ATOM   3873  C  C   . GLN   B  1 221 ? 44.335 -45.900 27.320  1.00 24.37 ? 221  GLN   B C   1 
ATOM   3874  O  O   . GLN   B  1 221 ? 43.817 -46.896 27.831  1.00 23.51 ? 221  GLN   B O   1 
ATOM   3875  C  CB  . GLN   B  1 221 ? 44.464 -43.676 28.477  1.00 25.13 ? 221  GLN   B CB  1 
ATOM   3876  C  CG  . GLN   B  1 221 ? 45.046 -42.902 29.655  1.00 25.73 ? 221  GLN   B CG  1 
ATOM   3877  C  CD  . GLN   B  1 221 ? 44.335 -41.592 29.918  1.00 27.07 ? 221  GLN   B CD  1 
ATOM   3878  O  OE1 . GLN   B  1 221 ? 44.007 -40.848 28.982  1.00 25.70 ? 221  GLN   B OE1 1 
ATOM   3879  N  NE2 . GLN   B  1 221 ? 44.077 -41.301 31.186  1.00 26.10 ? 221  GLN   B NE2 1 
ATOM   3880  N  N   . VAL   B  1 222 ? 44.159 -45.609 26.018  1.00 22.97 ? 222  VAL   B N   1 
ATOM   3881  C  CA  . VAL   B  1 222 ? 43.356 -46.507 25.206  1.00 22.04 ? 222  VAL   B CA  1 
ATOM   3882  C  C   . VAL   B  1 222 ? 43.970 -47.895 25.129  1.00 23.80 ? 222  VAL   B C   1 
ATOM   3883  O  O   . VAL   B  1 222 ? 43.237 -48.895 25.053  1.00 22.58 ? 222  VAL   B O   1 
ATOM   3884  C  CB  . VAL   B  1 222 ? 43.151 -45.942 23.783  1.00 26.14 ? 222  VAL   B CB  1 
ATOM   3885  C  CG1 . VAL   B  1 222 ? 42.138 -46.839 23.019  1.00 24.63 ? 222  VAL   B CG1 1 
ATOM   3886  C  CG2 . VAL   B  1 222 ? 42.660 -44.545 23.848  1.00 32.07 ? 222  VAL   B CG2 1 
ATOM   3887  N  N   . SER   B  1 223 ? 45.308 -48.002 25.120  1.00 24.48 ? 223  SER   B N   1 
ATOM   3888  C  CA  . SER   B  1 223 ? 45.895 -49.331 25.013  1.00 24.59 ? 223  SER   B CA  1 
ATOM   3889  C  C   . SER   B  1 223 ? 45.501 -50.189 26.208  1.00 24.11 ? 223  SER   B C   1 
ATOM   3890  O  O   . SER   B  1 223 ? 45.439 -51.424 26.108  1.00 23.86 ? 223  SER   B O   1 
ATOM   3891  C  CB  . SER   B  1 223 ? 47.422 -49.252 24.903  1.00 27.03 ? 223  SER   B CB  1 
ATOM   3892  O  OG  . SER   B  1 223 ? 47.981 -48.994 26.189  1.00 32.10 ? 223  SER   B OG  1 
ATOM   3893  N  N   . LYS   B  1 224 ? 45.276 -49.557 27.352  1.00 22.57 ? 224  LYS   B N   1 
ATOM   3894  C  CA  . LYS   B  1 224 ? 44.843 -50.329 28.499  1.00 22.92 ? 224  LYS   B CA  1 
ATOM   3895  C  C   . LYS   B  1 224 ? 43.476 -50.963 28.268  1.00 21.41 ? 224  LYS   B C   1 
ATOM   3896  O  O   . LYS   B  1 224 ? 43.200 -52.034 28.825  1.00 22.28 ? 224  LYS   B O   1 
ATOM   3897  C  CB  . LYS   B  1 224 ? 44.817 -49.458 29.751  1.00 23.10 ? 224  LYS   B CB  1 
ATOM   3898  C  CG  . LYS   B  1 224 ? 46.196 -48.853 30.145  1.00 28.57 ? 224  LYS   B CG  1 
ATOM   3899  C  CD  . LYS   B  1 224 ? 47.181 -49.931 30.434  1.00 34.61 ? 224  LYS   B CD  1 
ATOM   3900  C  CE  . LYS   B  1 224 ? 48.561 -49.347 30.842  1.00 43.22 ? 224  LYS   B CE  1 
ATOM   3901  N  NZ  . LYS   B  1 224 ? 49.626 -50.411 30.826  1.00 48.74 ? 224  LYS   B NZ  1 
ATOM   3902  N  N   . PHE   B  1 225 ? 42.587 -50.307 27.501  1.00 19.80 ? 225  PHE   B N   1 
ATOM   3903  C  CA  . PHE   B  1 225 ? 41.314 -50.950 27.154  1.00 21.51 ? 225  PHE   B CA  1 
ATOM   3904  C  C   . PHE   B  1 225 ? 41.559 -52.287 26.469  1.00 20.05 ? 225  PHE   B C   1 
ATOM   3905  O  O   . PHE   B  1 225 ? 40.813 -53.250 26.657  1.00 20.38 ? 225  PHE   B O   1 
ATOM   3906  C  CB  . PHE   B  1 225 ? 40.486 -50.081 26.185  1.00 20.95 ? 225  PHE   B CB  1 
ATOM   3907  C  CG  . PHE   B  1 225 ? 39.907 -48.795 26.773  1.00 20.71 ? 225  PHE   B CG  1 
ATOM   3908  C  CD1 . PHE   B  1 225 ? 40.070 -48.435 28.092  1.00 24.20 ? 225  PHE   B CD1 1 
ATOM   3909  C  CD2 . PHE   B  1 225 ? 39.238 -47.924 25.936  1.00 22.93 ? 225  PHE   B CD2 1 
ATOM   3910  C  CE1 . PHE   B  1 225 ? 39.563 -47.228 28.583  1.00 25.06 ? 225  PHE   B CE1 1 
ATOM   3911  C  CE2 . PHE   B  1 225 ? 38.694 -46.712 26.420  1.00 26.87 ? 225  PHE   B CE2 1 
ATOM   3912  C  CZ  . PHE   B  1 225 ? 38.843 -46.380 27.752  1.00 23.89 ? 225  PHE   B CZ  1 
ATOM   3913  N  N   . ARG   B  1 226 ? 42.581 -52.337 25.625  1.00 20.30 ? 226  ARG   B N   1 
ATOM   3914  C  CA  . ARG   B  1 226 ? 42.788 -53.491 24.766  1.00 20.08 ? 226  ARG   B CA  1 
ATOM   3915  C  C   . ARG   B  1 226 ? 43.379 -54.665 25.511  1.00 21.59 ? 226  ARG   B C   1 
ATOM   3916  O  O   . ARG   B  1 226 ? 43.457 -55.754 24.923  1.00 23.82 ? 226  ARG   B O   1 
ATOM   3917  C  CB  . ARG   B  1 226 ? 43.681 -53.122 23.588  1.00 19.92 ? 226  ARG   B CB  1 
ATOM   3918  C  CG  . ARG   B  1 226 ? 43.194 -51.894 22.775  1.00 20.31 ? 226  ARG   B CG  1 
ATOM   3919  C  CD  . ARG   B  1 226 ? 43.971 -51.810 21.427  1.00 21.77 ? 226  ARG   B CD  1 
ATOM   3920  N  NE  . ARG   B  1 226 ? 43.590 -50.551 20.752  1.00 22.67 ? 226  ARG   B NE  1 
ATOM   3921  C  CZ  . ARG   B  1 226 ? 44.277 -49.415 20.765  1.00 23.62 ? 226  ARG   B CZ  1 
ATOM   3922  N  NH1 . ARG   B  1 226 ? 45.492 -49.325 21.361  1.00 24.54 ? 226  ARG   B NH1 1 
ATOM   3923  N  NH2 . ARG   B  1 226 ? 43.779 -48.341 20.175  1.00 24.48 ? 226  ARG   B NH2 1 
ATOM   3924  N  N   . LYS   B  1 227 ? 43.757 -54.495 26.803  1.00 20.43 ? 227  LYS   B N   1 
ATOM   3925  C  CA  . LYS   B  1 227 ? 44.241 -55.613 27.593  1.00 21.71 ? 227  LYS   B CA  1 
ATOM   3926  C  C   . LYS   B  1 227 ? 43.116 -56.408 28.249  1.00 20.62 ? 227  LYS   B C   1 
ATOM   3927  O  O   . LYS   B  1 227 ? 43.388 -57.472 28.853  1.00 23.17 ? 227  LYS   B O   1 
ATOM   3928  C  CB  . LYS   B  1 227 ? 45.210 -55.109 28.665  1.00 24.09 ? 227  LYS   B CB  1 
ATOM   3929  C  CG  . LYS   B  1 227 ? 46.465 -54.465 28.090  1.00 26.64 ? 227  LYS   B CG  1 
ATOM   3930  C  CD  . LYS   B  1 227 ? 47.283 -53.885 29.256  1.00 36.93 ? 227  LYS   B CD  1 
ATOM   3931  C  CE  . LYS   B  1 227 ? 47.885 -54.974 30.140  1.00 44.69 ? 227  LYS   B CE  1 
ATOM   3932  N  NZ  . LYS   B  1 227 ? 48.692 -54.391 31.272  1.00 48.81 ? 227  LYS   B NZ  1 
ATOM   3933  N  N   . LEU   B  1 228 ? 41.882 -55.897 28.206  1.00 20.06 ? 228  LEU   B N   1 
ATOM   3934  C  CA  . LEU   B  1 228 ? 40.741 -56.731 28.572  1.00 19.47 ? 228  LEU   B CA  1 
ATOM   3935  C  C   . LEU   B  1 228 ? 40.547 -57.838 27.543  1.00 19.94 ? 228  LEU   B C   1 
ATOM   3936  O  O   . LEU   B  1 228 ? 41.025 -57.738 26.393  1.00 19.82 ? 228  LEU   B O   1 
ATOM   3937  C  CB  . LEU   B  1 228 ? 39.468 -55.875 28.615  1.00 20.48 ? 228  LEU   B CB  1 
ATOM   3938  C  CG  . LEU   B  1 228 ? 39.545 -54.765 29.672  1.00 20.44 ? 228  LEU   B CG  1 
ATOM   3939  C  CD1 . LEU   B  1 228 ? 38.466 -53.728 29.392  1.00 21.58 ? 228  LEU   B CD1 1 
ATOM   3940  C  CD2 . LEU   B  1 228 ? 39.309 -55.348 31.025  1.00 24.26 ? 228  LEU   B CD2 1 
ATOM   3941  N  N   . ASN   B  1 229 ? 39.779 -58.861 27.949  1.00 18.96 ? 229  ASN   B N   1 
ATOM   3942  C  CA  . ASN   B  1 229 ? 39.464 -60.025 27.119  1.00 19.30 ? 229  ASN   B CA  1 
ATOM   3943  C  C   . ASN   B  1 229 ? 37.941 -60.201 27.016  1.00 19.85 ? 229  ASN   B C   1 
ATOM   3944  O  O   . ASN   B  1 229 ? 37.208 -59.993 27.997  1.00 20.17 ? 229  ASN   B O   1 
ATOM   3945  C  CB  . ASN   B  1 229 ? 40.086 -61.313 27.710  1.00 22.36 ? 229  ASN   B CB  1 
ATOM   3946  C  CG  . ASN   B  1 229 ? 41.590 -61.407 27.496  1.00 28.04 ? 229  ASN   B CG  1 
ATOM   3947  O  OD1 . ASN   B  1 229 ? 42.181 -60.598 26.813  1.00 28.48 ? 229  ASN   B OD1 1 
ATOM   3948  N  ND2 . ASN   B  1 229 ? 42.203 -62.442 28.066  1.00 34.29 ? 229  ASN   B ND2 1 
ATOM   3949  N  N   . PHE   B  1 230 ? 37.477 -60.620 25.829  1.00 18.50 ? 230  PHE   B N   1 
ATOM   3950  C  CA  . PHE   B  1 230 ? 36.071 -61.008 25.688  1.00 18.11 ? 230  PHE   B CA  1 
ATOM   3951  C  C   . PHE   B  1 230 ? 35.764 -62.302 26.394  1.00 20.41 ? 230  PHE   B C   1 
ATOM   3952  O  O   . PHE   B  1 230 ? 34.630 -62.504 26.847  1.00 20.94 ? 230  PHE   B O   1 
ATOM   3953  C  CB  . PHE   B  1 230 ? 35.696 -61.234 24.223  1.00 18.25 ? 230  PHE   B CB  1 
ATOM   3954  C  CG  . PHE   B  1 230 ? 35.679 -59.999 23.355  1.00 17.65 ? 230  PHE   B CG  1 
ATOM   3955  C  CD1 . PHE   B  1 230 ? 34.778 -58.920 23.586  1.00 16.81 ? 230  PHE   B CD1 1 
ATOM   3956  C  CD2 . PHE   B  1 230 ? 36.473 -59.969 22.215  1.00 19.03 ? 230  PHE   B CD2 1 
ATOM   3957  C  CE1 . PHE   B  1 230 ? 34.719 -57.846 22.708  1.00 17.48 ? 230  PHE   B CE1 1 
ATOM   3958  C  CE2 . PHE   B  1 230 ? 36.402 -58.910 21.311  1.00 17.99 ? 230  PHE   B CE2 1 
ATOM   3959  C  CZ  . PHE   B  1 230 ? 35.527 -57.843 21.555  1.00 18.14 ? 230  PHE   B CZ  1 
ATOM   3960  N  N   . ASN   B  1 231 ? 36.719 -63.234 26.410  1.00 19.99 ? 231  ASN   B N   1 
ATOM   3961  C  CA  . ASN   B  1 231 ? 36.460 -64.581 26.883  1.00 21.95 ? 231  ASN   B CA  1 
ATOM   3962  C  C   . ASN   B  1 231 ? 36.389 -64.671 28.417  1.00 22.81 ? 231  ASN   B C   1 
ATOM   3963  O  O   . ASN   B  1 231 ? 36.816 -63.781 29.161  1.00 22.18 ? 231  ASN   B O   1 
ATOM   3964  C  CB  . ASN   B  1 231 ? 37.561 -65.507 26.385  1.00 23.23 ? 231  ASN   B CB  1 
ATOM   3965  C  CG  . ASN   B  1 231 ? 38.941 -65.012 26.812  1.00 22.81 ? 231  ASN   B CG  1 
ATOM   3966  O  OD1 . ASN   B  1 231 ? 39.458 -64.083 26.236  1.00 23.57 ? 231  ASN   B OD1 1 
ATOM   3967  N  ND2 . ASN   B  1 231 ? 39.536 -65.660 27.817  1.00 24.79 ? 231  ASN   B ND2 1 
ATOM   3968  N  N   . GLY   B  1 232 ? 35.796 -65.772 28.883  1.00 23.69 ? 232  GLY   B N   1 
ATOM   3969  C  CA  . GLY   B  1 232 ? 35.902 -66.146 30.277  1.00 27.23 ? 232  GLY   B CA  1 
ATOM   3970  C  C   . GLY   B  1 232 ? 37.200 -66.857 30.567  1.00 26.91 ? 232  GLY   B C   1 
ATOM   3971  O  O   . GLY   B  1 232 ? 37.888 -67.367 29.682  1.00 29.21 ? 232  GLY   B O   1 
ATOM   3972  N  N   . GLU   B  1 233 ? 37.533 -66.920 31.849  1.00 29.22 ? 233  GLU   B N   1 
ATOM   3973  C  CA  . GLU   B  1 233 ? 38.731 -67.636 32.285  1.00 36.40 ? 233  GLU   B CA  1 
ATOM   3974  C  C   . GLU   B  1 233 ? 38.677 -69.102 31.834  1.00 33.02 ? 233  GLU   B C   1 
ATOM   3975  O  O   . GLU   B  1 233 ? 37.636 -69.750 31.918  1.00 35.79 ? 233  GLU   B O   1 
ATOM   3976  C  CB  . GLU   B  1 233 ? 38.825 -67.506 33.811  1.00 42.46 ? 233  GLU   B CB  1 
ATOM   3977  C  CG  . GLU   B  1 233 ? 40.215 -67.597 34.398  1.00 51.14 ? 233  GLU   B CG  1 
ATOM   3978  C  CD  . GLU   B  1 233 ? 40.241 -67.297 35.911  1.00 59.56 ? 233  GLU   B CD  1 
ATOM   3979  O  OE1 . GLU   B  1 233 ? 40.146 -66.106 36.318  1.00 59.52 ? 233  GLU   B OE1 1 
ATOM   3980  O  OE2 . GLU   B  1 233 ? 40.361 -68.266 36.699  1.00 64.95 ? 233  GLU   B OE2 1 
ATOM   3981  N  N   . GLY   B  1 234 ? 39.787 -69.634 31.297  1.00 33.84 ? 234  GLY   B N   1 
ATOM   3982  C  CA  . GLY   B  1 234 ? 39.796 -71.020 30.835  1.00 35.71 ? 234  GLY   B CA  1 
ATOM   3983  C  C   . GLY   B  1 234 ? 39.348 -71.243 29.400  1.00 35.52 ? 234  GLY   B C   1 
ATOM   3984  O  O   . GLY   B  1 234 ? 39.380 -72.392 28.914  1.00 36.55 ? 234  GLY   B O   1 
ATOM   3985  N  N   . GLU   B  1 235 ? 38.987 -70.180 28.692  1.00 35.09 ? 235  GLU   B N   1 
ATOM   3986  C  CA  . GLU   B  1 235 ? 38.681 -70.233 27.276  1.00 33.80 ? 235  GLU   B CA  1 
ATOM   3987  C  C   . GLU   B  1 235 ? 39.797 -69.592 26.475  1.00 35.23 ? 235  GLU   B C   1 
ATOM   3988  O  O   . GLU   B  1 235 ? 40.582 -68.810 27.020  1.00 33.56 ? 235  GLU   B O   1 
ATOM   3989  C  CB  . GLU   B  1 235 ? 37.369 -69.512 27.006  1.00 34.02 ? 235  GLU   B CB  1 
ATOM   3990  C  CG  . GLU   B  1 235 ? 36.244 -69.983 27.910  1.00 35.61 ? 235  GLU   B CG  1 
ATOM   3991  C  CD  . GLU   B  1 235 ? 34.930 -69.273 27.590  1.00 38.87 ? 235  GLU   B CD  1 
ATOM   3992  O  OE1 . GLU   B  1 235 ? 33.860 -69.939 27.578  1.00 42.68 ? 235  GLU   B OE1 1 
ATOM   3993  O  OE2 . GLU   B  1 235 ? 34.973 -68.059 27.319  1.00 31.54 ? 235  GLU   B OE2 1 
ATOM   3994  N  N   . PRO   B  1 236 ? 39.914 -69.899 25.174  1.00 35.31 ? 236  PRO   B N   1 
ATOM   3995  C  CA  . PRO   B  1 236 ? 41.017 -69.316 24.397  1.00 36.09 ? 236  PRO   B CA  1 
ATOM   3996  C  C   . PRO   B  1 236 ? 40.945 -67.804 24.450  1.00 31.38 ? 236  PRO   B C   1 
ATOM   3997  O  O   . PRO   B  1 236 ? 39.861 -67.222 24.391  1.00 29.11 ? 236  PRO   B O   1 
ATOM   3998  C  CB  . PRO   B  1 236 ? 40.792 -69.858 22.979  1.00 39.23 ? 236  PRO   B CB  1 
ATOM   3999  C  CG  . PRO   B  1 236 ? 40.061 -71.193 23.218  1.00 40.23 ? 236  PRO   B CG  1 
ATOM   4000  C  CD  . PRO   B  1 236 ? 39.142 -70.892 24.398  1.00 37.09 ? 236  PRO   B CD  1 
ATOM   4001  N  N   . GLU   B  1 237 ? 42.113 -67.178 24.567  1.00 35.38 ? 237  GLU   B N   1 
ATOM   4002  C  CA  . GLU   B  1 237 ? 42.164 -65.736 24.779  1.00 36.98 ? 237  GLU   B CA  1 
ATOM   4003  C  C   . GLU   B  1 237 ? 41.665 -64.986 23.553  1.00 32.68 ? 237  GLU   B C   1 
ATOM   4004  O  O   . GLU   B  1 237 ? 42.095 -65.240 22.425  1.00 33.97 ? 237  GLU   B O   1 
ATOM   4005  C  CB  . GLU   B  1 237 ? 43.585 -65.282 25.110  1.00 43.37 ? 237  GLU   B CB  1 
ATOM   4006  C  CG  . GLU   B  1 237 ? 43.736 -63.771 25.014  1.00 49.85 ? 237  GLU   B CG  1 
ATOM   4007  C  CD  . GLU   B  1 237 ? 44.923 -63.226 25.804  1.00 58.35 ? 237  GLU   B CD  1 
ATOM   4008  O  OE1 . GLU   B  1 237 ? 45.012 -63.493 27.029  1.00 60.30 ? 237  GLU   B OE1 1 
ATOM   4009  O  OE2 . GLU   B  1 237 ? 45.769 -62.530 25.189  1.00 61.39 ? 237  GLU   B OE2 1 
ATOM   4010  N  N   . GLU   B  1 238 ? 40.751 -64.054 23.772  1.00 26.61 ? 238  GLU   B N   1 
ATOM   4011  C  CA  . GLU   B  1 238 ? 40.248 -63.188 22.707  1.00 25.03 ? 238  GLU   B CA  1 
ATOM   4012  C  C   . GLU   B  1 238 ? 40.350 -61.758 23.200  1.00 24.07 ? 238  GLU   B C   1 
ATOM   4013  O  O   . GLU   B  1 238 ? 39.462 -61.313 23.942  1.00 24.41 ? 238  GLU   B O   1 
ATOM   4014  C  CB  . GLU   B  1 238 ? 38.808 -63.490 22.341  1.00 26.86 ? 238  GLU   B CB  1 
ATOM   4015  C  CG  . GLU   B  1 238 ? 38.559 -64.947 21.951  1.00 33.17 ? 238  GLU   B CG  1 
ATOM   4016  C  CD  . GLU   B  1 238 ? 37.071 -65.277 21.910  1.00 41.99 ? 238  GLU   B CD  1 
ATOM   4017  O  OE1 . GLU   B  1 238 ? 36.248 -64.374 22.185  1.00 43.44 ? 238  GLU   B OE1 1 
ATOM   4018  O  OE2 . GLU   B  1 238 ? 36.713 -66.443 21.618  1.00 45.74 ? 238  GLU   B OE2 1 
ATOM   4019  N  N   . PRO   B  1 239 ? 41.354 -61.005 22.765  1.00 23.83 ? 239  PRO   B N   1 
ATOM   4020  C  CA  . PRO   B  1 239 ? 41.471 -59.609 23.216  1.00 23.13 ? 239  PRO   B CA  1 
ATOM   4021  C  C   . PRO   B  1 239 ? 40.200 -58.814 22.931  1.00 19.98 ? 239  PRO   B C   1 
ATOM   4022  O  O   . PRO   B  1 239 ? 39.612 -58.909 21.854  1.00 21.16 ? 239  PRO   B O   1 
ATOM   4023  C  CB  . PRO   B  1 239 ? 42.661 -59.070 22.413  1.00 24.77 ? 239  PRO   B CB  1 
ATOM   4024  C  CG  . PRO   B  1 239 ? 43.504 -60.341 22.114  1.00 27.95 ? 239  PRO   B CG  1 
ATOM   4025  C  CD  . PRO   B  1 239 ? 42.489 -61.436 21.925  1.00 26.03 ? 239  PRO   B CD  1 
ATOM   4026  N  N   . MET   B  1 240 ? 39.813 -57.997 23.911  1.00 19.03 ? 240  MET   B N   1 
ATOM   4027  C  CA  . MET   B  1 240 ? 38.607 -57.183 23.786  1.00 17.28 ? 240  MET   B CA  1 
ATOM   4028  C  C   . MET   B  1 240 ? 39.020 -55.942 22.981  1.00 19.34 ? 240  MET   B C   1 
ATOM   4029  O  O   . MET   B  1 240 ? 39.504 -54.950 23.540  1.00 17.79 ? 240  MET   B O   1 
ATOM   4030  C  CB  . MET   B  1 240 ? 38.077 -56.812 25.174  1.00 16.80 ? 240  MET   B CB  1 
ATOM   4031  C  CG  . MET   B  1 240 ? 36.704 -56.055 25.053  1.00 18.08 ? 240  MET   B CG  1 
ATOM   4032  S  SD  . MET   B  1 240 ? 36.076 -55.582 26.666  1.00 18.13 ? 240  MET   B SD  1 
ATOM   4033  C  CE  . MET   B  1 240 ? 35.334 -57.140 27.139  1.00 17.78 ? 240  MET   B CE  1 
ATOM   4034  N  N   . VAL   B  1 241 ? 38.845 -56.025 21.661  1.00 18.42 ? 241  VAL   B N   1 
ATOM   4035  C  CA  . VAL   B  1 241 ? 39.149 -54.943 20.727  1.00 17.58 ? 241  VAL   B CA  1 
ATOM   4036  C  C   . VAL   B  1 241 ? 38.076 -54.972 19.633  1.00 17.55 ? 241  VAL   B C   1 
ATOM   4037  O  O   . VAL   B  1 241 ? 37.454 -56.004 19.367  1.00 18.13 ? 241  VAL   B O   1 
ATOM   4038  C  CB  . VAL   B  1 241 ? 40.548 -55.057 20.089  1.00 20.00 ? 241  VAL   B CB  1 
ATOM   4039  C  CG1 . VAL   B  1 241 ? 41.663 -54.936 21.183  1.00 19.50 ? 241  VAL   B CG1 1 
ATOM   4040  C  CG2 . VAL   B  1 241 ? 40.680 -56.335 19.270  1.00 19.27 ? 241  VAL   B CG2 1 
ATOM   4041  N  N   . ASP   B  1 242 ? 37.868 -53.812 18.988  1.00 17.52 ? 242  ASP   B N   1 
ATOM   4042  C  CA  . ASP   B  1 242 ? 36.896 -53.709 17.866  1.00 17.61 ? 242  ASP   B CA  1 
ATOM   4043  C  C   . ASP   B  1 242 ? 35.500 -54.154 18.319  1.00 16.13 ? 242  ASP   B C   1 
ATOM   4044  O  O   . ASP   B  1 242 ? 34.781 -54.896 17.631  1.00 17.74 ? 242  ASP   B O   1 
ATOM   4045  C  CB  . ASP   B  1 242 ? 37.383 -54.484 16.629  1.00 19.25 ? 242  ASP   B CB  1 
ATOM   4046  C  CG  . ASP   B  1 242 ? 38.615 -53.810 15.998  1.00 20.46 ? 242  ASP   B CG  1 
ATOM   4047  O  OD1 . ASP   B  1 242 ? 38.657 -52.549 15.989  1.00 18.93 ? 242  ASP   B OD1 1 
ATOM   4048  O  OD2 . ASP   B  1 242 ? 39.519 -54.547 15.549  1.00 23.10 ? 242  ASP   B OD2 1 
ATOM   4049  N  N   . ASN   B  1 243 ? 35.096 -53.653 19.484  1.00 15.15 ? 243  ASN   B N   1 
ATOM   4050  C  CA  . ASN   B  1 243 ? 33.748 -53.885 20.010  1.00 15.24 ? 243  ASN   B CA  1 
ATOM   4051  C  C   . ASN   B  1 243 ? 32.826 -52.737 19.628  1.00 16.92 ? 243  ASN   B C   1 
ATOM   4052  O  O   . ASN   B  1 243 ? 32.137 -52.163 20.468  1.00 16.75 ? 243  ASN   B O   1 
ATOM   4053  C  CB  . ASN   B  1 243 ? 33.762 -54.108 21.531  1.00 16.51 ? 243  ASN   B CB  1 
ATOM   4054  C  CG  . ASN   B  1 243 ? 34.475 -52.999 22.334  1.00 15.85 ? 243  ASN   B CG  1 
ATOM   4055  O  OD1 . ASN   B  1 243 ? 35.002 -52.055 21.768  1.00 17.72 ? 243  ASN   B OD1 1 
ATOM   4056  N  ND2 . ASN   B  1 243 ? 34.435 -53.136 23.688  1.00 17.14 ? 243  ASN   B ND2 1 
ATOM   4057  N  N   . TRP   B  1 244 ? 32.835 -52.445 18.336  1.00 16.75 ? 244  TRP   B N   1 
ATOM   4058  C  CA  . TRP   B  1 244 ? 31.991 -51.402 17.743  1.00 16.58 ? 244  TRP   B CA  1 
ATOM   4059  C  C   . TRP   B  1 244 ? 31.165 -51.986 16.617  1.00 17.63 ? 244  TRP   B C   1 
ATOM   4060  O  O   . TRP   B  1 244 ? 31.559 -52.947 15.942  1.00 18.66 ? 244  TRP   B O   1 
ATOM   4061  C  CB  . TRP   B  1 244 ? 32.841 -50.232 17.195  1.00 17.81 ? 244  TRP   B CB  1 
ATOM   4062  C  CG  . TRP   B  1 244 ? 33.993 -50.648 16.310  1.00 19.11 ? 244  TRP   B CG  1 
ATOM   4063  C  CD1 . TRP   B  1 244 ? 35.277 -50.883 16.723  1.00 19.59 ? 244  TRP   B CD1 1 
ATOM   4064  C  CD2 . TRP   B  1 244 ? 33.984 -50.852 14.869  1.00 22.09 ? 244  TRP   B CD2 1 
ATOM   4065  N  NE1 . TRP   B  1 244 ? 36.065 -51.224 15.632  1.00 18.42 ? 244  TRP   B NE1 1 
ATOM   4066  C  CE2 . TRP   B  1 244 ? 35.289 -51.229 14.491  1.00 22.76 ? 244  TRP   B CE2 1 
ATOM   4067  C  CE3 . TRP   B  1 244 ? 32.979 -50.806 13.866  1.00 22.13 ? 244  TRP   B CE3 1 
ATOM   4068  C  CZ2 . TRP   B  1 244 ? 35.653 -51.540 13.141  1.00 26.85 ? 244  TRP   B CZ2 1 
ATOM   4069  C  CZ3 . TRP   B  1 244 ? 33.329 -51.114 12.530  1.00 25.05 ? 244  TRP   B CZ3 1 
ATOM   4070  C  CH2 . TRP   B  1 244 ? 34.662 -51.455 12.175  1.00 25.45 ? 244  TRP   B CH2 1 
ATOM   4071  N  N   . ARG   B  1 245 ? 29.976 -51.410 16.453  1.00 16.80 ? 245  ARG   B N   1 
ATOM   4072  C  CA  . ARG   B  1 245 ? 29.090 -51.730 15.313  1.00 15.34 ? 245  ARG   B CA  1 
ATOM   4073  C  C   . ARG   B  1 245 ? 29.352 -50.762 14.154  1.00 16.36 ? 245  ARG   B C   1 
ATOM   4074  O  O   . ARG   B  1 245 ? 29.483 -49.567 14.407  1.00 18.01 ? 245  ARG   B O   1 
ATOM   4075  C  CB  . ARG   B  1 245 ? 27.616 -51.610 15.751  1.00 14.63 ? 245  ARG   B CB  1 
ATOM   4076  C  CG  . ARG   B  1 245 ? 26.676 -52.177 14.679  1.00 13.85 ? 245  ARG   B CG  1 
ATOM   4077  C  CD  . ARG   B  1 245 ? 25.207 -51.904 15.009  1.00 15.63 ? 245  ARG   B CD  1 
ATOM   4078  N  NE  . ARG   B  1 245 ? 24.417 -52.667 14.046  1.00 14.78 ? 245  ARG   B NE  1 
ATOM   4079  C  CZ  . ARG   B  1 245 ? 23.106 -52.513 13.869  1.00 13.73 ? 245  ARG   B CZ  1 
ATOM   4080  N  NH1 . ARG   B  1 245 ? 22.404 -51.548 14.508  1.00 14.01 ? 245  ARG   B NH1 1 
ATOM   4081  N  NH2 . ARG   B  1 245 ? 22.461 -53.344 12.987  1.00 14.72 ? 245  ARG   B NH2 1 
ATOM   4082  N  N   . PRO   B  1 246 ? 29.406 -51.258 12.890  1.00 17.75 ? 246  PRO   B N   1 
ATOM   4083  C  CA  . PRO   B  1 246 ? 29.510 -50.350 11.706  1.00 18.89 ? 246  PRO   B CA  1 
ATOM   4084  C  C   . PRO   B  1 246 ? 28.315 -49.407 11.661  1.00 16.98 ? 246  PRO   B C   1 
ATOM   4085  O  O   . PRO   B  1 246 ? 27.245 -49.706 12.199  1.00 16.65 ? 246  PRO   B O   1 
ATOM   4086  C  CB  . PRO   B  1 246 ? 29.504 -51.294 10.489  1.00 21.98 ? 246  PRO   B CB  1 
ATOM   4087  C  CG  . PRO   B  1 246 ? 29.971 -52.651 11.018  1.00 19.52 ? 246  PRO   B CG  1 
ATOM   4088  C  CD  . PRO   B  1 246 ? 29.420 -52.686 12.492  1.00 20.23 ? 246  PRO   B CD  1 
ATOM   4089  N  N   . THR   B  1 247 ? 28.515 -48.239 11.064  1.00 18.96 ? 247  THR   B N   1 
ATOM   4090  C  CA  . THR   B  1 247 ? 27.396 -47.320 10.907  1.00 17.66 ? 247  THR   B CA  1 
ATOM   4091  C  C   . THR   B  1 247 ? 26.346 -47.906 9.960   1.00 17.04 ? 247  THR   B C   1 
ATOM   4092  O  O   . THR   B  1 247 ? 26.638 -48.684 9.030   1.00 19.05 ? 247  THR   B O   1 
ATOM   4093  C  CB  . THR   B  1 247 ? 27.832 -45.942 10.375  1.00 18.59 ? 247  THR   B CB  1 
ATOM   4094  O  OG1 . THR   B  1 247 ? 28.583 -46.095 9.168   1.00 19.53 ? 247  THR   B OG1 1 
ATOM   4095  C  CG2 . THR   B  1 247 ? 28.719 -45.236 11.414  1.00 19.57 ? 247  THR   B CG2 1 
ATOM   4096  N  N   . GLN   B  1 248 ? 25.096 -47.573 10.258  1.00 16.86 ? 248  GLN   B N   1 
ATOM   4097  C  CA  . GLN   B  1 248 ? 23.905 -48.110 9.616   1.00 14.49 ? 248  GLN   B CA  1 
ATOM   4098  C  C   . GLN   B  1 248 ? 23.197 -47.028 8.811   1.00 16.49 ? 248  GLN   B C   1 
ATOM   4099  O  O   . GLN   B  1 248 ? 23.404 -45.838 9.043   1.00 17.52 ? 248  GLN   B O   1 
ATOM   4100  C  CB  . GLN   B  1 248 ? 22.941 -48.703 10.667  1.00 14.98 ? 248  GLN   B CB  1 
ATOM   4101  C  CG  . GLN   B  1 248 ? 23.593 -49.823 11.534  1.00 15.88 ? 248  GLN   B CG  1 
ATOM   4102  C  CD  . GLN   B  1 248 ? 24.028 -50.982 10.638  1.00 15.64 ? 248  GLN   B CD  1 
ATOM   4103  O  OE1 . GLN   B  1 248 ? 23.277 -51.461 9.775   1.00 18.58 ? 248  GLN   B OE1 1 
ATOM   4104  N  NE2 . GLN   B  1 248 ? 25.296 -51.355 10.786  1.00 15.83 ? 248  GLN   B NE2 1 
ATOM   4105  N  N   . PRO   B  1 249 ? 22.349 -47.403 7.854   1.00 16.37 ? 249  PRO   B N   1 
ATOM   4106  C  CA  . PRO   B  1 249 ? 21.692 -46.409 6.997   1.00 17.68 ? 249  PRO   B CA  1 
ATOM   4107  C  C   . PRO   B  1 249 ? 20.784 -45.499 7.822   1.00 18.03 ? 249  PRO   B C   1 
ATOM   4108  O  O   . PRO   B  1 249 ? 20.025 -45.962 8.676   1.00 18.04 ? 249  PRO   B O   1 
ATOM   4109  C  CB  . PRO   B  1 249 ? 20.864 -47.267 6.035   1.00 19.65 ? 249  PRO   B CB  1 
ATOM   4110  C  CG  . PRO   B  1 249 ? 21.588 -48.603 5.999   1.00 19.66 ? 249  PRO   B CG  1 
ATOM   4111  C  CD  . PRO   B  1 249 ? 22.057 -48.792 7.422   1.00 17.80 ? 249  PRO   B CD  1 
ATOM   4112  N  N   . LEU   B  1 250 ? 20.853 -44.211 7.541   1.00 18.23 ? 250  LEU   B N   1 
ATOM   4113  C  CA  . LEU   B  1 250 ? 19.971 -43.257 8.211   1.00 18.69 ? 250  LEU   B CA  1 
ATOM   4114  C  C   . LEU   B  1 250 ? 18.513 -43.473 7.819   1.00 18.72 ? 250  LEU   B C   1 
ATOM   4115  O  O   . LEU   B  1 250 ? 17.599 -43.175 8.613   1.00 20.79 ? 250  LEU   B O   1 
ATOM   4116  C  CB  . LEU   B  1 250 ? 20.424 -41.822 7.856   1.00 22.36 ? 250  LEU   B CB  1 
ATOM   4117  C  CG  . LEU   B  1 250 ? 19.844 -40.663 8.657   1.00 24.84 ? 250  LEU   B CG  1 
ATOM   4118  C  CD1 . LEU   B  1 250 ? 20.027 -40.885 10.159  1.00 22.68 ? 250  LEU   B CD1 1 
ATOM   4119  C  CD2 . LEU   B  1 250 ? 20.501 -39.327 8.198   1.00 25.71 ? 250  LEU   B CD2 1 
ATOM   4120  N  N   . LYS   B  1 251 ? 18.237 -43.942 6.581   1.00 18.21 ? 251  LYS   B N   1 
ATOM   4121  C  CA  . LYS   B  1 251 ? 16.876 -44.131 6.116   1.00 19.64 ? 251  LYS   B CA  1 
ATOM   4122  C  C   . LYS   B  1 251 ? 16.089 -42.840 6.300   1.00 22.60 ? 251  LYS   B C   1 
ATOM   4123  O  O   . LYS   B  1 251 ? 16.587 -41.760 5.941   1.00 23.66 ? 251  LYS   B O   1 
ATOM   4124  C  CB  . LYS   B  1 251 ? 16.245 -45.353 6.789   1.00 20.01 ? 251  LYS   B CB  1 
ATOM   4125  C  CG  . LYS   B  1 251 ? 17.074 -46.644 6.479   1.00 25.63 ? 251  LYS   B CG  1 
ATOM   4126  C  CD  . LYS   B  1 251 ? 16.385 -47.957 6.851   1.00 27.89 ? 251  LYS   B CD  1 
ATOM   4127  C  CE  . LYS   B  1 251 ? 17.300 -49.128 6.509   1.00 32.67 ? 251  LYS   B CE  1 
ATOM   4128  N  NZ  . LYS   B  1 251 ? 16.708 -50.457 6.814   1.00 33.71 ? 251  LYS   B NZ  1 
ATOM   4129  N  N   . ASN   B  1 252 ? 14.850 -42.918 6.784   1.00 21.57 ? 252  ASN   B N   1 
ATOM   4130  C  CA  . ASN   B  1 252 ? 13.957 -41.776 6.763   1.00 24.89 ? 252  ASN   B CA  1 
ATOM   4131  C  C   . ASN   B  1 252 ? 14.028 -41.079 8.114   1.00 28.05 ? 252  ASN   B C   1 
ATOM   4132  O  O   . ASN   B  1 252 ? 13.040 -41.043 8.873   1.00 31.54 ? 252  ASN   B O   1 
ATOM   4133  C  CB  . ASN   B  1 252 ? 12.537 -42.224 6.426   1.00 30.31 ? 252  ASN   B CB  1 
ATOM   4134  C  CG  . ASN   B  1 252 ? 11.658 -41.079 6.110   1.00 35.94 ? 252  ASN   B CG  1 
ATOM   4135  O  OD1 . ASN   B  1 252 ? 12.124 -39.937 5.992   1.00 34.38 ? 252  ASN   B OD1 1 
ATOM   4136  N  ND2 . ASN   B  1 252 ? 10.362 -41.348 5.982   1.00 39.74 ? 252  ASN   B ND2 1 
ATOM   4137  N  N   . ARG   B  1 253 ? 15.237 -40.573 8.417   1.00 23.17 ? 253  ARG   B N   1 
ATOM   4138  C  CA  . ARG   B  1 253 ? 15.520 -39.849 9.659   1.00 22.32 ? 253  ARG   B CA  1 
ATOM   4139  C  C   . ARG   B  1 253 ? 16.319 -38.584 9.353   1.00 23.52 ? 253  ARG   B C   1 
ATOM   4140  O  O   . ARG   B  1 253 ? 16.954 -38.474 8.296   1.00 25.41 ? 253  ARG   B O   1 
ATOM   4141  C  CB  . ARG   B  1 253 ? 16.307 -40.716 10.702  1.00 19.97 ? 253  ARG   B CB  1 
ATOM   4142  C  CG  . ARG   B  1 253 ? 15.470 -41.855 11.208  1.00 19.99 ? 253  ARG   B CG  1 
ATOM   4143  C  CD  . ARG   B  1 253 ? 16.261 -42.751 12.163  1.00 18.31 ? 253  ARG   B CD  1 
ATOM   4144  N  NE  . ARG   B  1 253 ? 17.314 -43.454 11.445  1.00 18.45 ? 253  ARG   B NE  1 
ATOM   4145  C  CZ  . ARG   B  1 253 ? 18.240 -44.209 12.026  1.00 17.27 ? 253  ARG   B CZ  1 
ATOM   4146  N  NH1 . ARG   B  1 253 ? 18.317 -44.298 13.364  1.00 18.37 ? 253  ARG   B NH1 1 
ATOM   4147  N  NH2 . ARG   B  1 253 ? 19.105 -44.886 11.284  1.00 16.52 ? 253  ARG   B NH2 1 
ATOM   4148  N  N   . GLN   B  1 254 ? 16.278 -37.636 10.293  1.00 22.99 ? 254  GLN   B N   1 
ATOM   4149  C  CA  . GLN   B  1 254 ? 16.987 -36.357 10.190  1.00 27.11 ? 254  GLN   B CA  1 
ATOM   4150  C  C   . GLN   B  1 254 ? 17.838 -36.210 11.435  1.00 26.14 ? 254  GLN   B C   1 
ATOM   4151  O  O   . GLN   B  1 254 ? 17.365 -36.466 12.555  1.00 29.34 ? 254  GLN   B O   1 
ATOM   4152  C  CB  . GLN   B  1 254 ? 16.024 -35.160 10.056  1.00 32.28 ? 254  GLN   B CB  1 
ATOM   4153  C  CG  . GLN   B  1 254 ? 15.074 -35.342 8.926   1.00 39.62 ? 254  GLN   B CG  1 
ATOM   4154  C  CD  . GLN   B  1 254 ? 13.969 -34.309 8.905   1.00 48.61 ? 254  GLN   B CD  1 
ATOM   4155  O  OE1 . GLN   B  1 254 ? 13.356 -34.016 9.942   1.00 49.88 ? 254  GLN   B OE1 1 
ATOM   4156  N  NE2 . GLN   B  1 254 ? 13.699 -33.754 7.720   1.00 52.73 ? 254  GLN   B NE2 1 
ATOM   4157  N  N   . ILE   B  1 255 ? 19.100 -35.843 11.238  1.00 23.77 ? 255  ILE   B N   1 
ATOM   4158  C  CA  . ILE   B  1 255 ? 19.970 -35.536 12.356  1.00 22.58 ? 255  ILE   B CA  1 
ATOM   4159  C  C   . ILE   B  1 255 ? 19.844 -34.045 12.598  1.00 24.13 ? 255  ILE   B C   1 
ATOM   4160  O  O   . ILE   B  1 255 ? 19.995 -33.241 11.673  1.00 25.26 ? 255  ILE   B O   1 
ATOM   4161  C  CB  . ILE   B  1 255 ? 21.416 -35.982 12.088  1.00 21.97 ? 255  ILE   B CB  1 
ATOM   4162  C  CG1 . ILE   B  1 255 ? 21.445 -37.503 11.822  1.00 24.26 ? 255  ILE   B CG1 1 
ATOM   4163  C  CG2 . ILE   B  1 255 ? 22.310 -35.683 13.306  1.00 23.76 ? 255  ILE   B CG2 1 
ATOM   4164  C  CD1 . ILE   B  1 255 ? 22.866 -38.068 11.535  1.00 24.06 ? 255  ILE   B CD1 1 
ATOM   4165  N  N   . LYS   B  1 256 ? 19.486 -33.670 13.830  1.00 23.82 ? 256  LYS   B N   1 
ATOM   4166  C  CA  . LYS   B  1 256 ? 19.319 -32.266 14.189  1.00 24.53 ? 256  LYS   B CA  1 
ATOM   4167  C  C   . LYS   B  1 256 ? 20.523 -31.808 15.003  1.00 22.55 ? 256  LYS   B C   1 
ATOM   4168  O  O   . LYS   B  1 256 ? 21.142 -32.593 15.710  1.00 24.11 ? 256  LYS   B O   1 
ATOM   4169  C  CB  . LYS   B  1 256 ? 18.031 -32.054 15.003  1.00 24.66 ? 256  LYS   B CB  1 
ATOM   4170  C  CG  . LYS   B  1 256 ? 16.729 -32.429 14.276  1.00 27.33 ? 256  LYS   B CG  1 
ATOM   4171  C  CD  . LYS   B  1 256 ? 16.591 -31.664 12.943  1.00 33.12 ? 256  LYS   B CD  1 
ATOM   4172  C  CE  . LYS   B  1 256 ? 15.206 -31.825 12.344  1.00 38.51 ? 256  LYS   B CE  1 
ATOM   4173  N  NZ  . LYS   B  1 256 ? 15.174 -31.039 11.045  1.00 41.90 ? 256  LYS   B NZ  1 
ATOM   4174  N  N   . ALA   B  1 257 ? 20.875 -30.540 14.868  1.00 25.10 ? 257  ALA   B N   1 
ATOM   4175  C  CA  . ALA   B  1 257 ? 21.938 -29.906 15.642  1.00 26.11 ? 257  ALA   B CA  1 
ATOM   4176  C  C   . ALA   B  1 257 ? 21.361 -28.939 16.668  1.00 26.75 ? 257  ALA   B C   1 
ATOM   4177  O  O   . ALA   B  1 257 ? 20.373 -28.251 16.406  1.00 28.04 ? 257  ALA   B O   1 
ATOM   4178  C  CB  . ALA   B  1 257 ? 22.896 -29.149 14.717  1.00 26.00 ? 257  ALA   B CB  1 
ATOM   4179  N  N   . SER   B  1 258 ? 21.993 -28.903 17.849  1.00 25.88 ? 258  SER   B N   1 
ATOM   4180  C  CA  . SER   B  1 258 ? 21.631 -28.005 18.932  1.00 25.15 ? 258  SER   B CA  1 
ATOM   4181  C  C   . SER   B  1 258 ? 22.143 -26.617 18.692  1.00 29.33 ? 258  SER   B C   1 
ATOM   4182  O  O   . SER   B  1 258 ? 21.752 -25.681 19.412  1.00 30.93 ? 258  SER   B O   1 
ATOM   4183  C  CB  . SER   B  1 258 ? 22.230 -28.527 20.259  1.00 23.87 ? 258  SER   B CB  1 
ATOM   4184  O  OG  . SER   B  1 258 ? 23.639 -28.316 20.283  1.00 24.98 ? 258  SER   B OG  1 
ATOM   4185  N  N   . PHE   B  1 259 ? 23.059 -26.495 17.732  1.00 27.90 ? 259  PHE   B N   1 
ATOM   4186  C  CA  . PHE   B  1 259 ? 23.712 -25.187 17.477  1.00 28.79 ? 259  PHE   B CA  1 
ATOM   4187  C  C   . PHE   B  1 259 ? 23.335 -24.681 16.089  1.00 32.59 ? 259  PHE   B C   1 
ATOM   4188  O  O   . PHE   B  1 259 ? 23.086 -25.487 15.173  1.00 33.47 ? 259  PHE   B O   1 
ATOM   4189  C  CB  . PHE   B  1 259 ? 25.218 -25.412 17.645  1.00 30.11 ? 259  PHE   B CB  1 
ATOM   4190  C  CG  . PHE   B  1 259 ? 25.776 -26.612 16.890  1.00 30.52 ? 259  PHE   B CG  1 
ATOM   4191  C  CD1 . PHE   B  1 259 ? 25.814 -27.872 17.476  1.00 28.73 ? 259  PHE   B CD1 1 
ATOM   4192  C  CD2 . PHE   B  1 259 ? 26.267 -26.475 15.597  1.00 32.58 ? 259  PHE   B CD2 1 
ATOM   4193  C  CE1 . PHE   B  1 259 ? 26.322 -28.961 16.787  1.00 30.17 ? 259  PHE   B CE1 1 
ATOM   4194  C  CE2 . PHE   B  1 259 ? 26.775 -27.567 14.912  1.00 32.02 ? 259  PHE   B CE2 1 
ATOM   4195  C  CZ  . PHE   B  1 259 ? 26.802 -28.806 15.508  1.00 32.96 ? 259  PHE   B CZ  1 
ATOM   4196  N  N   . LYS   B  1 260 ? 23.301 -23.354 15.950  1.00 63.04 ? 260  LYS   B N   1 
ATOM   4197  C  CA  . LYS   B  1 260 ? 23.195 -22.695 14.624  1.00 59.07 ? 260  LYS   B CA  1 
ATOM   4198  C  C   . LYS   B  1 260 ? 24.540 -22.830 13.895  1.00 54.97 ? 260  LYS   B C   1 
ATOM   4199  O  O   . LYS   B  1 260 ? 25.573 -22.885 14.555  1.00 52.55 ? 260  LYS   B O   1 
ATOM   4200  C  CB  . LYS   B  1 260 ? 22.798 -21.226 14.800  1.00 59.80 ? 260  LYS   B CB  1 
ATOM   4201  C  CG  . LYS   B  1 260 ? 21.436 -20.999 15.437  1.00 61.96 ? 260  LYS   B CG  1 
ATOM   4202  C  CD  . LYS   B  1 260 ? 21.207 -19.546 15.831  1.00 65.05 ? 260  LYS   B CD  1 
ATOM   4203  C  CE  . LYS   B  1 260 ? 19.820 -19.283 16.319  1.00 68.12 ? 260  LYS   B CE  1 
ATOM   4204  N  NZ  . LYS   B  1 260 ? 18.836 -19.427 15.244  1.00 69.92 ? 260  LYS   B NZ  1 
ATOM   4205  O  OXT . LYS   B  1 260 ? 24.510 -22.885 12.659  1.00 54.04 ? 260  LYS   B OXT 1 
ATOM   4206  N  N   . ALA   C  1 2   ? 72.438 -13.484 64.339  1.00 17.54 ? 2    ALA   C N   1 
ATOM   4207  C  CA  . ALA   C  1 2   ? 73.369 -14.499 63.808  1.00 16.88 ? 2    ALA   C CA  1 
ATOM   4208  C  C   . ALA   C  1 2   ? 73.110 -14.698 62.332  1.00 17.80 ? 2    ALA   C C   1 
ATOM   4209  O  O   . ALA   C  1 2   ? 72.763 -13.725 61.646  1.00 17.03 ? 2    ALA   C O   1 
ATOM   4210  C  CB  . ALA   C  1 2   ? 73.191 -15.802 64.648  1.00 16.38 ? 2    ALA   C CB  1 
ATOM   4211  N  N   . HIS   C  1 3   ? 73.233 -15.917 61.788  1.00 16.55 ? 3    HIS   C N   1 
ATOM   4212  C  CA  . HIS   C  1 3   ? 73.009 -16.058 60.344  1.00 16.04 ? 3    HIS   C CA  1 
ATOM   4213  C  C   . HIS   C  1 3   ? 71.542 -15.896 59.973  1.00 15.87 ? 3    HIS   C C   1 
ATOM   4214  O  O   . HIS   C  1 3   ? 70.671 -16.469 60.609  1.00 16.97 ? 3    HIS   C O   1 
ATOM   4215  C  CB  . HIS   C  1 3   ? 73.538 -17.421 59.879  1.00 18.00 ? 3    HIS   C CB  1 
ATOM   4216  C  CG  . HIS   C  1 3   ? 75.021 -17.456 59.869  1.00 22.00 ? 3    HIS   C CG  1 
ATOM   4217  N  ND1 . HIS   C  1 3   ? 75.755 -17.736 58.742  1.00 26.19 ? 3    HIS   C ND1 1 
ATOM   4218  C  CD2 . HIS   C  1 3   ? 75.911 -17.129 60.830  1.00 23.87 ? 3    HIS   C CD2 1 
ATOM   4219  C  CE1 . HIS   C  1 3   ? 77.043 -17.638 59.026  1.00 26.74 ? 3    HIS   C CE1 1 
ATOM   4220  N  NE2 . HIS   C  1 3   ? 77.156 -17.268 60.288  1.00 23.75 ? 3    HIS   C NE2 1 
ATOM   4221  N  N   . HIS   C  1 4   ? 71.252 -15.105 58.936  1.00 15.03 ? 4    HIS   C N   1 
ATOM   4222  C  CA  . HIS   C  1 4   ? 69.869 -14.935 58.504  1.00 16.19 ? 4    HIS   C CA  1 
ATOM   4223  C  C   . HIS   C  1 4   ? 69.390 -16.195 57.792  1.00 14.76 ? 4    HIS   C C   1 
ATOM   4224  O  O   . HIS   C  1 4   ? 70.170 -16.922 57.135  1.00 16.13 ? 4    HIS   C O   1 
ATOM   4225  C  CB  . HIS   C  1 4   ? 69.835 -13.667 57.611  1.00 15.31 ? 4    HIS   C CB  1 
ATOM   4226  C  CG  . HIS   C  1 4   ? 68.502 -13.209 57.123  1.00 14.38 ? 4    HIS   C CG  1 
ATOM   4227  N  ND1 . HIS   C  1 4   ? 67.495 -12.747 57.971  1.00 12.14 ? 4    HIS   C ND1 1 
ATOM   4228  C  CD2 . HIS   C  1 4   ? 68.055 -13.041 55.864  1.00 15.81 ? 4    HIS   C CD2 1 
ATOM   4229  C  CE1 . HIS   C  1 4   ? 66.476 -12.340 57.213  1.00 13.15 ? 4    HIS   C CE1 1 
ATOM   4230  N  NE2 . HIS   C  1 4   ? 66.784 -12.526 55.941  1.00 14.51 ? 4    HIS   C NE2 1 
ATOM   4231  N  N   . TRP   C  1 5   ? 68.067 -16.428 57.889  1.00 14.37 ? 5    TRP   C N   1 
ATOM   4232  C  CA  . TRP   C  1 5   ? 67.487 -17.618 57.260  1.00 13.28 ? 5    TRP   C CA  1 
ATOM   4233  C  C   . TRP   C  1 5   ? 67.612 -17.575 55.736  1.00 16.42 ? 5    TRP   C C   1 
ATOM   4234  O  O   . TRP   C  1 5   ? 67.840 -16.523 55.105  1.00 16.23 ? 5    TRP   C O   1 
ATOM   4235  C  CB  . TRP   C  1 5   ? 66.000 -17.750 57.659  1.00 14.69 ? 5    TRP   C CB  1 
ATOM   4236  C  CG  . TRP   C  1 5   ? 65.074 -16.662 57.104  1.00 12.99 ? 5    TRP   C CG  1 
ATOM   4237  C  CD1 . TRP   C  1 5   ? 64.773 -15.462 57.688  1.00 14.77 ? 5    TRP   C CD1 1 
ATOM   4238  C  CD2 . TRP   C  1 5   ? 64.411 -16.702 55.842  1.00 13.18 ? 5    TRP   C CD2 1 
ATOM   4239  N  NE1 . TRP   C  1 5   ? 63.923 -14.746 56.860  1.00 14.39 ? 5    TRP   C NE1 1 
ATOM   4240  C  CE2 . TRP   C  1 5   ? 63.702 -15.465 55.712  1.00 13.22 ? 5    TRP   C CE2 1 
ATOM   4241  C  CE3 . TRP   C  1 5   ? 64.381 -17.615 54.790  1.00 13.31 ? 5    TRP   C CE3 1 
ATOM   4242  C  CZ2 . TRP   C  1 5   ? 62.905 -15.187 54.604  1.00 14.32 ? 5    TRP   C CZ2 1 
ATOM   4243  C  CZ3 . TRP   C  1 5   ? 63.586 -17.352 53.672  1.00 14.99 ? 5    TRP   C CZ3 1 
ATOM   4244  C  CH2 . TRP   C  1 5   ? 62.872 -16.137 53.578  1.00 14.96 ? 5    TRP   C CH2 1 
ATOM   4245  N  N   . GLY   C  1 6   ? 67.517 -18.746 55.153  1.00 14.73 ? 6    GLY   C N   1 
ATOM   4246  C  CA  . GLY   C  1 6   ? 67.604 -18.851 53.710  1.00 15.21 ? 6    GLY   C CA  1 
ATOM   4247  C  C   . GLY   C  1 6   ? 67.038 -20.195 53.219  1.00 13.73 ? 6    GLY   C C   1 
ATOM   4248  O  O   . GLY   C  1 6   ? 66.093 -20.752 53.790  1.00 15.19 ? 6    GLY   C O   1 
ATOM   4249  N  N   . TYR   C  1 7   ? 67.600 -20.670 52.108  1.00 15.92 ? 7    TYR   C N   1 
ATOM   4250  C  CA  . TYR   C  1 7   ? 67.240 -21.945 51.493  1.00 15.32 ? 7    TYR   C CA  1 
ATOM   4251  C  C   . TYR   C  1 7   ? 68.450 -22.840 51.308  1.00 17.54 ? 7    TYR   C C   1 
ATOM   4252  O  O   . TYR   C  1 7   ? 68.394 -23.812 50.520  1.00 19.38 ? 7    TYR   C O   1 
ATOM   4253  C  CB  . TYR   C  1 7   ? 66.551 -21.723 50.130  1.00 16.41 ? 7    TYR   C CB  1 
ATOM   4254  C  CG  . TYR   C  1 7   ? 65.182 -21.048 50.239  1.00 15.32 ? 7    TYR   C CG  1 
ATOM   4255  C  CD1 . TYR   C  1 7   ? 64.027 -21.817 50.536  1.00 15.39 ? 7    TYR   C CD1 1 
ATOM   4256  C  CD2 . TYR   C  1 7   ? 65.026 -19.663 50.058  1.00 16.67 ? 7    TYR   C CD2 1 
ATOM   4257  C  CE1 . TYR   C  1 7   ? 62.765 -21.220 50.645  1.00 15.49 ? 7    TYR   C CE1 1 
ATOM   4258  C  CE2 . TYR   C  1 7   ? 63.760 -19.067 50.117  1.00 15.62 ? 7    TYR   C CE2 1 
ATOM   4259  C  CZ  . TYR   C  1 7   ? 62.660 -19.836 50.405  1.00 14.72 ? 7    TYR   C CZ  1 
ATOM   4260  O  OH  . TYR   C  1 7   ? 61.417 -19.277 50.473  1.00 17.21 ? 7    TYR   C OH  1 
ATOM   4261  N  N   . GLY   C  1 8   ? 69.561 -22.532 51.981  1.00 18.01 ? 8    GLY   C N   1 
ATOM   4262  C  CA  . GLY   C  1 8   ? 70.768 -23.306 51.836  1.00 19.07 ? 8    GLY   C CA  1 
ATOM   4263  C  C   . GLY   C  1 8   ? 70.799 -24.477 52.808  1.00 18.87 ? 8    GLY   C C   1 
ATOM   4264  O  O   . GLY   C  1 8   ? 69.839 -24.765 53.529  1.00 17.51 ? 8    GLY   C O   1 
ATOM   4265  N  N   . LYS   C  1 9   ? 71.952 -25.114 52.831  1.00 19.00 ? 9    LYS   C N   1 
ATOM   4266  C  CA  . LYS   C  1 9   ? 72.125 -26.340 53.613  1.00 19.47 ? 9    LYS   C CA  1 
ATOM   4267  C  C   . LYS   C  1 9   ? 72.055 -26.088 55.099  1.00 19.63 ? 9    LYS   C C   1 
ATOM   4268  O  O   . LYS   C  1 9   ? 71.613 -26.968 55.846  1.00 20.79 ? 9    LYS   C O   1 
ATOM   4269  C  CB  . LYS   C  1 9   ? 73.469 -26.984 53.289  1.00 21.94 ? 9    LYS   C CB  1 
ATOM   4270  C  CG  . LYS   C  1 9   ? 73.693 -27.193 51.819  1.00 26.34 ? 9    LYS   C CG  1 
ATOM   4271  C  CD  . LYS   C  1 9   ? 72.658 -28.145 51.314  1.00 28.38 ? 9    LYS   C CD  1 
ATOM   4272  C  CE  . LYS   C  1 9   ? 73.006 -28.649 49.853  1.00 34.63 ? 9    LYS   C CE  1 
ATOM   4273  N  NZ  . LYS   C  1 9   ? 74.126 -29.629 49.869  1.00 39.85 ? 9    LYS   C NZ  1 
ATOM   4274  N  N   . HIS   C  1 10  ? 72.514 -24.924 55.569  1.00 19.76 ? 10   HIS   C N   1 
ATOM   4275  C  CA  . HIS   C  1 10  ? 72.538 -24.656 56.993  1.00 19.25 ? 10   HIS   C CA  1 
ATOM   4276  C  C   . HIS   C  1 10  ? 71.390 -23.796 57.449  1.00 18.79 ? 10   HIS   C C   1 
ATOM   4277  O  O   . HIS   C  1 10  ? 70.966 -23.888 58.605  1.00 20.19 ? 10   HIS   C O   1 
ATOM   4278  C  CB  . HIS   C  1 10  ? 73.849 -23.946 57.362  1.00 20.62 ? 10   HIS   C CB  1 
ATOM   4279  C  CG  . HIS   C  1 10  ? 75.080 -24.754 57.107  1.00 24.21 ? 10   HIS   C CG  1 
ATOM   4280  N  ND1 . HIS   C  1 10  ? 75.294 -25.953 57.731  1.00 28.41 ? 10   HIS   C ND1 1 
ATOM   4281  C  CD2 . HIS   C  1 10  ? 76.174 -24.518 56.353  1.00 27.96 ? 10   HIS   C CD2 1 
ATOM   4282  C  CE1 . HIS   C  1 10  ? 76.437 -26.475 57.322  1.00 25.66 ? 10   HIS   C CE1 1 
ATOM   4283  N  NE2 . HIS   C  1 10  ? 77.005 -25.623 56.494  1.00 30.91 ? 10   HIS   C NE2 1 
ATOM   4284  N  N   . ASN   C  1 11  ? 70.826 -22.992 56.551  1.00 16.59 ? 11   ASN   C N   1 
ATOM   4285  C  CA  . ASN   C  1 11  ? 69.819 -22.020 56.955  1.00 15.24 ? 11   ASN   C CA  1 
ATOM   4286  C  C   . ASN   C  1 11  ? 68.455 -22.243 56.328  1.00 15.78 ? 11   ASN   C C   1 
ATOM   4287  O  O   . ASN   C  1 11  ? 67.577 -21.386 56.464  1.00 14.89 ? 11   ASN   C O   1 
ATOM   4288  C  CB  . ASN   C  1 11  ? 70.334 -20.593 56.660  1.00 15.29 ? 11   ASN   C CB  1 
ATOM   4289  C  CG  . ASN   C  1 11  ? 70.487 -20.316 55.187  1.00 18.21 ? 11   ASN   C CG  1 
ATOM   4290  O  OD1 . ASN   C  1 11  ? 70.103 -21.124 54.350  1.00 18.95 ? 11   ASN   C OD1 1 
ATOM   4291  N  ND2 . ASN   C  1 11  ? 71.002 -19.138 54.869  1.00 20.13 ? 11   ASN   C ND2 1 
ATOM   4292  N  N   . GLY   C  1 12  ? 68.245 -23.379 55.655  1.00 15.30 ? 12   GLY   C N   1 
ATOM   4293  C  CA  . GLY   C  1 12  ? 67.054 -23.603 54.872  1.00 15.58 ? 12   GLY   C CA  1 
ATOM   4294  C  C   . GLY   C  1 12  ? 65.868 -24.178 55.622  1.00 15.09 ? 12   GLY   C C   1 
ATOM   4295  O  O   . GLY   C  1 12  ? 65.911 -24.362 56.841  1.00 15.49 ? 12   GLY   C O   1 
ATOM   4296  N  N   . PRO   C  1 13  ? 64.824 -24.523 54.874  1.00 15.09 ? 13   PRO   C N   1 
ATOM   4297  C  CA  . PRO   C  1 13  ? 63.528 -24.887 55.463  1.00 15.49 ? 13   PRO   C CA  1 
ATOM   4298  C  C   . PRO   C  1 13  ? 63.598 -25.911 56.589  1.00 15.07 ? 13   PRO   C C   1 
ATOM   4299  O  O   . PRO   C  1 13  ? 62.897 -25.719 57.606  1.00 15.76 ? 13   PRO   C O   1 
ATOM   4300  C  CB  . PRO   C  1 13  ? 62.760 -25.422 54.240  1.00 17.20 ? 13   PRO   C CB  1 
ATOM   4301  C  CG  . PRO   C  1 13  ? 63.260 -24.523 53.120  1.00 16.05 ? 13   PRO   C CG  1 
ATOM   4302  C  CD  . PRO   C  1 13  ? 64.722 -24.237 53.428  1.00 15.35 ? 13   PRO   C CD  1 
ATOM   4303  N  N   . GLU   C  1 14  ? 64.387 -26.994 56.463  1.00 15.45 ? 14   GLU   C N   1 
ATOM   4304  C  CA  . GLU   C  1 14  ? 64.369 -28.020 57.526  1.00 15.34 ? 14   GLU   C CA  1 
ATOM   4305  C  C   . GLU   C  1 14  ? 64.923 -27.485 58.841  1.00 17.20 ? 14   GLU   C C   1 
ATOM   4306  O  O   . GLU   C  1 14  ? 64.721 -28.116 59.869  1.00 18.44 ? 14   GLU   C O   1 
ATOM   4307  C  CB  . GLU   C  1 14  ? 65.151 -29.289 57.123  1.00 16.28 ? 14   GLU   C CB  1 
ATOM   4308  C  CG  . GLU   C  1 14  ? 66.655 -29.082 57.088  1.00 17.22 ? 14   GLU   C CG  1 
ATOM   4309  C  CD  . GLU   C  1 14  ? 67.392 -30.398 57.002  1.00 21.55 ? 14   GLU   C CD  1 
ATOM   4310  O  OE1 . GLU   C  1 14  ? 66.756 -31.495 57.186  1.00 22.18 ? 14   GLU   C OE1 1 
ATOM   4311  O  OE2 . GLU   C  1 14  ? 68.622 -30.332 56.786  1.00 24.39 ? 14   GLU   C OE2 1 
ATOM   4312  N  N   . HIS   C  1 15  ? 65.616 -26.350 58.827  1.00 15.80 ? 15   HIS   C N   1 
ATOM   4313  C  CA  . HIS   C  1 15  ? 66.209 -25.745 60.022  1.00 16.20 ? 15   HIS   C CA  1 
ATOM   4314  C  C   . HIS   C  1 15  ? 65.444 -24.534 60.530  1.00 15.00 ? 15   HIS   C C   1 
ATOM   4315  O  O   . HIS   C  1 15  ? 65.795 -24.011 61.613  1.00 16.01 ? 15   HIS   C O   1 
ATOM   4316  C  CB  . HIS   C  1 15  ? 67.662 -25.308 59.740  1.00 16.27 ? 15   HIS   C CB  1 
ATOM   4317  C  CG  . HIS   C  1 15  ? 68.541 -26.441 59.347  1.00 20.83 ? 15   HIS   C CG  1 
ATOM   4318  N  ND1 . HIS   C  1 15  ? 68.632 -27.594 60.112  1.00 23.75 ? 15   HIS   C ND1 1 
ATOM   4319  C  CD2 . HIS   C  1 15  ? 69.289 -26.661 58.234  1.00 22.18 ? 15   HIS   C CD2 1 
ATOM   4320  C  CE1 . HIS   C  1 15  ? 69.429 -28.459 59.497  1.00 25.72 ? 15   HIS   C CE1 1 
ATOM   4321  N  NE2 . HIS   C  1 15  ? 69.863 -27.898 58.379  1.00 24.23 ? 15   HIS   C NE2 1 
ATOM   4322  N  N   . TRP   C  1 16  ? 64.424 -24.042 59.795  1.00 13.64 ? 16   TRP   C N   1 
ATOM   4323  C  CA  . TRP   C  1 16  ? 63.791 -22.798 60.203  1.00 13.36 ? 16   TRP   C CA  1 
ATOM   4324  C  C   . TRP   C  1 16  ? 63.235 -22.877 61.607  1.00 14.96 ? 16   TRP   C C   1 
ATOM   4325  O  O   . TRP   C  1 16  ? 63.259 -21.863 62.326  1.00 15.04 ? 16   TRP   C O   1 
ATOM   4326  C  CB  . TRP   C  1 16  ? 62.675 -22.417 59.231  1.00 12.61 ? 16   TRP   C CB  1 
ATOM   4327  C  CG  . TRP   C  1 16  ? 63.200 -21.970 57.899  1.00 14.27 ? 16   TRP   C CG  1 
ATOM   4328  C  CD1 . TRP   C  1 16  ? 64.488 -21.609 57.573  1.00 13.66 ? 16   TRP   C CD1 1 
ATOM   4329  C  CD2 . TRP   C  1 16  ? 62.419 -21.808 56.706  1.00 14.28 ? 16   TRP   C CD2 1 
ATOM   4330  N  NE1 . TRP   C  1 16  ? 64.532 -21.201 56.250  1.00 13.65 ? 16   TRP   C NE1 1 
ATOM   4331  C  CE2 . TRP   C  1 16  ? 63.290 -21.332 55.697  1.00 12.85 ? 16   TRP   C CE2 1 
ATOM   4332  C  CE3 . TRP   C  1 16  ? 61.078 -22.019 56.400  1.00 13.73 ? 16   TRP   C CE3 1 
ATOM   4333  C  CZ2 . TRP   C  1 16  ? 62.850 -21.063 54.385  1.00 14.00 ? 16   TRP   C CZ2 1 
ATOM   4334  C  CZ3 . TRP   C  1 16  ? 60.633 -21.790 55.106  1.00 14.76 ? 16   TRP   C CZ3 1 
ATOM   4335  C  CH2 . TRP   C  1 16  ? 61.508 -21.282 54.108  1.00 14.20 ? 16   TRP   C CH2 1 
ATOM   4336  N  N   . HIS   C  1 17  ? 62.701 -24.046 62.018  1.00 14.47 ? 17   HIS   C N   1 
ATOM   4337  C  CA  . HIS   C  1 17  ? 62.141 -24.172 63.382  1.00 14.30 ? 17   HIS   C CA  1 
ATOM   4338  C  C   . HIS   C  1 17  ? 63.112 -23.805 64.483  1.00 15.79 ? 17   HIS   C C   1 
ATOM   4339  O  O   . HIS   C  1 17  ? 62.651 -23.506 65.596  1.00 17.49 ? 17   HIS   C O   1 
ATOM   4340  C  CB  . HIS   C  1 17  ? 61.628 -25.605 63.628  1.00 17.48 ? 17   HIS   C CB  1 
ATOM   4341  C  CG  . HIS   C  1 17  ? 62.728 -26.610 63.636  1.00 16.98 ? 17   HIS   C CG  1 
ATOM   4342  N  ND1 . HIS   C  1 17  ? 63.311 -27.062 64.806  1.00 21.89 ? 17   HIS   C ND1 1 
ATOM   4343  C  CD2 . HIS   C  1 17  ? 63.437 -27.167 62.612  1.00 14.68 ? 17   HIS   C CD2 1 
ATOM   4344  C  CE1 . HIS   C  1 17  ? 64.297 -27.891 64.495  1.00 21.01 ? 17   HIS   C CE1 1 
ATOM   4345  N  NE2 . HIS   C  1 17  ? 64.396 -27.953 63.177  1.00 19.14 ? 17   HIS   C NE2 1 
ATOM   4346  N  N   . LYS   C  1 18  ? 64.439 -23.853 64.226  1.00 14.16 ? 18   LYS   C N   1 
ATOM   4347  C  CA  . LYS   C  1 18  ? 65.418 -23.574 65.284  1.00 14.14 ? 18   LYS   C CA  1 
ATOM   4348  C  C   . LYS   C  1 18  ? 65.328 -22.130 65.732  1.00 15.54 ? 18   LYS   C C   1 
ATOM   4349  O  O   . LYS   C  1 18  ? 65.699 -21.843 66.882  1.00 15.79 ? 18   LYS   C O   1 
ATOM   4350  C  CB  . LYS   C  1 18  ? 66.837 -23.894 64.783  1.00 15.63 ? 18   LYS   C CB  1 
ATOM   4351  C  CG  . LYS   C  1 18  ? 66.960 -25.380 64.530  1.00 23.75 ? 18   LYS   C CG  1 
ATOM   4352  C  CD  . LYS   C  1 18  ? 68.346 -25.646 63.896  1.00 25.76 ? 18   LYS   C CD  1 
ATOM   4353  C  CE  . LYS   C  1 18  ? 68.494 -27.102 63.473  1.00 28.68 ? 18   LYS   C CE  1 
ATOM   4354  N  NZ  . LYS   C  1 18  ? 69.908 -27.265 62.860  1.00 33.07 ? 18   LYS   C NZ  1 
ATOM   4355  N  N   . ASP   C  1 19  ? 64.882 -21.245 64.843  1.00 14.34 ? 19   ASP   C N   1 
ATOM   4356  C  CA  . ASP   C  1 19  ? 64.695 -19.825 65.191  1.00 14.30 ? 19   ASP   C CA  1 
ATOM   4357  C  C   . ASP   C  1 19  ? 63.245 -19.398 65.185  1.00 15.75 ? 19   ASP   C C   1 
ATOM   4358  O  O   . ASP   C  1 19  ? 62.918 -18.414 65.864  1.00 14.97 ? 19   ASP   C O   1 
ATOM   4359  C  CB  . ASP   C  1 19  ? 65.481 -18.931 64.204  1.00 13.98 ? 19   ASP   C CB  1 
ATOM   4360  C  CG  . ASP   C  1 19  ? 66.945 -19.191 64.253  1.00 16.85 ? 19   ASP   C CG  1 
ATOM   4361  O  OD1 . ASP   C  1 19  ? 67.573 -18.896 65.279  1.00 19.79 ? 19   ASP   C OD1 1 
ATOM   4362  O  OD2 . ASP   C  1 19  ? 67.493 -19.747 63.268  1.00 18.92 ? 19   ASP   C OD2 1 
ATOM   4363  N  N   . PHE   C  1 20  ? 62.381 -20.098 64.447  1.00 14.33 ? 20   PHE   C N   1 
ATOM   4364  C  CA  . PHE   C  1 20  ? 60.977 -19.723 64.270  1.00 14.98 ? 20   PHE   C CA  1 
ATOM   4365  C  C   . PHE   C  1 20  ? 60.152 -20.931 64.661  1.00 14.45 ? 20   PHE   C C   1 
ATOM   4366  O  O   . PHE   C  1 20  ? 59.743 -21.728 63.797  1.00 16.86 ? 20   PHE   C O   1 
ATOM   4367  C  CB  . PHE   C  1 20  ? 60.706 -19.290 62.833  1.00 14.84 ? 20   PHE   C CB  1 
ATOM   4368  C  CG  . PHE   C  1 20  ? 61.634 -18.184 62.364  1.00 13.42 ? 20   PHE   C CG  1 
ATOM   4369  C  CD1 . PHE   C  1 20  ? 61.328 -16.882 62.658  1.00 15.37 ? 20   PHE   C CD1 1 
ATOM   4370  C  CD2 . PHE   C  1 20  ? 62.790 -18.482 61.635  1.00 14.91 ? 20   PHE   C CD2 1 
ATOM   4371  C  CE1 . PHE   C  1 20  ? 62.199 -15.848 62.266  1.00 13.36 ? 20   PHE   C CE1 1 
ATOM   4372  C  CE2 . PHE   C  1 20  ? 63.672 -17.452 61.199  1.00 14.17 ? 20   PHE   C CE2 1 
ATOM   4373  C  CZ  . PHE   C  1 20  ? 63.369 -16.117 61.537  1.00 15.32 ? 20   PHE   C CZ  1 
ATOM   4374  N  N   . PRO   C  1 21  ? 59.907 -21.128 65.952  1.00 13.37 ? 21   PRO   C N   1 
ATOM   4375  C  CA  . PRO   C  1 21  ? 59.292 -22.403 66.369  1.00 15.61 ? 21   PRO   C CA  1 
ATOM   4376  C  C   . PRO   C  1 21  ? 57.881 -22.603 65.808  1.00 14.30 ? 21   PRO   C C   1 
ATOM   4377  O  O   . PRO   C  1 21  ? 57.411 -23.766 65.798  1.00 16.39 ? 21   PRO   C O   1 
ATOM   4378  C  CB  . PRO   C  1 21  ? 59.310 -22.359 67.906  1.00 18.65 ? 21   PRO   C CB  1 
ATOM   4379  C  CG  . PRO   C  1 21  ? 59.766 -20.973 68.255  1.00 19.44 ? 21   PRO   C CG  1 
ATOM   4380  C  CD  . PRO   C  1 21  ? 60.470 -20.352 67.072  1.00 14.24 ? 21   PRO   C CD  1 
ATOM   4381  N  N   A ILE   C  1 22  ? 57.203 -21.536 65.370  0.53 14.30 ? 22   ILE   C N   1 
ATOM   4382  N  N   B ILE   C  1 22  ? 57.208 -21.537 65.362  0.47 14.27 ? 22   ILE   C N   1 
ATOM   4383  C  CA  A ILE   C  1 22  ? 55.884 -21.683 64.756  0.53 14.17 ? 22   ILE   C CA  1 
ATOM   4384  C  CA  B ILE   C  1 22  ? 55.885 -21.682 64.758  0.47 14.21 ? 22   ILE   C CA  1 
ATOM   4385  C  C   A ILE   C  1 22  ? 55.964 -22.521 63.492  0.53 15.12 ? 22   ILE   C C   1 
ATOM   4386  C  C   B ILE   C  1 22  ? 55.962 -22.491 63.474  0.47 15.05 ? 22   ILE   C C   1 
ATOM   4387  O  O   A ILE   C  1 22  ? 54.928 -22.999 63.001  0.53 15.68 ? 22   ILE   C O   1 
ATOM   4388  O  O   B ILE   C  1 22  ? 54.921 -22.925 62.953  0.47 15.65 ? 22   ILE   C O   1 
ATOM   4389  C  CB  A ILE   C  1 22  ? 55.266 -20.288 64.500  0.53 14.81 ? 22   ILE   C CB  1 
ATOM   4390  C  CB  B ILE   C  1 22  ? 55.244 -20.286 64.556  0.47 14.75 ? 22   ILE   C CB  1 
ATOM   4391  C  CG1 A ILE   C  1 22  ? 53.774 -20.401 64.125  0.53 14.76 ? 22   ILE   C CG1 1 
ATOM   4392  C  CG1 B ILE   C  1 22  ? 53.724 -20.391 64.397  0.47 15.09 ? 22   ILE   C CG1 1 
ATOM   4393  C  CG2 A ILE   C  1 22  ? 56.045 -19.575 63.413  0.53 15.88 ? 22   ILE   C CG2 1 
ATOM   4394  C  CG2 B ILE   C  1 22  ? 55.822 -19.583 63.331  0.47 15.64 ? 22   ILE   C CG2 1 
ATOM   4395  C  CD1 A ILE   C  1 22  ? 52.925 -21.001 65.236  0.53 15.12 ? 22   ILE   C CD1 1 
ATOM   4396  C  CD1 B ILE   C  1 22  ? 53.081 -19.050 64.081  0.47 15.16 ? 22   ILE   C CD1 1 
ATOM   4397  N  N   . ALA   C  1 23  ? 57.182 -22.755 62.975  1.00 13.76 ? 23   ALA   C N   1 
ATOM   4398  C  CA  . ALA   C  1 23  ? 57.317 -23.697 61.855  1.00 15.31 ? 23   ALA   C CA  1 
ATOM   4399  C  C   . ALA   C  1 23  ? 56.628 -25.035 62.093  1.00 14.56 ? 23   ALA   C C   1 
ATOM   4400  O  O   . ALA   C  1 23  ? 56.275 -25.712 61.114  1.00 16.26 ? 23   ALA   C O   1 
ATOM   4401  C  CB  . ALA   C  1 23  ? 58.820 -23.973 61.598  1.00 15.22 ? 23   ALA   C CB  1 
ATOM   4402  N  N   . LYS   C  1 24  ? 56.493 -25.456 63.361  1.00 15.18 ? 24   LYS   C N   1 
ATOM   4403  C  CA  . LYS   C  1 24  ? 55.865 -26.721 63.738  1.00 15.37 ? 24   LYS   C CA  1 
ATOM   4404  C  C   . LYS   C  1 24  ? 54.443 -26.504 64.243  1.00 16.43 ? 24   LYS   C C   1 
ATOM   4405  O  O   . LYS   C  1 24  ? 53.885 -27.381 64.929  1.00 19.59 ? 24   LYS   C O   1 
ATOM   4406  C  CB  . LYS   C  1 24  ? 56.720 -27.431 64.785  1.00 19.58 ? 24   LYS   C CB  1 
ATOM   4407  C  CG  . LYS   C  1 24  ? 58.088 -27.870 64.170  1.00 23.06 ? 24   LYS   C CG  1 
ATOM   4408  C  CD  . LYS   C  1 24  ? 58.853 -28.698 65.156  1.00 30.89 ? 24   LYS   C CD  1 
ATOM   4409  C  CE  . LYS   C  1 24  ? 60.237 -29.062 64.633  1.00 34.55 ? 24   LYS   C CE  1 
ATOM   4410  N  NZ  . LYS   C  1 24  ? 60.239 -30.079 63.487  1.00 38.47 ? 24   LYS   C NZ  1 
ATOM   4411  N  N   . GLY   C  1 25  ? 53.835 -25.377 63.865  1.00 18.07 ? 25   GLY   C N   1 
ATOM   4412  C  CA  . GLY   C  1 25  ? 52.523 -24.953 64.334  1.00 16.84 ? 25   GLY   C CA  1 
ATOM   4413  C  C   . GLY   C  1 25  ? 51.371 -25.759 63.715  1.00 18.48 ? 25   GLY   C C   1 
ATOM   4414  O  O   . GLY   C  1 25  ? 51.548 -26.710 62.944  1.00 18.61 ? 25   GLY   C O   1 
ATOM   4415  N  N   . GLU   C  1 26  ? 50.164 -25.298 64.042  1.00 16.65 ? 26   GLU   C N   1 
ATOM   4416  C  CA  . GLU   C  1 26  ? 48.943 -25.994 63.685  1.00 20.13 ? 26   GLU   C CA  1 
ATOM   4417  C  C   . GLU   C  1 26  ? 48.378 -25.540 62.353  1.00 18.89 ? 26   GLU   C C   1 
ATOM   4418  O  O   . GLU   C  1 26  ? 47.442 -26.188 61.839  1.00 23.68 ? 26   GLU   C O   1 
ATOM   4419  C  CB  . GLU   C  1 26  ? 47.897 -25.774 64.787  1.00 20.11 ? 26   GLU   C CB  1 
ATOM   4420  C  CG  . GLU   C  1 26  ? 48.302 -26.343 66.159  1.00 22.97 ? 26   GLU   C CG  1 
ATOM   4421  C  CD  . GLU   C  1 26  ? 48.472 -27.852 66.044  1.00 30.70 ? 26   GLU   C CD  1 
ATOM   4422  O  OE1 . GLU   C  1 26  ? 47.526 -28.519 65.568  1.00 33.87 ? 26   GLU   C OE1 1 
ATOM   4423  O  OE2 . GLU   C  1 26  ? 49.568 -28.335 66.378  1.00 34.54 ? 26   GLU   C OE2 1 
ATOM   4424  N  N   . ARG   C  1 27  ? 48.881 -24.436 61.796  1.00 17.21 ? 27   ARG   C N   1 
ATOM   4425  C  CA  A ARG   C  1 27  ? 48.303 -23.820 60.615  0.52 16.69 ? 27   ARG   C CA  1 
ATOM   4426  C  CA  B ARG   C  1 27  ? 48.296 -23.942 60.549  0.48 16.60 ? 27   ARG   C CA  1 
ATOM   4427  C  C   . ARG   C  1 27  ? 49.392 -23.475 59.594  1.00 15.35 ? 27   ARG   C C   1 
ATOM   4428  O  O   . ARG   C  1 27  ? 49.427 -22.349 59.085  1.00 17.24 ? 27   ARG   C O   1 
ATOM   4429  C  CB  A ARG   C  1 27  ? 47.515 -22.569 61.053  0.52 17.80 ? 27   ARG   C CB  1 
ATOM   4430  C  CB  B ARG   C  1 27  ? 47.281 -22.831 60.783  0.48 17.51 ? 27   ARG   C CB  1 
ATOM   4431  C  CG  A ARG   C  1 27  ? 46.600 -21.914 60.001  0.52 20.08 ? 27   ARG   C CG  1 
ATOM   4432  C  CG  B ARG   C  1 27  ? 46.258 -23.109 61.849  0.48 17.48 ? 27   ARG   C CG  1 
ATOM   4433  C  CD  A ARG   C  1 27  ? 45.861 -20.659 60.573  0.52 19.06 ? 27   ARG   C CD  1 
ATOM   4434  C  CD  B ARG   C  1 27  ? 45.126 -22.026 61.805  0.48 18.20 ? 27   ARG   C CD  1 
ATOM   4435  N  NE  A ARG   C  1 27  ? 45.803 -19.562 59.591  0.52 11.06 ? 27   ARG   C NE  1 
ATOM   4436  N  NE  B ARG   C  1 27  ? 45.534 -20.607 61.882  0.48 18.33 ? 27   ARG   C NE  1 
ATOM   4437  C  CZ  A ARG   C  1 27  ? 44.950 -18.571 59.643  0.52 20.09 ? 27   ARG   C CZ  1 
ATOM   4438  C  CZ  B ARG   C  1 27  ? 45.911 -19.977 63.012  0.48 19.89 ? 27   ARG   C CZ  1 
ATOM   4439  N  NH1 A ARG   C  1 27  ? 44.038 -18.481 60.622  0.52 22.47 ? 27   ARG   C NH1 1 
ATOM   4440  N  NH1 B ARG   C  1 27  ? 46.234 -18.667 63.038  0.48 17.04 ? 27   ARG   C NH1 1 
ATOM   4441  N  NH2 A ARG   C  1 27  ? 44.987 -17.660 58.714  0.52 21.49 ? 27   ARG   C NH2 1 
ATOM   4442  N  NH2 B ARG   C  1 27  ? 46.028 -20.686 64.151  0.48 21.86 ? 27   ARG   C NH2 1 
ATOM   4443  N  N   . GLN   C  1 28  ? 50.314 -24.394 59.322  1.00 15.90 ? 28   GLN   C N   1 
ATOM   4444  C  CA  . GLN   C  1 28  ? 51.471 -24.069 58.473  1.00 14.90 ? 28   GLN   C CA  1 
ATOM   4445  C  C   . GLN   C  1 28  ? 51.212 -24.369 56.990  1.00 15.68 ? 28   GLN   C C   1 
ATOM   4446  O  O   . GLN   C  1 28  ? 50.404 -25.223 56.628  1.00 16.42 ? 28   GLN   C O   1 
ATOM   4447  C  CB  . GLN   C  1 28  ? 52.682 -24.870 58.961  1.00 16.17 ? 28   GLN   C CB  1 
ATOM   4448  C  CG  . GLN   C  1 28  ? 53.177 -24.348 60.334  1.00 14.79 ? 28   GLN   C CG  1 
ATOM   4449  C  CD  . GLN   C  1 28  ? 53.805 -22.964 60.145  1.00 14.27 ? 28   GLN   C CD  1 
ATOM   4450  O  OE1 . GLN   C  1 28  ? 54.857 -22.829 59.519  1.00 14.87 ? 28   GLN   C OE1 1 
ATOM   4451  N  NE2 . GLN   C  1 28  ? 53.144 -21.926 60.673  1.00 14.53 ? 28   GLN   C NE2 1 
ATOM   4452  N  N   . SER   C  1 29  ? 51.947 -23.668 56.141  1.00 14.78 ? 29   SER   C N   1 
ATOM   4453  C  CA  . SER   C  1 29  ? 51.860 -23.743 54.680  1.00 14.26 ? 29   SER   C CA  1 
ATOM   4454  C  C   . SER   C  1 29  ? 53.254 -23.930 54.101  1.00 16.74 ? 29   SER   C C   1 
ATOM   4455  O  O   . SER   C  1 29  ? 54.245 -23.515 54.711  1.00 15.82 ? 29   SER   C O   1 
ATOM   4456  C  CB  . SER   C  1 29  ? 51.253 -22.447 54.102  1.00 15.85 ? 29   SER   C CB  1 
ATOM   4457  O  OG  . SER   C  1 29  ? 49.917 -22.289 54.563  1.00 15.36 ? 29   SER   C OG  1 
ATOM   4458  N  N   . PRO   C  1 30  ? 53.360 -24.512 52.905  1.00 15.59 ? 30   PRO   C N   1 
ATOM   4459  C  CA  . PRO   C  1 30  ? 52.296 -25.022 52.037  1.00 14.50 ? 30   PRO   C CA  1 
ATOM   4460  C  C   . PRO   C  1 30  ? 51.846 -26.389 52.482  1.00 15.74 ? 30   PRO   C C   1 
ATOM   4461  O  O   . PRO   C  1 30  ? 52.400 -26.929 53.461  1.00 16.74 ? 30   PRO   C O   1 
ATOM   4462  C  CB  . PRO   C  1 30  ? 52.994 -25.094 50.677  1.00 16.65 ? 30   PRO   C CB  1 
ATOM   4463  C  CG  . PRO   C  1 30  ? 54.443 -25.525 51.063  1.00 16.39 ? 30   PRO   C CG  1 
ATOM   4464  C  CD  . PRO   C  1 30  ? 54.708 -24.709 52.315  1.00 16.15 ? 30   PRO   C CD  1 
ATOM   4465  N  N   . VAL   C  1 31  ? 50.836 -26.928 51.812  1.00 16.27 ? 31   VAL   C N   1 
ATOM   4466  C  CA  . VAL   C  1 31  ? 50.316 -28.268 52.085  1.00 16.31 ? 31   VAL   C CA  1 
ATOM   4467  C  C   . VAL   C  1 31  ? 50.102 -28.985 50.761  1.00 17.82 ? 31   VAL   C C   1 
ATOM   4468  O  O   . VAL   C  1 31  ? 50.018 -28.364 49.667  1.00 19.06 ? 31   VAL   C O   1 
ATOM   4469  C  CB  . VAL   C  1 31  ? 48.992 -28.220 52.865  1.00 16.89 ? 31   VAL   C CB  1 
ATOM   4470  C  CG1 . VAL   C  1 31  ? 49.162 -27.508 54.227  1.00 18.41 ? 31   VAL   C CG1 1 
ATOM   4471  C  CG2 . VAL   C  1 31  ? 47.916 -27.477 52.025  1.00 18.10 ? 31   VAL   C CG2 1 
ATOM   4472  N  N   . ASP   C  1 32  ? 49.969 -30.316 50.849  1.00 16.70 ? 32   ASP   C N   1 
ATOM   4473  C  CA  . ASP   C  1 32  ? 49.468 -31.073 49.727  1.00 17.70 ? 32   ASP   C CA  1 
ATOM   4474  C  C   . ASP   C  1 32  ? 47.958 -30.890 49.639  1.00 20.68 ? 32   ASP   C C   1 
ATOM   4475  O  O   . ASP   C  1 32  ? 47.236 -30.976 50.652  1.00 21.88 ? 32   ASP   C O   1 
ATOM   4476  C  CB  . ASP   C  1 32  ? 49.822 -32.551 49.890  1.00 18.05 ? 32   ASP   C CB  1 
ATOM   4477  C  CG  . ASP   C  1 32  ? 49.290 -33.393 48.741  1.00 20.85 ? 32   ASP   C CG  1 
ATOM   4478  O  OD1 . ASP   C  1 32  ? 49.600 -33.070 47.563  1.00 21.52 ? 32   ASP   C OD1 1 
ATOM   4479  O  OD2 . ASP   C  1 32  ? 48.574 -34.374 49.003  1.00 23.53 ? 32   ASP   C OD2 1 
ATOM   4480  N  N   . ILE   C  1 33  ? 47.478 -30.633 48.425  1.00 18.81 ? 33   ILE   C N   1 
ATOM   4481  C  CA  . ILE   C  1 33  ? 46.039 -30.569 48.157  1.00 18.33 ? 33   ILE   C CA  1 
ATOM   4482  C  C   . ILE   C  1 33  ? 45.621 -31.894 47.558  1.00 20.49 ? 33   ILE   C C   1 
ATOM   4483  O  O   . ILE   C  1 33  ? 45.974 -32.224 46.416  1.00 22.92 ? 33   ILE   C O   1 
ATOM   4484  C  CB  . ILE   C  1 33  ? 45.728 -29.409 47.193  1.00 18.63 ? 33   ILE   C CB  1 
ATOM   4485  C  CG1 . ILE   C  1 33  ? 46.253 -28.133 47.811  1.00 21.51 ? 33   ILE   C CG1 1 
ATOM   4486  C  CG2 . ILE   C  1 33  ? 44.231 -29.410 46.878  1.00 22.38 ? 33   ILE   C CG2 1 
ATOM   4487  C  CD1 . ILE   C  1 33  ? 46.390 -26.983 46.834  1.00 23.65 ? 33   ILE   C CD1 1 
ATOM   4488  N  N   . ASP   C  1 34  ? 44.907 -32.716 48.337  1.00 22.87 ? 34   ASP   C N   1 
ATOM   4489  C  CA  . ASP   C  1 34  ? 44.446 -33.975 47.810  1.00 23.67 ? 34   ASP   C CA  1 
ATOM   4490  C  C   . ASP   C  1 34  ? 43.052 -33.803 47.228  1.00 28.17 ? 34   ASP   C C   1 
ATOM   4491  O  O   . ASP   C  1 34  ? 42.130 -33.384 47.934  1.00 28.51 ? 34   ASP   C O   1 
ATOM   4492  C  CB  . ASP   C  1 34  ? 44.454 -35.064 48.890  1.00 24.47 ? 34   ASP   C CB  1 
ATOM   4493  C  CG  . ASP   C  1 34  ? 44.000 -36.380 48.319  1.00 25.28 ? 34   ASP   C CG  1 
ATOM   4494  O  OD1 . ASP   C  1 34  ? 42.786 -36.502 48.086  1.00 28.18 ? 34   ASP   C OD1 1 
ATOM   4495  O  OD2 . ASP   C  1 34  ? 44.886 -37.190 48.112  1.00 29.62 ? 34   ASP   C OD2 1 
ATOM   4496  N  N   . THR   C  1 35  ? 42.924 -34.057 45.923  1.00 28.46 ? 35   THR   C N   1 
ATOM   4497  C  CA  . THR   C  1 35  ? 41.711 -33.710 45.199  1.00 29.22 ? 35   THR   C CA  1 
ATOM   4498  C  C   . THR   C  1 35  ? 40.563 -34.637 45.518  1.00 35.33 ? 35   THR   C C   1 
ATOM   4499  O  O   . THR   C  1 35  ? 39.424 -34.331 45.127  1.00 39.90 ? 35   THR   C O   1 
ATOM   4500  C  CB  . THR   C  1 35  ? 41.952 -33.701 43.687  1.00 28.99 ? 35   THR   C CB  1 
ATOM   4501  O  OG1 . THR   C  1 35  ? 42.288 -35.017 43.228  1.00 28.34 ? 35   THR   C OG1 1 
ATOM   4502  C  CG2 . THR   C  1 35  ? 43.096 -32.705 43.375  1.00 27.68 ? 35   THR   C CG2 1 
ATOM   4503  N  N   . HIS   C  1 36  ? 40.851 -35.772 46.137  1.00 30.47 ? 36   HIS   C N   1 
ATOM   4504  C  CA  . HIS   C  1 36  ? 39.790 -36.705 46.493  1.00 35.61 ? 36   HIS   C CA  1 
ATOM   4505  C  C   . HIS   C  1 36  ? 39.106 -36.294 47.782  1.00 35.37 ? 36   HIS   C C   1 
ATOM   4506  O  O   . HIS   C  1 36  ? 37.948 -36.673 48.007  1.00 38.14 ? 36   HIS   C O   1 
ATOM   4507  C  CB  . HIS   C  1 36  ? 40.375 -38.099 46.622  1.00 39.21 ? 36   HIS   C CB  1 
ATOM   4508  C  CG  . HIS   C  1 36  ? 41.348 -38.413 45.537  1.00 49.18 ? 36   HIS   C CG  1 
ATOM   4509  N  ND1 . HIS   C  1 36  ? 42.565 -39.016 45.776  1.00 50.94 ? 36   HIS   C ND1 1 
ATOM   4510  C  CD2 . HIS   C  1 36  ? 41.296 -38.179 44.202  1.00 52.51 ? 36   HIS   C CD2 1 
ATOM   4511  C  CE1 . HIS   C  1 36  ? 43.229 -39.123 44.638  1.00 52.54 ? 36   HIS   C CE1 1 
ATOM   4512  N  NE2 . HIS   C  1 36  ? 42.477 -38.630 43.667  1.00 52.03 ? 36   HIS   C NE2 1 
ATOM   4513  N  N   . THR   C  1 37  ? 39.808 -35.567 48.649  1.00 29.62 ? 37   THR   C N   1 
ATOM   4514  C  CA  . THR   C  1 37  ? 39.255 -35.196 49.936  1.00 27.70 ? 37   THR   C CA  1 
ATOM   4515  C  C   . THR   C  1 37  ? 38.868 -33.723 50.052  1.00 26.57 ? 37   THR   C C   1 
ATOM   4516  O  O   . THR   C  1 37  ? 38.048 -33.397 50.919  1.00 30.29 ? 37   THR   C O   1 
ATOM   4517  C  CB  . THR   C  1 37  ? 40.227 -35.579 51.068  1.00 29.05 ? 37   THR   C CB  1 
ATOM   4518  O  OG1 . THR   C  1 37  ? 41.510 -35.021 50.836  1.00 31.60 ? 37   THR   C OG1 1 
ATOM   4519  C  CG2 . THR   C  1 37  ? 40.354 -37.105 51.175  1.00 31.01 ? 37   THR   C CG2 1 
ATOM   4520  N  N   . ALA   C  1 38  ? 39.438 -32.829 49.235  1.00 26.64 ? 38   ALA   C N   1 
ATOM   4521  C  CA  . ALA   C  1 38  ? 38.979 -31.447 49.242  1.00 27.96 ? 38   ALA   C CA  1 
ATOM   4522  C  C   . ALA   C  1 38  ? 37.478 -31.407 48.927  1.00 33.30 ? 38   ALA   C C   1 
ATOM   4523  O  O   . ALA   C  1 38  ? 37.012 -32.140 48.056  1.00 39.69 ? 38   ALA   C O   1 
ATOM   4524  C  CB  . ALA   C  1 38  ? 39.803 -30.642 48.241  1.00 27.59 ? 38   ALA   C CB  1 
ATOM   4525  N  N   . LYS   C  1 39  ? 36.706 -30.601 49.677  1.00 28.60 ? 39   LYS   C N   1 
ATOM   4526  C  CA  . LYS   C  1 39  ? 35.238 -30.588 49.605  1.00 30.09 ? 39   LYS   C CA  1 
ATOM   4527  C  C   . LYS   C  1 39  ? 34.683 -29.232 49.160  1.00 30.48 ? 39   LYS   C C   1 
ATOM   4528  O  O   . LYS   C  1 39  ? 35.055 -28.192 49.707  1.00 27.75 ? 39   LYS   C O   1 
ATOM   4529  C  CB  . LYS   C  1 39  ? 34.611 -30.933 50.955  1.00 34.87 ? 39   LYS   C CB  1 
ATOM   4530  C  CG  . LYS   C  1 39  ? 34.667 -32.414 51.326  1.00 42.53 ? 39   LYS   C CG  1 
ATOM   4531  C  CD  . LYS   C  1 39  ? 33.819 -32.701 52.563  1.00 47.73 ? 39   LYS   C CD  1 
ATOM   4532  C  CE  . LYS   C  1 39  ? 32.385 -32.207 52.358  1.00 53.50 ? 39   LYS   C CE  1 
ATOM   4533  N  NZ  . LYS   C  1 39  ? 31.461 -32.592 53.490  1.00 56.75 ? 39   LYS   C NZ  1 
ATOM   4534  N  N   . TYR   C  1 40  ? 33.705 -29.259 48.249  1.00 32.24 ? 40   TYR   C N   1 
ATOM   4535  C  CA  . TYR   C  1 40  ? 32.999 -28.043 47.872  1.00 31.99 ? 40   TYR   C CA  1 
ATOM   4536  C  C   . TYR   C  1 40  ? 32.353 -27.383 49.091  1.00 31.40 ? 40   TYR   C C   1 
ATOM   4537  O  O   . TYR   C  1 40  ? 31.737 -28.054 49.935  1.00 32.53 ? 40   TYR   C O   1 
ATOM   4538  C  CB  . TYR   C  1 40  ? 31.943 -28.386 46.822  1.00 32.93 ? 40   TYR   C CB  1 
ATOM   4539  C  CG  . TYR   C  1 40  ? 30.952 -27.281 46.581  1.00 33.37 ? 40   TYR   C CG  1 
ATOM   4540  C  CD1 . TYR   C  1 40  ? 31.330 -26.099 45.931  1.00 34.06 ? 40   TYR   C CD1 1 
ATOM   4541  C  CD2 . TYR   C  1 40  ? 29.637 -27.415 47.006  1.00 36.21 ? 40   TYR   C CD2 1 
ATOM   4542  C  CE1 . TYR   C  1 40  ? 30.400 -25.084 45.713  1.00 35.88 ? 40   TYR   C CE1 1 
ATOM   4543  C  CE2 . TYR   C  1 40  ? 28.698 -26.426 46.774  1.00 40.24 ? 40   TYR   C CE2 1 
ATOM   4544  C  CZ  . TYR   C  1 40  ? 29.098 -25.254 46.153  1.00 38.55 ? 40   TYR   C CZ  1 
ATOM   4545  O  OH  . TYR   C  1 40  ? 28.160 -24.258 45.924  1.00 43.44 ? 40   TYR   C OH  1 
ATOM   4546  N  N   . ASP   C  1 41  ? 32.526 -26.064 49.201  1.00 32.62 ? 41   ASP   C N   1 
ATOM   4547  C  CA  . ASP   C  1 41  ? 31.950 -25.289 50.297  1.00 33.73 ? 41   ASP   C CA  1 
ATOM   4548  C  C   . ASP   C  1 41  ? 30.913 -24.333 49.721  1.00 36.48 ? 41   ASP   C C   1 
ATOM   4549  O  O   . ASP   C  1 41  ? 31.270 -23.273 49.171  1.00 33.23 ? 41   ASP   C O   1 
ATOM   4550  C  CB  . ASP   C  1 41  ? 33.036 -24.515 51.047  1.00 31.63 ? 41   ASP   C CB  1 
ATOM   4551  C  CG  . ASP   C  1 41  ? 32.500 -23.773 52.251  1.00 35.79 ? 41   ASP   C CG  1 
ATOM   4552  O  OD1 . ASP   C  1 41  ? 31.253 -23.688 52.445  1.00 37.88 ? 41   ASP   C OD1 1 
ATOM   4553  O  OD2 . ASP   C  1 41  ? 33.361 -23.270 53.016  1.00 36.44 ? 41   ASP   C OD2 1 
ATOM   4554  N  N   . PRO   C  1 42  ? 29.624 -24.636 49.844  1.00 36.31 ? 42   PRO   C N   1 
ATOM   4555  C  CA  . PRO   C  1 42  ? 28.607 -23.745 49.268  1.00 35.79 ? 42   PRO   C CA  1 
ATOM   4556  C  C   . PRO   C  1 42  ? 28.569 -22.358 49.888  1.00 36.64 ? 42   PRO   C C   1 
ATOM   4557  O  O   . PRO   C  1 42  ? 27.904 -21.475 49.319  1.00 40.88 ? 42   PRO   C O   1 
ATOM   4558  C  CB  . PRO   C  1 42  ? 27.291 -24.501 49.526  1.00 38.88 ? 42   PRO   C CB  1 
ATOM   4559  C  CG  . PRO   C  1 42  ? 27.610 -25.452 50.675  1.00 40.33 ? 42   PRO   C CG  1 
ATOM   4560  C  CD  . PRO   C  1 42  ? 29.060 -25.786 50.575  1.00 37.03 ? 42   PRO   C CD  1 
ATOM   4561  N  N   . SER   C  1 43  ? 29.209 -22.148 51.037  1.00 35.01 ? 43   SER   C N   1 
ATOM   4562  C  CA  . SER   C  1 43  ? 29.240 -20.847 51.700  1.00 38.10 ? 43   SER   C CA  1 
ATOM   4563  C  C   . SER   C  1 43  ? 30.223 -19.867 51.063  1.00 38.32 ? 43   SER   C C   1 
ATOM   4564  O  O   . SER   C  1 43  ? 30.166 -18.674 51.376  1.00 40.81 ? 43   SER   C O   1 
ATOM   4565  C  CB  . SER   C  1 43  ? 29.577 -21.014 53.196  1.00 37.89 ? 43   SER   C CB  1 
ATOM   4566  O  OG  . SER   C  1 43  ? 30.971 -21.207 53.437  1.00 37.78 ? 43   SER   C OG  1 
ATOM   4567  N  N   . LEU   C  1 44  ? 31.125 -20.327 50.205  1.00 33.97 ? 44   LEU   C N   1 
ATOM   4568  C  CA  . LEU   C  1 44  ? 32.030 -19.412 49.521  1.00 32.94 ? 44   LEU   C CA  1 
ATOM   4569  C  C   . LEU   C  1 44  ? 31.256 -18.496 48.572  1.00 36.45 ? 44   LEU   C C   1 
ATOM   4570  O  O   . LEU   C  1 44  ? 30.373 -18.938 47.831  1.00 36.90 ? 44   LEU   C O   1 
ATOM   4571  C  CB  . LEU   C  1 44  ? 33.090 -20.198 48.740  1.00 31.31 ? 44   LEU   C CB  1 
ATOM   4572  C  CG  . LEU   C  1 44  ? 34.033 -20.998 49.655  1.00 29.63 ? 44   LEU   C CG  1 
ATOM   4573  C  CD1 . LEU   C  1 44  ? 34.861 -22.025 48.885  1.00 28.04 ? 44   LEU   C CD1 1 
ATOM   4574  C  CD2 . LEU   C  1 44  ? 34.973 -20.037 50.397  1.00 28.73 ? 44   LEU   C CD2 1 
ATOM   4575  N  N   . LYS   C  1 45  ? 31.586 -17.211 48.599  1.00 36.33 ? 45   LYS   C N   1 
ATOM   4576  C  CA  . LYS   C  1 45  ? 30.984 -16.266 47.664  1.00 34.82 ? 45   LYS   C CA  1 
ATOM   4577  C  C   . LYS   C  1 45  ? 31.834 -16.208 46.414  1.00 32.14 ? 45   LYS   C C   1 
ATOM   4578  O  O   . LYS   C  1 45  ? 33.000 -16.628 46.419  1.00 31.60 ? 45   LYS   C O   1 
ATOM   4579  C  CB  . LYS   C  1 45  ? 30.881 -14.891 48.314  1.00 35.96 ? 45   LYS   C CB  1 
ATOM   4580  C  CG  . LYS   C  1 45  ? 30.240 -14.893 49.691  1.00 42.04 ? 45   LYS   C CG  1 
ATOM   4581  C  CD  . LYS   C  1 45  ? 28.827 -15.420 49.658  1.00 49.72 ? 45   LYS   C CD  1 
ATOM   4582  C  CE  . LYS   C  1 45  ? 28.251 -15.592 51.077  1.00 55.80 ? 45   LYS   C CE  1 
ATOM   4583  N  NZ  . LYS   C  1 45  ? 26.818 -16.024 51.072  1.00 60.94 ? 45   LYS   C NZ  1 
ATOM   4584  N  N   . PRO   C  1 46  ? 31.314 -15.645 45.323  1.00 31.90 ? 46   PRO   C N   1 
ATOM   4585  C  CA  . PRO   C  1 46  ? 32.128 -15.509 44.108  1.00 32.87 ? 46   PRO   C CA  1 
ATOM   4586  C  C   . PRO   C  1 46  ? 33.413 -14.744 44.402  1.00 30.86 ? 46   PRO   C C   1 
ATOM   4587  O  O   . PRO   C  1 46  ? 33.396 -13.748 45.124  1.00 31.45 ? 46   PRO   C O   1 
ATOM   4588  C  CB  . PRO   C  1 46  ? 31.221 -14.719 43.157  1.00 33.43 ? 46   PRO   C CB  1 
ATOM   4589  C  CG  . PRO   C  1 46  ? 29.787 -15.021 43.680  1.00 35.88 ? 46   PRO   C CG  1 
ATOM   4590  C  CD  . PRO   C  1 46  ? 29.962 -15.065 45.165  1.00 37.34 ? 46   PRO   C CD  1 
ATOM   4591  N  N   . LEU   C  1 47  ? 34.519 -15.219 43.831  1.00 27.96 ? 47   LEU   C N   1 
ATOM   4592  C  CA  . LEU   C  1 47  ? 35.819 -14.568 43.996  1.00 27.63 ? 47   LEU   C CA  1 
ATOM   4593  C  C   . LEU   C  1 47  ? 35.974 -13.439 42.979  1.00 29.01 ? 47   LEU   C C   1 
ATOM   4594  O  O   . LEU   C  1 47  ? 35.658 -13.611 41.788  1.00 33.10 ? 47   LEU   C O   1 
ATOM   4595  C  CB  . LEU   C  1 47  ? 36.959 -15.562 43.826  1.00 29.39 ? 47   LEU   C CB  1 
ATOM   4596  C  CG  . LEU   C  1 47  ? 38.332 -14.961 44.102  1.00 28.61 ? 47   LEU   C CG  1 
ATOM   4597  C  CD1 . LEU   C  1 47  ? 38.531 -14.708 45.584  1.00 28.54 ? 47   LEU   C CD1 1 
ATOM   4598  C  CD2 . LEU   C  1 47  ? 39.407 -15.919 43.590  1.00 30.48 ? 47   LEU   C CD2 1 
ATOM   4599  N  N   . SER   C  1 48  ? 36.396 -12.274 43.472  1.00 26.88 ? 48   SER   C N   1 
ATOM   4600  C  CA  A SER   C  1 48  ? 36.602 -11.089 42.652  0.57 29.58 ? 48   SER   C CA  1 
ATOM   4601  C  CA  B SER   C  1 48  ? 36.605 -11.068 42.670  0.43 29.51 ? 48   SER   C CA  1 
ATOM   4602  C  C   . SER   C  1 48  ? 38.090 -10.734 42.664  1.00 27.62 ? 48   SER   C C   1 
ATOM   4603  O  O   . SER   C  1 48  ? 38.657 -10.400 43.714  1.00 28.27 ? 48   SER   C O   1 
ATOM   4604  C  CB  A SER   C  1 48  ? 35.732 -9.941  43.169  0.57 31.34 ? 48   SER   C CB  1 
ATOM   4605  C  CB  B SER   C  1 48  ? 35.821 -9.881  43.238  0.43 31.46 ? 48   SER   C CB  1 
ATOM   4606  O  OG  A SER   C  1 48  ? 36.035 -8.752  42.483  0.57 32.74 ? 48   SER   C OG  1 
ATOM   4607  O  OG  B SER   C  1 48  ? 34.442 -9.993  43.008  0.43 35.31 ? 48   SER   C OG  1 
ATOM   4608  N  N   . VAL   C  1 49  ? 38.713 -10.788 41.487  1.00 28.95 ? 49   VAL   C N   1 
ATOM   4609  C  CA  . VAL   C  1 49  ? 40.116 -10.415 41.314  1.00 29.72 ? 49   VAL   C CA  1 
ATOM   4610  C  C   . VAL   C  1 49  ? 40.120 -9.139  40.483  1.00 29.70 ? 49   VAL   C C   1 
ATOM   4611  O  O   . VAL   C  1 49  ? 39.890 -9.194  39.273  1.00 34.81 ? 49   VAL   C O   1 
ATOM   4612  C  CB  . VAL   C  1 49  ? 40.913 -11.516 40.599  1.00 31.06 ? 49   VAL   C CB  1 
ATOM   4613  C  CG1 . VAL   C  1 49  ? 42.391 -11.048 40.408  1.00 33.63 ? 49   VAL   C CG1 1 
ATOM   4614  C  CG2 . VAL   C  1 49  ? 40.806 -12.834 41.357  1.00 31.09 ? 49   VAL   C CG2 1 
ATOM   4615  N  N   . SER   C  1 50  ? 40.395 -7.986  41.106  1.00 29.39 ? 50   SER   C N   1 
ATOM   4616  C  CA  . SER   C  1 50  ? 40.183 -6.683  40.444  1.00 30.44 ? 50   SER   C CA  1 
ATOM   4617  C  C   . SER   C  1 50  ? 41.546 -6.039  40.291  1.00 28.09 ? 50   SER   C C   1 
ATOM   4618  O  O   . SER   C  1 50  ? 42.037 -5.337  41.184  1.00 29.80 ? 50   SER   C O   1 
ATOM   4619  C  CB  . SER   C  1 50  ? 39.250 -5.747  41.210  1.00 35.73 ? 50   SER   C CB  1 
ATOM   4620  O  OG  . SER   C  1 50  ? 38.000 -6.349  41.422  1.00 43.08 ? 50   SER   C OG  1 
ATOM   4621  N  N   . TYR   C  1 51  ? 42.151 -6.255  39.128  1.00 28.52 ? 51   TYR   C N   1 
ATOM   4622  C  CA  . TYR   C  1 51  ? 43.520 -5.839  38.886  1.00 28.45 ? 51   TYR   C CA  1 
ATOM   4623  C  C   . TYR   C  1 51  ? 43.614 -4.843  37.743  1.00 31.97 ? 51   TYR   C C   1 
ATOM   4624  O  O   . TYR   C  1 51  ? 44.725 -4.566  37.282  1.00 33.20 ? 51   TYR   C O   1 
ATOM   4625  C  CB  . TYR   C  1 51  ? 44.395 -7.053  38.559  1.00 29.11 ? 51   TYR   C CB  1 
ATOM   4626  C  CG  . TYR   C  1 51  ? 44.781 -7.957  39.697  1.00 25.02 ? 51   TYR   C CG  1 
ATOM   4627  C  CD1 . TYR   C  1 51  ? 44.471 -7.653  41.024  1.00 25.91 ? 51   TYR   C CD1 1 
ATOM   4628  C  CD2 . TYR   C  1 51  ? 45.487 -9.109  39.429  1.00 23.75 ? 51   TYR   C CD2 1 
ATOM   4629  C  CE1 . TYR   C  1 51  ? 44.884 -8.497  42.076  1.00 23.56 ? 51   TYR   C CE1 1 
ATOM   4630  C  CE2 . TYR   C  1 51  ? 45.874 -9.963  40.437  1.00 21.91 ? 51   TYR   C CE2 1 
ATOM   4631  C  CZ  . TYR   C  1 51  ? 45.586 -9.673  41.765  1.00 22.27 ? 51   TYR   C CZ  1 
ATOM   4632  O  OH  . TYR   C  1 51  ? 46.029 -10.539 42.716  1.00 22.36 ? 51   TYR   C OH  1 
ATOM   4633  N  N   . ASP   C  1 52  ? 42.475 -4.311  37.290  1.00 32.33 ? 52   ASP   C N   1 
ATOM   4634  C  CA  . ASP   C  1 52  ? 42.466 -3.406  36.138  1.00 35.29 ? 52   ASP   C CA  1 
ATOM   4635  C  C   . ASP   C  1 52  ? 43.280 -2.138  36.398  1.00 34.54 ? 52   ASP   C C   1 
ATOM   4636  O  O   . ASP   C  1 52  ? 43.789 -1.529  35.448  1.00 38.46 ? 52   ASP   C O   1 
ATOM   4637  C  CB  . ASP   C  1 52  ? 41.018 -3.033  35.761  1.00 38.48 ? 52   ASP   C CB  1 
ATOM   4638  C  CG  . ASP   C  1 52  ? 40.228 -4.196  35.201  1.00 45.14 ? 52   ASP   C CG  1 
ATOM   4639  O  OD1 . ASP   C  1 52  ? 40.796 -5.289  34.980  1.00 45.90 ? 52   ASP   C OD1 1 
ATOM   4640  O  OD2 . ASP   C  1 52  ? 39.001 -4.025  34.957  1.00 47.88 ? 52   ASP   C OD2 1 
ATOM   4641  N  N   . GLN   C  1 53  ? 43.403 -1.701  37.649  1.00 30.92 ? 53   GLN   C N   1 
ATOM   4642  C  CA  . GLN   C  1 53  ? 44.066 -0.434  37.950  1.00 31.53 ? 53   GLN   C CA  1 
ATOM   4643  C  C   . GLN   C  1 53  ? 45.342 -0.624  38.761  1.00 31.83 ? 53   GLN   C C   1 
ATOM   4644  O  O   . GLN   C  1 53  ? 45.704 0.240   39.562  1.00 33.67 ? 53   GLN   C O   1 
ATOM   4645  C  CB  . GLN   C  1 53  ? 43.130 0.519   38.689  1.00 34.62 ? 53   GLN   C CB  1 
ATOM   4646  C  CG  . GLN   C  1 53  ? 41.919 0.933   37.861  1.00 37.36 ? 53   GLN   C CG  1 
ATOM   4647  C  CD  . GLN   C  1 53  ? 41.159 2.091   38.486  1.00 44.37 ? 53   GLN   C CD  1 
ATOM   4648  O  OE1 . GLN   C  1 53  ? 40.556 1.956   39.543  1.00 46.84 ? 53   GLN   C OE1 1 
ATOM   4649  N  NE2 . GLN   C  1 53  ? 41.204 3.250   37.832  1.00 49.99 ? 53   GLN   C NE2 1 
ATOM   4650  N  N   . ALA   C  1 54  ? 46.009 -1.754  38.591  1.00 29.80 ? 54   ALA   C N   1 
ATOM   4651  C  CA  . ALA   C  1 54  ? 47.190 -2.034  39.401  1.00 28.93 ? 54   ALA   C CA  1 
ATOM   4652  C  C   . ALA   C  1 54  ? 48.376 -1.179  38.973  1.00 28.84 ? 54   ALA   C C   1 
ATOM   4653  O  O   . ALA   C  1 54  ? 48.592 -0.946  37.778  1.00 29.96 ? 54   ALA   C O   1 
ATOM   4654  C  CB  . ALA   C  1 54  ? 47.530 -3.509  39.273  1.00 28.92 ? 54   ALA   C CB  1 
ATOM   4655  N  N   . THR   C  1 55  ? 49.139 -0.674  39.940  1.00 25.46 ? 55   THR   C N   1 
ATOM   4656  C  CA  . THR   C  1 55  ? 50.257 0.225   39.644  1.00 23.51 ? 55   THR   C CA  1 
ATOM   4657  C  C   . THR   C  1 55  ? 51.510 -0.465  40.169  1.00 23.12 ? 55   THR   C C   1 
ATOM   4658  O  O   . THR   C  1 55  ? 51.805 -0.363  41.358  1.00 23.88 ? 55   THR   C O   1 
ATOM   4659  C  CB  . THR   C  1 55  ? 50.089 1.610   40.291  1.00 27.05 ? 55   THR   C CB  1 
ATOM   4660  O  OG1 . THR   C  1 55  ? 48.886 2.189   39.797  1.00 31.33 ? 55   THR   C OG1 1 
ATOM   4661  C  CG2 . THR   C  1 55  ? 51.268 2.525   39.990  1.00 27.75 ? 55   THR   C CG2 1 
ATOM   4662  N  N   . SER   C  1 56  ? 52.259 -1.132  39.286  1.00 20.86 ? 56   SER   C N   1 
ATOM   4663  C  CA  . SER   C  1 56  ? 53.541 -1.682  39.724  1.00 19.82 ? 56   SER   C CA  1 
ATOM   4664  C  C   . SER   C  1 56  ? 54.602 -0.594  39.810  1.00 20.08 ? 56   SER   C C   1 
ATOM   4665  O  O   . SER   C  1 56  ? 54.539 0.437   39.120  1.00 22.97 ? 56   SER   C O   1 
ATOM   4666  C  CB  . SER   C  1 56  ? 54.003 -2.785  38.769  1.00 18.79 ? 56   SER   C CB  1 
ATOM   4667  O  OG  . SER   C  1 56  ? 54.381 -2.265  37.500  1.00 21.79 ? 56   SER   C OG  1 
ATOM   4668  N  N   . LEU   C  1 57  ? 55.556 -0.801  40.744  1.00 20.89 ? 57   LEU   C N   1 
ATOM   4669  C  CA  . LEU   C  1 57  ? 56.582 0.204   40.953  1.00 20.93 ? 57   LEU   C CA  1 
ATOM   4670  C  C   . LEU   C  1 57  ? 57.993 -0.297  40.712  1.00 19.81 ? 57   LEU   C C   1 
ATOM   4671  O  O   . LEU   C  1 57  ? 58.784 0.416   40.076  1.00 21.30 ? 57   LEU   C O   1 
ATOM   4672  C  CB  . LEU   C  1 57  ? 56.514 0.756   42.388  1.00 26.28 ? 57   LEU   C CB  1 
ATOM   4673  C  CG  . LEU   C  1 57  ? 55.261 1.570   42.657  1.00 29.38 ? 57   LEU   C CG  1 
ATOM   4674  C  CD1 . LEU   C  1 57  ? 55.251 1.844   44.191  1.00 30.61 ? 57   LEU   C CD1 1 
ATOM   4675  C  CD2 . LEU   C  1 57  ? 55.238 2.860   41.788  1.00 29.94 ? 57   LEU   C CD2 1 
ATOM   4676  N  N   . ARG   C  1 58  ? 58.359 -1.439  41.300  1.00 17.74 ? 58   ARG   C N   1 
ATOM   4677  C  CA  . ARG   C  1 58  ? 59.761 -1.830  41.361  1.00 19.43 ? 58   ARG   C CA  1 
ATOM   4678  C  C   . ARG   C  1 58  ? 59.858 -3.326  41.581  1.00 17.97 ? 58   ARG   C C   1 
ATOM   4679  O  O   . ARG   C  1 58  ? 58.899 -3.996  42.021  1.00 19.66 ? 58   ARG   C O   1 
ATOM   4680  C  CB  . ARG   C  1 58  ? 60.531 -1.030  42.432  1.00 24.32 ? 58   ARG   C CB  1 
ATOM   4681  C  CG  . ARG   C  1 58  ? 60.029 -1.172  43.796  1.00 27.73 ? 58   ARG   C CG  1 
ATOM   4682  C  CD  . ARG   C  1 58  ? 60.815 -0.215  44.740  1.00 31.48 ? 58   ARG   C CD  1 
ATOM   4683  N  NE  . ARG   C  1 58  ? 60.790 1.147   44.222  1.00 35.96 ? 58   ARG   C NE  1 
ATOM   4684  C  CZ  . ARG   C  1 58  ? 59.903 2.081   44.579  1.00 36.30 ? 58   ARG   C CZ  1 
ATOM   4685  N  NH1 . ARG   C  1 58  ? 60.011 3.280   44.017  1.00 33.54 ? 58   ARG   C NH1 1 
ATOM   4686  N  NH2 . ARG   C  1 58  ? 58.916 1.810   45.464  1.00 33.66 ? 58   ARG   C NH2 1 
ATOM   4687  N  N   . ILE   C  1 59  ? 61.045 -3.849  41.283  1.00 17.04 ? 59   ILE   C N   1 
ATOM   4688  C  CA  . ILE   C  1 59  ? 61.343 -5.262  41.485  1.00 18.21 ? 59   ILE   C CA  1 
ATOM   4689  C  C   . ILE   C  1 59  ? 62.634 -5.369  42.275  1.00 17.35 ? 59   ILE   C C   1 
ATOM   4690  O  O   . ILE   C  1 59  ? 63.600 -4.637  42.007  1.00 19.16 ? 59   ILE   C O   1 
ATOM   4691  C  CB  . ILE   C  1 59  ? 61.414 -5.988  40.126  1.00 16.54 ? 59   ILE   C CB  1 
ATOM   4692  C  CG1 . ILE   C  1 59  ? 61.516 -7.517  40.348  1.00 18.99 ? 59   ILE   C CG1 1 
ATOM   4693  C  CG2 . ILE   C  1 59  ? 62.552 -5.395  39.212  1.00 19.04 ? 59   ILE   C CG2 1 
ATOM   4694  C  CD1 . ILE   C  1 59  ? 61.487 -8.308  39.019  1.00 20.32 ? 59   ILE   C CD1 1 
ATOM   4695  N  N   . LEU   C  1 60  ? 62.636 -6.250  43.269  1.00 18.33 ? 60   LEU   C N   1 
ATOM   4696  C  CA  . LEU   C  1 60  ? 63.715 -6.328  44.239  1.00 18.59 ? 60   LEU   C CA  1 
ATOM   4697  C  C   . LEU   C  1 60  ? 64.151 -7.766  44.380  1.00 17.30 ? 60   LEU   C C   1 
ATOM   4698  O  O   . LEU   C  1 60  ? 63.308 -8.644  44.567  1.00 18.45 ? 60   LEU   C O   1 
ATOM   4699  C  CB  . LEU   C  1 60  ? 63.239 -5.827  45.613  1.00 19.16 ? 60   LEU   C CB  1 
ATOM   4700  C  CG  . LEU   C  1 60  ? 64.142 -6.085  46.826  1.00 17.82 ? 60   LEU   C CG  1 
ATOM   4701  C  CD1 . LEU   C  1 60  ? 65.372 -5.190  46.785  1.00 18.85 ? 60   LEU   C CD1 1 
ATOM   4702  C  CD2 . LEU   C  1 60  ? 63.381 -5.785  48.124  1.00 20.09 ? 60   LEU   C CD2 1 
ATOM   4703  N  N   . ASN   C  1 61  ? 65.449 -8.007  44.335  1.00 17.60 ? 61   ASN   C N   1 
ATOM   4704  C  CA  . ASN   C  1 61  ? 66.002 -9.300  44.764  1.00 14.74 ? 61   ASN   C CA  1 
ATOM   4705  C  C   . ASN   C  1 61  ? 66.225 -9.210  46.279  1.00 15.30 ? 61   ASN   C C   1 
ATOM   4706  O  O   . ASN   C  1 61  ? 67.067 -8.412  46.741  1.00 17.60 ? 61   ASN   C O   1 
ATOM   4707  C  CB  . ASN   C  1 61  ? 67.320 -9.538  44.006  1.00 17.44 ? 61   ASN   C CB  1 
ATOM   4708  C  CG  . ASN   C  1 61  ? 68.024 -10.829 44.446  1.00 16.63 ? 61   ASN   C CG  1 
ATOM   4709  O  OD1 . ASN   C  1 61  ? 67.822 -11.323 45.554  1.00 16.60 ? 61   ASN   C OD1 1 
ATOM   4710  N  ND2 . ASN   C  1 61  ? 68.821 -11.406 43.547  1.00 18.45 ? 61   ASN   C ND2 1 
ATOM   4711  N  N   . ASN   C  1 62  ? 65.411 -9.930  47.058  1.00 15.86 ? 62   ASN   C N   1 
ATOM   4712  C  CA  . ASN   C  1 62  ? 65.528 -9.836  48.522  1.00 16.63 ? 62   ASN   C CA  1 
ATOM   4713  C  C   . ASN   C  1 62  ? 66.441 -10.902 49.118  1.00 14.83 ? 62   ASN   C C   1 
ATOM   4714  O  O   . ASN   C  1 62  ? 66.451 -11.103 50.337  1.00 17.41 ? 62   ASN   C O   1 
ATOM   4715  C  CB  . ASN   C  1 62  ? 64.154 -9.857  49.201  1.00 14.76 ? 62   ASN   C CB  1 
ATOM   4716  C  CG  . ASN   C  1 62  ? 63.493 -11.230 49.161  1.00 16.85 ? 62   ASN   C CG  1 
ATOM   4717  O  OD1 . ASN   C  1 62  ? 63.989 -12.143 48.498  1.00 15.79 ? 62   ASN   C OD1 1 
ATOM   4718  N  ND2 . ASN   C  1 62  ? 62.347 -11.381 49.868  1.00 16.16 ? 62   ASN   C ND2 1 
ATOM   4719  N  N   . GLY   C  1 63  ? 67.248 -11.553 48.290  1.00 15.83 ? 63   GLY   C N   1 
ATOM   4720  C  CA  . GLY   C  1 63  ? 68.117 -12.621 48.760  1.00 14.94 ? 63   GLY   C CA  1 
ATOM   4721  C  C   . GLY   C  1 63  ? 67.427 -13.950 48.952  1.00 16.02 ? 63   GLY   C C   1 
ATOM   4722  O  O   . GLY   C  1 63  ? 68.092 -14.911 49.390  1.00 18.37 ? 63   GLY   C O   1 
ATOM   4723  N  N   . HIS   C  1 64  ? 66.125 -14.039 48.665  1.00 15.44 ? 64   HIS   C N   1 
ATOM   4724  C  CA  . HIS   C  1 64  ? 65.313 -15.241 48.826  1.00 14.05 ? 64   HIS   C CA  1 
ATOM   4725  C  C   . HIS   C  1 64  ? 64.590 -15.526 47.533  1.00 17.35 ? 64   HIS   C C   1 
ATOM   4726  O  O   . HIS   C  1 64  ? 64.576 -16.676 47.064  1.00 18.10 ? 64   HIS   C O   1 
ATOM   4727  C  CB  . HIS   C  1 64  ? 64.295 -15.098 49.987  1.00 14.17 ? 64   HIS   C CB  1 
ATOM   4728  C  CG  . HIS   C  1 64  ? 64.886 -14.608 51.279  1.00 14.01 ? 64   HIS   C CG  1 
ATOM   4729  N  ND1 . HIS   C  1 64  ? 65.771 -15.358 52.040  1.00 15.19 ? 64   HIS   C ND1 1 
ATOM   4730  C  CD2 . HIS   C  1 64  ? 64.703 -13.448 51.953  1.00 15.89 ? 64   HIS   C CD2 1 
ATOM   4731  C  CE1 . HIS   C  1 64  ? 66.081 -14.679 53.148  1.00 16.65 ? 64   HIS   C CE1 1 
ATOM   4732  N  NE2 . HIS   C  1 64  ? 65.451 -13.510 53.110  1.00 15.16 ? 64   HIS   C NE2 1 
ATOM   4733  N  N   . THR   C  1 65  ? 64.022 -14.506 46.926  1.00 15.10 ? 65   THR   C N   1 
ATOM   4734  C  CA  . THR   C  1 65  ? 63.283 -14.538 45.667  1.00 14.27 ? 65   THR   C CA  1 
ATOM   4735  C  C   . THR   C  1 65  ? 63.347 -13.125 45.081  1.00 14.73 ? 65   THR   C C   1 
ATOM   4736  O  O   . THR   C  1 65  ? 64.207 -12.316 45.469  1.00 16.74 ? 65   THR   C O   1 
ATOM   4737  C  CB  . THR   C  1 65  ? 61.858 -15.017 45.928  1.00 16.16 ? 65   THR   C CB  1 
ATOM   4738  O  OG1 . THR   C  1 65  ? 61.218 -15.130 44.651  1.00 17.63 ? 65   THR   C OG1 1 
ATOM   4739  C  CG2 . THR   C  1 65  ? 61.065 -14.048 46.820  1.00 16.16 ? 65   THR   C CG2 1 
ATOM   4740  N  N   . PHE   C  1 66  ? 62.527 -12.834 44.046  1.00 15.69 ? 66   PHE   C N   1 
ATOM   4741  C  CA  . PHE   C  1 66  ? 62.358 -11.449 43.622  1.00 15.14 ? 66   PHE   C CA  1 
ATOM   4742  C  C   . PHE   C  1 66  ? 60.893 -11.070 43.841  1.00 15.07 ? 66   PHE   C C   1 
ATOM   4743  O  O   . PHE   C  1 66  ? 59.985 -11.868 43.593  1.00 16.50 ? 66   PHE   C O   1 
ATOM   4744  C  CB  . PHE   C  1 66  ? 62.817 -11.169 42.143  1.00 17.47 ? 66   PHE   C CB  1 
ATOM   4745  C  CG  . PHE   C  1 66  ? 62.043 -11.956 41.096  1.00 17.10 ? 66   PHE   C CG  1 
ATOM   4746  C  CD1 . PHE   C  1 66  ? 60.885 -11.421 40.575  1.00 16.77 ? 66   PHE   C CD1 1 
ATOM   4747  C  CD2 . PHE   C  1 66  ? 62.457 -13.223 40.648  1.00 17.71 ? 66   PHE   C CD2 1 
ATOM   4748  C  CE1 . PHE   C  1 66  ? 60.153 -12.101 39.625  1.00 18.75 ? 66   PHE   C CE1 1 
ATOM   4749  C  CE2 . PHE   C  1 66  ? 61.699 -13.936 39.716  1.00 18.57 ? 66   PHE   C CE2 1 
ATOM   4750  C  CZ  . PHE   C  1 66  ? 60.551 -13.351 39.172  1.00 19.71 ? 66   PHE   C CZ  1 
ATOM   4751  N  N   . ASN   C  1 67  ? 60.684 -9.863  44.378  1.00 16.90 ? 67   ASN   C N   1 
ATOM   4752  C  CA  . ASN   C  1 67  ? 59.366 -9.314  44.659  1.00 16.11 ? 67   ASN   C CA  1 
ATOM   4753  C  C   . ASN   C  1 67  ? 59.089 -8.169  43.701  1.00 18.26 ? 67   ASN   C C   1 
ATOM   4754  O  O   . ASN   C  1 67  ? 59.921 -7.238  43.580  1.00 18.87 ? 67   ASN   C O   1 
ATOM   4755  C  CB  . ASN   C  1 67  ? 59.287 -8.753  46.080  1.00 16.13 ? 67   ASN   C CB  1 
ATOM   4756  C  CG  . ASN   C  1 67  ? 59.474 -9.782  47.144  1.00 17.23 ? 67   ASN   C CG  1 
ATOM   4757  O  OD1 . ASN   C  1 67  ? 59.309 -11.010 46.917  1.00 17.34 ? 67   ASN   C OD1 1 
ATOM   4758  N  ND2 . ASN   C  1 67  ? 59.845 -9.301  48.338  1.00 19.02 ? 67   ASN   C ND2 1 
ATOM   4759  N  N   . VAL   C  1 68  ? 57.917 -8.190  43.057  1.00 17.52 ? 68   VAL   C N   1 
ATOM   4760  C  CA  . VAL   C  1 68  ? 57.436 -7.052  42.285  1.00 17.51 ? 68   VAL   C CA  1 
ATOM   4761  C  C   . VAL   C  1 68  ? 56.442 -6.310  43.166  1.00 18.54 ? 68   VAL   C C   1 
ATOM   4762  O  O   . VAL   C  1 68  ? 55.415 -6.884  43.555  1.00 18.71 ? 68   VAL   C O   1 
ATOM   4763  C  CB  . VAL   C  1 68  ? 56.787 -7.510  40.967  1.00 18.86 ? 68   VAL   C CB  1 
ATOM   4764  C  CG1 . VAL   C  1 68  ? 56.078 -6.339  40.320  1.00 20.71 ? 68   VAL   C CG1 1 
ATOM   4765  C  CG2 . VAL   C  1 68  ? 57.822 -8.116  40.002  1.00 17.46 ? 68   VAL   C CG2 1 
ATOM   4766  N  N   . GLU   C  1 69  ? 56.742 -5.065  43.509  1.00 18.62 ? 69   GLU   C N   1 
ATOM   4767  C  CA  . GLU   C  1 69  ? 55.994 -4.302  44.496  1.00 20.62 ? 69   GLU   C CA  1 
ATOM   4768  C  C   . GLU   C  1 69  ? 55.023 -3.374  43.773  1.00 20.26 ? 69   GLU   C C   1 
ATOM   4769  O  O   . GLU   C  1 69  ? 55.364 -2.817  42.711  1.00 23.37 ? 69   GLU   C O   1 
ATOM   4770  C  CB  . GLU   C  1 69  ? 56.958 -3.467  45.356  1.00 27.78 ? 69   GLU   C CB  1 
ATOM   4771  C  CG  . GLU   C  1 69  ? 56.327 -2.674  46.494  1.00 39.18 ? 69   GLU   C CG  1 
ATOM   4772  C  CD  . GLU   C  1 69  ? 57.201 -1.471  46.948  1.00 48.51 ? 69   GLU   C CD  1 
ATOM   4773  O  OE1 . GLU   C  1 69  ? 58.344 -1.294  46.442  1.00 49.80 ? 69   GLU   C OE1 1 
ATOM   4774  O  OE2 . GLU   C  1 69  ? 56.716 -0.676  47.788  1.00 51.13 ? 69   GLU   C OE2 1 
ATOM   4775  N  N   . PHE   C  1 70  ? 53.833 -3.206  44.357  1.00 19.22 ? 70   PHE   C N   1 
ATOM   4776  C  CA  . PHE   C  1 70  ? 52.767 -2.340  43.848  1.00 19.69 ? 70   PHE   C CA  1 
ATOM   4777  C  C   . PHE   C  1 70  ? 52.450 -1.212  44.814  1.00 23.21 ? 70   PHE   C C   1 
ATOM   4778  O  O   . PHE   C  1 70  ? 52.661 -1.320  46.025  1.00 23.29 ? 70   PHE   C O   1 
ATOM   4779  C  CB  . PHE   C  1 70  ? 51.492 -3.154  43.611  1.00 19.37 ? 70   PHE   C CB  1 
ATOM   4780  C  CG  . PHE   C  1 70  ? 51.608 -4.107  42.486  1.00 20.22 ? 70   PHE   C CG  1 
ATOM   4781  C  CD1 . PHE   C  1 70  ? 52.326 -5.309  42.645  1.00 21.79 ? 70   PHE   C CD1 1 
ATOM   4782  C  CD2 . PHE   C  1 70  ? 51.057 -3.795  41.247  1.00 21.97 ? 70   PHE   C CD2 1 
ATOM   4783  C  CE1 . PHE   C  1 70  ? 52.447 -6.175  41.543  1.00 19.78 ? 70   PHE   C CE1 1 
ATOM   4784  C  CE2 . PHE   C  1 70  ? 51.164 -4.645  40.158  1.00 21.28 ? 70   PHE   C CE2 1 
ATOM   4785  C  CZ  . PHE   C  1 70  ? 51.888 -5.843  40.310  1.00 22.07 ? 70   PHE   C CZ  1 
ATOM   4786  N  N   . ASP   C  1 71  ? 51.894 -0.125  44.265  1.00 22.26 ? 71   ASP   C N   1 
ATOM   4787  C  CA  . ASP   C  1 71  ? 51.360 0.934   45.111  1.00 22.10 ? 71   ASP   C CA  1 
ATOM   4788  C  C   . ASP   C  1 71  ? 50.084 0.411   45.763  1.00 24.39 ? 71   ASP   C C   1 
ATOM   4789  O  O   . ASP   C  1 71  ? 49.115 0.115   45.068  1.00 26.18 ? 71   ASP   C O   1 
ATOM   4790  C  CB  . ASP   C  1 71  ? 51.089 2.156   44.241  1.00 23.31 ? 71   ASP   C CB  1 
ATOM   4791  C  CG  . ASP   C  1 71  ? 50.598 3.357   45.052  1.00 26.63 ? 71   ASP   C CG  1 
ATOM   4792  O  OD1 . ASP   C  1 71  ? 49.814 3.148   45.993  1.00 26.80 ? 71   ASP   C OD1 1 
ATOM   4793  O  OD2 . ASP   C  1 71  ? 50.946 4.542   44.705  1.00 27.92 ? 71   ASP   C OD2 1 
ATOM   4794  N  N   . ASP   C  1 72  ? 50.104 0.193   47.082  1.00 21.62 ? 72   ASP   C N   1 
ATOM   4795  C  CA  . ASP   C  1 72  ? 48.942 -0.332  47.800  1.00 20.32 ? 72   ASP   C CA  1 
ATOM   4796  C  C   . ASP   C  1 72  ? 48.260 0.737   48.647  1.00 22.50 ? 72   ASP   C C   1 
ATOM   4797  O  O   . ASP   C  1 72  ? 47.660 0.420   49.686  1.00 22.20 ? 72   ASP   C O   1 
ATOM   4798  C  CB  . ASP   C  1 72  ? 49.357 -1.525  48.670  1.00 20.28 ? 72   ASP   C CB  1 
ATOM   4799  C  CG  . ASP   C  1 72  ? 50.373 -1.139  49.749  1.00 21.23 ? 72   ASP   C CG  1 
ATOM   4800  O  OD1 . ASP   C  1 72  ? 50.919 0.008   49.735  1.00 23.87 ? 72   ASP   C OD1 1 
ATOM   4801  O  OD2 . ASP   C  1 72  ? 50.631 -1.988  50.647  1.00 22.10 ? 72   ASP   C OD2 1 
ATOM   4802  N  N   . SER   C  1 73  ? 48.264 1.996   48.180  1.00 22.77 ? 73   SER   C N   1 
ATOM   4803  C  CA  . SER   C  1 73  ? 47.680 3.077   48.955  1.00 23.19 ? 73   SER   C CA  1 
ATOM   4804  C  C   . SER   C  1 73  ? 46.180 3.226   48.759  1.00 26.41 ? 73   SER   C C   1 
ATOM   4805  O  O   . SER   C  1 73  ? 45.547 3.992   49.508  1.00 28.43 ? 73   SER   C O   1 
ATOM   4806  C  CB  . SER   C  1 73  ? 48.376 4.405   48.598  1.00 25.58 ? 73   SER   C CB  1 
ATOM   4807  O  OG  . SER   C  1 73  ? 48.072 4.806   47.279  1.00 26.82 ? 73   SER   C OG  1 
ATOM   4808  N  N   . GLN   C  1 74  ? 45.601 2.551   47.767  1.00 24.09 ? 74   GLN   C N   1 
ATOM   4809  C  CA  . GLN   C  1 74  ? 44.194 2.719   47.438  1.00 24.64 ? 74   GLN   C CA  1 
ATOM   4810  C  C   . GLN   C  1 74  ? 43.557 1.377   47.158  1.00 24.49 ? 74   GLN   C C   1 
ATOM   4811  O  O   . GLN   C  1 74  ? 44.237 0.393   46.831  1.00 25.88 ? 74   GLN   C O   1 
ATOM   4812  C  CB  . GLN   C  1 74  ? 43.987 3.623   46.224  1.00 26.24 ? 74   GLN   C CB  1 
ATOM   4813  C  CG  . GLN   C  1 74  ? 44.465 5.010   46.496  1.00 26.31 ? 74   GLN   C CG  1 
ATOM   4814  C  CD  . GLN   C  1 74  ? 44.209 5.924   45.310  1.00 31.98 ? 74   GLN   C CD  1 
ATOM   4815  O  OE1 . GLN   C  1 74  ? 44.619 5.626   44.180  1.00 33.27 ? 74   GLN   C OE1 1 
ATOM   4816  N  NE2 . GLN   C  1 74  ? 43.475 7.011   45.550  1.00 34.74 ? 74   GLN   C NE2 1 
ATOM   4817  N  N   . ASP   C  1 75  ? 42.223 1.356   47.317  1.00 28.37 ? 75   ASP   C N   1 
ATOM   4818  C  CA  . ASP   C  1 75  ? 41.427 0.139   47.119  1.00 31.39 ? 75   ASP   C CA  1 
ATOM   4819  C  C   . ASP   C  1 75  ? 41.235 -0.106  45.622  1.00 35.41 ? 75   ASP   C C   1 
ATOM   4820  O  O   . ASP   C  1 75  ? 40.118 -0.137  45.112  1.00 40.29 ? 75   ASP   C O   1 
ATOM   4821  C  CB  . ASP   C  1 75  ? 40.066 0.247   47.809  1.00 34.39 ? 75   ASP   C CB  1 
ATOM   4822  C  CG  . ASP   C  1 75  ? 40.115 0.015   49.310  1.00 37.04 ? 75   ASP   C CG  1 
ATOM   4823  O  OD1 . ASP   C  1 75  ? 41.162 -0.388  49.823  1.00 33.95 ? 75   ASP   C OD1 1 
ATOM   4824  O  OD2 . ASP   C  1 75  ? 39.066 0.209   49.991  1.00 39.26 ? 75   ASP   C OD2 1 
ATOM   4825  N  N   . LYS   C  1 76  ? 42.343 -0.212  44.901  1.00 32.29 ? 76   LYS   C N   1 
ATOM   4826  C  CA  . LYS   C  1 76  ? 42.253 -0.413  43.462  1.00 33.08 ? 76   LYS   C CA  1 
ATOM   4827  C  C   . LYS   C  1 76  ? 42.562 -1.869  43.129  1.00 33.36 ? 76   LYS   C C   1 
ATOM   4828  O  O   . LYS   C  1 76  ? 41.617 -2.632  42.876  1.00 36.00 ? 76   LYS   C O   1 
ATOM   4829  C  CB  . LYS   C  1 76  ? 43.152 0.586   42.724  1.00 34.61 ? 76   LYS   C CB  1 
ATOM   4830  C  CG  . LYS   C  1 76  ? 42.534 2.029   42.775  1.00 37.35 ? 76   LYS   C CG  1 
ATOM   4831  C  CD  . LYS   C  1 76  ? 43.357 3.125   42.035  1.00 37.23 ? 76   LYS   C CD  1 
ATOM   4832  C  CE  . LYS   C  1 76  ? 42.523 4.429   41.961  1.00 37.74 ? 76   LYS   C CE  1 
ATOM   4833  N  NZ  . LYS   C  1 76  ? 43.331 5.630   41.636  1.00 38.77 ? 76   LYS   C NZ  1 
ATOM   4834  N  N   . ALA   C  1 77  ? 43.828 -2.301  43.205  1.00 27.18 ? 77   ALA   C N   1 
ATOM   4835  C  CA  . ALA   C  1 77  ? 44.154 -3.693  42.907  1.00 26.39 ? 77   ALA   C CA  1 
ATOM   4836  C  C   . ALA   C  1 77  ? 43.826 -4.494  44.154  1.00 26.59 ? 77   ALA   C C   1 
ATOM   4837  O  O   . ALA   C  1 77  ? 44.573 -4.460  45.141  1.00 24.67 ? 77   ALA   C O   1 
ATOM   4838  C  CB  . ALA   C  1 77  ? 45.615 -3.850  42.522  1.00 28.34 ? 77   ALA   C CB  1 
ATOM   4839  N  N   . VAL   C  1 78  ? 42.701 -5.222  44.126  1.00 26.36 ? 78   VAL   C N   1 
ATOM   4840  C  CA  . VAL   C  1 78  ? 42.200 -5.875  45.323  1.00 27.09 ? 78   VAL   C CA  1 
ATOM   4841  C  C   . VAL   C  1 78  ? 41.670 -7.250  44.995  1.00 26.44 ? 78   VAL   C C   1 
ATOM   4842  O  O   . VAL   C  1 78  ? 41.251 -7.534  43.871  1.00 27.21 ? 78   VAL   C O   1 
ATOM   4843  C  CB  . VAL   C  1 78  ? 41.071 -5.081  46.002  1.00 25.42 ? 78   VAL   C CB  1 
ATOM   4844  C  CG1 . VAL   C  1 78  ? 41.553 -3.672  46.350  1.00 26.65 ? 78   VAL   C CG1 1 
ATOM   4845  C  CG2 . VAL   C  1 78  ? 39.882 -5.022  45.150  1.00 28.88 ? 78   VAL   C CG2 1 
ATOM   4846  N  N   . LEU   C  1 79  ? 41.590 -8.056  46.051  1.00 25.32 ? 79   LEU   C N   1 
ATOM   4847  C  CA  . LEU   C  1 79  ? 40.926 -9.343  46.050  1.00 24.85 ? 79   LEU   C CA  1 
ATOM   4848  C  C   . LEU   C  1 79  ? 39.769 -9.269  47.043  1.00 26.54 ? 79   LEU   C C   1 
ATOM   4849  O  O   . LEU   C  1 79  ? 39.950 -8.754  48.153  1.00 29.02 ? 79   LEU   C O   1 
ATOM   4850  C  CB  . LEU   C  1 79  ? 41.977 -10.375 46.460  1.00 26.19 ? 79   LEU   C CB  1 
ATOM   4851  C  CG  . LEU   C  1 79  ? 41.716 -11.833 46.369  1.00 29.99 ? 79   LEU   C CG  1 
ATOM   4852  C  CD1 . LEU   C  1 79  ? 41.498 -12.097 44.907  1.00 33.43 ? 79   LEU   C CD1 1 
ATOM   4853  C  CD2 . LEU   C  1 79  ? 42.962 -12.536 46.876  1.00 23.50 ? 79   LEU   C CD2 1 
ATOM   4854  N  N   . LYS   C  1 80  ? 38.581 -9.757  46.658  1.00 26.54 ? 80   LYS   C N   1 
ATOM   4855  C  CA  . LYS   C  1 80  ? 37.385 -9.736  47.495  1.00 28.63 ? 80   LYS   C CA  1 
ATOM   4856  C  C   . LYS   C  1 80  ? 36.604 -11.016 47.216  1.00 28.31 ? 80   LYS   C C   1 
ATOM   4857  O  O   . LYS   C  1 80  ? 36.862 -11.702 46.225  1.00 29.70 ? 80   LYS   C O   1 
ATOM   4858  C  CB  . LYS   C  1 80  ? 36.482 -8.525  47.209  1.00 33.66 ? 80   LYS   C CB  1 
ATOM   4859  C  CG  . LYS   C  1 80  ? 37.128 -7.156  47.508  1.00 35.20 ? 80   LYS   C CG  1 
ATOM   4860  C  CD  . LYS   C  1 80  ? 36.151 -5.994  47.344  1.00 36.86 ? 80   LYS   C CD  1 
ATOM   4861  C  CE  . LYS   C  1 80  ? 35.600 -5.975  45.950  1.00 43.69 ? 80   LYS   C CE  1 
ATOM   4862  N  NZ  . LYS   C  1 80  ? 34.845 -4.702  45.641  1.00 49.36 ? 80   LYS   C NZ  1 
ATOM   4863  N  N   . GLY   C  1 81  ? 35.625 -11.332 48.099  1.00 27.09 ? 81   GLY   C N   1 
ATOM   4864  C  CA  . GLY   C  1 81  ? 34.782 -12.505 47.890  1.00 27.53 ? 81   GLY   C CA  1 
ATOM   4865  C  C   . GLY   C  1 81  ? 35.517 -13.796 48.235  1.00 27.74 ? 81   GLY   C C   1 
ATOM   4866  O  O   . GLY   C  1 81  ? 36.480 -13.836 49.004  1.00 26.42 ? 81   GLY   C O   1 
ATOM   4867  N  N   . GLY   C  1 82  ? 35.020 -14.886 47.652  1.00 27.83 ? 82   GLY   C N   1 
ATOM   4868  C  CA  . GLY   C  1 82  ? 35.531 -16.189 47.991  1.00 27.35 ? 82   GLY   C CA  1 
ATOM   4869  C  C   . GLY   C  1 82  ? 35.395 -16.423 49.482  1.00 27.65 ? 82   GLY   C C   1 
ATOM   4870  O  O   . GLY   C  1 82  ? 34.319 -16.230 50.047  1.00 30.04 ? 82   GLY   C O   1 
ATOM   4871  N  N   . PRO   C  1 83  ? 36.490 -16.844 50.139  1.00 26.24 ? 83   PRO   C N   1 
ATOM   4872  C  CA  . PRO   C  1 83  ? 36.486 -17.037 51.601  1.00 25.98 ? 83   PRO   C CA  1 
ATOM   4873  C  C   . PRO   C  1 83  ? 36.700 -15.761 52.398  1.00 29.17 ? 83   PRO   C C   1 
ATOM   4874  O  O   . PRO   C  1 83  ? 36.727 -15.837 53.636  1.00 31.81 ? 83   PRO   C O   1 
ATOM   4875  C  CB  . PRO   C  1 83  ? 37.678 -17.994 51.816  1.00 23.85 ? 83   PRO   C CB  1 
ATOM   4876  C  CG  . PRO   C  1 83  ? 38.677 -17.521 50.763  1.00 22.93 ? 83   PRO   C CG  1 
ATOM   4877  C  CD  . PRO   C  1 83  ? 37.784 -17.197 49.541  1.00 25.03 ? 83   PRO   C CD  1 
ATOM   4878  N  N   . LEU   C  1 84  ? 36.910 -14.611 51.727  1.00 26.60 ? 84   LEU   C N   1 
ATOM   4879  C  CA  . LEU   C  1 84  ? 37.378 -13.398 52.387  1.00 24.51 ? 84   LEU   C CA  1 
ATOM   4880  C  C   . LEU   C  1 84  ? 36.215 -12.545 52.866  1.00 24.31 ? 84   LEU   C C   1 
ATOM   4881  O  O   . LEU   C  1 84  ? 35.236 -12.339 52.140  1.00 26.78 ? 84   LEU   C O   1 
ATOM   4882  C  CB  . LEU   C  1 84  ? 38.206 -12.560 51.409  1.00 23.04 ? 84   LEU   C CB  1 
ATOM   4883  C  CG  . LEU   C  1 84  ? 39.334 -13.379 50.774  1.00 23.77 ? 84   LEU   C CG  1 
ATOM   4884  C  CD1 . LEU   C  1 84  ? 40.024 -12.489 49.671  1.00 24.78 ? 84   LEU   C CD1 1 
ATOM   4885  C  CD2 . LEU   C  1 84  ? 40.366 -13.843 51.839  1.00 22.23 ? 84   LEU   C CD2 1 
ATOM   4886  N  N   . ASP   C  1 85  ? 36.385 -11.978 54.051  1.00 28.55 ? 85   ASP   C N   1 
ATOM   4887  C  CA  . ASP   C  1 85  ? 35.555 -10.874 54.518  1.00 29.81 ? 85   ASP   C CA  1 
ATOM   4888  C  C   . ASP   C  1 85  ? 36.313 -9.579  54.298  1.00 28.69 ? 85   ASP   C C   1 
ATOM   4889  O  O   . ASP   C  1 85  ? 37.480 -9.475  54.705  1.00 29.28 ? 85   ASP   C O   1 
ATOM   4890  C  CB  . ASP   C  1 85  ? 35.223 -11.055 55.994  1.00 31.78 ? 85   ASP   C CB  1 
ATOM   4891  C  CG  . ASP   C  1 85  ? 34.380 -12.302 56.230  1.00 39.67 ? 85   ASP   C CG  1 
ATOM   4892  O  OD1 . ASP   C  1 85  ? 33.358 -12.466 55.513  1.00 42.47 ? 85   ASP   C OD1 1 
ATOM   4893  O  OD2 . ASP   C  1 85  ? 34.769 -13.132 57.083  1.00 41.40 ? 85   ASP   C OD2 1 
ATOM   4894  N  N   . GLY   C  1 86  ? 35.686 -8.612  53.640  1.00 30.71 ? 86   GLY   C N   1 
ATOM   4895  C  CA  . GLY   C  1 86  ? 36.365 -7.331  53.435  1.00 30.15 ? 86   GLY   C CA  1 
ATOM   4896  C  C   . GLY   C  1 86  ? 37.198 -7.292  52.163  1.00 31.60 ? 86   GLY   C C   1 
ATOM   4897  O  O   . GLY   C  1 86  ? 37.026 -8.086  51.232  1.00 31.12 ? 86   GLY   C O   1 
ATOM   4898  N  N   . THR   C  1 87  ? 38.160 -6.368  52.154  1.00 26.17 ? 87   THR   C N   1 
ATOM   4899  C  CA  . THR   C  1 87  ? 38.899 -6.027  50.951  1.00 23.83 ? 87   THR   C CA  1 
ATOM   4900  C  C   . THR   C  1 87  ? 40.366 -6.248  51.220  1.00 24.00 ? 87   THR   C C   1 
ATOM   4901  O  O   . THR   C  1 87  ? 40.879 -5.799  52.259  1.00 25.37 ? 87   THR   C O   1 
ATOM   4902  C  CB  . THR   C  1 87  ? 38.658 -4.567  50.575  1.00 25.82 ? 87   THR   C CB  1 
ATOM   4903  O  OG1 . THR   C  1 87  ? 37.264 -4.405  50.247  1.00 29.64 ? 87   THR   C OG1 1 
ATOM   4904  C  CG2 . THR   C  1 87  ? 39.540 -4.129  49.368  1.00 27.17 ? 87   THR   C CG2 1 
ATOM   4905  N  N   . TYR   C  1 88  ? 41.054 -6.936  50.304  1.00 23.35 ? 88   TYR   C N   1 
ATOM   4906  C  CA  . TYR   C  1 88  ? 42.485 -7.208  50.488  1.00 20.44 ? 88   TYR   C CA  1 
ATOM   4907  C  C   . TYR   C  1 88  ? 43.279 -6.595  49.340  1.00 22.23 ? 88   TYR   C C   1 
ATOM   4908  O  O   . TYR   C  1 88  ? 43.041 -6.918  48.171  1.00 22.62 ? 88   TYR   C O   1 
ATOM   4909  C  CB  . TYR   C  1 88  ? 42.746 -8.715  50.555  1.00 20.11 ? 88   TYR   C CB  1 
ATOM   4910  C  CG  . TYR   C  1 88  ? 42.277 -9.390  51.828  1.00 18.51 ? 88   TYR   C CG  1 
ATOM   4911  C  CD1 . TYR   C  1 88  ? 40.902 -9.525  52.101  1.00 20.10 ? 88   TYR   C CD1 1 
ATOM   4912  C  CD2 . TYR   C  1 88  ? 43.209 -9.939  52.711  1.00 17.96 ? 88   TYR   C CD2 1 
ATOM   4913  C  CE1 . TYR   C  1 88  ? 40.475 -10.201 53.263  1.00 20.81 ? 88   TYR   C CE1 1 
ATOM   4914  C  CE2 . TYR   C  1 88  ? 42.791 -10.571 53.879  1.00 17.85 ? 88   TYR   C CE2 1 
ATOM   4915  C  CZ  . TYR   C  1 88  ? 41.425 -10.716 54.145  1.00 22.26 ? 88   TYR   C CZ  1 
ATOM   4916  O  OH  . TYR   C  1 88  ? 41.010 -11.396 55.306  1.00 22.95 ? 88   TYR   C OH  1 
ATOM   4917  N  N   . ARG   C  1 89  ? 44.208 -5.692  49.673  1.00 21.73 ? 89   ARG   C N   1 
ATOM   4918  C  CA  . ARG   C  1 89  ? 44.983 -4.951  48.672  1.00 21.40 ? 89   ARG   C CA  1 
ATOM   4919  C  C   . ARG   C  1 89  ? 46.224 -5.716  48.240  1.00 19.51 ? 89   ARG   C C   1 
ATOM   4920  O  O   . ARG   C  1 89  ? 46.977 -6.201  49.082  1.00 19.40 ? 89   ARG   C O   1 
ATOM   4921  C  CB  . ARG   C  1 89  ? 45.444 -3.602  49.219  1.00 20.58 ? 89   ARG   C CB  1 
ATOM   4922  C  CG  . ARG   C  1 89  ? 44.332 -2.569  49.314  1.00 24.80 ? 89   ARG   C CG  1 
ATOM   4923  C  CD  . ARG   C  1 89  ? 44.959 -1.213  49.708  1.00 22.34 ? 89   ARG   C CD  1 
ATOM   4924  N  NE  . ARG   C  1 89  ? 43.914 -0.283  50.164  1.00 24.89 ? 89   ARG   C NE  1 
ATOM   4925  C  CZ  . ARG   C  1 89  ? 44.132 0.815   50.883  1.00 23.78 ? 89   ARG   C CZ  1 
ATOM   4926  N  NH1 . ARG   C  1 89  ? 45.367 1.177   51.222  1.00 24.26 ? 89   ARG   C NH1 1 
ATOM   4927  N  NH2 . ARG   C  1 89  ? 43.080 1.531   51.285  1.00 29.89 ? 89   ARG   C NH2 1 
ATOM   4928  N  N   . LEU   C  1 90  ? 46.445 -5.796  46.924  1.00 19.38 ? 90   LEU   C N   1 
ATOM   4929  C  CA  . LEU   C  1 90  ? 47.685 -6.352  46.376  1.00 18.51 ? 90   LEU   C CA  1 
ATOM   4930  C  C   . LEU   C  1 90  ? 48.880 -5.496  46.780  1.00 19.09 ? 90   LEU   C C   1 
ATOM   4931  O  O   . LEU   C  1 90  ? 48.890 -4.278  46.512  1.00 20.57 ? 90   LEU   C O   1 
ATOM   4932  C  CB  . LEU   C  1 90  ? 47.563 -6.384  44.839  1.00 20.18 ? 90   LEU   C CB  1 
ATOM   4933  C  CG  . LEU   C  1 90  ? 48.849 -6.902  44.145  1.00 19.83 ? 90   LEU   C CG  1 
ATOM   4934  C  CD1 . LEU   C  1 90  ? 49.130 -8.367  44.470  1.00 19.43 ? 90   LEU   C CD1 1 
ATOM   4935  C  CD2 . LEU   C  1 90  ? 48.744 -6.659  42.643  1.00 22.32 ? 90   LEU   C CD2 1 
ATOM   4936  N  N   . ILE   C  1 91  ? 49.880 -6.106  47.433  1.00 17.24 ? 91   ILE   C N   1 
ATOM   4937  C  CA  . ILE   C  1 91  ? 51.117 -5.395  47.745  1.00 18.17 ? 91   ILE   C CA  1 
ATOM   4938  C  C   . ILE   C  1 91  ? 52.289 -5.859  46.872  1.00 19.01 ? 91   ILE   C C   1 
ATOM   4939  O  O   . ILE   C  1 91  ? 53.131 -5.042  46.484  1.00 17.96 ? 91   ILE   C O   1 
ATOM   4940  C  CB  . ILE   C  1 91  ? 51.452 -5.469  49.257  1.00 17.77 ? 91   ILE   C CB  1 
ATOM   4941  C  CG1 . ILE   C  1 91  ? 52.778 -4.735  49.519  1.00 18.36 ? 91   ILE   C CG1 1 
ATOM   4942  C  CG2 . ILE   C  1 91  ? 51.555 -6.904  49.787  1.00 18.93 ? 91   ILE   C CG2 1 
ATOM   4943  C  CD1 . ILE   C  1 91  ? 53.015 -4.451  50.987  1.00 19.56 ? 91   ILE   C CD1 1 
ATOM   4944  N  N   . GLN   C  1 92  ? 52.377 -7.143  46.543  1.00 17.49 ? 92   GLN   C N   1 
ATOM   4945  C  CA  . GLN   C  1 92  ? 53.535 -7.637  45.785  1.00 16.72 ? 92   GLN   C CA  1 
ATOM   4946  C  C   . GLN   C  1 92  ? 53.214 -9.026  45.246  1.00 17.36 ? 92   GLN   C C   1 
ATOM   4947  O  O   . GLN   C  1 92  ? 52.315 -9.710  45.759  1.00 18.61 ? 92   GLN   C O   1 
ATOM   4948  C  CB  . GLN   C  1 92  ? 54.822 -7.699  46.635  1.00 16.92 ? 92   GLN   C CB  1 
ATOM   4949  C  CG  . GLN   C  1 92  ? 54.685 -8.616  47.898  1.00 17.55 ? 92   GLN   C CG  1 
ATOM   4950  C  CD  . GLN   C  1 92  ? 55.516 -9.887  47.794  1.00 16.50 ? 92   GLN   C CD  1 
ATOM   4951  O  OE1 . GLN   C  1 92  ? 55.422 -10.633 46.811  1.00 17.89 ? 92   GLN   C OE1 1 
ATOM   4952  N  NE2 . GLN   C  1 92  ? 56.332 -10.161 48.841  1.00 19.24 ? 92   GLN   C NE2 1 
ATOM   4953  N  N   . PHE   C  1 93  ? 53.969 -9.435  44.209  1.00 16.61 ? 93   PHE   C N   1 
ATOM   4954  C  CA  . PHE   C  1 93  ? 54.017 -10.859 43.880  1.00 15.75 ? 93   PHE   C CA  1 
ATOM   4955  C  C   . PHE   C  1 93  ? 55.461 -11.325 43.755  1.00 17.54 ? 93   PHE   C C   1 
ATOM   4956  O  O   . PHE   C  1 93  ? 56.378 -10.539 43.541  1.00 16.68 ? 93   PHE   C O   1 
ATOM   4957  C  CB  . PHE   C  1 93  ? 53.207 -11.201 42.589  1.00 18.25 ? 93   PHE   C CB  1 
ATOM   4958  C  CG  . PHE   C  1 93  ? 53.789 -10.681 41.305  1.00 17.51 ? 93   PHE   C CG  1 
ATOM   4959  C  CD1 . PHE   C  1 93  ? 54.901 -11.308 40.688  1.00 17.34 ? 93   PHE   C CD1 1 
ATOM   4960  C  CD2 . PHE   C  1 93  ? 53.182 -9.602  40.672  1.00 18.69 ? 93   PHE   C CD2 1 
ATOM   4961  C  CE1 . PHE   C  1 93  ? 55.406 -10.845 39.488  1.00 18.30 ? 93   PHE   C CE1 1 
ATOM   4962  C  CE2 . PHE   C  1 93  ? 53.687 -9.111  39.454  1.00 20.17 ? 93   PHE   C CE2 1 
ATOM   4963  C  CZ  . PHE   C  1 93  ? 54.787 -9.725  38.865  1.00 19.61 ? 93   PHE   C CZ  1 
ATOM   4964  N  N   . HIS   C  1 94  ? 55.649 -12.633 43.867  1.00 16.26 ? 94   HIS   C N   1 
ATOM   4965  C  CA  . HIS   C  1 94  ? 56.958 -13.267 43.761  1.00 16.50 ? 94   HIS   C CA  1 
ATOM   4966  C  C   . HIS   C  1 94  ? 56.693 -14.720 43.372  1.00 16.17 ? 94   HIS   C C   1 
ATOM   4967  O  O   . HIS   C  1 94  ? 55.553 -15.165 43.360  1.00 16.96 ? 94   HIS   C O   1 
ATOM   4968  C  CB  . HIS   C  1 94  ? 57.736 -13.212 45.092  1.00 14.44 ? 94   HIS   C CB  1 
ATOM   4969  C  CG  . HIS   C  1 94  ? 56.994 -13.911 46.204  1.00 13.13 ? 94   HIS   C CG  1 
ATOM   4970  N  ND1 . HIS   C  1 94  ? 56.014 -13.289 46.959  1.00 15.26 ? 94   HIS   C ND1 1 
ATOM   4971  C  CD2 . HIS   C  1 94  ? 57.026 -15.197 46.608  1.00 14.66 ? 94   HIS   C CD2 1 
ATOM   4972  C  CE1 . HIS   C  1 94  ? 55.490 -14.167 47.809  1.00 15.51 ? 94   HIS   C CE1 1 
ATOM   4973  N  NE2 . HIS   C  1 94  ? 56.063 -15.344 47.602  1.00 14.38 ? 94   HIS   C NE2 1 
ATOM   4974  N  N   . PHE   C  1 95  ? 57.769 -15.472 43.134  1.00 15.94 ? 95   PHE   C N   1 
ATOM   4975  C  CA  . PHE   C  1 95  ? 57.700 -16.863 42.715  1.00 15.79 ? 95   PHE   C CA  1 
ATOM   4976  C  C   . PHE   C  1 95  ? 58.584 -17.713 43.613  1.00 17.59 ? 95   PHE   C C   1 
ATOM   4977  O  O   . PHE   C  1 95  ? 59.499 -17.227 44.304  1.00 17.48 ? 95   PHE   C O   1 
ATOM   4978  C  CB  . PHE   C  1 95  ? 58.163 -17.076 41.247  1.00 16.50 ? 95   PHE   C CB  1 
ATOM   4979  C  CG  . PHE   C  1 95  ? 57.385 -16.317 40.209  1.00 16.93 ? 95   PHE   C CG  1 
ATOM   4980  C  CD1 . PHE   C  1 95  ? 57.626 -14.946 40.015  1.00 17.43 ? 95   PHE   C CD1 1 
ATOM   4981  C  CD2 . PHE   C  1 95  ? 56.421 -16.946 39.426  1.00 18.27 ? 95   PHE   C CD2 1 
ATOM   4982  C  CE1 . PHE   C  1 95  ? 56.937 -14.252 39.023  1.00 18.46 ? 95   PHE   C CE1 1 
ATOM   4983  C  CE2 . PHE   C  1 95  ? 55.705 -16.221 38.433  1.00 19.80 ? 95   PHE   C CE2 1 
ATOM   4984  C  CZ  . PHE   C  1 95  ? 55.976 -14.868 38.240  1.00 21.15 ? 95   PHE   C CZ  1 
ATOM   4985  N  N   . HIS   C  1 96  ? 58.306 -19.015 43.563  1.00 16.12 ? 96   HIS   C N   1 
ATOM   4986  C  CA  . HIS   C  1 96  ? 59.147 -20.068 44.107  1.00 15.90 ? 96   HIS   C CA  1 
ATOM   4987  C  C   . HIS   C  1 96  ? 59.429 -21.036 42.968  1.00 16.46 ? 96   HIS   C C   1 
ATOM   4988  O  O   . HIS   C  1 96  ? 58.532 -21.326 42.189  1.00 17.11 ? 96   HIS   C O   1 
ATOM   4989  C  CB  . HIS   C  1 96  ? 58.413 -20.795 45.265  1.00 16.45 ? 96   HIS   C CB  1 
ATOM   4990  C  CG  . HIS   C  1 96  ? 58.000 -19.884 46.391  1.00 15.71 ? 96   HIS   C CG  1 
ATOM   4991  N  ND1 . HIS   C  1 96  ? 58.743 -19.734 47.548  1.00 17.19 ? 96   HIS   C ND1 1 
ATOM   4992  C  CD2 . HIS   C  1 96  ? 56.944 -19.026 46.501  1.00 15.23 ? 96   HIS   C CD2 1 
ATOM   4993  C  CE1 . HIS   C  1 96  ? 58.130 -18.853 48.343  1.00 15.66 ? 96   HIS   C CE1 1 
ATOM   4994  N  NE2 . HIS   C  1 96  ? 57.050 -18.382 47.722  1.00 16.33 ? 96   HIS   C NE2 1 
ATOM   4995  N  N   . TRP   C  1 97  ? 60.669 -21.524 42.845  1.00 15.76 ? 97   TRP   C N   1 
ATOM   4996  C  CA  . TRP   C  1 97  ? 61.008 -22.414 41.723  1.00 15.57 ? 97   TRP   C CA  1 
ATOM   4997  C  C   . TRP   C  1 97  ? 62.144 -23.344 42.096  1.00 18.89 ? 97   TRP   C C   1 
ATOM   4998  O  O   . TRP   C  1 97  ? 62.734 -23.244 43.171  1.00 17.71 ? 97   TRP   C O   1 
ATOM   4999  C  CB  . TRP   C  1 97  ? 61.403 -21.626 40.479  1.00 16.98 ? 97   TRP   C CB  1 
ATOM   5000  C  CG  . TRP   C  1 97  ? 62.614 -20.739 40.669  1.00 17.44 ? 97   TRP   C CG  1 
ATOM   5001  C  CD1 . TRP   C  1 97  ? 63.912 -21.055 40.436  1.00 17.63 ? 97   TRP   C CD1 1 
ATOM   5002  C  CD2 . TRP   C  1 97  ? 62.606 -19.364 41.111  1.00 15.58 ? 97   TRP   C CD2 1 
ATOM   5003  N  NE1 . TRP   C  1 97  ? 64.749 -19.971 40.714  1.00 17.54 ? 97   TRP   C NE1 1 
ATOM   5004  C  CE2 . TRP   C  1 97  ? 63.968 -18.925 41.123  1.00 17.85 ? 97   TRP   C CE2 1 
ATOM   5005  C  CE3 . TRP   C  1 97  ? 61.585 -18.464 41.504  1.00 14.83 ? 97   TRP   C CE3 1 
ATOM   5006  C  CZ2 . TRP   C  1 97  ? 64.342 -17.601 41.502  1.00 17.55 ? 97   TRP   C CZ2 1 
ATOM   5007  C  CZ3 . TRP   C  1 97  ? 61.963 -17.185 41.885  1.00 16.61 ? 97   TRP   C CZ3 1 
ATOM   5008  C  CH2 . TRP   C  1 97  ? 63.325 -16.758 41.843  1.00 17.52 ? 97   TRP   C CH2 1 
ATOM   5009  N  N   . GLY   C  1 98  ? 62.436 -24.291 41.207  1.00 18.03 ? 98   GLY   C N   1 
ATOM   5010  C  CA  . GLY   C  1 98  ? 63.367 -25.356 41.498  1.00 18.43 ? 98   GLY   C CA  1 
ATOM   5011  C  C   . GLY   C  1 98  ? 64.702 -25.214 40.761  1.00 19.74 ? 98   GLY   C C   1 
ATOM   5012  O  O   . GLY   C  1 98  ? 64.940 -24.297 39.962  1.00 19.71 ? 98   GLY   C O   1 
ATOM   5013  N  N   . SER   C  1 99  ? 65.598 -26.166 41.074  1.00 20.27 ? 99   SER   C N   1 
ATOM   5014  C  CA  . SER   C  1 99  ? 66.839 -26.287 40.326  1.00 21.76 ? 99   SER   C CA  1 
ATOM   5015  C  C   . SER   C  1 99  ? 66.662 -27.011 38.995  1.00 22.32 ? 99   SER   C C   1 
ATOM   5016  O  O   . SER   C  1 99  ? 67.597 -27.006 38.194  1.00 24.50 ? 99   SER   C O   1 
ATOM   5017  C  CB  . SER   C  1 99  ? 67.903 -26.983 41.180  1.00 22.38 ? 99   SER   C CB  1 
ATOM   5018  O  OG  . SER   C  1 99  ? 67.388 -28.166 41.761  1.00 25.22 ? 99   SER   C OG  1 
ATOM   5019  N  N   . HIS   C  1 100 ? 65.503 -27.609 38.754  1.00 22.85 ? 100  HIS   C N   1 
ATOM   5020  C  CA  . HIS   C  1 100 ? 65.166 -28.216 37.477  1.00 22.83 ? 100  HIS   C CA  1 
ATOM   5021  C  C   . HIS   C  1 100 ? 63.657 -28.184 37.378  1.00 22.78 ? 100  HIS   C C   1 
ATOM   5022  O  O   . HIS   C  1 100 ? 62.973 -27.906 38.362  1.00 24.54 ? 100  HIS   C O   1 
ATOM   5023  C  CB  . HIS   C  1 100 ? 65.731 -29.643 37.366  1.00 24.19 ? 100  HIS   C CB  1 
ATOM   5024  C  CG  . HIS   C  1 100 ? 65.243 -30.562 38.427  1.00 24.76 ? 100  HIS   C CG  1 
ATOM   5025  N  ND1 . HIS   C  1 100 ? 64.078 -31.289 38.295  1.00 27.08 ? 100  HIS   C ND1 1 
ATOM   5026  C  CD2 . HIS   C  1 100 ? 65.736 -30.852 39.654  1.00 26.31 ? 100  HIS   C CD2 1 
ATOM   5027  C  CE1 . HIS   C  1 100 ? 63.883 -32.005 39.392  1.00 27.31 ? 100  HIS   C CE1 1 
ATOM   5028  N  NE2 . HIS   C  1 100 ? 64.873 -31.759 40.236  1.00 25.45 ? 100  HIS   C NE2 1 
ATOM   5029  N  N   . ASP   C  1 101 ? 63.134 -28.484 36.185  1.00 22.86 ? 101  ASP   C N   1 
ATOM   5030  C  CA  . ASP   C  1 101 ? 61.705 -28.298 35.954  1.00 24.33 ? 101  ASP   C CA  1 
ATOM   5031  C  C   . ASP   C  1 101 ? 60.825 -29.266 36.746  1.00 24.39 ? 101  ASP   C C   1 
ATOM   5032  O  O   . ASP   C  1 101 ? 59.609 -29.064 36.777  1.00 25.20 ? 101  ASP   C O   1 
ATOM   5033  C  CB  . ASP   C  1 101 ? 61.385 -28.471 34.482  1.00 27.00 ? 101  ASP   C CB  1 
ATOM   5034  C  CG  . ASP   C  1 101 ? 61.907 -27.334 33.607  1.00 25.93 ? 101  ASP   C CG  1 
ATOM   5035  O  OD1 . ASP   C  1 101 ? 62.396 -26.290 34.117  1.00 28.49 ? 101  ASP   C OD1 1 
ATOM   5036  O  OD2 . ASP   C  1 101 ? 61.792 -27.509 32.361  1.00 29.73 ? 101  ASP   C OD2 1 
ATOM   5037  N  N   . GLY   C  1 102 ? 61.390 -30.323 37.330  1.00 23.63 ? 102  GLY   C N   1 
ATOM   5038  C  CA  . GLY   C  1 102 ? 60.589 -31.313 38.014  1.00 23.56 ? 102  GLY   C CA  1 
ATOM   5039  C  C   . GLY   C  1 102 ? 60.210 -30.985 39.437  1.00 24.41 ? 102  GLY   C C   1 
ATOM   5040  O  O   . GLY   C  1 102 ? 59.489 -31.758 40.090  1.00 26.27 ? 102  GLY   C O   1 
ATOM   5041  N  N   . GLN   C  1 103 ? 60.664 -29.848 39.955  1.00 21.73 ? 103  GLN   C N   1 
ATOM   5042  C  CA  . GLN   C  1 103 ? 60.244 -29.394 41.276  1.00 21.02 ? 103  GLN   C CA  1 
ATOM   5043  C  C   . GLN   C  1 103 ? 60.280 -27.888 41.263  1.00 21.39 ? 103  GLN   C C   1 
ATOM   5044  O  O   . GLN   C  1 103 ? 60.797 -27.275 40.324  1.00 20.76 ? 103  GLN   C O   1 
ATOM   5045  C  CB  . GLN   C  1 103 ? 61.115 -29.970 42.420  1.00 21.33 ? 103  GLN   C CB  1 
ATOM   5046  C  CG  . GLN   C  1 103 ? 62.601 -29.559 42.335  1.00 23.14 ? 103  GLN   C CG  1 
ATOM   5047  C  CD  . GLN   C  1 103 ? 63.489 -30.357 43.275  1.00 23.13 ? 103  GLN   C CD  1 
ATOM   5048  O  OE1 . GLN   C  1 103 ? 63.191 -31.506 43.586  1.00 25.51 ? 103  GLN   C OE1 1 
ATOM   5049  N  NE2 . GLN   C  1 103 ? 64.567 -29.757 43.760  1.00 21.32 ? 103  GLN   C NE2 1 
ATOM   5050  N  N   . GLY   C  1 104 ? 59.753 -27.290 42.337  1.00 20.58 ? 104  GLY   C N   1 
ATOM   5051  C  CA  . GLY   C  1 104 ? 59.730 -25.842 42.419  1.00 17.45 ? 104  GLY   C CA  1 
ATOM   5052  C  C   . GLY   C  1 104 ? 58.505 -25.301 43.106  1.00 17.59 ? 104  GLY   C C   1 
ATOM   5053  O  O   . GLY   C  1 104 ? 58.611 -24.325 43.856  1.00 18.76 ? 104  GLY   C O   1 
ATOM   5054  N  N   . SER   C  1 105 ? 57.329 -25.888 42.830  1.00 17.60 ? 105  SER   C N   1 
ATOM   5055  C  CA  . SER   C  1 105 ? 56.154 -25.371 43.517  1.00 17.32 ? 105  SER   C CA  1 
ATOM   5056  C  C   . SER   C  1 105 ? 56.204 -25.681 45.014  1.00 16.96 ? 105  SER   C C   1 
ATOM   5057  O  O   . SER   C  1 105 ? 56.918 -26.593 45.480  1.00 17.28 ? 105  SER   C O   1 
ATOM   5058  C  CB  . SER   C  1 105 ? 54.870 -25.926 42.897  1.00 17.29 ? 105  SER   C CB  1 
ATOM   5059  O  OG  . SER   C  1 105 ? 54.673 -27.322 43.121  1.00 18.91 ? 105  SER   C OG  1 
ATOM   5060  N  N   . GLU   C  1 106 ? 55.406 -24.914 45.774  1.00 16.61 ? 106  GLU   C N   1 
ATOM   5061  C  CA  . GLU   C  1 106 ? 55.298 -25.083 47.229  1.00 14.38 ? 106  GLU   C CA  1 
ATOM   5062  C  C   . GLU   C  1 106 ? 54.112 -25.982 47.562  1.00 16.57 ? 106  GLU   C C   1 
ATOM   5063  O  O   . GLU   C  1 106 ? 54.280 -27.067 48.120  1.00 17.09 ? 106  GLU   C O   1 
ATOM   5064  C  CB  . GLU   C  1 106 ? 55.187 -23.710 47.913  1.00 17.28 ? 106  GLU   C CB  1 
ATOM   5065  C  CG  . GLU   C  1 106 ? 56.456 -22.878 47.693  1.00 17.02 ? 106  GLU   C CG  1 
ATOM   5066  C  CD  . GLU   C  1 106 ? 56.725 -21.947 48.848  1.00 16.40 ? 106  GLU   C CD  1 
ATOM   5067  O  OE1 . GLU   C  1 106 ? 55.843 -21.093 49.108  1.00 16.11 ? 106  GLU   C OE1 1 
ATOM   5068  O  OE2 . GLU   C  1 106 ? 57.795 -22.104 49.457  1.00 17.75 ? 106  GLU   C OE2 1 
ATOM   5069  N  N   . HIS   C  1 107 ? 52.917 -25.580 47.157  1.00 17.05 ? 107  HIS   C N   1 
ATOM   5070  C  CA  . HIS   C  1 107 ? 51.800 -26.494 47.206  1.00 18.42 ? 107  HIS   C CA  1 
ATOM   5071  C  C   . HIS   C  1 107 ? 52.010 -27.642 46.218  1.00 18.37 ? 107  HIS   C C   1 
ATOM   5072  O  O   . HIS   C  1 107 ? 52.702 -27.502 45.204  1.00 18.20 ? 107  HIS   C O   1 
ATOM   5073  C  CB  . HIS   C  1 107 ? 50.477 -25.751 46.933  1.00 16.68 ? 107  HIS   C CB  1 
ATOM   5074  C  CG  . HIS   C  1 107 ? 50.128 -24.806 48.036  1.00 17.12 ? 107  HIS   C CG  1 
ATOM   5075  N  ND1 . HIS   C  1 107 ? 50.584 -23.512 48.033  1.00 17.53 ? 107  HIS   C ND1 1 
ATOM   5076  C  CD2 . HIS   C  1 107 ? 49.498 -24.993 49.226  1.00 17.65 ? 107  HIS   C CD2 1 
ATOM   5077  C  CE1 . HIS   C  1 107 ? 50.190 -22.910 49.151  1.00 18.12 ? 107  HIS   C CE1 1 
ATOM   5078  N  NE2 . HIS   C  1 107 ? 49.534 -23.779 49.896  1.00 17.71 ? 107  HIS   C NE2 1 
ATOM   5079  N  N   . THR   C  1 108 ? 51.432 -28.795 46.541  1.00 17.09 ? 108  THR   C N   1 
ATOM   5080  C  CA  . THR   C  1 108 ? 51.363 -29.921 45.601  1.00 18.20 ? 108  THR   C CA  1 
ATOM   5081  C  C   . THR   C  1 108 ? 49.914 -30.305 45.414  1.00 19.85 ? 108  THR   C C   1 
ATOM   5082  O  O   . THR   C  1 108 ? 49.080 -29.970 46.241  1.00 19.43 ? 108  THR   C O   1 
ATOM   5083  C  CB  . THR   C  1 108 ? 52.175 -31.151 46.094  1.00 17.66 ? 108  THR   C CB  1 
ATOM   5084  O  OG1 . THR   C  1 108 ? 51.750 -31.537 47.408  1.00 19.49 ? 108  THR   C OG1 1 
ATOM   5085  C  CG2 . THR   C  1 108 ? 53.662 -30.864 46.174  1.00 20.24 ? 108  THR   C CG2 1 
ATOM   5086  N  N   . VAL   C  1 109 ? 49.617 -31.007 44.316  1.00 17.81 ? 109  VAL   C N   1 
ATOM   5087  C  CA  . VAL   C  1 109 ? 48.267 -31.489 43.995  1.00 19.00 ? 109  VAL   C CA  1 
ATOM   5088  C  C   . VAL   C  1 109 ? 48.392 -32.974 43.828  1.00 22.35 ? 109  VAL   C C   1 
ATOM   5089  O  O   . VAL   C  1 109 ? 49.046 -33.460 42.902  1.00 22.91 ? 109  VAL   C O   1 
ATOM   5090  C  CB  . VAL   C  1 109 ? 47.662 -30.795 42.756  1.00 21.41 ? 109  VAL   C CB  1 
ATOM   5091  C  CG1 . VAL   C  1 109 ? 46.229 -31.319 42.513  1.00 24.37 ? 109  VAL   C CG1 1 
ATOM   5092  C  CG2 . VAL   C  1 109 ? 47.610 -29.283 42.995  1.00 22.94 ? 109  VAL   C CG2 1 
ATOM   5093  N  N   . ASP   C  1 110 ? 47.766 -33.717 44.743  1.00 20.78 ? 110  ASP   C N   1 
ATOM   5094  C  CA  . ASP   C  1 110 ? 47.886 -35.172 44.758  1.00 20.87 ? 110  ASP   C CA  1 
ATOM   5095  C  C   . ASP   C  1 110 ? 49.357 -35.559 44.682  1.00 23.13 ? 110  ASP   C C   1 
ATOM   5096  O  O   . ASP   C  1 110 ? 49.765 -36.473 43.960  1.00 27.09 ? 110  ASP   C O   1 
ATOM   5097  C  CB  . ASP   C  1 110 ? 47.056 -35.820 43.629  1.00 24.72 ? 110  ASP   C CB  1 
ATOM   5098  C  CG  . ASP   C  1 110 ? 45.578 -35.528 43.779  1.00 31.29 ? 110  ASP   C CG  1 
ATOM   5099  O  OD1 . ASP   C  1 110 ? 45.086 -35.373 44.941  1.00 26.97 ? 110  ASP   C OD1 1 
ATOM   5100  O  OD2 . ASP   C  1 110 ? 44.891 -35.505 42.731  1.00 33.86 ? 110  ASP   C OD2 1 
ATOM   5101  N  N   . LYS   C  1 111 ? 50.169 -34.835 45.451  1.00 21.83 ? 111  LYS   C N   1 
ATOM   5102  C  CA  . LYS   C  1 111 ? 51.604 -35.040 45.663  1.00 22.75 ? 111  LYS   C CA  1 
ATOM   5103  C  C   . LYS   C  1 111 ? 52.447 -34.595 44.480  1.00 26.02 ? 111  LYS   C C   1 
ATOM   5104  O  O   . LYS   C  1 111 ? 53.686 -34.620 44.568  1.00 29.51 ? 111  LYS   C O   1 
ATOM   5105  C  CB  . LYS   C  1 111 ? 51.939 -36.504 46.011  1.00 25.59 ? 111  LYS   C CB  1 
ATOM   5106  C  CG  . LYS   C  1 111 ? 51.167 -37.042 47.203  1.00 32.64 ? 111  LYS   C CG  1 
ATOM   5107  C  CD  . LYS   C  1 111 ? 51.411 -36.173 48.427  1.00 39.55 ? 111  LYS   C CD  1 
ATOM   5108  C  CE  . LYS   C  1 111 ? 52.925 -36.134 48.727  1.00 43.55 ? 111  LYS   C CE  1 
ATOM   5109  N  NZ  . LYS   C  1 111 ? 53.296 -35.308 49.872  1.00 39.29 ? 111  LYS   C NZ  1 
ATOM   5110  N  N   . LYS   C  1 112 ? 51.839 -34.099 43.423  1.00 23.73 ? 112  LYS   C N   1 
ATOM   5111  C  CA  . LYS   C  1 112 ? 52.580 -33.687 42.239  1.00 26.31 ? 112  LYS   C CA  1 
ATOM   5112  C  C   . LYS   C  1 112 ? 53.080 -32.268 42.388  1.00 23.30 ? 112  LYS   C C   1 
ATOM   5113  O  O   . LYS   C  1 112 ? 52.349 -31.388 42.858  1.00 21.79 ? 112  LYS   C O   1 
ATOM   5114  C  CB  . LYS   C  1 112 ? 51.693 -33.759 41.005  1.00 31.38 ? 112  LYS   C CB  1 
ATOM   5115  C  CG  . LYS   C  1 112 ? 52.340 -33.173 39.755  1.00 40.70 ? 112  LYS   C CG  1 
ATOM   5116  C  CD  . LYS   C  1 112 ? 51.257 -32.837 38.698  1.00 46.81 ? 112  LYS   C CD  1 
ATOM   5117  C  CE  . LYS   C  1 112 ? 51.566 -31.493 38.048  1.00 47.96 ? 112  LYS   C CE  1 
ATOM   5118  N  NZ  . LYS   C  1 112 ? 52.870 -31.547 37.321  1.00 49.51 ? 112  LYS   C NZ  1 
ATOM   5119  N  N   . LYS   C  1 113 ? 54.325 -32.042 41.954  1.00 20.31 ? 113  LYS   C N   1 
ATOM   5120  C  CA  . LYS   C  1 113 ? 54.902 -30.707 41.933  1.00 20.73 ? 113  LYS   C CA  1 
ATOM   5121  C  C   . LYS   C  1 113 ? 54.889 -30.077 40.542  1.00 21.00 ? 113  LYS   C C   1 
ATOM   5122  O  O   . LYS   C  1 113 ? 54.942 -30.767 39.516  1.00 25.81 ? 113  LYS   C O   1 
ATOM   5123  C  CB  . LYS   C  1 113 ? 56.340 -30.774 42.440  1.00 20.38 ? 113  LYS   C CB  1 
ATOM   5124  C  CG  . LYS   C  1 113 ? 56.415 -31.037 43.903  1.00 22.63 ? 113  LYS   C CG  1 
ATOM   5125  C  CD  . LYS   C  1 113 ? 57.865 -31.044 44.377  1.00 26.60 ? 113  LYS   C CD  1 
ATOM   5126  C  CE  . LYS   C  1 113 ? 57.877 -31.060 45.906  1.00 25.80 ? 113  LYS   C CE  1 
ATOM   5127  N  NZ  . LYS   C  1 113 ? 59.211 -30.563 46.485  1.00 27.17 ? 113  LYS   C NZ  1 
ATOM   5128  N  N   . TYR   C  1 114 ? 54.773 -28.744 40.530  1.00 20.25 ? 114  TYR   C N   1 
ATOM   5129  C  CA  . TYR   C  1 114 ? 54.948 -27.977 39.305  1.00 24.06 ? 114  TYR   C CA  1 
ATOM   5130  C  C   . TYR   C  1 114 ? 56.333 -27.349 39.291  1.00 21.24 ? 114  TYR   C C   1 
ATOM   5131  O  O   . TYR   C  1 114 ? 57.019 -27.322 40.307  1.00 19.96 ? 114  TYR   C O   1 
ATOM   5132  C  CB  . TYR   C  1 114 ? 53.882 -26.888 39.202  1.00 23.56 ? 114  TYR   C CB  1 
ATOM   5133  C  CG  . TYR   C  1 114 ? 52.492 -27.439 38.997  1.00 24.14 ? 114  TYR   C CG  1 
ATOM   5134  C  CD1 . TYR   C  1 114 ? 51.688 -27.756 40.079  1.00 24.32 ? 114  TYR   C CD1 1 
ATOM   5135  C  CD2 . TYR   C  1 114 ? 51.979 -27.617 37.711  1.00 28.72 ? 114  TYR   C CD2 1 
ATOM   5136  C  CE1 . TYR   C  1 114 ? 50.406 -28.234 39.885  1.00 28.37 ? 114  TYR   C CE1 1 
ATOM   5137  C  CE2 . TYR   C  1 114 ? 50.695 -28.130 37.523  1.00 29.46 ? 114  TYR   C CE2 1 
ATOM   5138  C  CZ  . TYR   C  1 114 ? 49.934 -28.435 38.623  1.00 30.18 ? 114  TYR   C CZ  1 
ATOM   5139  O  OH  . TYR   C  1 114 ? 48.640 -28.912 38.444  1.00 35.01 ? 114  TYR   C OH  1 
ATOM   5140  N  N   . ALA   C  1 115 ? 56.712 -26.777 38.142  1.00 20.94 ? 115  ALA   C N   1 
ATOM   5141  C  CA  . ALA   C  1 115 ? 58.032 -26.171 38.014  1.00 19.65 ? 115  ALA   C CA  1 
ATOM   5142  C  C   . ALA   C  1 115 ? 58.170 -24.896 38.812  1.00 20.46 ? 115  ALA   C C   1 
ATOM   5143  O  O   . ALA   C  1 115 ? 59.300 -24.506 39.182  1.00 20.33 ? 115  ALA   C O   1 
ATOM   5144  C  CB  . ALA   C  1 115 ? 58.314 -25.867 36.526  1.00 22.93 ? 115  ALA   C CB  1 
ATOM   5145  N  N   . ALA   C  1 116 ? 57.067 -24.212 39.107  1.00 18.98 ? 116  ALA   C N   1 
ATOM   5146  C  CA  . ALA   C  1 116 ? 57.203 -23.005 39.913  1.00 19.59 ? 116  ALA   C CA  1 
ATOM   5147  C  C   . ALA   C  1 116 ? 55.816 -22.685 40.454  1.00 19.41 ? 116  ALA   C C   1 
ATOM   5148  O  O   . ALA   C  1 116 ? 54.824 -23.303 40.052  1.00 18.99 ? 116  ALA   C O   1 
ATOM   5149  C  CB  . ALA   C  1 116 ? 57.833 -21.828 39.110  1.00 19.24 ? 116  ALA   C CB  1 
ATOM   5150  N  N   . GLU   C  1 117 ? 55.764 -21.718 41.361  1.00 18.57 ? 117  GLU   C N   1 
ATOM   5151  C  CA  . GLU   C  1 117 ? 54.504 -21.257 41.927  1.00 17.70 ? 117  GLU   C CA  1 
ATOM   5152  C  C   . GLU   C  1 117 ? 54.601 -19.750 42.122  1.00 17.25 ? 117  GLU   C C   1 
ATOM   5153  O  O   . GLU   C  1 117 ? 55.604 -19.242 42.633  1.00 17.85 ? 117  GLU   C O   1 
ATOM   5154  C  CB  . GLU   C  1 117 ? 54.192 -21.975 43.254  1.00 17.05 ? 117  GLU   C CB  1 
ATOM   5155  C  CG  . GLU   C  1 117 ? 52.824 -21.654 43.833  1.00 17.82 ? 117  GLU   C CG  1 
ATOM   5156  C  CD  . GLU   C  1 117 ? 52.510 -22.530 45.032  1.00 18.93 ? 117  GLU   C CD  1 
ATOM   5157  O  OE1 . GLU   C  1 117 ? 52.915 -23.727 45.055  1.00 17.87 ? 117  GLU   C OE1 1 
ATOM   5158  O  OE2 . GLU   C  1 117 ? 51.829 -22.054 45.964  1.00 18.02 ? 117  GLU   C OE2 1 
ATOM   5159  N  N   . LEU   C  1 118 ? 53.545 -19.057 41.683  1.00 16.35 ? 118  LEU   C N   1 
ATOM   5160  C  CA  . LEU   C  1 118 ? 53.389 -17.619 41.792  1.00 16.55 ? 118  LEU   C CA  1 
ATOM   5161  C  C   . LEU   C  1 118 ? 52.514 -17.285 42.980  1.00 16.36 ? 118  LEU   C C   1 
ATOM   5162  O  O   . LEU   C  1 118 ? 51.449 -17.894 43.174  1.00 17.85 ? 118  LEU   C O   1 
ATOM   5163  C  CB  . LEU   C  1 118 ? 52.724 -17.106 40.509  1.00 17.11 ? 118  LEU   C CB  1 
ATOM   5164  C  CG  . LEU   C  1 118 ? 52.181 -15.680 40.545  1.00 17.78 ? 118  LEU   C CG  1 
ATOM   5165  C  CD1 . LEU   C  1 118 ? 53.288 -14.613 40.770  1.00 18.12 ? 118  LEU   C CD1 1 
ATOM   5166  C  CD2 . LEU   C  1 118 ? 51.489 -15.399 39.197  1.00 18.87 ? 118  LEU   C CD2 1 
ATOM   5167  N  N   . HIS   C  1 119 ? 52.958 -16.321 43.799  1.00 16.61 ? 119  HIS   C N   1 
ATOM   5168  C  CA  . HIS   C  1 119 ? 52.190 -15.843 44.957  1.00 15.91 ? 119  HIS   C CA  1 
ATOM   5169  C  C   . HIS   C  1 119 ? 51.898 -14.362 44.787  1.00 16.92 ? 119  HIS   C C   1 
ATOM   5170  O  O   . HIS   C  1 119 ? 52.841 -13.543 44.799  1.00 16.86 ? 119  HIS   C O   1 
ATOM   5171  C  CB  . HIS   C  1 119 ? 52.960 -16.038 46.268  1.00 16.24 ? 119  HIS   C CB  1 
ATOM   5172  C  CG  . HIS   C  1 119 ? 53.072 -17.477 46.631  1.00 15.29 ? 119  HIS   C CG  1 
ATOM   5173  N  ND1 . HIS   C  1 119 ? 53.986 -17.978 47.533  1.00 15.07 ? 119  HIS   C ND1 1 
ATOM   5174  C  CD2 . HIS   C  1 119 ? 52.324 -18.535 46.213  1.00 15.28 ? 119  HIS   C CD2 1 
ATOM   5175  C  CE1 . HIS   C  1 119 ? 53.826 -19.296 47.626  1.00 17.42 ? 119  HIS   C CE1 1 
ATOM   5176  N  NE2 . HIS   C  1 119 ? 52.838 -19.653 46.827  1.00 16.91 ? 119  HIS   C NE2 1 
ATOM   5177  N  N   . LEU   C  1 120 ? 50.616 -14.023 44.700  1.00 17.80 ? 120  LEU   C N   1 
ATOM   5178  C  CA  . LEU   C  1 120 ? 50.146 -12.633 44.719  1.00 16.91 ? 120  LEU   C CA  1 
ATOM   5179  C  C   . LEU   C  1 120 ? 49.679 -12.353 46.152  1.00 18.44 ? 120  LEU   C C   1 
ATOM   5180  O  O   . LEU   C  1 120 ? 48.737 -12.988 46.648  1.00 17.17 ? 120  LEU   C O   1 
ATOM   5181  C  CB  . LEU   C  1 120 ? 49.036 -12.436 43.691  1.00 18.99 ? 120  LEU   C CB  1 
ATOM   5182  C  CG  . LEU   C  1 120 ? 49.526 -12.570 42.255  1.00 19.27 ? 120  LEU   C CG  1 
ATOM   5183  C  CD1 . LEU   C  1 120 ? 48.626 -13.598 41.469  1.00 23.67 ? 120  LEU   C CD1 1 
ATOM   5184  C  CD2 . LEU   C  1 120 ? 49.600 -11.239 41.513  1.00 20.94 ? 120  LEU   C CD2 1 
ATOM   5185  N  N   . VAL   C  1 121 ? 50.342 -11.419 46.834  1.00 18.75 ? 121  VAL   C N   1 
ATOM   5186  C  CA  . VAL   C  1 121 ? 50.197 -11.204 48.269  1.00 17.43 ? 121  VAL   C CA  1 
ATOM   5187  C  C   . VAL   C  1 121 ? 49.309 -9.995  48.523  1.00 18.26 ? 121  VAL   C C   1 
ATOM   5188  O  O   . VAL   C  1 121 ? 49.577 -8.904  47.988  1.00 18.35 ? 121  VAL   C O   1 
ATOM   5189  C  CB  . VAL   C  1 121 ? 51.581 -10.972 48.892  1.00 15.84 ? 121  VAL   C CB  1 
ATOM   5190  C  CG1 . VAL   C  1 121 ? 51.469 -10.763 50.421  1.00 16.38 ? 121  VAL   C CG1 1 
ATOM   5191  C  CG2 . VAL   C  1 121 ? 52.523 -12.144 48.563  1.00 18.26 ? 121  VAL   C CG2 1 
ATOM   5192  N  N   . HIS   C  1 122 ? 48.275 -10.163 49.353  1.00 17.06 ? 122  HIS   C N   1 
ATOM   5193  C  CA  . HIS   C  1 122 ? 47.305 -9.104  49.641  1.00 17.78 ? 122  HIS   C CA  1 
ATOM   5194  C  C   . HIS   C  1 122 ? 47.082 -8.973  51.147  1.00 18.23 ? 122  HIS   C C   1 
ATOM   5195  O  O   . HIS   C  1 122 ? 47.134 -9.976  51.875  1.00 17.94 ? 122  HIS   C O   1 
ATOM   5196  C  CB  . HIS   C  1 122 ? 45.936 -9.385  48.995  1.00 18.52 ? 122  HIS   C CB  1 
ATOM   5197  C  CG  . HIS   C  1 122 ? 45.999 -9.828  47.562  1.00 17.50 ? 122  HIS   C CG  1 
ATOM   5198  N  ND1 . HIS   C  1 122 ? 46.411 -11.102 47.192  1.00 17.84 ? 122  HIS   C ND1 1 
ATOM   5199  C  CD2 . HIS   C  1 122 ? 45.638 -9.187  46.411  1.00 18.26 ? 122  HIS   C CD2 1 
ATOM   5200  C  CE1 . HIS   C  1 122 ? 46.347 -11.191 45.862  1.00 17.84 ? 122  HIS   C CE1 1 
ATOM   5201  N  NE2 . HIS   C  1 122 ? 45.852 -10.062 45.373  1.00 20.45 ? 122  HIS   C NE2 1 
ATOM   5202  N  N   . TRP   C  1 123 ? 46.781 -7.732  51.599  1.00 18.68 ? 123  TRP   C N   1 
ATOM   5203  C  CA  . TRP   C  1 123 ? 46.516 -7.508  53.022  1.00 18.31 ? 123  TRP   C CA  1 
ATOM   5204  C  C   . TRP   C  1 123 ? 45.175 -6.831  53.252  1.00 18.53 ? 123  TRP   C C   1 
ATOM   5205  O  O   . TRP   C  1 123 ? 44.663 -6.059  52.423  1.00 20.69 ? 123  TRP   C O   1 
ATOM   5206  C  CB  . TRP   C  1 123 ? 47.656 -6.700  53.699  1.00 16.82 ? 123  TRP   C CB  1 
ATOM   5207  C  CG  . TRP   C  1 123 ? 47.932 -5.368  53.031  1.00 18.21 ? 123  TRP   C CG  1 
ATOM   5208  C  CD1 . TRP   C  1 123 ? 48.771 -5.116  51.960  1.00 17.30 ? 123  TRP   C CD1 1 
ATOM   5209  C  CD2 . TRP   C  1 123 ? 47.349 -4.093  53.394  1.00 18.58 ? 123  TRP   C CD2 1 
ATOM   5210  N  NE1 . TRP   C  1 123 ? 48.782 -3.745  51.673  1.00 18.90 ? 123  TRP   C NE1 1 
ATOM   5211  C  CE2 . TRP   C  1 123 ? 47.884 -3.116  52.508  1.00 18.26 ? 123  TRP   C CE2 1 
ATOM   5212  C  CE3 . TRP   C  1 123 ? 46.436 -3.689  54.387  1.00 19.63 ? 123  TRP   C CE3 1 
ATOM   5213  C  CZ2 . TRP   C  1 123 ? 47.563 -1.766  52.623  1.00 18.42 ? 123  TRP   C CZ2 1 
ATOM   5214  C  CZ3 . TRP   C  1 123 ? 46.066 -2.353  54.466  1.00 19.96 ? 123  TRP   C CZ3 1 
ATOM   5215  C  CH2 . TRP   C  1 123 ? 46.637 -1.402  53.584  1.00 21.54 ? 123  TRP   C CH2 1 
ATOM   5216  N  N   . ASN   C  1 124 ? 44.598 -7.176  54.404  1.00 19.86 ? 124  ASN   C N   1 
ATOM   5217  C  CA  . ASN   C  1 124 ? 43.245 -6.789  54.786  1.00 19.71 ? 124  ASN   C CA  1 
ATOM   5218  C  C   . ASN   C  1 124 ? 43.200 -5.319  55.184  1.00 22.05 ? 124  ASN   C C   1 
ATOM   5219  O  O   . ASN   C  1 124 ? 43.862 -4.933  56.157  1.00 22.41 ? 124  ASN   C O   1 
ATOM   5220  C  CB  . ASN   C  1 124 ? 42.831 -7.703  55.945  1.00 20.76 ? 124  ASN   C CB  1 
ATOM   5221  C  CG  . ASN   C  1 124 ? 41.379 -7.556  56.310  1.00 23.35 ? 124  ASN   C CG  1 
ATOM   5222  O  OD1 . ASN   C  1 124 ? 40.714 -6.579  55.942  1.00 23.99 ? 124  ASN   C OD1 1 
ATOM   5223  N  ND2 . ASN   C  1 124 ? 40.849 -8.560  57.033  1.00 23.34 ? 124  ASN   C ND2 1 
ATOM   5224  N  N   . THR   C  1 125 ? 42.376 -4.509  54.466  1.00 21.17 ? 125  THR   C N   1 
ATOM   5225  C  CA  . THR   C  1 125 ? 42.312 -3.084  54.797  1.00 21.50 ? 125  THR   C CA  1 
ATOM   5226  C  C   . THR   C  1 125 ? 41.630 -2.820  56.142  1.00 25.30 ? 125  THR   C C   1 
ATOM   5227  O  O   . THR   C  1 125 ? 41.524 -1.659  56.562  1.00 29.02 ? 125  THR   C O   1 
ATOM   5228  C  CB  . THR   C  1 125 ? 41.586 -2.317  53.699  1.00 24.45 ? 125  THR   C CB  1 
ATOM   5229  O  OG1 . THR   C  1 125 ? 40.235 -2.805  53.610  1.00 27.20 ? 125  THR   C OG1 1 
ATOM   5230  C  CG2 . THR   C  1 125 ? 42.275 -2.485  52.384  1.00 23.04 ? 125  THR   C CG2 1 
ATOM   5231  N  N   . LYS   C  1 126 ? 41.129 -3.856  56.800  1.00 24.97 ? 126  LYS   C N   1 
ATOM   5232  C  CA  . LYS   C  1 126 ? 40.735 -3.761  58.201  1.00 28.36 ? 126  LYS   C CA  1 
ATOM   5233  C  C   . LYS   C  1 126 ? 41.880 -3.213  59.050  1.00 26.87 ? 126  LYS   C C   1 
ATOM   5234  O  O   . LYS   C  1 126 ? 41.654 -2.505  60.043  1.00 28.27 ? 126  LYS   C O   1 
ATOM   5235  C  CB  . LYS   C  1 126 ? 40.286 -5.168  58.648  1.00 30.40 ? 126  LYS   C CB  1 
ATOM   5236  C  CG  . LYS   C  1 126 ? 40.063 -5.397  60.133  1.00 30.58 ? 126  LYS   C CG  1 
ATOM   5237  C  CD  . LYS   C  1 126 ? 39.588 -6.850  60.396  1.00 31.25 ? 126  LYS   C CD  1 
ATOM   5238  C  CE  . LYS   C  1 126 ? 39.346 -7.056  61.914  1.00 34.15 ? 126  LYS   C CE  1 
ATOM   5239  N  NZ  . LYS   C  1 126 ? 39.013 -8.466  62.264  1.00 33.56 ? 126  LYS   C NZ  1 
ATOM   5240  N  N   . TYR   C  1 127 ? 43.113 -3.510  58.657  1.00 24.02 ? 127  TYR   C N   1 
ATOM   5241  C  CA  . TYR   C  1 127 ? 44.314 -3.145  59.390  1.00 24.40 ? 127  TYR   C CA  1 
ATOM   5242  C  C   . TYR   C  1 127 ? 45.004 -2.024  58.625  1.00 28.35 ? 127  TYR   C C   1 
ATOM   5243  O  O   . TYR   C  1 127 ? 44.641 -1.705  57.491  1.00 30.05 ? 127  TYR   C O   1 
ATOM   5244  C  CB  . TYR   C  1 127 ? 45.206 -4.404  59.600  1.00 21.54 ? 127  TYR   C CB  1 
ATOM   5245  C  CG  . TYR   C  1 127 ? 44.422 -5.530  60.250  1.00 23.66 ? 127  TYR   C CG  1 
ATOM   5246  C  CD1 . TYR   C  1 127 ? 43.927 -5.374  61.541  1.00 24.01 ? 127  TYR   C CD1 1 
ATOM   5247  C  CD2 . TYR   C  1 127 ? 44.128 -6.737  59.568  1.00 20.84 ? 127  TYR   C CD2 1 
ATOM   5248  C  CE1 . TYR   C  1 127 ? 43.191 -6.334  62.141  1.00 24.55 ? 127  TYR   C CE1 1 
ATOM   5249  C  CE2 . TYR   C  1 127 ? 43.385 -7.731  60.166  1.00 22.41 ? 127  TYR   C CE2 1 
ATOM   5250  C  CZ  . TYR   C  1 127 ? 42.904 -7.519  61.470  1.00 23.93 ? 127  TYR   C CZ  1 
ATOM   5251  O  OH  . TYR   C  1 127 ? 42.146 -8.471  62.102  1.00 25.98 ? 127  TYR   C OH  1 
ATOM   5252  N  N   . GLY   C  1 128 ? 45.991 -1.380  59.236  1.00 30.17 ? 128  GLY   C N   1 
ATOM   5253  C  CA  . GLY   C  1 128 ? 46.448 -0.129  58.636  1.00 28.85 ? 128  GLY   C CA  1 
ATOM   5254  C  C   . GLY   C  1 128 ? 47.330 -0.317  57.415  1.00 25.63 ? 128  GLY   C C   1 
ATOM   5255  O  O   . GLY   C  1 128 ? 47.424 0.577   56.552  1.00 28.69 ? 128  GLY   C O   1 
ATOM   5256  N  N   . ASP   C  1 129 ? 48.034 -1.429  57.358  1.00 22.67 ? 129  ASP   C N   1 
ATOM   5257  C  CA  . ASP   C  1 129 ? 49.064 -1.670  56.346  1.00 20.94 ? 129  ASP   C CA  1 
ATOM   5258  C  C   . ASP   C  1 129 ? 49.464 -3.138  56.463  1.00 21.39 ? 129  ASP   C C   1 
ATOM   5259  O  O   . ASP   C  1 129 ? 48.987 -3.867  57.356  1.00 20.46 ? 129  ASP   C O   1 
ATOM   5260  C  CB  . ASP   C  1 129 ? 50.289 -0.740  56.533  1.00 22.32 ? 129  ASP   C CB  1 
ATOM   5261  C  CG  . ASP   C  1 129 ? 50.803 -0.736  57.974  1.00 27.86 ? 129  ASP   C CG  1 
ATOM   5262  O  OD1 . ASP   C  1 129 ? 50.945 -1.812  58.541  1.00 25.24 ? 129  ASP   C OD1 1 
ATOM   5263  O  OD2 . ASP   C  1 129 ? 51.032 0.351   58.552  1.00 31.08 ? 129  ASP   C OD2 1 
ATOM   5264  N  N   . PHE   C  1 130 ? 50.380 -3.551  55.588  1.00 19.25 ? 130  PHE   C N   1 
ATOM   5265  C  CA  . PHE   C  1 130 ? 50.800 -4.946  55.561  1.00 19.17 ? 130  PHE   C CA  1 
ATOM   5266  C  C   . PHE   C  1 130 ? 51.397 -5.366  56.905  1.00 19.26 ? 130  PHE   C C   1 
ATOM   5267  O  O   . PHE   C  1 130 ? 51.087 -6.455  57.411  1.00 18.69 ? 130  PHE   C O   1 
ATOM   5268  C  CB  . PHE   C  1 130 ? 51.822 -5.194  54.438  1.00 19.23 ? 130  PHE   C CB  1 
ATOM   5269  C  CG  . PHE   C  1 130 ? 52.353 -6.582  54.436  1.00 17.56 ? 130  PHE   C CG  1 
ATOM   5270  C  CD1 . PHE   C  1 130 ? 53.460 -6.947  55.204  1.00 18.35 ? 130  PHE   C CD1 1 
ATOM   5271  C  CD2 . PHE   C  1 130 ? 51.754 -7.584  53.658  1.00 18.56 ? 130  PHE   C CD2 1 
ATOM   5272  C  CE1 . PHE   C  1 130 ? 53.926 -8.276  55.238  1.00 18.92 ? 130  PHE   C CE1 1 
ATOM   5273  C  CE2 . PHE   C  1 130 ? 52.238 -8.893  53.670  1.00 18.04 ? 130  PHE   C CE2 1 
ATOM   5274  C  CZ  . PHE   C  1 130 ? 53.323 -9.253  54.460  1.00 18.55 ? 130  PHE   C CZ  1 
ATOM   5275  N  N   . GLY   C  1 131 ? 52.240 -4.503  57.494  1.00 19.66 ? 131  GLY   C N   1 
ATOM   5276  C  CA  . GLY   C  1 131 ? 52.900 -4.880  58.745  1.00 19.10 ? 131  GLY   C CA  1 
ATOM   5277  C  C   . GLY   C  1 131 ? 51.935 -5.145  59.879  1.00 19.40 ? 131  GLY   C C   1 
ATOM   5278  O  O   . GLY   C  1 131 ? 52.163 -6.027  60.716  1.00 19.51 ? 131  GLY   C O   1 
ATOM   5279  N  N   . LYS   C  1 132 ? 50.848 -4.386  59.942  1.00 19.11 ? 132  LYS   C N   1 
ATOM   5280  C  CA  . LYS   C  1 132 ? 49.843 -4.673  60.952  1.00 18.32 ? 132  LYS   C CA  1 
ATOM   5281  C  C   . LYS   C  1 132 ? 49.058 -5.923  60.584  1.00 21.47 ? 132  LYS   C C   1 
ATOM   5282  O  O   . LYS   C  1 132 ? 48.733 -6.744  61.456  1.00 20.70 ? 132  LYS   C O   1 
ATOM   5283  C  CB  . LYS   C  1 132 ? 48.914 -3.455  61.102  1.00 18.99 ? 132  LYS   C CB  1 
ATOM   5284  C  CG  . LYS   C  1 132 ? 49.640 -2.276  61.721  1.00 22.61 ? 132  LYS   C CG  1 
ATOM   5285  C  CD  . LYS   C  1 132 ? 48.777 -1.001  61.681  1.00 27.43 ? 132  LYS   C CD  1 
ATOM   5286  C  CE  . LYS   C  1 132 ? 49.495 0.144   62.337  1.00 33.98 ? 132  LYS   C CE  1 
ATOM   5287  N  NZ  . LYS   C  1 132 ? 50.651 0.518   61.467  1.00 40.47 ? 132  LYS   C NZ  1 
ATOM   5288  N  N   . ALA   C  1 133 ? 48.733 -6.089  59.299  1.00 19.22 ? 133  ALA   C N   1 
ATOM   5289  C  CA  . ALA   C  1 133 ? 47.868 -7.198  58.905  1.00 18.19 ? 133  ALA   C CA  1 
ATOM   5290  C  C   . ALA   C  1 133 ? 48.544 -8.538  59.138  1.00 20.07 ? 133  ALA   C C   1 
ATOM   5291  O  O   . ALA   C  1 133 ? 47.874 -9.511  59.479  1.00 18.19 ? 133  ALA   C O   1 
ATOM   5292  C  CB  . ALA   C  1 133 ? 47.501 -7.083  57.418  1.00 18.07 ? 133  ALA   C CB  1 
ATOM   5293  N  N   . VAL   C  1 134 ? 49.853 -8.615  58.906  1.00 17.67 ? 134  VAL   C N   1 
ATOM   5294  C  CA  . VAL   C  1 134 ? 50.519 -9.926  58.938  1.00 16.61 ? 134  VAL   C CA  1 
ATOM   5295  C  C   . VAL   C  1 134 ? 50.549 -10.506 60.342  1.00 19.11 ? 134  VAL   C C   1 
ATOM   5296  O  O   . VAL   C  1 134 ? 50.831 -11.697 60.505  1.00 17.70 ? 134  VAL   C O   1 
ATOM   5297  C  CB  . VAL   C  1 134 ? 51.927 -9.791  58.330  1.00 17.27 ? 134  VAL   C CB  1 
ATOM   5298  C  CG1 . VAL   C  1 134 ? 52.837 -8.934  59.187  1.00 18.22 ? 134  VAL   C CG1 1 
ATOM   5299  C  CG2 . VAL   C  1 134 ? 52.566 -11.189 58.077  1.00 16.83 ? 134  VAL   C CG2 1 
ATOM   5300  N  N   . GLN   C  1 135 ? 50.230 -9.693  61.332  1.00 18.58 ? 135  GLN   C N   1 
ATOM   5301  C  CA  . GLN   C  1 135 ? 50.156 -10.157 62.715  1.00 18.31 ? 135  GLN   C CA  1 
ATOM   5302  C  C   . GLN   C  1 135 ? 48.790 -10.686 63.087  1.00 21.86 ? 135  GLN   C C   1 
ATOM   5303  O  O   . GLN   C  1 135 ? 48.602 -11.086 64.249  1.00 25.14 ? 135  GLN   C O   1 
ATOM   5304  C  CB  . GLN   C  1 135 ? 50.539 -9.046  63.682  1.00 19.08 ? 135  GLN   C CB  1 
ATOM   5305  C  CG  . GLN   C  1 135 ? 51.978 -8.496  63.443  1.00 17.91 ? 135  GLN   C CG  1 
ATOM   5306  C  CD  . GLN   C  1 135 ? 53.056 -9.565  63.661  1.00 18.74 ? 135  GLN   C CD  1 
ATOM   5307  O  OE1 . GLN   C  1 135 ? 52.866 -10.502 64.463  1.00 22.77 ? 135  GLN   C OE1 1 
ATOM   5308  N  NE2 . GLN   C  1 135 ? 54.173 -9.435  62.936  1.00 16.41 ? 135  GLN   C NE2 1 
ATOM   5309  N  N   . GLN   C  1 136 ? 47.843 -10.733 62.149  1.00 20.68 ? 136  GLN   C N   1 
ATOM   5310  C  CA  . GLN   C  1 136 ? 46.467 -11.100 62.465  1.00 21.05 ? 136  GLN   C CA  1 
ATOM   5311  C  C   . GLN   C  1 136 ? 46.031 -12.340 61.704  1.00 19.79 ? 136  GLN   C C   1 
ATOM   5312  O  O   . GLN   C  1 136 ? 46.397 -12.509 60.542  1.00 20.04 ? 136  GLN   C O   1 
ATOM   5313  C  CB  . GLN   C  1 136 ? 45.507 -9.939  62.130  1.00 21.32 ? 136  GLN   C CB  1 
ATOM   5314  C  CG  . GLN   C  1 136 ? 45.856 -8.644  62.838  1.00 24.73 ? 136  GLN   C CG  1 
ATOM   5315  C  CD  . GLN   C  1 136 ? 45.670 -8.751  64.346  1.00 29.38 ? 136  GLN   C CD  1 
ATOM   5316  O  OE1 . GLN   C  1 136 ? 44.932 -9.614  64.847  1.00 34.20 ? 136  GLN   C OE1 1 
ATOM   5317  N  NE2 . GLN   C  1 136 ? 46.391 -7.903  65.089  1.00 32.25 ? 136  GLN   C NE2 1 
ATOM   5318  N  N   . PRO   C  1 137 ? 45.235 -13.222 62.312  1.00 20.21 ? 137  PRO   C N   1 
ATOM   5319  C  CA  . PRO   C  1 137 ? 44.863 -14.458 61.602  1.00 22.21 ? 137  PRO   C CA  1 
ATOM   5320  C  C   . PRO   C  1 137 ? 44.131 -14.194 60.312  1.00 22.16 ? 137  PRO   C C   1 
ATOM   5321  O  O   . PRO   C  1 137 ? 44.269 -14.984 59.363  1.00 23.38 ? 137  PRO   C O   1 
ATOM   5322  C  CB  . PRO   C  1 137 ? 43.975 -15.197 62.615  1.00 23.01 ? 137  PRO   C CB  1 
ATOM   5323  C  CG  . PRO   C  1 137 ? 44.457 -14.737 63.930  1.00 27.87 ? 137  PRO   C CG  1 
ATOM   5324  C  CD  . PRO   C  1 137 ? 44.806 -13.248 63.728  1.00 23.71 ? 137  PRO   C CD  1 
ATOM   5325  N  N   . ASP   C  1 138 ? 43.328 -13.119 60.247  1.00 19.14 ? 138  ASP   C N   1 
ATOM   5326  C  CA  . ASP   C  1 138 ? 42.613 -12.738 59.037  1.00 19.98 ? 138  ASP   C CA  1 
ATOM   5327  C  C   . ASP   C  1 138 ? 43.339 -11.647 58.263  1.00 19.65 ? 138  ASP   C C   1 
ATOM   5328  O  O   . ASP   C  1 138 ? 42.721 -10.933 57.457  1.00 21.59 ? 138  ASP   C O   1 
ATOM   5329  C  CB  . ASP   C  1 138 ? 41.186 -12.276 59.358  1.00 20.33 ? 138  ASP   C CB  1 
ATOM   5330  C  CG  . ASP   C  1 138 ? 41.150 -11.077 60.276  1.00 24.65 ? 138  ASP   C CG  1 
ATOM   5331  O  OD1 . ASP   C  1 138 ? 42.186 -10.673 60.813  1.00 24.91 ? 138  ASP   C OD1 1 
ATOM   5332  O  OD2 . ASP   C  1 138 ? 40.041 -10.519 60.480  1.00 27.60 ? 138  ASP   C OD2 1 
ATOM   5333  N  N   . GLY   C  1 139 ? 44.640 -11.525 58.472  1.00 19.43 ? 139  GLY   C N   1 
ATOM   5334  C  CA  . GLY   C  1 139 ? 45.364 -10.371 57.929  1.00 19.60 ? 139  GLY   C CA  1 
ATOM   5335  C  C   . GLY   C  1 139 ? 45.701 -10.418 56.441  1.00 18.54 ? 139  GLY   C C   1 
ATOM   5336  O  O   . GLY   C  1 139 ? 45.661 -9.385  55.759  1.00 19.22 ? 139  GLY   C O   1 
ATOM   5337  N  N   . LEU   C  1 140 ? 46.051 -11.602 55.927  1.00 18.69 ? 140  LEU   C N   1 
ATOM   5338  C  CA  . LEU   C  1 140 ? 46.578 -11.716 54.572  1.00 16.71 ? 140  LEU   C CA  1 
ATOM   5339  C  C   . LEU   C  1 140 ? 45.767 -12.698 53.752  1.00 18.85 ? 140  LEU   C C   1 
ATOM   5340  O  O   . LEU   C  1 140 ? 45.150 -13.630 54.288  1.00 18.79 ? 140  LEU   C O   1 
ATOM   5341  C  CB  . LEU   C  1 140 ? 48.041 -12.204 54.570  1.00 16.54 ? 140  LEU   C CB  1 
ATOM   5342  C  CG  . LEU   C  1 140 ? 49.008 -11.308 55.360  1.00 16.82 ? 140  LEU   C CG  1 
ATOM   5343  C  CD1 . LEU   C  1 140 ? 50.398 -11.924 55.142  1.00 17.67 ? 140  LEU   C CD1 1 
ATOM   5344  C  CD2 . LEU   C  1 140 ? 48.998 -9.807  54.934  1.00 18.99 ? 140  LEU   C CD2 1 
ATOM   5345  N  N   . ALA   C  1 141 ? 45.810 -12.486 52.434  1.00 17.95 ? 141  ALA   C N   1 
ATOM   5346  C  CA  . ALA   C  1 141 ? 45.272 -13.439 51.466  1.00 18.36 ? 141  ALA   C CA  1 
ATOM   5347  C  C   . ALA   C  1 141 ? 46.313 -13.594 50.384  1.00 18.91 ? 141  ALA   C C   1 
ATOM   5348  O  O   . ALA   C  1 141 ? 46.745 -12.601 49.782  1.00 19.51 ? 141  ALA   C O   1 
ATOM   5349  C  CB  . ALA   C  1 141 ? 43.934 -12.990 50.874  1.00 20.48 ? 141  ALA   C CB  1 
ATOM   5350  N  N   . VAL   C  1 142 ? 46.739 -14.828 50.138  1.00 17.02 ? 142  VAL   C N   1 
ATOM   5351  C  CA  . VAL   C  1 142 ? 47.727 -15.072 49.090  1.00 17.38 ? 142  VAL   C CA  1 
ATOM   5352  C  C   . VAL   C  1 142 ? 47.047 -15.912 48.004  1.00 17.97 ? 142  VAL   C C   1 
ATOM   5353  O  O   . VAL   C  1 142 ? 46.449 -16.976 48.281  1.00 19.31 ? 142  VAL   C O   1 
ATOM   5354  C  CB  . VAL   C  1 142 ? 49.012 -15.728 49.594  1.00 16.98 ? 142  VAL   C CB  1 
ATOM   5355  C  CG1 . VAL   C  1 142 ? 49.990 -15.869 48.392  1.00 17.78 ? 142  VAL   C CG1 1 
ATOM   5356  C  CG2 . VAL   C  1 142 ? 49.695 -14.840 50.644  1.00 17.67 ? 142  VAL   C CG2 1 
ATOM   5357  N  N   . LEU   C  1 143 ? 47.099 -15.405 46.783  1.00 18.06 ? 143  LEU   C N   1 
ATOM   5358  C  CA  . LEU   C  1 143 ? 46.582 -16.072 45.601  1.00 20.39 ? 143  LEU   C CA  1 
ATOM   5359  C  C   . LEU   C  1 143 ? 47.752 -16.834 44.991  1.00 20.65 ? 143  LEU   C C   1 
ATOM   5360  O  O   . LEU   C  1 143 ? 48.758 -16.220 44.579  1.00 19.68 ? 143  LEU   C O   1 
ATOM   5361  C  CB  . LEU   C  1 143 ? 45.973 -15.044 44.635  1.00 21.42 ? 143  LEU   C CB  1 
ATOM   5362  C  CG  . LEU   C  1 143 ? 45.362 -15.581 43.355  1.00 23.75 ? 143  LEU   C CG  1 
ATOM   5363  C  CD1 . LEU   C  1 143 ? 44.192 -16.526 43.658  1.00 24.49 ? 143  LEU   C CD1 1 
ATOM   5364  C  CD2 . LEU   C  1 143 ? 44.846 -14.417 42.478  1.00 22.68 ? 143  LEU   C CD2 1 
ATOM   5365  N  N   . GLY   C  1 144 ? 47.677 -18.164 45.028  1.00 18.01 ? 144  GLY   C N   1 
ATOM   5366  C  CA  . GLY   C  1 144 ? 48.745 -19.020 44.543  1.00 19.80 ? 144  GLY   C CA  1 
ATOM   5367  C  C   . GLY   C  1 144 ? 48.373 -19.635 43.207  1.00 19.23 ? 144  GLY   C C   1 
ATOM   5368  O  O   . GLY   C  1 144 ? 47.248 -20.097 43.031  1.00 19.99 ? 144  GLY   C O   1 
ATOM   5369  N  N   . ILE   C  1 145 ? 49.314 -19.567 42.266  1.00 17.38 ? 145  ILE   C N   1 
ATOM   5370  C  CA  . ILE   C  1 145 ? 49.100 -20.012 40.890  1.00 19.99 ? 145  ILE   C CA  1 
ATOM   5371  C  C   . ILE   C  1 145 ? 50.268 -20.897 40.471  1.00 20.13 ? 145  ILE   C C   1 
ATOM   5372  O  O   . ILE   C  1 145 ? 51.433 -20.504 40.621  1.00 20.84 ? 145  ILE   C O   1 
ATOM   5373  C  CB  . ILE   C  1 145 ? 48.955 -18.815 39.945  1.00 21.36 ? 145  ILE   C CB  1 
ATOM   5374  C  CG1 . ILE   C  1 145 ? 47.783 -17.940 40.439  1.00 22.53 ? 145  ILE   C CG1 1 
ATOM   5375  C  CG2 . ILE   C  1 145 ? 48.801 -19.314 38.489  1.00 21.47 ? 145  ILE   C CG2 1 
ATOM   5376  C  CD1 . ILE   C  1 145 ? 47.516 -16.638 39.624  1.00 22.90 ? 145  ILE   C CD1 1 
ATOM   5377  N  N   . PHE   C  1 146 ? 49.962 -22.089 39.959  1.00 20.19 ? 146  PHE   C N   1 
ATOM   5378  C  CA  . PHE   C  1 146 ? 51.011 -22.998 39.522  1.00 18.81 ? 146  PHE   C CA  1 
ATOM   5379  C  C   . PHE   C  1 146 ? 51.515 -22.644 38.135  1.00 21.01 ? 146  PHE   C C   1 
ATOM   5380  O  O   . PHE   C  1 146 ? 50.738 -22.215 37.273  1.00 22.56 ? 146  PHE   C O   1 
ATOM   5381  C  CB  . PHE   C  1 146 ? 50.500 -24.444 39.501  1.00 19.78 ? 146  PHE   C CB  1 
ATOM   5382  C  CG  . PHE   C  1 146 ? 50.107 -24.952 40.852  1.00 20.56 ? 146  PHE   C CG  1 
ATOM   5383  C  CD1 . PHE   C  1 146 ? 51.040 -25.081 41.886  1.00 19.94 ? 146  PHE   C CD1 1 
ATOM   5384  C  CD2 . PHE   C  1 146 ? 48.783 -25.313 41.085  1.00 20.56 ? 146  PHE   C CD2 1 
ATOM   5385  C  CE1 . PHE   C  1 146 ? 50.672 -25.583 43.144  1.00 21.28 ? 146  PHE   C CE1 1 
ATOM   5386  C  CE2 . PHE   C  1 146 ? 48.376 -25.805 42.358  1.00 20.23 ? 146  PHE   C CE2 1 
ATOM   5387  C  CZ  . PHE   C  1 146 ? 49.338 -25.952 43.393  1.00 20.88 ? 146  PHE   C CZ  1 
ATOM   5388  N  N   . LEU   C  1 147 ? 52.818 -22.860 37.910  1.00 21.66 ? 147  LEU   C N   1 
ATOM   5389  C  CA  . LEU   C  1 147 ? 53.429 -22.699 36.584  1.00 21.38 ? 147  LEU   C CA  1 
ATOM   5390  C  C   . LEU   C  1 147 ? 53.797 -24.076 36.045  1.00 22.52 ? 147  LEU   C C   1 
ATOM   5391  O  O   . LEU   C  1 147 ? 54.613 -24.788 36.659  1.00 23.29 ? 147  LEU   C O   1 
ATOM   5392  C  CB  . LEU   C  1 147 ? 54.686 -21.834 36.621  1.00 21.64 ? 147  LEU   C CB  1 
ATOM   5393  C  CG  . LEU   C  1 147 ? 54.470 -20.308 36.681  1.00 19.23 ? 147  LEU   C CG  1 
ATOM   5394  C  CD1 . LEU   C  1 147 ? 53.765 -19.800 37.964  1.00 20.78 ? 147  LEU   C CD1 1 
ATOM   5395  C  CD2 . LEU   C  1 147 ? 55.787 -19.548 36.516  1.00 20.42 ? 147  LEU   C CD2 1 
ATOM   5396  N  N   . LYS   C  1 148 ? 53.255 -24.412 34.890  1.00 24.02 ? 148  LYS   C N   1 
ATOM   5397  C  CA  . LYS   C  1 148 ? 53.535 -25.667 34.227  1.00 26.60 ? 148  LYS   C CA  1 
ATOM   5398  C  C   . LYS   C  1 148 ? 54.374 -25.394 32.987  1.00 29.64 ? 148  LYS   C C   1 
ATOM   5399  O  O   . LYS   C  1 148 ? 54.102 -24.441 32.259  1.00 34.90 ? 148  LYS   C O   1 
ATOM   5400  C  CB  . LYS   C  1 148 ? 52.206 -26.344 33.851  1.00 32.91 ? 148  LYS   C CB  1 
ATOM   5401  C  CG  . LYS   C  1 148 ? 52.301 -27.609 33.079  1.00 39.77 ? 148  LYS   C CG  1 
ATOM   5402  C  CD  . LYS   C  1 148 ? 50.871 -28.064 32.725  1.00 44.00 ? 148  LYS   C CD  1 
ATOM   5403  C  CE  . LYS   C  1 148 ? 50.092 -26.927 32.061  1.00 49.39 ? 148  LYS   C CE  1 
ATOM   5404  N  NZ  . LYS   C  1 148 ? 48.839 -27.427 31.353  1.00 56.31 ? 148  LYS   C NZ  1 
ATOM   5405  N  N   . VAL   C  1 149 ? 55.367 -26.248 32.730  1.00 28.32 ? 149  VAL   C N   1 
ATOM   5406  C  CA  . VAL   C  1 149 ? 56.227 -26.091 31.551  1.00 32.03 ? 149  VAL   C CA  1 
ATOM   5407  C  C   . VAL   C  1 149 ? 55.468 -26.442 30.273  1.00 31.87 ? 149  VAL   C C   1 
ATOM   5408  O  O   . VAL   C  1 149 ? 54.849 -27.511 30.154  1.00 34.81 ? 149  VAL   C O   1 
ATOM   5409  C  CB  . VAL   C  1 149 ? 57.498 -26.944 31.692  1.00 35.64 ? 149  VAL   C CB  1 
ATOM   5410  C  CG1 . VAL   C  1 149 ? 58.266 -26.959 30.371  1.00 38.17 ? 149  VAL   C CG1 1 
ATOM   5411  C  CG2 . VAL   C  1 149 ? 58.381 -26.362 32.771  1.00 36.37 ? 149  VAL   C CG2 1 
ATOM   5412  N  N   . GLY   C  1 150 ? 55.539 -25.544 29.300  1.00 30.87 ? 150  GLY   C N   1 
ATOM   5413  C  CA  . GLY   C  1 150 ? 54.864 -25.690 28.033  1.00 32.55 ? 150  GLY   C CA  1 
ATOM   5414  C  C   . GLY   C  1 150 ? 55.225 -24.519 27.157  1.00 31.74 ? 150  GLY   C C   1 
ATOM   5415  O  O   . GLY   C  1 150 ? 56.414 -24.191 27.046  1.00 31.36 ? 150  GLY   C O   1 
ATOM   5416  N  N   . SER   C  1 151 ? 54.218 -23.875 26.559  1.00 33.58 ? 151  SER   C N   1 
ATOM   5417  C  CA  . SER   C  1 151 ? 54.420 -22.701 25.723  1.00 31.18 ? 151  SER   C CA  1 
ATOM   5418  C  C   . SER   C  1 151 ? 54.825 -21.496 26.573  1.00 29.05 ? 151  SER   C C   1 
ATOM   5419  O  O   . SER   C  1 151 ? 54.471 -21.392 27.741  1.00 31.84 ? 151  SER   C O   1 
ATOM   5420  C  CB  . SER   C  1 151 ? 53.143 -22.375 24.970  1.00 34.70 ? 151  SER   C CB  1 
ATOM   5421  O  OG  . SER   C  1 151 ? 52.886 -23.370 24.000  1.00 43.46 ? 151  SER   C OG  1 
ATOM   5422  N  N   . ALA   C  1 152 ? 55.568 -20.584 25.961  1.00 32.51 ? 152  ALA   C N   1 
ATOM   5423  C  CA  . ALA   C  1 152 ? 55.992 -19.374 26.657  1.00 32.40 ? 152  ALA   C CA  1 
ATOM   5424  C  C   . ALA   C  1 152 ? 54.776 -18.510 26.980  1.00 33.82 ? 152  ALA   C C   1 
ATOM   5425  O  O   . ALA   C  1 152 ? 53.812 -18.458 26.207  1.00 35.18 ? 152  ALA   C O   1 
ATOM   5426  C  CB  . ALA   C  1 152 ? 56.986 -18.598 25.785  1.00 33.13 ? 152  ALA   C CB  1 
ATOM   5427  N  N   . LEU   C  1 153 ? 54.816 -17.841 28.139  1.00 30.71 ? 153  LEU   C N   1 
ATOM   5428  C  CA  . LEU   C  1 153 ? 53.732 -16.969 28.571  1.00 29.15 ? 153  LEU   C CA  1 
ATOM   5429  C  C   . LEU   C  1 153 ? 54.090 -15.531 28.245  1.00 26.32 ? 153  LEU   C C   1 
ATOM   5430  O  O   . LEU   C  1 153 ? 55.030 -14.989 28.857  1.00 25.90 ? 153  LEU   C O   1 
ATOM   5431  C  CB  . LEU   C  1 153 ? 53.502 -17.113 30.078  1.00 28.67 ? 153  LEU   C CB  1 
ATOM   5432  C  CG  . LEU   C  1 153 ? 52.245 -16.425 30.624  1.00 31.05 ? 153  LEU   C CG  1 
ATOM   5433  C  CD1 . LEU   C  1 153 ? 50.968 -17.044 30.026  1.00 33.13 ? 153  LEU   C CD1 1 
ATOM   5434  C  CD2 . LEU   C  1 153 ? 52.205 -16.484 32.139  1.00 28.17 ? 153  LEU   C CD2 1 
ATOM   5435  N  N   . PRO   C  1 154 ? 53.373 -14.857 27.364  1.00 26.97 ? 154  PRO   C N   1 
ATOM   5436  C  CA  . PRO   C  1 154 ? 53.779 -13.488 27.012  1.00 27.27 ? 154  PRO   C CA  1 
ATOM   5437  C  C   . PRO   C  1 154 ? 53.699 -12.554 28.200  1.00 27.34 ? 154  PRO   C C   1 
ATOM   5438  O  O   . PRO   C  1 154 ? 54.526 -11.638 28.322  1.00 30.39 ? 154  PRO   C O   1 
ATOM   5439  C  CB  . PRO   C  1 154 ? 52.795 -13.102 25.880  1.00 32.44 ? 154  PRO   C CB  1 
ATOM   5440  C  CG  . PRO   C  1 154 ? 52.381 -14.415 25.301  1.00 33.72 ? 154  PRO   C CG  1 
ATOM   5441  C  CD  . PRO   C  1 154 ? 52.304 -15.366 26.471  1.00 29.98 ? 154  PRO   C CD  1 
ATOM   5442  N  N   . GLY   C  1 155 ? 52.752 -12.798 29.111  1.00 29.18 ? 155  GLY   C N   1 
ATOM   5443  C  CA  . GLY   C  1 155 ? 52.579 -11.949 30.273  1.00 29.42 ? 155  GLY   C CA  1 
ATOM   5444  C  C   . GLY   C  1 155 ? 53.725 -12.018 31.251  1.00 26.43 ? 155  GLY   C C   1 
ATOM   5445  O  O   . GLY   C  1 155 ? 53.825 -11.167 32.139  1.00 29.34 ? 155  GLY   C O   1 
ATOM   5446  N  N   . LEU   C  1 156 ? 54.574 -13.023 31.121  1.00 25.34 ? 156  LEU   C N   1 
ATOM   5447  C  CA  . LEU   C  1 156 ? 55.734 -13.159 31.981  1.00 22.77 ? 156  LEU   C CA  1 
ATOM   5448  C  C   . LEU   C  1 156 ? 56.980 -12.506 31.390  1.00 23.85 ? 156  LEU   C C   1 
ATOM   5449  O  O   . LEU   C  1 156 ? 57.975 -12.328 32.112  1.00 25.17 ? 156  LEU   C O   1 
ATOM   5450  C  CB  . LEU   C  1 156 ? 55.988 -14.660 32.262  1.00 24.66 ? 156  LEU   C CB  1 
ATOM   5451  C  CG  . LEU   C  1 156 ? 57.081 -15.067 33.263  1.00 25.70 ? 156  LEU   C CG  1 
ATOM   5452  C  CD1 . LEU   C  1 156 ? 56.820 -14.480 34.665  1.00 21.59 ? 156  LEU   C CD1 1 
ATOM   5453  C  CD2 . LEU   C  1 156 ? 57.216 -16.586 33.325  1.00 24.71 ? 156  LEU   C CD2 1 
ATOM   5454  N  N   . GLN   C  1 157 ? 56.953 -12.130 30.112  1.00 25.44 ? 157  GLN   C N   1 
ATOM   5455  C  CA  . GLN   C  1 157 ? 58.206 -11.794 29.452  1.00 26.06 ? 157  GLN   C CA  1 
ATOM   5456  C  C   . GLN   C  1 157 ? 58.831 -10.532 30.053  1.00 26.13 ? 157  GLN   C C   1 
ATOM   5457  O  O   . GLN   C  1 157 ? 60.049 -10.456 30.202  1.00 26.10 ? 157  GLN   C O   1 
ATOM   5458  C  CB  . GLN   C  1 157 ? 58.005 -11.645 27.937  1.00 29.96 ? 157  GLN   C CB  1 
ATOM   5459  C  CG  . GLN   C  1 157 ? 59.322 -11.767 27.163  1.00 35.08 ? 157  GLN   C CG  1 
ATOM   5460  C  CD  . GLN   C  1 157 ? 60.135 -13.058 27.491  1.00 37.64 ? 157  GLN   C CD  1 
ATOM   5461  O  OE1 . GLN   C  1 157 ? 59.592 -14.171 27.589  1.00 36.29 ? 157  GLN   C OE1 1 
ATOM   5462  N  NE2 . GLN   C  1 157 ? 61.447 -12.909 27.587  1.00 34.90 ? 157  GLN   C NE2 1 
ATOM   5463  N  N   . LYS   C  1 158 ? 58.020 -9.554  30.463  1.00 26.26 ? 158  LYS   C N   1 
ATOM   5464  C  CA  . LYS   C  1 158 ? 58.599 -8.337  31.028  1.00 26.36 ? 158  LYS   C CA  1 
ATOM   5465  C  C   . LYS   C  1 158 ? 59.347 -8.633  32.315  1.00 23.89 ? 158  LYS   C C   1 
ATOM   5466  O  O   . LYS   C  1 158 ? 60.356 -7.999  32.622  1.00 25.76 ? 158  LYS   C O   1 
ATOM   5467  C  CB  . LYS   C  1 158 ? 57.504 -7.311  31.305  1.00 28.55 ? 158  LYS   C CB  1 
ATOM   5468  C  CG  . LYS   C  1 158 ? 58.048 -5.938  31.722  1.00 32.61 ? 158  LYS   C CG  1 
ATOM   5469  C  CD  . LYS   C  1 158 ? 56.959 -5.051  32.301  1.00 34.40 ? 158  LYS   C CD  1 
ATOM   5470  C  CE  . LYS   C  1 158 ? 57.550 -3.714  32.871  1.00 34.27 ? 158  LYS   C CE  1 
ATOM   5471  N  NZ  . LYS   C  1 158 ? 57.579 -2.727  31.763  1.00 34.59 ? 158  LYS   C NZ  1 
ATOM   5472  N  N   . VAL   C  1 159 ? 58.828 -9.573  33.097  1.00 21.64 ? 159  VAL   C N   1 
ATOM   5473  C  CA  . VAL   C  1 159 ? 59.516 -9.990  34.311  1.00 19.38 ? 159  VAL   C CA  1 
ATOM   5474  C  C   . VAL   C  1 159 ? 60.864 -10.609 33.960  1.00 22.43 ? 159  VAL   C C   1 
ATOM   5475  O  O   . VAL   C  1 159 ? 61.913 -10.215 34.481  1.00 22.91 ? 159  VAL   C O   1 
ATOM   5476  C  CB  . VAL   C  1 159 ? 58.644 -10.990 35.085  1.00 21.00 ? 159  VAL   C CB  1 
ATOM   5477  C  CG1 . VAL   C  1 159 ? 59.458 -11.569 36.239  1.00 22.21 ? 159  VAL   C CG1 1 
ATOM   5478  C  CG2 . VAL   C  1 159 ? 57.342 -10.344 35.647  1.00 22.73 ? 159  VAL   C CG2 1 
ATOM   5479  N  N   . VAL   C  1 160 ? 60.853 -11.629 33.098  1.00 24.90 ? 160  VAL   C N   1 
ATOM   5480  C  CA  A VAL   C  1 160 ? 62.072 -12.371 32.771  0.42 27.94 ? 160  VAL   C CA  1 
ATOM   5481  C  CA  B VAL   C  1 160 ? 62.113 -12.326 32.918  0.58 27.58 ? 160  VAL   C CA  1 
ATOM   5482  C  C   . VAL   C  1 160 ? 63.139 -11.428 32.254  1.00 29.19 ? 160  VAL   C C   1 
ATOM   5483  O  O   . VAL   C  1 160 ? 64.331 -11.567 32.550  1.00 29.81 ? 160  VAL   C O   1 
ATOM   5484  C  CB  A VAL   C  1 160 ? 61.753 -13.473 31.738  0.42 31.36 ? 160  VAL   C CB  1 
ATOM   5485  C  CB  B VAL   C  1 160 ? 61.917 -13.660 32.171  0.58 30.92 ? 160  VAL   C CB  1 
ATOM   5486  C  CG1 A VAL   C  1 160 ? 62.989 -13.823 30.927  0.42 32.35 ? 160  VAL   C CG1 1 
ATOM   5487  C  CG1 B VAL   C  1 160 ? 61.177 -14.647 33.075  0.58 30.94 ? 160  VAL   C CG1 1 
ATOM   5488  C  CG2 A VAL   C  1 160 ? 61.197 -14.698 32.429  0.42 31.92 ? 160  VAL   C CG2 1 
ATOM   5489  C  CG2 B VAL   C  1 160 ? 61.181 -13.440 30.881  0.58 31.02 ? 160  VAL   C CG2 1 
ATOM   5490  N  N   . ASP   C  1 161 ? 62.714 -10.449 31.455  1.00 26.42 ? 161  ASP   C N   1 
ATOM   5491  C  CA  . ASP   C  1 161 ? 63.641 -9.562  30.759  1.00 29.70 ? 161  ASP   C CA  1 
ATOM   5492  C  C   . ASP   C  1 161 ? 64.414 -8.649  31.704  1.00 31.15 ? 161  ASP   C C   1 
ATOM   5493  O  O   . ASP   C  1 161 ? 65.467 -8.139  31.306  1.00 38.61 ? 161  ASP   C O   1 
ATOM   5494  C  CB  . ASP   C  1 161 ? 62.907 -8.700  29.728  1.00 33.15 ? 161  ASP   C CB  1 
ATOM   5495  C  CG  . ASP   C  1 161 ? 62.507 -9.487  28.454  1.00 34.90 ? 161  ASP   C CG  1 
ATOM   5496  O  OD1 . ASP   C  1 161 ? 62.978 -10.642 28.257  1.00 35.98 ? 161  ASP   C OD1 1 
ATOM   5497  O  OD2 . ASP   C  1 161 ? 61.729 -8.927  27.661  1.00 46.37 ? 161  ASP   C OD2 1 
ATOM   5498  N  N   . VAL   C  1 162 ? 63.900 -8.387  32.918  1.00 25.84 ? 162  VAL   C N   1 
ATOM   5499  C  CA  . VAL   C  1 162 ? 64.537 -7.462  33.860  1.00 25.27 ? 162  VAL   C CA  1 
ATOM   5500  C  C   . VAL   C  1 162 ? 65.436 -8.205  34.858  1.00 24.74 ? 162  VAL   C C   1 
ATOM   5501  O  O   . VAL   C  1 162 ? 66.215 -7.559  35.564  1.00 25.16 ? 162  VAL   C O   1 
ATOM   5502  C  CB  . VAL   C  1 162 ? 63.473 -6.647  34.648  1.00 24.67 ? 162  VAL   C CB  1 
ATOM   5503  C  CG1 . VAL   C  1 162 ? 62.876 -7.437  35.781  1.00 25.77 ? 162  VAL   C CG1 1 
ATOM   5504  C  CG2 . VAL   C  1 162 ? 64.014 -5.315  35.157  1.00 28.56 ? 162  VAL   C CG2 1 
ATOM   5505  N  N   . LEU   C  1 163 ? 65.388 -9.547  34.893  1.00 23.75 ? 163  LEU   C N   1 
ATOM   5506  C  CA  . LEU   C  1 163 ? 66.046 -10.241 36.005  1.00 22.91 ? 163  LEU   C CA  1 
ATOM   5507  C  C   . LEU   C  1 163 ? 67.567 -10.088 35.955  1.00 26.99 ? 163  LEU   C C   1 
ATOM   5508  O  O   . LEU   C  1 163 ? 68.227 -10.102 37.007  1.00 25.31 ? 163  LEU   C O   1 
ATOM   5509  C  CB  . LEU   C  1 163 ? 65.643 -11.717 36.024  1.00 23.96 ? 163  LEU   C CB  1 
ATOM   5510  C  CG  . LEU   C  1 163 ? 64.143 -11.954 36.275  1.00 22.44 ? 163  LEU   C CG  1 
ATOM   5511  C  CD1 . LEU   C  1 163 ? 63.880 -13.493 36.293  1.00 22.98 ? 163  LEU   C CD1 1 
ATOM   5512  C  CD2 . LEU   C  1 163 ? 63.725 -11.303 37.607  1.00 22.03 ? 163  LEU   C CD2 1 
ATOM   5513  N  N   . ASP   C  1 164 ? 68.159 -9.989  34.751  1.00 29.77 ? 164  ASP   C N   1 
ATOM   5514  C  CA  . ASP   C  1 164 ? 69.607 -9.859  34.726  1.00 31.20 ? 164  ASP   C CA  1 
ATOM   5515  C  C   . ASP   C  1 164 ? 70.082 -8.558  35.354  1.00 28.78 ? 164  ASP   C C   1 
ATOM   5516  O  O   . ASP   C  1 164 ? 71.270 -8.441  35.680  1.00 32.38 ? 164  ASP   C O   1 
ATOM   5517  C  CB  . ASP   C  1 164 ? 70.156 -9.970  33.286  1.00 41.73 ? 164  ASP   C CB  1 
ATOM   5518  C  CG  . ASP   C  1 164 ? 70.360 -11.434 32.840  1.00 52.85 ? 164  ASP   C CG  1 
ATOM   5519  O  OD1 . ASP   C  1 164 ? 70.437 -12.341 33.711  1.00 54.89 ? 164  ASP   C OD1 1 
ATOM   5520  O  OD2 . ASP   C  1 164 ? 70.432 -11.695 31.615  1.00 57.72 ? 164  ASP   C OD2 1 
ATOM   5521  N  N   . SER   C  1 165 ? 69.185 -7.600  35.579  1.00 26.90 ? 165  SER   C N   1 
ATOM   5522  C  CA  . SER   C  1 165 ? 69.555 -6.363  36.240  1.00 25.99 ? 165  SER   C CA  1 
ATOM   5523  C  C   . SER   C  1 165 ? 69.466 -6.424  37.765  1.00 24.99 ? 165  SER   C C   1 
ATOM   5524  O  O   . SER   C  1 165 ? 69.908 -5.461  38.438  1.00 27.69 ? 165  SER   C O   1 
ATOM   5525  C  CB  . SER   C  1 165 ? 68.712 -5.190  35.719  1.00 33.06 ? 165  SER   C CB  1 
ATOM   5526  O  OG  . SER   C  1 165 ? 67.386 -5.215  36.207  1.00 32.48 ? 165  SER   C OG  1 
ATOM   5527  N  N   . ILE   C  1 166 ? 68.956 -7.527  38.327  1.00 21.94 ? 166  ILE   C N   1 
ATOM   5528  C  CA  . ILE   C  1 166 ? 68.866 -7.626  39.786  1.00 20.22 ? 166  ILE   C CA  1 
ATOM   5529  C  C   . ILE   C  1 166 ? 69.458 -8.951  40.265  1.00 20.91 ? 166  ILE   C C   1 
ATOM   5530  O  O   . ILE   C  1 166 ? 68.822 -9.670  41.038  1.00 19.09 ? 166  ILE   C O   1 
ATOM   5531  C  CB  . ILE   C  1 166 ? 67.396 -7.458  40.243  1.00 19.17 ? 166  ILE   C CB  1 
ATOM   5532  C  CG1 . ILE   C  1 166 ? 66.462 -8.421  39.512  1.00 17.62 ? 166  ILE   C CG1 1 
ATOM   5533  C  CG2 . ILE   C  1 166 ? 66.953 -5.975  39.964  1.00 19.94 ? 166  ILE   C CG2 1 
ATOM   5534  C  CD1 . ILE   C  1 166 ? 65.202 -8.721  40.399  1.00 18.68 ? 166  ILE   C CD1 1 
ATOM   5535  N  N   . LYS   C  1 167 ? 70.682 -9.266  39.825  1.00 21.92 ? 167  LYS   C N   1 
ATOM   5536  C  CA  . LYS   C  1 167 ? 71.184 -10.624 39.969  1.00 22.67 ? 167  LYS   C CA  1 
ATOM   5537  C  C   . LYS   C  1 167 ? 71.440 -10.974 41.435  1.00 21.42 ? 167  LYS   C C   1 
ATOM   5538  O  O   . LYS   C  1 167 ? 71.287 -12.125 41.817  1.00 20.79 ? 167  LYS   C O   1 
ATOM   5539  C  CB  . LYS   C  1 167 ? 72.485 -10.805 39.149  1.00 23.70 ? 167  LYS   C CB  1 
ATOM   5540  C  CG  . LYS   C  1 167 ? 73.041 -12.247 39.235  1.00 30.05 ? 167  LYS   C CG  1 
ATOM   5541  C  CD  . LYS   C  1 167 ? 74.375 -12.401 38.447  1.00 35.16 ? 167  LYS   C CD  1 
ATOM   5542  C  CE  . LYS   C  1 167 ? 74.869 -13.840 38.587  1.00 43.00 ? 167  LYS   C CE  1 
ATOM   5543  N  NZ  . LYS   C  1 167 ? 76.230 -14.016 38.044  1.00 50.28 ? 167  LYS   C NZ  1 
ATOM   5544  N  N   . THR   C  1 168 ? 71.893 -10.017 42.256  1.00 19.85 ? 168  THR   C N   1 
ATOM   5545  C  CA  . THR   C  1 168 ? 72.302 -10.321 43.620  1.00 19.61 ? 168  THR   C CA  1 
ATOM   5546  C  C   . THR   C  1 168 ? 71.421 -9.639  44.663  1.00 20.27 ? 168  THR   C C   1 
ATOM   5547  O  O   . THR   C  1 168 ? 70.692 -8.676  44.390  1.00 18.59 ? 168  THR   C O   1 
ATOM   5548  C  CB  . THR   C  1 168 ? 73.783 -9.920  43.824  1.00 21.63 ? 168  THR   C CB  1 
ATOM   5549  O  OG1 . THR   C  1 168 ? 73.963 -8.581  43.384  1.00 23.12 ? 168  THR   C OG1 1 
ATOM   5550  C  CG2 . THR   C  1 168 ? 74.674 -10.819 43.001  1.00 23.53 ? 168  THR   C CG2 1 
ATOM   5551  N  N   . LYS   C  1 169 ? 71.536 -10.138 45.890  1.00 19.96 ? 169  LYS   C N   1 
ATOM   5552  C  CA  . LYS   C  1 169 ? 70.700 -9.656  46.979  1.00 20.00 ? 169  LYS   C CA  1 
ATOM   5553  C  C   . LYS   C  1 169 ? 70.791 -8.135  47.120  1.00 19.37 ? 169  LYS   C C   1 
ATOM   5554  O  O   . LYS   C  1 169 ? 71.897 -7.558  47.170  1.00 20.68 ? 169  LYS   C O   1 
ATOM   5555  C  CB  . LYS   C  1 169 ? 71.121 -10.300 48.315  1.00 19.26 ? 169  LYS   C CB  1 
ATOM   5556  C  CG  . LYS   C  1 169 ? 70.220 -9.850  49.463  1.00 18.76 ? 169  LYS   C CG  1 
ATOM   5557  C  CD  . LYS   C  1 169 ? 70.610 -10.536 50.788  1.00 19.47 ? 169  LYS   C CD  1 
ATOM   5558  C  CE  . LYS   C  1 169 ? 69.701 -9.996  51.902  1.00 22.76 ? 169  LYS   C CE  1 
ATOM   5559  N  NZ  . LYS   C  1 169 ? 69.936 -10.807 53.187  1.00 27.20 ? 169  LYS   C NZ  1 
ATOM   5560  N  N   . GLY   C  1 170 ? 69.614 -7.502  47.268  1.00 18.14 ? 170  GLY   C N   1 
ATOM   5561  C  CA  . GLY   C  1 170 ? 69.534 -6.080  47.527  1.00 19.63 ? 170  GLY   C CA  1 
ATOM   5562  C  C   . GLY   C  1 170 ? 69.374 -5.253  46.273  1.00 19.79 ? 170  GLY   C C   1 
ATOM   5563  O  O   . GLY   C  1 170 ? 69.058 -4.051  46.371  1.00 22.03 ? 170  GLY   C O   1 
ATOM   5564  N  N   . LYS   C  1 171 ? 69.656 -5.825  45.101  1.00 18.02 ? 171  LYS   C N   1 
ATOM   5565  C  CA  . LYS   C  1 171 ? 69.517 -5.046  43.880  1.00 18.71 ? 171  LYS   C CA  1 
ATOM   5566  C  C   . LYS   C  1 171 ? 68.041 -4.876  43.561  1.00 19.16 ? 171  LYS   C C   1 
ATOM   5567  O  O   . LYS   C  1 171 ? 67.235 -5.785  43.763  1.00 18.93 ? 171  LYS   C O   1 
ATOM   5568  C  CB  . LYS   C  1 171 ? 70.218 -5.707  42.687  1.00 20.34 ? 171  LYS   C CB  1 
ATOM   5569  C  CG  . LYS   C  1 171 ? 71.713 -5.771  42.830  1.00 22.60 ? 171  LYS   C CG  1 
ATOM   5570  C  CD  . LYS   C  1 171 ? 72.379 -6.049  41.504  1.00 29.33 ? 171  LYS   C CD  1 
ATOM   5571  C  CE  . LYS   C  1 171 ? 72.347 -4.828  40.572  1.00 30.36 ? 171  LYS   C CE  1 
ATOM   5572  N  NZ  . LYS   C  1 171 ? 73.134 -5.057  39.282  1.00 34.15 ? 171  LYS   C NZ  1 
ATOM   5573  N  N   . SER   C  1 172 ? 67.700 -3.705  43.025  1.00 19.49 ? 172  SER   C N   1 
ATOM   5574  C  CA  A SER   C  1 172 ? 66.335 -3.417  42.638  0.54 19.59 ? 172  SER   C CA  1 
ATOM   5575  C  CA  B SER   C  1 172 ? 66.335 -3.304  42.710  0.46 19.53 ? 172  SER   C CA  1 
ATOM   5576  C  C   . SER   C  1 172 ? 66.338 -2.617  41.352  1.00 20.15 ? 172  SER   C C   1 
ATOM   5577  O  O   . SER   C  1 172 ? 67.393 -2.124  40.880  1.00 22.50 ? 172  SER   C O   1 
ATOM   5578  C  CB  A SER   C  1 172 ? 65.606 -2.647  43.722  0.54 20.90 ? 172  SER   C CB  1 
ATOM   5579  C  CB  B SER   C  1 172 ? 65.770 -2.356  43.789  0.46 20.94 ? 172  SER   C CB  1 
ATOM   5580  O  OG  A SER   C  1 172 ? 66.265 -1.411  43.918  0.54 20.79 ? 172  SER   C OG  1 
ATOM   5581  O  OG  B SER   C  1 172 ? 64.422 -1.948  43.552  0.46 19.45 ? 172  SER   C OG  1 
ATOM   5582  N  N   . ALA   C  1 173 ? 65.165 -2.541  40.726  1.00 18.75 ? 173  ALA   C N   1 
ATOM   5583  C  CA  . ALA   C  1 173 ? 65.032 -1.784  39.473  1.00 19.91 ? 173  ALA   C CA  1 
ATOM   5584  C  C   . ALA   C  1 173 ? 63.612 -1.248  39.380  1.00 17.84 ? 173  ALA   C C   1 
ATOM   5585  O  O   . ALA   C  1 173 ? 62.672 -1.874  39.867  1.00 19.68 ? 173  ALA   C O   1 
ATOM   5586  C  CB  . ALA   C  1 173 ? 65.362 -2.640  38.219  1.00 20.36 ? 173  ALA   C CB  1 
ATOM   5587  N  N   . ASP   C  1 174 ? 63.446 -0.084  38.713  1.00 18.60 ? 174  ASP   C N   1 
ATOM   5588  C  CA  . ASP   C  1 174 ? 62.089 0.343   38.413  1.00 19.99 ? 174  ASP   C CA  1 
ATOM   5589  C  C   . ASP   C  1 174 ? 61.368 -0.713  37.580  1.00 22.77 ? 174  ASP   C C   1 
ATOM   5590  O  O   . ASP   C  1 174 ? 61.957 -1.361  36.725  1.00 22.24 ? 174  ASP   C O   1 
ATOM   5591  C  CB  . ASP   C  1 174 ? 62.079 1.626   37.592  1.00 19.95 ? 174  ASP   C CB  1 
ATOM   5592  C  CG  . ASP   C  1 174 ? 62.808 2.798   38.267  1.00 23.58 ? 174  ASP   C CG  1 
ATOM   5593  O  OD1 . ASP   C  1 174 ? 62.845 2.852   39.489  1.00 24.92 ? 174  ASP   C OD1 1 
ATOM   5594  O  OD2 . ASP   C  1 174 ? 63.255 3.699   37.506  1.00 31.26 ? 174  ASP   C OD2 1 
ATOM   5595  N  N   . PHE   C  1 175 ? 60.072 -0.845  37.811  1.00 18.65 ? 175  PHE   C N   1 
ATOM   5596  C  CA  . PHE   C  1 175 ? 59.327 -1.907  37.131  1.00 19.25 ? 175  PHE   C CA  1 
ATOM   5597  C  C   . PHE   C  1 175 ? 57.891 -1.403  37.060  1.00 17.85 ? 175  PHE   C C   1 
ATOM   5598  O  O   . PHE   C  1 175 ? 57.051 -1.733  37.921  1.00 21.69 ? 175  PHE   C O   1 
ATOM   5599  C  CB  . PHE   C  1 175 ? 59.431 -3.221  37.885  1.00 19.43 ? 175  PHE   C CB  1 
ATOM   5600  C  CG  . PHE   C  1 175 ? 58.983 -4.406  37.061  1.00 20.50 ? 175  PHE   C CG  1 
ATOM   5601  C  CD1 . PHE   C  1 175 ? 59.811 -4.884  36.043  1.00 22.62 ? 175  PHE   C CD1 1 
ATOM   5602  C  CD2 . PHE   C  1 175 ? 57.723 -4.981  37.250  1.00 19.68 ? 175  PHE   C CD2 1 
ATOM   5603  C  CE1 . PHE   C  1 175 ? 59.416 -6.018  35.251  1.00 24.80 ? 175  PHE   C CE1 1 
ATOM   5604  C  CE2 . PHE   C  1 175 ? 57.340 -6.121  36.465  1.00 22.56 ? 175  PHE   C CE2 1 
ATOM   5605  C  CZ  . PHE   C  1 175 ? 58.175 -6.610  35.480  1.00 24.27 ? 175  PHE   C CZ  1 
ATOM   5606  N  N   . THR   C  1 176 ? 57.600 -0.686  35.987  1.00 18.99 ? 176  THR   C N   1 
ATOM   5607  C  CA  . THR   C  1 176 ? 56.383 0.087   35.881  1.00 20.49 ? 176  THR   C CA  1 
ATOM   5608  C  C   . THR   C  1 176 ? 55.491 -0.480  34.786  1.00 24.93 ? 176  THR   C C   1 
ATOM   5609  O  O   . THR   C  1 176 ? 55.934 -1.231  33.913  1.00 24.27 ? 176  THR   C O   1 
ATOM   5610  C  CB  . THR   C  1 176 ? 56.697 1.553   35.587  1.00 22.53 ? 176  THR   C CB  1 
ATOM   5611  O  OG1 . THR   C  1 176 ? 57.518 1.643   34.421  1.00 23.48 ? 176  THR   C OG1 1 
ATOM   5612  C  CG2 . THR   C  1 176 ? 57.476 2.169   36.758  1.00 22.94 ? 176  THR   C CG2 1 
ATOM   5613  N  N   . ASN   C  1 177 ? 54.211 -0.157  34.896  1.00 24.24 ? 177  ASN   C N   1 
ATOM   5614  C  CA  . ASN   C  1 177 ? 53.236 -0.486  33.858  1.00 26.97 ? 177  ASN   C CA  1 
ATOM   5615  C  C   . ASN   C  1 177 ? 53.086 -1.998  33.645  1.00 27.38 ? 177  ASN   C C   1 
ATOM   5616  O  O   . ASN   C  1 177 ? 52.729 -2.438  32.542  1.00 31.40 ? 177  ASN   C O   1 
ATOM   5617  C  CB  . ASN   C  1 177 ? 53.611 0.218   32.534  1.00 29.55 ? 177  ASN   C CB  1 
ATOM   5618  C  CG  . ASN   C  1 177 ? 53.800 1.738   32.712  1.00 29.28 ? 177  ASN   C CG  1 
ATOM   5619  O  OD1 . ASN   C  1 177 ? 54.855 2.362   32.382  1.00 32.96 ? 177  ASN   C OD1 1 
ATOM   5620  N  ND2 . ASN   C  1 177 ? 52.747 2.350   33.216  1.00 27.39 ? 177  ASN   C ND2 1 
ATOM   5621  N  N   . PHE   C  1 178 ? 53.302 -2.807  34.676  1.00 24.18 ? 178  PHE   C N   1 
ATOM   5622  C  CA  . PHE   C  1 178 ? 53.147 -4.251  34.560  1.00 22.66 ? 178  PHE   C CA  1 
ATOM   5623  C  C   . PHE   C  1 178 ? 51.718 -4.644  34.914  1.00 26.41 ? 178  PHE   C C   1 
ATOM   5624  O  O   . PHE   C  1 178 ? 51.197 -4.261  35.966  1.00 27.33 ? 178  PHE   C O   1 
ATOM   5625  C  CB  . PHE   C  1 178 ? 54.113 -5.021  35.473  1.00 23.65 ? 178  PHE   C CB  1 
ATOM   5626  C  CG  . PHE   C  1 178 ? 53.995 -6.509  35.278  1.00 22.18 ? 178  PHE   C CG  1 
ATOM   5627  C  CD1 . PHE   C  1 178 ? 54.443 -7.095  34.106  1.00 26.03 ? 178  PHE   C CD1 1 
ATOM   5628  C  CD2 . PHE   C  1 178 ? 53.353 -7.279  36.206  1.00 19.38 ? 178  PHE   C CD2 1 
ATOM   5629  C  CE1 . PHE   C  1 178 ? 54.261 -8.494  33.906  1.00 25.73 ? 178  PHE   C CE1 1 
ATOM   5630  C  CE2 . PHE   C  1 178 ? 53.183 -8.651  36.018  1.00 23.00 ? 178  PHE   C CE2 1 
ATOM   5631  C  CZ  . PHE   C  1 178 ? 53.647 -9.252  34.883  1.00 22.80 ? 178  PHE   C CZ  1 
ATOM   5632  N  N   . ASP   C  1 179 ? 51.103 -5.454  34.045  1.00 25.16 ? 179  ASP   C N   1 
ATOM   5633  C  CA  . ASP   C  1 179 ? 49.736 -5.914  34.225  1.00 25.55 ? 179  ASP   C CA  1 
ATOM   5634  C  C   . ASP   C  1 179 ? 49.728 -7.304  34.850  1.00 26.48 ? 179  ASP   C C   1 
ATOM   5635  O  O   . ASP   C  1 179 ? 49.982 -8.293  34.145  1.00 24.81 ? 179  ASP   C O   1 
ATOM   5636  C  CB  . ASP   C  1 179 ? 49.064 -5.942  32.848  1.00 24.52 ? 179  ASP   C CB  1 
ATOM   5637  C  CG  . ASP   C  1 179 ? 47.631 -6.436  32.907  1.00 28.63 ? 179  ASP   C CG  1 
ATOM   5638  O  OD1 . ASP   C  1 179 ? 47.145 -6.662  34.039  1.00 27.91 ? 179  ASP   C OD1 1 
ATOM   5639  O  OD2 . ASP   C  1 179 ? 47.018 -6.567  31.808  1.00 32.97 ? 179  ASP   C OD2 1 
ATOM   5640  N  N   . PRO   C  1 180 ? 49.432 -7.461  36.151  1.00 23.42 ? 180  PRO   C N   1 
ATOM   5641  C  CA  . PRO   C  1 180 ? 49.448 -8.818  36.740  1.00 23.33 ? 180  PRO   C CA  1 
ATOM   5642  C  C   . PRO   C  1 180 ? 48.307 -9.699  36.234  1.00 23.13 ? 180  PRO   C C   1 
ATOM   5643  O  O   . PRO   C  1 180 ? 48.349 -10.919 36.431  1.00 23.57 ? 180  PRO   C O   1 
ATOM   5644  C  CB  . PRO   C  1 180 ? 49.359 -8.566  38.257  1.00 23.33 ? 180  PRO   C CB  1 
ATOM   5645  C  CG  . PRO   C  1 180 ? 48.609 -7.235  38.331  1.00 24.96 ? 180  PRO   C CG  1 
ATOM   5646  C  CD  . PRO   C  1 180 ? 49.064 -6.416  37.124  1.00 24.05 ? 180  PRO   C CD  1 
ATOM   5647  N  N   . ARG   C  1 181 ? 47.311 -9.135  35.546  1.00 24.29 ? 181  ARG   C N   1 
ATOM   5648  C  CA  . ARG   C  1 181 ? 46.294 -10.010 34.964  1.00 27.64 ? 181  ARG   C CA  1 
ATOM   5649  C  C   . ARG   C  1 181 ? 46.891 -10.968 33.949  1.00 24.73 ? 181  ARG   C C   1 
ATOM   5650  O  O   . ARG   C  1 181 ? 46.292 -12.021 33.656  1.00 26.44 ? 181  ARG   C O   1 
ATOM   5651  C  CB  . ARG   C  1 181 ? 45.196 -9.185  34.311  1.00 30.00 ? 181  ARG   C CB  1 
ATOM   5652  C  CG  . ARG   C  1 181 ? 44.414 -8.341  35.286  1.00 31.05 ? 181  ARG   C CG  1 
ATOM   5653  C  CD  . ARG   C  1 181 ? 43.518 -7.373  34.562  1.00 30.57 ? 181  ARG   C CD  1 
ATOM   5654  N  NE  . ARG   C  1 181 ? 44.310 -6.546  33.662  1.00 34.52 ? 181  ARG   C NE  1 
ATOM   5655  C  CZ  . ARG   C  1 181 ? 43.772 -5.751  32.754  1.00 38.06 ? 181  ARG   C CZ  1 
ATOM   5656  N  NH1 . ARG   C  1 181 ? 42.448 -5.704  32.673  1.00 42.96 ? 181  ARG   C NH1 1 
ATOM   5657  N  NH2 . ARG   C  1 181 ? 44.533 -5.022  31.938  1.00 37.78 ? 181  ARG   C NH2 1 
ATOM   5658  N  N   . GLY   C  1 182 ? 48.020 -10.604 33.359  1.00 26.76 ? 182  GLY   C N   1 
ATOM   5659  C  CA  . GLY   C  1 182 ? 48.629 -11.493 32.399  1.00 26.28 ? 182  GLY   C CA  1 
ATOM   5660  C  C   . GLY   C  1 182 ? 49.235 -12.736 33.003  1.00 26.16 ? 182  GLY   C C   1 
ATOM   5661  O  O   . GLY   C  1 182 ? 49.697 -13.610 32.246  1.00 27.26 ? 182  GLY   C O   1 
ATOM   5662  N  N   . LEU   C  1 183 ? 49.266 -12.824 34.344  1.00 24.18 ? 183  LEU   C N   1 
ATOM   5663  C  CA  . LEU   C  1 183 ? 49.765 -14.002 35.047  1.00 21.76 ? 183  LEU   C CA  1 
ATOM   5664  C  C   . LEU   C  1 183 ? 48.636 -14.866 35.584  1.00 24.01 ? 183  LEU   C C   1 
ATOM   5665  O  O   . LEU   C  1 183 ? 48.901 -15.827 36.314  1.00 23.51 ? 183  LEU   C O   1 
ATOM   5666  C  CB  . LEU   C  1 183 ? 50.700 -13.595 36.196  1.00 21.70 ? 183  LEU   C CB  1 
ATOM   5667  C  CG  . LEU   C  1 183 ? 51.932 -12.809 35.715  1.00 23.56 ? 183  LEU   C CG  1 
ATOM   5668  C  CD1 . LEU   C  1 183 ? 52.765 -12.359 36.903  1.00 22.92 ? 183  LEU   C CD1 1 
ATOM   5669  C  CD2 . LEU   C  1 183 ? 52.800 -13.608 34.760  1.00 23.74 ? 183  LEU   C CD2 1 
ATOM   5670  N  N   . LEU   C  1 184 ? 47.389 -14.570 35.223  1.00 25.14 ? 184  LEU   C N   1 
ATOM   5671  C  CA  . LEU   C  1 184 ? 46.236 -15.348 35.704  1.00 24.88 ? 184  LEU   C CA  1 
ATOM   5672  C  C   . LEU   C  1 184 ? 45.780 -16.354 34.650  1.00 24.45 ? 184  LEU   C C   1 
ATOM   5673  O  O   . LEU   C  1 184 ? 45.760 -16.041 33.462  1.00 26.28 ? 184  LEU   C O   1 
ATOM   5674  C  CB  . LEU   C  1 184 ? 45.053 -14.429 36.024  1.00 27.40 ? 184  LEU   C CB  1 
ATOM   5675  C  CG  . LEU   C  1 184 ? 45.337 -13.297 37.021  1.00 29.04 ? 184  LEU   C CG  1 
ATOM   5676  C  CD1 . LEU   C  1 184 ? 44.088 -12.424 37.120  1.00 28.43 ? 184  LEU   C CD1 1 
ATOM   5677  C  CD2 . LEU   C  1 184 ? 45.719 -13.878 38.370  1.00 27.52 ? 184  LEU   C CD2 1 
ATOM   5678  N  N   . PRO   C  1 185 ? 45.337 -17.541 35.049  1.00 24.71 ? 185  PRO   C N   1 
ATOM   5679  C  CA  . PRO   C  1 185 ? 44.701 -18.473 34.109  1.00 27.59 ? 185  PRO   C CA  1 
ATOM   5680  C  C   . PRO   C  1 185 ? 43.278 -18.027 33.797  1.00 27.25 ? 185  PRO   C C   1 
ATOM   5681  O  O   . PRO   C  1 185 ? 42.740 -17.119 34.429  1.00 29.71 ? 185  PRO   C O   1 
ATOM   5682  C  CB  . PRO   C  1 185 ? 44.682 -19.809 34.881  1.00 25.38 ? 185  PRO   C CB  1 
ATOM   5683  C  CG  . PRO   C  1 185 ? 44.521 -19.361 36.365  1.00 25.36 ? 185  PRO   C CG  1 
ATOM   5684  C  CD  . PRO   C  1 185 ? 45.307 -18.006 36.460  1.00 24.17 ? 185  PRO   C CD  1 
ATOM   5685  N  N   . GLU   C  1 186 ? 42.651 -18.701 32.820  1.00 28.03 ? 186  GLU   C N   1 
ATOM   5686  C  CA  . GLU   C  1 186 ? 41.299 -18.310 32.454  1.00 31.98 ? 186  GLU   C CA  1 
ATOM   5687  C  C   . GLU   C  1 186 ? 40.287 -18.654 33.551  1.00 32.15 ? 186  GLU   C C   1 
ATOM   5688  O  O   . GLU   C  1 186 ? 39.354 -17.883 33.799  1.00 35.16 ? 186  GLU   C O   1 
ATOM   5689  C  CB  . GLU   C  1 186 ? 40.935 -18.972 31.130  1.00 39.09 ? 186  GLU   C CB  1 
ATOM   5690  C  CG  . GLU   C  1 186 ? 39.539 -18.658 30.600  1.00 51.42 ? 186  GLU   C CG  1 
ATOM   5691  C  CD  . GLU   C  1 186 ? 39.335 -19.095 29.129  1.00 62.01 ? 186  GLU   C CD  1 
ATOM   5692  O  OE1 . GLU   C  1 186 ? 38.379 -18.599 28.484  1.00 65.89 ? 186  GLU   C OE1 1 
ATOM   5693  O  OE2 . GLU   C  1 186 ? 40.132 -19.920 28.612  1.00 65.11 ? 186  GLU   C OE2 1 
ATOM   5694  N  N   . SER   C  1 187 ? 40.424 -19.819 34.189  1.00 27.33 ? 187  SER   C N   1 
ATOM   5695  C  CA  . SER   C  1 187 ? 39.489 -20.243 35.231  1.00 28.64 ? 187  SER   C CA  1 
ATOM   5696  C  C   . SER   C  1 187 ? 39.973 -19.785 36.598  1.00 27.88 ? 187  SER   C C   1 
ATOM   5697  O  O   . SER   C  1 187 ? 41.153 -19.900 36.913  1.00 26.64 ? 187  SER   C O   1 
ATOM   5698  C  CB  . SER   C  1 187 ? 39.362 -21.760 35.273  1.00 29.44 ? 187  SER   C CB  1 
ATOM   5699  O  OG  . SER   C  1 187 ? 38.487 -22.123 36.352  1.00 31.43 ? 187  SER   C OG  1 
ATOM   5700  N  N   . LEU   C  1 188 ? 39.049 -19.301 37.422  1.00 29.00 ? 188  LEU   C N   1 
ATOM   5701  C  CA  . LEU   C  1 188 ? 39.412 -18.927 38.786  1.00 28.29 ? 188  LEU   C CA  1 
ATOM   5702  C  C   . LEU   C  1 188 ? 38.887 -19.931 39.804  1.00 29.21 ? 188  LEU   C C   1 
ATOM   5703  O  O   . LEU   C  1 188 ? 38.825 -19.608 40.994  1.00 30.34 ? 188  LEU   C O   1 
ATOM   5704  C  CB  . LEU   C  1 188 ? 38.934 -17.511 39.122  1.00 32.13 ? 188  LEU   C CB  1 
ATOM   5705  C  CG  . LEU   C  1 188 ? 39.467 -16.351 38.278  1.00 32.44 ? 188  LEU   C CG  1 
ATOM   5706  C  CD1 . LEU   C  1 188 ? 38.926 -14.995 38.765  1.00 34.94 ? 188  LEU   C CD1 1 
ATOM   5707  C  CD2 . LEU   C  1 188 ? 40.986 -16.323 38.283  1.00 30.44 ? 188  LEU   C CD2 1 
ATOM   5708  N  N   . ASP   C  1 189 ? 38.560 -21.151 39.366  1.00 26.07 ? 189  ASP   C N   1 
ATOM   5709  C  CA  . ASP   C  1 189 ? 38.301 -22.251 40.299  1.00 25.22 ? 189  ASP   C CA  1 
ATOM   5710  C  C   . ASP   C  1 189 ? 39.476 -22.382 41.271  1.00 23.29 ? 189  ASP   C C   1 
ATOM   5711  O  O   . ASP   C  1 189 ? 40.642 -22.293 40.872  1.00 23.74 ? 189  ASP   C O   1 
ATOM   5712  C  CB  . ASP   C  1 189 ? 38.127 -23.563 39.530  1.00 26.56 ? 189  ASP   C CB  1 
ATOM   5713  C  CG  . ASP   C  1 189 ? 36.795 -23.647 38.790  1.00 31.69 ? 189  ASP   C CG  1 
ATOM   5714  O  OD1 . ASP   C  1 189 ? 35.975 -22.714 38.885  1.00 35.00 ? 189  ASP   C OD1 1 
ATOM   5715  O  OD2 . ASP   C  1 189 ? 36.554 -24.662 38.115  1.00 33.85 ? 189  ASP   C OD2 1 
ATOM   5716  N  N   . TYR   C  1 190 ? 39.190 -22.634 42.555  1.00 21.58 ? 190  TYR   C N   1 
ATOM   5717  C  CA  . TYR   C  1 190 ? 40.294 -22.606 43.516  1.00 21.43 ? 190  TYR   C CA  1 
ATOM   5718  C  C   . TYR   C  1 190 ? 40.015 -23.529 44.699  1.00 22.65 ? 190  TYR   C C   1 
ATOM   5719  O  O   . TYR   C  1 190 ? 38.877 -23.980 44.934  1.00 23.51 ? 190  TYR   C O   1 
ATOM   5720  C  CB  . TYR   C  1 190 ? 40.580 -21.183 44.037  1.00 20.83 ? 190  TYR   C CB  1 
ATOM   5721  C  CG  . TYR   C  1 190 ? 39.419 -20.601 44.821  1.00 22.12 ? 190  TYR   C CG  1 
ATOM   5722  C  CD1 . TYR   C  1 190 ? 39.275 -20.882 46.179  1.00 23.28 ? 190  TYR   C CD1 1 
ATOM   5723  C  CD2 . TYR   C  1 190 ? 38.454 -19.803 44.214  1.00 22.80 ? 190  TYR   C CD2 1 
ATOM   5724  C  CE1 . TYR   C  1 190 ? 38.183 -20.348 46.931  1.00 24.90 ? 190  TYR   C CE1 1 
ATOM   5725  C  CE2 . TYR   C  1 190 ? 37.347 -19.274 44.961  1.00 24.20 ? 190  TYR   C CE2 1 
ATOM   5726  C  CZ  . TYR   C  1 190 ? 37.222 -19.544 46.317  1.00 23.51 ? 190  TYR   C CZ  1 
ATOM   5727  O  OH  . TYR   C  1 190 ? 36.097 -19.061 47.024  1.00 26.32 ? 190  TYR   C OH  1 
ATOM   5728  N  N   . TRP   C  1 191 ? 41.094 -23.839 45.424  1.00 21.04 ? 191  TRP   C N   1 
ATOM   5729  C  CA  . TRP   C  1 191 ? 41.042 -24.458 46.739  1.00 20.49 ? 191  TRP   C CA  1 
ATOM   5730  C  C   . TRP   C  1 191 ? 41.432 -23.418 47.769  1.00 21.63 ? 191  TRP   C C   1 
ATOM   5731  O  O   . TRP   C  1 191 ? 42.262 -22.543 47.480  1.00 20.64 ? 191  TRP   C O   1 
ATOM   5732  C  CB  . TRP   C  1 191 ? 41.984 -25.648 46.832  1.00 21.84 ? 191  TRP   C CB  1 
ATOM   5733  C  CG  . TRP   C  1 191 ? 41.684 -26.764 45.901  1.00 22.53 ? 191  TRP   C CG  1 
ATOM   5734  C  CD1 . TRP   C  1 191 ? 40.704 -27.692 46.023  1.00 23.03 ? 191  TRP   C CD1 1 
ATOM   5735  C  CD2 . TRP   C  1 191 ? 42.427 -27.124 44.723  1.00 22.08 ? 191  TRP   C CD2 1 
ATOM   5736  N  NE1 . TRP   C  1 191 ? 40.761 -28.593 44.991  1.00 26.49 ? 191  TRP   C NE1 1 
ATOM   5737  C  CE2 . TRP   C  1 191 ? 41.833 -28.290 44.196  1.00 24.84 ? 191  TRP   C CE2 1 
ATOM   5738  C  CE3 . TRP   C  1 191 ? 43.547 -26.584 44.082  1.00 25.61 ? 191  TRP   C CE3 1 
ATOM   5739  C  CZ2 . TRP   C  1 191 ? 42.293 -28.906 42.995  1.00 24.89 ? 191  TRP   C CZ2 1 
ATOM   5740  C  CZ3 . TRP   C  1 191 ? 44.017 -27.208 42.909  1.00 24.48 ? 191  TRP   C CZ3 1 
ATOM   5741  C  CH2 . TRP   C  1 191 ? 43.408 -28.352 42.403  1.00 26.51 ? 191  TRP   C CH2 1 
ATOM   5742  N  N   . THR   C  1 192 ? 40.876 -23.501 48.981  1.00 20.38 ? 192  THR   C N   1 
ATOM   5743  C  CA  . THR   C  1 192 ? 41.227 -22.530 50.020  1.00 19.74 ? 192  THR   C CA  1 
ATOM   5744  C  C   . THR   C  1 192 ? 41.360 -23.211 51.371  1.00 20.20 ? 192  THR   C C   1 
ATOM   5745  O  O   . THR   C  1 192 ? 40.631 -24.166 51.689  1.00 21.88 ? 192  THR   C O   1 
ATOM   5746  C  CB  . THR   C  1 192 ? 40.192 -21.359 50.088  1.00 18.79 ? 192  THR   C CB  1 
ATOM   5747  O  OG1 . THR   C  1 192 ? 40.619 -20.370 51.051  1.00 19.20 ? 192  THR   C OG1 1 
ATOM   5748  C  CG2 . THR   C  1 192 ? 38.777 -21.830 50.442  1.00 21.11 ? 192  THR   C CG2 1 
ATOM   5749  N  N   . TYR   C  1 193 ? 42.264 -22.687 52.181  1.00 19.00 ? 193  TYR   C N   1 
ATOM   5750  C  CA  . TYR   C  1 193 ? 42.450 -23.205 53.527  1.00 18.26 ? 193  TYR   C CA  1 
ATOM   5751  C  C   . TYR   C  1 193 ? 43.187 -22.150 54.353  1.00 18.20 ? 193  TYR   C C   1 
ATOM   5752  O  O   . TYR   C  1 193 ? 43.836 -21.272 53.786  1.00 18.99 ? 193  TYR   C O   1 
ATOM   5753  C  CB  . TYR   C  1 193 ? 43.228 -24.554 53.519  1.00 18.61 ? 193  TYR   C CB  1 
ATOM   5754  C  CG  . TYR   C  1 193 ? 44.703 -24.364 53.219  1.00 16.13 ? 193  TYR   C CG  1 
ATOM   5755  C  CD1 . TYR   C  1 193 ? 45.136 -24.227 51.915  1.00 18.27 ? 193  TYR   C CD1 1 
ATOM   5756  C  CD2 . TYR   C  1 193 ? 45.665 -24.324 54.259  1.00 15.35 ? 193  TYR   C CD2 1 
ATOM   5757  C  CE1 . TYR   C  1 193 ? 46.501 -24.033 51.635  1.00 17.64 ? 193  TYR   C CE1 1 
ATOM   5758  C  CE2 . TYR   C  1 193 ? 47.020 -24.116 53.991  1.00 15.82 ? 193  TYR   C CE2 1 
ATOM   5759  C  CZ  . TYR   C  1 193 ? 47.422 -23.987 52.665  1.00 16.89 ? 193  TYR   C CZ  1 
ATOM   5760  O  OH  . TYR   C  1 193 ? 48.760 -23.736 52.392  1.00 17.08 ? 193  TYR   C OH  1 
ATOM   5761  N  N   . PRO   C  1 194 ? 43.053 -22.181 55.682  1.00 17.47 ? 194  PRO   C N   1 
ATOM   5762  C  CA  . PRO   C  1 194 ? 43.788 -21.230 56.541  1.00 18.91 ? 194  PRO   C CA  1 
ATOM   5763  C  C   . PRO   C  1 194 ? 45.205 -21.724 56.768  1.00 16.78 ? 194  PRO   C C   1 
ATOM   5764  O  O   . PRO   C  1 194 ? 45.422 -22.874 57.173  1.00 16.38 ? 194  PRO   C O   1 
ATOM   5765  C  CB  . PRO   C  1 194 ? 42.987 -21.257 57.849  1.00 18.05 ? 194  PRO   C CB  1 
ATOM   5766  C  CG  . PRO   C  1 194 ? 42.282 -22.616 57.832  1.00 20.48 ? 194  PRO   C CG  1 
ATOM   5767  C  CD  . PRO   C  1 194 ? 42.062 -23.002 56.422  1.00 19.04 ? 194  PRO   C CD  1 
ATOM   5768  N  N   . GLY   C  1 195 ? 46.176 -20.866 56.518  1.00 15.16 ? 195  GLY   C N   1 
ATOM   5769  C  CA  . GLY   C  1 195 ? 47.577 -21.243 56.666  1.00 14.77 ? 195  GLY   C CA  1 
ATOM   5770  C  C   . GLY   C  1 195 ? 48.471 -20.104 57.064  1.00 14.75 ? 195  GLY   C C   1 
ATOM   5771  O  O   . GLY   C  1 195 ? 48.077 -19.218 57.839  1.00 16.22 ? 195  GLY   C O   1 
ATOM   5772  N  N   . SER   C  1 196 ? 49.701 -20.130 56.529  1.00 14.36 ? 196  SER   C N   1 
ATOM   5773  C  CA  . SER   C  1 196 ? 50.776 -19.274 57.043  1.00 15.38 ? 196  SER   C CA  1 
ATOM   5774  C  C   . SER   C  1 196 ? 51.584 -18.696 55.896  1.00 15.34 ? 196  SER   C C   1 
ATOM   5775  O  O   . SER   C  1 196 ? 51.489 -19.129 54.738  1.00 15.10 ? 196  SER   C O   1 
ATOM   5776  C  CB  . SER   C  1 196 ? 51.729 -20.093 57.964  1.00 14.95 ? 196  SER   C CB  1 
ATOM   5777  O  OG  . SER   C  1 196 ? 52.530 -20.997 57.168  1.00 15.72 ? 196  SER   C OG  1 
ATOM   5778  N  N   . LEU   C  1 197 ? 52.447 -17.734 56.256  1.00 14.01 ? 197  LEU   C N   1 
ATOM   5779  C  CA  . LEU   C  1 197 ? 53.538 -17.425 55.346  1.00 13.99 ? 197  LEU   C CA  1 
ATOM   5780  C  C   . LEU   C  1 197 ? 54.360 -18.691 55.105  1.00 15.34 ? 197  LEU   C C   1 
ATOM   5781  O  O   . LEU   C  1 197 ? 54.560 -19.496 56.027  1.00 14.70 ? 197  LEU   C O   1 
ATOM   5782  C  CB  . LEU   C  1 197 ? 54.454 -16.364 55.972  1.00 14.15 ? 197  LEU   C CB  1 
ATOM   5783  C  CG  . LEU   C  1 197 ? 53.809 -15.027 56.317  1.00 13.34 ? 197  LEU   C CG  1 
ATOM   5784  C  CD1 . LEU   C  1 197 ? 54.913 -14.192 56.979  1.00 15.62 ? 197  LEU   C CD1 1 
ATOM   5785  C  CD2 . LEU   C  1 197 ? 53.248 -14.292 55.080  1.00 15.62 ? 197  LEU   C CD2 1 
ATOM   5786  N  N   . THR   C  1 198 ? 54.885 -18.847 53.887  1.00 14.25 ? 198  THR   C N   1 
ATOM   5787  C  CA  . THR   C  1 198 ? 55.717 -20.038 53.645  1.00 14.11 ? 198  THR   C CA  1 
ATOM   5788  C  C   . THR   C  1 198 ? 57.208 -19.742 53.830  1.00 13.87 ? 198  THR   C C   1 
ATOM   5789  O  O   . THR   C  1 198 ? 58.034 -20.631 53.546  1.00 13.08 ? 198  THR   C O   1 
ATOM   5790  C  CB  . THR   C  1 198 ? 55.513 -20.640 52.241  1.00 14.73 ? 198  THR   C CB  1 
ATOM   5791  O  OG1 . THR   C  1 198 ? 55.979 -19.630 51.307  1.00 15.13 ? 198  THR   C OG1 1 
ATOM   5792  C  CG2 . THR   C  1 198 ? 54.040 -20.974 51.963  1.00 14.71 ? 198  THR   C CG2 1 
ATOM   5793  N  N   . THR   C  1 199 ? 57.549 -18.567 54.347  1.00 14.02 ? 199  THR   C N   1 
ATOM   5794  C  CA  . THR   C  1 199 ? 58.912 -18.221 54.729  1.00 14.69 ? 199  THR   C CA  1 
ATOM   5795  C  C   . THR   C  1 199 ? 58.850 -17.729 56.161  1.00 13.62 ? 199  THR   C C   1 
ATOM   5796  O  O   . THR   C  1 199 ? 57.791 -17.284 56.632  1.00 14.94 ? 199  THR   C O   1 
ATOM   5797  C  CB  . THR   C  1 199 ? 59.547 -17.094 53.871  1.00 15.11 ? 199  THR   C CB  1 
ATOM   5798  O  OG1 . THR   C  1 199 ? 58.825 -15.866 54.088  1.00 15.61 ? 199  THR   C OG1 1 
ATOM   5799  C  CG2 . THR   C  1 199 ? 59.516 -17.470 52.389  1.00 15.31 ? 199  THR   C CG2 1 
ATOM   5800  N  N   . PRO   C  1 200 ? 59.966 -17.768 56.876  1.00 14.61 ? 200  PRO   C N   1 
ATOM   5801  C  CA  . PRO   C  1 200 ? 60.042 -17.015 58.125  1.00 12.51 ? 200  PRO   C CA  1 
ATOM   5802  C  C   . PRO   C  1 200 ? 59.496 -15.610 57.929  1.00 14.13 ? 200  PRO   C C   1 
ATOM   5803  O  O   . PRO   C  1 200 ? 59.754 -14.965 56.895  1.00 14.12 ? 200  PRO   C O   1 
ATOM   5804  C  CB  . PRO   C  1 200 ? 61.569 -17.009 58.444  1.00 14.63 ? 200  PRO   C CB  1 
ATOM   5805  C  CG  . PRO   C  1 200 ? 62.032 -18.390 57.860  1.00 15.19 ? 200  PRO   C CG  1 
ATOM   5806  C  CD  . PRO   C  1 200 ? 61.271 -18.368 56.488  1.00 14.40 ? 200  PRO   C CD  1 
ATOM   5807  N  N   . PRO   C  1 201 ? 58.758 -15.085 58.909  1.00 13.73 ? 201  PRO   C N   1 
ATOM   5808  C  CA  . PRO   C  1 201 ? 58.540 -15.674 60.249  1.00 13.40 ? 201  PRO   C CA  1 
ATOM   5809  C  C   . PRO   C  1 201 ? 57.436 -16.718 60.350  1.00 13.08 ? 201  PRO   C C   1 
ATOM   5810  O  O   . PRO   C  1 201 ? 57.105 -17.117 61.476  1.00 14.48 ? 201  PRO   C O   1 
ATOM   5811  C  CB  . PRO   C  1 201 ? 58.179 -14.439 61.128  1.00 13.75 ? 201  PRO   C CB  1 
ATOM   5812  C  CG  . PRO   C  1 201 ? 57.443 -13.496 60.130  1.00 13.46 ? 201  PRO   C CG  1 
ATOM   5813  C  CD  . PRO   C  1 201 ? 58.220 -13.705 58.821  1.00 14.52 ? 201  PRO   C CD  1 
ATOM   5814  N  N   . LEU   C  1 202 ? 56.878 -17.177 59.222  1.00 13.80 ? 202  LEU   C N   1 
ATOM   5815  C  CA  . LEU   C  1 202 ? 55.960 -18.340 59.210  1.00 13.08 ? 202  LEU   C CA  1 
ATOM   5816  C  C   . LEU   C  1 202 ? 54.663 -18.065 59.985  1.00 13.75 ? 202  LEU   C C   1 
ATOM   5817  O  O   . LEU   C  1 202 ? 53.991 -19.016 60.466  1.00 14.68 ? 202  LEU   C O   1 
ATOM   5818  C  CB  . LEU   C  1 202 ? 56.651 -19.618 59.721  1.00 14.31 ? 202  LEU   C CB  1 
ATOM   5819  C  CG  . LEU   C  1 202 ? 57.871 -20.019 58.875  1.00 13.52 ? 202  LEU   C CG  1 
ATOM   5820  C  CD1 . LEU   C  1 202 ? 58.691 -21.115 59.551  1.00 14.47 ? 202  LEU   C CD1 1 
ATOM   5821  C  CD2 . LEU   C  1 202 ? 57.435 -20.512 57.485  1.00 14.07 ? 202  LEU   C CD2 1 
ATOM   5822  N  N   . LEU   C  1 203 ? 54.297 -16.796 60.099  1.00 14.77 ? 203  LEU   C N   1 
ATOM   5823  C  CA  . LEU   C  1 203 ? 53.099 -16.437 60.875  1.00 13.61 ? 203  LEU   C CA  1 
ATOM   5824  C  C   . LEU   C  1 203 ? 51.826 -16.998 60.243  1.00 13.57 ? 203  LEU   C C   1 
ATOM   5825  O  O   . LEU   C  1 203 ? 51.652 -16.999 59.018  1.00 13.99 ? 203  LEU   C O   1 
ATOM   5826  C  CB  . LEU   C  1 203 ? 53.003 -14.906 60.992  1.00 14.71 ? 203  LEU   C CB  1 
ATOM   5827  C  CG  . LEU   C  1 203 ? 54.193 -14.318 61.806  1.00 15.40 ? 203  LEU   C CG  1 
ATOM   5828  C  CD1 . LEU   C  1 203 ? 54.139 -12.767 61.740  1.00 17.67 ? 203  LEU   C CD1 1 
ATOM   5829  C  CD2 . LEU   C  1 203 ? 54.118 -14.807 63.303  1.00 16.79 ? 203  LEU   C CD2 1 
ATOM   5830  N  N   . GLU   C  1 204 ? 50.886 -17.383 61.105  1.00 14.74 ? 204  GLU   C N   1 
ATOM   5831  C  CA  . GLU   C  1 204 ? 49.655 -18.064 60.659  1.00 15.04 ? 204  GLU   C CA  1 
ATOM   5832  C  C   . GLU   C  1 204 ? 48.553 -17.031 60.421  1.00 15.98 ? 204  GLU   C C   1 
ATOM   5833  O  O   . GLU   C  1 204 ? 47.486 -17.025 61.045  1.00 17.97 ? 204  GLU   C O   1 
ATOM   5834  C  CB  . GLU   C  1 204 ? 49.289 -19.116 61.695  1.00 16.47 ? 204  GLU   C CB  1 
ATOM   5835  C  CG  . GLU   C  1 204 ? 50.404 -20.192 61.714  1.00 15.30 ? 204  GLU   C CG  1 
ATOM   5836  C  CD  . GLU   C  1 204 ? 50.180 -21.323 62.718  1.00 16.69 ? 204  GLU   C CD  1 
ATOM   5837  O  OE1 . GLU   C  1 204 ? 49.497 -21.093 63.763  1.00 18.26 ? 204  GLU   C OE1 1 
ATOM   5838  O  OE2 . GLU   C  1 204 ? 50.754 -22.419 62.472  1.00 16.35 ? 204  GLU   C OE2 1 
ATOM   5839  N  N   . SER   C  1 205 ? 48.832 -16.189 59.418  1.00 15.12 ? 205  SER   C N   1 
ATOM   5840  C  CA  A SER   C  1 205 ? 47.990 -15.034 59.115  0.59 15.13 ? 205  SER   C CA  1 
ATOM   5841  C  CA  B SER   C  1 205 ? 48.004 -15.031 59.108  0.41 15.15 ? 205  SER   C CA  1 
ATOM   5842  C  C   . SER   C  1 205 ? 47.457 -15.050 57.693  1.00 14.76 ? 205  SER   C C   1 
ATOM   5843  O  O   . SER   C  1 205 ? 46.916 -14.027 57.237  1.00 17.46 ? 205  SER   C O   1 
ATOM   5844  C  CB  A SER   C  1 205 ? 48.770 -13.747 59.339  0.59 16.26 ? 205  SER   C CB  1 
ATOM   5845  C  CB  B SER   C  1 205 ? 48.816 -13.763 59.331  0.41 16.01 ? 205  SER   C CB  1 
ATOM   5846  O  OG  A SER   C  1 205 ? 49.970 -13.843 58.630  0.59 16.32 ? 205  SER   C OG  1 
ATOM   5847  O  OG  B SER   C  1 205 ? 49.468 -13.885 60.576  0.41 15.99 ? 205  SER   C OG  1 
ATOM   5848  N  N   . VAL   C  1 206 ? 47.528 -16.182 56.981  1.00 16.14 ? 206  VAL   C N   1 
ATOM   5849  C  CA  . VAL   C  1 206 ? 47.222 -16.197 55.544  1.00 16.67 ? 206  VAL   C CA  1 
ATOM   5850  C  C   . VAL   C  1 206 ? 45.984 -17.037 55.277  1.00 18.32 ? 206  VAL   C C   1 
ATOM   5851  O  O   . VAL   C  1 206 ? 45.918 -18.200 55.667  1.00 18.97 ? 206  VAL   C O   1 
ATOM   5852  C  CB  . VAL   C  1 206 ? 48.402 -16.742 54.716  1.00 16.06 ? 206  VAL   C CB  1 
ATOM   5853  C  CG1 . VAL   C  1 206 ? 48.015 -16.813 53.206  1.00 16.50 ? 206  VAL   C CG1 1 
ATOM   5854  C  CG2 . VAL   C  1 206 ? 49.706 -15.903 54.888  1.00 15.12 ? 206  VAL   C CG2 1 
ATOM   5855  N  N   . THR   C  1 207 ? 45.034 -16.469 54.551  1.00 16.43 ? 207  THR   C N   1 
ATOM   5856  C  CA  . THR   C  1 207 ? 43.998 -17.267 53.871  1.00 16.64 ? 207  THR   C CA  1 
ATOM   5857  C  C   . THR   C  1 207 ? 44.536 -17.570 52.484  1.00 18.65 ? 207  THR   C C   1 
ATOM   5858  O  O   . THR   C  1 207 ? 44.767 -16.643 51.703  1.00 18.16 ? 207  THR   C O   1 
ATOM   5859  C  CB  . THR   C  1 207 ? 42.683 -16.486 53.761  1.00 17.24 ? 207  THR   C CB  1 
ATOM   5860  O  OG1 . THR   C  1 207 ? 42.194 -16.226 55.070  1.00 20.62 ? 207  THR   C OG1 1 
ATOM   5861  C  CG2 . THR   C  1 207 ? 41.657 -17.332 53.032  1.00 19.69 ? 207  THR   C CG2 1 
ATOM   5862  N  N   . TRP   C  1 208 ? 44.826 -18.847 52.227  1.00 16.76 ? 208  TRP   C N   1 
ATOM   5863  C  CA  . TRP   C  1 208 ? 45.357 -19.310 50.938  1.00 17.64 ? 208  TRP   C CA  1 
ATOM   5864  C  C   . TRP   C  1 208 ? 44.231 -19.554 49.954  1.00 19.15 ? 208  TRP   C C   1 
ATOM   5865  O  O   . TRP   C  1 208 ? 43.238 -20.215 50.287  1.00 18.57 ? 208  TRP   C O   1 
ATOM   5866  C  CB  . TRP   C  1 208 ? 46.155 -20.623 51.116  1.00 16.69 ? 208  TRP   C CB  1 
ATOM   5867  C  CG  . TRP   C  1 208 ? 47.540 -20.267 51.583  1.00 15.14 ? 208  TRP   C CG  1 
ATOM   5868  C  CD1 . TRP   C  1 208 ? 48.013 -20.261 52.886  1.00 15.44 ? 208  TRP   C CD1 1 
ATOM   5869  C  CD2 . TRP   C  1 208 ? 48.622 -19.807 50.760  1.00 16.25 ? 208  TRP   C CD2 1 
ATOM   5870  N  NE1 . TRP   C  1 208 ? 49.329 -19.771 52.905  1.00 15.91 ? 208  TRP   C NE1 1 
ATOM   5871  C  CE2 . TRP   C  1 208 ? 49.701 -19.497 51.613  1.00 16.34 ? 208  TRP   C CE2 1 
ATOM   5872  C  CE3 . TRP   C  1 208 ? 48.767 -19.621 49.366  1.00 17.69 ? 208  TRP   C CE3 1 
ATOM   5873  C  CZ2 . TRP   C  1 208 ? 50.942 -19.035 51.141  1.00 15.03 ? 208  TRP   C CZ2 1 
ATOM   5874  C  CZ3 . TRP   C  1 208 ? 50.024 -19.133 48.872  1.00 17.38 ? 208  TRP   C CZ3 1 
ATOM   5875  C  CH2 . TRP   C  1 208 ? 51.079 -18.831 49.760  1.00 15.57 ? 208  TRP   C CH2 1 
ATOM   5876  N  N   . ILE   C  1 209 ? 44.417 -19.047 48.732  1.00 18.50 ? 209  ILE   C N   1 
ATOM   5877  C  CA  . ILE   C  1 209 ? 43.496 -19.279 47.633  1.00 18.07 ? 209  ILE   C CA  1 
ATOM   5878  C  C   . ILE   C  1 209 ? 44.384 -19.799 46.512  1.00 19.77 ? 209  ILE   C C   1 
ATOM   5879  O  O   . ILE   C  1 209 ? 45.141 -19.016 45.911  1.00 19.91 ? 209  ILE   C O   1 
ATOM   5880  C  CB  . ILE   C  1 209 ? 42.785 -17.979 47.237  1.00 20.61 ? 209  ILE   C CB  1 
ATOM   5881  C  CG1 . ILE   C  1 209 ? 41.945 -17.469 48.417  1.00 22.90 ? 209  ILE   C CG1 1 
ATOM   5882  C  CG2 . ILE   C  1 209 ? 41.915 -18.199 46.013  1.00 20.54 ? 209  ILE   C CG2 1 
ATOM   5883  C  CD1 . ILE   C  1 209 ? 41.398 -16.023 48.236  1.00 22.58 ? 209  ILE   C CD1 1 
ATOM   5884  N  N   . VAL   C  1 210 ? 44.351 -21.107 46.255  1.00 19.31 ? 210  VAL   C N   1 
ATOM   5885  C  CA  . VAL   C  1 210 ? 45.244 -21.740 45.283  1.00 19.47 ? 210  VAL   C CA  1 
ATOM   5886  C  C   . VAL   C  1 210 ? 44.426 -22.117 44.054  1.00 21.14 ? 210  VAL   C C   1 
ATOM   5887  O  O   . VAL   C  1 210 ? 43.471 -22.908 44.144  1.00 20.35 ? 210  VAL   C O   1 
ATOM   5888  C  CB  . VAL   C  1 210 ? 45.926 -22.979 45.871  1.00 20.43 ? 210  VAL   C CB  1 
ATOM   5889  C  CG1 . VAL   C  1 210 ? 46.829 -23.637 44.810  1.00 19.04 ? 210  VAL   C CG1 1 
ATOM   5890  C  CG2 . VAL   C  1 210 ? 46.767 -22.579 47.091  1.00 18.50 ? 210  VAL   C CG2 1 
ATOM   5891  N  N   . LEU   C  1 211 ? 44.746 -21.485 42.898  1.00 19.89 ? 211  LEU   C N   1 
ATOM   5892  C  CA  . LEU   C  1 211 ? 43.957 -21.745 41.694  1.00 21.15 ? 211  LEU   C CA  1 
ATOM   5893  C  C   . LEU   C  1 211 ? 44.232 -23.139 41.140  1.00 22.68 ? 211  LEU   C C   1 
ATOM   5894  O  O   . LEU   C  1 211 ? 45.361 -23.636 41.149  1.00 23.56 ? 211  LEU   C O   1 
ATOM   5895  C  CB  . LEU   C  1 211 ? 44.263 -20.713 40.632  1.00 21.12 ? 211  LEU   C CB  1 
ATOM   5896  C  CG  . LEU   C  1 211 ? 43.938 -19.249 40.986  1.00 22.06 ? 211  LEU   C CG  1 
ATOM   5897  C  CD1 . LEU   C  1 211 ? 44.207 -18.401 39.719  1.00 21.31 ? 211  LEU   C CD1 1 
ATOM   5898  C  CD2 . LEU   C  1 211 ? 42.466 -19.132 41.401  1.00 23.92 ? 211  LEU   C CD2 1 
ATOM   5899  N  N   . LYS   C  1 212 ? 43.173 -23.796 40.684  1.00 23.48 ? 212  LYS   C N   1 
ATOM   5900  C  CA  . LYS   C  1 212 ? 43.329 -25.135 40.139  1.00 22.56 ? 212  LYS   C CA  1 
ATOM   5901  C  C   . LYS   C  1 212 ? 44.029 -25.144 38.779  1.00 25.23 ? 212  LYS   C C   1 
ATOM   5902  O  O   . LYS   C  1 212 ? 44.794 -26.072 38.470  1.00 26.76 ? 212  LYS   C O   1 
ATOM   5903  C  CB  . LYS   C  1 212 ? 41.955 -25.770 40.047  1.00 26.37 ? 212  LYS   C CB  1 
ATOM   5904  C  CG  . LYS   C  1 212 ? 41.948 -27.095 39.341  1.00 27.96 ? 212  LYS   C CG  1 
ATOM   5905  C  CD  . LYS   C  1 212 ? 40.639 -27.832 39.576  1.00 35.13 ? 212  LYS   C CD  1 
ATOM   5906  C  CE  . LYS   C  1 212 ? 40.626 -29.139 38.777  1.00 40.07 ? 212  LYS   C CE  1 
ATOM   5907  N  NZ  . LYS   C  1 212 ? 39.293 -29.781 38.866  1.00 43.73 ? 212  LYS   C NZ  1 
ATOM   5908  N  N   . GLU   C  1 213 ? 43.759 -24.164 37.927  1.00 22.94 ? 213  GLU   C N   1 
ATOM   5909  C  CA  . GLU   C  1 213 ? 44.321 -24.171 36.584  1.00 24.47 ? 213  GLU   C CA  1 
ATOM   5910  C  C   . GLU   C  1 213 ? 45.705 -23.544 36.580  1.00 23.99 ? 213  GLU   C C   1 
ATOM   5911  O  O   . GLU   C  1 213 ? 45.840 -22.388 36.990  1.00 23.54 ? 213  GLU   C O   1 
ATOM   5912  C  CB  . GLU   C  1 213 ? 43.427 -23.408 35.617  1.00 25.72 ? 213  GLU   C CB  1 
ATOM   5913  C  CG  . GLU   C  1 213 ? 43.952 -23.430 34.174  1.00 29.22 ? 213  GLU   C CG  1 
ATOM   5914  C  CD  . GLU   C  1 213 ? 43.005 -22.800 33.143  1.00 33.89 ? 213  GLU   C CD  1 
ATOM   5915  O  OE1 . GLU   C  1 213 ? 42.070 -22.049 33.501  1.00 34.09 ? 213  GLU   C OE1 1 
ATOM   5916  O  OE2 . GLU   C  1 213 ? 43.182 -23.101 31.931  1.00 40.13 ? 213  GLU   C OE2 1 
ATOM   5917  N  N   . PRO   C  1 214 ? 46.740 -24.231 36.120  1.00 23.73 ? 214  PRO   C N   1 
ATOM   5918  C  CA  . PRO   C  1 214 ? 48.058 -23.582 36.035  1.00 24.47 ? 214  PRO   C CA  1 
ATOM   5919  C  C   . PRO   C  1 214 ? 48.114 -22.642 34.852  1.00 23.54 ? 214  PRO   C C   1 
ATOM   5920  O  O   . PRO   C  1 214 ? 47.331 -22.739 33.888  1.00 27.88 ? 214  PRO   C O   1 
ATOM   5921  C  CB  . PRO   C  1 214 ? 49.029 -24.745 35.815  1.00 25.63 ? 214  PRO   C CB  1 
ATOM   5922  C  CG  . PRO   C  1 214 ? 48.170 -26.007 35.888  1.00 34.14 ? 214  PRO   C CG  1 
ATOM   5923  C  CD  . PRO   C  1 214 ? 46.780 -25.604 35.573  1.00 27.69 ? 214  PRO   C CD  1 
ATOM   5924  N  N   . ILE   C  1 215 ? 49.114 -21.726 34.918  1.00 23.56 ? 215  ILE   C N   1 
ATOM   5925  C  CA  . ILE   C  1 215 ? 49.547 -20.988 33.741  1.00 23.30 ? 215  ILE   C CA  1 
ATOM   5926  C  C   . ILE   C  1 215 ? 50.733 -21.714 33.132  1.00 25.47 ? 215  ILE   C C   1 
ATOM   5927  O  O   . ILE   C  1 215 ? 51.487 -22.423 33.824  1.00 26.01 ? 215  ILE   C O   1 
ATOM   5928  C  CB  . ILE   C  1 215 ? 49.852 -19.510 34.087  1.00 22.82 ? 215  ILE   C CB  1 
ATOM   5929  C  CG1 . ILE   C  1 215 ? 51.012 -19.397 35.109  1.00 23.56 ? 215  ILE   C CG1 1 
ATOM   5930  C  CG2 . ILE   C  1 215 ? 48.573 -18.835 34.590  1.00 24.10 ? 215  ILE   C CG2 1 
ATOM   5931  C  CD1 . ILE   C  1 215 ? 51.443 -17.917 35.470  1.00 25.15 ? 215  ILE   C CD1 1 
ATOM   5932  N  N   . SER   C  1 216 ? 50.867 -21.603 31.817  1.00 27.89 ? 216  SER   C N   1 
ATOM   5933  C  CA  A SER   C  1 216 ? 51.913 -22.270 31.062  0.48 29.04 ? 216  SER   C CA  1 
ATOM   5934  C  CA  B SER   C  1 216 ? 51.923 -22.281 31.090  0.52 28.93 ? 216  SER   C CA  1 
ATOM   5935  C  C   . SER   C  1 216 ? 53.047 -21.298 30.813  1.00 32.01 ? 216  SER   C C   1 
ATOM   5936  O  O   . SER   C  1 216 ? 52.805 -20.216 30.255  1.00 34.73 ? 216  SER   C O   1 
ATOM   5937  C  CB  A SER   C  1 216 ? 51.384 -22.757 29.712  0.48 31.55 ? 216  SER   C CB  1 
ATOM   5938  C  CB  B SER   C  1 216 ? 51.404 -22.875 29.775  0.52 31.80 ? 216  SER   C CB  1 
ATOM   5939  O  OG  A SER   C  1 216 ? 52.452 -23.060 28.837  0.48 32.07 ? 216  SER   C OG  1 
ATOM   5940  O  OG  B SER   C  1 216 ? 50.590 -24.030 30.009  0.52 30.09 ? 216  SER   C OG  1 
ATOM   5941  N  N   . VAL   C  1 217 ? 54.272 -21.700 31.167  1.00 27.74 ? 217  VAL   C N   1 
ATOM   5942  C  CA  . VAL   C  1 217 ? 55.491 -20.941 30.884  1.00 28.68 ? 217  VAL   C CA  1 
ATOM   5943  C  C   . VAL   C  1 217 ? 56.486 -21.846 30.162  1.00 28.46 ? 217  VAL   C C   1 
ATOM   5944  O  O   . VAL   C  1 217 ? 56.400 -23.078 30.239  1.00 29.47 ? 217  VAL   C O   1 
ATOM   5945  C  CB  . VAL   C  1 217 ? 56.112 -20.400 32.166  1.00 30.04 ? 217  VAL   C CB  1 
ATOM   5946  C  CG1 . VAL   C  1 217 ? 55.119 -19.470 32.853  1.00 31.25 ? 217  VAL   C CG1 1 
ATOM   5947  C  CG2 . VAL   C  1 217 ? 56.525 -21.596 33.036  1.00 27.21 ? 217  VAL   C CG2 1 
ATOM   5948  N  N   . SER   C  1 218 ? 57.443 -21.237 29.447  1.00 28.31 ? 218  SER   C N   1 
ATOM   5949  C  CA  . SER   C  1 218 ? 58.423 -22.078 28.761  1.00 29.04 ? 218  SER   C CA  1 
ATOM   5950  C  C   . SER   C  1 218 ? 59.582 -22.461 29.694  1.00 27.14 ? 218  SER   C C   1 
ATOM   5951  O  O   . SER   C  1 218 ? 59.906 -21.741 30.641  1.00 25.08 ? 218  SER   C O   1 
ATOM   5952  C  CB  . SER   C  1 218 ? 58.979 -21.384 27.520  1.00 29.76 ? 218  SER   C CB  1 
ATOM   5953  O  OG  . SER   C  1 218 ? 59.830 -20.293 27.876  1.00 28.69 ? 218  SER   C OG  1 
ATOM   5954  N  N   . SER   C  1 219 ? 60.261 -23.574 29.355  1.00 29.11 ? 219  SER   C N   1 
ATOM   5955  C  CA  . SER   C  1 219 ? 61.472 -23.949 30.092  1.00 28.49 ? 219  SER   C CA  1 
ATOM   5956  C  C   . SER   C  1 219 ? 62.500 -22.825 30.054  1.00 27.01 ? 219  SER   C C   1 
ATOM   5957  O  O   . SER   C  1 219 ? 63.142 -22.534 31.067  1.00 27.25 ? 219  SER   C O   1 
ATOM   5958  C  CB  . SER   C  1 219 ? 62.094 -25.216 29.517  1.00 33.80 ? 219  SER   C CB  1 
ATOM   5959  O  OG  . SER   C  1 219 ? 61.270 -26.336 29.761  1.00 41.45 ? 219  SER   C OG  1 
ATOM   5960  N  N   . GLU   C  1 220 ? 62.616 -22.154 28.910  1.00 29.91 ? 220  GLU   C N   1 
ATOM   5961  C  CA  . GLU   C  1 220 ? 63.556 -21.044 28.769  1.00 30.31 ? 220  GLU   C CA  1 
ATOM   5962  C  C   . GLU   C  1 220 ? 63.218 -19.926 29.728  1.00 29.48 ? 220  GLU   C C   1 
ATOM   5963  O  O   . GLU   C  1 220 ? 64.117 -19.360 30.367  1.00 28.29 ? 220  GLU   C O   1 
ATOM   5964  C  CB  . GLU   C  1 220 ? 63.536 -20.510 27.332  1.00 35.33 ? 220  GLU   C CB  1 
ATOM   5965  C  CG  . GLU   C  1 220 ? 63.972 -21.522 26.265  1.00 47.44 ? 220  GLU   C CG  1 
ATOM   5966  C  CD  . GLU   C  1 220 ? 62.815 -22.367 25.625  1.00 51.24 ? 220  GLU   C CD  1 
ATOM   5967  O  OE1 . GLU   C  1 220 ? 62.739 -22.402 24.367  1.00 54.44 ? 220  GLU   C OE1 1 
ATOM   5968  O  OE2 . GLU   C  1 220 ? 61.987 -22.985 26.339  1.00 47.06 ? 220  GLU   C OE2 1 
ATOM   5969  N  N   . GLN   C  1 221 ? 61.925 -19.615 29.887  1.00 27.13 ? 221  GLN   C N   1 
ATOM   5970  C  CA  . GLN   C  1 221 ? 61.546 -18.568 30.844  1.00 25.88 ? 221  GLN   C CA  1 
ATOM   5971  C  C   . GLN   C  1 221 ? 61.925 -18.947 32.280  1.00 25.22 ? 221  GLN   C C   1 
ATOM   5972  O  O   . GLN   C  1 221 ? 62.485 -18.130 33.019  1.00 24.18 ? 221  GLN   C O   1 
ATOM   5973  C  CB  . GLN   C  1 221 ? 60.050 -18.269 30.754  1.00 25.97 ? 221  GLN   C CB  1 
ATOM   5974  C  CG  . GLN   C  1 221 ? 59.671 -17.458 29.497  1.00 25.66 ? 221  GLN   C CG  1 
ATOM   5975  C  CD  . GLN   C  1 221 ? 58.187 -17.208 29.371  1.00 28.07 ? 221  GLN   C CD  1 
ATOM   5976  O  OE1 . GLN   C  1 221 ? 57.385 -18.114 29.606  1.00 27.11 ? 221  GLN   C OE1 1 
ATOM   5977  N  NE2 . GLN   C  1 221 ? 57.796 -15.972 29.016  1.00 26.43 ? 221  GLN   C NE2 1 
ATOM   5978  N  N   . VAL   C  1 222 ? 61.618 -20.181 32.712  1.00 22.64 ? 222  VAL   C N   1 
ATOM   5979  C  CA  . VAL   C  1 222 ? 61.966 -20.560 34.068  1.00 21.56 ? 222  VAL   C CA  1 
ATOM   5980  C  C   . VAL   C  1 222 ? 63.476 -20.566 34.261  1.00 23.47 ? 222  VAL   C C   1 
ATOM   5981  O  O   . VAL   C  1 222 ? 63.970 -20.300 35.368  1.00 22.90 ? 222  VAL   C O   1 
ATOM   5982  C  CB  . VAL   C  1 222 ? 61.377 -21.943 34.433  1.00 24.54 ? 222  VAL   C CB  1 
ATOM   5983  C  CG1 . VAL   C  1 222 ? 61.586 -22.201 35.946  1.00 24.52 ? 222  VAL   C CG1 1 
ATOM   5984  C  CG2 . VAL   C  1 222 ? 59.935 -22.003 34.110  1.00 29.46 ? 222  VAL   C CG2 1 
ATOM   5985  N  N   . SER   C  1 223 ? 64.234 -20.959 33.222  1.00 23.84 ? 223  SER   C N   1 
ATOM   5986  C  CA  . SER   C  1 223 ? 65.687 -21.002 33.380  1.00 24.95 ? 223  SER   C CA  1 
ATOM   5987  C  C   . SER   C  1 223 ? 66.238 -19.613 33.696  1.00 24.45 ? 223  SER   C C   1 
ATOM   5988  O  O   . SER   C  1 223 ? 67.284 -19.487 34.354  1.00 23.50 ? 223  SER   C O   1 
ATOM   5989  C  CB  . SER   C  1 223 ? 66.374 -21.558 32.124  1.00 28.75 ? 223  SER   C CB  1 
ATOM   5990  O  OG  . SER   C  1 223 ? 66.435 -20.566 31.109  1.00 32.86 ? 223  SER   C OG  1 
ATOM   5991  N  N   . LYS   C  1 224 ? 65.572 -18.567 33.215  1.00 22.62 ? 224  LYS   C N   1 
ATOM   5992  C  CA  . LYS   C  1 224 ? 66.009 -17.216 33.546  1.00 23.22 ? 224  LYS   C CA  1 
ATOM   5993  C  C   . LYS   C  1 224 ? 65.873 -16.923 35.033  1.00 21.35 ? 224  LYS   C C   1 
ATOM   5994  O  O   . LYS   C  1 224 ? 66.686 -16.166 35.587  1.00 21.69 ? 224  LYS   C O   1 
ATOM   5995  C  CB  . LYS   C  1 224 ? 65.205 -16.203 32.741  1.00 23.54 ? 224  LYS   C CB  1 
ATOM   5996  C  CG  . LYS   C  1 224 ? 65.391 -16.350 31.215  1.00 30.14 ? 224  LYS   C CG  1 
ATOM   5997  C  CD  . LYS   C  1 224 ? 66.831 -16.130 30.835  1.00 36.06 ? 224  LYS   C CD  1 
ATOM   5998  C  CE  . LYS   C  1 224 ? 67.057 -16.266 29.300  1.00 44.98 ? 224  LYS   C CE  1 
ATOM   5999  N  NZ  . LYS   C  1 224 ? 68.518 -16.358 28.936  1.00 50.84 ? 224  LYS   C NZ  1 
ATOM   6000  N  N   . PHE   C  1 225 ? 64.868 -17.502 35.699  1.00 19.19 ? 225  PHE   C N   1 
ATOM   6001  C  CA  . PHE   C  1 225 ? 64.781 -17.376 37.157  1.00 21.63 ? 225  PHE   C CA  1 
ATOM   6002  C  C   . PHE   C  1 225 ? 66.068 -17.880 37.830  1.00 19.96 ? 225  PHE   C C   1 
ATOM   6003  O  O   . PHE   C  1 225 ? 66.525 -17.336 38.842  1.00 20.01 ? 225  PHE   C O   1 
ATOM   6004  C  CB  . PHE   C  1 225 ? 63.612 -18.200 37.731  1.00 20.90 ? 225  PHE   C CB  1 
ATOM   6005  C  CG  . PHE   C  1 225 ? 62.215 -17.702 37.411  1.00 20.91 ? 225  PHE   C CG  1 
ATOM   6006  C  CD1 . PHE   C  1 225 ? 61.980 -16.552 36.678  1.00 24.59 ? 225  PHE   C CD1 1 
ATOM   6007  C  CD2 . PHE   C  1 225 ? 61.146 -18.464 37.830  1.00 23.30 ? 225  PHE   C CD2 1 
ATOM   6008  C  CE1 . PHE   C  1 225 ? 60.688 -16.152 36.364  1.00 25.02 ? 225  PHE   C CE1 1 
ATOM   6009  C  CE2 . PHE   C  1 225 ? 59.814 -18.069 37.559  1.00 27.32 ? 225  PHE   C CE2 1 
ATOM   6010  C  CZ  . PHE   C  1 225 ? 59.594 -16.883 36.822  1.00 24.23 ? 225  PHE   C CZ  1 
ATOM   6011  N  N   . ARG   C  1 226 ? 66.626 -18.961 37.302  1.00 19.85 ? 226  ARG   C N   1 
ATOM   6012  C  CA  . ARG   C  1 226 ? 67.728 -19.645 37.958  1.00 19.84 ? 226  ARG   C CA  1 
ATOM   6013  C  C   . ARG   C  1 226 ? 69.036 -18.924 37.779  1.00 21.25 ? 226  ARG   C C   1 
ATOM   6014  O  O   . ARG   C  1 226 ? 70.028 -19.312 38.422  1.00 23.22 ? 226  ARG   C O   1 
ATOM   6015  C  CB  . ARG   C  1 226 ? 67.850 -21.078 37.433  1.00 20.26 ? 226  ARG   C CB  1 
ATOM   6016  C  CG  . ARG   C  1 226 ? 66.535 -21.888 37.539  1.00 21.44 ? 226  ARG   C CG  1 
ATOM   6017  C  CD  . ARG   C  1 226 ? 66.844 -23.379 37.280  1.00 21.67 ? 226  ARG   C CD  1 
ATOM   6018  N  NE  . ARG   C  1 226 ? 65.581 -24.140 37.252  1.00 22.67 ? 226  ARG   C NE  1 
ATOM   6019  C  CZ  . ARG   C  1 226 ? 64.925 -24.508 36.152  1.00 22.75 ? 226  ARG   C CZ  1 
ATOM   6020  N  NH1 . ARG   C  1 226 ? 65.426 -24.271 34.916  1.00 24.82 ? 226  ARG   C NH1 1 
ATOM   6021  N  NH2 . ARG   C  1 226 ? 63.752 -25.100 36.249  1.00 23.95 ? 226  ARG   C NH2 1 
ATOM   6022  N  N   . LYS   C  1 227 ? 69.064 -17.848 36.968  1.00 20.76 ? 227  LYS   C N   1 
ATOM   6023  C  CA  . LYS   C  1 227 ? 70.277 -17.056 36.848  1.00 21.82 ? 227  LYS   C CA  1 
ATOM   6024  C  C   . LYS   C  1 227 ? 70.388 -15.984 37.921  1.00 20.85 ? 227  LYS   C C   1 
ATOM   6025  O  O   . LYS   C  1 227 ? 71.442 -15.326 38.021  1.00 22.92 ? 227  LYS   C O   1 
ATOM   6026  C  CB  . LYS   C  1 227 ? 70.342 -16.397 35.475  1.00 24.24 ? 227  LYS   C CB  1 
ATOM   6027  C  CG  . LYS   C  1 227 ? 70.409 -17.411 34.332  1.00 27.05 ? 227  LYS   C CG  1 
ATOM   6028  C  CD  . LYS   C  1 227 ? 70.340 -16.642 33.024  1.00 37.19 ? 227  LYS   C CD  1 
ATOM   6029  C  CE  . LYS   C  1 227 ? 71.608 -15.825 32.819  1.00 44.06 ? 227  LYS   C CE  1 
ATOM   6030  N  NZ  . LYS   C  1 227 ? 71.599 -15.059 31.526  1.00 48.84 ? 227  LYS   C NZ  1 
ATOM   6031  N  N   . LEU   C  1 228 ? 69.322 -15.759 38.686  1.00 19.44 ? 228  LEU   C N   1 
ATOM   6032  C  CA  . LEU   C  1 228 ? 69.475 -14.952 39.881  1.00 18.95 ? 228  LEU   C CA  1 
ATOM   6033  C  C   . LEU   C  1 228 ? 70.342 -15.671 40.907  1.00 19.41 ? 228  LEU   C C   1 
ATOM   6034  O  O   . LEU   C  1 228 ? 70.526 -16.902 40.853  1.00 19.31 ? 228  LEU   C O   1 
ATOM   6035  C  CB  . LEU   C  1 228 ? 68.099 -14.693 40.500  1.00 19.13 ? 228  LEU   C CB  1 
ATOM   6036  C  CG  . LEU   C  1 228 ? 67.204 -13.891 39.554  1.00 19.84 ? 228  LEU   C CG  1 
ATOM   6037  C  CD1 . LEU   C  1 228 ? 65.753 -14.010 40.040  1.00 21.11 ? 228  LEU   C CD1 1 
ATOM   6038  C  CD2 . LEU   C  1 228 ? 67.626 -12.469 39.592  1.00 22.20 ? 228  LEU   C CD2 1 
ATOM   6039  N  N   . ASN   C  1 229 ? 70.833 -14.882 41.885  1.00 19.08 ? 229  ASN   C N   1 
ATOM   6040  C  CA  . ASN   C  1 229 ? 71.695 -15.359 42.960  1.00 19.44 ? 229  ASN   C CA  1 
ATOM   6041  C  C   . ASN   C  1 229 ? 71.098 -14.988 44.319  1.00 19.60 ? 229  ASN   C C   1 
ATOM   6042  O  O   . ASN   C  1 229 ? 70.547 -13.885 44.489  1.00 18.73 ? 229  ASN   C O   1 
ATOM   6043  C  CB  . ASN   C  1 229 ? 73.136 -14.752 42.849  1.00 22.49 ? 229  ASN   C CB  1 
ATOM   6044  C  CG  . ASN   C  1 229 ? 73.970 -15.384 41.741  1.00 27.56 ? 229  ASN   C CG  1 
ATOM   6045  O  OD1 . ASN   C  1 229 ? 73.566 -16.342 41.108  1.00 28.14 ? 229  ASN   C OD1 1 
ATOM   6046  N  ND2 . ASN   C  1 229 ? 75.171 -14.857 41.540  1.00 33.11 ? 229  ASN   C ND2 1 
ATOM   6047  N  N   . PHE   C  1 230 ? 71.246 -15.910 45.286  1.00 18.49 ? 230  PHE   C N   1 
ATOM   6048  C  CA  . PHE   C  1 230 ? 70.866 -15.594 46.669  1.00 18.55 ? 230  PHE   C CA  1 
ATOM   6049  C  C   . PHE   C  1 230 ? 71.823 -14.616 47.306  1.00 20.73 ? 230  PHE   C C   1 
ATOM   6050  O  O   . PHE   C  1 230 ? 71.417 -13.837 48.167  1.00 21.76 ? 230  PHE   C O   1 
ATOM   6051  C  CB  . PHE   C  1 230 ? 70.883 -16.838 47.554  1.00 19.05 ? 230  PHE   C CB  1 
ATOM   6052  C  CG  . PHE   C  1 230 ? 69.809 -17.833 47.287  1.00 18.07 ? 230  PHE   C CG  1 
ATOM   6053  C  CD1 . PHE   C  1 230 ? 68.435 -17.518 47.435  1.00 16.85 ? 230  PHE   C CD1 1 
ATOM   6054  C  CD2 . PHE   C  1 230 ? 70.167 -19.142 47.016  1.00 19.32 ? 230  PHE   C CD2 1 
ATOM   6055  C  CE1 . PHE   C  1 230 ? 67.439 -18.523 47.286  1.00 17.58 ? 230  PHE   C CE1 1 
ATOM   6056  C  CE2 . PHE   C  1 230 ? 69.184 -20.142 46.882  1.00 17.95 ? 230  PHE   C CE2 1 
ATOM   6057  C  CZ  . PHE   C  1 230 ? 67.840 -19.848 47.020  1.00 17.67 ? 230  PHE   C CZ  1 
ATOM   6058  N  N   . ASN   C  1 231 ? 73.107 -14.705 46.963  1.00 20.10 ? 231  ASN   C N   1 
ATOM   6059  C  CA  . ASN   C  1 231 ? 74.154 -13.960 47.647  1.00 21.31 ? 231  ASN   C CA  1 
ATOM   6060  C  C   . ASN   C  1 231 ? 74.202 -12.487 47.221  1.00 23.23 ? 231  ASN   C C   1 
ATOM   6061  O  O   . ASN   C  1 231 ? 73.645 -12.078 46.200  1.00 22.71 ? 231  ASN   C O   1 
ATOM   6062  C  CB  . ASN   C  1 231 ? 75.504 -14.601 47.361  1.00 23.36 ? 231  ASN   C CB  1 
ATOM   6063  C  CG  . ASN   C  1 231 ? 75.778 -14.684 45.856  1.00 23.06 ? 231  ASN   C CG  1 
ATOM   6064  O  OD1 . ASN   C  1 231 ? 75.233 -15.524 45.191  1.00 22.44 ? 231  ASN   C OD1 1 
ATOM   6065  N  ND2 . ASN   C  1 231 ? 76.632 -13.795 45.337  1.00 26.10 ? 231  ASN   C ND2 1 
ATOM   6066  N  N   . GLY   C  1 232 ? 74.873 -11.686 48.063  1.00 25.27 ? 232  GLY   C N   1 
ATOM   6067  C  CA  . GLY   C  1 232 ? 75.247 -10.345 47.676  1.00 27.47 ? 232  GLY   C CA  1 
ATOM   6068  C  C   . GLY   C  1 232 ? 76.507 -10.327 46.851  1.00 27.56 ? 232  GLY   C C   1 
ATOM   6069  O  O   . GLY   C  1 232 ? 77.294 -11.279 46.822  1.00 28.85 ? 232  GLY   C O   1 
ATOM   6070  N  N   . GLU   C  1 233 ? 76.720 -9.209  46.172  1.00 29.81 ? 233  GLU   C N   1 
ATOM   6071  C  CA  . GLU   C  1 233 ? 77.955 -9.033  45.407  1.00 37.29 ? 233  GLU   C CA  1 
ATOM   6072  C  C   . GLU   C  1 233 ? 79.183 -9.181  46.309  1.00 34.76 ? 233  GLU   C C   1 
ATOM   6073  O  O   . GLU   C  1 233 ? 79.212 -8.674  47.432  1.00 36.76 ? 233  GLU   C O   1 
ATOM   6074  C  CB  . GLU   C  1 233 ? 77.941 -7.664  44.720  1.00 45.75 ? 233  GLU   C CB  1 
ATOM   6075  C  CG  . GLU   C  1 233 ? 78.860 -7.590  43.519  1.00 55.77 ? 233  GLU   C CG  1 
ATOM   6076  C  CD  . GLU   C  1 233 ? 78.744 -6.274  42.741  1.00 66.66 ? 233  GLU   C CD  1 
ATOM   6077  O  OE1 . GLU   C  1 233 ? 77.677 -5.612  42.810  1.00 67.75 ? 233  GLU   C OE1 1 
ATOM   6078  O  OE2 . GLU   C  1 233 ? 79.746 -5.884  42.083  1.00 72.20 ? 233  GLU   C OE2 1 
ATOM   6079  N  N   . GLY   C  1 234 ? 80.201 -9.925  45.844  1.00 35.42 ? 234  GLY   C N   1 
ATOM   6080  C  CA  . GLY   C  1 234 ? 81.409 -10.136 46.633  1.00 36.91 ? 234  GLY   C CA  1 
ATOM   6081  C  C   . GLY   C  1 234 ? 81.387 -11.316 47.585  1.00 36.60 ? 234  GLY   C C   1 
ATOM   6082  O  O   . GLY   C  1 234 ? 82.399 -11.581 48.259  1.00 38.56 ? 234  GLY   C O   1 
ATOM   6083  N  N   . GLU   C  1 235 ? 80.293 -12.053 47.627  1.00 35.10 ? 235  GLU   C N   1 
ATOM   6084  C  CA  . GLU   C  1 235 ? 80.176 -13.288 48.375  1.00 33.09 ? 235  GLU   C CA  1 
ATOM   6085  C  C   . GLU   C  1 235 ? 80.172 -14.468 47.428  1.00 35.55 ? 235  GLU   C C   1 
ATOM   6086  O  O   . GLU   C  1 235 ? 79.892 -14.305 46.235  1.00 32.93 ? 235  GLU   C O   1 
ATOM   6087  C  CB  . GLU   C  1 235 ? 78.889 -13.267 49.184  1.00 34.41 ? 235  GLU   C CB  1 
ATOM   6088  C  CG  . GLU   C  1 235 ? 78.747 -12.005 50.009  1.00 36.40 ? 235  GLU   C CG  1 
ATOM   6089  C  CD  . GLU   C  1 235 ? 77.455 -12.032 50.822  1.00 39.87 ? 235  GLU   C CD  1 
ATOM   6090  O  OE1 . GLU   C  1 235 ? 76.427 -12.506 50.289  1.00 35.24 ? 235  GLU   C OE1 1 
ATOM   6091  O  OE2 . GLU   C  1 235 ? 77.480 -11.609 52.006  1.00 42.94 ? 235  GLU   C OE2 1 
ATOM   6092  N  N   . PRO   C  1 236 ? 80.490 -15.681 47.909  1.00 35.63 ? 236  PRO   C N   1 
ATOM   6093  C  CA  . PRO   C  1 236 ? 80.531 -16.829 46.991  1.00 35.72 ? 236  PRO   C CA  1 
ATOM   6094  C  C   . PRO   C  1 236 ? 79.183 -17.013 46.320  1.00 30.28 ? 236  PRO   C C   1 
ATOM   6095  O  O   . PRO   C  1 236 ? 78.137 -16.814 46.935  1.00 29.98 ? 236  PRO   C O   1 
ATOM   6096  C  CB  . PRO   C  1 236 ? 80.904 -18.009 47.896  1.00 39.62 ? 236  PRO   C CB  1 
ATOM   6097  C  CG  . PRO   C  1 236 ? 81.723 -17.348 49.028  1.00 41.14 ? 236  PRO   C CG  1 
ATOM   6098  C  CD  . PRO   C  1 236 ? 80.998 -16.019 49.256  1.00 38.50 ? 236  PRO   C CD  1 
ATOM   6099  N  N   . GLU   C  1 237 ? 79.232 -17.349 45.036  1.00 34.39 ? 237  GLU   C N   1 
ATOM   6100  C  CA  . GLU   C  1 237 ? 78.016 -17.395 44.236  1.00 35.64 ? 237  GLU   C CA  1 
ATOM   6101  C  C   . GLU   C  1 237 ? 77.121 -18.533 44.693  1.00 32.15 ? 237  GLU   C C   1 
ATOM   6102  O  O   . GLU   C  1 237 ? 77.567 -19.676 44.824  1.00 33.44 ? 237  GLU   C O   1 
ATOM   6103  C  CB  . GLU   C  1 237 ? 78.342 -17.566 42.753  1.00 42.80 ? 237  GLU   C CB  1 
ATOM   6104  C  CG  . GLU   C  1 237 ? 77.118 -17.940 41.939  1.00 49.91 ? 237  GLU   C CG  1 
ATOM   6105  C  CD  . GLU   C  1 237 ? 77.250 -17.614 40.455  1.00 59.36 ? 237  GLU   C CD  1 
ATOM   6106  O  OE1 . GLU   C  1 237 ? 77.531 -16.438 40.110  1.00 61.34 ? 237  GLU   C OE1 1 
ATOM   6107  O  OE2 . GLU   C  1 237 ? 77.068 -18.545 39.633  1.00 62.65 ? 237  GLU   C OE2 1 
ATOM   6108  N  N   . GLU   C  1 238 ? 75.856 -18.218 44.939  1.00 27.46 ? 238  GLU   C N   1 
ATOM   6109  C  CA  . GLU   C  1 238 ? 74.849 -19.218 45.288  1.00 25.18 ? 238  GLU   C CA  1 
ATOM   6110  C  C   . GLU   C  1 238 ? 73.664 -19.010 44.362  1.00 24.24 ? 238  GLU   C C   1 
ATOM   6111  O  O   . GLU   C  1 238 ? 72.832 -18.127 44.620  1.00 24.35 ? 238  GLU   C O   1 
ATOM   6112  C  CB  . GLU   C  1 238 ? 74.383 -19.112 46.731  1.00 25.79 ? 238  GLU   C CB  1 
ATOM   6113  C  CG  . GLU   C  1 238 ? 75.530 -19.139 47.743  1.00 35.12 ? 238  GLU   C CG  1 
ATOM   6114  C  CD  . GLU   C  1 238 ? 75.074 -18.678 49.128  1.00 45.38 ? 238  GLU   C CD  1 
ATOM   6115  O  OE1 . GLU   C  1 238 ? 75.912 -18.645 50.064  1.00 49.50 ? 238  GLU   C OE1 1 
ATOM   6116  O  OE2 . GLU   C  1 238 ? 73.881 -18.337 49.281  1.00 46.89 ? 238  GLU   C OE2 1 
ATOM   6117  N  N   . PRO   C  1 239 ? 73.515 -19.834 43.338  1.00 23.85 ? 239  PRO   C N   1 
ATOM   6118  C  CA  . PRO   C  1 239 ? 72.372 -19.683 42.428  1.00 23.14 ? 239  PRO   C CA  1 
ATOM   6119  C  C   . PRO   C  1 239 ? 71.050 -19.727 43.171  1.00 19.81 ? 239  PRO   C C   1 
ATOM   6120  O  O   . PRO   C  1 239 ? 70.841 -20.550 44.066  1.00 20.72 ? 239  PRO   C O   1 
ATOM   6121  C  CB  . PRO   C  1 239 ? 72.522 -20.864 41.464  1.00 26.35 ? 239  PRO   C CB  1 
ATOM   6122  C  CG  . PRO   C  1 239 ? 74.024 -21.160 41.474  1.00 30.18 ? 239  PRO   C CG  1 
ATOM   6123  C  CD  . PRO   C  1 239 ? 74.473 -20.868 42.879  1.00 27.90 ? 239  PRO   C CD  1 
ATOM   6124  N  N   . MET   C  1 240 ? 70.147 -18.823 42.770  1.00 19.12 ? 240  MET   C N   1 
ATOM   6125  C  CA  . MET   C  1 240 ? 68.835 -18.747 43.415  1.00 17.60 ? 240  MET   C CA  1 
ATOM   6126  C  C   . MET   C  1 240 ? 67.954 -19.830 42.788  1.00 19.77 ? 240  MET   C C   1 
ATOM   6127  O  O   . MET   C  1 240 ? 67.291 -19.599 41.768  1.00 17.85 ? 240  MET   C O   1 
ATOM   6128  C  CB  . MET   C  1 240 ? 68.211 -17.367 43.212  1.00 17.90 ? 240  MET   C CB  1 
ATOM   6129  C  CG  . MET   C  1 240 ? 66.886 -17.215 44.020  1.00 17.72 ? 240  MET   C CG  1 
ATOM   6130  S  SD  . MET   C  1 240 ? 66.165 -15.581 43.781  1.00 17.69 ? 240  MET   C SD  1 
ATOM   6131  C  CE  . MET   C  1 240 ? 67.136 -14.637 44.948  1.00 18.55 ? 240  MET   C CE  1 
ATOM   6132  N  N   . VAL   C  1 241 ? 67.936 -21.004 43.420  1.00 18.69 ? 241  VAL   C N   1 
ATOM   6133  C  CA  . VAL   C  1 241 ? 67.151 -22.151 42.957  1.00 17.61 ? 241  VAL   C CA  1 
ATOM   6134  C  C   . VAL   C  1 241 ? 66.616 -22.865 44.203  1.00 18.22 ? 241  VAL   C C   1 
ATOM   6135  O  O   . VAL   C  1 241 ? 67.204 -22.770 45.285  1.00 19.18 ? 241  VAL   C O   1 
ATOM   6136  C  CB  . VAL   C  1 241 ? 67.969 -23.132 42.088  1.00 19.45 ? 241  VAL   C CB  1 
ATOM   6137  C  CG1 . VAL   C  1 241 ? 68.435 -22.447 40.770  1.00 19.49 ? 241  VAL   C CG1 1 
ATOM   6138  C  CG2 . VAL   C  1 241 ? 69.165 -23.737 42.858  1.00 20.45 ? 241  VAL   C CG2 1 
ATOM   6139  N  N   . ASP   C  1 242 ? 65.506 -23.618 44.044  1.00 16.74 ? 242  ASP   C N   1 
ATOM   6140  C  CA  . ASP   C  1 242 ? 64.954 -24.409 45.173  1.00 17.01 ? 242  ASP   C CA  1 
ATOM   6141  C  C   . ASP   C  1 242 ? 64.659 -23.505 46.376  1.00 16.90 ? 242  ASP   C C   1 
ATOM   6142  O  O   . ASP   C  1 242 ? 64.949 -23.828 47.545  1.00 18.18 ? 242  ASP   C O   1 
ATOM   6143  C  CB  . ASP   C  1 242 ? 65.878 -25.578 45.525  1.00 19.48 ? 242  ASP   C CB  1 
ATOM   6144  C  CG  . ASP   C  1 242 ? 65.881 -26.643 44.426  1.00 20.83 ? 242  ASP   C CG  1 
ATOM   6145  O  OD1 . ASP   C  1 242 ? 64.810 -26.893 43.809  1.00 19.25 ? 242  ASP   C OD1 1 
ATOM   6146  O  OD2 . ASP   C  1 242 ? 66.967 -27.224 44.222  1.00 22.72 ? 242  ASP   C OD2 1 
ATOM   6147  N  N   . ASN   C  1 243 ? 64.025 -22.376 46.075  1.00 15.69 ? 243  ASN   C N   1 
ATOM   6148  C  CA  . ASN   C  1 243 ? 63.541 -21.448 47.104  1.00 15.72 ? 243  ASN   C CA  1 
ATOM   6149  C  C   . ASN   C  1 243 ? 62.075 -21.738 47.436  1.00 16.60 ? 243  ASN   C C   1 
ATOM   6150  O  O   . ASN   C  1 243 ? 61.229 -20.841 47.458  1.00 16.75 ? 243  ASN   C O   1 
ATOM   6151  C  CB  . ASN   C  1 243 ? 63.759 -19.982 46.694  1.00 15.26 ? 243  ASN   C CB  1 
ATOM   6152  C  CG  . ASN   C  1 243 ? 63.170 -19.623 45.328  1.00 15.80 ? 243  ASN   C CG  1 
ATOM   6153  O  OD1 . ASN   C  1 243 ? 62.595 -20.476 44.654  1.00 17.97 ? 243  ASN   C OD1 1 
ATOM   6154  N  ND2 . ASN   C  1 243 ? 63.277 -18.314 44.955  1.00 17.31 ? 243  ASN   C ND2 1 
ATOM   6155  N  N   . TRP   C  1 244 ? 61.822 -23.013 47.734  1.00 15.98 ? 244  TRP   C N   1 
ATOM   6156  C  CA  . TRP   C  1 244 ? 60.504 -23.490 48.130  1.00 15.75 ? 244  TRP   C CA  1 
ATOM   6157  C  C   . TRP   C  1 244 ? 60.606 -24.204 49.462  1.00 16.85 ? 244  TRP   C C   1 
ATOM   6158  O  O   . TRP   C  1 244 ? 61.633 -24.809 49.806  1.00 17.78 ? 244  TRP   C O   1 
ATOM   6159  C  CB  . TRP   C  1 244 ? 59.907 -24.443 47.061  1.00 18.04 ? 244  TRP   C CB  1 
ATOM   6160  C  CG  . TRP   C  1 244 ? 60.844 -25.561 46.612  1.00 19.82 ? 244  TRP   C CG  1 
ATOM   6161  C  CD1 . TRP   C  1 244 ? 61.701 -25.493 45.546  1.00 19.41 ? 244  TRP   C CD1 1 
ATOM   6162  C  CD2 . TRP   C  1 244 ? 61.018 -26.884 47.194  1.00 21.49 ? 244  TRP   C CD2 1 
ATOM   6163  N  NE1 . TRP   C  1 244 ? 62.369 -26.696 45.414  1.00 18.17 ? 244  TRP   C NE1 1 
ATOM   6164  C  CE2 . TRP   C  1 244 ? 62.005 -27.554 46.435  1.00 22.09 ? 244  TRP   C CE2 1 
ATOM   6165  C  CE3 . TRP   C  1 244 ? 60.471 -27.545 48.312  1.00 22.09 ? 244  TRP   C CE3 1 
ATOM   6166  C  CZ2 . TRP   C  1 244 ? 62.461 -28.862 46.733  1.00 26.62 ? 244  TRP   C CZ2 1 
ATOM   6167  C  CZ3 . TRP   C  1 244 ? 60.917 -28.843 48.623  1.00 25.14 ? 244  TRP   C CZ3 1 
ATOM   6168  C  CH2 . TRP   C  1 244 ? 61.886 -29.509 47.817  1.00 25.47 ? 244  TRP   C CH2 1 
ATOM   6169  N  N   . ARG   C  1 245 ? 59.505 -24.123 50.211  1.00 15.87 ? 245  ARG   C N   1 
ATOM   6170  C  CA  . ARG   C  1 245 ? 59.350 -24.885 51.475  1.00 15.76 ? 245  ARG   C CA  1 
ATOM   6171  C  C   . ARG   C  1 245 ? 58.647 -26.219 51.194  1.00 17.48 ? 245  ARG   C C   1 
ATOM   6172  O  O   . ARG   C  1 245 ? 57.686 -26.216 50.436  1.00 18.49 ? 245  ARG   C O   1 
ATOM   6173  C  CB  . ARG   C  1 245 ? 58.511 -24.066 52.453  1.00 15.01 ? 245  ARG   C CB  1 
ATOM   6174  C  CG  . ARG   C  1 245 ? 58.528 -24.723 53.842  1.00 14.15 ? 245  ARG   C CG  1 
ATOM   6175  C  CD  . ARG   C  1 245 ? 57.566 -24.033 54.817  1.00 16.01 ? 245  ARG   C CD  1 
ATOM   6176  N  NE  . ARG   C  1 245 ? 57.822 -24.568 56.161  1.00 15.04 ? 245  ARG   C NE  1 
ATOM   6177  C  CZ  . ARG   C  1 245 ? 57.024 -24.393 57.212  1.00 13.54 ? 245  ARG   C CZ  1 
ATOM   6178  N  NH1 . ARG   C  1 245 ? 55.825 -23.758 57.109  1.00 14.05 ? 245  ARG   C NH1 1 
ATOM   6179  N  NH2 . ARG   C  1 245 ? 57.434 -24.870 58.431  1.00 14.21 ? 245  ARG   C NH2 1 
ATOM   6180  N  N   . PRO   C  1 246 ? 59.111 -27.347 51.792  1.00 18.01 ? 246  PRO   C N   1 
ATOM   6181  C  CA  . PRO   C  1 246 ? 58.373 -28.644 51.679  1.00 17.31 ? 246  PRO   C CA  1 
ATOM   6182  C  C   . PRO   C  1 246 ? 56.951 -28.501 52.208  1.00 18.01 ? 246  PRO   C C   1 
ATOM   6183  O  O   . PRO   C  1 246 ? 56.669 -27.651 53.069  1.00 17.61 ? 246  PRO   C O   1 
ATOM   6184  C  CB  . PRO   C  1 246 ? 59.178 -29.628 52.559  1.00 21.70 ? 246  PRO   C CB  1 
ATOM   6185  C  CG  . PRO   C  1 246 ? 60.586 -29.045 52.628  1.00 19.73 ? 246  PRO   C CG  1 
ATOM   6186  C  CD  . PRO   C  1 246 ? 60.359 -27.491 52.572  1.00 20.05 ? 246  PRO   C CD  1 
ATOM   6187  N  N   . THR   C  1 247 ? 56.046 -29.325 51.685  1.00 18.78 ? 247  THR   C N   1 
ATOM   6188  C  CA  . THR   C  1 247 ? 54.691 -29.293 52.231  1.00 17.74 ? 247  THR   C CA  1 
ATOM   6189  C  C   . THR   C  1 247 ? 54.665 -29.780 53.681  1.00 17.06 ? 247  THR   C C   1 
ATOM   6190  O  O   . THR   C  1 247 ? 55.475 -30.612 54.125  1.00 19.09 ? 247  THR   C O   1 
ATOM   6191  C  CB  . THR   C  1 247 ? 53.721 -30.146 51.413  1.00 18.87 ? 247  THR   C CB  1 
ATOM   6192  O  OG1 . THR   C  1 247 ? 54.248 -31.472 51.248  1.00 19.97 ? 247  THR   C OG1 1 
ATOM   6193  C  CG2 . THR   C  1 247 ? 53.523 -29.542 50.031  1.00 19.12 ? 247  THR   C CG2 1 
ATOM   6194  N  N   . GLN   C  1 248 ? 53.741 -29.200 54.437  1.00 16.40 ? 248  GLN   C N   1 
ATOM   6195  C  CA  . GLN   C  1 248 ? 53.608 -29.385 55.876  1.00 14.83 ? 248  GLN   C CA  1 
ATOM   6196  C  C   . GLN   C  1 248 ? 52.305 -30.090 56.225  1.00 15.56 ? 248  GLN   C C   1 
ATOM   6197  O  O   . GLN   C  1 248 ? 51.379 -30.152 55.410  1.00 17.80 ? 248  GLN   C O   1 
ATOM   6198  C  CB  . GLN   C  1 248 ? 53.665 -28.019 56.590  1.00 15.56 ? 248  GLN   C CB  1 
ATOM   6199  C  CG  . GLN   C  1 248 ? 54.956 -27.223 56.301  1.00 15.89 ? 248  GLN   C CG  1 
ATOM   6200  C  CD  . GLN   C  1 248 ? 56.174 -27.982 56.795  1.00 14.81 ? 248  GLN   C CD  1 
ATOM   6201  O  OE1 . GLN   C  1 248 ? 56.218 -28.475 57.937  1.00 17.22 ? 248  GLN   C OE1 1 
ATOM   6202  N  NE2 . GLN   C  1 248 ? 57.126 -28.139 55.899  1.00 16.29 ? 248  GLN   C NE2 1 
ATOM   6203  N  N   . PRO   C  1 249 ? 52.222 -30.697 57.411  1.00 16.40 ? 249  PRO   C N   1 
ATOM   6204  C  CA  . PRO   C  1 249 ? 51.035 -31.480 57.768  1.00 18.57 ? 249  PRO   C CA  1 
ATOM   6205  C  C   . PRO   C  1 249 ? 49.797 -30.596 57.802  1.00 17.79 ? 249  PRO   C C   1 
ATOM   6206  O  O   . PRO   C  1 249 ? 49.818 -29.501 58.358  1.00 18.10 ? 249  PRO   C O   1 
ATOM   6207  C  CB  . PRO   C  1 249 ? 51.359 -31.993 59.178  1.00 19.63 ? 249  PRO   C CB  1 
ATOM   6208  C  CG  . PRO   C  1 249 ? 52.885 -32.014 59.225  1.00 19.94 ? 249  PRO   C CG  1 
ATOM   6209  C  CD  . PRO   C  1 249 ? 53.289 -30.775 58.435  1.00 19.03 ? 249  PRO   C CD  1 
ATOM   6210  N  N   . LEU   C  1 250 ? 48.709 -31.097 57.228  1.00 18.11 ? 250  LEU   C N   1 
ATOM   6211  C  CA  . LEU   C  1 250 ? 47.439 -30.372 57.277  1.00 19.44 ? 250  LEU   C CA  1 
ATOM   6212  C  C   . LEU   C  1 250 ? 46.892 -30.289 58.707  1.00 19.31 ? 250  LEU   C C   1 
ATOM   6213  O  O   . LEU   C  1 250 ? 46.191 -29.323 59.039  1.00 20.19 ? 250  LEU   C O   1 
ATOM   6214  C  CB  . LEU   C  1 250 ? 46.428 -31.071 56.341  1.00 22.85 ? 250  LEU   C CB  1 
ATOM   6215  C  CG  . LEU   C  1 250 ? 45.145 -30.318 55.990  1.00 24.55 ? 250  LEU   C CG  1 
ATOM   6216  C  CD1 . LEU   C  1 250 ? 45.427 -28.916 55.447  1.00 22.28 ? 250  LEU   C CD1 1 
ATOM   6217  C  CD2 . LEU   C  1 250 ? 44.313 -31.155 54.982  1.00 26.70 ? 250  LEU   C CD2 1 
ATOM   6218  N  N   . LYS   C  1 251 ? 47.164 -31.286 59.578  1.00 18.59 ? 251  LYS   C N   1 
ATOM   6219  C  CA  . LYS   C  1 251 ? 46.652 -31.276 60.938  1.00 19.76 ? 251  LYS   C CA  1 
ATOM   6220  C  C   . LYS   C  1 251 ? 45.140 -31.105 60.914  1.00 23.44 ? 251  LYS   C C   1 
ATOM   6221  O  O   . LYS   C  1 251 ? 44.474 -31.754 60.103  1.00 24.54 ? 251  LYS   C O   1 
ATOM   6222  C  CB  . LYS   C  1 251 ? 47.392 -30.248 61.797  1.00 21.60 ? 251  LYS   C CB  1 
ATOM   6223  C  CG  . LYS   C  1 251 ? 48.927 -30.576 61.802  1.00 25.61 ? 251  LYS   C CG  1 
ATOM   6224  C  CD  . LYS   C  1 251 ? 49.725 -29.828 62.861  1.00 26.63 ? 251  LYS   C CD  1 
ATOM   6225  C  CE  . LYS   C  1 251 ? 51.206 -30.219 62.797  1.00 30.02 ? 251  LYS   C CE  1 
ATOM   6226  N  NZ  . LYS   C  1 251 ? 52.030 -29.527 63.828  1.00 32.01 ? 251  LYS   C NZ  1 
ATOM   6227  N  N   . ASN   C  1 252 ? 44.578 -30.287 61.797  1.00 20.87 ? 252  ASN   C N   1 
ATOM   6228  C  CA  . ASN   C  1 252 ? 43.137 -30.246 61.982  1.00 24.22 ? 252  ASN   C CA  1 
ATOM   6229  C  C   . ASN   C  1 252 ? 42.575 -29.108 61.145  1.00 29.00 ? 252  ASN   C C   1 
ATOM   6230  O  O   . ASN   C  1 252 ? 42.051 -28.113 61.681  1.00 31.46 ? 252  ASN   C O   1 
ATOM   6231  C  CB  . ASN   C  1 252 ? 42.806 -30.083 63.463  1.00 29.57 ? 252  ASN   C CB  1 
ATOM   6232  C  CG  . ASN   C  1 252 ? 41.373 -30.311 63.734  1.00 36.45 ? 252  ASN   C CG  1 
ATOM   6233  O  OD1 . ASN   C  1 252 ? 40.630 -30.744 62.842  1.00 34.95 ? 252  ASN   C OD1 1 
ATOM   6234  N  ND2 . ASN   C  1 252 ? 40.939 -29.993 64.950  1.00 40.91 ? 252  ASN   C ND2 1 
ATOM   6235  N  N   . ARG   C  1 253 ? 42.750 -29.252 59.819  1.00 23.10 ? 253  ARG   C N   1 
ATOM   6236  C  CA  . ARG   C  1 253 ? 42.268 -28.287 58.836  1.00 22.01 ? 253  ARG   C CA  1 
ATOM   6237  C  C   . ARG   C  1 253 ? 41.576 -29.022 57.691  1.00 23.95 ? 253  ARG   C C   1 
ATOM   6238  O  O   . ARG   C  1 253 ? 41.792 -30.226 57.502  1.00 26.01 ? 253  ARG   C O   1 
ATOM   6239  C  CB  . ARG   C  1 253 ? 43.410 -27.406 58.255  1.00 19.18 ? 253  ARG   C CB  1 
ATOM   6240  C  CG  . ARG   C  1 253 ? 43.968 -26.489 59.314  1.00 20.00 ? 253  ARG   C CG  1 
ATOM   6241  C  CD  . ARG   C  1 253 ? 45.116 -25.668 58.748  1.00 19.44 ? 253  ARG   C CD  1 
ATOM   6242  N  NE  . ARG   C  1 253 ? 46.281 -26.518 58.481  1.00 18.13 ? 253  ARG   C NE  1 
ATOM   6243  C  CZ  . ARG   C  1 253 ? 47.391 -26.103 57.885  1.00 17.04 ? 253  ARG   C CZ  1 
ATOM   6244  N  NH1 . ARG   C  1 253 ? 47.501 -24.850 57.412  1.00 17.85 ? 253  ARG   C NH1 1 
ATOM   6245  N  NH2 . ARG   C  1 253 ? 48.424 -26.945 57.757  1.00 16.40 ? 253  ARG   C NH2 1 
ATOM   6246  N  N   . GLN   C  1 254 ? 40.726 -28.281 56.962  1.00 22.90 ? 254  GLN   C N   1 
ATOM   6247  C  CA  . GLN   C  1 254 ? 39.969 -28.780 55.812  1.00 26.99 ? 254  GLN   C CA  1 
ATOM   6248  C  C   . GLN   C  1 254 ? 40.269 -27.876 54.638  1.00 27.45 ? 254  GLN   C C   1 
ATOM   6249  O  O   . GLN   C  1 254 ? 40.245 -26.645 54.779  1.00 29.81 ? 254  GLN   C O   1 
ATOM   6250  C  CB  . GLN   C  1 254 ? 38.453 -28.806 56.095  1.00 32.14 ? 254  GLN   C CB  1 
ATOM   6251  C  CG  . GLN   C  1 254 ? 38.123 -29.541 57.357  1.00 41.55 ? 254  GLN   C CG  1 
ATOM   6252  C  CD  . GLN   C  1 254 ? 36.674 -29.372 57.771  1.00 48.94 ? 254  GLN   C CD  1 
ATOM   6253  O  OE1 . GLN   C  1 254 ? 36.113 -28.272 57.684  1.00 51.66 ? 254  GLN   C OE1 1 
ATOM   6254  N  NE2 . GLN   C  1 254 ? 36.057 -30.464 58.224  1.00 53.13 ? 254  GLN   C NE2 1 
ATOM   6255  N  N   . ILE   C  1 255 ? 40.602 -28.484 53.497  1.00 24.40 ? 255  ILE   C N   1 
ATOM   6256  C  CA  . ILE   C  1 255 ? 40.766 -27.741 52.261  1.00 22.98 ? 255  ILE   C CA  1 
ATOM   6257  C  C   . ILE   C  1 255 ? 39.406 -27.732 51.577  1.00 24.49 ? 255  ILE   C C   1 
ATOM   6258  O  O   . ILE   C  1 255 ? 38.783 -28.782 51.386  1.00 27.42 ? 255  ILE   C O   1 
ATOM   6259  C  CB  . ILE   C  1 255 ? 41.864 -28.351 51.379  1.00 23.35 ? 255  ILE   C CB  1 
ATOM   6260  C  CG1 . ILE   C  1 255 ? 43.206 -28.380 52.145  1.00 24.96 ? 255  ILE   C CG1 1 
ATOM   6261  C  CG2 . ILE   C  1 255 ? 42.014 -27.501 50.101  1.00 25.04 ? 255  ILE   C CG2 1 
ATOM   6262  C  CD1 . ILE   C  1 255 ? 44.430 -28.961 51.324  1.00 22.06 ? 255  ILE   C CD1 1 
ATOM   6263  N  N   . LYS   C  1 256 ? 38.906 -26.536 51.278  1.00 23.68 ? 256  LYS   C N   1 
ATOM   6264  C  CA  . LYS   C  1 256 ? 37.610 -26.383 50.628  1.00 24.33 ? 256  LYS   C CA  1 
ATOM   6265  C  C   . LYS   C  1 256 ? 37.818 -26.046 49.159  1.00 23.21 ? 256  LYS   C C   1 
ATOM   6266  O  O   . LYS   C  1 256 ? 38.794 -25.404 48.783  1.00 23.73 ? 256  LYS   C O   1 
ATOM   6267  C  CB  . LYS   C  1 256 ? 36.787 -25.278 51.301  1.00 25.38 ? 256  LYS   C CB  1 
ATOM   6268  C  CG  . LYS   C  1 256 ? 36.465 -25.508 52.787  1.00 28.61 ? 256  LYS   C CG  1 
ATOM   6269  C  CD  . LYS   C  1 256 ? 35.737 -26.856 52.983  1.00 33.45 ? 256  LYS   C CD  1 
ATOM   6270  C  CE  . LYS   C  1 256 ? 35.187 -26.997 54.394  1.00 38.42 ? 256  LYS   C CE  1 
ATOM   6271  N  NZ  . LYS   C  1 256 ? 34.530 -28.358 54.546  1.00 41.32 ? 256  LYS   C NZ  1 
ATOM   6272  N  N   . ALA   C  1 257 ? 36.883 -26.483 48.329  1.00 25.49 ? 257  ALA   C N   1 
ATOM   6273  C  CA  . ALA   C  1 257 ? 36.871 -26.163 46.911  1.00 26.78 ? 257  ALA   C CA  1 
ATOM   6274  C  C   . ALA   C  1 257 ? 35.754 -25.177 46.591  1.00 26.67 ? 257  ALA   C C   1 
ATOM   6275  O  O   . ALA   C  1 257 ? 34.656 -25.262 47.150  1.00 27.23 ? 257  ALA   C O   1 
ATOM   6276  C  CB  . ALA   C  1 257 ? 36.684 -27.424 46.061  1.00 28.53 ? 257  ALA   C CB  1 
ATOM   6277  N  N   . SER   C  1 258 ? 36.040 -24.253 45.669  1.00 26.68 ? 258  SER   C N   1 
ATOM   6278  C  CA  . SER   C  1 258 ? 35.068 -23.288 45.174  1.00 25.84 ? 258  SER   C CA  1 
ATOM   6279  C  C   . SER   C  1 258 ? 34.127 -23.899 44.185  1.00 28.45 ? 258  SER   C C   1 
ATOM   6280  O  O   . SER   C  1 258 ? 33.116 -23.269 43.828  1.00 29.80 ? 258  SER   C O   1 
ATOM   6281  C  CB  . SER   C  1 258 ? 35.800 -22.116 44.485  1.00 23.48 ? 258  SER   C CB  1 
ATOM   6282  O  OG  . SER   C  1 258 ? 36.317 -22.519 43.218  1.00 24.81 ? 258  SER   C OG  1 
ATOM   6283  N  N   . PHE   C  1 259 ? 34.477 -25.089 43.701  1.00 26.72 ? 259  PHE   C N   1 
ATOM   6284  C  CA  . PHE   C  1 259 ? 33.672 -25.729 42.631  1.00 27.57 ? 259  PHE   C CA  1 
ATOM   6285  C  C   . PHE   C  1 259 ? 33.044 -27.013 43.158  1.00 33.60 ? 259  PHE   C C   1 
ATOM   6286  O  O   . PHE   C  1 259 ? 33.618 -27.676 44.041  1.00 33.76 ? 259  PHE   C O   1 
ATOM   6287  C  CB  . PHE   C  1 259 ? 34.618 -25.961 41.448  1.00 29.22 ? 259  PHE   C CB  1 
ATOM   6288  C  CG  . PHE   C  1 259 ? 35.938 -26.634 41.797  1.00 30.29 ? 259  PHE   C CG  1 
ATOM   6289  C  CD1 . PHE   C  1 259 ? 37.050 -25.881 42.163  1.00 28.13 ? 259  PHE   C CD1 1 
ATOM   6290  C  CD2 . PHE   C  1 259 ? 36.069 -28.017 41.751  1.00 32.43 ? 259  PHE   C CD2 1 
ATOM   6291  C  CE1 . PHE   C  1 259 ? 38.250 -26.496 42.478  1.00 28.82 ? 259  PHE   C CE1 1 
ATOM   6292  C  CE2 . PHE   C  1 259 ? 37.273 -28.626 42.066  1.00 31.17 ? 259  PHE   C CE2 1 
ATOM   6293  C  CZ  . PHE   C  1 259 ? 38.359 -27.865 42.429  1.00 30.67 ? 259  PHE   C CZ  1 
ATOM   6294  N  N   . LYS   C  1 260 ? 31.878 -27.353 42.605  1.00 61.83 ? 260  LYS   C N   1 
ATOM   6295  C  CA  . LYS   C  1 260 ? 31.253 -28.680 42.832  1.00 58.15 ? 260  LYS   C CA  1 
ATOM   6296  C  C   . LYS   C  1 260 ? 32.041 -29.742 42.052  1.00 53.39 ? 260  LYS   C C   1 
ATOM   6297  O  O   . LYS   C  1 260 ? 32.609 -29.420 41.013  1.00 50.97 ? 260  LYS   C O   1 
ATOM   6298  C  CB  . LYS   C  1 260 ? 29.782 -28.647 42.403  1.00 58.60 ? 260  LYS   C CB  1 
ATOM   6299  C  CG  . LYS   C  1 260 ? 28.896 -27.711 43.210  1.00 60.05 ? 260  LYS   C CG  1 
ATOM   6300  C  CD  . LYS   C  1 260 ? 27.511 -27.533 42.602  1.00 63.28 ? 260  LYS   C CD  1 
ATOM   6301  C  CE  . LYS   C  1 260 ? 26.601 -26.700 43.447  1.00 66.19 ? 260  LYS   C CE  1 
ATOM   6302  N  NZ  . LYS   C  1 260 ? 26.239 -27.386 44.689  1.00 67.95 ? 260  LYS   C NZ  1 
ATOM   6303  O  OXT . LYS   C  1 260 ? 32.067 -30.888 42.522  1.00 52.34 ? 260  LYS   C OXT 1 
ATOM   6304  N  N   . ALA   D  1 2   ? 38.985 -52.615 63.333  1.00 16.98 ? 2    ALA   D N   1 
ATOM   6305  C  CA  . ALA   D  1 2   ? 39.257 -52.877 64.764  1.00 16.45 ? 2    ALA   D CA  1 
ATOM   6306  C  C   . ALA   D  1 2   ? 40.661 -52.388 65.124  1.00 16.44 ? 2    ALA   D C   1 
ATOM   6307  O  O   . ALA   D  1 2   ? 41.080 -51.335 64.615  1.00 16.39 ? 2    ALA   D O   1 
ATOM   6308  C  CB  . ALA   D  1 2   ? 39.086 -54.352 65.044  1.00 15.34 ? 2    ALA   D CB  1 
ATOM   6309  N  N   . HIS   D  1 3   ? 41.362 -53.133 65.983  1.00 16.27 ? 3    HIS   D N   1 
ATOM   6310  C  CA  . HIS   D  1 3   ? 42.710 -52.690 66.434  1.00 16.92 ? 3    HIS   D CA  1 
ATOM   6311  C  C   . HIS   D  1 3   ? 43.699 -52.810 65.272  1.00 16.94 ? 3    HIS   D C   1 
ATOM   6312  O  O   . HIS   D  1 3   ? 43.758 -53.868 64.618  1.00 17.42 ? 3    HIS   D O   1 
ATOM   6313  C  CB  . HIS   D  1 3   ? 43.171 -53.455 67.680  1.00 17.90 ? 3    HIS   D CB  1 
ATOM   6314  C  CG  . HIS   D  1 3   ? 42.449 -53.054 68.922  1.00 22.10 ? 3    HIS   D CG  1 
ATOM   6315  N  ND1 . HIS   D  1 3   ? 43.081 -52.920 70.138  1.00 24.68 ? 3    HIS   D ND1 1 
ATOM   6316  C  CD2 . HIS   D  1 3   ? 41.170 -52.723 69.130  1.00 24.42 ? 3    HIS   D CD2 1 
ATOM   6317  C  CE1 . HIS   D  1 3   ? 42.197 -52.540 71.048  1.00 21.83 ? 3    HIS   D CE1 1 
ATOM   6318  N  NE2 . HIS   D  1 3   ? 41.029 -52.417 70.458  1.00 28.50 ? 3    HIS   D NE2 1 
ATOM   6319  N  N   . HIS   D  1 4   ? 44.452 -51.737 65.032  1.00 14.74 ? 4    HIS   D N   1 
ATOM   6320  C  CA  . HIS   D  1 4   ? 45.458 -51.736 63.938  1.00 15.63 ? 4    HIS   D CA  1 
ATOM   6321  C  C   . HIS   D  1 4   ? 46.631 -52.624 64.358  1.00 14.54 ? 4    HIS   D C   1 
ATOM   6322  O  O   . HIS   D  1 4   ? 46.949 -52.710 65.559  1.00 16.02 ? 4    HIS   D O   1 
ATOM   6323  C  CB  . HIS   D  1 4   ? 45.864 -50.291 63.624  1.00 14.51 ? 4    HIS   D CB  1 
ATOM   6324  C  CG  . HIS   D  1 4   ? 46.785 -50.095 62.467  1.00 13.54 ? 4    HIS   D CG  1 
ATOM   6325  N  ND1 . HIS   D  1 4   ? 46.452 -50.325 61.148  1.00 12.69 ? 4    HIS   D ND1 1 
ATOM   6326  C  CD2 . HIS   D  1 4   ? 48.050 -49.659 62.458  1.00 14.83 ? 4    HIS   D CD2 1 
ATOM   6327  C  CE1 . HIS   D  1 4   ? 47.493 -50.034 60.383  1.00 15.05 ? 4    HIS   D CE1 1 
ATOM   6328  N  NE2 . HIS   D  1 4   ? 48.472 -49.628 61.157  1.00 14.39 ? 4    HIS   D NE2 1 
ATOM   6329  N  N   . TRP   D  1 5   ? 47.261 -53.268 63.378  1.00 13.85 ? 5    TRP   D N   1 
ATOM   6330  C  CA  . TRP   D  1 5   ? 48.419 -54.122 63.682  1.00 13.95 ? 5    TRP   D CA  1 
ATOM   6331  C  C   . TRP   D  1 5   ? 49.602 -53.340 64.264  1.00 15.70 ? 5    TRP   D C   1 
ATOM   6332  O  O   . TRP   D  1 5   ? 49.701 -52.108 64.161  1.00 15.77 ? 5    TRP   D O   1 
ATOM   6333  C  CB  . TRP   D  1 5   ? 48.899 -54.852 62.424  1.00 13.66 ? 5    TRP   D CB  1 
ATOM   6334  C  CG  . TRP   D  1 5   ? 49.483 -53.956 61.342  1.00 13.76 ? 5    TRP   D CG  1 
ATOM   6335  C  CD1 . TRP   D  1 5   ? 48.797 -53.333 60.336  1.00 15.20 ? 5    TRP   D CD1 1 
ATOM   6336  C  CD2 . TRP   D  1 5   ? 50.859 -53.594 61.208  1.00 13.49 ? 5    TRP   D CD2 1 
ATOM   6337  N  NE1 . TRP   D  1 5   ? 49.687 -52.575 59.558  1.00 14.28 ? 5    TRP   D NE1 1 
ATOM   6338  C  CE2 . TRP   D  1 5   ? 50.949 -52.714 60.078  1.00 13.42 ? 5    TRP   D CE2 1 
ATOM   6339  C  CE3 . TRP   D  1 5   ? 52.009 -53.872 61.953  1.00 13.33 ? 5    TRP   D CE3 1 
ATOM   6340  C  CZ2 . TRP   D  1 5   ? 52.150 -52.201 59.649  1.00 14.95 ? 5    TRP   D CZ2 1 
ATOM   6341  C  CZ3 . TRP   D  1 5   ? 53.228 -53.352 61.531  1.00 14.53 ? 5    TRP   D CZ3 1 
ATOM   6342  C  CH2 . TRP   D  1 5   ? 53.289 -52.515 60.394  1.00 15.35 ? 5    TRP   D CH2 1 
ATOM   6343  N  N   . GLY   D  1 6   ? 50.481 -54.062 64.939  1.00 14.78 ? 6    GLY   D N   1 
ATOM   6344  C  CA  . GLY   D  1 6   ? 51.652 -53.439 65.535  1.00 15.57 ? 6    GLY   D CA  1 
ATOM   6345  C  C   . GLY   D  1 6   ? 52.714 -54.483 65.877  1.00 13.90 ? 6    GLY   D C   1 
ATOM   6346  O  O   . GLY   D  1 6   ? 52.860 -55.503 65.193  1.00 15.04 ? 6    GLY   D O   1 
ATOM   6347  N  N   . TYR   D  1 7   ? 53.441 -54.197 66.950  1.00 15.59 ? 7    TYR   D N   1 
ATOM   6348  C  CA  . TYR   D  1 7   ? 54.494 -55.076 67.448  1.00 15.49 ? 7    TYR   D CA  1 
ATOM   6349  C  C   . TYR   D  1 7   ? 54.312 -55.391 68.914  1.00 18.01 ? 7    TYR   D C   1 
ATOM   6350  O  O   . TYR   D  1 7   ? 55.262 -55.851 69.572  1.00 19.69 ? 7    TYR   D O   1 
ATOM   6351  C  CB  . TYR   D  1 7   ? 55.890 -54.460 67.219  1.00 16.37 ? 7    TYR   D CB  1 
ATOM   6352  C  CG  . TYR   D  1 7   ? 56.286 -54.342 65.751  1.00 15.22 ? 7    TYR   D CG  1 
ATOM   6353  C  CD1 . TYR   D  1 7   ? 56.824 -55.458 65.068  1.00 15.18 ? 7    TYR   D CD1 1 
ATOM   6354  C  CD2 . TYR   D  1 7   ? 56.131 -53.139 65.038  1.00 15.97 ? 7    TYR   D CD2 1 
ATOM   6355  C  CE1 . TYR   D  1 7   ? 57.214 -55.387 63.729  1.00 15.06 ? 7    TYR   D CE1 1 
ATOM   6356  C  CE2 . TYR   D  1 7   ? 56.551 -53.060 63.702  1.00 16.22 ? 7    TYR   D CE2 1 
ATOM   6357  C  CZ  . TYR   D  1 7   ? 57.076 -54.166 63.078  1.00 15.46 ? 7    TYR   D CZ  1 
ATOM   6358  O  OH  . TYR   D  1 7   ? 57.500 -54.073 61.776  1.00 17.27 ? 7    TYR   D OH  1 
ATOM   6359  N  N   . GLY   D  1 8   ? 53.125 -55.129 69.445  1.00 17.46 ? 8    GLY   D N   1 
ATOM   6360  C  CA  . GLY   D  1 8   ? 52.850 -55.367 70.840  1.00 18.06 ? 8    GLY   D CA  1 
ATOM   6361  C  C   . GLY   D  1 8   ? 52.391 -56.796 71.090  1.00 18.47 ? 8    GLY   D C   1 
ATOM   6362  O  O   . GLY   D  1 8   ? 52.412 -57.661 70.204  1.00 18.44 ? 8    GLY   D O   1 
ATOM   6363  N  N   . LYS   D  1 9   ? 51.982 -57.013 72.337  1.00 19.23 ? 9    LYS   D N   1 
ATOM   6364  C  CA  . LYS   D  1 9   ? 51.618 -58.354 72.808  1.00 20.22 ? 9    LYS   D CA  1 
ATOM   6365  C  C   . LYS   D  1 9   ? 50.367 -58.868 72.139  1.00 19.64 ? 9    LYS   D C   1 
ATOM   6366  O  O   . LYS   D  1 9   ? 50.224 -60.084 71.966  1.00 20.16 ? 9    LYS   D O   1 
ATOM   6367  C  CB  . LYS   D  1 9   ? 51.381 -58.345 74.323  1.00 22.19 ? 9    LYS   D CB  1 
ATOM   6368  C  CG  . LYS   D  1 9   ? 52.520 -57.770 75.115  1.00 26.54 ? 9    LYS   D CG  1 
ATOM   6369  C  CD  . LYS   D  1 9   ? 53.715 -58.629 74.880  1.00 27.31 ? 9    LYS   D CD  1 
ATOM   6370  C  CE  . LYS   D  1 9   ? 54.884 -58.275 75.886  1.00 36.47 ? 9    LYS   D CE  1 
ATOM   6371  N  NZ  . LYS   D  1 9   ? 54.606 -58.757 77.277  1.00 42.97 ? 9    LYS   D NZ  1 
ATOM   6372  N  N   . HIS   D  1 10  ? 49.412 -57.989 71.798  1.00 19.13 ? 10   HIS   D N   1 
ATOM   6373  C  CA  . HIS   D  1 10  ? 48.177 -58.448 71.194  1.00 19.22 ? 10   HIS   D CA  1 
ATOM   6374  C  C   . HIS   D  1 10  ? 48.123 -58.259 69.698  1.00 19.34 ? 10   HIS   D C   1 
ATOM   6375  O  O   . HIS   D  1 10  ? 47.398 -59.001 69.009  1.00 20.45 ? 10   HIS   D O   1 
ATOM   6376  C  CB  . HIS   D  1 10  ? 46.972 -57.717 71.798  1.00 21.31 ? 10   HIS   D CB  1 
ATOM   6377  C  CG  . HIS   D  1 10  ? 46.790 -57.947 73.253  1.00 24.36 ? 10   HIS   D CG  1 
ATOM   6378  N  ND1 . HIS   D  1 10  ? 46.792 -56.920 74.167  1.00 29.86 ? 10   HIS   D ND1 1 
ATOM   6379  C  CD2 . HIS   D  1 10  ? 46.553 -59.081 73.939  1.00 27.40 ? 10   HIS   D CD2 1 
ATOM   6380  C  CE1 . HIS   D  1 10  ? 46.599 -57.428 75.378  1.00 30.90 ? 10   HIS   D CE1 1 
ATOM   6381  N  NE2 . HIS   D  1 10  ? 46.486 -58.741 75.266  1.00 27.39 ? 10   HIS   D NE2 1 
ATOM   6382  N  N   . ASN   D  1 11  ? 48.887 -57.314 69.158  1.00 17.06 ? 11   ASN   D N   1 
ATOM   6383  C  CA  . ASN   D  1 11  ? 48.765 -56.979 67.742  1.00 14.87 ? 11   ASN   D CA  1 
ATOM   6384  C  C   . ASN   D  1 11  ? 50.020 -57.264 66.949  1.00 15.30 ? 11   ASN   D C   1 
ATOM   6385  O  O   . ASN   D  1 11  ? 50.118 -56.868 65.787  1.00 14.64 ? 11   ASN   D O   1 
ATOM   6386  C  CB  . ASN   D  1 11  ? 48.350 -55.511 67.573  1.00 15.97 ? 11   ASN   D CB  1 
ATOM   6387  C  CG  . ASN   D  1 11  ? 49.389 -54.537 68.069  1.00 19.12 ? 11   ASN   D CG  1 
ATOM   6388  O  OD1 . ASN   D  1 11  ? 50.500 -54.932 68.429  1.00 18.95 ? 11   ASN   D OD1 1 
ATOM   6389  N  ND2 . ASN   D  1 11  ? 49.046 -53.251 68.065  1.00 20.48 ? 11   ASN   D ND2 1 
ATOM   6390  N  N   . GLY   D  1 12  ? 50.981 -57.954 67.539  1.00 15.13 ? 12   GLY   D N   1 
ATOM   6391  C  CA  . GLY   D  1 12  ? 52.282 -58.109 66.919  1.00 15.21 ? 12   GLY   D CA  1 
ATOM   6392  C  C   . GLY   D  1 12  ? 52.448 -59.295 65.986  1.00 14.85 ? 12   GLY   D C   1 
ATOM   6393  O  O   . GLY   D  1 12  ? 51.491 -60.008 65.692  1.00 15.63 ? 12   GLY   D O   1 
ATOM   6394  N  N   . PRO   D  1 13  ? 53.689 -59.529 65.544  1.00 14.22 ? 13   PRO   D N   1 
ATOM   6395  C  CA  . PRO   D  1 13  ? 53.947 -60.509 64.478  1.00 14.80 ? 13   PRO   D CA  1 
ATOM   6396  C  C   . PRO   D  1 13  ? 53.294 -61.865 64.655  1.00 15.58 ? 13   PRO   D C   1 
ATOM   6397  O  O   . PRO   D  1 13  ? 52.776 -62.370 63.636  1.00 16.01 ? 13   PRO   D O   1 
ATOM   6398  C  CB  . PRO   D  1 13  ? 55.484 -60.621 64.517  1.00 17.03 ? 13   PRO   D CB  1 
ATOM   6399  C  CG  . PRO   D  1 13  ? 55.913 -59.215 64.863  1.00 16.25 ? 13   PRO   D CG  1 
ATOM   6400  C  CD  . PRO   D  1 13  ? 54.863 -58.670 65.821  1.00 15.38 ? 13   PRO   D CD  1 
ATOM   6401  N  N   . GLU   D  1 14  ? 53.293 -62.475 65.865  1.00 14.43 ? 14   GLU   D N   1 
ATOM   6402  C  CA  . GLU   D  1 14  ? 52.749 -63.840 65.952  1.00 15.73 ? 14   GLU   D CA  1 
ATOM   6403  C  C   . GLU   D  1 14  ? 51.256 -63.861 65.692  1.00 16.39 ? 14   GLU   D C   1 
ATOM   6404  O  O   . GLU   D  1 14  ? 50.693 -64.936 65.487  1.00 18.34 ? 14   GLU   D O   1 
ATOM   6405  C  CB  . GLU   D  1 14  ? 53.080 -64.477 67.312  1.00 16.03 ? 14   GLU   D CB  1 
ATOM   6406  C  CG  . GLU   D  1 14  ? 52.339 -63.852 68.463  1.00 16.51 ? 14   GLU   D CG  1 
ATOM   6407  C  CD  . GLU   D  1 14  ? 52.422 -64.697 69.700  1.00 20.74 ? 14   GLU   D CD  1 
ATOM   6408  O  OE1 . GLU   D  1 14  ? 52.854 -65.901 69.659  1.00 22.07 ? 14   GLU   D OE1 1 
ATOM   6409  O  OE2 . GLU   D  1 14  ? 51.990 -64.158 70.737  1.00 23.90 ? 14   GLU   D OE2 1 
ATOM   6410  N  N   . HIS   D  1 15  ? 50.603 -62.712 65.744  1.00 16.42 ? 15   HIS   D N   1 
ATOM   6411  C  CA  . HIS   D  1 15  ? 49.149 -62.579 65.547  1.00 15.95 ? 15   HIS   D CA  1 
ATOM   6412  C  C   . HIS   D  1 15  ? 48.769 -62.031 64.186  1.00 15.17 ? 15   HIS   D C   1 
ATOM   6413  O  O   . HIS   D  1 15  ? 47.575 -62.021 63.861  1.00 15.71 ? 15   HIS   D O   1 
ATOM   6414  C  CB  . HIS   D  1 15  ? 48.543 -61.646 66.630  1.00 17.78 ? 15   HIS   D CB  1 
ATOM   6415  C  CG  . HIS   D  1 15  ? 48.753 -62.153 68.021  1.00 21.60 ? 15   HIS   D CG  1 
ATOM   6416  N  ND1 . HIS   D  1 15  ? 48.392 -63.433 68.403  1.00 25.38 ? 15   HIS   D ND1 1 
ATOM   6417  C  CD2 . HIS   D  1 15  ? 49.366 -61.596 69.094  1.00 23.36 ? 15   HIS   D CD2 1 
ATOM   6418  C  CE1 . HIS   D  1 15  ? 48.744 -63.625 69.671  1.00 25.94 ? 15   HIS   D CE1 1 
ATOM   6419  N  NE2 . HIS   D  1 15  ? 49.318 -62.516 70.109  1.00 24.77 ? 15   HIS   D NE2 1 
ATOM   6420  N  N   . TRP   D  1 16  ? 49.736 -61.571 63.377  1.00 12.93 ? 16   TRP   D N   1 
ATOM   6421  C  CA  . TRP   D  1 16  ? 49.358 -60.905 62.126  1.00 13.54 ? 16   TRP   D CA  1 
ATOM   6422  C  C   . TRP   D  1 16  ? 48.525 -61.791 61.229  1.00 14.88 ? 16   TRP   D C   1 
ATOM   6423  O  O   . TRP   D  1 16  ? 47.637 -61.269 60.524  1.00 15.25 ? 16   TRP   D O   1 
ATOM   6424  C  CB  . TRP   D  1 16  ? 50.588 -60.458 61.355  1.00 13.43 ? 16   TRP   D CB  1 
ATOM   6425  C  CG  . TRP   D  1 16  ? 51.285 -59.278 62.012  1.00 13.79 ? 16   TRP   D CG  1 
ATOM   6426  C  CD1 . TRP   D  1 16  ? 50.816 -58.466 63.023  1.00 13.75 ? 16   TRP   D CD1 1 
ATOM   6427  C  CD2 . TRP   D  1 16  ? 52.613 -58.815 61.695  1.00 13.82 ? 16   TRP   D CD2 1 
ATOM   6428  N  NE1 . TRP   D  1 16  ? 51.768 -57.487 63.295  1.00 13.79 ? 16   TRP   D NE1 1 
ATOM   6429  C  CE2 . TRP   D  1 16  ? 52.883 -57.706 62.535  1.00 12.19 ? 16   TRP   D CE2 1 
ATOM   6430  C  CE3 . TRP   D  1 16  ? 53.599 -59.253 60.800  1.00 13.43 ? 16   TRP   D CE3 1 
ATOM   6431  C  CZ2 . TRP   D  1 16  ? 54.096 -56.984 62.484  1.00 13.57 ? 16   TRP   D CZ2 1 
ATOM   6432  C  CZ3 . TRP   D  1 16  ? 54.818 -58.563 60.740  1.00 14.57 ? 16   TRP   D CZ3 1 
ATOM   6433  C  CH2 . TRP   D  1 16  ? 55.063 -57.424 61.594  1.00 15.02 ? 16   TRP   D CH2 1 
ATOM   6434  N  N   . HIS   D  1 17  ? 48.782 -63.111 61.217  1.00 14.92 ? 17   HIS   D N   1 
ATOM   6435  C  CA  . HIS   D  1 17  ? 48.003 -64.032 60.361  1.00 13.87 ? 17   HIS   D CA  1 
ATOM   6436  C  C   . HIS   D  1 17  ? 46.508 -63.964 60.621  1.00 15.67 ? 17   HIS   D C   1 
ATOM   6437  O  O   . HIS   D  1 17  ? 45.741 -64.370 59.724  1.00 16.83 ? 17   HIS   D O   1 
ATOM   6438  C  CB  . HIS   D  1 17  ? 48.471 -65.494 60.548  1.00 16.98 ? 17   HIS   D CB  1 
ATOM   6439  C  CG  . HIS   D  1 17  ? 48.199 -66.014 61.908  1.00 16.78 ? 17   HIS   D CG  1 
ATOM   6440  N  ND1 . HIS   D  1 17  ? 47.076 -66.755 62.212  1.00 21.86 ? 17   HIS   D ND1 1 
ATOM   6441  C  CD2 . HIS   D  1 17  ? 48.852 -65.792 63.081  1.00 15.91 ? 17   HIS   D CD2 1 
ATOM   6442  C  CE1 . HIS   D  1 17  ? 47.085 -67.013 63.513  1.00 19.71 ? 17   HIS   D CE1 1 
ATOM   6443  N  NE2 . HIS   D  1 17  ? 48.142 -66.427 64.053  1.00 19.39 ? 17   HIS   D NE2 1 
ATOM   6444  N  N   . LYS   D  1 18  ? 46.067 -63.491 61.806  1.00 14.99 ? 18   LYS   D N   1 
ATOM   6445  C  CA  . LYS   D  1 18  ? 44.631 -63.486 62.109  1.00 14.53 ? 18   LYS   D CA  1 
ATOM   6446  C  C   . LYS   D  1 18  ? 43.886 -62.519 61.207  1.00 16.10 ? 18   LYS   D C   1 
ATOM   6447  O  O   . LYS   D  1 18  ? 42.679 -62.703 60.985  1.00 15.78 ? 18   LYS   D O   1 
ATOM   6448  C  CB  . LYS   D  1 18  ? 44.421 -63.104 63.574  1.00 16.55 ? 18   LYS   D CB  1 
ATOM   6449  C  CG  . LYS   D  1 18  ? 44.983 -64.168 64.480  1.00 23.63 ? 18   LYS   D CG  1 
ATOM   6450  C  CD  . LYS   D  1 18  ? 44.889 -63.682 65.939  1.00 25.60 ? 18   LYS   D CD  1 
ATOM   6451  C  CE  . LYS   D  1 18  ? 45.578 -64.658 66.907  1.00 27.90 ? 18   LYS   D CE  1 
ATOM   6452  N  NZ  . LYS   D  1 18  ? 45.410 -64.064 68.322  1.00 32.08 ? 18   LYS   D NZ  1 
ATOM   6453  N  N   . ASP   D  1 19  ? 44.576 -61.480 60.731  1.00 14.46 ? 19   ASP   D N   1 
ATOM   6454  C  CA  . ASP   D  1 19  ? 43.988 -60.510 59.793  1.00 14.89 ? 19   ASP   D CA  1 
ATOM   6455  C  C   . ASP   D  1 19  ? 44.589 -60.569 58.402  1.00 15.83 ? 19   ASP   D C   1 
ATOM   6456  O  O   . ASP   D  1 19  ? 43.918 -60.159 57.445  1.00 15.38 ? 19   ASP   D O   1 
ATOM   6457  C  CB  . ASP   D  1 19  ? 44.141 -59.077 60.343  1.00 14.62 ? 19   ASP   D CB  1 
ATOM   6458  C  CG  . ASP   D  1 19  ? 43.440 -58.909 61.641  1.00 16.15 ? 19   ASP   D CG  1 
ATOM   6459  O  OD1 . ASP   D  1 19  ? 42.196 -58.970 61.649  1.00 18.57 ? 19   ASP   D OD1 1 
ATOM   6460  O  OD2 . ASP   D  1 19  ? 44.133 -58.733 62.685  1.00 18.22 ? 19   ASP   D OD2 1 
ATOM   6461  N  N   . PHE   D  1 20  ? 45.826 -61.058 58.268  1.00 14.75 ? 20   PHE   D N   1 
ATOM   6462  C  CA  . PHE   D  1 20  ? 46.580 -61.084 57.008  1.00 14.64 ? 20   PHE   D CA  1 
ATOM   6463  C  C   . PHE   D  1 20  ? 47.020 -62.513 56.778  1.00 15.27 ? 20   PHE   D C   1 
ATOM   6464  O  O   . PHE   D  1 20  ? 48.162 -62.887 57.100  1.00 17.47 ? 20   PHE   D O   1 
ATOM   6465  C  CB  . PHE   D  1 20  ? 47.762 -60.118 57.094  1.00 15.57 ? 20   PHE   D CB  1 
ATOM   6466  C  CG  . PHE   D  1 20  ? 47.352 -58.697 57.474  1.00 13.42 ? 20   PHE   D CG  1 
ATOM   6467  C  CD1 . PHE   D  1 20  ? 46.890 -57.848 56.512  1.00 15.44 ? 20   PHE   D CD1 1 
ATOM   6468  C  CD2 . PHE   D  1 20  ? 47.458 -58.261 58.780  1.00 13.52 ? 20   PHE   D CD2 1 
ATOM   6469  C  CE1 . PHE   D  1 20  ? 46.493 -56.558 56.843  1.00 13.66 ? 20   PHE   D CE1 1 
ATOM   6470  C  CE2 . PHE   D  1 20  ? 47.078 -56.924 59.149  1.00 13.56 ? 20   PHE   D CE2 1 
ATOM   6471  C  CZ  . PHE   D  1 20  ? 46.566 -56.075 58.156  1.00 14.99 ? 20   PHE   D CZ  1 
ATOM   6472  N  N   . PRO   D  1 21  ? 46.136 -63.359 56.268  1.00 13.21 ? 21   PRO   D N   1 
ATOM   6473  C  CA  . PRO   D  1 21  ? 46.475 -64.792 56.229  1.00 15.06 ? 21   PRO   D CA  1 
ATOM   6474  C  C   . PRO   D  1 21  ? 47.697 -65.091 55.350  1.00 14.54 ? 21   PRO   D C   1 
ATOM   6475  O  O   . PRO   D  1 21  ? 48.270 -66.188 55.500  1.00 16.57 ? 21   PRO   D O   1 
ATOM   6476  C  CB  . PRO   D  1 21  ? 45.197 -65.471 55.709  1.00 18.62 ? 21   PRO   D CB  1 
ATOM   6477  C  CG  . PRO   D  1 21  ? 44.314 -64.358 55.274  1.00 18.11 ? 21   PRO   D CG  1 
ATOM   6478  C  CD  . PRO   D  1 21  ? 44.722 -63.086 55.947  1.00 14.78 ? 21   PRO   D CD  1 
ATOM   6479  N  N   A ILE   D  1 22  ? 48.089 -64.188 54.445  0.57 13.83 ? 22   ILE   D N   1 
ATOM   6480  N  N   B ILE   D  1 22  ? 48.084 -64.186 54.447  0.43 13.86 ? 22   ILE   D N   1 
ATOM   6481  C  CA  A ILE   D  1 22  ? 49.284 -64.414 53.630  0.57 14.03 ? 22   ILE   D CA  1 
ATOM   6482  C  CA  B ILE   D  1 22  ? 49.276 -64.395 53.630  0.43 14.12 ? 22   ILE   D CA  1 
ATOM   6483  C  C   A ILE   D  1 22  ? 50.518 -64.487 54.502  0.57 15.36 ? 22   ILE   D C   1 
ATOM   6484  C  C   B ILE   D  1 22  ? 50.518 -64.462 54.497  0.43 15.20 ? 22   ILE   D C   1 
ATOM   6485  O  O   A ILE   D  1 22  ? 51.576 -64.926 54.035  0.57 15.50 ? 22   ILE   D O   1 
ATOM   6486  O  O   B ILE   D  1 22  ? 51.582 -64.869 54.019  0.43 15.39 ? 22   ILE   D O   1 
ATOM   6487  C  CB  A ILE   D  1 22  ? 49.406 -63.337 52.524  0.57 14.77 ? 22   ILE   D CB  1 
ATOM   6488  C  CB  B ILE   D  1 22  ? 49.371 -63.303 52.538  0.43 14.74 ? 22   ILE   D CB  1 
ATOM   6489  C  CG1 A ILE   D  1 22  ? 50.484 -63.718 51.493  0.57 15.16 ? 22   ILE   D CG1 1 
ATOM   6490  C  CG1 B ILE   D  1 22  ? 50.255 -63.757 51.370  0.43 15.21 ? 22   ILE   D CG1 1 
ATOM   6491  C  CG2 A ILE   D  1 22  ? 49.711 -62.009 53.145  0.57 14.76 ? 22   ILE   D CG2 1 
ATOM   6492  C  CG2 B ILE   D  1 22  ? 49.898 -62.012 53.125  0.43 14.79 ? 22   ILE   D CG2 1 
ATOM   6493  C  CD1 A ILE   D  1 22  ? 50.122 -64.939 50.692  0.57 15.71 ? 22   ILE   D CD1 1 
ATOM   6494  C  CD1 B ILE   D  1 22  ? 50.436 -62.681 50.332  0.43 14.52 ? 22   ILE   D CD1 1 
ATOM   6495  N  N   . ALA   D  1 23  ? 50.393 -64.096 55.782  1.00 14.07 ? 23   ALA   D N   1 
ATOM   6496  C  CA  . ALA   D  1 23  ? 51.507 -64.296 56.715  1.00 15.07 ? 23   ALA   D CA  1 
ATOM   6497  C  C   . ALA   D  1 23  ? 52.030 -65.724 56.711  1.00 14.98 ? 23   ALA   D C   1 
ATOM   6498  O  O   . ALA   D  1 23  ? 53.200 -65.927 57.057  1.00 16.43 ? 23   ALA   D O   1 
ATOM   6499  C  CB  . ALA   D  1 23  ? 51.059 -63.984 58.159  1.00 15.39 ? 23   ALA   D CB  1 
ATOM   6500  N  N   . LYS   D  1 24  ? 51.192 -66.721 56.358  1.00 15.33 ? 24   LYS   D N   1 
ATOM   6501  C  CA  . LYS   D  1 24  ? 51.575 -68.135 56.321  1.00 15.93 ? 24   LYS   D CA  1 
ATOM   6502  C  C   . LYS   D  1 24  ? 51.813 -68.610 54.888  1.00 15.38 ? 24   LYS   D C   1 
ATOM   6503  O  O   . LYS   D  1 24  ? 51.772 -69.836 54.631  1.00 18.30 ? 24   LYS   D O   1 
ATOM   6504  C  CB  . LYS   D  1 24  ? 50.498 -68.975 57.015  1.00 18.87 ? 24   LYS   D CB  1 
ATOM   6505  C  CG  . LYS   D  1 24  ? 50.426 -68.670 58.552  1.00 23.05 ? 24   LYS   D CG  1 
ATOM   6506  C  CD  . LYS   D  1 24  ? 49.462 -69.607 59.289  1.00 29.19 ? 24   LYS   D CD  1 
ATOM   6507  C  CE  . LYS   D  1 24  ? 49.342 -69.226 60.765  1.00 34.24 ? 24   LYS   D CE  1 
ATOM   6508  N  NZ  . LYS   D  1 24  ? 50.575 -69.540 61.618  1.00 37.54 ? 24   LYS   D NZ  1 
ATOM   6509  N  N   . GLY   D  1 25  ? 52.097 -67.672 53.974  1.00 17.02 ? 25   GLY   D N   1 
ATOM   6510  C  CA  . GLY   D  1 25  ? 52.258 -67.919 52.543  1.00 17.17 ? 25   GLY   D CA  1 
ATOM   6511  C  C   . GLY   D  1 25  ? 53.570 -68.627 52.208  1.00 18.71 ? 25   GLY   D C   1 
ATOM   6512  O  O   . GLY   D  1 25  ? 54.379 -69.011 53.064  1.00 18.68 ? 25   GLY   D O   1 
ATOM   6513  N  N   . GLU   D  1 26  ? 53.776 -68.748 50.904  1.00 16.24 ? 26   GLU   D N   1 
ATOM   6514  C  CA  . GLU   D  1 26  ? 54.881 -69.519 50.356  1.00 19.07 ? 26   GLU   D CA  1 
ATOM   6515  C  C   . GLU   D  1 26  ? 56.118 -68.675 50.121  1.00 18.44 ? 26   GLU   D C   1 
ATOM   6516  O  O   . GLU   D  1 26  ? 57.186 -69.241 49.834  1.00 22.37 ? 26   GLU   D O   1 
ATOM   6517  C  CB  . GLU   D  1 26  ? 54.448 -70.158 49.026  1.00 20.23 ? 26   GLU   D CB  1 
ATOM   6518  C  CG  . GLU   D  1 26  ? 53.294 -71.143 49.144  1.00 22.25 ? 26   GLU   D CG  1 
ATOM   6519  C  CD  . GLU   D  1 26  ? 53.726 -72.285 50.029  1.00 30.18 ? 26   GLU   D CD  1 
ATOM   6520  O  OE1 . GLU   D  1 26  ? 54.785 -72.897 49.739  1.00 34.35 ? 26   GLU   D OE1 1 
ATOM   6521  O  OE2 . GLU   D  1 26  ? 53.049 -72.503 51.044  1.00 35.21 ? 26   GLU   D OE2 1 
ATOM   6522  N  N   . ARG   D  1 27  ? 56.018 -67.350 50.190  1.00 17.65 ? 27   ARG   D N   1 
ATOM   6523  C  CA  A ARG   D  1 27  ? 57.109 -66.452 49.820  0.53 17.00 ? 27   ARG   D CA  1 
ATOM   6524  C  CA  B ARG   D  1 27  ? 57.184 -66.500 49.876  0.47 16.75 ? 27   ARG   D CA  1 
ATOM   6525  C  C   . ARG   D  1 27  ? 57.271 -65.346 50.872  1.00 15.35 ? 27   ARG   D C   1 
ATOM   6526  O  O   . ARG   D  1 27  ? 57.321 -64.154 50.537  1.00 17.86 ? 27   ARG   D O   1 
ATOM   6527  C  CB  A ARG   D  1 27  ? 56.804 -65.863 48.433  0.53 18.23 ? 27   ARG   D CB  1 
ATOM   6528  C  CB  B ARG   D  1 27  ? 57.152 -65.954 48.453  0.47 17.92 ? 27   ARG   D CB  1 
ATOM   6529  C  CG  A ARG   D  1 27  ? 57.902 -65.070 47.727  0.53 19.98 ? 27   ARG   D CG  1 
ATOM   6530  C  CG  B ARG   D  1 27  ? 56.826 -66.951 47.373  0.47 16.46 ? 27   ARG   D CG  1 
ATOM   6531  C  CD  A ARG   D  1 27  ? 57.401 -64.513 46.369  0.53 18.45 ? 27   ARG   D CD  1 
ATOM   6532  C  CD  B ARG   D  1 27  ? 57.172 -66.342 45.970  0.47 17.08 ? 27   ARG   D CD  1 
ATOM   6533  N  NE  A ARG   D  1 27  ? 57.911 -63.141 46.152  0.53 12.25 ? 27   ARG   D NE  1 
ATOM   6534  N  NE  B ARG   D  1 27  ? 56.447 -65.105 45.619  0.47 17.59 ? 27   ARG   D NE  1 
ATOM   6535  C  CZ  A ARG   D  1 27  ? 58.030 -62.562 44.982  0.53 18.53 ? 27   ARG   D CZ  1 
ATOM   6536  C  CZ  B ARG   D  1 27  ? 55.170 -65.030 45.228  0.47 20.14 ? 27   ARG   D CZ  1 
ATOM   6537  N  NH1 A ARG   D  1 27  ? 57.674 -63.184 43.846  0.53 22.80 ? 27   ARG   D NH1 1 
ATOM   6538  N  NH1 B ARG   D  1 27  ? 54.409 -66.130 45.225  0.47 21.67 ? 27   ARG   D NH1 1 
ATOM   6539  N  NH2 A ARG   D  1 27  ? 58.518 -61.352 44.920  0.53 22.09 ? 27   ARG   D NH2 1 
ATOM   6540  N  NH2 B ARG   D  1 27  ? 54.614 -63.857 44.881  0.47 18.07 ? 27   ARG   D NH2 1 
ATOM   6541  N  N   . GLN   D  1 28  ? 57.282 -65.706 52.154  1.00 16.20 ? 28   GLN   D N   1 
ATOM   6542  C  CA  . GLN   D  1 28  ? 57.305 -64.698 53.223  1.00 14.83 ? 28   GLN   D CA  1 
ATOM   6543  C  C   . GLN   D  1 28  ? 58.727 -64.321 53.652  1.00 16.12 ? 28   GLN   D C   1 
ATOM   6544  O  O   . GLN   D  1 28  ? 59.670 -65.106 53.546  1.00 17.20 ? 28   GLN   D O   1 
ATOM   6545  C  CB  . GLN   D  1 28  ? 56.555 -65.240 54.439  1.00 15.87 ? 28   GLN   D CB  1 
ATOM   6546  C  CG  . GLN   D  1 28  ? 55.036 -65.324 54.136  1.00 15.43 ? 28   GLN   D CG  1 
ATOM   6547  C  CD  . GLN   D  1 28  ? 54.479 -63.916 54.051  1.00 14.54 ? 28   GLN   D CD  1 
ATOM   6548  O  OE1 . GLN   D  1 28  ? 54.410 -63.193 55.062  1.00 14.27 ? 28   GLN   D OE1 1 
ATOM   6549  N  NE2 . GLN   D  1 28  ? 54.065 -63.503 52.860  1.00 15.16 ? 28   GLN   D NE2 1 
ATOM   6550  N  N   . SER   D  1 29  ? 58.842 -63.130 54.209  1.00 14.58 ? 29   SER   D N   1 
ATOM   6551  C  CA  . SER   D  1 29  ? 60.104 -62.555 54.663  1.00 14.24 ? 29   SER   D CA  1 
ATOM   6552  C  C   . SER   D  1 29  ? 59.937 -62.034 56.089  1.00 16.79 ? 29   SER   D C   1 
ATOM   6553  O  O   . SER   D  1 29  ? 58.825 -61.682 56.506  1.00 15.72 ? 29   SER   D O   1 
ATOM   6554  C  CB  . SER   D  1 29  ? 60.520 -61.377 53.756  1.00 15.80 ? 29   SER   D CB  1 
ATOM   6555  O  OG  . SER   D  1 29  ? 60.767 -61.826 52.430  1.00 15.18 ? 29   SER   D OG  1 
ATOM   6556  N  N   . PRO   D  1 30  ? 61.029 -61.921 56.852  1.00 15.20 ? 30   PRO   D N   1 
ATOM   6557  C  CA  . PRO   D  1 30  ? 62.420 -62.225 56.508  1.00 14.92 ? 30   PRO   D CA  1 
ATOM   6558  C  C   . PRO   D  1 30  ? 62.679 -63.721 56.651  1.00 15.85 ? 30   PRO   D C   1 
ATOM   6559  O  O   . PRO   D  1 30  ? 61.752 -64.451 57.010  1.00 16.53 ? 30   PRO   D O   1 
ATOM   6560  C  CB  . PRO   D  1 30  ? 63.191 -61.427 57.553  1.00 15.99 ? 30   PRO   D CB  1 
ATOM   6561  C  CG  . PRO   D  1 30  ? 62.287 -61.563 58.821  1.00 15.76 ? 30   PRO   D CG  1 
ATOM   6562  C  CD  . PRO   D  1 30  ? 60.904 -61.401 58.236  1.00 16.30 ? 30   PRO   D CD  1 
ATOM   6563  N  N   . VAL   D  1 31  ? 63.894 -64.147 56.315  1.00 16.15 ? 31   VAL   D N   1 
ATOM   6564  C  CA  . VAL   D  1 31  ? 64.328 -65.544 56.418  1.00 16.48 ? 31   VAL   D CA  1 
ATOM   6565  C  C   . VAL   D  1 31  ? 65.718 -65.564 57.027  1.00 18.29 ? 31   VAL   D C   1 
ATOM   6566  O  O   . VAL   D  1 31  ? 66.468 -64.554 57.039  1.00 18.96 ? 31   VAL   D O   1 
ATOM   6567  C  CB  . VAL   D  1 31  ? 64.344 -66.256 55.043  1.00 16.84 ? 31   VAL   D CB  1 
ATOM   6568  C  CG1 . VAL   D  1 31  ? 62.955 -66.235 54.398  1.00 17.08 ? 31   VAL   D CG1 1 
ATOM   6569  C  CG2 . VAL   D  1 31  ? 65.331 -65.532 54.056  1.00 18.99 ? 31   VAL   D CG2 1 
ATOM   6570  N  N   . ASP   D  1 32  ? 66.097 -66.750 57.495  1.00 16.85 ? 32   ASP   D N   1 
ATOM   6571  C  CA  . ASP   D  1 32  ? 67.486 -66.996 57.819  1.00 18.42 ? 32   ASP   D CA  1 
ATOM   6572  C  C   . ASP   D  1 32  ? 68.261 -67.241 56.529  1.00 20.16 ? 32   ASP   D C   1 
ATOM   6573  O  O   . ASP   D  1 32  ? 67.825 -68.000 55.640  1.00 21.56 ? 32   ASP   D O   1 
ATOM   6574  C  CB  . ASP   D  1 32  ? 67.605 -68.205 58.754  1.00 18.74 ? 32   ASP   D CB  1 
ATOM   6575  C  CG  . ASP   D  1 32  ? 69.052 -68.525 59.093  1.00 21.76 ? 32   ASP   D CG  1 
ATOM   6576  O  OD1 . ASP   D  1 32  ? 69.742 -67.603 59.585  1.00 21.83 ? 32   ASP   D OD1 1 
ATOM   6577  O  OD2 . ASP   D  1 32  ? 69.497 -69.672 58.861  1.00 23.80 ? 32   ASP   D OD2 1 
ATOM   6578  N  N   . ILE   D  1 33  ? 69.426 -66.603 56.425  1.00 18.77 ? 33   ILE   D N   1 
ATOM   6579  C  CA  . ILE   D  1 33  ? 70.344 -66.834 55.308  1.00 19.77 ? 33   ILE   D CA  1 
ATOM   6580  C  C   . ILE   D  1 33  ? 71.420 -67.769 55.804  1.00 21.03 ? 33   ILE   D C   1 
ATOM   6581  O  O   . ILE   D  1 33  ? 72.260 -67.400 56.641  1.00 22.38 ? 33   ILE   D O   1 
ATOM   6582  C  CB  . ILE   D  1 33  ? 70.954 -65.506 54.826  1.00 19.28 ? 33   ILE   D CB  1 
ATOM   6583  C  CG1 . ILE   D  1 33  ? 69.818 -64.605 54.404  1.00 21.56 ? 33   ILE   D CG1 1 
ATOM   6584  C  CG2 . ILE   D  1 33  ? 71.979 -65.769 53.735  1.00 21.90 ? 33   ILE   D CG2 1 
ATOM   6585  C  CD1 . ILE   D  1 33  ? 70.168 -63.118 54.315  1.00 23.35 ? 33   ILE   D CD1 1 
ATOM   6586  N  N   . ASP   D  1 34  ? 71.376 -69.027 55.353  1.00 23.57 ? 34   ASP   D N   1 
ATOM   6587  C  CA  . ASP   D  1 34  ? 72.399 -69.972 55.731  1.00 23.49 ? 34   ASP   D CA  1 
ATOM   6588  C  C   . ASP   D  1 34  ? 73.514 -69.948 54.707  1.00 27.77 ? 34   ASP   D C   1 
ATOM   6589  O  O   . ASP   D  1 34  ? 73.272 -70.197 53.522  1.00 28.45 ? 34   ASP   D O   1 
ATOM   6590  C  CB  . ASP   D  1 34  ? 71.826 -71.390 55.880  1.00 23.01 ? 34   ASP   D CB  1 
ATOM   6591  C  CG  . ASP   D  1 34  ? 72.913 -72.342 56.215  1.00 25.13 ? 34   ASP   D CG  1 
ATOM   6592  O  OD1 . ASP   D  1 34  ? 73.682 -72.691 55.305  1.00 28.49 ? 34   ASP   D OD1 1 
ATOM   6593  O  OD2 . ASP   D  1 34  ? 72.997 -72.584 57.405  1.00 24.98 ? 34   ASP   D OD2 1 
ATOM   6594  N  N   . THR   D  1 35  ? 74.722 -69.569 55.156  1.00 28.16 ? 35   THR   D N   1 
ATOM   6595  C  CA  . THR   D  1 35  ? 75.819 -69.298 54.233  1.00 30.42 ? 35   THR   D CA  1 
ATOM   6596  C  C   . THR   D  1 35  ? 76.395 -70.556 53.627  1.00 36.14 ? 35   THR   D C   1 
ATOM   6597  O  O   . THR   D  1 35  ? 77.188 -70.448 52.679  1.00 39.29 ? 35   THR   D O   1 
ATOM   6598  C  CB  . THR   D  1 35  ? 76.942 -68.517 54.919  1.00 30.04 ? 35   THR   D CB  1 
ATOM   6599  O  OG1 . THR   D  1 35  ? 77.523 -69.283 55.978  1.00 31.23 ? 35   THR   D OG1 1 
ATOM   6600  C  CG2 . THR   D  1 35  ? 76.378 -67.205 55.469  1.00 28.27 ? 35   THR   D CG2 1 
ATOM   6601  N  N   . HIS   D  1 36  ? 76.075 -71.714 54.194  1.00 30.53 ? 36   HIS   D N   1 
ATOM   6602  C  CA  . HIS   D  1 36  ? 76.582 -72.966 53.646  1.00 35.42 ? 36   HIS   D CA  1 
ATOM   6603  C  C   . HIS   D  1 36  ? 75.755 -73.429 52.465  1.00 35.86 ? 36   HIS   D C   1 
ATOM   6604  O  O   . HIS   D  1 36  ? 76.258 -74.187 51.625  1.00 37.45 ? 36   HIS   D O   1 
ATOM   6605  C  CB  . HIS   D  1 36  ? 76.584 -74.017 54.741  1.00 40.12 ? 36   HIS   D CB  1 
ATOM   6606  C  CG  . HIS   D  1 36  ? 77.122 -73.486 56.026  1.00 50.82 ? 36   HIS   D CG  1 
ATOM   6607  N  ND1 . HIS   D  1 36  ? 76.495 -73.678 57.238  1.00 52.92 ? 36   HIS   D ND1 1 
ATOM   6608  C  CD2 . HIS   D  1 36  ? 78.232 -72.749 56.282  1.00 54.51 ? 36   HIS   D CD2 1 
ATOM   6609  C  CE1 . HIS   D  1 36  ? 77.188 -73.066 58.185  1.00 54.77 ? 36   HIS   D CE1 1 
ATOM   6610  N  NE2 . HIS   D  1 36  ? 78.249 -72.499 57.631  1.00 54.21 ? 36   HIS   D NE2 1 
ATOM   6611  N  N   . THR   D  1 37  ? 74.487 -73.029 52.410  1.00 28.84 ? 37   THR   D N   1 
ATOM   6612  C  CA  . THR   D  1 37  ? 73.604 -73.495 51.353  1.00 26.69 ? 37   THR   D CA  1 
ATOM   6613  C  C   . THR   D  1 37  ? 73.261 -72.432 50.303  1.00 26.42 ? 37   THR   D C   1 
ATOM   6614  O  O   . THR   D  1 37  ? 72.865 -72.806 49.192  1.00 30.30 ? 37   THR   D O   1 
ATOM   6615  C  CB  . THR   D  1 37  ? 72.317 -74.078 51.959  1.00 28.48 ? 37   THR   D CB  1 
ATOM   6616  O  OG1 . THR   D  1 37  ? 71.701 -73.125 52.807  1.00 31.87 ? 37   THR   D OG1 1 
ATOM   6617  C  CG2 . THR   D  1 37  ? 72.652 -75.324 52.783  1.00 30.88 ? 37   THR   D CG2 1 
ATOM   6618  N  N   . ALA   D  1 38  ? 73.381 -71.142 50.620  1.00 28.02 ? 38   ALA   D N   1 
ATOM   6619  C  CA  . ALA   D  1 38  ? 73.209 -70.115 49.592  1.00 27.84 ? 38   ALA   D CA  1 
ATOM   6620  C  C   . ALA   D  1 38  ? 74.214 -70.348 48.457  1.00 32.62 ? 38   ALA   D C   1 
ATOM   6621  O  O   . ALA   D  1 38  ? 75.375 -70.665 48.714  1.00 38.53 ? 38   ALA   D O   1 
ATOM   6622  C  CB  . ALA   D  1 38  ? 73.375 -68.728 50.224  1.00 26.18 ? 38   ALA   D CB  1 
ATOM   6623  N  N   . LYS   D  1 39  ? 73.757 -70.260 47.194  1.00 28.54 ? 39   LYS   D N   1 
ATOM   6624  C  CA  . LYS   D  1 39  ? 74.561 -70.632 46.020  1.00 29.11 ? 39   LYS   D CA  1 
ATOM   6625  C  C   . LYS   D  1 39  ? 74.786 -69.458 45.061  1.00 31.54 ? 39   LYS   D C   1 
ATOM   6626  O  O   . LYS   D  1 39  ? 73.838 -68.758 44.695  1.00 29.50 ? 39   LYS   D O   1 
ATOM   6627  C  CB  . LYS   D  1 39  ? 73.903 -71.778 45.247  1.00 35.73 ? 39   LYS   D CB  1 
ATOM   6628  C  CG  . LYS   D  1 39  ? 74.064 -73.128 45.938  1.00 44.94 ? 39   LYS   D CG  1 
ATOM   6629  C  CD  . LYS   D  1 39  ? 73.638 -74.295 45.076  1.00 51.09 ? 39   LYS   D CD  1 
ATOM   6630  C  CE  . LYS   D  1 39  ? 74.415 -74.308 43.763  1.00 58.91 ? 39   LYS   D CE  1 
ATOM   6631  N  NZ  . LYS   D  1 39  ? 74.146 -75.563 42.986  1.00 62.75 ? 39   LYS   D NZ  1 
ATOM   6632  N  N   . TYR   D  1 40  ? 76.026 -69.312 44.578  1.00 31.57 ? 40   TYR   D N   1 
ATOM   6633  C  CA  . TYR   D  1 40  ? 76.342 -68.335 43.544  1.00 30.74 ? 40   TYR   D CA  1 
ATOM   6634  C  C   . TYR   D  1 40  ? 75.490 -68.553 42.294  1.00 31.55 ? 40   TYR   D C   1 
ATOM   6635  O  O   . TYR   D  1 40  ? 75.308 -69.685 41.826  1.00 31.90 ? 40   TYR   D O   1 
ATOM   6636  C  CB  . TYR   D  1 40  ? 77.824 -68.446 43.177  1.00 31.92 ? 40   TYR   D CB  1 
ATOM   6637  C  CG  . TYR   D  1 40  ? 78.186 -67.695 41.928  1.00 34.59 ? 40   TYR   D CG  1 
ATOM   6638  C  CD1 . TYR   D  1 40  ? 78.196 -66.293 41.914  1.00 34.75 ? 40   TYR   D CD1 1 
ATOM   6639  C  CD2 . TYR   D  1 40  ? 78.515 -68.372 40.767  1.00 38.47 ? 40   TYR   D CD2 1 
ATOM   6640  C  CE1 . TYR   D  1 40  ? 78.540 -65.602 40.757  1.00 36.77 ? 40   TYR   D CE1 1 
ATOM   6641  C  CE2 . TYR   D  1 40  ? 78.866 -67.690 39.615  1.00 41.46 ? 40   TYR   D CE2 1 
ATOM   6642  C  CZ  . TYR   D  1 40  ? 78.851 -66.310 39.618  1.00 39.08 ? 40   TYR   D CZ  1 
ATOM   6643  O  OH  . TYR   D  1 40  ? 79.206 -65.643 38.459  1.00 42.89 ? 40   TYR   D OH  1 
ATOM   6644  N  N   . ASP   D  1 41  ? 74.951 -67.459 41.760  1.00 30.20 ? 41   ASP   D N   1 
ATOM   6645  C  CA  . ASP   D  1 41  ? 74.119 -67.486 40.559  1.00 31.95 ? 41   ASP   D CA  1 
ATOM   6646  C  C   . ASP   D  1 41  ? 74.824 -66.702 39.464  1.00 33.12 ? 41   ASP   D C   1 
ATOM   6647  O  O   . ASP   D  1 41  ? 74.792 -65.454 39.449  1.00 30.83 ? 41   ASP   D O   1 
ATOM   6648  C  CB  . ASP   D  1 41  ? 72.741 -66.901 40.863  1.00 30.11 ? 41   ASP   D CB  1 
ATOM   6649  C  CG  . ASP   D  1 41  ? 71.788 -67.002 39.708  1.00 34.35 ? 41   ASP   D CG  1 
ATOM   6650  O  OD1 . ASP   D  1 41  ? 72.203 -67.344 38.568  1.00 36.96 ? 41   ASP   D OD1 1 
ATOM   6651  O  OD2 . ASP   D  1 41  ? 70.580 -66.762 39.981  1.00 36.09 ? 41   ASP   D OD2 1 
ATOM   6652  N  N   . PRO   D  1 42  ? 75.452 -67.378 38.513  1.00 35.41 ? 42   PRO   D N   1 
ATOM   6653  C  CA  . PRO   D  1 42  ? 76.153 -66.652 37.454  1.00 35.53 ? 42   PRO   D CA  1 
ATOM   6654  C  C   . PRO   D  1 42  ? 75.233 -65.829 36.571  1.00 36.79 ? 42   PRO   D C   1 
ATOM   6655  O  O   . PRO   D  1 42  ? 75.734 -64.989 35.810  1.00 40.75 ? 42   PRO   D O   1 
ATOM   6656  C  CB  . PRO   D  1 42  ? 76.847 -67.775 36.658  1.00 38.32 ? 42   PRO   D CB  1 
ATOM   6657  C  CG  . PRO   D  1 42  ? 76.047 -69.014 36.980  1.00 40.12 ? 42   PRO   D CG  1 
ATOM   6658  C  CD  . PRO   D  1 42  ? 75.475 -68.842 38.347  1.00 36.54 ? 42   PRO   D CD  1 
ATOM   6659  N  N   . SER   D  1 43  ? 73.924 -66.048 36.625  1.00 35.21 ? 43   SER   D N   1 
ATOM   6660  C  CA  . SER   D  1 43  ? 73.005 -65.268 35.809  1.00 38.98 ? 43   SER   D CA  1 
ATOM   6661  C  C   . SER   D  1 43  ? 72.768 -63.863 36.365  1.00 38.30 ? 43   SER   D C   1 
ATOM   6662  O  O   . SER   D  1 43  ? 72.219 -63.023 35.647  1.00 41.46 ? 43   SER   D O   1 
ATOM   6663  C  CB  . SER   D  1 43  ? 71.664 -66.010 35.652  1.00 39.19 ? 43   SER   D CB  1 
ATOM   6664  O  OG  . SER   D  1 43  ? 70.835 -65.873 36.805  1.00 37.97 ? 43   SER   D OG  1 
ATOM   6665  N  N   . LEU   D  1 44  ? 73.157 -63.589 37.608  1.00 33.07 ? 44   LEU   D N   1 
ATOM   6666  C  CA  . LEU   D  1 44  ? 73.000 -62.244 38.160  1.00 33.01 ? 44   LEU   D CA  1 
ATOM   6667  C  C   . LEU   D  1 44  ? 73.890 -61.247 37.420  1.00 36.70 ? 44   LEU   D C   1 
ATOM   6668  O  O   . LEU   D  1 44  ? 75.059 -61.518 37.140  1.00 36.11 ? 44   LEU   D O   1 
ATOM   6669  C  CB  . LEU   D  1 44  ? 73.345 -62.229 39.654  1.00 31.73 ? 44   LEU   D CB  1 
ATOM   6670  C  CG  . LEU   D  1 44  ? 72.372 -63.044 40.503  1.00 28.52 ? 44   LEU   D CG  1 
ATOM   6671  C  CD1 . LEU   D  1 44  ? 72.901 -63.308 41.921  1.00 29.10 ? 44   LEU   D CD1 1 
ATOM   6672  C  CD2 . LEU   D  1 44  ? 71.041 -62.262 40.566  1.00 27.66 ? 44   LEU   D CD2 1 
ATOM   6673  N  N   . LYS   D  1 45  ? 73.325 -60.076 37.094  1.00 36.24 ? 45   LYS   D N   1 
ATOM   6674  C  CA  . LYS   D  1 45  ? 74.138 -59.037 36.472  1.00 35.74 ? 45   LYS   D CA  1 
ATOM   6675  C  C   . LYS   D  1 45  ? 74.705 -58.128 37.546  1.00 32.60 ? 45   LYS   D C   1 
ATOM   6676  O  O   . LYS   D  1 45  ? 74.221 -58.129 38.686  1.00 30.66 ? 45   LYS   D O   1 
ATOM   6677  C  CB  . LYS   D  1 45  ? 73.295 -58.244 35.487  1.00 37.42 ? 45   LYS   D CB  1 
ATOM   6678  C  CG  . LYS   D  1 45  ? 72.532 -59.138 34.508  1.00 46.26 ? 45   LYS   D CG  1 
ATOM   6679  C  CD  . LYS   D  1 45  ? 71.533 -58.327 33.672  1.00 54.50 ? 45   LYS   D CD  1 
ATOM   6680  C  CE  . LYS   D  1 45  ? 70.332 -59.156 33.169  1.00 59.04 ? 45   LYS   D CE  1 
ATOM   6681  N  NZ  . LYS   D  1 45  ? 69.219 -59.318 34.163  1.00 58.49 ? 45   LYS   D NZ  1 
ATOM   6682  N  N   . PRO   D  1 46  ? 75.713 -57.306 37.218  1.00 32.68 ? 46   PRO   D N   1 
ATOM   6683  C  CA  . PRO   D  1 46  ? 76.254 -56.385 38.224  1.00 32.27 ? 46   PRO   D CA  1 
ATOM   6684  C  C   . PRO   D  1 46  ? 75.148 -55.508 38.796  1.00 30.76 ? 46   PRO   D C   1 
ATOM   6685  O  O   . PRO   D  1 46  ? 74.272 -55.057 38.061  1.00 31.20 ? 46   PRO   D O   1 
ATOM   6686  C  CB  . PRO   D  1 46  ? 77.267 -55.549 37.442  1.00 33.21 ? 46   PRO   D CB  1 
ATOM   6687  C  CG  . PRO   D  1 46  ? 77.663 -56.476 36.254  1.00 36.57 ? 46   PRO   D CG  1 
ATOM   6688  C  CD  . PRO   D  1 46  ? 76.379 -57.159 35.903  1.00 38.33 ? 46   PRO   D CD  1 
ATOM   6689  N  N   . LEU   D  1 47  ? 75.191 -55.289 40.110  1.00 28.46 ? 47   LEU   D N   1 
ATOM   6690  C  CA  . LEU   D  1 47  ? 74.202 -54.468 40.809  1.00 27.90 ? 47   LEU   D CA  1 
ATOM   6691  C  C   . LEU   D  1 47  ? 74.631 -53.003 40.746  1.00 30.46 ? 47   LEU   D C   1 
ATOM   6692  O  O   . LEU   D  1 47  ? 75.809 -52.681 40.966  1.00 33.20 ? 47   LEU   D O   1 
ATOM   6693  C  CB  . LEU   D  1 47  ? 74.046 -54.893 42.262  1.00 29.30 ? 47   LEU   D CB  1 
ATOM   6694  C  CG  . LEU   D  1 47  ? 72.959 -54.145 43.026  1.00 28.64 ? 47   LEU   D CG  1 
ATOM   6695  C  CD1 . LEU   D  1 47  ? 71.548 -54.568 42.625  1.00 28.80 ? 47   LEU   D CD1 1 
ATOM   6696  C  CD2 . LEU   D  1 47  ? 73.203 -54.363 44.515  1.00 31.88 ? 47   LEU   D CD2 1 
ATOM   6697  N  N   . SER   D  1 48  ? 73.683 -52.143 40.387  1.00 28.50 ? 48   SER   D N   1 
ATOM   6698  C  CA  A SER   D  1 48  ? 73.905 -50.710 40.249  0.57 30.45 ? 48   SER   D CA  1 
ATOM   6699  C  CA  B SER   D  1 48  ? 73.891 -50.704 40.242  0.43 30.35 ? 48   SER   D CA  1 
ATOM   6700  C  C   . SER   D  1 48  ? 73.055 -49.996 41.294  1.00 28.29 ? 48   SER   D C   1 
ATOM   6701  O  O   . SER   D  1 48  ? 71.824 -50.069 41.250  1.00 28.11 ? 48   SER   D O   1 
ATOM   6702  C  CB  A SER   D  1 48  ? 73.542 -50.258 38.836  0.57 31.91 ? 48   SER   D CB  1 
ATOM   6703  C  CB  B SER   D  1 48  ? 73.472 -50.219 38.853  0.43 32.01 ? 48   SER   D CB  1 
ATOM   6704  O  OG  A SER   D  1 48  ? 73.643 -48.859 38.719  0.57 34.01 ? 48   SER   D OG  1 
ATOM   6705  O  OG  B SER   D  1 48  ? 74.382 -50.615 37.857  0.43 36.27 ? 48   SER   D OG  1 
ATOM   6706  N  N   . VAL   D  1 49  ? 73.718 -49.298 42.219  1.00 29.77 ? 49   VAL   D N   1 
ATOM   6707  C  CA  . VAL   D  1 49  ? 73.055 -48.510 43.259  1.00 29.94 ? 49   VAL   D CA  1 
ATOM   6708  C  C   . VAL   D  1 49  ? 73.352 -47.055 42.937  1.00 31.14 ? 49   VAL   D C   1 
ATOM   6709  O  O   . VAL   D  1 49  ? 74.462 -46.587 43.201  1.00 34.96 ? 49   VAL   D O   1 
ATOM   6710  C  CB  . VAL   D  1 49  ? 73.564 -48.858 44.666  1.00 30.87 ? 49   VAL   D CB  1 
ATOM   6711  C  CG1 . VAL   D  1 49  ? 72.829 -47.975 45.721  1.00 33.70 ? 49   VAL   D CG1 1 
ATOM   6712  C  CG2 . VAL   D  1 49  ? 73.388 -50.338 44.938  1.00 32.59 ? 49   VAL   D CG2 1 
ATOM   6713  N  N   . SER   D  1 50  ? 72.391 -46.327 42.360  1.00 30.15 ? 50   SER   D N   1 
ATOM   6714  C  CA  . SER   D  1 50  ? 72.676 -44.981 41.831  1.00 31.21 ? 50   SER   D CA  1 
ATOM   6715  C  C   . SER   D  1 50  ? 71.948 -43.978 42.704  1.00 29.06 ? 50   SER   D C   1 
ATOM   6716  O  O   . SER   D  1 50  ? 70.770 -43.672 42.475  1.00 31.42 ? 50   SER   D O   1 
ATOM   6717  C  CB  . SER   D  1 50  ? 72.254 -44.804 40.380  1.00 37.27 ? 50   SER   D CB  1 
ATOM   6718  O  OG  . SER   D  1 50  ? 72.831 -45.794 39.574  1.00 44.19 ? 50   SER   D OG  1 
ATOM   6719  N  N   . TYR   D  1 51  ? 72.658 -43.439 43.688  1.00 31.22 ? 51   TYR   D N   1 
ATOM   6720  C  CA  . TYR   D  1 51  ? 72.052 -42.582 44.685  1.00 28.77 ? 51   TYR   D CA  1 
ATOM   6721  C  C   . TYR   D  1 51  ? 72.636 -41.178 44.675  1.00 32.65 ? 51   TYR   D C   1 
ATOM   6722  O  O   . TYR   D  1 51  ? 72.395 -40.431 45.625  1.00 34.08 ? 51   TYR   D O   1 
ATOM   6723  C  CB  . TYR   D  1 51  ? 72.239 -43.168 46.082  1.00 28.80 ? 51   TYR   D CB  1 
ATOM   6724  C  CG  . TYR   D  1 51  ? 71.359 -44.358 46.441  1.00 26.10 ? 51   TYR   D CG  1 
ATOM   6725  C  CD1 . TYR   D  1 51  ? 70.363 -44.818 45.588  1.00 26.77 ? 51   TYR   D CD1 1 
ATOM   6726  C  CD2 . TYR   D  1 51  ? 71.535 -45.000 47.656  1.00 23.86 ? 51   TYR   D CD2 1 
ATOM   6727  C  CE1 . TYR   D  1 51  ? 69.529 -45.903 45.959  1.00 24.66 ? 51   TYR   D CE1 1 
ATOM   6728  C  CE2 . TYR   D  1 51  ? 70.757 -46.055 48.036  1.00 22.52 ? 51   TYR   D CE2 1 
ATOM   6729  C  CZ  . TYR   D  1 51  ? 69.725 -46.530 47.203  1.00 21.69 ? 51   TYR   D CZ  1 
ATOM   6730  O  OH  . TYR   D  1 51  ? 68.988 -47.585 47.658  1.00 22.70 ? 51   TYR   D OH  1 
ATOM   6731  N  N   . ASP   D  1 52  ? 73.406 -40.827 43.646  1.00 35.19 ? 52   ASP   D N   1 
ATOM   6732  C  CA  . ASP   D  1 52  ? 74.093 -39.531 43.622  1.00 37.07 ? 52   ASP   D CA  1 
ATOM   6733  C  C   . ASP   D  1 52  ? 73.109 -38.357 43.624  1.00 36.82 ? 52   ASP   D C   1 
ATOM   6734  O  O   . ASP   D  1 52  ? 73.442 -37.273 44.116  1.00 40.49 ? 52   ASP   D O   1 
ATOM   6735  C  CB  . ASP   D  1 52  ? 75.018 -39.443 42.389  1.00 41.05 ? 52   ASP   D CB  1 
ATOM   6736  C  CG  . ASP   D  1 52  ? 76.215 -40.402 42.448  1.00 47.60 ? 52   ASP   D CG  1 
ATOM   6737  O  OD1 . ASP   D  1 52  ? 76.448 -41.097 43.464  1.00 46.70 ? 52   ASP   D OD1 1 
ATOM   6738  O  OD2 . ASP   D  1 52  ? 76.977 -40.444 41.444  1.00 50.11 ? 52   ASP   D OD2 1 
ATOM   6739  N  N   . GLN   D  1 53  ? 71.904 -38.537 43.087  1.00 32.49 ? 53   GLN   D N   1 
ATOM   6740  C  CA  . GLN   D  1 53  ? 70.953 -37.435 42.931  1.00 33.65 ? 53   GLN   D CA  1 
ATOM   6741  C  C   . GLN   D  1 53  ? 69.710 -37.626 43.781  1.00 33.07 ? 53   GLN   D C   1 
ATOM   6742  O  O   . GLN   D  1 53  ? 68.622 -37.186 43.403  1.00 35.55 ? 53   GLN   D O   1 
ATOM   6743  C  CB  . GLN   D  1 53  ? 70.546 -37.261 41.470  1.00 34.79 ? 53   GLN   D CB  1 
ATOM   6744  C  CG  . GLN   D  1 53  ? 71.721 -36.913 40.592  1.00 37.35 ? 53   GLN   D CG  1 
ATOM   6745  C  CD  . GLN   D  1 53  ? 71.308 -36.452 39.201  1.00 44.24 ? 53   GLN   D CD  1 
ATOM   6746  O  OE1 . GLN   D  1 53  ? 70.776 -37.222 38.411  1.00 46.26 ? 53   GLN   D OE1 1 
ATOM   6747  N  NE2 . GLN   D  1 53  ? 71.564 -35.178 38.898  1.00 49.25 ? 53   GLN   D NE2 1 
ATOM   6748  N  N   . ALA   D  1 54  ? 69.845 -38.311 44.901  1.00 29.86 ? 54   ALA   D N   1 
ATOM   6749  C  CA  . ALA   D  1 54  ? 68.672 -38.596 45.721  1.00 28.82 ? 54   ALA   D CA  1 
ATOM   6750  C  C   . ALA   D  1 54  ? 68.178 -37.342 46.430  1.00 29.46 ? 54   ALA   D C   1 
ATOM   6751  O  O   . ALA   D  1 54  ? 68.978 -36.540 46.910  1.00 29.60 ? 54   ALA   D O   1 
ATOM   6752  C  CB  . ALA   D  1 54  ? 69.018 -39.668 46.750  1.00 30.42 ? 54   ALA   D CB  1 
ATOM   6753  N  N   . THR   D  1 55  ? 66.854 -37.166 46.500  1.00 27.28 ? 55   THR   D N   1 
ATOM   6754  C  CA  . THR   D  1 55  ? 66.282 -35.942 47.085  1.00 25.23 ? 55   THR   D CA  1 
ATOM   6755  C  C   . THR   D  1 55  ? 65.424 -36.390 48.262  1.00 23.38 ? 55   THR   D C   1 
ATOM   6756  O  O   . THR   D  1 55  ? 64.278 -36.788 48.071  1.00 24.01 ? 55   THR   D O   1 
ATOM   6757  C  CB  . THR   D  1 55  ? 65.441 -35.134 46.065  1.00 28.33 ? 55   THR   D CB  1 
ATOM   6758  O  OG1 . THR   D  1 55  ? 66.257 -34.765 44.960  1.00 32.27 ? 55   THR   D OG1 1 
ATOM   6759  C  CG2 . THR   D  1 55  ? 64.824 -33.866 46.703  1.00 27.64 ? 55   THR   D CG2 1 
ATOM   6760  N  N   . SER   D  1 56  ? 65.960 -36.324 49.479  1.00 20.96 ? 56   SER   D N   1 
ATOM   6761  C  CA  . SER   D  1 56  ? 65.122 -36.621 50.634  1.00 20.16 ? 56   SER   D CA  1 
ATOM   6762  C  C   . SER   D  1 56  ? 64.199 -35.443 50.951  1.00 19.96 ? 56   SER   D C   1 
ATOM   6763  O  O   . SER   D  1 56  ? 64.491 -34.269 50.633  1.00 24.01 ? 56   SER   D O   1 
ATOM   6764  C  CB  . SER   D  1 56  ? 65.978 -36.980 51.859  1.00 19.77 ? 56   SER   D CB  1 
ATOM   6765  O  OG  . SER   D  1 56  ? 66.673 -35.822 52.363  1.00 22.29 ? 56   SER   D OG  1 
ATOM   6766  N  N   . LEU   D  1 57  ? 63.024 -35.778 51.522  1.00 20.78 ? 57   LEU   D N   1 
ATOM   6767  C  CA  . LEU   D  1 57  ? 62.039 -34.748 51.812  1.00 20.75 ? 57   LEU   D CA  1 
ATOM   6768  C  C   . LEU   D  1 57  ? 61.671 -34.655 53.286  1.00 20.61 ? 57   LEU   D C   1 
ATOM   6769  O  O   . LEU   D  1 57  ? 61.609 -33.533 53.819  1.00 20.55 ? 57   LEU   D O   1 
ATOM   6770  C  CB  . LEU   D  1 57  ? 60.749 -34.985 50.994  1.00 26.02 ? 57   LEU   D CB  1 
ATOM   6771  C  CG  . LEU   D  1 57  ? 60.918 -34.760 49.502  1.00 29.30 ? 57   LEU   D CG  1 
ATOM   6772  C  CD1 . LEU   D  1 57  ? 59.609 -35.221 48.815  1.00 31.25 ? 57   LEU   D CD1 1 
ATOM   6773  C  CD2 . LEU   D  1 57  ? 61.263 -33.266 49.177  1.00 31.54 ? 57   LEU   D CD2 1 
ATOM   6774  N  N   . ARG   D  1 58  ? 61.332 -35.770 53.919  1.00 18.96 ? 58   ARG   D N   1 
ATOM   6775  C  CA  . ARG   D  1 58  ? 60.707 -35.718 55.239  1.00 18.37 ? 58   ARG   D CA  1 
ATOM   6776  C  C   . ARG   D  1 58  ? 60.922 -37.034 55.958  1.00 18.92 ? 58   ARG   D C   1 
ATOM   6777  O  O   . ARG   D  1 58  ? 61.262 -38.072 55.351  1.00 19.90 ? 58   ARG   D O   1 
ATOM   6778  C  CB  . ARG   D  1 58  ? 59.219 -35.328 55.153  1.00 24.97 ? 58   ARG   D CB  1 
ATOM   6779  C  CG  . ARG   D  1 58  ? 58.393 -36.240 54.335  1.00 28.06 ? 58   ARG   D CG  1 
ATOM   6780  C  CD  . ARG   D  1 58  ? 56.955 -35.672 54.211  1.00 32.14 ? 58   ARG   D CD  1 
ATOM   6781  N  NE  . ARG   D  1 58  ? 56.995 -34.292 53.751  1.00 36.75 ? 58   ARG   D NE  1 
ATOM   6782  C  CZ  . ARG   D  1 58  ? 56.882 -33.924 52.478  1.00 37.32 ? 58   ARG   D CZ  1 
ATOM   6783  N  NH1 . ARG   D  1 58  ? 56.735 -34.845 51.499  1.00 35.02 ? 58   ARG   D NH1 1 
ATOM   6784  N  NH2 . ARG   D  1 58  ? 56.940 -32.628 52.190  1.00 33.65 ? 58   ARG   D NH2 1 
ATOM   6785  N  N   . ILE   D  1 59  ? 60.739 -36.985 57.267  1.00 17.58 ? 59   ILE   D N   1 
ATOM   6786  C  CA  . ILE   D  1 59  ? 60.838 -38.168 58.111  1.00 17.79 ? 59   ILE   D CA  1 
ATOM   6787  C  C   . ILE   D  1 59  ? 59.568 -38.266 58.954  1.00 18.12 ? 59   ILE   D C   1 
ATOM   6788  O  O   . ILE   D  1 59  ? 59.072 -37.257 59.473  1.00 18.66 ? 59   ILE   D O   1 
ATOM   6789  C  CB  . ILE   D  1 59  ? 62.121 -38.099 58.967  1.00 16.40 ? 59   ILE   D CB  1 
ATOM   6790  C  CG1 . ILE   D  1 59  ? 62.315 -39.427 59.705  1.00 18.59 ? 59   ILE   D CG1 1 
ATOM   6791  C  CG2 . ILE   D  1 59  ? 62.122 -36.854 59.902  1.00 19.82 ? 59   ILE   D CG2 1 
ATOM   6792  C  CD1 . ILE   D  1 59  ? 63.646 -39.456 60.476  1.00 21.11 ? 59   ILE   D CD1 1 
ATOM   6793  N  N   . LEU   D  1 60  ? 59.006 -39.477 59.042  1.00 18.28 ? 60   LEU   D N   1 
ATOM   6794  C  CA  . LEU   D  1 60  ? 57.685 -39.677 59.619  1.00 19.01 ? 60   LEU   D CA  1 
ATOM   6795  C  C   . LEU   D  1 60  ? 57.755 -40.819 60.604  1.00 17.68 ? 60   LEU   D C   1 
ATOM   6796  O  O   . LEU   D  1 60  ? 58.271 -41.894 60.275  1.00 18.84 ? 60   LEU   D O   1 
ATOM   6797  C  CB  . LEU   D  1 60  ? 56.672 -40.056 58.523  1.00 17.70 ? 60   LEU   D CB  1 
ATOM   6798  C  CG  . LEU   D  1 60  ? 55.301 -40.565 58.976  1.00 17.04 ? 60   LEU   D CG  1 
ATOM   6799  C  CD1 . LEU   D  1 60  ? 54.434 -39.437 59.538  1.00 18.74 ? 60   LEU   D CD1 1 
ATOM   6800  C  CD2 . LEU   D  1 60  ? 54.538 -41.138 57.758  1.00 19.37 ? 60   LEU   D CD2 1 
ATOM   6801  N  N   . ASN   D  1 61  ? 57.218 -40.624 61.797  1.00 17.40 ? 61   ASN   D N   1 
ATOM   6802  C  CA  . ASN   D  1 61  ? 56.975 -41.758 62.709  1.00 15.31 ? 61   ASN   D CA  1 
ATOM   6803  C  C   . ASN   D  1 61  ? 55.597 -42.323 62.338  1.00 14.99 ? 61   ASN   D C   1 
ATOM   6804  O  O   . ASN   D  1 61  ? 54.565 -41.631 62.477  1.00 16.43 ? 61   ASN   D O   1 
ATOM   6805  C  CB  . ASN   D  1 61  ? 57.006 -41.228 64.153  1.00 17.69 ? 61   ASN   D CB  1 
ATOM   6806  C  CG  . ASN   D  1 61  ? 56.671 -42.297 65.178  1.00 17.20 ? 61   ASN   D CG  1 
ATOM   6807  O  OD1 . ASN   D  1 61  ? 55.989 -43.290 64.876  1.00 16.38 ? 61   ASN   D OD1 1 
ATOM   6808  N  ND2 . ASN   D  1 61  ? 57.177 -42.124 66.402  1.00 18.29 ? 61   ASN   D ND2 1 
ATOM   6809  N  N   . ASN   D  1 62  ? 55.571 -43.527 61.767  1.00 16.12 ? 62   ASN   D N   1 
ATOM   6810  C  CA  . ASN   D  1 62  ? 54.288 -44.093 61.333  1.00 15.77 ? 62   ASN   D CA  1 
ATOM   6811  C  C   . ASN   D  1 62  ? 53.658 -44.999 62.374  1.00 13.87 ? 62   ASN   D C   1 
ATOM   6812  O  O   . ASN   D  1 62  ? 52.709 -45.719 62.054  1.00 17.12 ? 62   ASN   D O   1 
ATOM   6813  C  CB  . ASN   D  1 62  ? 54.431 -44.813 59.976  1.00 14.43 ? 62   ASN   D CB  1 
ATOM   6814  C  CG  . ASN   D  1 62  ? 55.197 -46.149 60.083  1.00 16.22 ? 62   ASN   D CG  1 
ATOM   6815  O  OD1 . ASN   D  1 62  ? 55.742 -46.446 61.131  1.00 15.87 ? 62   ASN   D OD1 1 
ATOM   6816  N  ND2 . ASN   D  1 62  ? 55.259 -46.918 58.992  1.00 15.69 ? 62   ASN   D ND2 1 
ATOM   6817  N  N   . GLY   D  1 63  ? 54.148 -44.928 63.616  1.00 15.65 ? 63   GLY   D N   1 
ATOM   6818  C  CA  . GLY   D  1 63  ? 53.636 -45.768 64.695  1.00 16.19 ? 63   GLY   D CA  1 
ATOM   6819  C  C   . GLY   D  1 63  ? 54.182 -47.180 64.684  1.00 17.31 ? 63   GLY   D C   1 
ATOM   6820  O  O   . GLY   D  1 63  ? 53.759 -48.002 65.523  1.00 19.02 ? 63   GLY   D O   1 
ATOM   6821  N  N   . HIS   D  1 64  ? 55.087 -47.495 63.750  1.00 15.92 ? 64   HIS   D N   1 
ATOM   6822  C  CA  . HIS   D  1 64  ? 55.712 -48.799 63.585  1.00 14.04 ? 64   HIS   D CA  1 
ATOM   6823  C  C   . HIS   D  1 64  ? 57.210 -48.647 63.551  1.00 17.79 ? 64   HIS   D C   1 
ATOM   6824  O  O   . HIS   D  1 64  ? 57.936 -49.407 64.228  1.00 19.11 ? 64   HIS   D O   1 
ATOM   6825  C  CB  . HIS   D  1 64  ? 55.230 -49.504 62.297  1.00 15.38 ? 64   HIS   D CB  1 
ATOM   6826  C  CG  . HIS   D  1 64  ? 53.738 -49.528 62.117  1.00 14.01 ? 64   HIS   D CG  1 
ATOM   6827  N  ND1 . HIS   D  1 64  ? 52.902 -50.259 62.948  1.00 14.90 ? 64   HIS   D ND1 1 
ATOM   6828  C  CD2 . HIS   D  1 64  ? 52.935 -48.947 61.188  1.00 14.78 ? 64   HIS   D CD2 1 
ATOM   6829  C  CE1 . HIS   D  1 64  ? 51.645 -50.133 62.520  1.00 17.23 ? 64   HIS   D CE1 1 
ATOM   6830  N  NE2 . HIS   D  1 64  ? 51.641 -49.338 61.456  1.00 15.31 ? 64   HIS   D NE2 1 
ATOM   6831  N  N   . THR   D  1 65  ? 57.691 -47.662 62.826  1.00 15.20 ? 65   THR   D N   1 
ATOM   6832  C  CA  . THR   D  1 65  ? 59.093 -47.315 62.646  1.00 14.92 ? 65   THR   D CA  1 
ATOM   6833  C  C   . THR   D  1 65  ? 59.147 -45.837 62.252  1.00 16.03 ? 65   THR   D C   1 
ATOM   6834  O  O   . THR   D  1 65  ? 58.159 -45.109 62.426  1.00 16.08 ? 65   THR   D O   1 
ATOM   6835  C  CB  . THR   D  1 65  ? 59.732 -48.234 61.609  1.00 15.37 ? 65   THR   D CB  1 
ATOM   6836  O  OG1 . THR   D  1 65  ? 61.138 -47.936 61.580  1.00 17.72 ? 65   THR   D OG1 1 
ATOM   6837  C  CG2 . THR   D  1 65  ? 59.185 -48.021 60.203  1.00 16.27 ? 65   THR   D CG2 1 
ATOM   6838  N  N   . PHE   D  1 66  ? 60.310 -45.357 61.780  1.00 16.11 ? 66   PHE   D N   1 
ATOM   6839  C  CA  . PHE   D  1 66  ? 60.357 -44.049 61.137  1.00 14.86 ? 66   PHE   D CA  1 
ATOM   6840  C  C   . PHE   D  1 66  ? 60.803 -44.252 59.691  1.00 15.37 ? 66   PHE   D C   1 
ATOM   6841  O  O   . PHE   D  1 66  ? 61.689 -45.058 59.404  1.00 16.76 ? 66   PHE   D O   1 
ATOM   6842  C  CB  . PHE   D  1 66  ? 61.260 -43.011 61.881  1.00 16.81 ? 66   PHE   D CB  1 
ATOM   6843  C  CG  . PHE   D  1 66  ? 62.709 -43.400 61.948  1.00 16.61 ? 66   PHE   D CG  1 
ATOM   6844  C  CD1 . PHE   D  1 66  ? 63.579 -43.014 60.950  1.00 18.18 ? 66   PHE   D CD1 1 
ATOM   6845  C  CD2 . PHE   D  1 66  ? 63.217 -44.113 63.048  1.00 18.14 ? 66   PHE   D CD2 1 
ATOM   6846  C  CE1 . PHE   D  1 66  ? 64.940 -43.371 61.018  1.00 18.40 ? 66   PHE   D CE1 1 
ATOM   6847  C  CE2 . PHE   D  1 66  ? 64.556 -44.493 63.120  1.00 19.41 ? 66   PHE   D CE2 1 
ATOM   6848  C  CZ  . PHE   D  1 66  ? 65.449 -44.081 62.124  1.00 20.13 ? 66   PHE   D CZ  1 
ATOM   6849  N  N   . ASN   D  1 67  ? 60.120 -43.563 58.771  1.00 17.03 ? 67   ASN   D N   1 
ATOM   6850  C  CA  . ASN   D  1 67  ? 60.394 -43.635 57.349  1.00 16.71 ? 67   ASN   D CA  1 
ATOM   6851  C  C   . ASN   D  1 67  ? 60.979 -42.312 56.893  1.00 17.44 ? 67   ASN   D C   1 
ATOM   6852  O  O   . ASN   D  1 67  ? 60.381 -41.230 57.166  1.00 18.52 ? 67   ASN   D O   1 
ATOM   6853  C  CB  . ASN   D  1 67  ? 59.121 -43.850 56.538  1.00 16.65 ? 67   ASN   D CB  1 
ATOM   6854  C  CG  . ASN   D  1 67  ? 58.440 -45.143 56.803  1.00 18.09 ? 67   ASN   D CG  1 
ATOM   6855  O  OD1 . ASN   D  1 67  ? 59.061 -46.109 57.319  1.00 17.60 ? 67   ASN   D OD1 1 
ATOM   6856  N  ND2 . ASN   D  1 67  ? 57.158 -45.211 56.446  1.00 19.81 ? 67   ASN   D ND2 1 
ATOM   6857  N  N   . VAL   D  1 68  ? 62.098 -42.363 56.163  1.00 18.17 ? 68   VAL   D N   1 
ATOM   6858  C  CA  . VAL   D  1 68  ? 62.634 -41.190 55.489  1.00 18.45 ? 68   VAL   D CA  1 
ATOM   6859  C  C   . VAL   D  1 68  ? 62.200 -41.276 54.037  1.00 19.04 ? 68   VAL   D C   1 
ATOM   6860  O  O   . VAL   D  1 68  ? 62.550 -42.237 53.334  1.00 19.23 ? 68   VAL   D O   1 
ATOM   6861  C  CB  . VAL   D  1 68  ? 64.168 -41.126 55.619  1.00 18.38 ? 68   VAL   D CB  1 
ATOM   6862  C  CG1 . VAL   D  1 68  ? 64.727 -40.055 54.681  1.00 21.43 ? 68   VAL   D CG1 1 
ATOM   6863  C  CG2 . VAL   D  1 68  ? 64.588 -40.870 57.087  1.00 18.39 ? 68   VAL   D CG2 1 
ATOM   6864  N  N   . GLU   D  1 69  ? 61.410 -40.300 53.575  1.00 18.66 ? 69   GLU   D N   1 
ATOM   6865  C  CA  . GLU   D  1 69  ? 60.759 -40.332 52.273  1.00 21.25 ? 69   GLU   D CA  1 
ATOM   6866  C  C   . GLU   D  1 69  ? 61.568 -39.505 51.286  1.00 20.43 ? 69   GLU   D C   1 
ATOM   6867  O  O   . GLU   D  1 69  ? 62.090 -38.430 51.648  1.00 22.62 ? 69   GLU   D O   1 
ATOM   6868  C  CB  . GLU   D  1 69  ? 59.337 -39.747 52.380  1.00 26.92 ? 69   GLU   D CB  1 
ATOM   6869  C  CG  . GLU   D  1 69  ? 58.505 -39.787 51.118  1.00 38.24 ? 69   GLU   D CG  1 
ATOM   6870  C  CD  . GLU   D  1 69  ? 57.324 -38.761 51.128  1.00 47.40 ? 69   GLU   D CD  1 
ATOM   6871  O  OE1 . GLU   D  1 69  ? 57.086 -38.078 52.165  1.00 48.12 ? 69   GLU   D OE1 1 
ATOM   6872  O  OE2 . GLU   D  1 69  ? 56.667 -38.608 50.066  1.00 50.29 ? 69   GLU   D OE2 1 
ATOM   6873  N  N   . PHE   D  1 70  ? 61.629 -39.972 50.039  1.00 18.11 ? 70   PHE   D N   1 
ATOM   6874  C  CA  . PHE   D  1 70  ? 62.316 -39.327 48.924  1.00 19.91 ? 70   PHE   D CA  1 
ATOM   6875  C  C   . PHE   D  1 70  ? 61.362 -38.944 47.803  1.00 23.36 ? 70   PHE   D C   1 
ATOM   6876  O  O   . PHE   D  1 70  ? 60.294 -39.528 47.628  1.00 23.82 ? 70   PHE   D O   1 
ATOM   6877  C  CB  . PHE   D  1 70  ? 63.385 -40.257 48.344  1.00 20.41 ? 70   PHE   D CB  1 
ATOM   6878  C  CG  . PHE   D  1 70  ? 64.533 -40.492 49.272  1.00 20.47 ? 70   PHE   D CG  1 
ATOM   6879  C  CD1 . PHE   D  1 70  ? 64.379 -41.351 50.371  1.00 22.51 ? 70   PHE   D CD1 1 
ATOM   6880  C  CD2 . PHE   D  1 70  ? 65.739 -39.835 49.086  1.00 21.03 ? 70   PHE   D CD2 1 
ATOM   6881  C  CE1 . PHE   D  1 70  ? 65.465 -41.544 51.249  1.00 20.51 ? 70   PHE   D CE1 1 
ATOM   6882  C  CE2 . PHE   D  1 70  ? 66.809 -40.012 49.951  1.00 21.69 ? 70   PHE   D CE2 1 
ATOM   6883  C  CZ  . PHE   D  1 70  ? 66.650 -40.869 51.054  1.00 21.63 ? 70   PHE   D CZ  1 
ATOM   6884  N  N   . ASP   D  1 71  ? 61.771 -37.937 47.023  1.00 22.51 ? 71   ASP   D N   1 
ATOM   6885  C  CA  . ASP   D  1 71  ? 61.046 -37.607 45.804  1.00 22.07 ? 71   ASP   D CA  1 
ATOM   6886  C  C   . ASP   D  1 71  ? 61.314 -38.728 44.797  1.00 23.63 ? 71   ASP   D C   1 
ATOM   6887  O  O   . ASP   D  1 71  ? 62.460 -38.954 44.417  1.00 26.97 ? 71   ASP   D O   1 
ATOM   6888  C  CB  . ASP   D  1 71  ? 61.541 -36.255 45.295  1.00 25.86 ? 71   ASP   D CB  1 
ATOM   6889  C  CG  . ASP   D  1 71  ? 60.779 -35.774 44.063  1.00 26.23 ? 71   ASP   D CG  1 
ATOM   6890  O  OD1 . ASP   D  1 71  ? 60.433 -36.617 43.217  1.00 27.15 ? 71   ASP   D OD1 1 
ATOM   6891  O  OD2 . ASP   D  1 71  ? 60.565 -34.527 43.897  1.00 28.46 ? 71   ASP   D OD2 1 
ATOM   6892  N  N   . ASP   D  1 72  ? 60.299 -39.531 44.471  1.00 21.45 ? 72   ASP   D N   1 
ATOM   6893  C  CA  . ASP   D  1 72  ? 60.458 -40.633 43.528  1.00 19.92 ? 72   ASP   D CA  1 
ATOM   6894  C  C   . ASP   D  1 72  ? 59.799 -40.344 42.178  1.00 22.82 ? 72   ASP   D C   1 
ATOM   6895  O  O   . ASP   D  1 72  ? 59.338 -41.282 41.499  1.00 22.36 ? 72   ASP   D O   1 
ATOM   6896  C  CB  . ASP   D  1 72  ? 59.880 -41.921 44.128  1.00 20.42 ? 72   ASP   D CB  1 
ATOM   6897  C  CG  . ASP   D  1 72  ? 58.383 -41.803 44.414  1.00 21.32 ? 72   ASP   D CG  1 
ATOM   6898  O  OD1 . ASP   D  1 72  ? 57.799 -40.677 44.347  1.00 23.62 ? 72   ASP   D OD1 1 
ATOM   6899  O  OD2 . ASP   D  1 72  ? 57.752 -42.844 44.726  1.00 22.08 ? 72   ASP   D OD2 1 
ATOM   6900  N  N   . SER   D  1 73  ? 59.789 -39.069 41.756  1.00 23.29 ? 73   SER   D N   1 
ATOM   6901  C  CA  . SER   D  1 73  ? 59.121 -38.722 40.521  1.00 24.40 ? 73   SER   D CA  1 
ATOM   6902  C  C   . SER   D  1 73  ? 59.993 -38.927 39.298  1.00 28.53 ? 73   SER   D C   1 
ATOM   6903  O  O   . SER   D  1 73  ? 59.486 -38.793 38.176  1.00 29.79 ? 73   SER   D O   1 
ATOM   6904  C  CB  . SER   D  1 73  ? 58.647 -37.274 40.582  1.00 25.23 ? 73   SER   D CB  1 
ATOM   6905  O  OG  . SER   D  1 73  ? 59.750 -36.370 40.594  1.00 26.59 ? 73   SER   D OG  1 
ATOM   6906  N  N   . GLN   D  1 74  ? 61.289 -39.185 39.485  1.00 24.07 ? 74   GLN   D N   1 
ATOM   6907  C  CA  . GLN   D  1 74  ? 62.211 -39.303 38.365  1.00 24.93 ? 74   GLN   D CA  1 
ATOM   6908  C  C   . GLN   D  1 74  ? 63.148 -40.473 38.569  1.00 25.22 ? 74   GLN   D C   1 
ATOM   6909  O  O   . GLN   D  1 74  ? 63.360 -40.941 39.695  1.00 26.68 ? 74   GLN   D O   1 
ATOM   6910  C  CB  . GLN   D  1 74  ? 63.039 -38.038 38.173  1.00 27.28 ? 74   GLN   D CB  1 
ATOM   6911  C  CG  . GLN   D  1 74  ? 62.191 -36.847 37.831  1.00 26.35 ? 74   GLN   D CG  1 
ATOM   6912  C  CD  . GLN   D  1 74  ? 63.034 -35.610 37.578  1.00 32.39 ? 74   GLN   D CD  1 
ATOM   6913  O  OE1 . GLN   D  1 74  ? 63.857 -35.217 38.413  1.00 33.06 ? 74   GLN   D OE1 1 
ATOM   6914  N  NE2 . GLN   D  1 74  ? 62.853 -35.006 36.401  1.00 33.80 ? 74   GLN   D NE2 1 
ATOM   6915  N  N   . ASP   D  1 75  ? 63.709 -40.945 37.439  1.00 28.64 ? 75   ASP   D N   1 
ATOM   6916  C  CA  . ASP   D  1 75  ? 64.623 -42.096 37.433  1.00 31.34 ? 75   ASP   D CA  1 
ATOM   6917  C  C   . ASP   D  1 75  ? 66.014 -41.648 37.883  1.00 35.16 ? 75   ASP   D C   1 
ATOM   6918  O  O   . ASP   D  1 75  ? 67.008 -41.790 37.172  1.00 39.61 ? 75   ASP   D O   1 
ATOM   6919  C  CB  . ASP   D  1 75  ? 64.700 -42.732 36.047  1.00 34.96 ? 75   ASP   D CB  1 
ATOM   6920  C  CG  . ASP   D  1 75  ? 63.515 -43.600 35.701  1.00 35.25 ? 75   ASP   D CG  1 
ATOM   6921  O  OD1 . ASP   D  1 75  ? 62.679 -43.864 36.567  1.00 31.48 ? 75   ASP   D OD1 1 
ATOM   6922  O  OD2 . ASP   D  1 75  ? 63.442 -44.065 34.531  1.00 38.95 ? 75   ASP   D OD2 1 
ATOM   6923  N  N   . LYS   D  1 76  ? 66.075 -41.053 39.066  1.00 31.94 ? 76   LYS   D N   1 
ATOM   6924  C  CA  . LYS   D  1 76  ? 67.356 -40.560 39.554  1.00 31.60 ? 76   LYS   D CA  1 
ATOM   6925  C  C   . LYS   D  1 76  ? 67.894 -41.526 40.601  1.00 33.56 ? 76   LYS   D C   1 
ATOM   6926  O  O   . LYS   D  1 76  ? 68.810 -42.302 40.288  1.00 37.29 ? 76   LYS   D O   1 
ATOM   6927  C  CB  . LYS   D  1 76  ? 67.222 -39.137 40.075  1.00 32.70 ? 76   LYS   D CB  1 
ATOM   6928  C  CG  . LYS   D  1 76  ? 67.073 -38.131 38.890  1.00 34.85 ? 76   LYS   D CG  1 
ATOM   6929  C  CD  . LYS   D  1 76  ? 66.939 -36.649 39.330  1.00 35.23 ? 76   LYS   D CD  1 
ATOM   6930  C  CE  . LYS   D  1 76  ? 67.063 -35.748 38.092  1.00 36.93 ? 76   LYS   D CE  1 
ATOM   6931  N  NZ  . LYS   D  1 76  ? 66.584 -34.353 38.282  1.00 38.03 ? 76   LYS   D NZ  1 
ATOM   6932  N  N   . ALA   D  1 77  ? 67.307 -41.567 41.803  1.00 28.08 ? 77   ALA   D N   1 
ATOM   6933  C  CA  . ALA   D  1 77  ? 67.800 -42.496 42.811  1.00 25.82 ? 77   ALA   D CA  1 
ATOM   6934  C  C   . ALA   D  1 77  ? 67.186 -43.856 42.515  1.00 26.42 ? 77   ALA   D C   1 
ATOM   6935  O  O   . ALA   D  1 77  ? 66.003 -44.087 42.794  1.00 24.42 ? 77   ALA   D O   1 
ATOM   6936  C  CB  . ALA   D  1 77  ? 67.454 -42.018 44.215  1.00 28.73 ? 77   ALA   D CB  1 
ATOM   6937  N  N   . VAL   D  1 78  ? 67.974 -44.771 41.948  1.00 26.00 ? 78   VAL   D N   1 
ATOM   6938  C  CA  . VAL   D  1 78  ? 67.428 -46.026 41.458  1.00 26.04 ? 78   VAL   D CA  1 
ATOM   6939  C  C   . VAL   D  1 78  ? 68.357 -47.172 41.786  1.00 24.58 ? 78   VAL   D C   1 
ATOM   6940  O  O   . VAL   D  1 78  ? 69.561 -46.999 41.992  1.00 28.63 ? 78   VAL   D O   1 
ATOM   6941  C  CB  . VAL   D  1 78  ? 67.188 -46.033 39.935  1.00 25.91 ? 78   VAL   D CB  1 
ATOM   6942  C  CG1 . VAL   D  1 78  ? 66.244 -44.904 39.537  1.00 26.93 ? 78   VAL   D CG1 1 
ATOM   6943  C  CG2 . VAL   D  1 78  ? 68.450 -45.920 39.200  1.00 29.24 ? 78   VAL   D CG2 1 
ATOM   6944  N  N   . LEU   D  1 79  ? 67.761 -48.364 41.761  1.00 23.47 ? 79   LEU   D N   1 
ATOM   6945  C  CA  . LEU   D  1 79  ? 68.460 -49.627 41.835  1.00 24.75 ? 79   LEU   D CA  1 
ATOM   6946  C  C   . LEU   D  1 79  ? 68.204 -50.357 40.519  1.00 26.69 ? 79   LEU   D C   1 
ATOM   6947  O  O   . LEU   D  1 79  ? 67.054 -50.406 40.058  1.00 28.39 ? 79   LEU   D O   1 
ATOM   6948  C  CB  . LEU   D  1 79  ? 67.902 -50.391 43.032  1.00 26.68 ? 79   LEU   D CB  1 
ATOM   6949  C  CG  . LEU   D  1 79  ? 68.528 -51.625 43.555  1.00 30.65 ? 79   LEU   D CG  1 
ATOM   6950  C  CD1 . LEU   D  1 79  ? 69.879 -51.172 44.036  1.00 33.88 ? 79   LEU   D CD1 1 
ATOM   6951  C  CD2 . LEU   D  1 79  ? 67.663 -52.045 44.695  1.00 22.47 ? 79   LEU   D CD2 1 
ATOM   6952  N  N   . LYS   D  1 80  ? 69.257 -50.907 39.903  1.00 26.07 ? 80   LYS   D N   1 
ATOM   6953  C  CA  . LYS   D  1 80  ? 69.161 -51.642 38.641  1.00 28.64 ? 80   LYS   D CA  1 
ATOM   6954  C  C   . LYS   D  1 80  ? 70.160 -52.796 38.690  1.00 29.45 ? 80   LYS   D C   1 
ATOM   6955  O  O   . LYS   D  1 80  ? 71.033 -52.842 39.553  1.00 29.45 ? 80   LYS   D O   1 
ATOM   6956  C  CB  . LYS   D  1 80  ? 69.443 -50.778 37.395  1.00 34.49 ? 80   LYS   D CB  1 
ATOM   6957  C  CG  . LYS   D  1 80  ? 68.481 -49.581 37.198  1.00 36.70 ? 80   LYS   D CG  1 
ATOM   6958  C  CD  . LYS   D  1 80  ? 68.605 -48.983 35.804  1.00 38.84 ? 80   LYS   D CD  1 
ATOM   6959  C  CE  . LYS   D  1 80  ? 69.997 -48.602 35.506  1.00 47.36 ? 80   LYS   D CE  1 
ATOM   6960  N  NZ  . LYS   D  1 80  ? 70.588 -47.937 36.689  1.00 50.73 ? 80   LYS   D NZ  1 
ATOM   6961  N  N   . GLY   D  1 81  ? 70.014 -53.749 37.749  1.00 27.38 ? 81   GLY   D N   1 
ATOM   6962  C  CA  . GLY   D  1 81  ? 70.938 -54.873 37.682  1.00 28.50 ? 81   GLY   D CA  1 
ATOM   6963  C  C   . GLY   D  1 81  ? 70.676 -55.900 38.779  1.00 27.79 ? 81   GLY   D C   1 
ATOM   6964  O  O   . GLY   D  1 81  ? 69.587 -56.002 39.359  1.00 25.71 ? 81   GLY   D O   1 
ATOM   6965  N  N   . GLY   D  1 82  ? 71.716 -56.688 39.050  1.00 28.84 ? 82   GLY   D N   1 
ATOM   6966  C  CA  . GLY   D  1 82  ? 71.583 -57.797 39.964  1.00 29.62 ? 82   GLY   D CA  1 
ATOM   6967  C  C   . GLY   D  1 82  ? 70.492 -58.732 39.491  1.00 27.09 ? 82   GLY   D C   1 
ATOM   6968  O  O   . GLY   D  1 82  ? 70.482 -59.158 38.339  1.00 30.92 ? 82   GLY   D O   1 
ATOM   6969  N  N   . PRO   D  1 83  ? 69.546 -59.069 40.379  1.00 26.34 ? 83   PRO   D N   1 
ATOM   6970  C  CA  . PRO   D  1 83  ? 68.412 -59.912 39.986  1.00 27.75 ? 83   PRO   D CA  1 
ATOM   6971  C  C   . PRO   D  1 83  ? 67.288 -59.157 39.298  1.00 29.98 ? 83   PRO   D C   1 
ATOM   6972  O  O   . PRO   D  1 83  ? 66.290 -59.798 38.932  1.00 32.14 ? 83   PRO   D O   1 
ATOM   6973  C  CB  . PRO   D  1 83  ? 67.930 -60.471 41.341  1.00 22.99 ? 83   PRO   D CB  1 
ATOM   6974  C  CG  . PRO   D  1 83  ? 68.159 -59.301 42.276  1.00 22.53 ? 83   PRO   D CG  1 
ATOM   6975  C  CD  . PRO   D  1 83  ? 69.493 -58.703 41.797  1.00 24.68 ? 83   PRO   D CD  1 
ATOM   6976  N  N   . LEU   D  1 84  ? 67.413 -57.826 39.131  1.00 24.96 ? 84   LEU   D N   1 
ATOM   6977  C  CA  . LEU   D  1 84  ? 66.286 -56.993 38.728  1.00 24.02 ? 84   LEU   D CA  1 
ATOM   6978  C  C   . LEU   D  1 84  ? 66.225 -56.871 37.215  1.00 24.58 ? 84   LEU   D C   1 
ATOM   6979  O  O   . LEU   D  1 84  ? 67.245 -56.657 36.548  1.00 27.89 ? 84   LEU   D O   1 
ATOM   6980  C  CB  . LEU   D  1 84  ? 66.406 -55.594 39.331  1.00 21.96 ? 84   LEU   D CB  1 
ATOM   6981  C  CG  . LEU   D  1 84  ? 66.602 -55.666 40.848  1.00 22.56 ? 84   LEU   D CG  1 
ATOM   6982  C  CD1 . LEU   D  1 84  ? 66.869 -54.237 41.410  1.00 24.75 ? 84   LEU   D CD1 1 
ATOM   6983  C  CD2 . LEU   D  1 84  ? 65.353 -56.304 41.549  1.00 22.09 ? 84   LEU   D CD2 1 
ATOM   6984  N  N   . ASP   D  1 85  ? 65.006 -56.921 36.696  1.00 28.27 ? 85   ASP   D N   1 
ATOM   6985  C  CA  . ASP   D  1 85  ? 64.709 -56.457 35.348  1.00 30.03 ? 85   ASP   D CA  1 
ATOM   6986  C  C   . ASP   D  1 85  ? 64.127 -55.054 35.434  1.00 27.70 ? 85   ASP   D C   1 
ATOM   6987  O  O   . ASP   D  1 85  ? 63.160 -54.827 36.180  1.00 29.67 ? 85   ASP   D O   1 
ATOM   6988  C  CB  . ASP   D  1 85  ? 63.726 -57.406 34.678  1.00 33.44 ? 85   ASP   D CB  1 
ATOM   6989  C  CG  . ASP   D  1 85  ? 64.317 -58.792 34.511  1.00 41.16 ? 85   ASP   D CG  1 
ATOM   6990  O  OD1 . ASP   D  1 85  ? 65.465 -58.885 34.014  1.00 44.48 ? 85   ASP   D OD1 1 
ATOM   6991  O  OD2 . ASP   D  1 85  ? 63.657 -59.775 34.917  1.00 43.02 ? 85   ASP   D OD2 1 
ATOM   6992  N  N   . GLY   D  1 86  ? 64.713 -54.105 34.698  1.00 29.22 ? 86   GLY   D N   1 
ATOM   6993  C  CA  . GLY   D  1 86  ? 64.189 -52.744 34.709  1.00 30.16 ? 86   GLY   D CA  1 
ATOM   6994  C  C   . GLY   D  1 86  ? 64.781 -51.869 35.802  1.00 30.46 ? 86   GLY   D C   1 
ATOM   6995  O  O   . GLY   D  1 86  ? 65.851 -52.131 36.362  1.00 31.45 ? 86   GLY   D O   1 
ATOM   6996  N  N   . THR   D  1 87  ? 64.040 -50.809 36.128  1.00 25.60 ? 87   THR   D N   1 
ATOM   6997  C  CA  . THR   D  1 87  ? 64.548 -49.753 36.979  1.00 24.57 ? 87   THR   D CA  1 
ATOM   6998  C  C   . THR   D  1 87  ? 63.645 -49.643 38.191  1.00 25.73 ? 87   THR   D C   1 
ATOM   6999  O  O   . THR   D  1 87  ? 62.409 -49.604 38.041  1.00 26.37 ? 87   THR   D O   1 
ATOM   7000  C  CB  . THR   D  1 87  ? 64.564 -48.423 36.222  1.00 26.81 ? 87   THR   D CB  1 
ATOM   7001  O  OG1 . THR   D  1 87  ? 65.485 -48.505 35.115  1.00 30.34 ? 87   THR   D OG1 1 
ATOM   7002  C  CG2 . THR   D  1 87  ? 64.959 -47.264 37.147  1.00 27.02 ? 87   THR   D CG2 1 
ATOM   7003  N  N   . TYR   D  1 88  ? 64.240 -49.585 39.391  1.00 24.07 ? 88   TYR   D N   1 
ATOM   7004  C  CA  . TYR   D  1 88  ? 63.451 -49.499 40.637  1.00 21.65 ? 88   TYR   D CA  1 
ATOM   7005  C  C   . TYR   D  1 88  ? 63.804 -48.211 41.376  1.00 22.64 ? 88   TYR   D C   1 
ATOM   7006  O  O   . TYR   D  1 88  ? 64.974 -47.987 41.719  1.00 22.55 ? 88   TYR   D O   1 
ATOM   7007  C  CB  . TYR   D  1 88  ? 63.705 -50.704 41.539  1.00 20.91 ? 88   TYR   D CB  1 
ATOM   7008  C  CG  . TYR   D  1 88  ? 63.097 -52.000 41.051  1.00 19.61 ? 88   TYR   D CG  1 
ATOM   7009  C  CD1 . TYR   D  1 88  ? 63.579 -52.636 39.889  1.00 19.95 ? 88   TYR   D CD1 1 
ATOM   7010  C  CD2 . TYR   D  1 88  ? 62.068 -52.600 41.776  1.00 19.11 ? 88   TYR   D CD2 1 
ATOM   7011  C  CE1 . TYR   D  1 88  ? 63.038 -53.871 39.451  1.00 20.42 ? 88   TYR   D CE1 1 
ATOM   7012  C  CE2 . TYR   D  1 88  ? 61.509 -53.805 41.359  1.00 18.48 ? 88   TYR   D CE2 1 
ATOM   7013  C  CZ  . TYR   D  1 88  ? 61.991 -54.446 40.195  1.00 21.05 ? 88   TYR   D CZ  1 
ATOM   7014  O  OH  . TYR   D  1 88  ? 61.463 -55.683 39.789  1.00 22.76 ? 88   TYR   D OH  1 
ATOM   7015  N  N   . ARG   D  1 89  ? 62.800 -47.352 41.608  1.00 22.14 ? 89   ARG   D N   1 
ATOM   7016  C  CA  . ARG   D  1 89  ? 63.037 -46.037 42.205  1.00 21.38 ? 89   ARG   D CA  1 
ATOM   7017  C  C   . ARG   D  1 89  ? 63.004 -46.120 43.719  1.00 20.33 ? 89   ARG   D C   1 
ATOM   7018  O  O   . ARG   D  1 89  ? 62.076 -46.697 44.283  1.00 20.15 ? 89   ARG   D O   1 
ATOM   7019  C  CB  . ARG   D  1 89  ? 61.995 -45.020 41.752  1.00 20.59 ? 89   ARG   D CB  1 
ATOM   7020  C  CG  . ARG   D  1 89  ? 62.154 -44.549 40.312  1.00 23.26 ? 89   ARG   D CG  1 
ATOM   7021  C  CD  . ARG   D  1 89  ? 61.142 -43.412 40.057  1.00 22.78 ? 89   ARG   D CD  1 
ATOM   7022  N  NE  . ARG   D  1 89  ? 61.036 -43.182 38.606  1.00 24.10 ? 89   ARG   D NE  1 
ATOM   7023  C  CZ  . ARG   D  1 89  ? 60.038 -42.518 38.042  1.00 22.82 ? 89   ARG   D CZ  1 
ATOM   7024  N  NH1 . ARG   D  1 89  ? 59.069 -41.990 38.798  1.00 24.89 ? 89   ARG   D NH1 1 
ATOM   7025  N  NH2 . ARG   D  1 89  ? 60.008 -42.409 36.713  1.00 29.15 ? 89   ARG   D NH2 1 
ATOM   7026  N  N   . LEU   D  1 90  ? 63.996 -45.506 44.376  1.00 19.84 ? 90   LEU   D N   1 
ATOM   7027  C  CA  . LEU   D  1 90  ? 63.966 -45.358 45.834  1.00 18.91 ? 90   LEU   D CA  1 
ATOM   7028  C  C   . LEU   D  1 90  ? 62.782 -44.484 46.276  1.00 18.38 ? 90   LEU   D C   1 
ATOM   7029  O  O   . LEU   D  1 90  ? 62.647 -43.338 45.815  1.00 20.76 ? 90   LEU   D O   1 
ATOM   7030  C  CB  . LEU   D  1 90  ? 65.278 -44.690 46.286  1.00 21.62 ? 90   LEU   D CB  1 
ATOM   7031  C  CG  . LEU   D  1 90  ? 65.374 -44.389 47.796  1.00 20.63 ? 90   LEU   D CG  1 
ATOM   7032  C  CD1 . LEU   D  1 90  ? 65.392 -45.700 48.594  1.00 20.89 ? 90   LEU   D CD1 1 
ATOM   7033  C  CD2 . LEU   D  1 90  ? 66.615 -43.519 48.065  1.00 21.66 ? 90   LEU   D CD2 1 
ATOM   7034  N  N   . ILE   D  1 91  ? 61.926 -45.012 47.166  1.00 17.69 ? 91   ILE   D N   1 
ATOM   7035  C  CA  . ILE   D  1 91  ? 60.854 -44.208 47.728  1.00 19.04 ? 91   ILE   D CA  1 
ATOM   7036  C  C   . ILE   D  1 91  ? 61.100 -43.838 49.191  1.00 17.14 ? 91   ILE   D C   1 
ATOM   7037  O  O   . ILE   D  1 91  ? 60.782 -42.717 49.604  1.00 18.03 ? 91   ILE   D O   1 
ATOM   7038  C  CB  . ILE   D  1 91  ? 59.468 -44.873 47.545  1.00 17.23 ? 91   ILE   D CB  1 
ATOM   7039  C  CG1 . ILE   D  1 91  ? 58.386 -43.990 48.192  1.00 20.66 ? 91   ILE   D CG1 1 
ATOM   7040  C  CG2 . ILE   D  1 91  ? 59.373 -46.269 48.164  1.00 18.30 ? 91   ILE   D CG2 1 
ATOM   7041  C  CD1 . ILE   D  1 91  ? 56.992 -44.392 47.730  1.00 21.05 ? 91   ILE   D CD1 1 
ATOM   7042  N  N   . GLN   D  1 92  ? 61.681 -44.738 49.989  1.00 16.18 ? 92   GLN   D N   1 
ATOM   7043  C  CA  . GLN   D  1 92  ? 61.878 -44.431 51.407  1.00 16.06 ? 92   GLN   D CA  1 
ATOM   7044  C  C   . GLN   D  1 92  ? 62.887 -45.423 51.973  1.00 16.11 ? 92   GLN   D C   1 
ATOM   7045  O  O   . GLN   D  1 92  ? 63.128 -46.502 51.387  1.00 18.24 ? 92   GLN   D O   1 
ATOM   7046  C  CB  . GLN   D  1 92  ? 60.567 -44.511 52.220  1.00 16.50 ? 92   GLN   D CB  1 
ATOM   7047  C  CG  . GLN   D  1 92  ? 59.858 -45.907 52.099  1.00 17.63 ? 92   GLN   D CG  1 
ATOM   7048  C  CD  . GLN   D  1 92  ? 59.911 -46.686 53.392  1.00 16.18 ? 92   GLN   D CD  1 
ATOM   7049  O  OE1 . GLN   D  1 92  ? 60.965 -46.854 54.007  1.00 17.40 ? 92   GLN   D OE1 1 
ATOM   7050  N  NE2 . GLN   D  1 92  ? 58.725 -47.177 53.825  1.00 19.36 ? 92   GLN   D NE2 1 
ATOM   7051  N  N   . PHE   D  1 93  ? 63.474 -45.056 53.128  1.00 17.48 ? 93   PHE   D N   1 
ATOM   7052  C  CA  . PHE   D  1 93  ? 64.127 -46.094 53.943  1.00 16.31 ? 93   PHE   D CA  1 
ATOM   7053  C  C   . PHE   D  1 93  ? 63.628 -46.019 55.390  1.00 17.86 ? 93   PHE   D C   1 
ATOM   7054  O  O   . PHE   D  1 93  ? 63.140 -44.993 55.845  1.00 16.36 ? 93   PHE   D O   1 
ATOM   7055  C  CB  . PHE   D  1 93  ? 65.687 -46.011 53.876  1.00 18.31 ? 93   PHE   D CB  1 
ATOM   7056  C  CG  . PHE   D  1 93  ? 66.284 -44.800 54.531  1.00 17.78 ? 93   PHE   D CG  1 
ATOM   7057  C  CD1 . PHE   D  1 93  ? 66.396 -44.698 55.942  1.00 17.00 ? 93   PHE   D CD1 1 
ATOM   7058  C  CD2 . PHE   D  1 93  ? 66.805 -43.779 53.733  1.00 18.80 ? 93   PHE   D CD2 1 
ATOM   7059  C  CE1 . PHE   D  1 93  ? 66.990 -43.583 56.511  1.00 19.67 ? 93   PHE   D CE1 1 
ATOM   7060  C  CE2 . PHE   D  1 93  ? 67.388 -42.669 54.306  1.00 19.46 ? 93   PHE   D CE2 1 
ATOM   7061  C  CZ  . PHE   D  1 93  ? 67.493 -42.566 55.681  1.00 20.58 ? 93   PHE   D CZ  1 
ATOM   7062  N  N   . HIS   D  1 94  ? 63.832 -47.102 56.131  1.00 16.77 ? 94   HIS   D N   1 
ATOM   7063  C  CA  . HIS   D  1 94  ? 63.456 -47.191 57.534  1.00 16.99 ? 94   HIS   D CA  1 
ATOM   7064  C  C   . HIS   D  1 94  ? 64.320 -48.278 58.151  1.00 17.10 ? 94   HIS   D C   1 
ATOM   7065  O  O   . HIS   D  1 94  ? 65.040 -48.974 57.441  1.00 17.10 ? 94   HIS   D O   1 
ATOM   7066  C  CB  . HIS   D  1 94  ? 61.974 -47.555 57.704  1.00 14.70 ? 94   HIS   D CB  1 
ATOM   7067  C  CG  . HIS   D  1 94  ? 61.647 -48.882 57.065  1.00 13.84 ? 94   HIS   D CG  1 
ATOM   7068  N  ND1 . HIS   D  1 94  ? 61.326 -49.019 55.727  1.00 14.64 ? 94   HIS   D ND1 1 
ATOM   7069  C  CD2 . HIS   D  1 94  ? 61.693 -50.129 57.570  1.00 15.68 ? 94   HIS   D CD2 1 
ATOM   7070  C  CE1 . HIS   D  1 94  ? 61.146 -50.299 55.434  1.00 14.83 ? 94   HIS   D CE1 1 
ATOM   7071  N  NE2 . HIS   D  1 94  ? 61.376 -51.006 56.537  1.00 13.40 ? 94   HIS   D NE2 1 
ATOM   7072  N  N   . PHE   D  1 95  ? 64.194 -48.473 59.472  1.00 17.12 ? 95   PHE   D N   1 
ATOM   7073  C  CA  . PHE   D  1 95  ? 64.968 -49.476 60.192  1.00 16.13 ? 95   PHE   D CA  1 
ATOM   7074  C  C   . PHE   D  1 95  ? 64.040 -50.366 61.012  1.00 17.19 ? 95   PHE   D C   1 
ATOM   7075  O  O   . PHE   D  1 95  ? 62.885 -50.022 61.317  1.00 17.81 ? 95   PHE   D O   1 
ATOM   7076  C  CB  . PHE   D  1 95  ? 66.012 -48.861 61.153  1.00 16.03 ? 95   PHE   D CB  1 
ATOM   7077  C  CG  . PHE   D  1 95  ? 67.014 -47.944 60.499  1.00 17.45 ? 95   PHE   D CG  1 
ATOM   7078  C  CD1 . PHE   D  1 95  ? 66.656 -46.639 60.147  1.00 18.47 ? 95   PHE   D CD1 1 
ATOM   7079  C  CD2 . PHE   D  1 95  ? 68.324 -48.364 60.241  1.00 18.89 ? 95   PHE   D CD2 1 
ATOM   7080  C  CE1 . PHE   D  1 95  ? 67.608 -45.795 59.595  1.00 17.61 ? 95   PHE   D CE1 1 
ATOM   7081  C  CE2 . PHE   D  1 95  ? 69.264 -47.504 59.662  1.00 19.96 ? 95   PHE   D CE2 1 
ATOM   7082  C  CZ  . PHE   D  1 95  ? 68.905 -46.220 59.346  1.00 21.42 ? 95   PHE   D CZ  1 
ATOM   7083  N  N   . HIS   D  1 96  ? 64.601 -51.511 61.409  1.00 16.61 ? 96   HIS   D N   1 
ATOM   7084  C  CA  . HIS   D  1 96  ? 64.032 -52.391 62.400  1.00 16.62 ? 96   HIS   D CA  1 
ATOM   7085  C  C   . HIS   D  1 96  ? 65.112 -52.576 63.471  1.00 16.64 ? 96   HIS   D C   1 
ATOM   7086  O  O   . HIS   D  1 96  ? 66.291 -52.695 63.142  1.00 17.81 ? 96   HIS   D O   1 
ATOM   7087  C  CB  . HIS   D  1 96  ? 63.681 -53.745 61.758  1.00 16.83 ? 96   HIS   D CB  1 
ATOM   7088  C  CG  . HIS   D  1 96  ? 62.706 -53.633 60.616  1.00 14.78 ? 96   HIS   D CG  1 
ATOM   7089  N  ND1 . HIS   D  1 96  ? 61.340 -53.839 60.766  1.00 16.62 ? 96   HIS   D ND1 1 
ATOM   7090  C  CD2 . HIS   D  1 96  ? 62.892 -53.260 59.315  1.00 14.59 ? 96   HIS   D CD2 1 
ATOM   7091  C  CE1 . HIS   D  1 96  ? 60.740 -53.638 59.588  1.00 15.80 ? 96   HIS   D CE1 1 
ATOM   7092  N  NE2 . HIS   D  1 96  ? 61.653 -53.271 58.698  1.00 14.79 ? 96   HIS   D NE2 1 
ATOM   7093  N  N   . TRP   D  1 97  ? 64.741 -52.572 64.760  1.00 16.33 ? 97   TRP   D N   1 
ATOM   7094  C  CA  . TRP   D  1 97  ? 65.740 -52.679 65.824  1.00 15.70 ? 97   TRP   D CA  1 
ATOM   7095  C  C   . TRP   D  1 97  ? 65.131 -53.309 67.066  1.00 18.19 ? 97   TRP   D C   1 
ATOM   7096  O  O   . TRP   D  1 97  ? 63.923 -53.543 67.147  1.00 17.21 ? 97   TRP   D O   1 
ATOM   7097  C  CB  . TRP   D  1 97  ? 66.335 -51.330 66.177  1.00 17.29 ? 97   TRP   D CB  1 
ATOM   7098  C  CG  . TRP   D  1 97  ? 65.305 -50.321 66.709  1.00 17.48 ? 97   TRP   D CG  1 
ATOM   7099  C  CD1 . TRP   D  1 97  ? 64.944 -50.107 68.010  1.00 18.97 ? 97   TRP   D CD1 1 
ATOM   7100  C  CD2 . TRP   D  1 97  ? 64.549 -49.380 65.912  1.00 17.39 ? 97   TRP   D CD2 1 
ATOM   7101  N  NE1 . TRP   D  1 97  ? 64.000 -49.084 68.084  1.00 18.63 ? 97   TRP   D NE1 1 
ATOM   7102  C  CE2 . TRP   D  1 97  ? 63.721 -48.646 66.807  1.00 18.26 ? 97   TRP   D CE2 1 
ATOM   7103  C  CE3 . TRP   D  1 97  ? 64.475 -49.121 64.531  1.00 15.83 ? 97   TRP   D CE3 1 
ATOM   7104  C  CZ2 . TRP   D  1 97  ? 62.862 -47.599 66.366  1.00 17.73 ? 97   TRP   D CZ2 1 
ATOM   7105  C  CZ3 . TRP   D  1 97  ? 63.606 -48.137 64.090  1.00 16.66 ? 97   TRP   D CZ3 1 
ATOM   7106  C  CH2 . TRP   D  1 97  ? 62.829 -47.357 65.015  1.00 17.68 ? 97   TRP   D CH2 1 
ATOM   7107  N  N   . GLY   D  1 98  ? 65.994 -53.597 68.046  1.00 17.88 ? 98   GLY   D N   1 
ATOM   7108  C  CA  . GLY   D  1 98  ? 65.599 -54.359 69.207  1.00 18.62 ? 98   GLY   D CA  1 
ATOM   7109  C  C   . GLY   D  1 98  ? 65.478 -53.503 70.464  1.00 19.93 ? 98   GLY   D C   1 
ATOM   7110  O  O   . GLY   D  1 98  ? 65.770 -52.307 70.496  1.00 19.83 ? 98   GLY   D O   1 
ATOM   7111  N  N   . SER   D  1 99  ? 65.043 -54.165 71.542  1.00 19.67 ? 99   SER   D N   1 
ATOM   7112  C  CA  . SER   D  1 99  ? 65.072 -53.565 72.867  1.00 20.19 ? 99   SER   D CA  1 
ATOM   7113  C  C   . SER   D  1 99  ? 66.462 -53.593 73.521  1.00 21.70 ? 99   SER   D C   1 
ATOM   7114  O  O   . SER   D  1 99  ? 66.660 -52.948 74.556  1.00 24.82 ? 99   SER   D O   1 
ATOM   7115  C  CB  . SER   D  1 99  ? 64.047 -54.245 73.778  1.00 22.87 ? 99   SER   D CB  1 
ATOM   7116  O  OG  . SER   D  1 99  ? 64.180 -55.665 73.751  1.00 24.73 ? 99   SER   D OG  1 
ATOM   7117  N  N   . HIS   D  1 100 ? 67.413 -54.318 72.941  1.00 22.53 ? 100  HIS   D N   1 
ATOM   7118  C  CA  . HIS   D  1 100 ? 68.797 -54.326 73.384  1.00 22.90 ? 100  HIS   D CA  1 
ATOM   7119  C  C   . HIS   D  1 100 ? 69.626 -54.688 72.175  1.00 23.58 ? 100  HIS   D C   1 
ATOM   7120  O  O   . HIS   D  1 100 ? 69.076 -55.100 71.148  1.00 23.92 ? 100  HIS   D O   1 
ATOM   7121  C  CB  . HIS   D  1 100 ? 69.005 -55.309 74.552  1.00 22.83 ? 100  HIS   D CB  1 
ATOM   7122  C  CG  . HIS   D  1 100 ? 68.653 -56.721 74.229  1.00 24.70 ? 100  HIS   D CG  1 
ATOM   7123  N  ND1 . HIS   D  1 100 ? 69.558 -57.595 73.662  1.00 27.14 ? 100  HIS   D ND1 1 
ATOM   7124  C  CD2 . HIS   D  1 100 ? 67.504 -57.414 74.400  1.00 25.84 ? 100  HIS   D CD2 1 
ATOM   7125  C  CE1 . HIS   D  1 100 ? 68.971 -58.769 73.481  1.00 25.79 ? 100  HIS   D CE1 1 
ATOM   7126  N  NE2 . HIS   D  1 100 ? 67.719 -58.685 73.906  1.00 24.61 ? 100  HIS   D NE2 1 
ATOM   7127  N  N   . ASP   D  1 101 ? 70.954 -54.528 72.289  1.00 23.54 ? 101  ASP   D N   1 
ATOM   7128  C  CA  . ASP   D  1 101 ? 71.802 -54.671 71.106  1.00 23.77 ? 101  ASP   D CA  1 
ATOM   7129  C  C   . ASP   D  1 101 ? 71.880 -56.104 70.572  1.00 24.33 ? 101  ASP   D C   1 
ATOM   7130  O  O   . ASP   D  1 101 ? 72.350 -56.296 69.452  1.00 24.94 ? 101  ASP   D O   1 
ATOM   7131  C  CB  . ASP   D  1 101 ? 73.226 -54.217 71.409  1.00 26.90 ? 101  ASP   D CB  1 
ATOM   7132  C  CG  . ASP   D  1 101 ? 73.354 -52.700 71.582  1.00 25.64 ? 101  ASP   D CG  1 
ATOM   7133  O  OD1 . ASP   D  1 101 ? 72.388 -51.927 71.326  1.00 27.30 ? 101  ASP   D OD1 1 
ATOM   7134  O  OD2 . ASP   D  1 101 ? 74.490 -52.298 71.984  1.00 28.90 ? 101  ASP   D OD2 1 
ATOM   7135  N  N   . GLY   D  1 102 ? 71.457 -57.093 71.335  1.00 24.14 ? 102  GLY   D N   1 
ATOM   7136  C  CA  . GLY   D  1 102 ? 71.574 -58.470 70.913  1.00 24.02 ? 102  GLY   D CA  1 
ATOM   7137  C  C   . GLY   D  1 102 ? 70.475 -58.977 69.998  1.00 23.53 ? 102  GLY   D C   1 
ATOM   7138  O  O   . GLY   D  1 102 ? 70.498 -60.151 69.581  1.00 24.51 ? 102  GLY   D O   1 
ATOM   7139  N  N   . GLN   D  1 103 ? 69.496 -58.136 69.667  1.00 21.29 ? 103  GLN   D N   1 
ATOM   7140  C  CA  . GLN   D  1 103 ? 68.496 -58.504 68.668  1.00 21.18 ? 103  GLN   D CA  1 
ATOM   7141  C  C   . GLN   D  1 103 ? 68.046 -57.236 67.967  1.00 21.64 ? 103  GLN   D C   1 
ATOM   7142  O  O   . GLN   D  1 103 ? 68.369 -56.120 68.401  1.00 20.10 ? 103  GLN   D O   1 
ATOM   7143  C  CB  . GLN   D  1 103 ? 67.289 -59.266 69.276  1.00 22.88 ? 103  GLN   D CB  1 
ATOM   7144  C  CG  . GLN   D  1 103 ? 66.486 -58.444 70.296  1.00 24.41 ? 103  GLN   D CG  1 
ATOM   7145  C  CD  . GLN   D  1 103 ? 65.512 -59.302 71.094  1.00 23.39 ? 103  GLN   D CD  1 
ATOM   7146  O  OE1 . GLN   D  1 103 ? 65.771 -60.481 71.309  1.00 25.42 ? 103  GLN   D OE1 1 
ATOM   7147  N  NE2 . GLN   D  1 103 ? 64.387 -58.731 71.543  1.00 20.58 ? 103  GLN   D NE2 1 
ATOM   7148  N  N   . GLY   D  1 104 ? 67.274 -57.404 66.890  1.00 20.16 ? 104  GLY   D N   1 
ATOM   7149  C  CA  . GLY   D  1 104 ? 66.785 -56.245 66.164  1.00 16.34 ? 104  GLY   D CA  1 
ATOM   7150  C  C   . GLY   D  1 104 ? 66.690 -56.462 64.676  1.00 17.17 ? 104  GLY   D C   1 
ATOM   7151  O  O   . GLY   D  1 104 ? 65.746 -55.957 64.066  1.00 18.24 ? 104  GLY   D O   1 
ATOM   7152  N  N   . SER   D  1 105 ? 67.667 -57.156 64.071  1.00 16.42 ? 105  SER   D N   1 
ATOM   7153  C  CA  . SER   D  1 105 ? 67.553 -57.370 62.636  1.00 16.96 ? 105  SER   D CA  1 
ATOM   7154  C  C   . SER   D  1 105 ? 66.401 -58.335 62.313  1.00 16.97 ? 105  SER   D C   1 
ATOM   7155  O  O   . SER   D  1 105 ? 65.925 -59.119 63.157  1.00 18.14 ? 105  SER   D O   1 
ATOM   7156  C  CB  . SER   D  1 105 ? 68.859 -57.887 62.043  1.00 17.42 ? 105  SER   D CB  1 
ATOM   7157  O  OG  . SER   D  1 105 ? 69.180 -59.229 62.480  1.00 19.56 ? 105  SER   D OG  1 
ATOM   7158  N  N   . GLU   D  1 106 ? 65.956 -58.278 61.054  1.00 16.69 ? 106  GLU   D N   1 
ATOM   7159  C  CA  . GLU   D  1 106 ? 64.881 -59.134 60.562  1.00 15.31 ? 106  GLU   D CA  1 
ATOM   7160  C  C   . GLU   D  1 106 ? 65.448 -60.398 59.921  1.00 16.82 ? 106  GLU   D C   1 
ATOM   7161  O  O   . GLU   D  1 106 ? 65.216 -61.513 60.401  1.00 16.93 ? 106  GLU   D O   1 
ATOM   7162  C  CB  . GLU   D  1 106 ? 63.986 -58.342 59.593  1.00 16.32 ? 106  GLU   D CB  1 
ATOM   7163  C  CG  . GLU   D  1 106 ? 63.295 -57.191 60.347  1.00 15.96 ? 106  GLU   D CG  1 
ATOM   7164  C  CD  . GLU   D  1 106 ? 61.953 -56.877 59.759  1.00 16.54 ? 106  GLU   D CD  1 
ATOM   7165  O  OE1 . GLU   D  1 106 ? 61.895 -56.545 58.550  1.00 16.15 ? 106  GLU   D OE1 1 
ATOM   7166  O  OE2 . GLU   D  1 106 ? 60.952 -57.001 60.506  1.00 17.56 ? 106  GLU   D OE2 1 
ATOM   7167  N  N   . HIS   D  1 107 ? 66.266 -60.226 58.896  1.00 16.64 ? 107  HIS   D N   1 
ATOM   7168  C  CA  . HIS   D  1 107 ? 67.039 -61.345 58.406  1.00 17.57 ? 107  HIS   D CA  1 
ATOM   7169  C  C   . HIS   D  1 107 ? 68.083 -61.755 59.447  1.00 18.54 ? 107  HIS   D C   1 
ATOM   7170  O  O   . HIS   D  1 107 ? 68.497 -60.961 60.295  1.00 19.02 ? 107  HIS   D O   1 
ATOM   7171  C  CB  . HIS   D  1 107 ? 67.696 -60.990 57.066  1.00 16.28 ? 107  HIS   D CB  1 
ATOM   7172  C  CG  . HIS   D  1 107 ? 66.690 -60.811 55.975  1.00 16.30 ? 107  HIS   D CG  1 
ATOM   7173  N  ND1 . HIS   D  1 107 ? 66.086 -59.593 55.751  1.00 17.44 ? 107  HIS   D ND1 1 
ATOM   7174  C  CD2 . HIS   D  1 107 ? 66.111 -61.701 55.126  1.00 16.73 ? 107  HIS   D CD2 1 
ATOM   7175  C  CE1 . HIS   D  1 107 ? 65.216 -59.732 54.752  1.00 17.73 ? 107  HIS   D CE1 1 
ATOM   7176  N  NE2 . HIS   D  1 107 ? 65.198 -60.988 54.361  1.00 17.00 ? 107  HIS   D NE2 1 
ATOM   7177  N  N   . THR   D  1 108 ? 68.438 -63.034 59.425  1.00 17.59 ? 108  THR   D N   1 
ATOM   7178  C  CA  . THR   D  1 108 ? 69.563 -63.536 60.205  1.00 18.67 ? 108  THR   D CA  1 
ATOM   7179  C  C   . THR   D  1 108 ? 70.548 -64.186 59.264  1.00 18.94 ? 108  THR   D C   1 
ATOM   7180  O  O   . THR   D  1 108 ? 70.202 -64.530 58.144  1.00 20.08 ? 108  THR   D O   1 
ATOM   7181  C  CB  . THR   D  1 108 ? 69.114 -64.563 61.272  1.00 18.21 ? 108  THR   D CB  1 
ATOM   7182  O  OG1 . THR   D  1 108 ? 68.377 -65.622 60.654  1.00 19.61 ? 108  THR   D OG1 1 
ATOM   7183  C  CG2 . THR   D  1 108 ? 68.211 -63.926 62.314  1.00 19.75 ? 108  THR   D CG2 1 
ATOM   7184  N  N   . VAL   D  1 109 ? 71.794 -64.339 59.717  1.00 18.96 ? 109  VAL   D N   1 
ATOM   7185  C  CA  . VAL   D  1 109 ? 72.863 -64.975 58.938  1.00 18.73 ? 109  VAL   D CA  1 
ATOM   7186  C  C   . VAL   D  1 109 ? 73.358 -66.117 59.784  1.00 22.48 ? 109  VAL   D C   1 
ATOM   7187  O  O   . VAL   D  1 109 ? 73.913 -65.902 60.856  1.00 22.39 ? 109  VAL   D O   1 
ATOM   7188  C  CB  . VAL   D  1 109 ? 73.975 -63.985 58.557  1.00 21.58 ? 109  VAL   D CB  1 
ATOM   7189  C  CG1 . VAL   D  1 109 ? 75.015 -64.695 57.685  1.00 24.67 ? 109  VAL   D CG1 1 
ATOM   7190  C  CG2 . VAL   D  1 109 ? 73.352 -62.834 57.756  1.00 22.88 ? 109  VAL   D CG2 1 
ATOM   7191  N  N   . ASP   D  1 110 ? 73.140 -67.344 59.316  1.00 21.72 ? 110  ASP   D N   1 
ATOM   7192  C  CA  . ASP   D  1 110 ? 73.504 -68.526 60.120  1.00 21.38 ? 110  ASP   D CA  1 
ATOM   7193  C  C   . ASP   D  1 110 ? 72.950 -68.386 61.546  1.00 24.08 ? 110  ASP   D C   1 
ATOM   7194  O  O   . ASP   D  1 110 ? 73.621 -68.690 62.553  1.00 26.52 ? 110  ASP   D O   1 
ATOM   7195  C  CB  . ASP   D  1 110 ? 75.033 -68.769 60.106  1.00 22.90 ? 110  ASP   D CB  1 
ATOM   7196  C  CG  . ASP   D  1 110 ? 75.541 -69.048 58.716  1.00 28.48 ? 110  ASP   D CG  1 
ATOM   7197  O  OD1 . ASP   D  1 110 ? 74.771 -69.661 57.911  1.00 26.52 ? 110  ASP   D OD1 1 
ATOM   7198  O  OD2 . ASP   D  1 110 ? 76.732 -68.729 58.467  1.00 32.52 ? 110  ASP   D OD2 1 
ATOM   7199  N  N   . LYS   D  1 111 ? 71.694 -67.934 61.620  1.00 21.60 ? 111  LYS   D N   1 
ATOM   7200  C  CA  . LYS   D  1 111 ? 70.848 -67.784 62.807  1.00 23.72 ? 111  LYS   D CA  1 
ATOM   7201  C  C   . LYS   D  1 111 ? 71.269 -66.604 63.674  1.00 26.15 ? 111  LYS   D C   1 
ATOM   7202  O  O   . LYS   D  1 111 ? 70.608 -66.316 64.685  1.00 29.46 ? 111  LYS   D O   1 
ATOM   7203  C  CB  . LYS   D  1 111 ? 70.817 -69.068 63.656  1.00 29.07 ? 111  LYS   D CB  1 
ATOM   7204  C  CG  . LYS   D  1 111 ? 70.552 -70.318 62.818  1.00 38.92 ? 111  LYS   D CG  1 
ATOM   7205  C  CD  . LYS   D  1 111 ? 69.268 -70.258 62.021  1.00 48.37 ? 111  LYS   D CD  1 
ATOM   7206  C  CE  . LYS   D  1 111 ? 68.086 -70.148 62.961  1.00 54.25 ? 111  LYS   D CE  1 
ATOM   7207  N  NZ  . LYS   D  1 111 ? 66.736 -70.021 62.295  1.00 57.03 ? 111  LYS   D NZ  1 
ATOM   7208  N  N   . LYS   D  1 112 ? 72.307 -65.872 63.298  1.00 23.05 ? 112  LYS   D N   1 
ATOM   7209  C  CA  . LYS   D  1 112 ? 72.779 -64.749 64.098  1.00 26.17 ? 112  LYS   D CA  1 
ATOM   7210  C  C   . LYS   D  1 112 ? 72.012 -63.481 63.769  1.00 23.65 ? 112  LYS   D C   1 
ATOM   7211  O  O   . LYS   D  1 112 ? 71.735 -63.179 62.600  1.00 22.03 ? 112  LYS   D O   1 
ATOM   7212  C  CB  . LYS   D  1 112 ? 74.263 -64.508 63.843  1.00 32.02 ? 112  LYS   D CB  1 
ATOM   7213  C  CG  . LYS   D  1 112 ? 74.875 -63.266 64.521  1.00 42.93 ? 112  LYS   D CG  1 
ATOM   7214  C  CD  . LYS   D  1 112 ? 75.106 -62.110 63.515  1.00 46.65 ? 112  LYS   D CD  1 
ATOM   7215  C  CE  . LYS   D  1 112 ? 76.128 -61.090 64.024  1.00 49.92 ? 112  LYS   D CE  1 
ATOM   7216  N  NZ  . LYS   D  1 112 ? 75.822 -60.559 65.377  1.00 53.47 ? 112  LYS   D NZ  1 
ATOM   7217  N  N   . LYS   D  1 113 ? 71.678 -62.731 64.814  1.00 20.99 ? 113  LYS   D N   1 
ATOM   7218  C  CA  . LYS   D  1 113 ? 71.028 -61.437 64.664  1.00 20.22 ? 113  LYS   D CA  1 
ATOM   7219  C  C   . LYS   D  1 113 ? 71.981 -60.259 64.842  1.00 21.16 ? 113  LYS   D C   1 
ATOM   7220  O  O   . LYS   D  1 113 ? 72.974 -60.331 65.581  1.00 25.83 ? 113  LYS   D O   1 
ATOM   7221  C  CB  . LYS   D  1 113 ? 69.899 -61.321 65.695  1.00 19.90 ? 113  LYS   D CB  1 
ATOM   7222  C  CG  . LYS   D  1 113 ? 68.777 -62.248 65.414  1.00 21.17 ? 113  LYS   D CG  1 
ATOM   7223  C  CD  . LYS   D  1 113 ? 67.643 -62.054 66.443  1.00 25.46 ? 113  LYS   D CD  1 
ATOM   7224  C  CE  . LYS   D  1 113 ? 66.408 -62.818 65.980  1.00 25.46 ? 113  LYS   D CE  1 
ATOM   7225  N  NZ  . LYS   D  1 113 ? 65.133 -62.275 66.615  1.00 26.77 ? 113  LYS   D NZ  1 
ATOM   7226  N  N   . TYR   D  1 114 ? 71.685 -59.179 64.118  1.00 20.18 ? 114  TYR   D N   1 
ATOM   7227  C  CA  . TYR   D  1 114 ? 72.368 -57.911 64.311  1.00 22.17 ? 114  TYR   D CA  1 
ATOM   7228  C  C   . TYR   D  1 114 ? 71.497 -56.994 65.157  1.00 20.01 ? 114  TYR   D C   1 
ATOM   7229  O  O   . TYR   D  1 114 ? 70.308 -57.255 65.349  1.00 19.84 ? 114  TYR   D O   1 
ATOM   7230  C  CB  . TYR   D  1 114 ? 72.660 -57.274 62.945  1.00 22.35 ? 114  TYR   D CB  1 
ATOM   7231  C  CG  . TYR   D  1 114 ? 73.699 -58.032 62.142  1.00 23.45 ? 114  TYR   D CG  1 
ATOM   7232  C  CD1 . TYR   D  1 114 ? 73.343 -59.074 61.301  1.00 24.37 ? 114  TYR   D CD1 1 
ATOM   7233  C  CD2 . TYR   D  1 114 ? 75.051 -57.668 62.206  1.00 27.66 ? 114  TYR   D CD2 1 
ATOM   7234  C  CE1 . TYR   D  1 114 ? 74.295 -59.738 60.555  1.00 28.43 ? 114  TYR   D CE1 1 
ATOM   7235  C  CE2 . TYR   D  1 114 ? 76.010 -58.364 61.473  1.00 28.65 ? 114  TYR   D CE2 1 
ATOM   7236  C  CZ  . TYR   D  1 114 ? 75.611 -59.400 60.661  1.00 29.02 ? 114  TYR   D CZ  1 
ATOM   7237  O  OH  . TYR   D  1 114 ? 76.532 -60.089 59.891  1.00 36.17 ? 114  TYR   D OH  1 
ATOM   7238  N  N   . ALA   D  1 115 ? 72.064 -55.856 65.583  1.00 20.74 ? 115  ALA   D N   1 
ATOM   7239  C  CA  . ALA   D  1 115 ? 71.326 -54.920 66.422  1.00 19.34 ? 115  ALA   D CA  1 
ATOM   7240  C  C   . ALA   D  1 115 ? 70.227 -54.204 65.663  1.00 18.62 ? 115  ALA   D C   1 
ATOM   7241  O  O   . ALA   D  1 115 ? 69.245 -53.735 66.270  1.00 19.90 ? 115  ALA   D O   1 
ATOM   7242  C  CB  . ALA   D  1 115 ? 72.280 -53.854 66.997  1.00 21.40 ? 115  ALA   D CB  1 
ATOM   7243  N  N   . ALA   D  1 116 ? 70.356 -54.079 64.346  1.00 18.66 ? 116  ALA   D N   1 
ATOM   7244  C  CA  . ALA   D  1 116 ? 69.293 -53.443 63.583  1.00 18.63 ? 116  ALA   D CA  1 
ATOM   7245  C  C   . ALA   D  1 116 ? 69.464 -53.813 62.121  1.00 19.00 ? 116  ALA   D C   1 
ATOM   7246  O  O   . ALA   D  1 116 ? 70.457 -54.437 61.729  1.00 18.64 ? 116  ALA   D O   1 
ATOM   7247  C  CB  . ALA   D  1 116 ? 69.302 -51.901 63.778  1.00 19.52 ? 116  ALA   D CB  1 
ATOM   7248  N  N   . GLU   D  1 117 ? 68.478 -53.447 61.336  1.00 17.77 ? 117  GLU   D N   1 
ATOM   7249  C  CA  . GLU   D  1 117 ? 68.490 -53.686 59.901  1.00 17.15 ? 117  GLU   D CA  1 
ATOM   7250  C  C   . GLU   D  1 117 ? 67.854 -52.484 59.211  1.00 17.82 ? 117  GLU   D C   1 
ATOM   7251  O  O   . GLU   D  1 117 ? 66.779 -52.016 59.598  1.00 18.01 ? 117  GLU   D O   1 
ATOM   7252  C  CB  . GLU   D  1 117 ? 67.761 -55.004 59.564  1.00 16.79 ? 117  GLU   D CB  1 
ATOM   7253  C  CG  . GLU   D  1 117 ? 67.877 -55.424 58.109  1.00 16.83 ? 117  GLU   D CG  1 
ATOM   7254  C  CD  . GLU   D  1 117 ? 67.291 -56.812 57.860  1.00 17.18 ? 117  GLU   D CD  1 
ATOM   7255  O  OE1 . GLU   D  1 117 ? 67.436 -57.677 58.753  1.00 18.51 ? 117  GLU   D OE1 1 
ATOM   7256  O  OE2 . GLU   D  1 117 ? 66.751 -57.048 56.755  1.00 18.45 ? 117  GLU   D OE2 1 
ATOM   7257  N  N   . LEU   D  1 118 ? 68.530 -52.015 58.170  1.00 16.35 ? 118  LEU   D N   1 
ATOM   7258  C  CA  . LEU   D  1 118 ? 68.093 -50.907 57.334  1.00 16.48 ? 118  LEU   D CA  1 
ATOM   7259  C  C   . LEU   D  1 118 ? 67.477 -51.440 56.053  1.00 15.95 ? 118  LEU   D C   1 
ATOM   7260  O  O   . LEU   D  1 118 ? 68.038 -52.349 55.404  1.00 17.53 ? 118  LEU   D O   1 
ATOM   7261  C  CB  . LEU   D  1 118 ? 69.326 -50.045 56.996  1.00 17.83 ? 118  LEU   D CB  1 
ATOM   7262  C  CG  . LEU   D  1 118 ? 69.184 -49.052 55.846  1.00 18.05 ? 118  LEU   D CG  1 
ATOM   7263  C  CD1 . LEU   D  1 118 ? 68.119 -47.970 56.164  1.00 17.82 ? 118  LEU   D CD1 1 
ATOM   7264  C  CD2 . LEU   D  1 118 ? 70.560 -48.381 55.616  1.00 18.51 ? 118  LEU   D CD2 1 
ATOM   7265  N  N   . HIS   D  1 119 ? 66.297 -50.917 55.698  1.00 16.49 ? 119  HIS   D N   1 
ATOM   7266  C  CA  . HIS   D  1 119 ? 65.620 -51.283 54.448  1.00 16.88 ? 119  HIS   D CA  1 
ATOM   7267  C  C   . HIS   D  1 119 ? 65.458 -50.056 53.568  1.00 17.27 ? 119  HIS   D C   1 
ATOM   7268  O  O   . HIS   D  1 119 ? 64.739 -49.109 53.944  1.00 17.01 ? 119  HIS   D O   1 
ATOM   7269  C  CB  . HIS   D  1 119 ? 64.222 -51.843 54.731  1.00 16.63 ? 119  HIS   D CB  1 
ATOM   7270  C  CG  . HIS   D  1 119 ? 64.270 -53.191 55.363  1.00 16.03 ? 119  HIS   D CG  1 
ATOM   7271  N  ND1 . HIS   D  1 119 ? 63.220 -53.728 56.068  1.00 14.18 ? 119  HIS   D ND1 1 
ATOM   7272  C  CD2 . HIS   D  1 119 ? 65.278 -54.092 55.435  1.00 15.22 ? 119  HIS   D CD2 1 
ATOM   7273  C  CE1 . HIS   D  1 119 ? 63.568 -54.923 56.533  1.00 15.98 ? 119  HIS   D CE1 1 
ATOM   7274  N  NE2 . HIS   D  1 119 ? 64.819 -55.153 56.170  1.00 15.58 ? 119  HIS   D NE2 1 
ATOM   7275  N  N   . LEU   D  1 120 ? 66.078 -50.106 52.391  1.00 18.17 ? 120  LEU   D N   1 
ATOM   7276  C  CA  . LEU   D  1 120 ? 65.898 -49.093 51.347  1.00 17.98 ? 120  LEU   D CA  1 
ATOM   7277  C  C   . LEU   D  1 120 ? 64.886 -49.661 50.352  1.00 18.07 ? 120  LEU   D C   1 
ATOM   7278  O  O   . LEU   D  1 120 ? 65.148 -50.691 49.708  1.00 17.05 ? 120  LEU   D O   1 
ATOM   7279  C  CB  . LEU   D  1 120 ? 67.248 -48.765 50.711  1.00 18.20 ? 120  LEU   D CB  1 
ATOM   7280  C  CG  . LEU   D  1 120 ? 68.220 -48.028 51.635  1.00 18.51 ? 120  LEU   D CG  1 
ATOM   7281  C  CD1 . LEU   D  1 120 ? 69.590 -48.754 51.665  1.00 22.89 ? 120  LEU   D CD1 1 
ATOM   7282  C  CD2 . LEU   D  1 120 ? 68.408 -46.534 51.289  1.00 22.14 ? 120  LEU   D CD2 1 
ATOM   7283  N  N   . VAL   D  1 121 ? 63.723 -49.010 50.237  1.00 17.80 ? 121  VAL   D N   1 
ATOM   7284  C  CA  . VAL   D  1 121 ? 62.557 -49.548 49.532  1.00 17.24 ? 121  VAL   D CA  1 
ATOM   7285  C  C   . VAL   D  1 121 ? 62.450 -48.916 48.147  1.00 17.91 ? 121  VAL   D C   1 
ATOM   7286  O  O   . VAL   D  1 121 ? 62.447 -47.678 48.017  1.00 18.20 ? 121  VAL   D O   1 
ATOM   7287  C  CB  . VAL   D  1 121 ? 61.290 -49.268 50.357  1.00 17.03 ? 121  VAL   D CB  1 
ATOM   7288  C  CG1 . VAL   D  1 121 ? 60.034 -49.844 49.662  1.00 16.35 ? 121  VAL   D CG1 1 
ATOM   7289  C  CG2 . VAL   D  1 121 ? 61.436 -49.789 51.818  1.00 18.53 ? 121  VAL   D CG2 1 
ATOM   7290  N  N   . HIS   D  1 122 ? 62.332 -49.749 47.114  1.00 17.30 ? 122  HIS   D N   1 
ATOM   7291  C  CA  . HIS   D  1 122 ? 62.293 -49.274 45.733  1.00 17.71 ? 122  HIS   D CA  1 
ATOM   7292  C  C   . HIS   D  1 122 ? 61.132 -49.934 44.991  1.00 18.14 ? 122  HIS   D C   1 
ATOM   7293  O  O   . HIS   D  1 122 ? 60.786 -51.102 45.262  1.00 18.37 ? 122  HIS   D O   1 
ATOM   7294  C  CB  . HIS   D  1 122 ? 63.598 -49.585 44.968  1.00 18.35 ? 122  HIS   D CB  1 
ATOM   7295  C  CG  . HIS   D  1 122 ? 64.861 -49.274 45.706  1.00 18.50 ? 122  HIS   D CG  1 
ATOM   7296  N  ND1 . HIS   D  1 122 ? 65.326 -50.051 46.755  1.00 17.88 ? 122  HIS   D ND1 1 
ATOM   7297  C  CD2 . HIS   D  1 122 ? 65.782 -48.286 45.513  1.00 19.55 ? 122  HIS   D CD2 1 
ATOM   7298  C  CE1 . HIS   D  1 122 ? 66.476 -49.526 47.187  1.00 19.02 ? 122  HIS   D CE1 1 
ATOM   7299  N  NE2 . HIS   D  1 122 ? 66.785 -48.474 46.436  1.00 21.07 ? 122  HIS   D NE2 1 
ATOM   7300  N  N   . TRP   D  1 123 ? 60.554 -49.204 44.001  1.00 18.77 ? 123  TRP   D N   1 
ATOM   7301  C  CA  . TRP   D  1 123 ? 59.452 -49.759 43.214  1.00 18.48 ? 123  TRP   D CA  1 
ATOM   7302  C  C   . TRP   D  1 123 ? 59.737 -49.696 41.719  1.00 18.58 ? 123  TRP   D C   1 
ATOM   7303  O  O   . TRP   D  1 123 ? 60.413 -48.789 41.205  1.00 20.93 ? 123  TRP   D O   1 
ATOM   7304  C  CB  . TRP   D  1 123 ? 58.102 -49.081 43.539  1.00 17.33 ? 123  TRP   D CB  1 
ATOM   7305  C  CG  . TRP   D  1 123 ? 58.117 -47.580 43.336  1.00 18.21 ? 123  TRP   D CG  1 
ATOM   7306  C  CD1 . TRP   D  1 123 ? 58.491 -46.610 44.262  1.00 18.55 ? 123  TRP   D CD1 1 
ATOM   7307  C  CD2 . TRP   D  1 123 ? 57.737 -46.854 42.131  1.00 18.94 ? 123  TRP   D CD2 1 
ATOM   7308  N  NE1 . TRP   D  1 123 ? 58.315 -45.349 43.715  1.00 19.18 ? 123  TRP   D NE1 1 
ATOM   7309  C  CE2 . TRP   D  1 123 ? 57.909 -45.475 42.401  1.00 18.07 ? 123  TRP   D CE2 1 
ATOM   7310  C  CE3 . TRP   D  1 123 ? 57.274 -47.246 40.869  1.00 20.39 ? 123  TRP   D CE3 1 
ATOM   7311  C  CZ2 . TRP   D  1 123 ? 57.591 -44.494 41.472  1.00 18.39 ? 123  TRP   D CZ2 1 
ATOM   7312  C  CZ3 . TRP   D  1 123 ? 57.010 -46.281 39.920  1.00 20.88 ? 123  TRP   D CZ3 1 
ATOM   7313  C  CH2 . TRP   D  1 123 ? 57.164 -44.905 40.223  1.00 22.07 ? 123  TRP   D CH2 1 
ATOM   7314  N  N   . ASN   D  1 124 ? 59.194 -50.695 41.022  1.00 20.35 ? 124  ASN   D N   1 
ATOM   7315  C  CA  . ASN   D  1 124 ? 59.455 -50.941 39.605  1.00 19.97 ? 124  ASN   D CA  1 
ATOM   7316  C  C   . ASN   D  1 124 ? 58.731 -49.913 38.747  1.00 21.19 ? 124  ASN   D C   1 
ATOM   7317  O  O   . ASN   D  1 124 ? 57.502 -49.832 38.815  1.00 22.24 ? 124  ASN   D O   1 
ATOM   7318  C  CB  . ASN   D  1 124 ? 58.964 -52.363 39.304  1.00 20.12 ? 124  ASN   D CB  1 
ATOM   7319  C  CG  . ASN   D  1 124 ? 59.345 -52.841 37.924  1.00 23.94 ? 124  ASN   D CG  1 
ATOM   7320  O  OD1 . ASN   D  1 124 ? 59.682 -52.049 37.030  1.00 25.06 ? 124  ASN   D OD1 1 
ATOM   7321  N  ND2 . ASN   D  1 124 ? 59.323 -54.178 37.744  1.00 23.11 ? 124  ASN   D ND2 1 
ATOM   7322  N  N   . THR   D  1 125 ? 59.487 -49.134 37.938  1.00 20.82 ? 125  THR   D N   1 
ATOM   7323  C  CA  . THR   D  1 125 ? 58.832 -48.131 37.098  1.00 21.80 ? 125  THR   D CA  1 
ATOM   7324  C  C   . THR   D  1 125 ? 58.006 -48.739 35.969  1.00 23.96 ? 125  THR   D C   1 
ATOM   7325  O  O   . THR   D  1 125 ? 57.364 -47.998 35.204  1.00 28.97 ? 125  THR   D O   1 
ATOM   7326  C  CB  . THR   D  1 125 ? 59.858 -47.183 36.498  1.00 25.11 ? 125  THR   D CB  1 
ATOM   7327  O  OG1 . THR   D  1 125 ? 60.746 -47.933 35.646  1.00 28.73 ? 125  THR   D OG1 1 
ATOM   7328  C  CG2 . THR   D  1 125 ? 60.631 -46.503 37.596  1.00 24.85 ? 125  THR   D CG2 1 
ATOM   7329  N  N   . LYS   D  1 126 ? 58.031 -50.061 35.815  1.00 24.05 ? 126  LYS   D N   1 
ATOM   7330  C  CA  . LYS   D  1 126 ? 57.044 -50.747 34.988  1.00 29.06 ? 126  LYS   D CA  1 
ATOM   7331  C  C   . LYS   D  1 126 ? 55.619 -50.367 35.401  1.00 26.33 ? 126  LYS   D C   1 
ATOM   7332  O  O   . LYS   D  1 126 ? 54.709 -50.326 34.566  1.00 29.79 ? 126  LYS   D O   1 
ATOM   7333  C  CB  . LYS   D  1 126 ? 57.302 -52.258 35.122  1.00 30.74 ? 126  LYS   D CB  1 
ATOM   7334  C  CG  . LYS   D  1 126 ? 56.281 -53.205 34.550  1.00 29.57 ? 126  LYS   D CG  1 
ATOM   7335  C  CD  . LYS   D  1 126 ? 56.735 -54.682 34.760  1.00 30.50 ? 126  LYS   D CD  1 
ATOM   7336  C  CE  . LYS   D  1 126 ? 55.677 -55.619 34.158  1.00 34.04 ? 126  LYS   D CE  1 
ATOM   7337  N  NZ  . LYS   D  1 126 ? 55.888 -57.077 34.424  1.00 33.37 ? 126  LYS   D NZ  1 
ATOM   7338  N  N   . TYR   D  1 127 ? 55.409 -50.079 36.677  1.00 23.17 ? 127  TYR   D N   1 
ATOM   7339  C  CA  . TYR   D  1 127 ? 54.102 -49.781 37.236  1.00 24.43 ? 127  TYR   D CA  1 
ATOM   7340  C  C   . TYR   D  1 127 ? 54.061 -48.286 37.514  1.00 28.35 ? 127  TYR   D C   1 
ATOM   7341  O  O   . TYR   D  1 127 ? 55.082 -47.600 37.450  1.00 28.79 ? 127  TYR   D O   1 
ATOM   7342  C  CB  . TYR   D  1 127 ? 53.864 -50.663 38.488  1.00 21.73 ? 127  TYR   D CB  1 
ATOM   7343  C  CG  . TYR   D  1 127 ? 54.036 -52.136 38.141  1.00 22.40 ? 127  TYR   D CG  1 
ATOM   7344  C  CD1 . TYR   D  1 127 ? 53.166 -52.745 37.254  1.00 24.31 ? 127  TYR   D CD1 1 
ATOM   7345  C  CD2 . TYR   D  1 127 ? 55.085 -52.911 38.684  1.00 21.22 ? 127  TYR   D CD2 1 
ATOM   7346  C  CE1 . TYR   D  1 127 ? 53.321 -54.041 36.877  1.00 23.99 ? 127  TYR   D CE1 1 
ATOM   7347  C  CE2 . TYR   D  1 127 ? 55.252 -54.225 38.352  1.00 22.10 ? 127  TYR   D CE2 1 
ATOM   7348  C  CZ  . TYR   D  1 127 ? 54.352 -54.811 37.454  1.00 22.97 ? 127  TYR   D CZ  1 
ATOM   7349  O  OH  . TYR   D  1 127 ? 54.488 -56.107 37.055  1.00 25.99 ? 127  TYR   D OH  1 
ATOM   7350  N  N   . GLY   D  1 128 ? 52.885 -47.741 37.802  1.00 30.44 ? 128  GLY   D N   1 
ATOM   7351  C  CA  . GLY   D  1 128 ? 52.804 -46.280 37.790  1.00 29.62 ? 128  GLY   D CA  1 
ATOM   7352  C  C   . GLY   D  1 128 ? 53.413 -45.618 39.018  1.00 26.68 ? 128  GLY   D C   1 
ATOM   7353  O  O   . GLY   D  1 128 ? 53.863 -44.461 38.964  1.00 28.32 ? 128  GLY   D O   1 
ATOM   7354  N  N   . ASP   D  1 129 ? 53.405 -46.311 40.135  1.00 23.24 ? 129  ASP   D N   1 
ATOM   7355  C  CA  . ASP   D  1 129 ? 53.798 -45.742 41.425  1.00 22.35 ? 129  ASP   D CA  1 
ATOM   7356  C  C   . ASP   D  1 129 ? 53.913 -46.908 42.409  1.00 20.99 ? 129  ASP   D C   1 
ATOM   7357  O  O   . ASP   D  1 129 ? 53.612 -48.075 42.080  1.00 20.82 ? 129  ASP   D O   1 
ATOM   7358  C  CB  . ASP   D  1 129 ? 52.779 -44.692 41.909  1.00 23.58 ? 129  ASP   D CB  1 
ATOM   7359  C  CG  . ASP   D  1 129 ? 51.343 -45.219 41.856  1.00 28.15 ? 129  ASP   D CG  1 
ATOM   7360  O  OD1 . ASP   D  1 129 ? 51.124 -46.339 42.318  1.00 26.33 ? 129  ASP   D OD1 1 
ATOM   7361  O  OD2 . ASP   D  1 129 ? 50.444 -44.523 41.317  1.00 32.01 ? 129  ASP   D OD2 1 
ATOM   7362  N  N   . PHE   D  1 130 ? 54.309 -46.578 43.633  1.00 20.11 ? 130  PHE   D N   1 
ATOM   7363  C  CA  . PHE   D  1 130 ? 54.522 -47.606 44.642  1.00 20.01 ? 130  PHE   D CA  1 
ATOM   7364  C  C   . PHE   D  1 130 ? 53.251 -48.418 44.871  1.00 19.24 ? 130  PHE   D C   1 
ATOM   7365  O  O   . PHE   D  1 130 ? 53.302 -49.648 44.998  1.00 18.36 ? 130  PHE   D O   1 
ATOM   7366  C  CB  . PHE   D  1 130 ? 54.979 -46.976 45.959  1.00 20.66 ? 130  PHE   D CB  1 
ATOM   7367  C  CG  . PHE   D  1 130 ? 55.122 -47.985 47.058  1.00 17.36 ? 130  PHE   D CG  1 
ATOM   7368  C  CD1 . PHE   D  1 130 ? 54.049 -48.351 47.857  1.00 18.59 ? 130  PHE   D CD1 1 
ATOM   7369  C  CD2 . PHE   D  1 130 ? 56.343 -48.632 47.297  1.00 18.65 ? 130  PHE   D CD2 1 
ATOM   7370  C  CE1 . PHE   D  1 130 ? 54.167 -49.312 48.856  1.00 19.31 ? 130  PHE   D CE1 1 
ATOM   7371  C  CE2 . PHE   D  1 130 ? 56.481 -49.561 48.324  1.00 18.16 ? 130  PHE   D CE2 1 
ATOM   7372  C  CZ  . PHE   D  1 130 ? 55.395 -49.942 49.097  1.00 18.55 ? 130  PHE   D CZ  1 
ATOM   7373  N  N   . GLY   D  1 131 ? 52.108 -47.735 44.951  1.00 20.02 ? 131  GLY   D N   1 
ATOM   7374  C  CA  . GLY   D  1 131 ? 50.872 -48.441 45.261  1.00 18.40 ? 131  GLY   D CA  1 
ATOM   7375  C  C   . GLY   D  1 131 ? 50.489 -49.475 44.233  1.00 19.45 ? 131  GLY   D C   1 
ATOM   7376  O  O   . GLY   D  1 131 ? 49.938 -50.521 44.576  1.00 18.94 ? 131  GLY   D O   1 
ATOM   7377  N  N   . LYS   D  1 132 ? 50.738 -49.192 42.960  1.00 18.20 ? 132  LYS   D N   1 
ATOM   7378  C  CA  . LYS   D  1 132 ? 50.482 -50.208 41.942  1.00 18.38 ? 132  LYS   D CA  1 
ATOM   7379  C  C   . LYS   D  1 132 ? 51.541 -51.296 42.014  1.00 20.84 ? 132  LYS   D C   1 
ATOM   7380  O  O   . LYS   D  1 132 ? 51.235 -52.488 41.861  1.00 20.08 ? 132  LYS   D O   1 
ATOM   7381  C  CB  . LYS   D  1 132 ? 50.475 -49.549 40.556  1.00 20.24 ? 132  LYS   D CB  1 
ATOM   7382  C  CG  . LYS   D  1 132 ? 49.281 -48.633 40.397  1.00 22.10 ? 132  LYS   D CG  1 
ATOM   7383  C  CD  . LYS   D  1 132 ? 49.383 -47.778 39.116  1.00 27.25 ? 132  LYS   D CD  1 
ATOM   7384  C  CE  . LYS   D  1 132 ? 48.139 -46.948 38.990  1.00 32.95 ? 132  LYS   D CE  1 
ATOM   7385  N  NZ  . LYS   D  1 132 ? 48.240 -46.174 37.714  1.00 41.04 ? 132  LYS   D NZ  1 
ATOM   7386  N  N   . ALA   D  1 133 ? 52.799 -50.907 42.230  1.00 20.00 ? 133  ALA   D N   1 
ATOM   7387  C  CA  . ALA   D  1 133 ? 53.885 -51.883 42.195  1.00 18.17 ? 133  ALA   D CA  1 
ATOM   7388  C  C   . ALA   D  1 133 ? 53.753 -52.911 43.312  1.00 19.94 ? 133  ALA   D C   1 
ATOM   7389  O  O   . ALA   D  1 133 ? 54.090 -54.083 43.114  1.00 18.48 ? 133  ALA   D O   1 
ATOM   7390  C  CB  . ALA   D  1 133 ? 55.245 -51.172 42.328  1.00 17.65 ? 133  ALA   D CB  1 
ATOM   7391  N  N   . VAL   D  1 134 ? 53.318 -52.487 44.502  1.00 18.11 ? 134  VAL   D N   1 
ATOM   7392  C  CA  . VAL   D  1 134 ? 53.342 -53.412 45.642  1.00 17.28 ? 134  VAL   D CA  1 
ATOM   7393  C  C   . VAL   D  1 134 ? 52.336 -54.543 45.481  1.00 18.96 ? 134  VAL   D C   1 
ATOM   7394  O  O   . VAL   D  1 134 ? 52.404 -55.527 46.217  1.00 18.29 ? 134  VAL   D O   1 
ATOM   7395  C  CB  . VAL   D  1 134 ? 53.109 -52.620 46.933  1.00 17.38 ? 134  VAL   D CB  1 
ATOM   7396  C  CG1 . VAL   D  1 134 ? 51.699 -52.056 46.965  1.00 17.29 ? 134  VAL   D CG1 1 
ATOM   7397  C  CG2 . VAL   D  1 134 ? 53.354 -53.492 48.210  1.00 16.98 ? 134  VAL   D CG2 1 
ATOM   7398  N  N   . GLN   D  1 135 ? 51.428 -54.432 44.512  1.00 18.30 ? 135  GLN   D N   1 
ATOM   7399  C  CA  . GLN   D  1 135 ? 50.469 -55.496 44.210  1.00 18.09 ? 135  GLN   D CA  1 
ATOM   7400  C  C   . GLN   D  1 135 ? 51.017 -56.518 43.226  1.00 20.81 ? 135  GLN   D C   1 
ATOM   7401  O  O   . GLN   D  1 135 ? 50.278 -57.446 42.860  1.00 25.42 ? 135  GLN   D O   1 
ATOM   7402  C  CB  . GLN   D  1 135 ? 49.176 -54.908 43.645  1.00 19.99 ? 135  GLN   D CB  1 
ATOM   7403  C  CG  . GLN   D  1 135 ? 48.492 -53.926 44.648  1.00 18.88 ? 135  GLN   D CG  1 
ATOM   7404  C  CD  . GLN   D  1 135 ? 48.080 -54.626 45.964  1.00 18.35 ? 135  GLN   D CD  1 
ATOM   7405  O  OE1 . GLN   D  1 135 ? 47.799 -55.829 45.980  1.00 22.41 ? 135  GLN   D OE1 1 
ATOM   7406  N  NE2 . GLN   D  1 135 ? 48.041 -53.849 47.053  1.00 16.72 ? 135  GLN   D NE2 1 
ATOM   7407  N  N   . GLN   D  1 136 ? 52.275 -56.390 42.788  1.00 19.71 ? 136  GLN   D N   1 
ATOM   7408  C  CA  . GLN   D  1 136 ? 52.800 -57.243 41.723  1.00 21.60 ? 136  GLN   D CA  1 
ATOM   7409  C  C   . GLN   D  1 136 ? 54.004 -58.040 42.195  1.00 20.70 ? 136  GLN   D C   1 
ATOM   7410  O  O   . GLN   D  1 136 ? 54.824 -57.531 42.962  1.00 20.34 ? 136  GLN   D O   1 
ATOM   7411  C  CB  . GLN   D  1 136 ? 53.213 -56.403 40.492  1.00 22.49 ? 136  GLN   D CB  1 
ATOM   7412  C  CG  . GLN   D  1 136 ? 52.081 -55.556 39.941  1.00 25.22 ? 136  GLN   D CG  1 
ATOM   7413  C  CD  . GLN   D  1 136 ? 50.971 -56.401 39.337  1.00 29.70 ? 136  GLN   D CD  1 
ATOM   7414  O  OE1 . GLN   D  1 136 ? 51.184 -57.568 38.950  1.00 33.48 ? 136  GLN   D OE1 1 
ATOM   7415  N  NE2 . GLN   D  1 136 ? 49.760 -55.832 39.271  1.00 30.33 ? 136  GLN   D NE2 1 
ATOM   7416  N  N   . PRO   D  1 137 ? 54.155 -59.296 41.767  1.00 20.55 ? 137  PRO   D N   1 
ATOM   7417  C  CA  . PRO   D  1 137 ? 55.295 -60.080 42.269  1.00 21.22 ? 137  PRO   D CA  1 
ATOM   7418  C  C   . PRO   D  1 137 ? 56.634 -59.458 41.979  1.00 22.42 ? 137  PRO   D C   1 
ATOM   7419  O  O   . PRO   D  1 137 ? 57.571 -59.632 42.776  1.00 23.50 ? 137  PRO   D O   1 
ATOM   7420  C  CB  . PRO   D  1 137 ? 55.143 -61.429 41.543  1.00 23.55 ? 137  PRO   D CB  1 
ATOM   7421  C  CG  . PRO   D  1 137 ? 53.701 -61.544 41.276  1.00 27.61 ? 137  PRO   D CG  1 
ATOM   7422  C  CD  . PRO   D  1 137 ? 53.230 -60.113 40.946  1.00 25.16 ? 137  PRO   D CD  1 
ATOM   7423  N  N   . ASP   D  1 138 ? 56.784 -58.775 40.837  1.00 19.44 ? 138  ASP   D N   1 
ATOM   7424  C  CA  . ASP   D  1 138 ? 58.016 -58.095 40.477  1.00 20.36 ? 138  ASP   D CA  1 
ATOM   7425  C  C   . ASP   D  1 138 ? 57.968 -56.605 40.817  1.00 19.21 ? 138  ASP   D C   1 
ATOM   7426  O  O   . ASP   D  1 138 ? 58.716 -55.807 40.223  1.00 20.76 ? 138  ASP   D O   1 
ATOM   7427  C  CB  . ASP   D  1 138 ? 58.317 -58.285 38.986  1.00 20.64 ? 138  ASP   D CB  1 
ATOM   7428  C  CG  . ASP   D  1 138 ? 57.224 -57.731 38.078  1.00 24.49 ? 138  ASP   D CG  1 
ATOM   7429  O  OD1 . ASP   D  1 138 ? 56.159 -57.356 38.572  1.00 24.80 ? 138  ASP   D OD1 1 
ATOM   7430  O  OD2 . ASP   D  1 138 ? 57.438 -57.678 36.833  1.00 27.98 ? 138  ASP   D OD2 1 
ATOM   7431  N  N   . GLY   D  1 139 ? 57.101 -56.217 41.748  1.00 18.92 ? 139  GLY   D N   1 
ATOM   7432  C  CA  . GLY   D  1 139 ? 56.840 -54.795 41.968  1.00 18.84 ? 139  GLY   D CA  1 
ATOM   7433  C  C   . GLY   D  1 139 ? 57.915 -54.054 42.766  1.00 18.25 ? 139  GLY   D C   1 
ATOM   7434  O  O   . GLY   D  1 139 ? 58.175 -52.881 42.487  1.00 18.52 ? 139  GLY   D O   1 
ATOM   7435  N  N   . LEU   D  1 140 ? 58.501 -54.694 43.792  1.00 17.81 ? 140  LEU   D N   1 
ATOM   7436  C  CA  . LEU   D  1 140 ? 59.391 -53.991 44.710  1.00 15.99 ? 140  LEU   D CA  1 
ATOM   7437  C  C   . LEU   D  1 140 ? 60.738 -54.678 44.799  1.00 18.95 ? 140  LEU   D C   1 
ATOM   7438  O  O   . LEU   D  1 140 ? 60.871 -55.889 44.568  1.00 19.54 ? 140  LEU   D O   1 
ATOM   7439  C  CB  . LEU   D  1 140 ? 58.812 -53.948 46.135  1.00 15.43 ? 140  LEU   D CB  1 
ATOM   7440  C  CG  . LEU   D  1 140 ? 57.410 -53.326 46.294  1.00 17.68 ? 140  LEU   D CG  1 
ATOM   7441  C  CD1 . LEU   D  1 140 ? 57.069 -53.310 47.790  1.00 17.84 ? 140  LEU   D CD1 1 
ATOM   7442  C  CD2 . LEU   D  1 140 ? 57.308 -51.886 45.712  1.00 18.57 ? 140  LEU   D CD2 1 
ATOM   7443  N  N   . ALA   D  1 141 ? 61.727 -53.866 45.181  1.00 18.20 ? 141  ALA   D N   1 
ATOM   7444  C  CA  . ALA   D  1 141 ? 63.068 -54.347 45.510  1.00 18.58 ? 141  ALA   D CA  1 
ATOM   7445  C  C   . ALA   D  1 141 ? 63.476 -53.672 46.798  1.00 18.39 ? 141  ALA   D C   1 
ATOM   7446  O  O   . ALA   D  1 141 ? 63.456 -52.435 46.887  1.00 19.09 ? 141  ALA   D O   1 
ATOM   7447  C  CB  . ALA   D  1 141 ? 64.071 -54.040 44.399  1.00 20.66 ? 141  ALA   D CB  1 
ATOM   7448  N  N   . VAL   D  1 142 ? 63.829 -54.461 47.810  1.00 16.81 ? 142  VAL   D N   1 
ATOM   7449  C  CA  . VAL   D  1 142 ? 64.261 -53.885 49.075  1.00 17.67 ? 142  VAL   D CA  1 
ATOM   7450  C  C   . VAL   D  1 142 ? 65.723 -54.268 49.281  1.00 17.44 ? 142  VAL   D C   1 
ATOM   7451  O  O   . VAL   D  1 142 ? 66.095 -55.457 49.209  1.00 19.66 ? 142  VAL   D O   1 
ATOM   7452  C  CB  . VAL   D  1 142 ? 63.394 -54.288 50.271  1.00 17.05 ? 142  VAL   D CB  1 
ATOM   7453  C  CG1 . VAL   D  1 142 ? 63.890 -53.563 51.564  1.00 17.98 ? 142  VAL   D CG1 1 
ATOM   7454  C  CG2 . VAL   D  1 142 ? 61.935 -53.832 50.035  1.00 17.50 ? 142  VAL   D CG2 1 
ATOM   7455  N  N   . LEU   D  1 143 ? 66.544 -53.241 49.482  1.00 18.93 ? 143  LEU   D N   1 
ATOM   7456  C  CA  . LEU   D  1 143 ? 67.968 -53.392 49.762  1.00 19.35 ? 143  LEU   D CA  1 
ATOM   7457  C  C   . LEU   D  1 143 ? 68.088 -53.407 51.285  1.00 19.25 ? 143  LEU   D C   1 
ATOM   7458  O  O   . LEU   D  1 143 ? 67.732 -52.413 51.957  1.00 19.26 ? 143  LEU   D O   1 
ATOM   7459  C  CB  . LEU   D  1 143 ? 68.765 -52.253 49.106  1.00 20.79 ? 143  LEU   D CB  1 
ATOM   7460  C  CG  . LEU   D  1 143 ? 70.267 -52.282 49.270  1.00 23.05 ? 143  LEU   D CG  1 
ATOM   7461  C  CD1 . LEU   D  1 143 ? 70.883 -53.532 48.636  1.00 23.51 ? 143  LEU   D CD1 1 
ATOM   7462  C  CD2 . LEU   D  1 143 ? 70.864 -51.038 48.588  1.00 21.74 ? 143  LEU   D CD2 1 
ATOM   7463  N  N   . GLY   D  1 144 ? 68.477 -54.558 51.836  1.00 18.05 ? 144  GLY   D N   1 
ATOM   7464  C  CA  . GLY   D  1 144 ? 68.573 -54.730 53.273  1.00 19.79 ? 144  GLY   D CA  1 
ATOM   7465  C  C   . GLY   D  1 144 ? 70.027 -54.720 53.707  1.00 18.80 ? 144  GLY   D C   1 
ATOM   7466  O  O   . GLY   D  1 144 ? 70.870 -55.336 53.060  1.00 19.58 ? 144  GLY   D O   1 
ATOM   7467  N  N   . ILE   D  1 145 ? 70.310 -53.936 54.748  1.00 17.99 ? 145  ILE   D N   1 
ATOM   7468  C  CA  . ILE   D  1 145 ? 71.668 -53.734 55.250  1.00 20.26 ? 145  ILE   D CA  1 
ATOM   7469  C  C   . ILE   D  1 145 ? 71.690 -53.923 56.768  1.00 20.46 ? 145  ILE   D C   1 
ATOM   7470  O  O   . ILE   D  1 145 ? 70.885 -53.312 57.484  1.00 20.45 ? 145  ILE   D O   1 
ATOM   7471  C  CB  . ILE   D  1 145 ? 72.160 -52.332 54.881  1.00 20.40 ? 145  ILE   D CB  1 
ATOM   7472  C  CG1 . ILE   D  1 145 ? 72.081 -52.155 53.346  1.00 21.88 ? 145  ILE   D CG1 1 
ATOM   7473  C  CG2 . ILE   D  1 145 ? 73.593 -52.112 55.434  1.00 21.40 ? 145  ILE   D CG2 1 
ATOM   7474  C  CD1 . ILE   D  1 145 ? 72.495 -50.762 52.788  1.00 25.03 ? 145  ILE   D CD1 1 
ATOM   7475  N  N   . PHE   D  1 146 ? 72.598 -54.777 57.253  1.00 20.25 ? 146  PHE   D N   1 
ATOM   7476  C  CA  . PHE   D  1 146 ? 72.706 -55.037 58.683  1.00 19.24 ? 146  PHE   D CA  1 
ATOM   7477  C  C   . PHE   D  1 146 ? 73.489 -53.937 59.388  1.00 21.90 ? 146  PHE   D C   1 
ATOM   7478  O  O   . PHE   D  1 146 ? 74.446 -53.389 58.830  1.00 22.54 ? 146  PHE   D O   1 
ATOM   7479  C  CB  . PHE   D  1 146 ? 73.396 -56.382 58.946  1.00 18.77 ? 146  PHE   D CB  1 
ATOM   7480  C  CG  . PHE   D  1 146 ? 72.635 -57.563 58.405  1.00 20.64 ? 146  PHE   D CG  1 
ATOM   7481  C  CD1 . PHE   D  1 146 ? 71.371 -57.880 58.902  1.00 19.07 ? 146  PHE   D CD1 1 
ATOM   7482  C  CD2 . PHE   D  1 146 ? 73.172 -58.344 57.387  1.00 21.11 ? 146  PHE   D CD2 1 
ATOM   7483  C  CE1 . PHE   D  1 146 ? 70.662 -58.981 58.420  1.00 21.30 ? 146  PHE   D CE1 1 
ATOM   7484  C  CE2 . PHE   D  1 146 ? 72.489 -59.456 56.889  1.00 20.82 ? 146  PHE   D CE2 1 
ATOM   7485  C  CZ  . PHE   D  1 146 ? 71.208 -59.782 57.406  1.00 21.56 ? 146  PHE   D CZ  1 
ATOM   7486  N  N   . LEU   D  1 147 ? 73.084 -53.620 60.624  1.00 20.86 ? 147  LEU   D N   1 
ATOM   7487  C  CA  . LEU   D  1 147 ? 73.813 -52.688 61.489  1.00 21.29 ? 147  LEU   D CA  1 
ATOM   7488  C  C   . LEU   D  1 147 ? 74.464 -53.475 62.619  1.00 22.19 ? 147  LEU   D C   1 
ATOM   7489  O  O   . LEU   D  1 147 ? 73.765 -54.126 63.422  1.00 23.14 ? 147  LEU   D O   1 
ATOM   7490  C  CB  . LEU   D  1 147 ? 72.897 -51.622 62.085  1.00 21.35 ? 147  LEU   D CB  1 
ATOM   7491  C  CG  . LEU   D  1 147 ? 72.523 -50.431 61.189  1.00 20.35 ? 147  LEU   D CG  1 
ATOM   7492  C  CD1 . LEU   D  1 147 ? 71.682 -50.848 59.972  1.00 21.07 ? 147  LEU   D CD1 1 
ATOM   7493  C  CD2 . LEU   D  1 147 ? 71.793 -49.341 61.987  1.00 21.04 ? 147  LEU   D CD2 1 
ATOM   7494  N  N   . LYS   D  1 148 ? 75.784 -53.377 62.708  1.00 23.19 ? 148  LYS   D N   1 
ATOM   7495  C  CA  . LYS   D  1 148 ? 76.553 -54.022 63.749  1.00 25.00 ? 148  LYS   D CA  1 
ATOM   7496  C  C   . LYS   D  1 148 ? 77.073 -52.963 64.705  1.00 27.84 ? 148  LYS   D C   1 
ATOM   7497  O  O   . LYS   D  1 148 ? 77.587 -51.937 64.261  1.00 31.56 ? 148  LYS   D O   1 
ATOM   7498  C  CB  . LYS   D  1 148 ? 77.726 -54.802 63.110  1.00 30.59 ? 148  LYS   D CB  1 
ATOM   7499  C  CG  . LYS   D  1 148 ? 78.690 -55.459 64.041  1.00 38.10 ? 148  LYS   D CG  1 
ATOM   7500  C  CD  . LYS   D  1 148 ? 79.831 -56.080 63.192  1.00 43.64 ? 148  LYS   D CD  1 
ATOM   7501  C  CE  . LYS   D  1 148 ? 80.900 -56.822 64.034  1.00 51.48 ? 148  LYS   D CE  1 
ATOM   7502  N  NZ  . LYS   D  1 148 ? 80.349 -57.724 65.089  1.00 55.65 ? 148  LYS   D NZ  1 
ATOM   7503  N  N   . VAL   D  1 149 ? 77.012 -53.249 66.010  1.00 27.74 ? 149  VAL   D N   1 
ATOM   7504  C  CA  . VAL   D  1 149 ? 77.485 -52.312 67.031  1.00 32.05 ? 149  VAL   D CA  1 
ATOM   7505  C  C   . VAL   D  1 149 ? 79.007 -52.222 67.005  1.00 31.59 ? 149  VAL   D C   1 
ATOM   7506  O  O   . VAL   D  1 149 ? 79.717 -53.235 67.065  1.00 35.24 ? 149  VAL   D O   1 
ATOM   7507  C  CB  . VAL   D  1 149 ? 76.985 -52.728 68.425  1.00 35.05 ? 149  VAL   D CB  1 
ATOM   7508  C  CG1 . VAL   D  1 149 ? 77.682 -51.904 69.501  1.00 38.60 ? 149  VAL   D CG1 1 
ATOM   7509  C  CG2 . VAL   D  1 149 ? 75.487 -52.512 68.518  1.00 34.96 ? 149  VAL   D CG2 1 
ATOM   7510  N  N   . GLY   D  1 150 ? 79.510 -50.999 66.954  1.00 30.62 ? 150  GLY   D N   1 
ATOM   7511  C  CA  . GLY   D  1 150 ? 80.931 -50.730 66.911  1.00 32.59 ? 150  GLY   D CA  1 
ATOM   7512  C  C   . GLY   D  1 150 ? 81.119 -49.230 66.917  1.00 33.16 ? 150  GLY   D C   1 
ATOM   7513  O  O   . GLY   D  1 150 ? 80.528 -48.564 67.770  1.00 33.18 ? 150  GLY   D O   1 
ATOM   7514  N  N   . SER   D  1 151 ? 81.934 -48.700 65.995  1.00 34.76 ? 151  SER   D N   1 
ATOM   7515  C  CA  . SER   D  1 151 ? 82.186 -47.265 65.910  1.00 31.84 ? 151  SER   D CA  1 
ATOM   7516  C  C   . SER   D  1 151 ? 80.946 -46.546 65.398  1.00 29.54 ? 151  SER   D C   1 
ATOM   7517  O  O   . SER   D  1 151 ? 80.137 -47.116 64.680  1.00 30.81 ? 151  SER   D O   1 
ATOM   7518  C  CB  . SER   D  1 151 ? 83.333 -46.986 64.963  1.00 35.20 ? 151  SER   D CB  1 
ATOM   7519  O  OG  . SER   D  1 151 ? 84.529 -47.477 65.505  1.00 43.03 ? 151  SER   D OG  1 
ATOM   7520  N  N   . ALA   D  1 152 ? 80.807 -45.286 65.783  1.00 32.40 ? 152  ALA   D N   1 
ATOM   7521  C  CA  . ALA   D  1 152 ? 79.674 -44.490 65.322  1.00 32.38 ? 152  ALA   D CA  1 
ATOM   7522  C  C   . ALA   D  1 152 ? 79.767 -44.274 63.810  1.00 33.18 ? 152  ALA   D C   1 
ATOM   7523  O  O   . ALA   D  1 152 ? 80.863 -44.143 63.254  1.00 35.20 ? 152  ALA   D O   1 
ATOM   7524  C  CB  . ALA   D  1 152 ? 79.660 -43.147 66.062  1.00 31.70 ? 152  ALA   D CB  1 
ATOM   7525  N  N   . LEU   D  1 153 ? 78.604 -44.234 63.142  1.00 30.09 ? 153  LEU   D N   1 
ATOM   7526  C  CA  . LEU   D  1 153 ? 78.546 -44.029 61.703  1.00 27.97 ? 153  LEU   D CA  1 
ATOM   7527  C  C   . LEU   D  1 153 ? 78.228 -42.575 61.415  1.00 26.21 ? 153  LEU   D C   1 
ATOM   7528  O  O   . LEU   D  1 153 ? 77.104 -42.136 61.705  1.00 26.33 ? 153  LEU   D O   1 
ATOM   7529  C  CB  . LEU   D  1 153 ? 77.488 -44.929 61.069  1.00 28.02 ? 153  LEU   D CB  1 
ATOM   7530  C  CG  . LEU   D  1 153 ? 77.439 -44.993 59.532  1.00 30.74 ? 153  LEU   D CG  1 
ATOM   7531  C  CD1 . LEU   D  1 153 ? 78.761 -45.569 58.908  1.00 30.59 ? 153  LEU   D CD1 1 
ATOM   7532  C  CD2 . LEU   D  1 153 ? 76.240 -45.802 59.077  1.00 27.52 ? 153  LEU   D CD2 1 
ATOM   7533  N  N   . PRO   D  1 154 ? 79.111 -41.822 60.797  1.00 27.65 ? 154  PRO   D N   1 
ATOM   7534  C  CA  . PRO   D  1 154 ? 78.803 -40.392 60.595  1.00 28.64 ? 154  PRO   D CA  1 
ATOM   7535  C  C   . PRO   D  1 154 ? 77.607 -40.189 59.693  1.00 27.92 ? 154  PRO   D C   1 
ATOM   7536  O  O   . PRO   D  1 154 ? 76.817 -39.261 59.913  1.00 30.50 ? 154  PRO   D O   1 
ATOM   7537  C  CB  . PRO   D  1 154 ? 80.117 -39.827 60.003  1.00 31.93 ? 154  PRO   D CB  1 
ATOM   7538  C  CG  . PRO   D  1 154 ? 81.181 -40.789 60.500  1.00 33.69 ? 154  PRO   D CG  1 
ATOM   7539  C  CD  . PRO   D  1 154 ? 80.512 -42.144 60.466  1.00 31.82 ? 154  PRO   D CD  1 
ATOM   7540  N  N   . GLY   D  1 155 ? 77.402 -41.079 58.719  1.00 28.09 ? 155  GLY   D N   1 
ATOM   7541  C  CA  . GLY   D  1 155 ? 76.280 -40.970 57.815  1.00 27.26 ? 155  GLY   D CA  1 
ATOM   7542  C  C   . GLY   D  1 155 ? 74.939 -41.177 58.470  1.00 25.26 ? 155  GLY   D C   1 
ATOM   7543  O  O   . GLY   D  1 155 ? 73.913 -40.868 57.864  1.00 27.01 ? 155  GLY   D O   1 
ATOM   7544  N  N   . LEU   D  1 156 ? 74.918 -41.722 59.681  1.00 24.09 ? 156  LEU   D N   1 
ATOM   7545  C  CA  . LEU   D  1 156 ? 73.664 -41.897 60.404  1.00 24.29 ? 156  LEU   D CA  1 
ATOM   7546  C  C   . LEU   D  1 156 ? 73.342 -40.708 61.309  1.00 25.15 ? 156  LEU   D C   1 
ATOM   7547  O  O   . LEU   D  1 156 ? 72.214 -40.590 61.787  1.00 24.40 ? 156  LEU   D O   1 
ATOM   7548  C  CB  . LEU   D  1 156 ? 73.754 -43.194 61.235  1.00 24.29 ? 156  LEU   D CB  1 
ATOM   7549  C  CG  . LEU   D  1 156 ? 72.504 -43.692 61.979  1.00 24.36 ? 156  LEU   D CG  1 
ATOM   7550  C  CD1 . LEU   D  1 156 ? 71.339 -43.951 61.014  1.00 21.29 ? 156  LEU   D CD1 1 
ATOM   7551  C  CD2 . LEU   D  1 156 ? 72.832 -44.923 62.804  1.00 24.17 ? 156  LEU   D CD2 1 
ATOM   7552  N  N   . GLN   D  1 157 ? 74.283 -39.797 61.548  1.00 25.50 ? 157  GLN   D N   1 
ATOM   7553  C  CA  . GLN   D  1 157 ? 74.073 -38.848 62.632  1.00 27.21 ? 157  GLN   D CA  1 
ATOM   7554  C  C   . GLN   D  1 157 ? 72.907 -37.900 62.338  1.00 26.89 ? 157  GLN   D C   1 
ATOM   7555  O  O   . GLN   D  1 157 ? 72.151 -37.545 63.248  1.00 26.97 ? 157  GLN   D O   1 
ATOM   7556  C  CB  . GLN   D  1 157 ? 75.367 -38.072 62.905  1.00 29.97 ? 157  GLN   D CB  1 
ATOM   7557  C  CG  . GLN   D  1 157 ? 75.391 -37.425 64.294  1.00 34.71 ? 157  GLN   D CG  1 
ATOM   7558  C  CD  . GLN   D  1 157 ? 75.127 -38.439 65.447  1.00 39.56 ? 157  GLN   D CD  1 
ATOM   7559  O  OE1 . GLN   D  1 157 ? 75.673 -39.553 65.480  1.00 38.85 ? 157  GLN   D OE1 1 
ATOM   7560  N  NE2 . GLN   D  1 157 ? 74.316 -38.031 66.404  1.00 37.42 ? 157  GLN   D NE2 1 
ATOM   7561  N  N   . LYS   D  1 158 ? 72.691 -37.525 61.076  1.00 25.66 ? 158  LYS   D N   1 
ATOM   7562  C  CA  . LYS   D  1 158 ? 71.591 -36.611 60.787  1.00 27.46 ? 158  LYS   D CA  1 
ATOM   7563  C  C   . LYS   D  1 158 ? 70.251 -37.243 61.111  1.00 23.81 ? 158  LYS   D C   1 
ATOM   7564  O  O   . LYS   D  1 158 ? 69.306 -36.568 61.546  1.00 27.04 ? 158  LYS   D O   1 
ATOM   7565  C  CB  . LYS   D  1 158 ? 71.617 -36.193 59.321  1.00 29.70 ? 158  LYS   D CB  1 
ATOM   7566  C  CG  . LYS   D  1 158 ? 70.625 -35.065 59.001  1.00 32.64 ? 158  LYS   D CG  1 
ATOM   7567  C  CD  . LYS   D  1 158 ? 70.425 -34.934 57.506  1.00 34.68 ? 158  LYS   D CD  1 
ATOM   7568  C  CE  . LYS   D  1 158 ? 69.314 -33.898 57.129  1.00 34.98 ? 158  LYS   D CE  1 
ATOM   7569  N  NZ  . LYS   D  1 158 ? 69.949 -32.578 57.012  1.00 35.91 ? 158  LYS   D NZ  1 
ATOM   7570  N  N   . VAL   D  1 159 ? 70.135 -38.552 60.868  1.00 20.68 ? 159  VAL   D N   1 
ATOM   7571  C  CA  . VAL   D  1 159 ? 68.923 -39.268 61.225  1.00 20.16 ? 159  VAL   D CA  1 
ATOM   7572  C  C   . VAL   D  1 159 ? 68.732 -39.234 62.731  1.00 23.22 ? 159  VAL   D C   1 
ATOM   7573  O  O   . VAL   D  1 159 ? 67.682 -38.838 63.243  1.00 23.83 ? 159  VAL   D O   1 
ATOM   7574  C  CB  . VAL   D  1 159 ? 68.995 -40.711 60.715  1.00 21.81 ? 159  VAL   D CB  1 
ATOM   7575  C  CG1 . VAL   D  1 159 ? 67.805 -41.495 61.265  1.00 21.65 ? 159  VAL   D CG1 1 
ATOM   7576  C  CG2 . VAL   D  1 159 ? 69.000 -40.819 59.149  1.00 23.13 ? 159  VAL   D CG2 1 
ATOM   7577  N  N   . VAL   D  1 160 ? 69.731 -39.701 63.478  1.00 24.82 ? 160  VAL   D N   1 
ATOM   7578  C  CA  A VAL   D  1 160 ? 69.598 -39.807 64.932  0.39 27.92 ? 160  VAL   D CA  1 
ATOM   7579  C  CA  B VAL   D  1 160 ? 69.456 -39.822 64.899  0.61 27.59 ? 160  VAL   D CA  1 
ATOM   7580  C  C   . VAL   D  1 160 ? 69.248 -38.460 65.541  1.00 29.74 ? 160  VAL   D C   1 
ATOM   7581  O  O   . VAL   D  1 160 ? 68.475 -38.358 66.504  1.00 31.21 ? 160  VAL   D O   1 
ATOM   7582  C  CB  A VAL   D  1 160 ? 70.899 -40.374 65.534  0.39 31.22 ? 160  VAL   D CB  1 
ATOM   7583  C  CB  B VAL   D  1 160 ? 70.549 -40.652 65.595  0.61 30.88 ? 160  VAL   D CB  1 
ATOM   7584  C  CG1 A VAL   D  1 160 ? 71.048 -39.922 66.980  0.39 33.15 ? 160  VAL   D CG1 1 
ATOM   7585  C  CG1 B VAL   D  1 160 ? 70.504 -42.088 65.058  0.61 31.04 ? 160  VAL   D CG1 1 
ATOM   7586  C  CG2 A VAL   D  1 160 ? 70.903 -41.886 65.431  0.39 32.27 ? 160  VAL   D CG2 1 
ATOM   7587  C  CG2 B VAL   D  1 160 ? 71.892 -40.024 65.399  0.61 31.42 ? 160  VAL   D CG2 1 
ATOM   7588  N  N   . ASP   D  1 161 ? 69.812 -37.395 64.987  1.00 29.29 ? 161  ASP   D N   1 
ATOM   7589  C  CA  . ASP   D  1 161 ? 69.660 -36.079 65.585  1.00 32.06 ? 161  ASP   D CA  1 
ATOM   7590  C  C   . ASP   D  1 161 ? 68.234 -35.546 65.501  1.00 31.50 ? 161  ASP   D C   1 
ATOM   7591  O  O   . ASP   D  1 161 ? 67.887 -34.657 66.292  1.00 40.48 ? 161  ASP   D O   1 
ATOM   7592  C  CB  . ASP   D  1 161 ? 70.596 -35.073 64.921  1.00 34.89 ? 161  ASP   D CB  1 
ATOM   7593  C  CG  . ASP   D  1 161 ? 72.054 -35.227 65.371  1.00 35.08 ? 161  ASP   D CG  1 
ATOM   7594  O  OD1 . ASP   D  1 161 ? 72.312 -35.940 66.375  1.00 36.61 ? 161  ASP   D OD1 1 
ATOM   7595  O  OD2 . ASP   D  1 161 ? 72.934 -34.634 64.712  1.00 37.77 ? 161  ASP   D OD2 1 
ATOM   7596  N  N   . VAL   D  1 162 ? 67.425 -36.029 64.537  1.00 25.59 ? 162  VAL   D N   1 
ATOM   7597  C  CA  . VAL   D  1 162 ? 66.071 -35.506 64.307  1.00 26.24 ? 162  VAL   D CA  1 
ATOM   7598  C  C   . VAL   D  1 162 ? 65.021 -36.324 65.047  1.00 25.36 ? 162  VAL   D C   1 
ATOM   7599  O  O   . VAL   D  1 162 ? 63.866 -35.894 65.138  1.00 26.12 ? 162  VAL   D O   1 
ATOM   7600  C  CB  . VAL   D  1 162 ? 65.739 -35.512 62.790  1.00 25.14 ? 162  VAL   D CB  1 
ATOM   7601  C  CG1 . VAL   D  1 162 ? 65.307 -36.856 62.293  1.00 26.44 ? 162  VAL   D CG1 1 
ATOM   7602  C  CG2 . VAL   D  1 162 ? 64.694 -34.419 62.425  1.00 28.10 ? 162  VAL   D CG2 1 
ATOM   7603  N  N   . LEU   D  1 163 ? 65.397 -37.474 65.612  1.00 25.48 ? 163  LEU   D N   1 
ATOM   7604  C  CA  . LEU   D  1 163 ? 64.360 -38.377 66.119  1.00 23.98 ? 163  LEU   D CA  1 
ATOM   7605  C  C   . LEU   D  1 163 ? 63.595 -37.783 67.312  1.00 28.14 ? 163  LEU   D C   1 
ATOM   7606  O  O   . LEU   D  1 163 ? 62.409 -38.115 67.514  1.00 24.78 ? 163  LEU   D O   1 
ATOM   7607  C  CB  . LEU   D  1 163 ? 64.976 -39.728 66.480  1.00 23.40 ? 163  LEU   D CB  1 
ATOM   7608  C  CG  . LEU   D  1 163 ? 65.572 -40.494 65.277  1.00 22.72 ? 163  LEU   D CG  1 
ATOM   7609  C  CD1 . LEU   D  1 163 ? 66.152 -41.875 65.768  1.00 22.95 ? 163  LEU   D CD1 1 
ATOM   7610  C  CD2 . LEU   D  1 163 ? 64.554 -40.689 64.164  1.00 21.80 ? 163  LEU   D CD2 1 
ATOM   7611  N  N   . ASP   D  1 164 ? 64.248 -36.948 68.143  1.00 31.07 ? 164  ASP   D N   1 
ATOM   7612  C  CA  . ASP   D  1 164 ? 63.521 -36.391 69.282  1.00 34.00 ? 164  ASP   D CA  1 
ATOM   7613  C  C   . ASP   D  1 164 ? 62.392 -35.475 68.847  1.00 31.24 ? 164  ASP   D C   1 
ATOM   7614  O  O   . ASP   D  1 164 ? 61.513 -35.163 69.664  1.00 33.03 ? 164  ASP   D O   1 
ATOM   7615  C  CB  . ASP   D  1 164 ? 64.461 -35.629 70.234  1.00 45.17 ? 164  ASP   D CB  1 
ATOM   7616  C  CG  . ASP   D  1 164 ? 65.152 -36.555 71.257  1.00 55.28 ? 164  ASP   D CG  1 
ATOM   7617  O  OD1 . ASP   D  1 164 ? 64.661 -37.686 71.500  1.00 56.66 ? 164  ASP   D OD1 1 
ATOM   7618  O  OD2 . ASP   D  1 164 ? 66.203 -36.164 71.818  1.00 59.90 ? 164  ASP   D OD2 1 
ATOM   7619  N  N   . SER   D  1 165 ? 62.371 -35.062 67.586  1.00 26.31 ? 165  SER   D N   1 
ATOM   7620  C  CA  . SER   D  1 165 ? 61.291 -34.241 67.080  1.00 25.91 ? 165  SER   D CA  1 
ATOM   7621  C  C   . SER   D  1 165 ? 60.109 -35.042 66.521  1.00 23.29 ? 165  SER   D C   1 
ATOM   7622  O  O   . SER   D  1 165 ? 59.066 -34.429 66.189  1.00 26.75 ? 165  SER   D O   1 
ATOM   7623  C  CB  . SER   D  1 165 ? 61.808 -33.256 66.025  1.00 33.07 ? 165  SER   D CB  1 
ATOM   7624  O  OG  . SER   D  1 165 ? 62.061 -33.907 64.804  1.00 33.09 ? 165  SER   D OG  1 
ATOM   7625  N  N   . ILE   D  1 166 ? 60.212 -36.373 66.446  1.00 22.39 ? 166  ILE   D N   1 
ATOM   7626  C  CA  . ILE   D  1 166 ? 59.107 -37.179 65.910  1.00 20.56 ? 166  ILE   D CA  1 
ATOM   7627  C  C   . ILE   D  1 166 ? 58.818 -38.343 66.859  1.00 21.81 ? 166  ILE   D C   1 
ATOM   7628  O  O   . ILE   D  1 166 ? 58.728 -39.496 66.434  1.00 19.09 ? 166  ILE   D O   1 
ATOM   7629  C  CB  . ILE   D  1 166 ? 59.418 -37.662 64.475  1.00 18.29 ? 166  ILE   D CB  1 
ATOM   7630  C  CG1 . ILE   D  1 166 ? 60.732 -38.435 64.408  1.00 18.14 ? 166  ILE   D CG1 1 
ATOM   7631  C  CG2 . ILE   D  1 166 ? 59.440 -36.422 63.512  1.00 21.13 ? 166  ILE   D CG2 1 
ATOM   7632  C  CD1 . ILE   D  1 166 ? 60.746 -39.419 63.171  1.00 17.86 ? 166  ILE   D CD1 1 
ATOM   7633  N  N   . LYS   D  1 167 ? 58.655 -38.048 68.153  1.00 20.30 ? 167  LYS   D N   1 
ATOM   7634  C  CA  . LYS   D  1 167 ? 58.681 -39.105 69.149  1.00 21.62 ? 167  LYS   D CA  1 
ATOM   7635  C  C   . LYS   D  1 167 ? 57.461 -40.012 69.028  1.00 21.26 ? 167  LYS   D C   1 
ATOM   7636  O  O   . LYS   D  1 167 ? 57.545 -41.195 69.332  1.00 22.07 ? 167  LYS   D O   1 
ATOM   7637  C  CB  . LYS   D  1 167 ? 58.755 -38.491 70.575  1.00 23.50 ? 167  LYS   D CB  1 
ATOM   7638  C  CG  . LYS   D  1 167 ? 58.793 -39.551 71.687  1.00 31.48 ? 167  LYS   D CG  1 
ATOM   7639  C  CD  . LYS   D  1 167 ? 58.846 -38.862 73.083  1.00 36.80 ? 167  LYS   D CD  1 
ATOM   7640  C  CE  . LYS   D  1 167 ? 58.868 -39.891 74.193  1.00 44.22 ? 167  LYS   D CE  1 
ATOM   7641  N  NZ  . LYS   D  1 167 ? 58.719 -39.189 75.493  1.00 50.72 ? 167  LYS   D NZ  1 
ATOM   7642  N  N   . THR   D  1 168 ? 56.291 -39.447 68.693  1.00 19.38 ? 168  THR   D N   1 
ATOM   7643  C  CA  . THR   D  1 168 ? 55.057 -40.229 68.718  1.00 18.51 ? 168  THR   D CA  1 
ATOM   7644  C  C   . THR   D  1 168 ? 54.443 -40.405 67.330  1.00 19.84 ? 168  THR   D C   1 
ATOM   7645  O  O   . THR   D  1 168 ? 54.751 -39.687 66.368  1.00 18.55 ? 168  THR   D O   1 
ATOM   7646  C  CB  . THR   D  1 168 ? 54.043 -39.571 69.691  1.00 21.75 ? 168  THR   D CB  1 
ATOM   7647  O  OG1 . THR   D  1 168 ? 53.929 -38.194 69.357  1.00 23.16 ? 168  THR   D OG1 1 
ATOM   7648  C  CG2 . THR   D  1 168 ? 54.532 -39.687 71.128  1.00 23.55 ? 168  THR   D CG2 1 
ATOM   7649  N  N   . LYS   D  1 169 ? 53.530 -41.371 67.239  1.00 19.44 ? 169  LYS   D N   1 
ATOM   7650  C  CA  . LYS   D  1 169 ? 52.913 -41.708 65.967  1.00 19.46 ? 169  LYS   D CA  1 
ATOM   7651  C  C   . LYS   D  1 169 ? 52.304 -40.492 65.269  1.00 20.19 ? 169  LYS   D C   1 
ATOM   7652  O  O   . LYS   D  1 169 ? 51.539 -39.722 65.873  1.00 19.48 ? 169  LYS   D O   1 
ATOM   7653  C  CB  . LYS   D  1 169 ? 51.807 -42.763 66.180  1.00 18.65 ? 169  LYS   D CB  1 
ATOM   7654  C  CG  . LYS   D  1 169 ? 51.161 -43.178 64.870  1.00 18.32 ? 169  LYS   D CG  1 
ATOM   7655  C  CD  . LYS   D  1 169 ? 50.101 -44.315 65.046  1.00 19.49 ? 169  LYS   D CD  1 
ATOM   7656  C  CE  . LYS   D  1 169 ? 49.495 -44.654 63.685  1.00 21.12 ? 169  LYS   D CE  1 
ATOM   7657  N  NZ  . LYS   D  1 169 ? 48.552 -45.868 63.827  1.00 26.05 ? 169  LYS   D NZ  1 
ATOM   7658  N  N   . GLY   D  1 170 ? 52.577 -40.391 63.967  1.00 18.40 ? 170  GLY   D N   1 
ATOM   7659  C  CA  . GLY   D  1 170 ? 52.016 -39.354 63.136  1.00 18.98 ? 170  GLY   D CA  1 
ATOM   7660  C  C   . GLY   D  1 170 ? 52.894 -38.118 63.049  1.00 20.71 ? 170  GLY   D C   1 
ATOM   7661  O  O   . GLY   D  1 170 ? 52.616 -37.233 62.218  1.00 22.15 ? 170  GLY   D O   1 
ATOM   7662  N  N   . LYS   D  1 171 ? 53.879 -37.980 63.943  1.00 18.20 ? 171  LYS   D N   1 
ATOM   7663  C  CA  . LYS   D  1 171 ? 54.708 -36.786 63.883  1.00 19.47 ? 171  LYS   D CA  1 
ATOM   7664  C  C   . LYS   D  1 171 ? 55.649 -36.908 62.701  1.00 19.41 ? 171  LYS   D C   1 
ATOM   7665  O  O   . LYS   D  1 171 ? 56.152 -37.990 62.389  1.00 19.30 ? 171  LYS   D O   1 
ATOM   7666  C  CB  . LYS   D  1 171 ? 55.518 -36.570 65.158  1.00 20.34 ? 171  LYS   D CB  1 
ATOM   7667  C  CG  . LYS   D  1 171 ? 54.678 -36.269 66.377  1.00 22.24 ? 171  LYS   D CG  1 
ATOM   7668  C  CD  . LYS   D  1 171 ? 55.506 -35.675 67.506  1.00 27.95 ? 171  LYS   D CD  1 
ATOM   7669  C  CE  . LYS   D  1 171 ? 55.906 -34.223 67.250  1.00 29.68 ? 171  LYS   D CE  1 
ATOM   7670  N  NZ  . LYS   D  1 171 ? 56.624 -33.604 68.445  1.00 33.89 ? 171  LYS   D NZ  1 
ATOM   7671  N  N   . SER   D  1 172 ? 55.918 -35.776 62.055  1.00 20.22 ? 172  SER   D N   1 
ATOM   7672  C  CA  A SER   D  1 172 ? 56.839 -35.740 60.938  0.50 20.19 ? 172  SER   D CA  1 
ATOM   7673  C  CA  B SER   D  1 172 ? 56.764 -35.692 60.871  0.50 20.09 ? 172  SER   D CA  1 
ATOM   7674  C  C   . SER   D  1 172 ? 57.658 -34.462 60.991  1.00 20.28 ? 172  SER   D C   1 
ATOM   7675  O  O   . SER   D  1 172 ? 57.364 -33.524 61.756  1.00 22.62 ? 172  SER   D O   1 
ATOM   7676  C  CB  A SER   D  1 172 ? 56.105 -35.820 59.612  0.50 20.95 ? 172  SER   D CB  1 
ATOM   7677  C  CB  B SER   D  1 172 ? 55.911 -35.626 59.586  0.50 21.32 ? 172  SER   D CB  1 
ATOM   7678  O  OG  A SER   D  1 172 ? 55.268 -34.683 59.480  0.50 20.59 ? 172  SER   D OG  1 
ATOM   7679  O  OG  B SER   D  1 172 ? 56.659 -35.486 58.376  0.50 20.34 ? 172  SER   D OG  1 
ATOM   7680  N  N   . ALA   D  1 173 ? 58.725 -34.448 60.203  1.00 18.66 ? 173  ALA   D N   1 
ATOM   7681  C  CA  . ALA   D  1 173 ? 59.604 -33.274 60.145  1.00 18.94 ? 173  ALA   D CA  1 
ATOM   7682  C  C   . ALA   D  1 173 ? 60.245 -33.203 58.769  1.00 17.40 ? 173  ALA   D C   1 
ATOM   7683  O  O   . ALA   D  1 173 ? 60.513 -34.232 58.136  1.00 19.06 ? 173  ALA   D O   1 
ATOM   7684  C  CB  . ALA   D  1 173 ? 60.712 -33.306 61.233  1.00 20.88 ? 173  ALA   D CB  1 
ATOM   7685  N  N   . ASP   D  1 174 ? 60.524 -31.966 58.309  1.00 18.09 ? 174  ASP   D N   1 
ATOM   7686  C  CA  . ASP   D  1 174 ? 61.330 -31.837 57.106  1.00 20.51 ? 174  ASP   D CA  1 
ATOM   7687  C  C   . ASP   D  1 174 ? 62.677 -32.527 57.287  1.00 22.88 ? 174  ASP   D C   1 
ATOM   7688  O  O   . ASP   D  1 174 ? 63.270 -32.483 58.369  1.00 21.69 ? 174  ASP   D O   1 
ATOM   7689  C  CB  . ASP   D  1 174 ? 61.630 -30.374 56.776  1.00 19.87 ? 174  ASP   D CB  1 
ATOM   7690  C  CG  . ASP   D  1 174 ? 60.386 -29.505 56.569  1.00 24.56 ? 174  ASP   D CG  1 
ATOM   7691  O  OD1 . ASP   D  1 174 ? 59.348 -30.037 56.207  1.00 24.43 ? 174  ASP   D OD1 1 
ATOM   7692  O  OD2 . ASP   D  1 174 ? 60.533 -28.276 56.650  1.00 31.86 ? 174  ASP   D OD2 1 
ATOM   7693  N  N   . PHE   D  1 175 ? 63.168 -33.122 56.210  1.00 18.39 ? 175  PHE   D N   1 
ATOM   7694  C  CA  . PHE   D  1 175 ? 64.404 -33.907 56.321  1.00 19.31 ? 175  PHE   D CA  1 
ATOM   7695  C  C   . PHE   D  1 175 ? 65.045 -33.866 54.932  1.00 19.35 ? 175  PHE   D C   1 
ATOM   7696  O  O   . PHE   D  1 175 ? 64.867 -34.791 54.116  1.00 21.38 ? 175  PHE   D O   1 
ATOM   7697  C  CB  . PHE   D  1 175 ? 64.128 -35.328 56.777  1.00 20.05 ? 175  PHE   D CB  1 
ATOM   7698  C  CG  . PHE   D  1 175 ? 65.356 -36.054 57.256  1.00 21.73 ? 175  PHE   D CG  1 
ATOM   7699  C  CD1 . PHE   D  1 175 ? 65.894 -35.749 58.498  1.00 24.31 ? 175  PHE   D CD1 1 
ATOM   7700  C  CD2 . PHE   D  1 175 ? 65.981 -36.989 56.452  1.00 19.55 ? 175  PHE   D CD2 1 
ATOM   7701  C  CE1 . PHE   D  1 175 ? 67.050 -36.425 58.965  1.00 25.75 ? 175  PHE   D CE1 1 
ATOM   7702  C  CE2 . PHE   D  1 175 ? 67.132 -37.683 56.907  1.00 21.50 ? 175  PHE   D CE2 1 
ATOM   7703  C  CZ  . PHE   D  1 175 ? 67.654 -37.406 58.134  1.00 23.75 ? 175  PHE   D CZ  1 
ATOM   7704  N  N   . THR   D  1 176 ? 65.856 -32.851 54.714  1.00 19.06 ? 176  THR   D N   1 
ATOM   7705  C  CA  . THR   D  1 176 ? 66.335 -32.509 53.387  1.00 20.85 ? 176  THR   D CA  1 
ATOM   7706  C  C   . THR   D  1 176 ? 67.844 -32.713 53.280  1.00 24.75 ? 176  THR   D C   1 
ATOM   7707  O  O   . THR   D  1 176 ? 68.567 -32.799 54.273  1.00 25.06 ? 176  THR   D O   1 
ATOM   7708  C  CB  . THR   D  1 176 ? 65.968 -31.070 53.048  1.00 23.14 ? 176  THR   D CB  1 
ATOM   7709  O  OG1 . THR   D  1 176 ? 66.489 -30.217 54.061  1.00 23.30 ? 176  THR   D OG1 1 
ATOM   7710  C  CG2 . THR   D  1 176 ? 64.443 -30.896 53.014  1.00 24.33 ? 176  THR   D CG2 1 
ATOM   7711  N  N   . ASN   D  1 177 ? 68.294 -32.862 52.049  1.00 24.83 ? 177  ASN   D N   1 
ATOM   7712  C  CA  . ASN   D  1 177 ? 69.726 -32.952 51.753  1.00 27.31 ? 177  ASN   D CA  1 
ATOM   7713  C  C   . ASN   D  1 177 ? 70.404 -34.154 52.431  1.00 27.90 ? 177  ASN   D C   1 
ATOM   7714  O  O   . ASN   D  1 177 ? 71.608 -34.110 52.717  1.00 30.18 ? 177  ASN   D O   1 
ATOM   7715  C  CB  . ASN   D  1 177 ? 70.430 -31.640 52.147  1.00 30.34 ? 177  ASN   D CB  1 
ATOM   7716  C  CG  . ASN   D  1 177 ? 69.750 -30.404 51.526  1.00 31.88 ? 177  ASN   D CG  1 
ATOM   7717  O  OD1 . ASN   D  1 177 ? 69.326 -29.430 52.213  1.00 33.64 ? 177  ASN   D OD1 1 
ATOM   7718  N  ND2 . ASN   D  1 177 ? 69.661 -30.433 50.210  1.00 29.80 ? 177  ASN   D ND2 1 
ATOM   7719  N  N   . PHE   D  1 178 ? 69.687 -35.245 52.667  1.00 25.54 ? 178  PHE   D N   1 
ATOM   7720  C  CA  . PHE   D  1 178 ? 70.283 -36.442 53.256  1.00 22.71 ? 178  PHE   D CA  1 
ATOM   7721  C  C   . PHE   D  1 178 ? 70.814 -37.352 52.155  1.00 25.98 ? 178  PHE   D C   1 
ATOM   7722  O  O   . PHE   D  1 178 ? 70.099 -37.681 51.205  1.00 26.92 ? 178  PHE   D O   1 
ATOM   7723  C  CB  . PHE   D  1 178 ? 69.289 -37.228 54.110  1.00 24.23 ? 178  PHE   D CB  1 
ATOM   7724  C  CG  . PHE   D  1 178 ? 69.924 -38.416 54.761  1.00 23.23 ? 178  PHE   D CG  1 
ATOM   7725  C  CD1 . PHE   D  1 178 ? 70.835 -38.244 55.794  1.00 26.75 ? 178  PHE   D CD1 1 
ATOM   7726  C  CD2 . PHE   D  1 178 ? 69.700 -39.665 54.273  1.00 19.78 ? 178  PHE   D CD2 1 
ATOM   7727  C  CE1 . PHE   D  1 178 ? 71.475 -39.378 56.368  1.00 25.80 ? 178  PHE   D CE1 1 
ATOM   7728  C  CE2 . PHE   D  1 178 ? 70.294 -40.773 54.846  1.00 22.58 ? 178  PHE   D CE2 1 
ATOM   7729  C  CZ  . PHE   D  1 178 ? 71.191 -40.630 55.885  1.00 22.93 ? 178  PHE   D CZ  1 
ATOM   7730  N  N   . ASP   D  1 179 ? 72.060 -37.794 52.321  1.00 26.62 ? 179  ASP   D N   1 
ATOM   7731  C  CA  . ASP   D  1 179 ? 72.730 -38.657 51.360  1.00 24.90 ? 179  ASP   D CA  1 
ATOM   7732  C  C   . ASP   D  1 179 ? 72.623 -40.119 51.781  1.00 25.23 ? 179  ASP   D C   1 
ATOM   7733  O  O   . ASP   D  1 179 ? 73.364 -40.558 52.676  1.00 25.28 ? 179  ASP   D O   1 
ATOM   7734  C  CB  . ASP   D  1 179 ? 74.202 -38.231 51.298  1.00 24.94 ? 179  ASP   D CB  1 
ATOM   7735  C  CG  . ASP   D  1 179 ? 75.006 -39.063 50.333  1.00 29.70 ? 179  ASP   D CG  1 
ATOM   7736  O  OD1 . ASP   D  1 179 ? 74.395 -39.917 49.644  1.00 26.84 ? 179  ASP   D OD1 1 
ATOM   7737  O  OD2 . ASP   D  1 179 ? 76.246 -38.840 50.285  1.00 34.50 ? 179  ASP   D OD2 1 
ATOM   7738  N  N   . PRO   D  1 180 ? 71.755 -40.935 51.175  1.00 23.34 ? 180  PRO   D N   1 
ATOM   7739  C  CA  . PRO   D  1 180 ? 71.668 -42.332 51.636  1.00 24.01 ? 180  PRO   D CA  1 
ATOM   7740  C  C   . PRO   D  1 180 ? 72.902 -43.143 51.296  1.00 24.93 ? 180  PRO   D C   1 
ATOM   7741  O  O   . PRO   D  1 180 ? 73.059 -44.246 51.829  1.00 23.54 ? 180  PRO   D O   1 
ATOM   7742  C  CB  . PRO   D  1 180 ? 70.410 -42.875 50.929  1.00 22.38 ? 180  PRO   D CB  1 
ATOM   7743  C  CG  . PRO   D  1 180 ? 70.330 -42.007 49.654  1.00 24.72 ? 180  PRO   D CG  1 
ATOM   7744  C  CD  . PRO   D  1 180 ? 70.822 -40.626 50.075  1.00 23.47 ? 180  PRO   D CD  1 
ATOM   7745  N  N   . ARG   D  1 181 ? 73.802 -42.639 50.451  1.00 25.42 ? 181  ARG   D N   1 
ATOM   7746  C  CA  . ARG   D  1 181 ? 75.023 -43.411 50.223  1.00 26.11 ? 181  ARG   D CA  1 
ATOM   7747  C  C   . ARG   D  1 181 ? 75.836 -43.572 51.496  1.00 24.11 ? 181  ARG   D C   1 
ATOM   7748  O  O   . ARG   D  1 181 ? 76.677 -44.489 51.584  1.00 25.94 ? 181  ARG   D O   1 
ATOM   7749  C  CB  . ARG   D  1 181 ? 75.848 -42.736 49.145  1.00 28.04 ? 181  ARG   D CB  1 
ATOM   7750  C  CG  . ARG   D  1 181 ? 75.183 -42.680 47.802  1.00 29.11 ? 181  ARG   D CG  1 
ATOM   7751  C  CD  . ARG   D  1 181 ? 75.972 -41.790 46.874  1.00 30.59 ? 181  ARG   D CD  1 
ATOM   7752  N  NE  . ARG   D  1 181 ? 76.102 -40.463 47.458  1.00 33.96 ? 181  ARG   D NE  1 
ATOM   7753  C  CZ  . ARG   D  1 181 ? 76.913 -39.544 46.968  1.00 37.70 ? 181  ARG   D CZ  1 
ATOM   7754  N  NH1 . ARG   D  1 181 ? 77.635 -39.851 45.894  1.00 42.00 ? 181  ARG   D NH1 1 
ATOM   7755  N  NH2 . ARG   D  1 181 ? 77.001 -38.343 47.535  1.00 37.67 ? 181  ARG   D NH2 1 
ATOM   7756  N  N   . GLY   D  1 182 ? 75.669 -42.663 52.452  1.00 26.72 ? 182  GLY   D N   1 
ATOM   7757  C  CA  . GLY   D  1 182 ? 76.411 -42.787 53.698  1.00 25.87 ? 182  GLY   D CA  1 
ATOM   7758  C  C   . GLY   D  1 182 ? 75.965 -43.921 54.583  1.00 27.47 ? 182  GLY   D C   1 
ATOM   7759  O  O   . GLY   D  1 182 ? 76.612 -44.173 55.613  1.00 27.26 ? 182  GLY   D O   1 
ATOM   7760  N  N   . LEU   D  1 183 ? 74.878 -44.605 54.205  1.00 25.44 ? 183  LEU   D N   1 
ATOM   7761  C  CA  . LEU   D  1 183 ? 74.381 -45.773 54.923  1.00 22.49 ? 183  LEU   D CA  1 
ATOM   7762  C  C   . LEU   D  1 183 ? 74.749 -47.072 54.217  1.00 24.19 ? 183  LEU   D C   1 
ATOM   7763  O  O   . LEU   D  1 183 ? 74.299 -48.140 54.637  1.00 24.21 ? 183  LEU   D O   1 
ATOM   7764  C  CB  . LEU   D  1 183 ? 72.859 -45.679 55.100  1.00 21.86 ? 183  LEU   D CB  1 
ATOM   7765  C  CG  . LEU   D  1 183 ? 72.406 -44.443 55.895  1.00 22.74 ? 183  LEU   D CG  1 
ATOM   7766  C  CD1 . LEU   D  1 183 ? 70.882 -44.442 55.939  1.00 22.39 ? 183  LEU   D CD1 1 
ATOM   7767  C  CD2 . LEU   D  1 183 ? 73.010 -44.468 57.291  1.00 25.60 ? 183  LEU   D CD2 1 
ATOM   7768  N  N   . LEU   D  1 184 ? 75.595 -47.007 53.180  1.00 24.85 ? 184  LEU   D N   1 
ATOM   7769  C  CA  . LEU   D  1 184 ? 76.000 -48.210 52.438  1.00 24.95 ? 184  LEU   D CA  1 
ATOM   7770  C  C   . LEU   D  1 184 ? 77.371 -48.700 52.885  1.00 24.51 ? 184  LEU   D C   1 
ATOM   7771  O  O   . LEU   D  1 184 ? 78.276 -47.893 53.136  1.00 25.96 ? 184  LEU   D O   1 
ATOM   7772  C  CB  . LEU   D  1 184 ? 76.060 -47.939 50.932  1.00 25.90 ? 184  LEU   D CB  1 
ATOM   7773  C  CG  . LEU   D  1 184 ? 74.760 -47.402 50.305  1.00 29.96 ? 184  LEU   D CG  1 
ATOM   7774  C  CD1 . LEU   D  1 184 ? 75.040 -47.083 48.835  1.00 30.74 ? 184  LEU   D CD1 1 
ATOM   7775  C  CD2 . LEU   D  1 184 ? 73.681 -48.445 50.457  1.00 26.75 ? 184  LEU   D CD2 1 
ATOM   7776  N  N   . PRO   D  1 185 ? 77.608 -50.000 52.931  1.00 25.24 ? 185  PRO   D N   1 
ATOM   7777  C  CA  . PRO   D  1 185 ? 78.965 -50.501 53.162  1.00 26.74 ? 185  PRO   D CA  1 
ATOM   7778  C  C   . PRO   D  1 185 ? 79.811 -50.402 51.898  1.00 26.82 ? 185  PRO   D C   1 
ATOM   7779  O  O   . PRO   D  1 185 ? 79.315 -50.103 50.811  1.00 28.98 ? 185  PRO   D O   1 
ATOM   7780  C  CB  . PRO   D  1 185 ? 78.739 -51.974 53.541  1.00 25.23 ? 185  PRO   D CB  1 
ATOM   7781  C  CG  . PRO   D  1 185 ? 77.500 -52.366 52.737  1.00 25.32 ? 185  PRO   D CG  1 
ATOM   7782  C  CD  . PRO   D  1 185 ? 76.614 -51.079 52.702  1.00 24.70 ? 185  PRO   D CD  1 
ATOM   7783  N  N   . GLU   D  1 186 ? 81.114 -50.686 52.047  1.00 27.12 ? 186  GLU   D N   1 
ATOM   7784  C  CA  . GLU   D  1 186 ? 81.991 -50.594 50.891  1.00 31.88 ? 186  GLU   D CA  1 
ATOM   7785  C  C   . GLU   D  1 186 ? 81.703 -51.691 49.860  1.00 33.95 ? 186  GLU   D C   1 
ATOM   7786  O  O   . GLU   D  1 186 ? 81.720 -51.424 48.651  1.00 34.62 ? 186  GLU   D O   1 
ATOM   7787  C  CB  . GLU   D  1 186 ? 83.446 -50.626 51.363  1.00 39.53 ? 186  GLU   D CB  1 
ATOM   7788  C  CG  . GLU   D  1 186 ? 84.501 -50.559 50.276  1.00 52.02 ? 186  GLU   D CG  1 
ATOM   7789  C  CD  . GLU   D  1 186 ? 85.919 -50.299 50.832  1.00 61.86 ? 186  GLU   D CD  1 
ATOM   7790  O  OE1 . GLU   D  1 186 ? 86.814 -49.932 50.035  1.00 65.63 ? 186  GLU   D OE1 1 
ATOM   7791  O  OE2 . GLU   D  1 186 ? 86.143 -50.467 52.059  1.00 64.82 ? 186  GLU   D OE2 1 
ATOM   7792  N  N   . SER   D  1 187 ? 81.448 -52.932 50.304  1.00 29.09 ? 187  SER   D N   1 
ATOM   7793  C  CA  . SER   D  1 187 ? 81.177 -54.036 49.392  1.00 28.16 ? 187  SER   D CA  1 
ATOM   7794  C  C   . SER   D  1 187 ? 79.683 -54.153 49.132  1.00 28.15 ? 187  SER   D C   1 
ATOM   7795  O  O   . SER   D  1 187 ? 78.879 -54.054 50.057  1.00 26.65 ? 187  SER   D O   1 
ATOM   7796  C  CB  . SER   D  1 187 ? 81.657 -55.359 49.971  1.00 28.84 ? 187  SER   D CB  1 
ATOM   7797  O  OG  . SER   D  1 187 ? 81.293 -56.406 49.066  1.00 32.65 ? 187  SER   D OG  1 
ATOM   7798  N  N   . LEU   D  1 188 ? 79.319 -54.401 47.875  1.00 29.16 ? 188  LEU   D N   1 
ATOM   7799  C  CA  . LEU   D  1 188 ? 77.918 -54.627 47.545  1.00 27.74 ? 188  LEU   D CA  1 
ATOM   7800  C  C   . LEU   D  1 188 ? 77.630 -56.096 47.249  1.00 27.38 ? 188  LEU   D C   1 
ATOM   7801  O  O   . LEU   D  1 188 ? 76.586 -56.411 46.671  1.00 30.09 ? 188  LEU   D O   1 
ATOM   7802  C  CB  . LEU   D  1 188 ? 77.472 -53.740 46.377  1.00 31.61 ? 188  LEU   D CB  1 
ATOM   7803  C  CG  . LEU   D  1 188 ? 77.585 -52.237 46.560  1.00 33.20 ? 188  LEU   D CG  1 
ATOM   7804  C  CD1 . LEU   D  1 188 ? 77.044 -51.543 45.322  1.00 35.00 ? 188  LEU   D CD1 1 
ATOM   7805  C  CD2 . LEU   D  1 188 ? 76.806 -51.778 47.792  1.00 30.66 ? 188  LEU   D CD2 1 
ATOM   7806  N  N   . ASP   D  1 189 ? 78.501 -56.995 47.698  1.00 25.32 ? 189  ASP   D N   1 
ATOM   7807  C  CA  . ASP   D  1 189 ? 78.191 -58.423 47.699  1.00 25.49 ? 189  ASP   D CA  1 
ATOM   7808  C  C   . ASP   D  1 189 ? 76.861 -58.653 48.409  1.00 23.86 ? 189  ASP   D C   1 
ATOM   7809  O  O   . ASP   D  1 189 ? 76.571 -58.029 49.442  1.00 24.18 ? 189  ASP   D O   1 
ATOM   7810  C  CB  . ASP   D  1 189 ? 79.294 -59.199 48.425  1.00 26.00 ? 189  ASP   D CB  1 
ATOM   7811  C  CG  . ASP   D  1 189 ? 80.586 -59.319 47.603  1.00 31.75 ? 189  ASP   D CG  1 
ATOM   7812  O  OD1 . ASP   D  1 189 ? 80.622 -58.843 46.453  1.00 35.00 ? 189  ASP   D OD1 1 
ATOM   7813  O  OD2 . ASP   D  1 189 ? 81.573 -59.876 48.118  1.00 34.45 ? 189  ASP   D OD2 1 
ATOM   7814  N  N   . TYR   D  1 190 ? 76.036 -59.562 47.873  1.00 22.23 ? 190  TYR   D N   1 
ATOM   7815  C  CA  . TYR   D  1 190 ? 74.686 -59.684 48.426  1.00 20.31 ? 190  TYR   D CA  1 
ATOM   7816  C  C   . TYR   D  1 190 ? 74.141 -61.093 48.229  1.00 21.52 ? 190  TYR   D C   1 
ATOM   7817  O  O   . TYR   D  1 190 ? 74.652 -61.877 47.409  1.00 23.03 ? 190  TYR   D O   1 
ATOM   7818  C  CB  . TYR   D  1 190 ? 73.697 -58.667 47.794  1.00 19.84 ? 190  TYR   D CB  1 
ATOM   7819  C  CG  . TYR   D  1 190 ? 73.467 -58.889 46.309  1.00 20.90 ? 190  TYR   D CG  1 
ATOM   7820  C  CD1 . TYR   D  1 190 ? 72.494 -59.807 45.863  1.00 23.29 ? 190  TYR   D CD1 1 
ATOM   7821  C  CD2 . TYR   D  1 190 ? 74.202 -58.190 45.350  1.00 22.13 ? 190  TYR   D CD2 1 
ATOM   7822  C  CE1 . TYR   D  1 190 ? 72.288 -60.016 44.470  1.00 23.96 ? 190  TYR   D CE1 1 
ATOM   7823  C  CE2 . TYR   D  1 190 ? 74.009 -58.415 43.944  1.00 23.30 ? 190  TYR   D CE2 1 
ATOM   7824  C  CZ  . TYR   D  1 190 ? 73.038 -59.312 43.520  1.00 22.33 ? 190  TYR   D CZ  1 
ATOM   7825  O  OH  . TYR   D  1 190 ? 72.896 -59.562 42.142  1.00 26.38 ? 190  TYR   D OH  1 
ATOM   7826  N  N   . TRP   D  1 191 ? 73.091 -61.387 49.007  1.00 21.18 ? 191  TRP   D N   1 
ATOM   7827  C  CA  . TRP   D  1 191 ? 72.206 -62.532 48.819  1.00 20.39 ? 191  TRP   D CA  1 
ATOM   7828  C  C   . TRP   D  1 191 ? 70.873 -62.024 48.298  1.00 21.09 ? 191  TRP   D C   1 
ATOM   7829  O  O   . TRP   D  1 191 ? 70.450 -60.909 48.646  1.00 20.22 ? 191  TRP   D O   1 
ATOM   7830  C  CB  . TRP   D  1 191 ? 72.002 -63.288 50.122  1.00 21.90 ? 191  TRP   D CB  1 
ATOM   7831  C  CG  . TRP   D  1 191 ? 73.250 -63.848 50.713  1.00 22.12 ? 191  TRP   D CG  1 
ATOM   7832  C  CD1 . TRP   D  1 191 ? 73.931 -64.962 50.305  1.00 24.57 ? 191  TRP   D CD1 1 
ATOM   7833  C  CD2 . TRP   D  1 191 ? 73.919 -63.387 51.900  1.00 22.85 ? 191  TRP   D CD2 1 
ATOM   7834  N  NE1 . TRP   D  1 191 ? 74.996 -65.209 51.142  1.00 26.56 ? 191  TRP   D NE1 1 
ATOM   7835  C  CE2 . TRP   D  1 191 ? 75.016 -64.261 52.130  1.00 24.00 ? 191  TRP   D CE2 1 
ATOM   7836  C  CE3 . TRP   D  1 191 ? 73.707 -62.316 52.778  1.00 25.03 ? 191  TRP   D CE3 1 
ATOM   7837  C  CZ2 . TRP   D  1 191 ? 75.913 -64.094 53.220  1.00 25.08 ? 191  TRP   D CZ2 1 
ATOM   7838  C  CZ3 . TRP   D  1 191 ? 74.598 -62.147 53.854  1.00 25.21 ? 191  TRP   D CZ3 1 
ATOM   7839  C  CH2 . TRP   D  1 191 ? 75.669 -63.033 54.065  1.00 25.49 ? 191  TRP   D CH2 1 
ATOM   7840  N  N   . THR   D  1 192 ? 70.190 -62.828 47.477  1.00 19.90 ? 192  THR   D N   1 
ATOM   7841  C  CA  . THR   D  1 192 ? 68.896 -62.407 46.960  1.00 19.62 ? 192  THR   D CA  1 
ATOM   7842  C  C   . THR   D  1 192 ? 67.926 -63.570 46.940  1.00 19.44 ? 192  THR   D C   1 
ATOM   7843  O  O   . THR   D  1 192 ? 68.305 -64.730 46.741  1.00 22.25 ? 192  THR   D O   1 
ATOM   7844  C  CB  . THR   D  1 192 ? 69.014 -61.762 45.551  1.00 19.05 ? 192  THR   D CB  1 
ATOM   7845  O  OG1 . THR   D  1 192 ? 67.721 -61.264 45.105  1.00 19.63 ? 192  THR   D OG1 1 
ATOM   7846  C  CG2 . THR   D  1 192 ? 69.566 -62.748 44.554  1.00 21.46 ? 192  THR   D CG2 1 
ATOM   7847  N  N   . TYR   D  1 193 ? 66.663 -63.248 47.168  1.00 18.38 ? 193  TYR   D N   1 
ATOM   7848  C  CA  . TYR   D  1 193 ? 65.614 -64.262 47.119  1.00 18.85 ? 193  TYR   D CA  1 
ATOM   7849  C  C   . TYR   D  1 193 ? 64.266 -63.557 46.946  1.00 19.18 ? 193  TYR   D C   1 
ATOM   7850  O  O   . TYR   D  1 193 ? 64.137 -62.370 47.259  1.00 18.46 ? 193  TYR   D O   1 
ATOM   7851  C  CB  . TYR   D  1 193 ? 65.605 -65.171 48.396  1.00 18.10 ? 193  TYR   D CB  1 
ATOM   7852  C  CG  . TYR   D  1 193 ? 65.046 -64.444 49.611  1.00 16.94 ? 193  TYR   D CG  1 
ATOM   7853  C  CD1 . TYR   D  1 193 ? 65.867 -63.604 50.350  1.00 18.55 ? 193  TYR   D CD1 1 
ATOM   7854  C  CD2 . TYR   D  1 193 ? 63.696 -64.618 50.018  1.00 16.82 ? 193  TYR   D CD2 1 
ATOM   7855  C  CE1 . TYR   D  1 193 ? 65.372 -62.895 51.449  1.00 17.07 ? 193  TYR   D CE1 1 
ATOM   7856  C  CE2 . TYR   D  1 193 ? 63.195 -63.920 51.133  1.00 16.67 ? 193  TYR   D CE2 1 
ATOM   7857  C  CZ  . TYR   D  1 193 ? 64.052 -63.064 51.818  1.00 16.91 ? 193  TYR   D CZ  1 
ATOM   7858  O  OH  . TYR   D  1 193 ? 63.511 -62.341 52.867  1.00 17.55 ? 193  TYR   D OH  1 
ATOM   7859  N  N   . PRO   D  1 194 ? 63.259 -64.251 46.414  1.00 16.60 ? 194  PRO   D N   1 
ATOM   7860  C  CA  . PRO   D  1 194 ? 61.913 -63.666 46.276  1.00 17.24 ? 194  PRO   D CA  1 
ATOM   7861  C  C   . PRO   D  1 194 ? 61.169 -63.764 47.597  1.00 17.15 ? 194  PRO   D C   1 
ATOM   7862  O  O   . PRO   D  1 194 ? 61.057 -64.854 48.171  1.00 16.97 ? 194  PRO   D O   1 
ATOM   7863  C  CB  . PRO   D  1 194 ? 61.245 -64.573 45.229  1.00 18.38 ? 194  PRO   D CB  1 
ATOM   7864  C  CG  . PRO   D  1 194 ? 62.019 -65.901 45.348  1.00 21.02 ? 194  PRO   D CG  1 
ATOM   7865  C  CD  . PRO   D  1 194 ? 63.392 -65.586 45.787  1.00 18.39 ? 194  PRO   D CD  1 
ATOM   7866  N  N   . GLY   D  1 195 ? 60.644 -62.652 48.070  1.00 15.46 ? 195  GLY   D N   1 
ATOM   7867  C  CA  . GLY   D  1 195 ? 59.930 -62.632 49.347  1.00 15.07 ? 195  GLY   D CA  1 
ATOM   7868  C  C   . GLY   D  1 195 ? 58.836 -61.605 49.399  1.00 14.85 ? 195  GLY   D C   1 
ATOM   7869  O  O   . GLY   D  1 195 ? 58.135 -61.352 48.402  1.00 15.83 ? 195  GLY   D O   1 
ATOM   7870  N  N   . SER   D  1 196 ? 58.660 -61.024 50.585  1.00 14.84 ? 196  SER   D N   1 
ATOM   7871  C  CA  . SER   D  1 196 ? 57.456 -60.257 50.882  1.00 15.54 ? 196  SER   D CA  1 
ATOM   7872  C  C   . SER   D  1 196 ? 57.808 -59.001 51.651  1.00 15.60 ? 196  SER   D C   1 
ATOM   7873  O  O   . SER   D  1 196 ? 58.921 -58.838 52.160  1.00 15.29 ? 196  SER   D O   1 
ATOM   7874  C  CB  . SER   D  1 196 ? 56.454 -61.096 51.739  1.00 15.90 ? 196  SER   D CB  1 
ATOM   7875  O  OG  . SER   D  1 196 ? 56.929 -61.198 53.096  1.00 15.58 ? 196  SER   D OG  1 
ATOM   7876  N  N   . LEU   D  1 197 ? 56.805 -58.107 51.766  1.00 14.97 ? 197  LEU   D N   1 
ATOM   7877  C  CA  . LEU   D  1 197 ? 56.894 -57.109 52.831  1.00 14.33 ? 197  LEU   D CA  1 
ATOM   7878  C  C   . LEU   D  1 197 ? 57.043 -57.809 54.191  1.00 15.14 ? 197  LEU   D C   1 
ATOM   7879  O  O   . LEU   D  1 197 ? 56.420 -58.854 54.430  1.00 14.31 ? 197  LEU   D O   1 
ATOM   7880  C  CB  . LEU   D  1 197 ? 55.613 -56.266 52.861  1.00 14.85 ? 197  LEU   D CB  1 
ATOM   7881  C  CG  . LEU   D  1 197 ? 55.279 -55.509 51.569  1.00 14.27 ? 197  LEU   D CG  1 
ATOM   7882  C  CD1 . LEU   D  1 197 ? 53.905 -54.820 51.859  1.00 15.53 ? 197  LEU   D CD1 1 
ATOM   7883  C  CD2 . LEU   D  1 197 ? 56.387 -54.444 51.242  1.00 15.34 ? 197  LEU   D CD2 1 
ATOM   7884  N  N   . THR   D  1 198 ? 57.834 -57.211 55.090  1.00 14.65 ? 198  THR   D N   1 
ATOM   7885  C  CA  . THR   D  1 198 ? 57.950 -57.826 56.422  1.00 14.52 ? 198  THR   D CA  1 
ATOM   7886  C  C   . THR   D  1 198 ? 56.975 -57.236 57.439  1.00 13.32 ? 198  THR   D C   1 
ATOM   7887  O  O   . THR   D  1 198 ? 57.035 -57.627 58.628  1.00 14.33 ? 198  THR   D O   1 
ATOM   7888  C  CB  . THR   D  1 198 ? 59.370 -57.732 56.992  1.00 14.87 ? 198  THR   D CB  1 
ATOM   7889  O  OG1 . THR   D  1 198 ? 59.639 -56.333 57.250  1.00 14.50 ? 198  THR   D OG1 1 
ATOM   7890  C  CG2 . THR   D  1 198 ? 60.438 -58.294 56.025  1.00 14.81 ? 198  THR   D CG2 1 
ATOM   7891  N  N   . THR   D  1 199 ? 56.040 -56.414 56.982  1.00 14.11 ? 199  THR   D N   1 
ATOM   7892  C  CA  . THR   D  1 199 ? 54.955 -55.921 57.817  1.00 13.32 ? 199  THR   D CA  1 
ATOM   7893  C  C   . THR   D  1 199 ? 53.672 -56.199 57.053  1.00 12.72 ? 199  THR   D C   1 
ATOM   7894  O  O   . THR   D  1 199 ? 53.699 -56.367 55.826  1.00 14.95 ? 199  THR   D O   1 
ATOM   7895  C  CB  . THR   D  1 199 ? 55.009 -54.399 58.093  1.00 14.00 ? 199  THR   D CB  1 
ATOM   7896  O  OG1 . THR   D  1 199 ? 54.828 -53.670 56.861  1.00 15.00 ? 199  THR   D OG1 1 
ATOM   7897  C  CG2 . THR   D  1 199 ? 56.348 -54.007 58.704  1.00 15.80 ? 199  THR   D CG2 1 
ATOM   7898  N  N   . PRO   D  1 200 ? 52.533 -56.235 57.745  1.00 14.83 ? 200  PRO   D N   1 
ATOM   7899  C  CA  . PRO   D  1 200 ? 51.258 -56.173 57.049  1.00 13.16 ? 200  PRO   D CA  1 
ATOM   7900  C  C   . PRO   D  1 200 ? 51.297 -55.086 55.990  1.00 13.44 ? 200  PRO   D C   1 
ATOM   7901  O  O   . PRO   D  1 200 ? 51.825 -53.982 56.234  1.00 14.13 ? 200  PRO   D O   1 
ATOM   7902  C  CB  . PRO   D  1 200 ? 50.224 -55.875 58.180  1.00 13.49 ? 200  PRO   D CB  1 
ATOM   7903  C  CG  . PRO   D  1 200 ? 50.878 -56.630 59.395  1.00 14.52 ? 200  PRO   D CG  1 
ATOM   7904  C  CD  . PRO   D  1 200 ? 52.373 -56.191 59.221  1.00 14.32 ? 200  PRO   D CD  1 
ATOM   7905  N  N   . PRO   D  1 201 ? 50.713 -55.327 54.808  1.00 14.14 ? 201  PRO   D N   1 
ATOM   7906  C  CA  . PRO   D  1 201 ? 49.895 -56.514 54.472  1.00 14.39 ? 201  PRO   D CA  1 
ATOM   7907  C  C   . PRO   D  1 201 ? 50.669 -57.742 54.017  1.00 13.80 ? 201  PRO   D C   1 
ATOM   7908  O  O   . PRO   D  1 201 ? 50.041 -58.692 53.543  1.00 14.51 ? 201  PRO   D O   1 
ATOM   7909  C  CB  . PRO   D  1 201 ? 48.981 -56.004 53.346  1.00 14.02 ? 201  PRO   D CB  1 
ATOM   7910  C  CG  . PRO   D  1 201 ? 49.883 -54.994 52.595  1.00 13.99 ? 201  PRO   D CG  1 
ATOM   7911  C  CD  . PRO   D  1 201 ? 50.629 -54.296 53.746  1.00 15.94 ? 201  PRO   D CD  1 
ATOM   7912  N  N   . LEU   D  1 202 ? 52.012 -57.764 54.168  1.00 13.27 ? 202  LEU   D N   1 
ATOM   7913  C  CA  . LEU   D  1 202 ? 52.830 -59.007 53.965  1.00 12.82 ? 202  LEU   D CA  1 
ATOM   7914  C  C   . LEU   D  1 202 ? 52.749 -59.497 52.516  1.00 14.31 ? 202  LEU   D C   1 
ATOM   7915  O  O   . LEU   D  1 202 ? 52.955 -60.695 52.245  1.00 14.34 ? 202  LEU   D O   1 
ATOM   7916  C  CB  . LEU   D  1 202 ? 52.435 -60.116 54.971  1.00 14.65 ? 202  LEU   D CB  1 
ATOM   7917  C  CG  . LEU   D  1 202 ? 52.630 -59.693 56.430  1.00 14.68 ? 202  LEU   D CG  1 
ATOM   7918  C  CD1 . LEU   D  1 202 ? 51.988 -60.686 57.383  1.00 14.40 ? 202  LEU   D CD1 1 
ATOM   7919  C  CD2 . LEU   D  1 202 ? 54.124 -59.549 56.782  1.00 13.98 ? 202  LEU   D CD2 1 
ATOM   7920  N  N   . LEU   D  1 203 ? 52.465 -58.589 51.583  1.00 14.14 ? 203  LEU   D N   1 
ATOM   7921  C  CA  . LEU   D  1 203 ? 52.328 -59.004 50.165  1.00 13.59 ? 203  LEU   D CA  1 
ATOM   7922  C  C   . LEU   D  1 203 ? 53.635 -59.542 49.593  1.00 13.75 ? 203  LEU   D C   1 
ATOM   7923  O  O   . LEU   D  1 203 ? 54.721 -59.025 49.879  1.00 14.08 ? 203  LEU   D O   1 
ATOM   7924  C  CB  . LEU   D  1 203 ? 51.841 -57.817 49.316  1.00 13.55 ? 203  LEU   D CB  1 
ATOM   7925  C  CG  . LEU   D  1 203 ? 50.428 -57.381 49.762  1.00 15.70 ? 203  LEU   D CG  1 
ATOM   7926  C  CD1 . LEU   D  1 203 ? 50.089 -56.054 49.009  1.00 17.83 ? 203  LEU   D CD1 1 
ATOM   7927  C  CD2 . LEU   D  1 203 ? 49.362 -58.490 49.431  1.00 17.40 ? 203  LEU   D CD2 1 
ATOM   7928  N  N   . GLU   D  1 204 ? 53.524 -60.543 48.710  1.00 14.73 ? 204  GLU   D N   1 
ATOM   7929  C  CA  . GLU   D  1 204 ? 54.699 -61.279 48.200  1.00 15.54 ? 204  GLU   D CA  1 
ATOM   7930  C  C   . GLU   D  1 204 ? 55.151 -60.622 46.894  1.00 16.18 ? 204  GLU   D C   1 
ATOM   7931  O  O   . GLU   D  1 204 ? 55.155 -61.208 45.790  1.00 17.72 ? 204  GLU   D O   1 
ATOM   7932  C  CB  . GLU   D  1 204 ? 54.344 -62.754 48.067  1.00 15.84 ? 204  GLU   D CB  1 
ATOM   7933  C  CG  . GLU   D  1 204 ? 54.064 -63.316 49.489  1.00 14.65 ? 204  GLU   D CG  1 
ATOM   7934  C  CD  . GLU   D  1 204 ? 53.695 -64.799 49.489  1.00 15.16 ? 204  GLU   D CD  1 
ATOM   7935  O  OE1 . GLU   D  1 204 ? 53.141 -65.286 48.462  1.00 17.87 ? 204  GLU   D OE1 1 
ATOM   7936  O  OE2 . GLU   D  1 204 ? 53.912 -65.429 50.548  1.00 16.12 ? 204  GLU   D OE2 1 
ATOM   7937  N  N   . SER   D  1 205 ? 55.600 -59.373 47.069  1.00 16.00 ? 205  SER   D N   1 
ATOM   7938  C  CA  A SER   D  1 205 ? 55.918 -58.501 45.939  0.62 16.23 ? 205  SER   D CA  1 
ATOM   7939  C  CA  B SER   D  1 205 ? 55.911 -58.482 45.958  0.38 16.17 ? 205  SER   D CA  1 
ATOM   7940  C  C   . SER   D  1 205 ? 57.348 -57.984 45.977  1.00 16.22 ? 205  SER   D C   1 
ATOM   7941  O  O   . SER   D  1 205 ? 57.689 -57.061 45.211  1.00 17.90 ? 205  SER   D O   1 
ATOM   7942  C  CB  A SER   D  1 205 ? 54.945 -57.331 45.890  0.62 17.07 ? 205  SER   D CB  1 
ATOM   7943  C  CB  B SER   D  1 205 ? 54.940 -57.302 45.970  0.38 16.84 ? 205  SER   D CB  1 
ATOM   7944  O  OG  A SER   D  1 205 ? 54.965 -56.702 47.138  0.62 17.55 ? 205  SER   D OG  1 
ATOM   7945  O  OG  B SER   D  1 205 ? 53.624 -57.793 46.160  0.38 16.77 ? 205  SER   D OG  1 
ATOM   7946  N  N   . VAL   D  1 206 ? 58.223 -58.575 46.795  1.00 16.67 ? 206  VAL   D N   1 
ATOM   7947  C  CA  . VAL   D  1 206 ? 59.539 -57.990 47.049  1.00 16.84 ? 206  VAL   D CA  1 
ATOM   7948  C  C   . VAL   D  1 206 ? 60.624 -58.913 46.533  1.00 17.73 ? 206  VAL   D C   1 
ATOM   7949  O  O   . VAL   D  1 206 ? 60.671 -60.101 46.881  1.00 18.20 ? 206  VAL   D O   1 
ATOM   7950  C  CB  . VAL   D  1 206 ? 59.766 -57.728 48.551  1.00 15.14 ? 206  VAL   D CB  1 
ATOM   7951  C  CG1 . VAL   D  1 206 ? 61.213 -57.146 48.728  1.00 16.51 ? 206  VAL   D CG1 1 
ATOM   7952  C  CG2 . VAL   D  1 206 ? 58.749 -56.736 49.128  1.00 15.82 ? 206  VAL   D CG2 1 
ATOM   7953  N  N   . THR   D  1 207 ? 61.526 -58.373 45.724  1.00 16.37 ? 207  THR   D N   1 
ATOM   7954  C  CA  . THR   D  1 207 ? 62.820 -59.027 45.476  1.00 18.67 ? 207  THR   D CA  1 
ATOM   7955  C  C   . THR   D  1 207 ? 63.782 -58.481 46.516  1.00 18.58 ? 207  THR   D C   1 
ATOM   7956  O  O   . THR   D  1 207 ? 64.045 -57.277 46.528  1.00 18.18 ? 207  THR   D O   1 
ATOM   7957  C  CB  . THR   D  1 207 ? 63.336 -58.711 44.063  1.00 18.29 ? 207  THR   D CB  1 
ATOM   7958  O  OG1 . THR   D  1 207 ? 62.435 -59.254 43.077  1.00 19.58 ? 207  THR   D OG1 1 
ATOM   7959  C  CG2 . THR   D  1 207 ? 64.712 -59.356 43.851  1.00 20.11 ? 207  THR   D CG2 1 
ATOM   7960  N  N   . TRP   D  1 208 ? 64.221 -59.348 47.444  1.00 17.37 ? 208  TRP   D N   1 
ATOM   7961  C  CA  . TRP   D  1 208 ? 65.151 -58.960 48.505  1.00 17.55 ? 208  TRP   D CA  1 
ATOM   7962  C  C   . TRP   D  1 208 ? 66.585 -59.038 48.026  1.00 19.27 ? 208  TRP   D C   1 
ATOM   7963  O  O   . TRP   D  1 208 ? 66.993 -60.049 47.426  1.00 19.03 ? 208  TRP   D O   1 
ATOM   7964  C  CB  . TRP   D  1 208 ? 64.984 -59.878 49.735  1.00 17.94 ? 208  TRP   D CB  1 
ATOM   7965  C  CG  . TRP   D  1 208 ? 63.794 -59.409 50.530  1.00 16.36 ? 208  TRP   D CG  1 
ATOM   7966  C  CD1 . TRP   D  1 208 ? 62.480 -59.875 50.476  1.00 15.87 ? 208  TRP   D CD1 1 
ATOM   7967  C  CD2 . TRP   D  1 208 ? 63.797 -58.336 51.473  1.00 15.40 ? 208  TRP   D CD2 1 
ATOM   7968  N  NE1 . TRP   D  1 208 ? 61.682 -59.094 51.318  1.00 16.46 ? 208  TRP   D NE1 1 
ATOM   7969  C  CE2 . TRP   D  1 208 ? 62.478 -58.161 51.930  1.00 15.51 ? 208  TRP   D CE2 1 
ATOM   7970  C  CE3 . TRP   D  1 208 ? 64.820 -57.506 51.979  1.00 17.45 ? 208  TRP   D CE3 1 
ATOM   7971  C  CZ2 . TRP   D  1 208 ? 62.131 -57.190 52.895  1.00 15.63 ? 208  TRP   D CZ2 1 
ATOM   7972  C  CZ3 . TRP   D  1 208 ? 64.472 -56.506 52.938  1.00 17.34 ? 208  TRP   D CZ3 1 
ATOM   7973  C  CH2 . TRP   D  1 208 ? 63.134 -56.341 53.349  1.00 16.98 ? 208  TRP   D CH2 1 
ATOM   7974  N  N   . ILE   D  1 209 ? 67.345 -57.990 48.347  1.00 18.19 ? 209  ILE   D N   1 
ATOM   7975  C  CA  . ILE   D  1 209 ? 68.771 -57.915 48.091  1.00 18.22 ? 209  ILE   D CA  1 
ATOM   7976  C  C   . ILE   D  1 209 ? 69.386 -57.549 49.429  1.00 19.83 ? 209  ILE   D C   1 
ATOM   7977  O  O   . ILE   D  1 209 ? 69.261 -56.394 49.874  1.00 19.24 ? 209  ILE   D O   1 
ATOM   7978  C  CB  . ILE   D  1 209 ? 69.089 -56.863 47.021  1.00 19.95 ? 209  ILE   D CB  1 
ATOM   7979  C  CG1 . ILE   D  1 209 ? 68.416 -57.264 45.699  1.00 22.18 ? 209  ILE   D CG1 1 
ATOM   7980  C  CG2 . ILE   D  1 209 ? 70.587 -56.758 46.817  1.00 19.93 ? 209  ILE   D CG2 1 
ATOM   7981  C  CD1 . ILE   D  1 209 ? 68.427 -56.136 44.618  1.00 22.87 ? 209  ILE   D CD1 1 
ATOM   7982  N  N   . VAL   D  1 210 ? 69.995 -58.520 50.107  1.00 18.85 ? 210  VAL   D N   1 
ATOM   7983  C  CA  . VAL   D  1 210 ? 70.527 -58.338 51.464  1.00 19.05 ? 210  VAL   D CA  1 
ATOM   7984  C  C   . VAL   D  1 210 ? 72.051 -58.298 51.383  1.00 20.33 ? 210  VAL   D C   1 
ATOM   7985  O  O   . VAL   D  1 210 ? 72.697 -59.271 50.962  1.00 20.09 ? 210  VAL   D O   1 
ATOM   7986  C  CB  . VAL   D  1 210 ? 70.059 -59.455 52.404  1.00 19.37 ? 210  VAL   D CB  1 
ATOM   7987  C  CG1 . VAL   D  1 210 ? 70.621 -59.232 53.836  1.00 18.77 ? 210  VAL   D CG1 1 
ATOM   7988  C  CG2 . VAL   D  1 210 ? 68.525 -59.472 52.461  1.00 18.36 ? 210  VAL   D CG2 1 
ATOM   7989  N  N   . LEU   D  1 211 ? 72.639 -57.150 51.743  1.00 20.83 ? 211  LEU   D N   1 
ATOM   7990  C  CA  . LEU   D  1 211 ? 74.087 -57.020 51.618  1.00 20.82 ? 211  LEU   D CA  1 
ATOM   7991  C  C   . LEU   D  1 211 ? 74.807 -57.842 52.672  1.00 21.75 ? 211  LEU   D C   1 
ATOM   7992  O  O   . LEU   D  1 211 ? 74.371 -57.946 53.829  1.00 22.38 ? 211  LEU   D O   1 
ATOM   7993  C  CB  . LEU   D  1 211 ? 74.501 -55.580 51.754  1.00 19.78 ? 211  LEU   D CB  1 
ATOM   7994  C  CG  . LEU   D  1 211 ? 73.952 -54.627 50.678  1.00 22.17 ? 211  LEU   D CG  1 
ATOM   7995  C  CD1 . LEU   D  1 211 ? 74.609 -53.242 50.862  1.00 22.61 ? 211  LEU   D CD1 1 
ATOM   7996  C  CD2 . LEU   D  1 211 ? 74.287 -55.172 49.265  1.00 23.55 ? 211  LEU   D CD2 1 
ATOM   7997  N  N   . LYS   D  1 212 ? 75.895 -58.481 52.255  1.00 22.13 ? 212  LYS   D N   1 
ATOM   7998  C  CA  . LYS   D  1 212 ? 76.646 -59.300 53.190  1.00 22.14 ? 212  LYS   D CA  1 
ATOM   7999  C  C   . LYS   D  1 212 ? 77.411 -58.464 54.211  1.00 24.69 ? 212  LYS   D C   1 
ATOM   8000  O  O   . LYS   D  1 212 ? 77.542 -58.863 55.378  1.00 26.44 ? 212  LYS   D O   1 
ATOM   8001  C  CB  . LYS   D  1 212 ? 77.608 -60.195 52.413  1.00 25.63 ? 212  LYS   D CB  1 
ATOM   8002  C  CG  . LYS   D  1 212 ? 78.581 -60.943 53.293  1.00 28.39 ? 212  LYS   D CG  1 
ATOM   8003  C  CD  . LYS   D  1 212 ? 79.285 -62.039 52.523  1.00 36.66 ? 212  LYS   D CD  1 
ATOM   8004  C  CE  . LYS   D  1 212 ? 80.333 -62.728 53.399  1.00 40.79 ? 212  LYS   D CE  1 
ATOM   8005  N  NZ  . LYS   D  1 212 ? 81.093 -63.691 52.584  1.00 43.60 ? 212  LYS   D NZ  1 
ATOM   8006  N  N   . GLU   D  1 213 ? 77.943 -57.313 53.809  1.00 22.77 ? 213  GLU   D N   1 
ATOM   8007  C  CA  . GLU   D  1 213 ? 78.780 -56.544 54.726  1.00 23.05 ? 213  GLU   D CA  1 
ATOM   8008  C  C   . GLU   D  1 213 ? 77.911 -55.633 55.578  1.00 23.28 ? 213  GLU   D C   1 
ATOM   8009  O  O   . GLU   D  1 213 ? 77.167 -54.825 55.022  1.00 23.19 ? 213  GLU   D O   1 
ATOM   8010  C  CB  . GLU   D  1 213 ? 79.814 -55.697 53.971  1.00 24.61 ? 213  GLU   D CB  1 
ATOM   8011  C  CG  . GLU   D  1 213 ? 80.755 -54.895 54.902  1.00 28.30 ? 213  GLU   D CG  1 
ATOM   8012  C  CD  . GLU   D  1 213 ? 81.875 -54.141 54.188  1.00 33.37 ? 213  GLU   D CD  1 
ATOM   8013  O  OE1 . GLU   D  1 213 ? 81.810 -53.899 52.965  1.00 34.19 ? 213  GLU   D OE1 1 
ATOM   8014  O  OE2 . GLU   D  1 213 ? 82.875 -53.826 54.872  1.00 39.12 ? 213  GLU   D OE2 1 
ATOM   8015  N  N   . PRO   D  1 214 ? 77.976 -55.700 56.902  1.00 23.34 ? 214  PRO   D N   1 
ATOM   8016  C  CA  . PRO   D  1 214 ? 77.200 -54.739 57.706  1.00 23.40 ? 214  PRO   D CA  1 
ATOM   8017  C  C   . PRO   D  1 214 ? 77.859 -53.375 57.690  1.00 23.26 ? 214  PRO   D C   1 
ATOM   8018  O  O   . PRO   D  1 214 ? 79.062 -53.230 57.401  1.00 27.03 ? 214  PRO   D O   1 
ATOM   8019  C  CB  . PRO   D  1 214 ? 77.232 -55.324 59.129  1.00 24.93 ? 214  PRO   D CB  1 
ATOM   8020  C  CG  . PRO   D  1 214 ? 77.967 -56.692 58.990  1.00 32.77 ? 214  PRO   D CG  1 
ATOM   8021  C  CD  . PRO   D  1 214 ? 78.803 -56.588 57.754  1.00 26.62 ? 214  PRO   D CD  1 
ATOM   8022  N  N   . ILE   D  1 215 ? 77.039 -52.358 58.049  1.00 23.67 ? 215  ILE   D N   1 
ATOM   8023  C  CA  . ILE   D  1 215 ? 77.559 -51.055 58.440  1.00 23.05 ? 215  ILE   D CA  1 
ATOM   8024  C  C   . ILE   D  1 215 ? 77.685 -51.019 59.956  1.00 24.51 ? 215  ILE   D C   1 
ATOM   8025  O  O   . ILE   D  1 215 ? 76.954 -51.703 60.688  1.00 25.83 ? 215  ILE   D O   1 
ATOM   8026  C  CB  . ILE   D  1 215 ? 76.706 -49.892 57.893  1.00 23.11 ? 215  ILE   D CB  1 
ATOM   8027  C  CG1 . ILE   D  1 215 ? 75.269 -49.954 58.449  1.00 22.09 ? 215  ILE   D CG1 1 
ATOM   8028  C  CG2 . ILE   D  1 215 ? 76.738 -49.906 56.369  1.00 24.87 ? 215  ILE   D CG2 1 
ATOM   8029  C  CD1 . ILE   D  1 215 ? 74.344 -48.747 57.989  1.00 23.63 ? 215  ILE   D CD1 1 
ATOM   8030  N  N   . SER   D  1 216 ? 78.644 -50.239 60.435  1.00 26.27 ? 216  SER   D N   1 
ATOM   8031  C  CA  . SER   D  1 216 ? 78.944 -50.171 61.849  1.00 27.84 ? 216  SER   D CA  1 
ATOM   8032  C  C   . SER   D  1 216 ? 78.324 -48.910 62.421  1.00 32.01 ? 216  SER   D C   1 
ATOM   8033  O  O   . SER   D  1 216 ? 78.595 -47.814 61.908  1.00 35.51 ? 216  SER   D O   1 
ATOM   8034  C  CB  . SER   D  1 216 ? 80.453 -50.163 62.082  1.00 37.73 ? 216  SER   D CB  1 
ATOM   8035  O  OG  . SER   D  1 216 ? 80.726 -49.558 63.323  1.00 43.52 ? 216  SER   D OG  1 
ATOM   8036  N  N   . VAL   D  1 217 ? 77.530 -49.061 63.491  1.00 28.17 ? 217  VAL   D N   1 
ATOM   8037  C  CA  . VAL   D  1 217 ? 76.938 -47.943 64.234  1.00 30.00 ? 217  VAL   D CA  1 
ATOM   8038  C  C   . VAL   D  1 217 ? 77.299 -48.060 65.715  1.00 28.16 ? 217  VAL   D C   1 
ATOM   8039  O  O   . VAL   D  1 217 ? 77.629 -49.140 66.216  1.00 29.58 ? 217  VAL   D O   1 
ATOM   8040  C  CB  . VAL   D  1 217 ? 75.416 -47.903 64.068  1.00 31.02 ? 217  VAL   D CB  1 
ATOM   8041  C  CG1 . VAL   D  1 217 ? 75.079 -47.740 62.592  1.00 31.66 ? 217  VAL   D CG1 1 
ATOM   8042  C  CG2 . VAL   D  1 217 ? 74.800 -49.177 64.695  1.00 26.98 ? 217  VAL   D CG2 1 
ATOM   8043  N  N   . SER   D  1 218 ? 77.214 -46.940 66.442  1.00 28.18 ? 218  SER   D N   1 
ATOM   8044  C  CA  . SER   D  1 218 ? 77.522 -47.038 67.865  1.00 28.07 ? 218  SER   D CA  1 
ATOM   8045  C  C   . SER   D  1 218 ? 76.294 -47.478 68.678  1.00 27.60 ? 218  SER   D C   1 
ATOM   8046  O  O   . SER   D  1 218 ? 75.149 -47.255 68.283  1.00 25.30 ? 218  SER   D O   1 
ATOM   8047  C  CB  . SER   D  1 218 ? 78.052 -45.713 68.402  1.00 30.41 ? 218  SER   D CB  1 
ATOM   8048  O  OG  . SER   D  1 218 ? 77.004 -44.745 68.486  1.00 29.09 ? 218  SER   D OG  1 
ATOM   8049  N  N   . SER   D  1 219 ? 76.554 -48.054 69.870  1.00 30.41 ? 219  SER   D N   1 
ATOM   8050  C  CA  . SER   D  1 219 ? 75.461 -48.367 70.795  1.00 28.84 ? 219  SER   D CA  1 
ATOM   8051  C  C   . SER   D  1 219 ? 74.664 -47.112 71.131  1.00 27.11 ? 219  SER   D C   1 
ATOM   8052  O  O   . SER   D  1 219 ? 73.435 -47.152 71.200  1.00 27.03 ? 219  SER   D O   1 
ATOM   8053  C  CB  . SER   D  1 219 ? 75.982 -48.976 72.089  1.00 34.38 ? 219  SER   D CB  1 
ATOM   8054  O  OG  . SER   D  1 219 ? 76.432 -50.296 71.892  1.00 39.47 ? 219  SER   D OG  1 
ATOM   8055  N  N   . GLU   D  1 220 ? 75.347 -45.984 71.296  1.00 29.08 ? 220  GLU   D N   1 
ATOM   8056  C  CA  . GLU   D  1 220 ? 74.647 -44.745 71.595  1.00 30.96 ? 220  GLU   D CA  1 
ATOM   8057  C  C   . GLU   D  1 220 ? 73.714 -44.345 70.471  1.00 28.46 ? 220  GLU   D C   1 
ATOM   8058  O  O   . GLU   D  1 220 ? 72.599 -43.868 70.732  1.00 28.71 ? 220  GLU   D O   1 
ATOM   8059  C  CB  . GLU   D  1 220 ? 75.641 -43.619 71.861  1.00 37.51 ? 220  GLU   D CB  1 
ATOM   8060  C  CG  . GLU   D  1 220 ? 74.982 -42.275 71.823  1.00 48.94 ? 220  GLU   D CG  1 
ATOM   8061  C  CD  . GLU   D  1 220 ? 75.923 -41.156 72.187  1.00 61.99 ? 220  GLU   D CD  1 
ATOM   8062  O  OE1 . GLU   D  1 220 ? 77.161 -41.397 72.218  1.00 65.52 ? 220  GLU   D OE1 1 
ATOM   8063  O  OE2 . GLU   D  1 220 ? 75.412 -40.036 72.444  1.00 66.66 ? 220  GLU   D OE2 1 
ATOM   8064  N  N   . GLN   D  1 221 ? 74.131 -44.530 69.207  1.00 26.22 ? 221  GLN   D N   1 
ATOM   8065  C  CA  . GLN   D  1 221 ? 73.245 -44.189 68.094  1.00 25.52 ? 221  GLN   D CA  1 
ATOM   8066  C  C   . GLN   D  1 221 ? 71.988 -45.063 68.092  1.00 24.61 ? 221  GLN   D C   1 
ATOM   8067  O  O   . GLN   D  1 221 ? 70.873 -44.553 67.958  1.00 23.73 ? 221  GLN   D O   1 
ATOM   8068  C  CB  . GLN   D  1 221 ? 73.992 -44.289 66.766  1.00 25.65 ? 221  GLN   D CB  1 
ATOM   8069  C  CG  . GLN   D  1 221 ? 74.973 -43.128 66.490  1.00 26.10 ? 221  GLN   D CG  1 
ATOM   8070  C  CD  . GLN   D  1 221 ? 75.752 -43.318 65.200  1.00 27.70 ? 221  GLN   D CD  1 
ATOM   8071  O  OE1 . GLN   D  1 221 ? 76.220 -44.429 64.896  1.00 27.41 ? 221  GLN   D OE1 1 
ATOM   8072  N  NE2 . GLN   D  1 221 ? 75.861 -42.258 64.409  1.00 26.02 ? 221  GLN   D NE2 1 
ATOM   8073  N  N   . VAL   D  1 222 ? 72.137 -46.390 68.262  1.00 23.80 ? 222  VAL   D N   1 
ATOM   8074  C  CA  . VAL   D  1 222 ? 70.959 -47.246 68.286  1.00 23.44 ? 222  VAL   D CA  1 
ATOM   8075  C  C   . VAL   D  1 222 ? 70.059 -46.905 69.466  1.00 24.90 ? 222  VAL   D C   1 
ATOM   8076  O  O   . VAL   D  1 222 ? 68.828 -47.033 69.372  1.00 23.51 ? 222  VAL   D O   1 
ATOM   8077  C  CB  . VAL   D  1 222 ? 71.347 -48.740 68.331  1.00 26.07 ? 222  VAL   D CB  1 
ATOM   8078  C  CG1 . VAL   D  1 222 ? 70.078 -49.607 68.137  1.00 24.08 ? 222  VAL   D CG1 1 
ATOM   8079  C  CG2 . VAL   D  1 222 ? 72.355 -49.058 67.301  1.00 31.55 ? 222  VAL   D CG2 1 
ATOM   8080  N  N   . SER   D  1 223 ? 70.643 -46.521 70.611  1.00 24.12 ? 223  SER   D N   1 
ATOM   8081  C  CA  . SER   D  1 223 ? 69.787 -46.213 71.754  1.00 25.18 ? 223  SER   D CA  1 
ATOM   8082  C  C   . SER   D  1 223 ? 68.858 -45.051 71.429  1.00 25.08 ? 223  SER   D C   1 
ATOM   8083  O  O   . SER   D  1 223 ? 67.756 -44.942 72.004  1.00 25.67 ? 223  SER   D O   1 
ATOM   8084  C  CB  . SER   D  1 223 ? 70.606 -45.892 73.005  1.00 27.77 ? 223  SER   D CB  1 
ATOM   8085  O  OG  . SER   D  1 223 ? 71.160 -44.584 72.924  1.00 32.81 ? 223  SER   D OG  1 
ATOM   8086  N  N   . LYS   D  1 224 ? 69.294 -44.158 70.545  1.00 23.22 ? 224  LYS   D N   1 
ATOM   8087  C  CA  . LYS   D  1 224 ? 68.418 -43.060 70.164  1.00 24.17 ? 224  LYS   D CA  1 
ATOM   8088  C  C   . LYS   D  1 224 ? 67.184 -43.562 69.427  1.00 22.42 ? 224  LYS   D C   1 
ATOM   8089  O  O   . LYS   D  1 224 ? 66.114 -42.944 69.528  1.00 22.26 ? 224  LYS   D O   1 
ATOM   8090  C  CB  . LYS   D  1 224 ? 69.163 -42.054 69.296  1.00 23.53 ? 224  LYS   D CB  1 
ATOM   8091  C  CG  . LYS   D  1 224 ? 70.364 -41.400 70.012  1.00 29.07 ? 224  LYS   D CG  1 
ATOM   8092  C  CD  . LYS   D  1 224 ? 69.920 -40.674 71.246  1.00 35.40 ? 224  LYS   D CD  1 
ATOM   8093  C  CE  . LYS   D  1 224 ? 71.118 -40.022 71.978  1.00 44.31 ? 224  LYS   D CE  1 
ATOM   8094  N  NZ  . LYS   D  1 224 ? 70.740 -39.580 73.368  1.00 49.53 ? 224  LYS   D NZ  1 
ATOM   8095  N  N   . PHE   D  1 225 ? 67.308 -44.648 68.665  1.00 20.93 ? 225  PHE   D N   1 
ATOM   8096  C  CA  . PHE   D  1 225 ? 66.120 -45.240 68.054  1.00 21.59 ? 225  PHE   D CA  1 
ATOM   8097  C  C   . PHE   D  1 225 ? 65.085 -45.613 69.120  1.00 19.81 ? 225  PHE   D C   1 
ATOM   8098  O  O   . PHE   D  1 225 ? 63.874 -45.491 68.916  1.00 20.19 ? 225  PHE   D O   1 
ATOM   8099  C  CB  . PHE   D  1 225 ? 66.475 -46.523 67.284  1.00 21.09 ? 225  PHE   D CB  1 
ATOM   8100  C  CG  . PHE   D  1 225 ? 67.289 -46.340 66.013  1.00 20.14 ? 225  PHE   D CG  1 
ATOM   8101  C  CD1 . PHE   D  1 225 ? 67.657 -45.107 65.523  1.00 23.77 ? 225  PHE   D CD1 1 
ATOM   8102  C  CD2 . PHE   D  1 225 ? 67.732 -47.489 65.364  1.00 23.25 ? 225  PHE   D CD2 1 
ATOM   8103  C  CE1 . PHE   D  1 225 ? 68.437 -45.013 64.370  1.00 25.29 ? 225  PHE   D CE1 1 
ATOM   8104  C  CE2 . PHE   D  1 225 ? 68.495 -47.407 64.186  1.00 26.52 ? 225  PHE   D CE2 1 
ATOM   8105  C  CZ  . PHE   D  1 225 ? 68.839 -46.146 63.693  1.00 24.09 ? 225  PHE   D CZ  1 
ATOM   8106  N  N   . ARG   D  1 226 ? 65.562 -46.100 70.264  1.00 19.73 ? 226  ARG   D N   1 
ATOM   8107  C  CA  . ARG   D  1 226 ? 64.660 -46.658 71.262  1.00 19.38 ? 226  ARG   D CA  1 
ATOM   8108  C  C   . ARG   D  1 226 ? 63.933 -45.585 72.046  1.00 20.63 ? 226  ARG   D C   1 
ATOM   8109  O  O   . ARG   D  1 226 ? 63.012 -45.927 72.810  1.00 23.33 ? 226  ARG   D O   1 
ATOM   8110  C  CB  . ARG   D  1 226 ? 65.441 -47.573 72.212  1.00 18.81 ? 226  ARG   D CB  1 
ATOM   8111  C  CG  . ARG   D  1 226 ? 66.244 -48.699 71.499  1.00 19.74 ? 226  ARG   D CG  1 
ATOM   8112  C  CD  . ARG   D  1 226 ? 66.718 -49.736 72.536  1.00 22.64 ? 226  ARG   D CD  1 
ATOM   8113  N  NE  . ARG   D  1 226 ? 67.595 -50.702 71.861  1.00 22.60 ? 226  ARG   D NE  1 
ATOM   8114  C  CZ  . ARG   D  1 226 ? 68.925 -50.677 71.896  1.00 22.89 ? 226  ARG   D CZ  1 
ATOM   8115  N  NH1 . ARG   D  1 226 ? 69.589 -49.774 72.653  1.00 25.40 ? 226  ARG   D NH1 1 
ATOM   8116  N  NH2 . ARG   D  1 226 ? 69.622 -51.558 71.207  1.00 24.08 ? 226  ARG   D NH2 1 
ATOM   8117  N  N   . LYS   D  1 227 ? 64.259 -44.295 71.832  1.00 20.21 ? 227  LYS   D N   1 
ATOM   8118  C  CA  . LYS   D  1 227 ? 63.541 -43.216 72.494  1.00 22.63 ? 227  LYS   D CA  1 
ATOM   8119  C  C   . LYS   D  1 227 ? 62.297 -42.796 71.730  1.00 20.44 ? 227  LYS   D C   1 
ATOM   8120  O  O   . LYS   D  1 227 ? 61.496 -42.004 72.253  1.00 23.22 ? 227  LYS   D O   1 
ATOM   8121  C  CB  . LYS   D  1 227 ? 64.470 -42.012 72.717  1.00 24.64 ? 227  LYS   D CB  1 
ATOM   8122  C  CG  . LYS   D  1 227 ? 65.629 -42.342 73.648  1.00 26.92 ? 227  LYS   D CG  1 
ATOM   8123  C  CD  . LYS   D  1 227 ? 66.623 -41.189 73.739  1.00 38.89 ? 227  LYS   D CD  1 
ATOM   8124  C  CE  . LYS   D  1 227 ? 66.094 -39.981 74.488  1.00 46.35 ? 227  LYS   D CE  1 
ATOM   8125  N  NZ  . LYS   D  1 227 ? 67.195 -38.941 74.564  1.00 50.30 ? 227  LYS   D NZ  1 
ATOM   8126  N  N   . LEU   D  1 228 ? 62.127 -43.290 70.504  1.00 19.12 ? 228  LEU   D N   1 
ATOM   8127  C  CA  . LEU   D  1 228 ? 60.834 -43.132 69.854  1.00 18.75 ? 228  LEU   D CA  1 
ATOM   8128  C  C   . LEU   D  1 228 ? 59.777 -43.982 70.548  1.00 19.03 ? 228  LEU   D C   1 
ATOM   8129  O  O   . LEU   D  1 228 ? 60.099 -44.927 71.282  1.00 19.83 ? 228  LEU   D O   1 
ATOM   8130  C  CB  . LEU   D  1 228 ? 60.933 -43.573 68.396  1.00 20.11 ? 228  LEU   D CB  1 
ATOM   8131  C  CG  . LEU   D  1 228 ? 61.919 -42.719 67.577  1.00 21.04 ? 228  LEU   D CG  1 
ATOM   8132  C  CD1 . LEU   D  1 228 ? 62.222 -43.473 66.299  1.00 22.04 ? 228  LEU   D CD1 1 
ATOM   8133  C  CD2 . LEU   D  1 228 ? 61.277 -41.447 67.236  1.00 22.69 ? 228  LEU   D CD2 1 
ATOM   8134  N  N   . ASN   D  1 229 ? 58.503 -43.651 70.263  1.00 18.96 ? 229  ASN   D N   1 
ATOM   8135  C  CA  . ASN   D  1 229 ? 57.345 -44.324 70.833  1.00 19.94 ? 229  ASN   D CA  1 
ATOM   8136  C  C   . ASN   D  1 229 ? 56.434 -44.823 69.709  1.00 21.52 ? 229  ASN   D C   1 
ATOM   8137  O  O   . ASN   D  1 229 ? 56.256 -44.137 68.694  1.00 20.04 ? 229  ASN   D O   1 
ATOM   8138  C  CB  . ASN   D  1 229 ? 56.541 -43.358 71.749  1.00 22.74 ? 229  ASN   D CB  1 
ATOM   8139  C  CG  . ASN   D  1 229 ? 57.221 -43.095 73.094  1.00 28.03 ? 229  ASN   D CG  1 
ATOM   8140  O  OD1 . ASN   D  1 229 ? 58.215 -43.694 73.422  1.00 28.39 ? 229  ASN   D OD1 1 
ATOM   8141  N  ND2 . ASN   D  1 229 ? 56.646 -42.192 73.881  1.00 32.44 ? 229  ASN   D ND2 1 
ATOM   8142  N  N   . PHE   D  1 230 ? 55.819 -45.988 69.925  1.00 18.88 ? 230  PHE   D N   1 
ATOM   8143  C  CA  . PHE   D  1 230 ? 54.783 -46.473 69.004  1.00 17.99 ? 230  PHE   D CA  1 
ATOM   8144  C  C   . PHE   D  1 230 ? 53.508 -45.688 69.119  1.00 20.93 ? 230  PHE   D C   1 
ATOM   8145  O  O   . PHE   D  1 230 ? 52.766 -45.554 68.133  1.00 20.46 ? 230  PHE   D O   1 
ATOM   8146  C  CB  . PHE   D  1 230 ? 54.398 -47.924 69.303  1.00 19.00 ? 230  PHE   D CB  1 
ATOM   8147  C  CG  . PHE   D  1 230 ? 55.442 -48.941 69.001  1.00 17.70 ? 230  PHE   D CG  1 
ATOM   8148  C  CD1 . PHE   D  1 230 ? 55.923 -49.157 67.673  1.00 16.49 ? 230  PHE   D CD1 1 
ATOM   8149  C  CD2 . PHE   D  1 230 ? 55.873 -49.788 70.015  1.00 19.65 ? 230  PHE   D CD2 1 
ATOM   8150  C  CE1 . PHE   D  1 230 ? 56.857 -50.219 67.409  1.00 18.60 ? 230  PHE   D CE1 1 
ATOM   8151  C  CE2 . PHE   D  1 230 ? 56.806 -50.844 69.758  1.00 17.16 ? 230  PHE   D CE2 1 
ATOM   8152  C  CZ  . PHE   D  1 230 ? 57.274 -51.066 68.476  1.00 17.76 ? 230  PHE   D CZ  1 
ATOM   8153  N  N   . ASN   D  1 231 ? 53.182 -45.241 70.330  1.00 19.63 ? 231  ASN   D N   1 
ATOM   8154  C  CA  . ASN   D  1 231 ? 51.879 -44.652 70.599  1.00 21.73 ? 231  ASN   D CA  1 
ATOM   8155  C  C   . ASN   D  1 231 ? 51.776 -43.211 70.087  1.00 23.17 ? 231  ASN   D C   1 
ATOM   8156  O  O   . ASN   D  1 231 ? 52.772 -42.538 69.812  1.00 22.64 ? 231  ASN   D O   1 
ATOM   8157  C  CB  . ASN   D  1 231 ? 51.619 -44.655 72.098  1.00 24.39 ? 231  ASN   D CB  1 
ATOM   8158  C  CG  . ASN   D  1 231 ? 52.732 -43.933 72.870  1.00 23.83 ? 231  ASN   D CG  1 
ATOM   8159  O  OD1 . ASN   D  1 231 ? 53.803 -44.480 73.047  1.00 22.84 ? 231  ASN   D OD1 1 
ATOM   8160  N  ND2 . ASN   D  1 231 ? 52.481 -42.694 73.291  1.00 26.94 ? 231  ASN   D ND2 1 
ATOM   8161  N  N   . GLY   D  1 232 ? 50.530 -42.759 69.948  1.00 24.56 ? 232  GLY   D N   1 
ATOM   8162  C  CA  . GLY   D  1 232 ? 50.271 -41.354 69.767  1.00 26.45 ? 232  GLY   D CA  1 
ATOM   8163  C  C   . GLY   D  1 232 ? 50.296 -40.596 71.070  1.00 27.08 ? 232  GLY   D C   1 
ATOM   8164  O  O   . GLY   D  1 232 ? 50.147 -41.132 72.177  1.00 29.41 ? 232  GLY   D O   1 
ATOM   8165  N  N   . GLU   D  1 233 ? 50.437 -39.288 70.935  1.00 28.42 ? 233  GLU   D N   1 
ATOM   8166  C  CA  . GLU   D  1 233 ? 50.409 -38.405 72.102  1.00 35.67 ? 233  GLU   D CA  1 
ATOM   8167  C  C   . GLU   D  1 233 ? 49.113 -38.589 72.902  1.00 34.07 ? 233  GLU   D C   1 
ATOM   8168  O  O   . GLU   D  1 233 ? 48.021 -38.673 72.335  1.00 35.60 ? 233  GLU   D O   1 
ATOM   8169  C  CB  . GLU   D  1 233 ? 50.576 -36.963 71.610  1.00 41.38 ? 233  GLU   D CB  1 
ATOM   8170  C  CG  . GLU   D  1 233 ? 51.159 -35.993 72.598  1.00 50.30 ? 233  GLU   D CG  1 
ATOM   8171  C  CD  . GLU   D  1 233 ? 51.435 -34.623 71.965  1.00 59.27 ? 233  GLU   D CD  1 
ATOM   8172  O  OE1 . GLU   D  1 233 ? 52.453 -34.462 71.238  1.00 59.78 ? 233  GLU   D OE1 1 
ATOM   8173  O  OE2 . GLU   D  1 233 ? 50.621 -33.697 72.188  1.00 64.89 ? 233  GLU   D OE2 1 
ATOM   8174  N  N   . GLY   D  1 234 ? 49.217 -38.682 74.233  1.00 33.80 ? 234  GLY   D N   1 
ATOM   8175  C  CA  . GLY   D  1 234 ? 48.028 -38.865 75.057  1.00 34.38 ? 234  GLY   D CA  1 
ATOM   8176  C  C   . GLY   D  1 234 ? 47.590 -40.305 75.267  1.00 35.64 ? 234  GLY   D C   1 
ATOM   8177  O  O   . GLY   D  1 234 ? 46.599 -40.550 75.978  1.00 37.13 ? 234  GLY   D O   1 
ATOM   8178  N  N   . GLU   D  1 235 ? 48.301 -41.258 74.706  1.00 35.63 ? 235  GLU   D N   1 
ATOM   8179  C  CA  . GLU   D  1 235 ? 48.095 -42.671 74.952  1.00 32.92 ? 235  GLU   D CA  1 
ATOM   8180  C  C   . GLU   D  1 235 ? 49.210 -43.213 75.820  1.00 34.82 ? 235  GLU   D C   1 
ATOM   8181  O  O   . GLU   D  1 235 ? 50.277 -42.598 75.916  1.00 31.95 ? 235  GLU   D O   1 
ATOM   8182  C  CB  . GLU   D  1 235 ? 48.068 -43.432 73.635  1.00 34.45 ? 235  GLU   D CB  1 
ATOM   8183  C  CG  . GLU   D  1 235 ? 47.094 -42.825 72.649  1.00 35.33 ? 235  GLU   D CG  1 
ATOM   8184  C  CD  . GLU   D  1 235 ? 47.065 -43.625 71.347  1.00 38.37 ? 235  GLU   D CD  1 
ATOM   8185  O  OE1 . GLU   D  1 235 ? 45.954 -43.828 70.799  1.00 44.32 ? 235  GLU   D OE1 1 
ATOM   8186  O  OE2 . GLU   D  1 235 ? 48.145 -44.073 70.902  1.00 31.47 ? 235  GLU   D OE2 1 
ATOM   8187  N  N   . PRO   D  1 236 ? 49.006 -44.357 76.488  1.00 36.53 ? 236  PRO   D N   1 
ATOM   8188  C  CA  . PRO   D  1 236 ? 50.069 -44.878 77.363  1.00 36.67 ? 236  PRO   D CA  1 
ATOM   8189  C  C   . PRO   D  1 236 ? 51.346 -45.098 76.573  1.00 30.84 ? 236  PRO   D C   1 
ATOM   8190  O  O   . PRO   D  1 236 ? 51.316 -45.550 75.428  1.00 30.83 ? 236  PRO   D O   1 
ATOM   8191  C  CB  . PRO   D  1 236 ? 49.492 -46.193 77.898  1.00 39.92 ? 236  PRO   D CB  1 
ATOM   8192  C  CG  . PRO   D  1 236 ? 47.986 -45.953 77.876  1.00 41.22 ? 236  PRO   D CG  1 
ATOM   8193  C  CD  . PRO   D  1 236 ? 47.754 -45.134 76.607  1.00 37.60 ? 236  PRO   D CD  1 
ATOM   8194  N  N   . GLU   D  1 237 ? 52.464 -44.751 77.203  1.00 35.98 ? 237  GLU   D N   1 
ATOM   8195  C  CA  . GLU   D  1 237 ? 53.740 -44.765 76.500  1.00 36.47 ? 237  GLU   D CA  1 
ATOM   8196  C  C   . GLU   D  1 237 ? 54.144 -46.186 76.163  1.00 32.95 ? 237  GLU   D C   1 
ATOM   8197  O  O   . GLU   D  1 237 ? 54.140 -47.069 77.026  1.00 34.52 ? 237  GLU   D O   1 
ATOM   8198  C  CB  . GLU   D  1 237 ? 54.838 -44.115 77.338  1.00 42.62 ? 237  GLU   D CB  1 
ATOM   8199  C  CG  . GLU   D  1 237 ? 56.220 -44.406 76.770  1.00 49.39 ? 237  GLU   D CG  1 
ATOM   8200  C  CD  . GLU   D  1 237 ? 57.280 -43.426 77.230  1.00 58.14 ? 237  GLU   D CD  1 
ATOM   8201  O  OE1 . GLU   D  1 237 ? 57.096 -42.198 77.049  1.00 61.02 ? 237  GLU   D OE1 1 
ATOM   8202  O  OE2 . GLU   D  1 237 ? 58.301 -43.898 77.786  1.00 61.05 ? 237  GLU   D OE2 1 
ATOM   8203  N  N   . GLU   D  1 238 ? 54.492 -46.408 74.905  1.00 26.59 ? 238  GLU   D N   1 
ATOM   8204  C  CA  . GLU   D  1 238 ? 54.993 -47.704 74.448  1.00 25.03 ? 238  GLU   D CA  1 
ATOM   8205  C  C   . GLU   D  1 238 ? 56.273 -47.444 73.684  1.00 23.50 ? 238  GLU   D C   1 
ATOM   8206  O  O   . GLU   D  1 238 ? 56.208 -47.074 72.504  1.00 24.18 ? 238  GLU   D O   1 
ATOM   8207  C  CB  . GLU   D  1 238 ? 54.007 -48.416 73.554  1.00 27.33 ? 238  GLU   D CB  1 
ATOM   8208  C  CG  . GLU   D  1 238 ? 52.622 -48.593 74.169  1.00 34.83 ? 238  GLU   D CG  1 
ATOM   8209  C  CD  . GLU   D  1 238 ? 51.588 -49.028 73.134  1.00 43.76 ? 238  GLU   D CD  1 
ATOM   8210  O  OE1 . GLU   D  1 238 ? 50.398 -49.203 73.510  1.00 48.25 ? 238  GLU   D OE1 1 
ATOM   8211  O  OE2 . GLU   D  1 238 ? 51.956 -49.188 71.937  1.00 44.32 ? 238  GLU   D OE2 1 
ATOM   8212  N  N   . PRO   D  1 239 ? 57.424 -47.680 74.290  1.00 22.48 ? 239  PRO   D N   1 
ATOM   8213  C  CA  . PRO   D  1 239 ? 58.696 -47.467 73.585  1.00 22.41 ? 239  PRO   D CA  1 
ATOM   8214  C  C   . PRO   D  1 239 ? 58.739 -48.236 72.272  1.00 19.89 ? 239  PRO   D C   1 
ATOM   8215  O  O   . PRO   D  1 239 ? 58.335 -49.400 72.178  1.00 19.82 ? 239  PRO   D O   1 
ATOM   8216  C  CB  . PRO   D  1 239 ? 59.742 -47.990 74.573  1.00 23.60 ? 239  PRO   D CB  1 
ATOM   8217  C  CG  . PRO   D  1 239 ? 59.072 -47.841 75.952  1.00 28.39 ? 239  PRO   D CG  1 
ATOM   8218  C  CD  . PRO   D  1 239 ? 57.612 -48.089 75.701  1.00 26.99 ? 239  PRO   D CD  1 
ATOM   8219  N  N   . MET   D  1 240 ? 59.260 -47.566 71.250  1.00 18.63 ? 240  MET   D N   1 
ATOM   8220  C  CA  . MET   D  1 240 ? 59.378 -48.167 69.921  1.00 17.86 ? 240  MET   D CA  1 
ATOM   8221  C  C   . MET   D  1 240 ? 60.644 -49.029 69.929  1.00 18.66 ? 240  MET   D C   1 
ATOM   8222  O  O   . MET   D  1 240 ? 61.759 -48.528 69.678  1.00 17.98 ? 240  MET   D O   1 
ATOM   8223  C  CB  . MET   D  1 240 ? 59.439 -47.074 68.850  1.00 17.05 ? 240  MET   D CB  1 
ATOM   8224  C  CG  . MET   D  1 240 ? 59.447 -47.712 67.425  1.00 18.60 ? 240  MET   D CG  1 
ATOM   8225  S  SD  . MET   D  1 240 ? 59.497 -46.460 66.141  1.00 17.78 ? 240  MET   D SD  1 
ATOM   8226  C  CE  . MET   D  1 240 ? 57.784 -46.017 66.091  1.00 18.47 ? 240  MET   D CE  1 
ATOM   8227  N  N   . VAL   D  1 241 ? 60.476 -50.321 70.252  1.00 19.02 ? 241  VAL   D N   1 
ATOM   8228  C  CA  . VAL   D  1 241 ? 61.572 -51.281 70.317  1.00 17.70 ? 241  VAL   D CA  1 
ATOM   8229  C  C   . VAL   D  1 241 ? 61.015 -52.618 69.831  1.00 17.38 ? 241  VAL   D C   1 
ATOM   8230  O  O   . VAL   D  1 241 ? 59.813 -52.865 69.895  1.00 18.51 ? 241  VAL   D O   1 
ATOM   8231  C  CB  . VAL   D  1 241 ? 62.176 -51.452 71.726  1.00 19.12 ? 241  VAL   D CB  1 
ATOM   8232  C  CG1 . VAL   D  1 241 ? 62.797 -50.093 72.200  1.00 19.18 ? 241  VAL   D CG1 1 
ATOM   8233  C  CG2 . VAL   D  1 241 ? 61.161 -51.967 72.698  1.00 18.73 ? 241  VAL   D CG2 1 
ATOM   8234  N  N   . ASP   D  1 242 ? 61.915 -53.472 69.323  1.00 16.76 ? 242  ASP   D N   1 
ATOM   8235  C  CA  . ASP   D  1 242 ? 61.525 -54.823 68.859  1.00 17.52 ? 242  ASP   D CA  1 
ATOM   8236  C  C   . ASP   D  1 242 ? 60.436 -54.722 67.782  1.00 16.61 ? 242  ASP   D C   1 
ATOM   8237  O  O   . ASP   D  1 242 ? 59.434 -55.473 67.765  1.00 17.67 ? 242  ASP   D O   1 
ATOM   8238  C  CB  . ASP   D  1 242 ? 61.097 -55.703 70.043  1.00 19.30 ? 242  ASP   D CB  1 
ATOM   8239  C  CG  . ASP   D  1 242 ? 62.285 -56.066 70.928  1.00 20.64 ? 242  ASP   D CG  1 
ATOM   8240  O  OD1 . ASP   D  1 242 ? 63.387 -56.286 70.368  1.00 18.49 ? 242  ASP   D OD1 1 
ATOM   8241  O  OD2 . ASP   D  1 242 ? 62.095 -56.125 72.152  1.00 23.29 ? 242  ASP   D OD2 1 
ATOM   8242  N  N   . ASN   D  1 243 ? 60.674 -53.813 66.832  1.00 15.06 ? 243  ASN   D N   1 
ATOM   8243  C  CA  . ASN   D  1 243 ? 59.802 -53.673 65.650  1.00 15.15 ? 243  ASN   D CA  1 
ATOM   8244  C  C   . ASN   D  1 243 ? 60.350 -54.483 64.477  1.00 16.18 ? 243  ASN   D C   1 
ATOM   8245  O  O   . ASN   D  1 243 ? 60.481 -53.991 63.356  1.00 16.53 ? 243  ASN   D O   1 
ATOM   8246  C  CB  . ASN   D  1 243 ? 59.607 -52.202 65.259  1.00 16.29 ? 243  ASN   D CB  1 
ATOM   8247  C  CG  . ASN   D  1 243 ? 60.931 -51.429 65.058  1.00 15.31 ? 243  ASN   D CG  1 
ATOM   8248  O  OD1 . ASN   D  1 243 ? 62.012 -51.973 65.239  1.00 17.85 ? 243  ASN   D OD1 1 
ATOM   8249  N  ND2 . ASN   D  1 243 ? 60.804 -50.136 64.671  1.00 18.23 ? 243  ASN   D ND2 1 
ATOM   8250  N  N   . TRP   D  1 244 ? 60.604 -55.762 64.762  1.00 16.28 ? 244  TRP   D N   1 
ATOM   8251  C  CA  . TRP   D  1 244 ? 61.084 -56.740 63.778  1.00 16.05 ? 244  TRP   D CA  1 
ATOM   8252  C  C   . TRP   D  1 244 ? 60.157 -57.942 63.763  1.00 16.94 ? 244  TRP   D C   1 
ATOM   8253  O  O   . TRP   D  1 244 ? 59.534 -58.290 64.753  1.00 18.45 ? 244  TRP   D O   1 
ATOM   8254  C  CB  . TRP   D  1 244 ? 62.522 -57.216 64.115  1.00 18.15 ? 244  TRP   D CB  1 
ATOM   8255  C  CG  . TRP   D  1 244 ? 62.729 -57.651 65.561  1.00 18.86 ? 244  TRP   D CG  1 
ATOM   8256  C  CD1 . TRP   D  1 244 ? 63.152 -56.851 66.583  1.00 18.56 ? 244  TRP   D CD1 1 
ATOM   8257  C  CD2 . TRP   D  1 244 ? 62.529 -58.978 66.139  1.00 22.27 ? 244  TRP   D CD2 1 
ATOM   8258  N  NE1 . TRP   D  1 244 ? 63.233 -57.590 67.760  1.00 19.00 ? 244  TRP   D NE1 1 
ATOM   8259  C  CE2 . TRP   D  1 244 ? 62.859 -58.894 67.516  1.00 24.47 ? 244  TRP   D CE2 1 
ATOM   8260  C  CE3 . TRP   D  1 244 ? 62.102 -60.226 65.625  1.00 23.79 ? 244  TRP   D CE3 1 
ATOM   8261  C  CZ2 . TRP   D  1 244 ? 62.757 -59.997 68.414  1.00 27.90 ? 244  TRP   D CZ2 1 
ATOM   8262  C  CZ3 . TRP   D  1 244 ? 61.997 -61.319 66.498  1.00 25.65 ? 244  TRP   D CZ3 1 
ATOM   8263  C  CH2 . TRP   D  1 244 ? 62.347 -61.213 67.883  1.00 25.19 ? 244  TRP   D CH2 1 
ATOM   8264  N  N   . ARG   D  1 245 ? 60.042 -58.547 62.581  1.00 16.09 ? 245  ARG   D N   1 
ATOM   8265  C  CA  . ARG   D  1 245 ? 59.318 -59.834 62.407  1.00 14.73 ? 245  ARG   D CA  1 
ATOM   8266  C  C   . ARG   D  1 245 ? 60.293 -61.009 62.550  1.00 16.22 ? 245  ARG   D C   1 
ATOM   8267  O  O   . ARG   D  1 245 ? 61.391 -60.931 62.007  1.00 18.02 ? 245  ARG   D O   1 
ATOM   8268  C  CB  . ARG   D  1 245 ? 58.663 -59.841 61.021  1.00 14.11 ? 245  ARG   D CB  1 
ATOM   8269  C  CG  . ARG   D  1 245 ? 57.750 -61.055 60.852  1.00 14.59 ? 245  ARG   D CG  1 
ATOM   8270  C  CD  . ARG   D  1 245 ? 57.221 -61.191 59.421  1.00 15.90 ? 245  ARG   D CD  1 
ATOM   8271  N  NE  . ARG   D  1 245 ? 56.167 -62.208 59.428  1.00 15.65 ? 245  ARG   D NE  1 
ATOM   8272  C  CZ  . ARG   D  1 245 ? 55.643 -62.794 58.356  1.00 14.40 ? 245  ARG   D CZ  1 
ATOM   8273  N  NH1 . ARG   D  1 245 ? 56.124 -62.552 57.119  1.00 13.97 ? 245  ARG   D NH1 1 
ATOM   8274  N  NH2 . ARG   D  1 245 ? 54.594 -63.653 58.516  1.00 15.19 ? 245  ARG   D NH2 1 
ATOM   8275  N  N   . PRO   D  1 246 ? 59.901 -62.102 63.250  1.00 17.15 ? 246  PRO   D N   1 
ATOM   8276  C  CA  . PRO   D  1 246 ? 60.742 -63.338 63.297  1.00 18.02 ? 246  PRO   D CA  1 
ATOM   8277  C  C   . PRO   D  1 246 ? 60.970 -63.868 61.884  1.00 17.45 ? 246  PRO   D C   1 
ATOM   8278  O  O   . PRO   D  1 246 ? 60.163 -63.639 60.976  1.00 17.98 ? 246  PRO   D O   1 
ATOM   8279  C  CB  . PRO   D  1 246 ? 59.910 -64.338 64.130  1.00 22.02 ? 246  PRO   D CB  1 
ATOM   8280  C  CG  . PRO   D  1 246 ? 58.976 -63.475 64.975  1.00 19.64 ? 246  PRO   D CG  1 
ATOM   8281  C  CD  . PRO   D  1 246 ? 58.674 -62.237 64.062  1.00 19.38 ? 246  PRO   D CD  1 
ATOM   8282  N  N   . THR   D  1 247 ? 62.086 -64.572 61.698  1.00 19.10 ? 247  THR   D N   1 
ATOM   8283  C  CA  . THR   D  1 247 ? 62.300 -65.192 60.396  1.00 17.95 ? 247  THR   D CA  1 
ATOM   8284  C  C   . THR   D  1 247 ? 61.264 -66.291 60.140  1.00 17.43 ? 247  THR   D C   1 
ATOM   8285  O  O   . THR   D  1 247 ? 60.756 -66.962 61.053  1.00 18.73 ? 247  THR   D O   1 
ATOM   8286  C  CB  . THR   D  1 247 ? 63.702 -65.794 60.268  1.00 18.47 ? 247  THR   D CB  1 
ATOM   8287  O  OG1 . THR   D  1 247 ? 63.965 -66.678 61.369  1.00 19.34 ? 247  THR   D OG1 1 
ATOM   8288  C  CG2 . THR   D  1 247 ? 64.743 -64.697 60.262  1.00 19.35 ? 247  THR   D CG2 1 
ATOM   8289  N  N   . GLN   D  1 248 ? 60.935 -66.445 58.858  1.00 16.50 ? 248  GLN   D N   1 
ATOM   8290  C  CA  . GLN   D  1 248 ? 59.875 -67.309 58.352  1.00 14.87 ? 248  GLN   D CA  1 
ATOM   8291  C  C   . GLN   D  1 248 ? 60.461 -68.442 57.521  1.00 15.57 ? 248  GLN   D C   1 
ATOM   8292  O  O   . GLN   D  1 248 ? 61.600 -68.361 57.052  1.00 16.82 ? 248  GLN   D O   1 
ATOM   8293  C  CB  . GLN   D  1 248 ? 58.884 -66.485 57.506  1.00 15.73 ? 248  GLN   D CB  1 
ATOM   8294  C  CG  . GLN   D  1 248 ? 58.246 -65.306 58.278  1.00 15.76 ? 248  GLN   D CG  1 
ATOM   8295  C  CD  . GLN   D  1 248 ? 57.450 -65.830 59.474  1.00 15.67 ? 248  GLN   D CD  1 
ATOM   8296  O  OE1 . GLN   D  1 248 ? 56.636 -66.757 59.357  1.00 18.02 ? 248  GLN   D OE1 1 
ATOM   8297  N  NE2 . GLN   D  1 248 ? 57.748 -65.264 60.629  1.00 16.33 ? 248  GLN   D NE2 1 
ATOM   8298  N  N   . PRO   D  1 249 ? 59.721 -69.521 57.332  1.00 16.88 ? 249  PRO   D N   1 
ATOM   8299  C  CA  . PRO   D  1 249 ? 60.242 -70.681 56.619  1.00 18.26 ? 249  PRO   D CA  1 
ATOM   8300  C  C   . PRO   D  1 249 ? 60.573 -70.312 55.183  1.00 17.78 ? 249  PRO   D C   1 
ATOM   8301  O  O   . PRO   D  1 249 ? 59.791 -69.650 54.506  1.00 18.18 ? 249  PRO   D O   1 
ATOM   8302  C  CB  . PRO   D  1 249 ? 59.073 -71.669 56.660  1.00 19.38 ? 249  PRO   D CB  1 
ATOM   8303  C  CG  . PRO   D  1 249 ? 58.281 -71.283 57.922  1.00 19.73 ? 249  PRO   D CG  1 
ATOM   8304  C  CD  . PRO   D  1 249 ? 58.387 -69.760 57.926  1.00 17.47 ? 249  PRO   D CD  1 
ATOM   8305  N  N   . LEU   D  1 250 ? 61.724 -70.783 54.715  1.00 17.60 ? 250  LEU   D N   1 
ATOM   8306  C  CA  . LEU   D  1 250 ? 62.112 -70.566 53.320  1.00 18.83 ? 250  LEU   D CA  1 
ATOM   8307  C  C   . LEU   D  1 250 ? 61.192 -71.308 52.356  1.00 18.82 ? 250  LEU   D C   1 
ATOM   8308  O  O   . LEU   D  1 250 ? 60.991 -70.842 51.221  1.00 21.02 ? 250  LEU   D O   1 
ATOM   8309  C  CB  . LEU   D  1 250 ? 63.575 -71.008 53.124  1.00 22.66 ? 250  LEU   D CB  1 
ATOM   8310  C  CG  . LEU   D  1 250 ? 64.290 -70.606 51.826  1.00 24.57 ? 250  LEU   D CG  1 
ATOM   8311  C  CD1 . LEU   D  1 250 ? 64.200 -69.089 51.636  1.00 21.78 ? 250  LEU   D CD1 1 
ATOM   8312  C  CD2 . LEU   D  1 250 ? 65.784 -71.079 51.873  1.00 27.48 ? 250  LEU   D CD2 1 
ATOM   8313  N  N   . LYS   D  1 251 ? 60.636 -72.465 52.756  1.00 18.76 ? 251  LYS   D N   1 
ATOM   8314  C  CA  . LYS   D  1 251 ? 59.796 -73.262 51.885  1.00 19.33 ? 251  LYS   D CA  1 
ATOM   8315  C  C   . LYS   D  1 251 ? 60.530 -73.539 50.587  1.00 22.88 ? 251  LYS   D C   1 
ATOM   8316  O  O   . LYS   D  1 251 ? 61.708 -73.933 50.618  1.00 23.80 ? 251  LYS   D O   1 
ATOM   8317  C  CB  . LYS   D  1 251 ? 58.426 -72.612 51.702  1.00 20.70 ? 251  LYS   D CB  1 
ATOM   8318  C  CG  . LYS   D  1 251 ? 57.747 -72.435 53.111  1.00 26.46 ? 251  LYS   D CG  1 
ATOM   8319  C  CD  . LYS   D  1 251 ? 56.268 -72.108 53.059  1.00 27.67 ? 251  LYS   D CD  1 
ATOM   8320  C  CE  . LYS   D  1 251 ? 55.694 -71.964 54.472  1.00 32.00 ? 251  LYS   D CE  1 
ATOM   8321  N  NZ  . LYS   D  1 251 ? 54.246 -71.644 54.480  1.00 32.72 ? 251  LYS   D NZ  1 
ATOM   8322  N  N   . ASN   D  1 252 ? 59.846 -73.432 49.458  1.00 20.71 ? 252  ASN   D N   1 
ATOM   8323  C  CA  . ASN   D  1 252 ? 60.384 -73.904 48.188  1.00 25.11 ? 252  ASN   D CA  1 
ATOM   8324  C  C   . ASN   D  1 252 ? 61.016 -72.728 47.458  1.00 29.00 ? 252  ASN   D C   1 
ATOM   8325  O  O   . ASN   D  1 252 ? 60.566 -72.328 46.356  1.00 31.53 ? 252  ASN   D O   1 
ATOM   8326  C  CB  . ASN   D  1 252 ? 59.283 -74.555 47.356  1.00 28.25 ? 252  ASN   D CB  1 
ATOM   8327  C  CG  . ASN   D  1 252 ? 59.833 -75.310 46.192  1.00 35.77 ? 252  ASN   D CG  1 
ATOM   8328  O  OD1 . ASN   D  1 252 ? 61.056 -75.487 46.071  1.00 34.09 ? 252  ASN   D OD1 1 
ATOM   8329  N  ND2 . ASN   D  1 252 ? 58.947 -75.740 45.296  1.00 39.38 ? 252  ASN   D ND2 1 
ATOM   8330  N  N   . ARG   D  1 253 ? 62.047 -72.164 48.112  1.00 22.87 ? 253  ARG   D N   1 
ATOM   8331  C  CA  . ARG   D  1 253 ? 62.818 -71.037 47.581  1.00 21.63 ? 253  ARG   D CA  1 
ATOM   8332  C  C   . ARG   D  1 253 ? 64.311 -71.309 47.740  1.00 24.42 ? 253  ARG   D C   1 
ATOM   8333  O  O   . ARG   D  1 253 ? 64.719 -72.141 48.562  1.00 26.10 ? 253  ARG   D O   1 
ATOM   8334  C  CB  . ARG   D  1 253 ? 62.481 -69.697 48.274  1.00 20.75 ? 253  ARG   D CB  1 
ATOM   8335  C  CG  . ARG   D  1 253 ? 61.068 -69.279 47.964  1.00 20.62 ? 253  ARG   D CG  1 
ATOM   8336  C  CD  . ARG   D  1 253 ? 60.698 -68.007 48.728  1.00 19.22 ? 253  ARG   D CD  1 
ATOM   8337  N  NE  . ARG   D  1 253 ? 60.602 -68.272 50.170  1.00 18.67 ? 253  ARG   D NE  1 
ATOM   8338  C  CZ  . ARG   D  1 253 ? 60.420 -67.322 51.082  1.00 16.70 ? 253  ARG   D CZ  1 
ATOM   8339  N  NH1 . ARG   D  1 253 ? 60.391 -66.029 50.741  1.00 17.38 ? 253  ARG   D NH1 1 
ATOM   8340  N  NH2 . ARG   D  1 253 ? 60.256 -67.641 52.379  1.00 16.13 ? 253  ARG   D NH2 1 
ATOM   8341  N  N   . GLN   D  1 254 ? 65.114 -70.595 46.940  1.00 22.96 ? 254  GLN   D N   1 
ATOM   8342  C  CA  . GLN   D  1 254 ? 66.573 -70.691 46.938  1.00 27.64 ? 254  GLN   D CA  1 
ATOM   8343  C  C   . GLN   D  1 254 ? 67.125 -69.301 47.152  1.00 27.21 ? 254  GLN   D C   1 
ATOM   8344  O  O   . GLN   D  1 254 ? 66.672 -68.345 46.503  1.00 29.26 ? 254  GLN   D O   1 
ATOM   8345  C  CB  . GLN   D  1 254 ? 67.119 -71.266 45.614  1.00 33.20 ? 254  GLN   D CB  1 
ATOM   8346  C  CG  . GLN   D  1 254 ? 66.470 -72.549 45.225  1.00 42.13 ? 254  GLN   D CG  1 
ATOM   8347  C  CD  . GLN   D  1 254 ? 66.836 -73.010 43.825  1.00 50.58 ? 254  GLN   D CD  1 
ATOM   8348  O  OE1 . GLN   D  1 254 ? 67.236 -74.158 43.638  1.00 56.12 ? 254  GLN   D OE1 1 
ATOM   8349  N  NE2 . GLN   D  1 254 ? 66.684 -72.128 42.835  1.00 51.15 ? 254  GLN   D NE2 1 
ATOM   8350  N  N   . ILE   D  1 255 ? 68.067 -69.184 48.089  1.00 23.82 ? 255  ILE   D N   1 
ATOM   8351  C  CA  . ILE   D  1 255 ? 68.789 -67.938 48.299  1.00 22.80 ? 255  ILE   D CA  1 
ATOM   8352  C  C   . ILE   D  1 255 ? 70.020 -67.990 47.410  1.00 24.32 ? 255  ILE   D C   1 
ATOM   8353  O  O   . ILE   D  1 255 ? 70.803 -68.944 47.477  1.00 27.38 ? 255  ILE   D O   1 
ATOM   8354  C  CB  . ILE   D  1 255 ? 69.151 -67.733 49.778  1.00 22.94 ? 255  ILE   D CB  1 
ATOM   8355  C  CG1 . ILE   D  1 255 ? 67.860 -67.688 50.622  1.00 25.73 ? 255  ILE   D CG1 1 
ATOM   8356  C  CG2 . ILE   D  1 255 ? 69.830 -66.366 49.961  1.00 24.86 ? 255  ILE   D CG2 1 
ATOM   8357  C  CD1 . ILE   D  1 255 ? 68.092 -67.460 52.149  1.00 24.53 ? 255  ILE   D CD1 1 
ATOM   8358  N  N   . LYS   D  1 256 ? 70.163 -66.995 46.529  1.00 23.57 ? 256  LYS   D N   1 
ATOM   8359  C  CA  . LYS   D  1 256 ? 71.300 -66.950 45.618  1.00 24.58 ? 256  LYS   D CA  1 
ATOM   8360  C  C   . LYS   D  1 256 ? 72.304 -65.919 46.115  1.00 23.91 ? 256  LYS   D C   1 
ATOM   8361  O  O   . LYS   D  1 256 ? 71.940 -64.940 46.762  1.00 24.01 ? 256  LYS   D O   1 
ATOM   8362  C  CB  . LYS   D  1 256 ? 70.877 -66.586 44.190  1.00 25.94 ? 256  LYS   D CB  1 
ATOM   8363  C  CG  . LYS   D  1 256 ? 69.906 -67.559 43.536  1.00 27.37 ? 256  LYS   D CG  1 
ATOM   8364  C  CD  . LYS   D  1 256 ? 70.481 -68.996 43.547  1.00 33.45 ? 256  LYS   D CD  1 
ATOM   8365  C  CE  . LYS   D  1 256 ? 69.657 -69.950 42.686  1.00 39.80 ? 256  LYS   D CE  1 
ATOM   8366  N  NZ  . LYS   D  1 256 ? 70.264 -71.334 42.769  1.00 42.28 ? 256  LYS   D NZ  1 
ATOM   8367  N  N   . ALA   D  1 257 ? 73.579 -66.162 45.831  1.00 25.76 ? 257  ALA   D N   1 
ATOM   8368  C  CA  . ALA   D  1 257 ? 74.652 -65.225 46.150  1.00 26.71 ? 257  ALA   D CA  1 
ATOM   8369  C  C   . ALA   D  1 257 ? 75.186 -64.573 44.879  1.00 26.86 ? 257  ALA   D C   1 
ATOM   8370  O  O   . ALA   D  1 257 ? 75.274 -65.210 43.829  1.00 28.75 ? 257  ALA   D O   1 
ATOM   8371  C  CB  . ALA   D  1 257 ? 75.815 -65.915 46.888  1.00 26.82 ? 257  ALA   D CB  1 
ATOM   8372  N  N   . SER   D  1 258 ? 75.534 -63.281 44.988  1.00 25.78 ? 258  SER   D N   1 
ATOM   8373  C  CA  . SER   D  1 258 ? 76.146 -62.529 43.905  1.00 23.73 ? 258  SER   D CA  1 
ATOM   8374  C  C   . SER   D  1 258 ? 77.607 -62.848 43.752  1.00 28.42 ? 258  SER   D C   1 
ATOM   8375  O  O   . SER   D  1 258 ? 78.223 -62.431 42.754  1.00 30.19 ? 258  SER   D O   1 
ATOM   8376  C  CB  . SER   D  1 258 ? 75.994 -61.014 44.188  1.00 22.78 ? 258  SER   D CB  1 
ATOM   8377  O  OG  . SER   D  1 258 ? 76.858 -60.606 45.243  1.00 24.71 ? 258  SER   D OG  1 
ATOM   8378  N  N   . PHE   D  1 259 ? 78.166 -63.518 44.758  1.00 27.89 ? 259  PHE   D N   1 
ATOM   8379  C  CA  . PHE   D  1 259 ? 79.623 -63.795 44.760  1.00 30.12 ? 259  PHE   D CA  1 
ATOM   8380  C  C   . PHE   D  1 259 ? 79.860 -65.297 44.674  1.00 33.73 ? 259  PHE   D C   1 
ATOM   8381  O  O   . PHE   D  1 259 ? 79.030 -66.091 45.154  1.00 34.86 ? 259  PHE   D O   1 
ATOM   8382  C  CB  . PHE   D  1 259 ? 80.195 -63.177 46.040  1.00 29.41 ? 259  PHE   D CB  1 
ATOM   8383  C  CG  . PHE   D  1 259 ? 79.424 -63.498 47.314  1.00 28.83 ? 259  PHE   D CG  1 
ATOM   8384  C  CD1 . PHE   D  1 259 ? 78.376 -62.688 47.738  1.00 29.48 ? 259  PHE   D CD1 1 
ATOM   8385  C  CD2 . PHE   D  1 259 ? 79.755 -64.602 48.090  1.00 31.13 ? 259  PHE   D CD2 1 
ATOM   8386  C  CE1 . PHE   D  1 259 ? 77.678 -62.980 48.898  1.00 30.37 ? 259  PHE   D CE1 1 
ATOM   8387  C  CE2 . PHE   D  1 259 ? 79.054 -64.889 49.250  1.00 30.56 ? 259  PHE   D CE2 1 
ATOM   8388  C  CZ  . PHE   D  1 259 ? 78.018 -64.079 49.651  1.00 31.15 ? 259  PHE   D CZ  1 
ATOM   8389  N  N   . LYS   D  1 260 ? 80.991 -65.667 44.072  1.00 59.64 ? 260  LYS   D N   1 
ATOM   8390  C  CA  . LYS   D  1 260 ? 81.494 -67.062 44.126  1.00 56.78 ? 260  LYS   D CA  1 
ATOM   8391  C  C   . LYS   D  1 260 ? 82.038 -67.338 45.537  1.00 52.37 ? 260  LYS   D C   1 
ATOM   8392  O  O   . LYS   D  1 260 ? 82.498 -66.405 46.188  1.00 49.74 ? 260  LYS   D O   1 
ATOM   8393  C  CB  . LYS   D  1 260 ? 82.566 -67.266 43.051  1.00 58.28 ? 260  LYS   D CB  1 
ATOM   8394  C  CG  . LYS   D  1 260 ? 82.087 -67.093 41.618  1.00 60.36 ? 260  LYS   D CG  1 
ATOM   8395  C  CD  . LYS   D  1 260 ? 83.231 -67.119 40.613  1.00 63.55 ? 260  LYS   D CD  1 
ATOM   8396  C  CE  . LYS   D  1 260 ? 82.767 -67.052 39.193  1.00 67.02 ? 260  LYS   D CE  1 
ATOM   8397  N  NZ  . LYS   D  1 260 ? 82.072 -68.278 38.795  1.00 69.10 ? 260  LYS   D NZ  1 
ATOM   8398  O  OXT . LYS   D  1 260 ? 81.978 -68.503 45.953  1.00 51.20 ? 260  LYS   D OXT 1 
HETATM 8399  C  C1  . A1H9O E  2 .   ? 40.190 -4.329  0.584   1.00 15.84 ? 301  A1H9O A C1  1 
HETATM 8400  C  C2  . A1H9O E  2 .   ? 38.834 -4.624  0.603   1.00 16.17 ? 301  A1H9O A C2  1 
HETATM 8401  C  C3  . A1H9O E  2 .   ? 38.086 -4.526  -0.561  1.00 16.51 ? 301  A1H9O A C3  1 
HETATM 8402  C  C4  . A1H9O E  2 .   ? 40.799 -3.940  -0.599  1.00 15.61 ? 301  A1H9O A C4  1 
HETATM 8403  C  C5  . A1H9O E  2 .   ? 40.051 -3.843  -1.764  1.00 16.90 ? 301  A1H9O A C5  1 
HETATM 8404  C  C6  . A1H9O E  2 .   ? 38.692 -4.126  -1.742  1.00 17.47 ? 301  A1H9O A C6  1 
HETATM 8405  C  C7  . A1H9O E  2 .   ? 37.867 -4.038  -3.041  1.00 17.27 ? 301  A1H9O A C7  1 
HETATM 8406  C  C8  . A1H9O E  2 .   ? 38.013 -6.269  -6.056  1.00 17.11 ? 301  A1H9O A C8  1 
HETATM 8407  C  C9  . A1H9O E  2 .   ? 37.192 -6.811  -7.196  1.00 18.34 ? 301  A1H9O A C9  1 
HETATM 8408  C  C10 . A1H9O E  2 .   ? 35.799 -6.891  -7.088  1.00 20.40 ? 301  A1H9O A C10 1 
HETATM 8409  C  C11 . A1H9O E  2 .   ? 37.830 -7.248  -8.361  1.00 18.31 ? 301  A1H9O A C11 1 
HETATM 8410  C  C12 . A1H9O E  2 .   ? 35.045 -7.403  -8.151  1.00 26.86 ? 301  A1H9O A C12 1 
HETATM 8411  C  C13 . A1H9O E  2 .   ? 37.078 -7.759  -9.423  1.00 18.97 ? 301  A1H9O A C13 1 
HETATM 8412  C  C14 . A1H9O E  2 .   ? 35.685 -7.838  -9.318  1.00 23.52 ? 301  A1H9O A C14 1 
HETATM 8413  C  C15 . A1H9O E  2 .   ? 38.824 -8.205  -11.087 1.00 20.32 ? 301  A1H9O A C15 1 
HETATM 8414  C  C16 . A1H9O E  2 .   ? 33.828 -8.796  -10.618 1.00 25.17 ? 301  A1H9O A C16 1 
HETATM 8415  C  C17 . A1H9O E  2 .   ? 33.573 -9.482  -11.961 1.00 23.10 ? 301  A1H9O A C17 1 
HETATM 8416  C  C18 . A1H9O E  2 .   ? 39.001 -8.901  -12.434 1.00 19.60 ? 301  A1H9O A C18 1 
HETATM 8417  C  C19 . A1H9O E  2 .   ? 39.556 -7.871  -13.413 1.00 19.74 ? 301  A1H9O A C19 1 
HETATM 8418  C  C20 . A1H9O E  2 .   ? 39.991 -10.069 -12.204 1.00 20.48 ? 301  A1H9O A C20 1 
HETATM 8419  C  C21 . A1H9O E  2 .   ? 32.639 -8.566  -12.773 1.00 23.59 ? 301  A1H9O A C21 1 
HETATM 8420  C  C22 . A1H9O E  2 .   ? 32.914 -10.830 -11.638 1.00 22.69 ? 301  A1H9O A C22 1 
HETATM 8421  C  C23 . A1H9O E  2 .   ? 36.205 -11.257 -15.646 1.00 28.46 ? 301  A1H9O A C23 1 
HETATM 8422  C  C24 . A1H9O E  2 .   ? 37.514 -10.018 -14.034 1.00 23.42 ? 301  A1H9O A C24 1 
HETATM 8423  C  C25 . A1H9O E  2 .   ? 34.951 -10.297 -13.807 1.00 29.33 ? 301  A1H9O A C25 1 
HETATM 8424  C  C26 . A1H9O E  2 .   ? 38.415 -5.013  -4.069  1.00 17.36 ? 301  A1H9O A C26 1 
HETATM 8425  N  N1  . A1H9O E  2 .   ? 42.517 -5.194  1.713   1.00 14.44 ? 301  A1H9O A N1  1 
HETATM 8426  N  N2  . A1H9O E  2 .   ? 37.484 -5.470  -5.133  1.00 19.11 ? 301  A1H9O A N2  1 
HETATM 8427  N  N3  . A1H9O E  2 .   ? 36.223 -10.460 -14.422 1.00 26.86 ? 301  A1H9O A N3  1 
HETATM 8428  N  N4  . A1H9O E  2 .   ? 37.633 -9.357  -12.875 1.00 21.44 ? 301  A1H9O A N4  1 
HETATM 8429  N  N5  . A1H9O E  2 .   ? 34.885 -9.622  -12.652 1.00 19.11 ? 301  A1H9O A N5  1 
HETATM 8430  N  N6  . A1H9O E  2 .   ? 35.087 -8.369  -10.456 1.00 22.13 ? 301  A1H9O A N6  1 
HETATM 8431  N  N7  . A1H9O E  2 .   ? 37.561 -8.224  -10.639 1.00 18.00 ? 301  A1H9O A N7  1 
HETATM 8432  O  O1  . A1H9O E  2 .   ? 40.406 -5.303  2.951   1.00 15.87 ? 301  A1H9O A O1  1 
HETATM 8433  O  O2  . A1H9O E  2 .   ? 41.449 -3.128  2.477   1.00 16.53 ? 301  A1H9O A O2  1 
HETATM 8434  O  O3  . A1H9O E  2 .   ? 39.199 -6.574  -5.985  1.00 17.06 ? 301  A1H9O A O3  1 
HETATM 8435  O  O4  . A1H9O E  2 .   ? 39.753 -7.571  -10.595 1.00 18.23 ? 301  A1H9O A O4  1 
HETATM 8436  O  O5  . A1H9O E  2 .   ? 32.890 -8.580  -9.847  1.00 24.63 ? 301  A1H9O A O5  1 
HETATM 8437  O  O6  . A1H9O E  2 .   ? 38.456 -10.351 -14.783 1.00 24.16 ? 301  A1H9O A O6  1 
HETATM 8438  O  O7  . A1H9O E  2 .   ? 33.983 -10.715 -14.452 1.00 30.08 ? 301  A1H9O A O7  1 
HETATM 8439  S  S1  . A1H9O E  2 .   ? 41.140 -4.459  2.064   1.00 15.67 ? 301  A1H9O A S1  1 
HETATM 8440  FE FE1 . A1H9O E  2 .   ? 36.238 -8.563  -11.916 1.00 21.53 ? 301  A1H9O A FE1 1 
HETATM 8441  ZN ZN  . ZN    F  3 .   ? 42.630 -7.084  2.462   1.00 15.80 ? 302  ZN    A ZN  1 
HETATM 8442  C  C1  . EDO   G  4 .   ? 33.826 -4.833  -3.686  1.00 30.02 ? 303  EDO   A C1  1 
HETATM 8443  O  O1  . EDO   G  4 .   ? 34.703 -4.518  -4.796  1.00 26.95 ? 303  EDO   A O1  1 
HETATM 8444  C  C2  . EDO   G  4 .   ? 33.892 -6.263  -3.319  1.00 31.96 ? 303  EDO   A C2  1 
HETATM 8445  O  O2  . EDO   G  4 .   ? 35.236 -6.735  -3.411  1.00 25.09 ? 303  EDO   A O2  1 
HETATM 8446  C  C1  . EDO   H  4 .   ? 22.628 -5.067  -2.866  1.00 50.10 ? 304  EDO   A C1  1 
HETATM 8447  O  O1  . EDO   H  4 .   ? 23.302 -6.266  -3.275  1.00 48.34 ? 304  EDO   A O1  1 
HETATM 8448  C  C2  . EDO   H  4 .   ? 23.596 -3.888  -2.926  1.00 50.47 ? 304  EDO   A C2  1 
HETATM 8449  O  O2  . EDO   H  4 .   ? 24.483 -4.063  -4.044  1.00 50.31 ? 304  EDO   A O2  1 
HETATM 8450  ZN ZN  . ZN    I  3 .   ? 43.107 -5.159  -10.140 1.00 16.08 ? 305  ZN    A ZN  1 
HETATM 8451  ZN ZN  . ZN    J  3 .   ? 55.139 -1.275  22.789  1.00 27.31 ? 306  ZN    A ZN  1 
HETATM 8452  ZN ZN  . ZN    K  3 .   ? 44.793 -0.300  -13.119 1.00 15.87 ? 307  ZN    A ZN  1 
HETATM 8453  C  C1  . A1H9O L  2 .   ? 23.830 -49.887 24.967  1.00 15.76 ? 301  A1H9O B C1  1 
HETATM 8454  C  C2  . A1H9O L  2 .   ? 23.404 -49.432 26.207  1.00 16.04 ? 301  A1H9O B C2  1 
HETATM 8455  C  C3  . A1H9O L  2 .   ? 22.947 -50.332 27.158  1.00 15.66 ? 301  A1H9O B C3  1 
HETATM 8456  C  C4  . A1H9O L  2 .   ? 23.802 -51.243 24.679  1.00 15.18 ? 301  A1H9O B C4  1 
HETATM 8457  C  C5  . A1H9O L  2 .   ? 23.347 -52.145 25.631  1.00 16.58 ? 301  A1H9O B C5  1 
HETATM 8458  C  C6  . A1H9O L  2 .   ? 22.909 -51.687 26.867  1.00 17.27 ? 301  A1H9O B C6  1 
HETATM 8459  C  C7  . A1H9O L  2 .   ? 22.425 -52.693 27.931  1.00 17.80 ? 301  A1H9O B C7  1 
HETATM 8460  C  C8  . A1H9O L  2 .   ? 24.437 -55.190 29.883  1.00 16.93 ? 301  A1H9O B C8  1 
HETATM 8461  C  C9  . A1H9O L  2 .   ? 24.489 -55.949 31.183  1.00 18.33 ? 301  A1H9O B C9  1 
HETATM 8462  C  C10 . A1H9O L  2 .   ? 23.870 -55.433 32.327  1.00 20.67 ? 301  A1H9O B C10 1 
HETATM 8463  C  C11 . A1H9O L  2 .   ? 25.173 -57.167 31.247  1.00 18.90 ? 301  A1H9O B C11 1 
HETATM 8464  C  C12 . A1H9O L  2 .   ? 23.930 -56.142 33.533  1.00 25.36 ? 301  A1H9O B C12 1 
HETATM 8465  C  C13 . A1H9O L  2 .   ? 25.233 -57.877 32.451  1.00 18.44 ? 301  A1H9O B C13 1 
HETATM 8466  C  C14 . A1H9O L  2 .   ? 24.612 -57.364 33.595  1.00 22.89 ? 301  A1H9O B C14 1 
HETATM 8467  C  C15 . A1H9O L  2 .   ? 26.499 -59.869 31.784  1.00 20.49 ? 301  A1H9O B C15 1 
HETATM 8468  C  C16 . A1H9O L  2 .   ? 24.508 -57.901 35.989  1.00 23.57 ? 301  A1H9O B C16 1 
HETATM 8469  C  C17 . A1H9O L  2 .   ? 25.011 -58.957 36.971  1.00 23.39 ? 301  A1H9O B C17 1 
HETATM 8470  C  C18 . A1H9O L  2 .   ? 27.192 -61.075 32.413  1.00 19.31 ? 301  A1H9O B C18 1 
HETATM 8471  C  C19 . A1H9O L  2 .   ? 26.573 -62.329 31.802  1.00 18.94 ? 301  A1H9O B C19 1 
HETATM 8472  C  C20 . A1H9O L  2 .   ? 28.698 -60.951 32.073  1.00 20.10 ? 301  A1H9O B C20 1 
HETATM 8473  C  C21 . A1H9O L  2 .   ? 23.773 -59.599 37.628  1.00 24.25 ? 301  A1H9O B C21 1 
HETATM 8474  C  C22 . A1H9O L  2 .   ? 25.881 -58.214 37.994  1.00 24.65 ? 301  A1H9O B C22 1 
HETATM 8475  C  C23 . A1H9O L  2 .   ? 27.878 -62.879 36.883  1.00 28.31 ? 301  A1H9O B C23 1 
HETATM 8476  C  C24 . A1H9O L  2 .   ? 27.458 -61.940 34.694  1.00 21.48 ? 301  A1H9O B C24 1 
HETATM 8477  C  C25 . A1H9O L  2 .   ? 26.415 -60.948 36.842  1.00 28.82 ? 301  A1H9O B C25 1 
HETATM 8478  C  C26 . A1H9O L  2 .   ? 23.562 -53.626 28.310  1.00 18.32 ? 301  A1H9O B C26 1 
HETATM 8479  N  N1  . A1H9O L  2 .   ? 25.746 -49.339 23.103  1.00 14.56 ? 301  A1H9O B N1  1 
HETATM 8480  N  N2  . A1H9O L  2 .   ? 23.482 -54.296 29.633  1.00 18.35 ? 301  A1H9O B N2  1 
HETATM 8481  N  N3  . A1H9O L  2 .   ? 27.226 -61.840 36.090  1.00 25.85 ? 301  A1H9O B N3  1 
HETATM 8482  N  N4  . A1H9O L  2 .   ? 26.907 -61.019 33.893  1.00 20.70 ? 301  A1H9O B N4  1 
HETATM 8483  N  N5  . A1H9O L  2 .   ? 25.766 -59.976 36.191  1.00 19.03 ? 301  A1H9O B N5  1 
HETATM 8484  N  N6  . A1H9O L  2 .   ? 24.765 -58.184 34.707  1.00 22.21 ? 301  A1H9O B N6  1 
HETATM 8485  N  N7  . A1H9O L  2 .   ? 25.863 -59.094 32.673  1.00 17.19 ? 301  A1H9O B N7  1 
HETATM 8486  O  O1  . A1H9O L  2 .   ? 24.773 -47.549 24.463  1.00 16.49 ? 301  A1H9O B O1  1 
HETATM 8487  O  O2  . A1H9O L  2 .   ? 23.421 -48.664 22.740  1.00 16.75 ? 301  A1H9O B O2  1 
HETATM 8488  O  O3  . A1H9O L  2 .   ? 25.300 -55.402 29.038  1.00 16.69 ? 301  A1H9O B O3  1 
HETATM 8489  O  O4  . A1H9O L  2 .   ? 26.463 -59.744 30.562  1.00 17.83 ? 301  A1H9O B O4  1 
HETATM 8490  O  O5  . A1H9O L  2 .   ? 23.837 -56.949 36.397  1.00 23.66 ? 301  A1H9O B O5  1 
HETATM 8491  O  O6  . A1H9O L  2 .   ? 28.153 -62.908 34.322  1.00 24.20 ? 301  A1H9O B O6  1 
HETATM 8492  O  O7  . A1H9O L  2 .   ? 26.291 -61.215 38.043  1.00 29.18 ? 301  A1H9O B O7  1 
HETATM 8493  S  S1  . A1H9O L  2 .   ? 24.416 -48.740 23.760  1.00 16.05 ? 301  A1H9O B S1  1 
HETATM 8494  FE FE1 . A1H9O L  2 .   ? 25.510 -59.860 34.343  1.00 20.71 ? 301  A1H9O B FE1 1 
HETATM 8495  ZN ZN  . ZN    M  3 .   ? 27.447 -48.359 23.643  1.00 15.72 ? 302  ZN    B ZN  1 
HETATM 8496  C  C1  . EDO   N  4 .   ? 22.331 -51.427 32.298  1.00 33.26 ? 303  EDO   B C1  1 
HETATM 8497  O  O1  . EDO   N  4 .   ? 23.423 -51.807 31.474  1.00 25.12 ? 303  EDO   B O1  1 
HETATM 8498  C  C2  . EDO   N  4 .   ? 21.074 -51.990 31.771  1.00 31.21 ? 303  EDO   B C2  1 
HETATM 8499  O  O2  . EDO   N  4 .   ? 21.234 -53.363 31.317  1.00 26.39 ? 303  EDO   B O2  1 
HETATM 8500  C  C1  . EDO   O  4 .   ? 17.208 -54.854 26.543  1.00 29.52 ? 304  EDO   B C1  1 
HETATM 8501  O  O1  . EDO   O  4 .   ? 18.079 -54.796 27.689  1.00 26.80 ? 304  EDO   B O1  1 
HETATM 8502  C  C2  . EDO   O  4 .   ? 16.183 -56.032 26.499  1.00 26.27 ? 304  EDO   B C2  1 
HETATM 8503  O  O2  . EDO   O  4 .   ? 16.566 -57.154 27.254  1.00 28.63 ? 304  EDO   B O2  1 
HETATM 8504  C  C1  . EDO   P  4 .   ? 20.350 -68.108 13.379  1.00 63.20 ? 305  EDO   B C1  1 
HETATM 8505  O  O1  . EDO   P  4 .   ? 21.465 -67.878 14.212  1.00 65.75 ? 305  EDO   B O1  1 
HETATM 8506  C  C2  . EDO   P  4 .   ? 19.359 -69.028 13.983  1.00 60.93 ? 305  EDO   B C2  1 
HETATM 8507  O  O2  . EDO   P  4 .   ? 19.877 -70.323 14.213  1.00 56.53 ? 305  EDO   B O2  1 
HETATM 8508  ZN ZN  . ZN    Q  3 .   ? 34.439 -70.211 10.572  1.00 27.61 ? 306  ZN    B ZN  1 
HETATM 8509  ZN ZN  . ZN    R  3 .   ? 28.696 -33.791 3.912   1.00 27.79 ? 307  ZN    B ZN  1 
HETATM 8510  ZN ZN  . ZN    S  3 .   ? 22.464 -70.747 23.799  1.00 16.22 ? 308  ZN    B ZN  1 
HETATM 8511  C  C1  . A1H9O T  2 .   ? 55.117 -14.592 51.656  1.00 16.28 ? 301  A1H9O C C1  1 
HETATM 8512  C  C2  . A1H9O T  2 .   ? 54.554 -13.370 51.319  1.00 16.70 ? 301  A1H9O C C2  1 
HETATM 8513  C  C3  . A1H9O T  2 .   ? 55.105 -12.194 51.805  1.00 16.37 ? 301  A1H9O C C3  1 
HETATM 8514  C  C4  . A1H9O T  2 .   ? 56.231 -14.640 52.480  1.00 15.77 ? 301  A1H9O C C4  1 
HETATM 8515  C  C5  . A1H9O T  2 .   ? 56.782 -13.464 52.968  1.00 16.80 ? 301  A1H9O C C5  1 
HETATM 8516  C  C6  . A1H9O T  2 .   ? 56.212 -12.241 52.638  1.00 17.59 ? 301  A1H9O C C6  1 
HETATM 8517  C  C7  . A1H9O T  2 .   ? 56.840 -10.935 53.160  1.00 18.72 ? 301  A1H9O C C7  1 
HETATM 8518  C  C8  . A1H9O T  2 .   ? 60.004 -9.261  52.034  1.00 17.66 ? 301  A1H9O C C8  1 
HETATM 8519  C  C9  . A1H9O T  2 .   ? 60.683 -7.924  51.908  1.00 17.71 ? 301  A1H9O C C9  1 
HETATM 8520  C  C10 . A1H9O T  2 .   ? 59.924 -6.755  51.786  1.00 21.10 ? 301  A1H9O C C10 1 
HETATM 8521  C  C11 . A1H9O T  2 .   ? 62.080 -7.857  51.897  1.00 18.52 ? 301  A1H9O C C11 1 
HETATM 8522  C  C12 . A1H9O T  2 .   ? 60.566 -5.517  51.662  1.00 26.14 ? 301  A1H9O C C12 1 
HETATM 8523  C  C13 . A1H9O T  2 .   ? 62.722 -6.621  51.773  1.00 18.17 ? 301  A1H9O C C13 1 
HETATM 8524  C  C14 . A1H9O T  2 .   ? 61.965 -5.450  51.654  1.00 23.11 ? 301  A1H9O C C14 1 
HETATM 8525  C  C15 . A1H9O T  2 .   ? 65.082 -7.275  51.924  1.00 19.51 ? 301  A1H9O C C15 1 
HETATM 8526  C  C16 . A1H9O T  2 .   ? 62.379 -3.072  51.180  1.00 23.23 ? 301  A1H9O C C16 1 
HETATM 8527  C  C17 . A1H9O T  2 .   ? 63.548 -2.108  50.970  1.00 23.44 ? 301  A1H9O C C17 1 
HETATM 8528  C  C18 . A1H9O T  2 .   ? 66.473 -6.680  51.714  1.00 18.64 ? 301  A1H9O C C18 1 
HETATM 8529  C  C19 . A1H9O T  2 .   ? 67.254 -6.868  53.011  1.00 18.69 ? 301  A1H9O C C19 1 
HETATM 8530  C  C20 . A1H9O T  2 .   ? 67.115 -7.456  50.536  1.00 19.99 ? 301  A1H9O C C20 1 
HETATM 8531  C  C21 . A1H9O T  2 .   ? 63.466 -1.040  52.077  1.00 23.91 ? 301  A1H9O C C21 1 
HETATM 8532  C  C22 . A1H9O T  2 .   ? 63.363 -1.500  49.573  1.00 24.03 ? 301  A1H9O C C22 1 
HETATM 8533  C  C23 . A1H9O T  2 .   ? 68.373 -2.379  50.466  1.00 26.75 ? 301  A1H9O C C23 1 
HETATM 8534  C  C24 . A1H9O T  2 .   ? 67.358 -4.456  51.178  1.00 23.86 ? 301  A1H9O C C24 1 
HETATM 8535  C  C25 . A1H9O T  2 .   ? 65.978 -2.299  50.829  1.00 28.53 ? 301  A1H9O C C25 1 
HETATM 8536  C  C26 . A1H9O T  2 .   ? 58.215 -10.752 52.540  1.00 19.41 ? 301  A1H9O C C26 1 
HETATM 8537  N  N1  . A1H9O T  2 .   ? 55.599 -16.976 50.421  1.00 14.32 ? 301  A1H9O C N1  1 
HETATM 8538  N  N2  . A1H9O T  2 .   ? 58.750 -9.369  52.469  1.00 19.20 ? 301  A1H9O C N2  1 
HETATM 8539  N  N3  . A1H9O T  2 .   ? 67.154 -3.096  50.832  1.00 25.45 ? 301  A1H9O C N3  1 
HETATM 8540  N  N4  . A1H9O T  2 .   ? 66.281 -5.212  51.427  1.00 20.74 ? 301  A1H9O C N4  1 
HETATM 8541  N  N5  . A1H9O T  2 .   ? 64.808 -2.890  51.104  1.00 19.97 ? 301  A1H9O C N5  1 
HETATM 8542  N  N6  . A1H9O T  2 .   ? 62.750 -4.307  51.538  1.00 22.32 ? 301  A1H9O C N6  1 
HETATM 8543  N  N7  . A1H9O T  2 .   ? 64.091 -6.390  51.752  1.00 18.19 ? 301  A1H9O C N7  1 
HETATM 8544  O  O1  . A1H9O T  2 .   ? 53.549 -15.718 49.961  1.00 16.40 ? 301  A1H9O C O1  1 
HETATM 8545  O  O2  . A1H9O T  2 .   ? 53.875 -16.789 52.149  1.00 16.63 ? 301  A1H9O C O2  1 
HETATM 8546  O  O3  . A1H9O T  2 .   ? 60.627 -10.272 51.728  1.00 17.06 ? 301  A1H9O C O3  1 
HETATM 8547  O  O4  . A1H9O T  2 .   ? 64.961 -8.423  52.341  1.00 17.68 ? 301  A1H9O C O4  1 
HETATM 8548  O  O5  . A1H9O T  2 .   ? 61.222 -2.647  51.156  1.00 24.74 ? 301  A1H9O C O5  1 
HETATM 8549  O  O6  . A1H9O T  2 .   ? 68.540 -4.857  51.148  1.00 24.80 ? 301  A1H9O C O6  1 
HETATM 8550  O  O7  . A1H9O T  2 .   ? 66.151 -1.084  50.673  1.00 28.86 ? 301  A1H9O C O7  1 
HETATM 8551  S  S1  . A1H9O T  2 .   ? 54.419 -16.086 51.032  1.00 15.60 ? 301  A1H9O C S1  1 
HETATM 8552  FE FE1 . A1H9O T  2 .   ? 64.572 -4.586  51.853  1.00 21.41 ? 301  A1H9O C FE1 1 
HETATM 8553  ZN ZN  . ZN    U  3 .   ? 55.606 -17.121 48.436  1.00 15.68 ? 302  ZN    C ZN  1 
HETATM 8554  C  C1  . EDO   V  4 .   ? 55.664 -7.036  51.201  1.00 32.27 ? 303  EDO   C C1  1 
HETATM 8555  O  O1  . EDO   V  4 .   ? 56.572 -8.009  50.711  1.00 25.18 ? 303  EDO   C O1  1 
HETATM 8556  C  C2  . EDO   V  4 .   ? 55.574 -7.063  52.671  1.00 31.43 ? 303  EDO   C C2  1 
HETATM 8557  O  O2  . EDO   V  4 .   ? 56.853 -7.250  53.331  1.00 25.44 ? 303  EDO   C O2  1 
HETATM 8558  C  C1  . EDO   W  4 .   ? 49.468 -14.996 63.187  1.00 38.62 ? 304  EDO   C C1  1 
HETATM 8559  O  O1  . EDO   W  4 .   ? 48.328 -14.386 63.780  1.00 40.65 ? 304  EDO   C O1  1 
HETATM 8560  C  C2  . EDO   W  4 .   ? 50.451 -15.545 64.229  1.00 35.56 ? 304  EDO   C C2  1 
HETATM 8561  O  O2  . EDO   W  4 .   ? 50.993 -16.889 63.919  1.00 26.58 ? 304  EDO   C O2  1 
HETATM 8562  C  C1  . EDO   X  4 .   ? 56.254 -10.446 58.833  1.00 25.57 ? 305  EDO   C C1  1 
HETATM 8563  O  O1  . EDO   X  4 .   ? 56.443 -9.535  57.761  1.00 25.59 ? 305  EDO   C O1  1 
HETATM 8564  C  C2  . EDO   X  4 .   ? 56.475 -9.775  60.214  1.00 25.78 ? 305  EDO   C C2  1 
HETATM 8565  O  O2  . EDO   X  4 .   ? 57.748 -9.165  60.302  1.00 27.84 ? 305  EDO   C O2  1 
HETATM 8566  C  C1  . EDO   Y  4 .   ? 59.421 -13.871 50.820  1.00 24.30 ? 306  EDO   C C1  1 
HETATM 8567  O  O1  . EDO   Y  4 .   ? 60.823 -13.976 50.441  1.00 18.07 ? 306  EDO   C O1  1 
HETATM 8568  C  C2  . EDO   Y  4 .   ? 58.467 -13.671 49.621  1.00 28.26 ? 306  EDO   C C2  1 
HETATM 8569  O  O2  . EDO   Y  4 .   ? 58.571 -12.312 49.205  1.00 20.03 ? 306  EDO   C O2  1 
HETATM 8570  C  C1  . EDO   Z  4 .   ? 69.976 -20.908 68.496  1.00 64.39 ? 307  EDO   C C1  1 
HETATM 8571  O  O1  . EDO   Z  4 .   ? 71.036 -20.050 68.131  1.00 61.77 ? 307  EDO   C O1  1 
HETATM 8572  C  C2  . EDO   Z  4 .   ? 68.837 -20.872 67.551  1.00 66.74 ? 307  EDO   C C2  1 
HETATM 8573  O  O2  . EDO   Z  4 .   ? 69.202 -21.187 66.225  1.00 64.75 ? 307  EDO   C O2  1 
HETATM 8574  ZN ZN  . ZN    AA 3 .   ? 65.569 -11.916 54.449  1.00 16.31 ? 308  ZN    C ZN  1 
HETATM 8575  C  C1  . A1H9O BA 2 .   ? 58.308 -52.546 54.030  1.00 14.95 ? 301  A1H9O D C1  1 
HETATM 8576  C  C2  . A1H9O BA 2 .   ? 58.501 -51.565 53.068  1.00 16.77 ? 301  A1H9O D C2  1 
HETATM 8577  C  C3  . A1H9O BA 2 .   ? 57.497 -50.647 52.802  1.00 16.55 ? 301  A1H9O D C3  1 
HETATM 8578  C  C4  . A1H9O BA 2 .   ? 57.110 -52.610 54.726  1.00 15.42 ? 301  A1H9O D C4  1 
HETATM 8579  C  C5  . A1H9O BA 2 .   ? 56.106 -51.691 54.461  1.00 16.54 ? 301  A1H9O D C5  1 
HETATM 8580  C  C6  . A1H9O BA 2 .   ? 56.296 -50.716 53.489  1.00 17.73 ? 301  A1H9O D C6  1 
HETATM 8581  C  C7  . A1H9O BA 2 .   ? 55.188 -49.682 53.211  1.00 18.34 ? 301  A1H9O D C7  1 
HETATM 8582  C  C8  . A1H9O BA 2 .   ? 54.015 -46.858 55.381  1.00 17.75 ? 301  A1H9O D C8  1 
HETATM 8583  C  C9  . A1H9O BA 2 .   ? 53.389 -45.490 55.344  1.00 17.71 ? 301  A1H9O D C9  1 
HETATM 8584  C  C10 . A1H9O BA 2 .   ? 53.525 -44.683 54.209  1.00 21.61 ? 301  A1H9O D C10 1 
HETATM 8585  C  C11 . A1H9O BA 2 .   ? 52.684 -45.020 56.457  1.00 17.96 ? 301  A1H9O D C11 1 
HETATM 8586  C  C12 . A1H9O BA 2 .   ? 52.945 -43.409 54.185  1.00 26.34 ? 301  A1H9O D C12 1 
HETATM 8587  C  C13 . A1H9O BA 2 .   ? 52.106 -43.748 56.434  1.00 17.89 ? 301  A1H9O D C13 1 
HETATM 8588  C  C14 . A1H9O BA 2 .   ? 52.237 -42.940 55.299  1.00 22.56 ? 301  A1H9O D C14 1 
HETATM 8589  C  C15 . A1H9O BA 2 .   ? 51.000 -43.673 58.622  1.00 19.67 ? 301  A1H9O D C15 1 
HETATM 8590  C  C16 . A1H9O BA 2 .   ? 51.731 -40.620 54.667  1.00 24.47 ? 301  A1H9O D C16 1 
HETATM 8591  C  C17 . A1H9O BA 2 .   ? 51.035 -39.381 55.229  1.00 24.21 ? 301  A1H9O D C17 1 
HETATM 8592  C  C18 . A1H9O BA 2 .   ? 50.302 -42.675 59.543  1.00 19.92 ? 301  A1H9O D C18 1 
HETATM 8593  C  C19 . A1H9O BA 2 .   ? 48.908 -43.220 59.839  1.00 21.26 ? 301  A1H9O D C19 1 
HETATM 8594  C  C20 . A1H9O BA 2 .   ? 51.165 -42.571 60.826  1.00 20.27 ? 301  A1H9O D C20 1 
HETATM 8595  C  C21 . A1H9O BA 2 .   ? 49.855 -39.054 54.293  1.00 24.88 ? 301  A1H9O D C21 1 
HETATM 8596  C  C22 . A1H9O BA 2 .   ? 52.085 -38.262 55.236  1.00 24.76 ? 301  A1H9O D C22 1 
HETATM 8597  C  C23 . A1H9O BA 2 .   ? 49.116 -37.956 59.459  1.00 27.92 ? 301  A1H9O D C23 1 
HETATM 8598  C  C24 . A1H9O BA 2 .   ? 49.662 -40.311 59.391  1.00 23.36 ? 301  A1H9O D C24 1 
HETATM 8599  C  C25 . A1H9O BA 2 .   ? 49.996 -38.761 57.349  1.00 29.62 ? 301  A1H9O D C25 1 
HETATM 8600  C  C26 . A1H9O BA 2 .   ? 54.945 -48.845 54.455  1.00 18.43 ? 301  A1H9O D C26 1 
HETATM 8601  N  N1  . A1H9O BA 2 .   ? 59.739 -53.842 55.957  1.00 14.36 ? 301  A1H9O D N1  1 
HETATM 8602  N  N2  . A1H9O BA 2 .   ? 54.332 -47.507 54.264  1.00 18.46 ? 301  A1H9O D N2  1 
HETATM 8603  N  N3  . A1H9O BA 2 .   ? 49.609 -39.087 58.677  1.00 26.47 ? 301  A1H9O D N3  1 
HETATM 8604  N  N4  . A1H9O BA 2 .   ? 50.203 -41.376 58.784  1.00 20.21 ? 301  A1H9O D N4  1 
HETATM 8605  N  N5  . A1H9O BA 2 .   ? 50.533 -39.722 56.588  1.00 19.72 ? 301  A1H9O D N5  1 
HETATM 8606  N  N6  . A1H9O BA 2 .   ? 51.609 -41.708 55.436  1.00 22.37 ? 301  A1H9O D N6  1 
HETATM 8607  N  N7  . A1H9O BA 2 .   ? 51.375 -43.145 57.449  1.00 17.54 ? 301  A1H9O D N7  1 
HETATM 8608  O  O1  . A1H9O BA 2 .   ? 60.799 -53.150 53.860  1.00 15.39 ? 301  A1H9O D O1  1 
HETATM 8609  O  O2  . A1H9O BA 2 .   ? 59.149 -54.970 53.867  1.00 16.63 ? 301  A1H9O D O2  1 
HETATM 8610  O  O3  . A1H9O BA 2 .   ? 54.237 -47.380 56.469  1.00 17.39 ? 301  A1H9O D O3  1 
HETATM 8611  O  O4  . A1H9O BA 2 .   ? 51.069 -44.858 58.935  1.00 17.84 ? 301  A1H9O D O4  1 
HETATM 8612  O  O5  . A1H9O BA 2 .   ? 52.223 -40.589 53.537  1.00 23.70 ? 301  A1H9O D O5  1 
HETATM 8613  O  O6  . A1H9O BA 2 .   ? 49.215 -40.285 60.557  1.00 25.82 ? 301  A1H9O D O6  1 
HETATM 8614  O  O7  . A1H9O BA 2 .   ? 49.690 -37.627 56.964  1.00 29.72 ? 301  A1H9O D O7  1 
HETATM 8615  S  S1  . A1H9O BA 2 .   ? 59.589 -53.709 54.370  1.00 15.41 ? 301  A1H9O D S1  1 
HETATM 8616  FE FE1 . A1H9O BA 2 .   ? 50.523 -41.556 56.951  1.00 21.77 ? 301  A1H9O D FE1 1 
HETATM 8617  ZN ZN  . ZN    CA 3 .   ? 61.429 -52.998 56.687  1.00 15.89 ? 302  ZN    D ZN  1 
HETATM 8618  C  C1  . EDO   DA 4 .   ? 56.220 -45.868 51.071  1.00 32.10 ? 303  EDO   D C1  1 
HETATM 8619  O  O1  . EDO   DA 4 .   ? 56.457 -46.162 52.442  1.00 25.70 ? 303  EDO   D O1  1 
HETATM 8620  C  C2  . EDO   DA 4 .   ? 55.072 -46.610 50.525  1.00 30.31 ? 303  EDO   D C2  1 
HETATM 8621  O  O2  . EDO   DA 4 .   ? 53.950 -46.695 51.426  1.00 25.75 ? 303  EDO   D O2  1 
HETATM 8622  ZN ZN  . ZN    EA 3 .   ? 74.609 -73.715 57.548  1.00 30.73 ? 304  ZN    D ZN  1 
HETATM 8623  ZN ZN  . ZN    FA 3 .   ? 44.795 -51.422 60.444  1.00 15.77 ? 305  ZN    D ZN  1 
HETATM 8624  ZN ZN  . ZN    GA 3 .   ? 39.554 -50.561 63.118  1.00 16.13 ? 306  ZN    D ZN  1 
HETATM 8625  O  O   . HOH   HA 5 .   ? 47.431 -3.711  -0.270  1.00 34.43 ? 1701 HOH   A O   1 
HETATM 8626  O  O   . HOH   HA 5 .   ? 36.709 -21.396 -13.157 1.00 48.62 ? 1702 HOH   A O   1 
HETATM 8627  O  O   . HOH   HA 5 .   ? 27.272 -24.438 -11.423 1.00 17.67 ? 1703 HOH   A O   1 
HETATM 8628  O  O   . HOH   HA 5 .   ? 25.377 -8.143  14.032  1.00 42.82 ? 1704 HOH   A O   1 
HETATM 8629  O  O   . HOH   HA 5 .   ? 53.321 -12.281 -15.945 1.00 33.35 ? 1705 HOH   A O   1 
HETATM 8630  O  O   . HOH   HA 5 .   ? 23.696 -14.089 13.041  1.00 38.48 ? 1706 HOH   A O   1 
HETATM 8631  O  O   . HOH   HA 5 .   ? 25.423 4.372   17.082  1.00 48.61 ? 1707 HOH   A O   1 
HETATM 8632  O  O   . HOH   HA 5 .   ? 59.925 -2.827  -5.905  1.00 26.20 ? 1708 HOH   A O   1 
HETATM 8633  O  O   . HOH   HA 5 .   ? 47.079 -29.341 -3.717  1.00 53.78 ? 1709 HOH   A O   1 
HETATM 8634  O  O   . HOH   HA 5 .   ? 21.524 -0.152  11.858  1.00 52.44 ? 1710 HOH   A O   1 
HETATM 8635  O  O   . HOH   HA 5 .   ? 29.477 7.767   -1.835  1.00 37.30 ? 1711 HOH   A O   1 
HETATM 8636  O  O   . HOH   HA 5 .   ? 43.966 -18.985 20.802  1.00 54.65 ? 1712 HOH   A O   1 
HETATM 8637  O  O   . HOH   HA 5 .   ? 27.540 -9.839  -4.112  1.00 42.92 ? 1713 HOH   A O   1 
HETATM 8638  O  O   . HOH   HA 5 .   ? 21.689 -14.341 2.721   1.00 40.14 ? 1714 HOH   A O   1 
HETATM 8639  O  O   . HOH   HA 5 .   ? 60.854 2.873   -2.873  1.00 42.11 ? 1715 HOH   A O   1 
HETATM 8640  O  O   . HOH   HA 5 .   ? 55.207 -3.195  11.404  1.00 22.97 ? 1716 HOH   A O   1 
HETATM 8641  O  O   . HOH   HA 5 .   ? 20.371 -3.629  11.400  1.00 43.18 ? 1717 HOH   A O   1 
HETATM 8642  O  O   . HOH   HA 5 .   ? 36.045 -29.331 0.254   1.00 47.81 ? 1718 HOH   A O   1 
HETATM 8643  O  O   . HOH   HA 5 .   ? 50.931 2.455   -8.838  1.00 33.61 ? 1719 HOH   A O   1 
HETATM 8644  O  O   . HOH   HA 5 .   ? 30.343 -9.083  21.598  1.00 55.75 ? 1720 HOH   A O   1 
HETATM 8645  O  O   . HOH   HA 5 .   ? 42.843 -29.721 12.915  1.00 47.71 ? 1721 HOH   A O   1 
HETATM 8646  O  O   . HOH   HA 5 .   ? 47.641 -5.071  0.283   1.00 16.15 ? 1722 HOH   A O   1 
HETATM 8647  O  O   . HOH   HA 5 .   ? 28.318 7.056   10.430  1.00 37.86 ? 1723 HOH   A O   1 
HETATM 8648  O  O   . HOH   HA 5 .   ? 26.548 -11.074 -7.018  1.00 45.31 ? 1724 HOH   A O   1 
HETATM 8649  O  O   . HOH   HA 5 .   ? 52.964 2.943   -12.063 1.00 27.69 ? 1725 HOH   A O   1 
HETATM 8650  O  O   . HOH   HA 5 .   ? 29.385 -18.450 -10.242 1.00 36.00 ? 1726 HOH   A O   1 
HETATM 8651  O  O   . HOH   HA 5 .   ? 32.315 12.349  1.880   1.00 52.28 ? 1727 HOH   A O   1 
HETATM 8652  O  O   . HOH   HA 5 .   ? 51.470 7.952   5.469   1.00 38.84 ? 1728 HOH   A O   1 
HETATM 8653  O  O   . HOH   HA 5 .   ? 42.178 -14.594 -0.433  1.00 26.89 ? 1729 HOH   A O   1 
HETATM 8654  O  O   . HOH   HA 5 .   ? 56.228 -22.801 9.758   1.00 40.96 ? 1730 HOH   A O   1 
HETATM 8655  O  O   . HOH   HA 5 .   ? 57.942 -12.727 -3.164  1.00 32.19 ? 1731 HOH   A O   1 
HETATM 8656  O  O   . HOH   HA 5 .   ? 52.205 8.983   15.316  1.00 36.03 ? 1732 HOH   A O   1 
HETATM 8657  O  O   . HOH   HA 5 .   ? 35.515 -15.700 -14.410 1.00 27.07 ? 1733 HOH   A O   1 
HETATM 8658  O  O   . HOH   HA 5 .   ? 23.843 -22.878 3.025   1.00 43.91 ? 1734 HOH   A O   1 
HETATM 8659  O  O   . HOH   HA 5 .   ? 54.576 0.915   16.304  1.00 39.82 ? 1735 HOH   A O   1 
HETATM 8660  O  O   . HOH   HA 5 .   ? 28.548 1.027   18.202  1.00 33.48 ? 1736 HOH   A O   1 
HETATM 8661  O  O   . HOH   HA 5 .   ? 20.405 -16.660 13.838  1.00 48.24 ? 1737 HOH   A O   1 
HETATM 8662  O  O   . HOH   HA 5 .   ? 48.509 5.029   25.296  1.00 47.44 ? 1738 HOH   A O   1 
HETATM 8663  O  O   . HOH   HA 5 .   ? 24.673 -5.507  -6.231  1.00 48.90 ? 1739 HOH   A O   1 
HETATM 8664  O  O   . HOH   HA 5 .   ? 53.332 -23.169 4.599   1.00 26.51 ? 1740 HOH   A O   1 
HETATM 8665  O  O   . HOH   HA 5 .   ? 33.177 4.454   20.412  1.00 52.64 ? 1741 HOH   A O   1 
HETATM 8666  O  O   . HOH   HA 5 .   ? 26.218 -0.334  15.000  1.00 28.79 ? 1742 HOH   A O   1 
HETATM 8667  O  O   . HOH   HA 5 .   ? 47.321 -10.411 -16.286 1.00 48.68 ? 1743 HOH   A O   1 
HETATM 8668  O  O   . HOH   HA 5 .   ? 36.614 4.969   11.511  1.00 31.88 ? 1744 HOH   A O   1 
HETATM 8669  O  O   . HOH   HA 5 .   ? 45.257 -30.732 -6.612  1.00 51.79 ? 1745 HOH   A O   1 
HETATM 8670  O  O   . HOH   HA 5 .   ? 17.302 -10.081 -1.740  1.00 28.59 ? 1746 HOH   A O   1 
HETATM 8671  O  O   . HOH   HA 5 .   ? 43.337 -16.625 -16.366 1.00 26.48 ? 1747 HOH   A O   1 
HETATM 8672  O  O   . HOH   HA 5 .   ? 33.625 -2.882  -6.582  1.00 38.20 ? 1748 HOH   A O   1 
HETATM 8673  O  O   . HOH   HA 5 .   ? 42.377 -6.984  -10.820 1.00 16.94 ? 1749 HOH   A O   1 
HETATM 8674  O  O   . HOH   HA 5 .   ? 20.204 -1.233  7.327   1.00 36.43 ? 1750 HOH   A O   1 
HETATM 8675  O  O   . HOH   HA 5 .   ? 22.870 1.843   -4.873  1.00 53.50 ? 1751 HOH   A O   1 
HETATM 8676  O  O   . HOH   HA 5 .   ? 37.634 8.981   -4.783  1.00 21.19 ? 1752 HOH   A O   1 
HETATM 8677  O  O   . HOH   HA 5 .   ? 38.956 -31.892 2.051   1.00 36.38 ? 1753 HOH   A O   1 
HETATM 8678  O  O   . HOH   HA 5 .   ? 21.556 -15.387 -3.511  1.00 25.26 ? 1754 HOH   A O   1 
HETATM 8679  O  O   . HOH   HA 5 .   ? 43.380 -2.487  27.086  1.00 39.26 ? 1755 HOH   A O   1 
HETATM 8680  O  O   . HOH   HA 5 .   ? 36.343 7.226   25.229  1.00 52.06 ? 1756 HOH   A O   1 
HETATM 8681  O  O   . HOH   HA 5 .   ? 37.775 -20.644 13.698  1.00 45.11 ? 1757 HOH   A O   1 
HETATM 8682  O  O   . HOH   HA 5 .   ? 25.284 -20.252 -0.626  1.00 26.26 ? 1758 HOH   A O   1 
HETATM 8683  O  O   . HOH   HA 5 .   ? 47.063 -24.444 -8.850  1.00 44.82 ? 1759 HOH   A O   1 
HETATM 8684  O  O   . HOH   HA 5 .   ? 50.118 4.519   -14.510 1.00 19.65 ? 1760 HOH   A O   1 
HETATM 8685  O  O   . HOH   HA 5 .   ? 44.977 -21.111 -15.880 1.00 34.58 ? 1761 HOH   A O   1 
HETATM 8686  O  O   . HOH   HA 5 .   ? 60.730 -15.599 0.015   1.00 47.27 ? 1762 HOH   A O   1 
HETATM 8687  O  O   . HOH   HA 5 .   ? 52.677 1.491   11.825  1.00 20.93 ? 1763 HOH   A O   1 
HETATM 8688  O  O   . HOH   HA 5 .   ? 33.508 -13.324 -14.831 1.00 46.88 ? 1764 HOH   A O   1 
HETATM 8689  O  O   . HOH   HA 5 .   ? 33.765 -0.358  25.644  1.00 29.96 ? 1765 HOH   A O   1 
HETATM 8690  O  O   . HOH   HA 5 .   ? 57.966 1.125   -10.843 1.00 31.60 ? 1766 HOH   A O   1 
HETATM 8691  O  O   . HOH   HA 5 .   ? 33.954 -22.395 7.652   1.00 32.34 ? 1767 HOH   A O   1 
HETATM 8692  O  O   . HOH   HA 5 .   ? 42.980 -24.937 13.796  1.00 41.28 ? 1768 HOH   A O   1 
HETATM 8693  O  O   . HOH   HA 5 .   ? 40.171 8.356   19.046  1.00 51.69 ? 1769 HOH   A O   1 
HETATM 8694  O  O   . HOH   HA 5 .   ? 25.733 -25.290 -4.992  1.00 18.76 ? 1770 HOH   A O   1 
HETATM 8695  O  O   . HOH   HA 5 .   ? 48.574 6.814   18.970  1.00 31.06 ? 1771 HOH   A O   1 
HETATM 8696  O  O   . HOH   HA 5 .   ? 41.495 -5.160  -5.921  1.00 17.37 ? 1772 HOH   A O   1 
HETATM 8697  O  O   . HOH   HA 5 .   ? 50.532 14.102  10.274  1.00 44.61 ? 1773 HOH   A O   1 
HETATM 8698  O  O   . HOH   HA 5 .   ? 60.304 -12.362 6.780   1.00 28.92 ? 1774 HOH   A O   1 
HETATM 8699  O  O   . HOH   HA 5 .   ? 51.476 5.946   4.282   1.00 22.67 ? 1775 HOH   A O   1 
HETATM 8700  O  O   . HOH   HA 5 .   ? 30.451 3.851   11.824  1.00 23.22 ? 1776 HOH   A O   1 
HETATM 8701  O  O   . HOH   HA 5 .   ? 40.044 -11.715 19.710  1.00 25.50 ? 1777 HOH   A O   1 
HETATM 8702  O  O   . HOH   HA 5 .   ? 21.019 6.891   4.198   1.00 56.07 ? 1778 HOH   A O   1 
HETATM 8703  O  O   . HOH   HA 5 .   ? 33.815 -8.943  -4.084  1.00 27.37 ? 1779 HOH   A O   1 
HETATM 8704  O  O   . HOH   HA 5 .   ? 46.584 -29.581 6.659   1.00 38.91 ? 1780 HOH   A O   1 
HETATM 8705  O  O   . HOH   HA 5 .   ? 48.684 -8.349  -8.052  1.00 17.12 ? 1781 HOH   A O   1 
HETATM 8706  O  O   . HOH   HA 5 .   ? 30.145 -22.224 12.579  1.00 43.53 ? 1782 HOH   A O   1 
HETATM 8707  O  O   . HOH   HA 5 .   ? 52.795 -16.893 4.558   1.00 21.46 ? 1783 HOH   A O   1 
HETATM 8708  O  O   . HOH   HA 5 .   ? 49.309 13.365  3.967   1.00 51.88 ? 1784 HOH   A O   1 
HETATM 8709  O  O   . HOH   HA 5 .   ? 33.253 3.891   -5.929  1.00 21.60 ? 1785 HOH   A O   1 
HETATM 8710  O  O   . HOH   HA 5 .   ? 26.561 4.964   9.990   1.00 28.75 ? 1786 HOH   A O   1 
HETATM 8711  O  O   . HOH   HA 5 .   ? 28.041 10.948  4.549   1.00 51.74 ? 1787 HOH   A O   1 
HETATM 8712  O  O   . HOH   HA 5 .   ? 41.147 3.753   29.059  1.00 41.21 ? 1788 HOH   A O   1 
HETATM 8713  O  O   . HOH   HA 5 .   ? 53.019 -24.027 -2.074  1.00 32.33 ? 1789 HOH   A O   1 
HETATM 8714  O  O   . HOH   HA 5 .   ? 32.785 -12.589 -7.689  1.00 37.56 ? 1790 HOH   A O   1 
HETATM 8715  O  O   . HOH   HA 5 .   ? 55.182 0.777   10.396  1.00 29.89 ? 1791 HOH   A O   1 
HETATM 8716  O  O   . HOH   HA 5 .   ? 48.488 -6.339  -11.932 1.00 25.33 ? 1792 HOH   A O   1 
HETATM 8717  O  O   . HOH   HA 5 .   ? 51.285 -6.163  26.043  1.00 46.91 ? 1793 HOH   A O   1 
HETATM 8718  O  O   . HOH   HA 5 .   ? 23.298 -13.775 9.701   1.00 36.36 ? 1794 HOH   A O   1 
HETATM 8719  O  O   . HOH   HA 5 .   ? 55.318 -25.856 10.069  1.00 52.54 ? 1795 HOH   A O   1 
HETATM 8720  O  O   . HOH   HA 5 .   ? 26.612 -7.462  -4.662  1.00 47.45 ? 1796 HOH   A O   1 
HETATM 8721  O  O   . HOH   HA 5 .   ? 45.522 4.608   21.980  1.00 47.17 ? 1797 HOH   A O   1 
HETATM 8722  O  O   . HOH   HA 5 .   ? 44.784 11.846  4.159   1.00 21.96 ? 1798 HOH   A O   1 
HETATM 8723  O  O   . HOH   HA 5 .   ? 53.898 -9.533  5.917   1.00 24.86 ? 1799 HOH   A O   1 
HETATM 8724  O  O   . HOH   HA 5 .   ? 46.960 11.399  10.768  1.00 27.36 ? 1800 HOH   A O   1 
HETATM 8725  O  O   . HOH   HA 5 .   ? 34.159 3.488   8.189   1.00 26.22 ? 1801 HOH   A O   1 
HETATM 8726  O  O   . HOH   HA 5 .   ? 39.582 -19.586 19.221  1.00 33.73 ? 1802 HOH   A O   1 
HETATM 8727  O  O   . HOH   HA 5 .   ? 32.543 -6.174  21.949  1.00 32.60 ? 1803 HOH   A O   1 
HETATM 8728  O  O   . HOH   HA 5 .   ? 55.723 -14.022 -7.381  1.00 31.89 ? 1804 HOH   A O   1 
HETATM 8729  O  O   . HOH   HA 5 .   ? 57.356 -3.237  -5.488  1.00 27.67 ? 1805 HOH   A O   1 
HETATM 8730  O  O   . HOH   HA 5 .   ? 33.950 5.033   15.659  1.00 46.09 ? 1806 HOH   A O   1 
HETATM 8731  O  O   . HOH   HA 5 .   ? 43.205 -12.304 14.885  1.00 22.21 ? 1807 HOH   A O   1 
HETATM 8732  O  O   . HOH   HA 5 .   ? 55.507 -2.116  18.455  1.00 27.56 ? 1808 HOH   A O   1 
HETATM 8733  O  O   . HOH   HA 5 .   ? 48.081 -10.129 -13.349 1.00 28.55 ? 1809 HOH   A O   1 
HETATM 8734  O  O   . HOH   HA 5 .   ? 39.945 -8.005  -2.471  1.00 20.52 ? 1810 HOH   A O   1 
HETATM 8735  O  O   . HOH   HA 5 .   ? 30.157 -8.270  -9.769  1.00 37.10 ? 1811 HOH   A O   1 
HETATM 8736  O  O   . HOH   HA 5 .   ? 42.461 12.443  8.606   1.00 41.91 ? 1812 HOH   A O   1 
HETATM 8737  O  O   . HOH   HA 5 .   ? 41.117 10.929  2.618   1.00 23.02 ? 1813 HOH   A O   1 
HETATM 8738  O  O   . HOH   HA 5 .   ? 51.331 2.087   -14.272 1.00 23.71 ? 1814 HOH   A O   1 
HETATM 8739  O  O   . HOH   HA 5 .   ? 25.060 -13.111 2.732   1.00 26.27 ? 1815 HOH   A O   1 
HETATM 8740  O  O   . HOH   HA 5 .   ? 55.113 -7.211  23.576  1.00 49.65 ? 1816 HOH   A O   1 
HETATM 8741  O  O   . HOH   HA 5 .   ? 22.938 -0.559  -6.150  1.00 56.39 ? 1817 HOH   A O   1 
HETATM 8742  O  O   . HOH   HA 5 .   ? 13.634 -12.200 1.786   1.00 33.88 ? 1818 HOH   A O   1 
HETATM 8743  O  O   . HOH   HA 5 .   ? 14.257 -14.318 4.627   1.00 47.61 ? 1819 HOH   A O   1 
HETATM 8744  O  O   . HOH   HA 5 .   ? 33.100 -10.025 -7.507  1.00 27.88 ? 1820 HOH   A O   1 
HETATM 8745  O  O   . HOH   HA 5 .   ? 31.863 -18.243 -11.357 1.00 31.69 ? 1821 HOH   A O   1 
HETATM 8746  O  O   . HOH   HA 5 .   ? 51.541 -4.389  -14.068 1.00 29.35 ? 1822 HOH   A O   1 
HETATM 8747  O  O   . HOH   HA 5 .   ? 36.569 7.382   21.732  1.00 57.13 ? 1823 HOH   A O   1 
HETATM 8748  O  O   . HOH   HA 5 .   ? 55.066 5.130   4.189   1.00 36.19 ? 1824 HOH   A O   1 
HETATM 8749  O  O   . HOH   HA 5 .   ? 46.023 -24.429 -4.302  1.00 33.13 ? 1825 HOH   A O   1 
HETATM 8750  O  O   . HOH   HA 5 .   ? 19.919 -12.710 1.376   1.00 29.08 ? 1826 HOH   A O   1 
HETATM 8751  O  O   . HOH   HA 5 .   ? 21.383 -10.379 11.082  1.00 41.41 ? 1827 HOH   A O   1 
HETATM 8752  O  O   . HOH   HA 5 .   ? 53.585 3.661   -2.365  1.00 18.61 ? 1828 HOH   A O   1 
HETATM 8753  O  O   . HOH   HA 5 .   ? 42.639 -5.544  -13.903 1.00 21.03 ? 1829 HOH   A O   1 
HETATM 8754  O  O   . HOH   HA 5 .   ? 36.137 -7.077  23.985  1.00 43.62 ? 1830 HOH   A O   1 
HETATM 8755  O  O   . HOH   HA 5 .   ? 56.745 -11.799 -14.567 1.00 45.66 ? 1831 HOH   A O   1 
HETATM 8756  O  O   . HOH   HA 5 .   ? 53.249 -9.833  19.091  1.00 32.90 ? 1832 HOH   A O   1 
HETATM 8757  O  O   . HOH   HA 5 .   ? 58.230 -21.089 1.180   1.00 48.87 ? 1833 HOH   A O   1 
HETATM 8758  O  O   . HOH   HA 5 .   ? 51.285 -26.662 10.572  1.00 33.03 ? 1834 HOH   A O   1 
HETATM 8759  O  O   . HOH   HA 5 .   ? 26.844 -19.436 2.680   1.00 26.05 ? 1835 HOH   A O   1 
HETATM 8760  O  O   . HOH   HA 5 .   ? 27.129 -3.769  -2.875  1.00 23.76 ? 1836 HOH   A O   1 
HETATM 8761  O  O   . HOH   HA 5 .   ? 43.596 -26.517 -4.162  1.00 45.35 ? 1837 HOH   A O   1 
HETATM 8762  O  O   . HOH   HA 5 .   ? 50.785 -9.814  -13.248 1.00 39.19 ? 1838 HOH   A O   1 
HETATM 8763  O  O   . HOH   HA 5 .   ? 40.801 -2.504  -5.219  1.00 20.11 ? 1839 HOH   A O   1 
HETATM 8764  O  O   . HOH   HA 5 .   ? 23.750 1.543   8.414   1.00 27.11 ? 1840 HOH   A O   1 
HETATM 8765  O  O   . HOH   HA 5 .   ? 41.452 -19.369 17.492  1.00 39.89 ? 1841 HOH   A O   1 
HETATM 8766  O  O   . HOH   HA 5 .   ? 43.664 -30.045 6.366   1.00 48.21 ? 1842 HOH   A O   1 
HETATM 8767  O  O   . HOH   HA 5 .   ? 18.134 -3.331  1.134   1.00 47.09 ? 1843 HOH   A O   1 
HETATM 8768  O  O   . HOH   HA 5 .   ? 34.268 -2.846  24.390  1.00 29.43 ? 1844 HOH   A O   1 
HETATM 8769  O  O   . HOH   HA 5 .   ? 42.809 -23.299 -12.342 1.00 28.18 ? 1845 HOH   A O   1 
HETATM 8770  O  O   . HOH   HA 5 .   ? 36.903 -22.676 -11.930 1.00 49.29 ? 1846 HOH   A O   1 
HETATM 8771  O  O   . HOH   HA 5 .   ? 50.361 -19.620 -15.058 1.00 33.00 ? 1847 HOH   A O   1 
HETATM 8772  O  O   . HOH   HA 5 .   ? 53.351 -20.617 14.675  1.00 49.26 ? 1848 HOH   A O   1 
HETATM 8773  O  O   . HOH   HA 5 .   ? 50.546 1.143   17.502  1.00 28.03 ? 1849 HOH   A O   1 
HETATM 8774  O  O   . HOH   HA 5 .   ? 47.431 -10.621 18.237  1.00 28.70 ? 1850 HOH   A O   1 
HETATM 8775  O  O   . HOH   HA 5 .   ? 33.154 -14.035 -10.372 1.00 33.08 ? 1851 HOH   A O   1 
HETATM 8776  O  O   . HOH   HA 5 .   ? 39.393 -17.477 23.332  1.00 37.55 ? 1852 HOH   A O   1 
HETATM 8777  O  O   . HOH   HA 5 .   ? 54.681 -7.172  -1.464  1.00 39.87 ? 1853 HOH   A O   1 
HETATM 8778  O  O   . HOH   HA 5 .   ? 57.721 4.209   -1.303  1.00 25.87 ? 1854 HOH   A O   1 
HETATM 8779  O  O   . HOH   HA 5 .   ? 25.776 -4.398  20.034  1.00 51.32 ? 1855 HOH   A O   1 
HETATM 8780  O  O   . HOH   HA 5 .   ? 25.562 -9.253  3.631   1.00 25.68 ? 1856 HOH   A O   1 
HETATM 8781  O  O   . HOH   HA 5 .   ? 52.309 12.876  2.567   1.00 49.84 ? 1857 HOH   A O   1 
HETATM 8782  O  O   . HOH   HA 5 .   ? 37.159 4.072   19.218  1.00 43.04 ? 1858 HOH   A O   1 
HETATM 8783  O  O   . HOH   HA 5 .   ? 43.554 6.980   -4.841  1.00 16.26 ? 1859 HOH   A O   1 
HETATM 8784  O  O   . HOH   HA 5 .   ? 50.990 -16.820 -24.631 1.00 40.82 ? 1860 HOH   A O   1 
HETATM 8785  O  O   . HOH   HA 5 .   ? 55.990 -5.554  -11.426 1.00 25.97 ? 1861 HOH   A O   1 
HETATM 8786  O  O   . HOH   HA 5 .   ? 51.315 2.290   14.308  1.00 43.11 ? 1862 HOH   A O   1 
HETATM 8787  O  O   . HOH   HA 5 .   ? 31.975 1.156   29.222  1.00 56.92 ? 1863 HOH   A O   1 
HETATM 8788  O  O   . HOH   HA 5 .   ? 58.039 -6.447  11.113  1.00 38.19 ? 1864 HOH   A O   1 
HETATM 8789  O  O   . HOH   HA 5 .   ? 24.014 2.381   15.529  1.00 38.91 ? 1865 HOH   A O   1 
HETATM 8790  O  O   . HOH   HA 5 .   ? 40.241 5.594   25.403  1.00 41.60 ? 1866 HOH   A O   1 
HETATM 8791  O  O   . HOH   HA 5 .   ? 31.345 -23.928 5.539   1.00 33.27 ? 1867 HOH   A O   1 
HETATM 8792  O  O   . HOH   HA 5 .   ? 40.030 8.757   0.928   1.00 30.00 ? 1868 HOH   A O   1 
HETATM 8793  O  O   . HOH   HA 5 .   ? 36.314 -27.162 -1.917  1.00 48.33 ? 1869 HOH   A O   1 
HETATM 8794  O  O   . HOH   HA 5 .   ? 57.193 -6.758  -4.218  1.00 38.44 ? 1870 HOH   A O   1 
HETATM 8795  O  O   . HOH   HA 5 .   ? 52.902 -5.517  6.689   1.00 24.36 ? 1871 HOH   A O   1 
HETATM 8796  O  O   . HOH   HA 5 .   ? 23.626 -11.027 3.992   1.00 31.73 ? 1872 HOH   A O   1 
HETATM 8797  O  O   . HOH   HA 5 .   ? 32.688 -19.042 15.296  1.00 59.69 ? 1873 HOH   A O   1 
HETATM 8798  O  O   . HOH   HA 5 .   ? 51.036 -23.384 -9.135  1.00 49.13 ? 1874 HOH   A O   1 
HETATM 8799  O  O   . HOH   HA 5 .   ? 56.856 -19.227 -2.001  1.00 36.91 ? 1875 HOH   A O   1 
HETATM 8800  O  O   . HOH   HA 5 .   ? 39.036 -30.256 -4.524  1.00 50.76 ? 1876 HOH   A O   1 
HETATM 8801  O  O   . HOH   HA 5 .   ? 34.417 -12.829 -5.494  1.00 27.48 ? 1877 HOH   A O   1 
HETATM 8802  O  O   . HOH   HA 5 .   ? 28.007 2.313   -6.782  1.00 33.52 ? 1878 HOH   A O   1 
HETATM 8803  O  O   . HOH   HA 5 .   ? 35.649 -25.940 5.297   1.00 27.56 ? 1879 HOH   A O   1 
HETATM 8804  O  O   . HOH   HA 5 .   ? 40.843 9.272   23.030  1.00 50.14 ? 1880 HOH   A O   1 
HETATM 8805  O  O   . HOH   HA 5 .   ? 51.375 -8.669  -8.714  1.00 18.70 ? 1881 HOH   A O   1 
HETATM 8806  O  O   . HOH   HA 5 .   ? 34.347 -12.307 22.813  1.00 42.53 ? 1882 HOH   A O   1 
HETATM 8807  O  O   . HOH   HA 5 .   ? 52.318 -9.012  21.570  1.00 45.58 ? 1883 HOH   A O   1 
HETATM 8808  O  O   . HOH   HA 5 .   ? 52.140 -20.463 -7.776  1.00 29.73 ? 1884 HOH   A O   1 
HETATM 8809  O  O   . HOH   HA 5 .   ? 43.269 -12.908 -17.158 1.00 46.80 ? 1885 HOH   A O   1 
HETATM 8810  O  O   . HOH   HA 5 .   ? 54.527 -15.968 11.269  1.00 49.28 ? 1886 HOH   A O   1 
HETATM 8811  O  O   . HOH   HA 5 .   ? 58.474 6.994   -1.703  1.00 33.37 ? 1887 HOH   A O   1 
HETATM 8812  O  O   . HOH   HA 5 .   ? 21.823 -10.724 1.747   1.00 25.84 ? 1888 HOH   A O   1 
HETATM 8813  O  O   . HOH   HA 5 .   ? 28.376 -11.501 17.921  1.00 40.79 ? 1889 HOH   A O   1 
HETATM 8814  O  O   . HOH   HA 5 .   ? 37.036 8.521   1.876   1.00 30.00 ? 1890 HOH   A O   1 
HETATM 8815  O  O   . HOH   HA 5 .   ? 58.862 -5.515  19.271  1.00 46.88 ? 1891 HOH   A O   1 
HETATM 8816  O  O   . HOH   HA 5 .   ? 53.505 8.125   12.848  1.00 24.99 ? 1892 HOH   A O   1 
HETATM 8817  O  O   . HOH   HA 5 .   ? 45.862 -13.717 -19.987 1.00 49.31 ? 1893 HOH   A O   1 
HETATM 8818  O  O   . HOH   HA 5 .   ? 41.051 -10.802 -15.983 1.00 45.95 ? 1894 HOH   A O   1 
HETATM 8819  O  O   . HOH   HA 5 .   ? 57.058 -1.948  21.959  1.00 12.78 ? 1895 HOH   A O   1 
HETATM 8820  O  O   . HOH   HA 5 .   ? 50.957 -23.101 16.847  1.00 50.97 ? 1896 HOH   A O   1 
HETATM 8821  O  O   . HOH   HA 5 .   ? 47.618 4.297   19.546  1.00 25.97 ? 1897 HOH   A O   1 
HETATM 8822  O  O   . HOH   HA 5 .   ? 19.777 -3.183  -0.438  1.00 42.30 ? 1898 HOH   A O   1 
HETATM 8823  O  O   . HOH   HA 5 .   ? 60.123 -10.862 0.904   1.00 38.29 ? 1899 HOH   A O   1 
HETATM 8824  O  O   . HOH   HA 5 .   ? 43.965 0.268   28.267  1.00 43.57 ? 1900 HOH   A O   1 
HETATM 8825  O  O   . HOH   HA 5 .   ? 38.131 3.144   15.166  1.00 25.43 ? 1901 HOH   A O   1 
HETATM 8826  O  O   . HOH   HA 5 .   ? 47.347 -25.023 16.742  1.00 44.96 ? 1902 HOH   A O   1 
HETATM 8827  O  O   . HOH   HA 5 .   ? 33.286 -16.527 17.355  1.00 41.72 ? 1903 HOH   A O   1 
HETATM 8828  O  O   . HOH   HA 5 .   ? 54.896 -10.441 -4.706  1.00 24.58 ? 1904 HOH   A O   1 
HETATM 8829  O  O   . HOH   HA 5 .   ? 51.078 -7.889  -11.425 1.00 32.56 ? 1905 HOH   A O   1 
HETATM 8830  O  O   . HOH   HA 5 .   ? 36.981 -24.126 11.881  1.00 40.81 ? 1906 HOH   A O   1 
HETATM 8831  O  O   . HOH   HA 5 .   ? 46.822 16.070  12.306  1.00 44.01 ? 1907 HOH   A O   1 
HETATM 8832  O  O   . HOH   HA 5 .   ? 51.652 11.494  -2.153  1.00 29.70 ? 1908 HOH   A O   1 
HETATM 8833  O  O   . HOH   HA 5 .   ? 46.961 -30.258 11.570  1.00 47.27 ? 1909 HOH   A O   1 
HETATM 8834  O  O   . HOH   HA 5 .   ? 46.854 -6.791  24.515  1.00 43.13 ? 1910 HOH   A O   1 
HETATM 8835  O  O   . HOH   HA 5 .   ? 19.625 -16.679 1.414   1.00 34.58 ? 1911 HOH   A O   1 
HETATM 8836  O  O   . HOH   HA 5 .   ? 45.940 -9.989  -0.938  1.00 25.76 ? 1912 HOH   A O   1 
HETATM 8837  O  O   . HOH   HA 5 .   ? 53.540 4.489   13.280  1.00 37.36 ? 1913 HOH   A O   1 
HETATM 8838  O  O   . HOH   HA 5 .   ? 21.586 -7.511  -5.297  1.00 51.74 ? 1914 HOH   A O   1 
HETATM 8839  O  O   . HOH   HA 5 .   ? 57.432 -21.537 5.282   1.00 37.35 ? 1915 HOH   A O   1 
HETATM 8840  O  O   . HOH   HA 5 .   ? 44.910 -7.897  -2.509  1.00 18.14 ? 1916 HOH   A O   1 
HETATM 8841  O  O   . HOH   HA 5 .   ? 53.531 2.992   20.246  1.00 34.27 ? 1917 HOH   A O   1 
HETATM 8842  O  O   . HOH   HA 5 .   ? 24.969 -11.911 16.597  1.00 50.36 ? 1918 HOH   A O   1 
HETATM 8843  O  O   . HOH   HA 5 .   ? 51.602 0.097   -9.600  1.00 23.29 ? 1919 HOH   A O   1 
HETATM 8844  O  O   . HOH   HA 5 .   ? 54.650 -23.122 0.094   1.00 27.89 ? 1920 HOH   A O   1 
HETATM 8845  O  O   . HOH   HA 5 .   ? 38.650 1.866   32.962  1.00 45.50 ? 1921 HOH   A O   1 
HETATM 8846  O  O   . HOH   HA 5 .   ? 27.102 -15.462 13.792  1.00 37.04 ? 1922 HOH   A O   1 
HETATM 8847  O  O   . HOH   HA 5 .   ? 20.857 -0.650  -0.226  1.00 49.32 ? 1923 HOH   A O   1 
HETATM 8848  O  O   . HOH   HA 5 .   ? 48.902 -4.322  -16.608 1.00 22.28 ? 1924 HOH   A O   1 
HETATM 8849  O  O   . HOH   HA 5 .   ? 17.252 -6.269  4.748   1.00 42.55 ? 1925 HOH   A O   1 
HETATM 8850  O  O   . HOH   HA 5 .   ? 54.626 -20.778 -4.948  1.00 36.32 ? 1926 HOH   A O   1 
HETATM 8851  O  O   . HOH   HA 5 .   ? 48.841 7.156   7.440   1.00 20.57 ? 1927 HOH   A O   1 
HETATM 8852  O  O   . HOH   HA 5 .   ? 45.802 -22.817 -7.395  1.00 55.18 ? 1928 HOH   A O   1 
HETATM 8853  O  O   . HOH   HA 5 .   ? 61.454 -12.894 3.247   1.00 33.96 ? 1929 HOH   A O   1 
HETATM 8854  O  O   . HOH   HA 5 .   ? 29.041 -1.704  -5.664  1.00 29.72 ? 1930 HOH   A O   1 
HETATM 8855  O  O   . HOH   HA 5 .   ? 52.940 1.620   -16.437 1.00 22.74 ? 1931 HOH   A O   1 
HETATM 8856  O  O   . HOH   HA 5 .   ? 35.028 -20.123 16.816  1.00 50.61 ? 1932 HOH   A O   1 
HETATM 8857  O  O   . HOH   HA 5 .   ? 33.096 -8.676  -16.410 1.00 55.37 ? 1933 HOH   A O   1 
HETATM 8858  O  O   . HOH   HA 5 .   ? 41.902 -1.308  -8.874  1.00 16.57 ? 1934 HOH   A O   1 
HETATM 8859  O  O   . HOH   HA 5 .   ? 42.293 7.923   15.750  1.00 30.03 ? 1935 HOH   A O   1 
HETATM 8860  O  O   . HOH   HA 5 .   ? 32.908 3.654   12.565  1.00 43.16 ? 1936 HOH   A O   1 
HETATM 8861  O  O   . HOH   HA 5 .   ? 53.731 -9.980  -9.662  1.00 29.39 ? 1937 HOH   A O   1 
HETATM 8862  O  O   . HOH   HA 5 .   ? 54.030 -8.201  -14.216 1.00 49.10 ? 1938 HOH   A O   1 
HETATM 8863  O  O   . HOH   HA 5 .   ? 48.931 1.655   19.613  1.00 31.32 ? 1939 HOH   A O   1 
HETATM 8864  O  O   . HOH   HA 5 .   ? 34.305 -7.852  21.638  1.00 43.58 ? 1940 HOH   A O   1 
HETATM 8865  O  O   . HOH   HA 5 .   ? 46.324 -3.817  23.841  1.00 36.80 ? 1941 HOH   A O   1 
HETATM 8866  O  O   . HOH   HA 5 .   ? 57.330 -20.063 -10.563 1.00 57.36 ? 1942 HOH   A O   1 
HETATM 8867  O  O   . HOH   HA 5 .   ? 40.479 13.378  4.901   1.00 50.41 ? 1943 HOH   A O   1 
HETATM 8868  O  O   . HOH   HA 5 .   ? 47.063 0.613   27.699  1.00 57.89 ? 1944 HOH   A O   1 
HETATM 8869  O  O   . HOH   HA 5 .   ? 40.368 -27.145 -7.041  1.00 48.76 ? 1945 HOH   A O   1 
HETATM 8870  O  O   . HOH   HA 5 .   ? 41.181 -30.246 -3.998  1.00 48.31 ? 1946 HOH   A O   1 
HETATM 8871  O  O   . HOH   HA 5 .   ? 61.461 3.979   -8.648  1.00 51.49 ? 1947 HOH   A O   1 
HETATM 8872  O  O   . HOH   HA 5 .   ? 29.647 2.471   25.945  1.00 48.86 ? 1948 HOH   A O   1 
HETATM 8873  O  O   . HOH   HA 5 .   ? 49.580 -14.849 18.813  1.00 46.32 ? 1949 HOH   A O   1 
HETATM 8874  O  O   . HOH   HA 5 .   ? 24.349 6.186   -1.099  1.00 36.72 ? 1950 HOH   A O   1 
HETATM 8875  O  O   . HOH   HA 5 .   ? 44.268 -6.851  28.796  1.00 44.63 ? 1951 HOH   A O   1 
HETATM 8876  O  O   . HOH   HA 5 .   ? 51.802 -0.076  -12.152 1.00 26.53 ? 1952 HOH   A O   1 
HETATM 8877  O  O   . HOH   HA 5 .   ? 30.137 6.680   12.080  1.00 48.27 ? 1953 HOH   A O   1 
HETATM 8878  O  O   . HOH   HA 5 .   ? 34.354 10.424  -4.421  1.00 50.80 ? 1954 HOH   A O   1 
HETATM 8879  O  O   . HOH   HA 5 .   ? 57.735 -8.555  -10.585 1.00 32.07 ? 1955 HOH   A O   1 
HETATM 8880  O  O   . HOH   HA 5 .   ? 61.789 -1.166  -8.219  1.00 31.19 ? 1956 HOH   A O   1 
HETATM 8881  O  O   . HOH   HA 5 .   ? 29.913 -10.740 -9.080  1.00 46.62 ? 1957 HOH   A O   1 
HETATM 8882  O  O   . HOH   HA 5 .   ? 41.663 -21.452 15.526  1.00 31.80 ? 1958 HOH   A O   1 
HETATM 8883  O  O   . HOH   HA 5 .   ? 50.692 -27.331 -1.690  1.00 47.34 ? 1959 HOH   A O   1 
HETATM 8884  O  O   . HOH   HA 5 .   ? 57.787 -11.173 12.549  1.00 27.78 ? 1960 HOH   A O   1 
HETATM 8885  O  O   . HOH   HA 5 .   ? 35.259 -10.111 -5.924  1.00 23.72 ? 1961 HOH   A O   1 
HETATM 8886  O  O   . HOH   HA 5 .   ? 25.682 9.276   10.079  1.00 52.23 ? 1962 HOH   A O   1 
HETATM 8887  O  O   . HOH   HA 5 .   ? 58.857 4.441   -5.239  1.00 35.11 ? 1963 HOH   A O   1 
HETATM 8888  O  O   . HOH   HA 5 .   ? 21.081 0.237   1.804   1.00 42.28 ? 1964 HOH   A O   1 
HETATM 8889  O  O   . HOH   HA 5 .   ? 45.034 11.334  17.829  1.00 59.17 ? 1965 HOH   A O   1 
HETATM 8890  O  O   . HOH   HA 5 .   ? 36.160 -18.574 -14.774 1.00 33.02 ? 1966 HOH   A O   1 
HETATM 8891  O  O   . HOH   HA 5 .   ? 56.801 -25.556 6.110   1.00 61.20 ? 1967 HOH   A O   1 
HETATM 8892  O  O   . HOH   HA 5 .   ? 17.010 -5.556  2.005   1.00 54.87 ? 1968 HOH   A O   1 
HETATM 8893  O  O   . HOH   HA 5 .   ? 54.100 5.589   -0.177  1.00 39.19 ? 1969 HOH   A O   1 
HETATM 8894  O  O   . HOH   HA 5 .   ? 64.031 -11.298 -5.853  1.00 63.33 ? 1970 HOH   A O   1 
HETATM 8895  O  O   . HOH   HA 5 .   ? 46.568 -8.212  -11.782 1.00 30.50 ? 1971 HOH   A O   1 
HETATM 8896  O  O   . HOH   HA 5 .   ? 14.748 -7.491  1.218   1.00 48.55 ? 1972 HOH   A O   1 
HETATM 8897  O  O   . HOH   HA 5 .   ? 36.712 -29.636 7.253   1.00 50.23 ? 1973 HOH   A O   1 
HETATM 8898  O  O   . HOH   HA 5 .   ? 42.514 -7.192  -3.980  1.00 18.87 ? 1974 HOH   A O   1 
HETATM 8899  O  O   . HOH   HA 5 .   ? 45.965 -25.413 -10.863 1.00 52.92 ? 1975 HOH   A O   1 
HETATM 8900  O  O   . HOH   HA 5 .   ? 32.066 -23.532 -10.893 1.00 37.19 ? 1976 HOH   A O   1 
HETATM 8901  O  O   . HOH   HA 5 .   ? 37.169 -5.749  29.308  1.00 45.66 ? 1977 HOH   A O   1 
HETATM 8902  O  O   . HOH   HA 5 .   ? 58.762 5.118   -12.205 1.00 43.66 ? 1978 HOH   A O   1 
HETATM 8903  O  O   . HOH   HA 5 .   ? 58.361 -8.478  16.557  1.00 57.22 ? 1979 HOH   A O   1 
HETATM 8904  O  O   . HOH   HA 5 .   ? 47.857 -1.317  27.262  1.00 58.17 ? 1980 HOH   A O   1 
HETATM 8905  O  O   . HOH   HA 5 .   ? 26.438 -19.144 7.478   1.00 51.31 ? 1981 HOH   A O   1 
HETATM 8906  O  O   . HOH   HA 5 .   ? 53.173 4.044   0.608   1.00 33.50 ? 1982 HOH   A O   1 
HETATM 8907  O  O   . HOH   HA 5 .   ? 35.410 7.734   10.219  1.00 49.01 ? 1983 HOH   A O   1 
HETATM 8908  O  O   . HOH   HA 5 .   ? 27.166 5.281   -7.896  1.00 56.32 ? 1984 HOH   A O   1 
HETATM 8909  O  O   . HOH   HA 5 .   ? 45.006 9.286   -4.598  1.00 15.13 ? 1985 HOH   A O   1 
HETATM 8910  O  O   . HOH   HA 5 .   ? 31.400 -8.993  -5.297  1.00 44.16 ? 1986 HOH   A O   1 
HETATM 8911  O  O   . HOH   HA 5 .   ? 45.081 -28.678 2.761   1.00 48.53 ? 1987 HOH   A O   1 
HETATM 8912  O  O   . HOH   HA 5 .   ? 46.430 0.517   -12.170 1.00 15.42 ? 1988 HOH   A O   1 
HETATM 8913  O  O   . HOH   HA 5 .   ? 55.654 2.958   8.601   1.00 29.34 ? 1989 HOH   A O   1 
HETATM 8914  O  O   . HOH   HA 5 .   ? 22.984 -11.540 -5.190  1.00 43.40 ? 1990 HOH   A O   1 
HETATM 8915  O  O   . HOH   HA 5 .   ? 55.350 -4.704  7.084   1.00 27.01 ? 1991 HOH   A O   1 
HETATM 8916  O  O   . HOH   HA 5 .   ? 29.943 5.046   18.120  1.00 47.35 ? 1992 HOH   A O   1 
HETATM 8917  O  O   . HOH   HA 5 .   ? 56.007 -19.600 -16.984 1.00 58.75 ? 1993 HOH   A O   1 
HETATM 8918  O  O   . HOH   HA 5 .   ? 40.479 6.618   17.074  1.00 41.21 ? 1994 HOH   A O   1 
HETATM 8919  O  O   . HOH   HA 5 .   ? 42.415 -6.941  -1.185  1.00 41.04 ? 1995 HOH   A O   1 
HETATM 8920  O  O   . HOH   HA 5 .   ? 41.569 -12.104 22.465  1.00 37.14 ? 1996 HOH   A O   1 
HETATM 8921  O  O   . HOH   HA 5 .   ? 44.186 12.549  11.593  1.00 49.68 ? 1997 HOH   A O   1 
HETATM 8922  O  O   . HOH   HA 5 .   ? 15.070 -14.654 7.451   1.00 64.98 ? 1998 HOH   A O   1 
HETATM 8923  O  O   . HOH   HA 5 .   ? 52.850 -13.276 -22.943 1.00 42.39 ? 1999 HOH   A O   1 
HETATM 8924  O  O   . HOH   HA 5 .   ? 53.215 -22.387 -8.696  1.00 53.45 ? 2000 HOH   A O   1 
HETATM 8925  O  O   . HOH   HA 5 .   ? 53.426 10.576  -4.257  1.00 38.05 ? 2001 HOH   A O   1 
HETATM 8926  O  O   . HOH   HA 5 .   ? 43.791 10.870  10.428  1.00 47.84 ? 2002 HOH   A O   1 
HETATM 8927  O  O   . HOH   HA 5 .   ? 33.551 11.642  -1.679  1.00 54.90 ? 2003 HOH   A O   1 
HETATM 8928  O  O   . HOH   HA 5 .   ? 45.969 14.745  10.330  1.00 51.48 ? 2004 HOH   A O   1 
HETATM 8929  O  O   . HOH   HA 5 .   ? 54.312 -3.640  -14.042 1.00 29.34 ? 2005 HOH   A O   1 
HETATM 8930  O  O   . HOH   HA 5 .   ? 31.596 -3.995  24.901  1.00 45.60 ? 2006 HOH   A O   1 
HETATM 8931  O  O   . HOH   HA 5 .   ? 24.567 -13.477 -8.490  1.00 28.04 ? 2007 HOH   A O   1 
HETATM 8932  O  O   . HOH   HA 5 .   ? 28.128 8.061   -2.147  1.00 44.84 ? 2008 HOH   A O   1 
HETATM 8933  O  O   . HOH   HA 5 .   ? 19.774 -16.836 4.051   1.00 59.37 ? 2009 HOH   A O   1 
HETATM 8934  O  O   . HOH   HA 5 .   ? 43.162 0.320   -10.945 1.00 18.12 ? 2010 HOH   A O   1 
HETATM 8935  O  O   . HOH   HA 5 .   ? 44.334 -23.511 -14.479 1.00 54.72 ? 2011 HOH   A O   1 
HETATM 8936  O  O   . HOH   HA 5 .   ? 47.944 1.913   -11.896 1.00 24.38 ? 2012 HOH   A O   1 
HETATM 8937  O  O   . HOH   HA 5 .   ? 21.579 -25.721 -0.238  1.00 49.10 ? 2013 HOH   A O   1 
HETATM 8938  O  O   . HOH   HA 5 .   ? 33.635 -26.942 -2.399  1.00 53.00 ? 2014 HOH   A O   1 
HETATM 8939  O  O   . HOH   HA 5 .   ? 57.447 -6.598  -15.347 1.00 56.09 ? 2015 HOH   A O   1 
HETATM 8940  O  O   . HOH   HA 5 .   ? 48.363 12.295  0.668   1.00 46.85 ? 2016 HOH   A O   1 
HETATM 8941  O  O   . HOH   HA 5 .   ? 52.608 -17.458 12.225  1.00 41.85 ? 2017 HOH   A O   1 
HETATM 8942  O  O   . HOH   HA 5 .   ? 54.285 -1.016  -13.216 1.00 26.00 ? 2018 HOH   A O   1 
HETATM 8943  O  O   . HOH   HA 5 .   ? 24.527 -9.990  -4.361  1.00 44.31 ? 2019 HOH   A O   1 
HETATM 8944  O  O   . HOH   HA 5 .   ? 34.426 -20.806 -15.036 1.00 42.49 ? 2020 HOH   A O   1 
HETATM 8945  O  O   . HOH   HA 5 .   ? 46.572 12.482  -1.375  1.00 28.75 ? 2021 HOH   A O   1 
HETATM 8946  O  O   . HOH   HA 5 .   ? 62.559 -3.184  -7.241  1.00 48.52 ? 2022 HOH   A O   1 
HETATM 8947  O  O   . HOH   HA 5 .   ? 31.974 6.383   27.339  1.00 51.53 ? 2023 HOH   A O   1 
HETATM 8948  O  O   . HOH   HA 5 .   ? 53.533 -27.439 3.764   1.00 43.59 ? 2024 HOH   A O   1 
HETATM 8949  O  O   . HOH   HA 5 .   ? 39.095 4.344   17.152  1.00 40.27 ? 2025 HOH   A O   1 
HETATM 8950  O  O   . HOH   HA 5 .   ? 58.695 -19.389 9.773   1.00 49.72 ? 2026 HOH   A O   1 
HETATM 8951  O  O   . HOH   HA 5 .   ? 36.155 -16.856 -16.539 1.00 49.54 ? 2027 HOH   A O   1 
HETATM 8952  O  O   . HOH   HA 5 .   ? 24.018 -20.432 1.867   1.00 45.93 ? 2028 HOH   A O   1 
HETATM 8953  O  O   . HOH   HA 5 .   ? 42.508 -9.091  -16.687 1.00 50.95 ? 2029 HOH   A O   1 
HETATM 8954  O  O   . HOH   HA 5 .   ? 53.703 -26.607 11.534  1.00 48.18 ? 2030 HOH   A O   1 
HETATM 8955  O  O   . HOH   HA 5 .   ? 60.732 0.247   -10.694 1.00 33.77 ? 2031 HOH   A O   1 
HETATM 8956  O  O   . HOH   HA 5 .   ? 39.202 9.720   11.538  1.00 52.56 ? 2032 HOH   A O   1 
HETATM 8957  O  O   . HOH   HA 5 .   ? 36.202 -2.510  -7.496  1.00 30.04 ? 2033 HOH   A O   1 
HETATM 8958  O  O   . HOH   HA 5 .   ? 54.603 -7.872  -11.460 1.00 42.32 ? 2034 HOH   A O   1 
HETATM 8959  O  O   . HOH   HA 5 .   ? 44.573 11.634  -3.035  1.00 19.58 ? 2035 HOH   A O   1 
HETATM 8960  O  O   . HOH   HA 5 .   ? 21.959 5.511   -2.632  1.00 56.90 ? 2036 HOH   A O   1 
HETATM 8961  O  O   . HOH   HA 5 .   ? 56.525 -12.028 -5.251  1.00 45.87 ? 2037 HOH   A O   1 
HETATM 8962  O  O   . HOH   HA 5 .   ? 33.228 -4.861  -10.408 1.00 50.31 ? 2038 HOH   A O   1 
HETATM 8963  O  O   . HOH   HA 5 .   ? 14.569 -8.640  -1.354  1.00 55.67 ? 2039 HOH   A O   1 
HETATM 8964  O  O   . HOH   HA 5 .   ? 44.786 -4.923  -16.319 1.00 48.68 ? 2040 HOH   A O   1 
HETATM 8965  O  O   . HOH   HA 5 .   ? 57.445 10.353  -6.193  1.00 54.38 ? 2041 HOH   A O   1 
HETATM 8966  O  O   . HOH   HA 5 .   ? 20.374 -6.478  11.389  1.00 47.92 ? 2042 HOH   A O   1 
HETATM 8967  O  O   . HOH   HA 5 .   ? 47.388 -31.595 -5.206  1.00 47.01 ? 2043 HOH   A O   1 
HETATM 8968  O  O   . HOH   HA 5 .   ? 23.200 -21.536 -2.224  1.00 44.99 ? 2044 HOH   A O   1 
HETATM 8969  O  O   . HOH   HA 5 .   ? 40.823 -29.767 8.184   1.00 46.81 ? 2045 HOH   A O   1 
HETATM 8970  O  O   . HOH   HA 5 .   ? 37.339 -27.506 -7.394  1.00 41.55 ? 2046 HOH   A O   1 
HETATM 8971  O  O   . HOH   HA 5 .   ? 38.386 -7.685  28.868  1.00 50.99 ? 2047 HOH   A O   1 
HETATM 8972  O  O   . HOH   HA 5 .   ? 57.007 -6.339  22.894  1.00 51.77 ? 2048 HOH   A O   1 
HETATM 8973  O  O   . HOH   HA 5 .   ? 24.173 -0.853  16.678  1.00 45.56 ? 2049 HOH   A O   1 
HETATM 8974  O  O   . HOH   HA 5 .   ? 59.883 7.040   -6.053  1.00 55.11 ? 2050 HOH   A O   1 
HETATM 8975  O  O   . HOH   HA 5 .   ? 23.668 5.707   13.111  1.00 50.17 ? 2051 HOH   A O   1 
HETATM 8976  O  O   . HOH   HA 5 .   ? 51.086 13.450  0.459   1.00 59.78 ? 2052 HOH   A O   1 
HETATM 8977  O  O   . HOH   HA 5 .   ? 39.174 -21.623 15.480  1.00 41.02 ? 2053 HOH   A O   1 
HETATM 8978  O  O   . HOH   HA 5 .   ? 43.648 13.863  5.828   1.00 42.54 ? 2054 HOH   A O   1 
HETATM 8979  O  O   . HOH   HA 5 .   ? 41.610 9.754   14.219  1.00 38.05 ? 2055 HOH   A O   1 
HETATM 8980  O  O   . HOH   HA 5 .   ? 53.015 -26.652 -2.342  1.00 49.51 ? 2056 HOH   A O   1 
HETATM 8981  O  O   . HOH   HA 5 .   ? 32.457 -23.529 12.794  1.00 47.97 ? 2057 HOH   A O   1 
HETATM 8982  O  O   . HOH   HA 5 .   ? 38.214 10.543  -2.670  1.00 26.33 ? 2058 HOH   A O   1 
HETATM 8983  O  O   . HOH   HA 5 .   ? 55.310 -11.062 -7.635  1.00 47.03 ? 2059 HOH   A O   1 
HETATM 8984  O  O   . HOH   HA 5 .   ? 31.787 -1.789  -6.732  1.00 48.61 ? 2060 HOH   A O   1 
HETATM 8985  O  O   . HOH   HA 5 .   ? 29.577 -16.184 15.123  1.00 47.30 ? 2061 HOH   A O   1 
HETATM 8986  O  O   . HOH   HA 5 .   ? 34.467 -22.396 14.911  1.00 49.27 ? 2062 HOH   A O   1 
HETATM 8987  O  O   . HOH   HA 5 .   ? 35.083 4.566   18.284  1.00 43.41 ? 2063 HOH   A O   1 
HETATM 8988  O  O   . HOH   HA 5 .   ? 28.394 -4.183  -5.312  1.00 51.56 ? 2064 HOH   A O   1 
HETATM 8989  O  O   . HOH   HA 5 .   ? 53.316 11.382  15.693  1.00 56.36 ? 2065 HOH   A O   1 
HETATM 8990  O  O   . HOH   HA 5 .   ? 39.730 -16.554 -17.435 1.00 44.94 ? 2066 HOH   A O   1 
HETATM 8991  O  O   . HOH   HA 5 .   ? 48.481 -10.606 20.680  1.00 37.45 ? 2067 HOH   A O   1 
HETATM 8992  O  O   . HOH   HA 5 .   ? 34.098 -24.835 11.673  1.00 50.37 ? 2068 HOH   A O   1 
HETATM 8993  O  O   . HOH   HA 5 .   ? 44.900 -11.027 -17.237 1.00 48.39 ? 2069 HOH   A O   1 
HETATM 8994  O  O   . HOH   HA 5 .   ? 56.766 -13.564 -9.675  1.00 38.59 ? 2070 HOH   A O   1 
HETATM 8995  O  O   . HOH   HA 5 .   ? 45.324 -14.981 21.606  1.00 60.05 ? 2071 HOH   A O   1 
HETATM 8996  O  O   . HOH   HA 5 .   ? 15.492 -17.844 4.569   1.00 53.50 ? 2072 HOH   A O   1 
HETATM 8997  O  O   . HOH   HA 5 .   ? 45.830 -5.218  27.714  1.00 48.74 ? 2073 HOH   A O   1 
HETATM 8998  O  O   . HOH   HA 5 .   ? 32.798 7.385   15.430  1.00 59.00 ? 2074 HOH   A O   1 
HETATM 8999  O  O   . HOH   HA 5 .   ? 23.371 -23.658 -4.812  1.00 30.00 ? 2075 HOH   A O   1 
HETATM 9000  O  O   . HOH   HA 5 .   ? 59.578 -21.354 6.694   1.00 53.13 ? 2076 HOH   A O   1 
HETATM 9001  O  O   . HOH   HA 5 .   ? 22.308 3.688   9.095   1.00 42.75 ? 2077 HOH   A O   1 
HETATM 9002  O  O   . HOH   HA 5 .   ? 48.358 -6.400  -14.759 1.00 40.25 ? 2078 HOH   A O   1 
HETATM 9003  O  O   . HOH   HA 5 .   ? 56.553 1.464   18.017  1.00 44.98 ? 2079 HOH   A O   1 
HETATM 9004  O  O   . HOH   HA 5 .   ? 41.924 9.719   11.837  1.00 49.99 ? 2080 HOH   A O   1 
HETATM 9005  O  O   . HOH   HA 5 .   ? 57.810 -22.439 3.195   1.00 49.85 ? 2081 HOH   A O   1 
HETATM 9006  O  O   . HOH   HA 5 .   ? 24.076 5.641   10.169  1.00 41.87 ? 2082 HOH   A O   1 
HETATM 9007  O  O   . HOH   HA 5 .   ? 61.409 -17.682 0.965   1.00 54.24 ? 2083 HOH   A O   1 
HETATM 9008  O  O   . HOH   HA 5 .   ? 39.807 -20.114 -17.610 1.00 55.68 ? 2084 HOH   A O   1 
HETATM 9009  O  O   . HOH   HA 5 .   ? 49.224 -9.056  22.464  1.00 44.66 ? 2085 HOH   A O   1 
HETATM 9010  O  O   . HOH   HA 5 .   ? 36.665 5.026   14.225  1.00 37.87 ? 2086 HOH   A O   1 
HETATM 9011  O  O   . HOH   HA 5 .   ? 36.073 -14.387 -17.777 1.00 44.62 ? 2087 HOH   A O   1 
HETATM 9012  O  O   . HOH   HA 5 .   ? 38.918 -26.670 -12.731 1.00 58.11 ? 2088 HOH   A O   1 
HETATM 9013  O  O   . HOH   HA 5 .   ? 43.309 -13.713 23.100  1.00 42.77 ? 2089 HOH   A O   1 
HETATM 9014  O  O   . HOH   HA 5 .   ? 52.518 2.874   17.537  1.00 52.19 ? 2090 HOH   A O   1 
HETATM 9015  O  O   . HOH   HA 5 .   ? 20.468 4.731   7.158   1.00 50.66 ? 2091 HOH   A O   1 
HETATM 9016  O  O   . HOH   HA 5 .   ? 32.899 -24.482 9.486   1.00 50.27 ? 2092 HOH   A O   1 
HETATM 9017  O  O   . HOH   HA 5 .   ? 59.136 -15.211 -4.006  1.00 50.85 ? 2093 HOH   A O   1 
HETATM 9018  O  O   . HOH   HA 5 .   ? 26.331 7.993   -1.603  1.00 39.99 ? 2094 HOH   A O   1 
HETATM 9019  O  O   . HOH   HA 5 .   ? 55.681 -25.379 1.521   1.00 48.06 ? 2095 HOH   A O   1 
HETATM 9020  O  O   . HOH   HA 5 .   ? 29.539 8.396   -4.477  1.00 44.57 ? 2096 HOH   A O   1 
HETATM 9021  O  O   . HOH   HA 5 .   ? 52.283 -12.713 -24.909 1.00 51.98 ? 2097 HOH   A O   1 
HETATM 9022  O  O   . HOH   HA 5 .   ? 53.187 -10.580 23.292  1.00 51.78 ? 2098 HOH   A O   1 
HETATM 9023  O  O   . HOH   HA 5 .   ? 58.789 -7.026  21.721  1.00 53.83 ? 2099 HOH   A O   1 
HETATM 9024  O  O   . HOH   HA 5 .   ? 42.540 12.993  1.018   1.00 30.45 ? 2100 HOH   A O   1 
HETATM 9025  O  O   . HOH   HA 5 .   ? 21.473 8.331   6.318   1.00 54.35 ? 2101 HOH   A O   1 
HETATM 9026  O  O   . HOH   HA 5 .   ? 48.451 14.331  -2.697  1.00 34.07 ? 2102 HOH   A O   1 
HETATM 9027  O  O   . HOH   HA 5 .   ? 30.064 -18.913 15.699  1.00 56.09 ? 2103 HOH   A O   1 
HETATM 9028  O  O   . HOH   HA 5 .   ? 45.393 12.991  1.794   1.00 33.30 ? 2104 HOH   A O   1 
HETATM 9029  O  O   . HOH   HA 5 .   ? 46.712 9.762   30.536  1.00 49.09 ? 2105 HOH   A O   1 
HETATM 9030  O  O   . HOH   HA 5 .   ? 51.386 13.652  -3.730  1.00 39.54 ? 2106 HOH   A O   1 
HETATM 9031  O  O   . HOH   HA 5 .   ? 37.487 -24.816 14.263  1.00 57.25 ? 2107 HOH   A O   1 
HETATM 9032  O  O   . HOH   HA 5 .   ? 32.064 -6.480  24.979  1.00 47.98 ? 2108 HOH   A O   1 
HETATM 9033  O  O   . HOH   HA 5 .   ? 48.417 -17.260 19.801  1.00 52.87 ? 2109 HOH   A O   1 
HETATM 9034  O  O   . HOH   HA 5 .   ? 37.666 7.230   15.177  1.00 41.24 ? 2110 HOH   A O   1 
HETATM 9035  O  O   . HOH   HA 5 .   ? 56.746 -18.723 -4.645  1.00 51.48 ? 2111 HOH   A O   1 
HETATM 9036  O  O   . HOH   HA 5 .   ? 40.498 10.316  -1.302  1.00 34.45 ? 2112 HOH   A O   1 
HETATM 9037  O  O   . HOH   HA 5 .   ? 36.942 -31.447 11.999  1.00 53.07 ? 2113 HOH   A O   1 
HETATM 9038  O  O   . HOH   IA 5 .   ? 14.773 -27.443 5.271   1.00 49.10 ? 401  HOH   B O   1 
HETATM 9039  O  O   . HOH   IA 5 .   ? 34.821 -54.131 48.991  1.00 18.73 ? 402  HOH   B O   1 
HETATM 9040  O  O   . HOH   IA 5 .   ? 23.436 -69.138 14.365  1.00 65.26 ? 403  HOH   B O   1 
HETATM 9041  O  O   . HOH   IA 5 .   ? 19.728 -32.277 34.354  1.00 49.90 ? 404  HOH   B O   1 
HETATM 9042  O  O   . HOH   IA 5 .   ? 32.392 -61.992 10.298  1.00 26.52 ? 405  HOH   B O   1 
HETATM 9043  O  O   . HOH   IA 5 .   ? 37.324 -67.957 23.451  1.00 39.39 ? 406  HOH   B O   1 
HETATM 9044  O  O   . HOH   IA 5 .   ? 31.673 -39.903 46.301  1.00 49.29 ? 407  HOH   B O   1 
HETATM 9045  O  O   . HOH   IA 5 .   ? 8.898  -31.582 27.541  1.00 50.27 ? 408  HOH   B O   1 
HETATM 9046  O  O   . HOH   IA 5 .   ? 16.445 -31.972 9.096   1.00 50.68 ? 409  HOH   B O   1 
HETATM 9047  O  O   . HOH   IA 5 .   ? 30.364 -44.214 8.572   1.00 22.57 ? 410  HOH   B O   1 
HETATM 9048  O  O   . HOH   IA 5 .   ? 47.959 -43.048 17.465  1.00 40.76 ? 411  HOH   B O   1 
HETATM 9049  O  O   . HOH   IA 5 .   ? 22.322 -49.762 39.475  1.00 39.77 ? 412  HOH   B O   1 
HETATM 9050  O  O   . HOH   IA 5 .   ? 32.754 -66.852 27.654  1.00 49.32 ? 413  HOH   B O   1 
HETATM 9051  O  O   . HOH   IA 5 .   ? 30.660 -54.593 44.061  1.00 39.40 ? 414  HOH   B O   1 
HETATM 9052  O  O   . HOH   IA 5 .   ? 23.265 -40.865 44.088  1.00 39.94 ? 415  HOH   B O   1 
HETATM 9053  O  O   . HOH   IA 5 .   ? 7.985  -39.114 26.067  1.00 37.72 ? 416  HOH   B O   1 
HETATM 9054  O  O   . HOH   IA 5 .   ? 34.349 -32.804 37.777  1.00 41.31 ? 417  HOH   B O   1 
HETATM 9055  O  O   . HOH   IA 5 .   ? 23.904 -66.703 15.325  1.00 27.43 ? 418  HOH   B O   1 
HETATM 9056  O  O   . HOH   IA 5 .   ? 27.895 -60.336 5.881   1.00 39.23 ? 419  HOH   B O   1 
HETATM 9057  O  O   . HOH   IA 5 .   ? 23.112 -26.479 28.200  1.00 52.63 ? 420  HOH   B O   1 
HETATM 9058  O  O   . HOH   IA 5 .   ? 13.317 -30.809 26.146  1.00 31.15 ? 421  HOH   B O   1 
HETATM 9059  O  O   . HOH   IA 5 .   ? 23.366 -62.997 16.089  1.00 33.85 ? 422  HOH   B O   1 
HETATM 9060  O  O   . HOH   IA 5 .   ? 37.157 -41.465 43.196  1.00 53.90 ? 423  HOH   B O   1 
HETATM 9061  O  O   . HOH   IA 5 .   ? 17.424 -44.538 47.140  1.00 30.97 ? 424  HOH   B O   1 
HETATM 9062  O  O   . HOH   IA 5 .   ? 47.175 -34.884 30.733  1.00 50.32 ? 425  HOH   B O   1 
HETATM 9063  O  O   . HOH   IA 5 .   ? 5.377  -48.990 23.081  1.00 51.96 ? 426  HOH   B O   1 
HETATM 9064  O  O   . HOH   IA 5 .   ? 24.043 -46.550 46.743  1.00 24.81 ? 427  HOH   B O   1 
HETATM 9065  O  O   . HOH   IA 5 .   ? 33.742 -49.790 28.484  1.00 27.86 ? 428  HOH   B O   1 
HETATM 9066  O  O   . HOH   IA 5 .   ? 24.239 -26.245 21.749  1.00 42.47 ? 429  HOH   B O   1 
HETATM 9067  O  O   . HOH   IA 5 .   ? 10.737 -34.668 34.509  1.00 52.69 ? 430  HOH   B O   1 
HETATM 9068  O  O   . HOH   IA 5 .   ? 13.330 -34.049 37.282  1.00 42.40 ? 431  HOH   B O   1 
HETATM 9069  O  O   . HOH   IA 5 .   ? 28.198 -52.213 19.348  1.00 16.20 ? 432  HOH   B O   1 
HETATM 9070  O  O   . HOH   IA 5 .   ? 18.828 -50.583 8.344   1.00 38.59 ? 433  HOH   B O   1 
HETATM 9071  O  O   . HOH   IA 5 .   ? 31.322 -60.782 39.123  1.00 26.10 ? 434  HOH   B O   1 
HETATM 9072  O  O   . HOH   IA 5 .   ? 19.678 -27.949 23.081  1.00 28.49 ? 435  HOH   B O   1 
HETATM 9073  O  O   . HOH   IA 5 .   ? 19.273 -37.060 49.420  1.00 46.51 ? 436  HOH   B O   1 
HETATM 9074  O  O   . HOH   IA 5 .   ? 46.741 -46.735 21.743  1.00 28.12 ? 437  HOH   B O   1 
HETATM 9075  O  O   . HOH   IA 5 .   ? 19.287 -55.003 31.996  1.00 37.96 ? 438  HOH   B O   1 
HETATM 9076  O  O   . HOH   IA 5 .   ? 26.524 -40.152 5.492   1.00 35.82 ? 439  HOH   B O   1 
HETATM 9077  O  O   . HOH   IA 5 .   ? 36.749 -34.106 30.266  1.00 41.78 ? 440  HOH   B O   1 
HETATM 9078  O  O   . HOH   IA 5 .   ? 13.990 -40.132 19.883  1.00 31.39 ? 441  HOH   B O   1 
HETATM 9079  O  O   . HOH   IA 5 .   ? 13.384 -32.926 29.730  1.00 29.06 ? 442  HOH   B O   1 
HETATM 9080  O  O   . HOH   IA 5 .   ? 48.855 -41.859 29.636  1.00 39.86 ? 443  HOH   B O   1 
HETATM 9081  O  O   . HOH   IA 5 .   ? 22.906 -52.023 41.836  1.00 48.21 ? 444  HOH   B O   1 
HETATM 9082  O  O   . HOH   IA 5 .   ? 20.629 -51.410 9.663   1.00 23.98 ? 445  HOH   B O   1 
HETATM 9083  O  O   . HOH   IA 5 .   ? 11.127 -38.321 37.628  1.00 35.87 ? 446  HOH   B O   1 
HETATM 9084  O  O   . HOH   IA 5 .   ? 39.980 -57.161 15.615  1.00 34.37 ? 447  HOH   B O   1 
HETATM 9085  O  O   . HOH   IA 5 .   ? 47.038 -43.530 38.507  1.00 38.11 ? 448  HOH   B O   1 
HETATM 9086  O  O   . HOH   IA 5 .   ? 30.229 -44.073 45.028  1.00 25.90 ? 449  HOH   B O   1 
HETATM 9087  O  O   . HOH   IA 5 .   ? 4.470  -42.984 34.034  1.00 54.44 ? 450  HOH   B O   1 
HETATM 9088  O  O   . HOH   IA 5 .   ? 31.738 -56.428 42.256  1.00 31.26 ? 451  HOH   B O   1 
HETATM 9089  O  O   . HOH   IA 5 .   ? 25.041 -43.876 8.295   1.00 19.60 ? 452  HOH   B O   1 
HETATM 9090  O  O   . HOH   IA 5 .   ? 36.062 -64.710 33.858  1.00 26.99 ? 453  HOH   B O   1 
HETATM 9091  O  O   . HOH   IA 5 .   ? 11.035 -56.447 22.570  1.00 21.73 ? 454  HOH   B O   1 
HETATM 9092  O  O   . HOH   IA 5 .   ? 20.415 -70.872 16.764  1.00 20.62 ? 455  HOH   B O   1 
HETATM 9093  O  O   . HOH   IA 5 .   ? 20.346 -56.142 27.304  1.00 20.43 ? 456  HOH   B O   1 
HETATM 9094  O  O   . HOH   IA 5 .   ? 21.142 -68.452 17.716  1.00 18.10 ? 457  HOH   B O   1 
HETATM 9095  O  O   . HOH   IA 5 .   ? 27.251 -60.856 28.234  1.00 16.30 ? 458  HOH   B O   1 
HETATM 9096  O  O   . HOH   IA 5 .   ? 28.271 -61.272 39.843  1.00 47.61 ? 459  HOH   B O   1 
HETATM 9097  O  O   . HOH   IA 5 .   ? 29.749 -63.656 23.304  1.00 26.31 ? 460  HOH   B O   1 
HETATM 9098  O  O   . HOH   IA 5 .   ? 48.691 -39.873 23.173  1.00 31.71 ? 461  HOH   B O   1 
HETATM 9099  O  O   . HOH   IA 5 .   ? 9.765  -51.006 38.022  1.00 50.98 ? 462  HOH   B O   1 
HETATM 9100  O  O   . HOH   IA 5 .   ? 36.337 -34.974 39.753  1.00 51.03 ? 463  HOH   B O   1 
HETATM 9101  O  O   . HOH   IA 5 .   ? 29.717 -24.381 23.413  1.00 48.23 ? 464  HOH   B O   1 
HETATM 9102  O  O   . HOH   IA 5 .   ? 13.041 -46.701 4.661   1.00 43.95 ? 465  HOH   B O   1 
HETATM 9103  O  O   . HOH   IA 5 .   ? 40.811 -48.478 10.253  1.00 29.41 ? 466  HOH   B O   1 
HETATM 9104  O  O   . HOH   IA 5 .   ? 11.871 -27.550 14.404  1.00 57.24 ? 467  HOH   B O   1 
HETATM 9105  O  O   . HOH   IA 5 .   ? 11.894 -37.854 25.346  1.00 23.15 ? 468  HOH   B O   1 
HETATM 9106  O  O   . HOH   IA 5 .   ? 23.556 -34.863 40.221  1.00 37.46 ? 469  HOH   B O   1 
HETATM 9107  O  O   . HOH   IA 5 .   ? 27.977 -66.717 11.706  1.00 33.01 ? 470  HOH   B O   1 
HETATM 9108  O  O   . HOH   IA 5 .   ? 12.143 -50.514 12.409  1.00 22.26 ? 471  HOH   B O   1 
HETATM 9109  O  O   . HOH   IA 5 .   ? 18.366 -36.796 6.717   1.00 32.10 ? 472  HOH   B O   1 
HETATM 9110  O  O   . HOH   IA 5 .   ? 30.153 -30.584 22.217  1.00 26.27 ? 473  HOH   B O   1 
HETATM 9111  O  O   . HOH   IA 5 .   ? 38.535 -67.847 20.199  1.00 43.59 ? 474  HOH   B O   1 
HETATM 9112  O  O   . HOH   IA 5 .   ? 17.343 -24.716 10.891  1.00 38.86 ? 475  HOH   B O   1 
HETATM 9113  O  O   . HOH   IA 5 .   ? 19.640 -50.378 39.438  1.00 49.96 ? 476  HOH   B O   1 
HETATM 9114  O  O   . HOH   IA 5 .   ? 44.719 -57.362 31.992  1.00 43.87 ? 477  HOH   B O   1 
HETATM 9115  O  O   . HOH   IA 5 .   ? 13.588 -44.858 8.699   1.00 27.18 ? 478  HOH   B O   1 
HETATM 9116  O  O   . HOH   IA 5 .   ? 25.255 -56.250 26.464  1.00 18.36 ? 479  HOH   B O   1 
HETATM 9117  O  O   . HOH   IA 5 .   ? 18.396 -41.702 3.911   1.00 38.23 ? 480  HOH   B O   1 
HETATM 9118  O  O   . HOH   IA 5 .   ? 30.787 -35.007 4.522   1.00 33.87 ? 481  HOH   B O   1 
HETATM 9119  O  O   . HOH   IA 5 .   ? 17.420 -57.830 29.749  1.00 32.43 ? 482  HOH   B O   1 
HETATM 9120  O  O   . HOH   IA 5 .   ? 47.735 -41.059 32.389  1.00 50.77 ? 483  HOH   B O   1 
HETATM 9121  O  O   . HOH   IA 5 .   ? 12.671 -35.509 20.646  1.00 44.92 ? 484  HOH   B O   1 
HETATM 9122  O  O   . HOH   IA 5 .   ? 20.949 -41.880 45.217  1.00 27.32 ? 485  HOH   B O   1 
HETATM 9123  O  O   . HOH   IA 5 .   ? 11.123 -50.768 16.351  1.00 23.08 ? 486  HOH   B O   1 
HETATM 9124  O  O   . HOH   IA 5 .   ? 7.795  -51.087 29.073  1.00 28.74 ? 487  HOH   B O   1 
HETATM 9125  O  O   . HOH   IA 5 .   ? 29.586 -37.803 5.502   1.00 28.17 ? 488  HOH   B O   1 
HETATM 9126  O  O   . HOH   IA 5 .   ? 13.301 -55.392 28.926  1.00 22.23 ? 489  HOH   B O   1 
HETATM 9127  O  O   . HOH   IA 5 .   ? 35.182 -47.914 14.441  1.00 24.93 ? 490  HOH   B O   1 
HETATM 9128  O  O   . HOH   IA 5 .   ? 34.792 -47.485 48.531  1.00 18.76 ? 491  HOH   B O   1 
HETATM 9129  O  O   . HOH   IA 5 .   ? 19.769 -33.521 39.596  1.00 40.13 ? 492  HOH   B O   1 
HETATM 9130  O  O   . HOH   IA 5 .   ? 13.071 -52.389 8.006   1.00 49.83 ? 493  HOH   B O   1 
HETATM 9131  O  O   . HOH   IA 5 .   ? 30.939 -28.727 8.355   1.00 47.13 ? 494  HOH   B O   1 
HETATM 9132  O  O   . HOH   IA 5 .   ? 26.912 -45.760 7.031   1.00 28.69 ? 495  HOH   B O   1 
HETATM 9133  O  O   . HOH   IA 5 .   ? 23.917 -42.078 40.755  1.00 25.84 ? 496  HOH   B O   1 
HETATM 9134  O  O   . HOH   IA 5 .   ? 41.046 -47.707 19.282  1.00 22.25 ? 497  HOH   B O   1 
HETATM 9135  O  O   . HOH   IA 5 .   ? 26.891 -52.095 27.953  1.00 19.04 ? 498  HOH   B O   1 
HETATM 9136  O  O   . HOH   IA 5 .   ? 31.543 -59.801 22.796  1.00 16.65 ? 499  HOH   B O   1 
HETATM 9137  O  O   . HOH   IA 5 .   ? 23.860 -26.122 12.624  1.00 40.45 ? 500  HOH   B O   1 
HETATM 9138  O  O   . HOH   IA 5 .   ? 24.674 -51.680 33.909  1.00 26.82 ? 501  HOH   B O   1 
HETATM 9139  O  O   . HOH   IA 5 .   ? 36.436 -38.448 36.204  1.00 32.49 ? 502  HOH   B O   1 
HETATM 9140  O  O   . HOH   IA 5 .   ? 29.554 -66.955 20.725  1.00 30.31 ? 503  HOH   B O   1 
HETATM 9141  O  O   . HOH   IA 5 .   ? 16.840 -49.411 36.547  1.00 23.83 ? 504  HOH   B O   1 
HETATM 9142  O  O   . HOH   IA 5 .   ? 8.933  -38.647 28.538  1.00 30.49 ? 505  HOH   B O   1 
HETATM 9143  O  O   . HOH   IA 5 .   ? 42.184 -64.997 29.071  1.00 32.65 ? 506  HOH   B O   1 
HETATM 9144  O  O   . HOH   IA 5 .   ? 17.287 -25.070 19.963  1.00 29.64 ? 507  HOH   B O   1 
HETATM 9145  O  O   . HOH   IA 5 .   ? 19.844 -47.112 46.850  1.00 28.91 ? 508  HOH   B O   1 
HETATM 9146  O  O   . HOH   IA 5 .   ? 40.007 -60.225 19.465  1.00 31.21 ? 509  HOH   B O   1 
HETATM 9147  O  O   . HOH   IA 5 .   ? 23.138 -52.346 7.168   1.00 35.84 ? 510  HOH   B O   1 
HETATM 9148  O  O   . HOH   IA 5 .   ? 11.873 -30.629 15.178  1.00 57.28 ? 511  HOH   B O   1 
HETATM 9149  O  O   . HOH   IA 5 .   ? 21.651 -27.201 24.947  1.00 32.08 ? 512  HOH   B O   1 
HETATM 9150  O  O   . HOH   IA 5 .   ? 10.521 -38.790 32.992  1.00 26.30 ? 513  HOH   B O   1 
HETATM 9151  O  O   . HOH   IA 5 .   ? 23.642 -57.851 11.256  1.00 19.77 ? 514  HOH   B O   1 
HETATM 9152  O  O   . HOH   IA 5 .   ? 22.231 -56.002 38.434  1.00 36.68 ? 515  HOH   B O   1 
HETATM 9153  O  O   . HOH   IA 5 .   ? 27.383 -54.259 37.647  1.00 36.21 ? 516  HOH   B O   1 
HETATM 9154  O  O   . HOH   IA 5 .   ? 14.040 -42.243 23.663  1.00 26.60 ? 517  HOH   B O   1 
HETATM 9155  O  O   . HOH   IA 5 .   ? 16.888 -54.648 30.184  1.00 28.88 ? 518  HOH   B O   1 
HETATM 9156  O  O   . HOH   IA 5 .   ? 32.246 -35.979 21.492  1.00 22.35 ? 519  HOH   B O   1 
HETATM 9157  O  O   . HOH   IA 5 .   ? 14.495 -21.361 19.384  1.00 55.74 ? 520  HOH   B O   1 
HETATM 9158  O  O   . HOH   IA 5 .   ? 43.125 -34.730 27.991  1.00 41.03 ? 521  HOH   B O   1 
HETATM 9159  O  O   . HOH   IA 5 .   ? 31.461 -60.737 12.459  1.00 27.53 ? 522  HOH   B O   1 
HETATM 9160  O  O   . HOH   IA 5 .   ? 30.647 -26.760 18.455  1.00 57.41 ? 523  HOH   B O   1 
HETATM 9161  O  O   . HOH   IA 5 .   ? 38.037 -57.931 40.388  1.00 39.54 ? 524  HOH   B O   1 
HETATM 9162  O  O   . HOH   IA 5 .   ? 22.582 -55.844 25.540  1.00 20.12 ? 525  HOH   B O   1 
HETATM 9163  O  O   . HOH   IA 5 .   ? 33.880 -32.795 10.196  1.00 45.38 ? 526  HOH   B O   1 
HETATM 9164  O  O   . HOH   IA 5 .   ? 24.280 -37.857 8.296   1.00 27.20 ? 527  HOH   B O   1 
HETATM 9165  O  O   . HOH   IA 5 .   ? 32.784 -64.311 25.819  1.00 27.60 ? 528  HOH   B O   1 
HETATM 9166  O  O   . HOH   IA 5 .   ? 18.948 -32.740 9.146   1.00 50.09 ? 529  HOH   B O   1 
HETATM 9167  O  O   . HOH   IA 5 .   ? 12.824 -34.689 12.588  1.00 57.77 ? 530  HOH   B O   1 
HETATM 9168  O  O   . HOH   IA 5 .   ? 17.390 -39.762 49.978  1.00 34.03 ? 531  HOH   B O   1 
HETATM 9169  O  O   . HOH   IA 5 .   ? 47.386 -51.622 18.019  1.00 51.10 ? 532  HOH   B O   1 
HETATM 9170  O  O   . HOH   IA 5 .   ? 25.163 -54.511 36.152  1.00 28.22 ? 533  HOH   B O   1 
HETATM 9171  O  O   . HOH   IA 5 .   ? 47.327 -52.796 24.584  1.00 33.09 ? 534  HOH   B O   1 
HETATM 9172  O  O   . HOH   IA 5 .   ? 40.759 -63.943 34.542  1.00 38.32 ? 535  HOH   B O   1 
HETATM 9173  O  O   . HOH   IA 5 .   ? 30.321 -41.516 42.248  1.00 26.00 ? 536  HOH   B O   1 
HETATM 9174  O  O   . HOH   IA 5 .   ? 9.933  -32.302 29.953  1.00 39.33 ? 537  HOH   B O   1 
HETATM 9175  O  O   . HOH   IA 5 .   ? 23.848 -68.229 17.779  1.00 23.64 ? 538  HOH   B O   1 
HETATM 9176  O  O   . HOH   IA 5 .   ? 35.171 -35.317 10.663  1.00 37.55 ? 539  HOH   B O   1 
HETATM 9177  O  O   . HOH   IA 5 .   ? 15.724 -57.818 18.708  1.00 16.84 ? 540  HOH   B O   1 
HETATM 9178  O  O   . HOH   IA 5 .   ? 12.641 -45.078 41.316  1.00 43.16 ? 541  HOH   B O   1 
HETATM 9179  O  O   . HOH   IA 5 .   ? 43.875 -54.607 13.635  1.00 43.48 ? 542  HOH   B O   1 
HETATM 9180  O  O   . HOH   IA 5 .   ? 37.485 -31.811 25.426  1.00 40.21 ? 543  HOH   B O   1 
HETATM 9181  O  O   . HOH   IA 5 .   ? 41.576 -59.661 36.072  1.00 28.53 ? 544  HOH   B O   1 
HETATM 9182  O  O   . HOH   IA 5 .   ? 33.885 -65.064 23.543  1.00 41.48 ? 545  HOH   B O   1 
HETATM 9183  O  O   . HOH   IA 5 .   ? 16.302 -27.152 29.886  1.00 44.52 ? 546  HOH   B O   1 
HETATM 9184  O  O   . HOH   IA 5 .   ? 44.230 -52.884 31.301  1.00 34.32 ? 547  HOH   B O   1 
HETATM 9185  O  O   . HOH   IA 5 .   ? 12.396 -31.210 10.605  1.00 52.04 ? 548  HOH   B O   1 
HETATM 9186  O  O   . HOH   IA 5 .   ? 19.568 -25.932 21.175  1.00 30.66 ? 549  HOH   B O   1 
HETATM 9187  O  O   . HOH   IA 5 .   ? 50.135 -41.833 19.537  1.00 52.48 ? 550  HOH   B O   1 
HETATM 9188  O  O   . HOH   IA 5 .   ? 36.353 -39.314 39.842  1.00 32.79 ? 551  HOH   B O   1 
HETATM 9189  O  O   . HOH   IA 5 .   ? 12.019 -54.388 34.310  1.00 31.44 ? 552  HOH   B O   1 
HETATM 9190  O  O   . HOH   IA 5 .   ? 32.753 -65.595 16.647  1.00 24.73 ? 553  HOH   B O   1 
HETATM 9191  O  O   . HOH   IA 5 .   ? 15.257 -28.182 12.029  1.00 36.38 ? 554  HOH   B O   1 
HETATM 9192  O  O   . HOH   IA 5 .   ? 12.760 -30.598 20.216  1.00 56.62 ? 555  HOH   B O   1 
HETATM 9193  O  O   . HOH   IA 5 .   ? 36.827 -29.641 26.370  1.00 38.40 ? 556  HOH   B O   1 
HETATM 9194  O  O   . HOH   IA 5 .   ? 35.602 -67.699 24.582  1.00 45.82 ? 557  HOH   B O   1 
HETATM 9195  O  O   . HOH   IA 5 .   ? 32.928 -34.267 16.122  1.00 28.05 ? 558  HOH   B O   1 
HETATM 9196  O  O   . HOH   IA 5 .   ? 41.680 -47.303 39.732  1.00 44.61 ? 559  HOH   B O   1 
HETATM 9197  O  O   . HOH   IA 5 .   ? 15.158 -32.810 17.281  1.00 43.18 ? 560  HOH   B O   1 
HETATM 9198  O  O   . HOH   IA 5 .   ? 28.326 -52.506 35.712  1.00 28.98 ? 561  HOH   B O   1 
HETATM 9199  O  O   . HOH   IA 5 .   ? 20.223 -42.460 42.561  1.00 25.97 ? 562  HOH   B O   1 
HETATM 9200  O  O   . HOH   IA 5 .   ? 43.689 -38.427 37.630  1.00 51.98 ? 563  HOH   B O   1 
HETATM 9201  O  O   . HOH   IA 5 .   ? 25.215 -58.090 7.289   1.00 25.76 ? 564  HOH   B O   1 
HETATM 9202  O  O   . HOH   IA 5 .   ? 21.308 -40.745 40.522  1.00 31.26 ? 565  HOH   B O   1 
HETATM 9203  O  O   . HOH   IA 5 .   ? 45.769 -50.031 39.772  1.00 54.11 ? 566  HOH   B O   1 
HETATM 9204  O  O   . HOH   IA 5 .   ? 33.201 -61.169 20.952  1.00 19.02 ? 567  HOH   B O   1 
HETATM 9205  O  O   . HOH   IA 5 .   ? 44.658 -51.729 34.612  1.00 45.87 ? 568  HOH   B O   1 
HETATM 9206  O  O   . HOH   IA 5 .   ? 28.692 -56.491 38.943  1.00 32.99 ? 569  HOH   B O   1 
HETATM 9207  O  O   . HOH   IA 5 .   ? 7.296  -40.762 36.456  1.00 56.69 ? 570  HOH   B O   1 
HETATM 9208  O  O   . HOH   IA 5 .   ? 26.120 -64.070 28.335  1.00 20.25 ? 571  HOH   B O   1 
HETATM 9209  O  O   . HOH   IA 5 .   ? 27.333 -66.163 6.954   1.00 49.45 ? 572  HOH   B O   1 
HETATM 9210  O  O   . HOH   IA 5 .   ? 20.801 -41.925 38.213  1.00 28.24 ? 573  HOH   B O   1 
HETATM 9211  O  O   . HOH   IA 5 .   ? 40.291 -40.534 37.284  1.00 28.16 ? 574  HOH   B O   1 
HETATM 9212  O  O   . HOH   IA 5 .   ? 27.780 -25.942 26.142  1.00 37.10 ? 575  HOH   B O   1 
HETATM 9213  O  O   . HOH   IA 5 .   ? 42.719 -55.877 31.879  1.00 49.60 ? 576  HOH   B O   1 
HETATM 9214  O  O   . HOH   IA 5 .   ? 33.792 -32.087 6.326   1.00 47.10 ? 577  HOH   B O   1 
HETATM 9215  O  O   . HOH   IA 5 .   ? 23.789 -41.322 8.082   1.00 43.89 ? 578  HOH   B O   1 
HETATM 9216  O  O   . HOH   IA 5 .   ? 16.714 -48.185 40.955  1.00 41.17 ? 579  HOH   B O   1 
HETATM 9217  O  O   . HOH   IA 5 .   ? 34.440 -58.895 13.825  1.00 37.03 ? 580  HOH   B O   1 
HETATM 9218  O  O   . HOH   IA 5 .   ? 10.462 -45.725 12.427  1.00 39.86 ? 581  HOH   B O   1 
HETATM 9219  O  O   . HOH   IA 5 .   ? 33.609 -55.323 15.046  1.00 30.00 ? 582  HOH   B O   1 
HETATM 9220  O  O   . HOH   IA 5 .   ? 40.195 -74.659 30.475  1.00 41.10 ? 583  HOH   B O   1 
HETATM 9221  O  O   . HOH   IA 5 .   ? 34.859 -25.982 24.209  1.00 39.71 ? 584  HOH   B O   1 
HETATM 9222  O  O   . HOH   IA 5 .   ? 15.855 -58.432 9.097   1.00 30.59 ? 585  HOH   B O   1 
HETATM 9223  O  O   . HOH   IA 5 .   ? 47.341 -47.580 17.367  1.00 35.07 ? 586  HOH   B O   1 
HETATM 9224  O  O   . HOH   IA 5 .   ? 37.601 -33.699 16.209  1.00 44.37 ? 587  HOH   B O   1 
HETATM 9225  O  O   . HOH   IA 5 .   ? 43.807 -58.541 25.629  1.00 28.71 ? 588  HOH   B O   1 
HETATM 9226  O  O   . HOH   IA 5 .   ? 36.479 -58.083 17.588  1.00 25.72 ? 589  HOH   B O   1 
HETATM 9227  O  O   . HOH   IA 5 .   ? 20.090 -35.536 8.551   1.00 26.54 ? 590  HOH   B O   1 
HETATM 9228  O  O   . HOH   IA 5 .   ? 21.498 -33.816 41.764  1.00 48.74 ? 591  HOH   B O   1 
HETATM 9229  O  O   . HOH   IA 5 .   ? 26.936 -31.857 36.564  1.00 37.84 ? 592  HOH   B O   1 
HETATM 9230  O  O   . HOH   IA 5 .   ? 44.630 -37.745 17.155  1.00 53.22 ? 593  HOH   B O   1 
HETATM 9231  O  O   . HOH   IA 5 .   ? 14.073 -39.083 43.200  1.00 40.92 ? 594  HOH   B O   1 
HETATM 9232  O  O   . HOH   IA 5 .   ? 22.111 -59.815 25.260  1.00 16.67 ? 595  HOH   B O   1 
HETATM 9233  O  O   . HOH   IA 5 .   ? 14.961 -54.410 6.268   1.00 52.98 ? 596  HOH   B O   1 
HETATM 9234  O  O   . HOH   IA 5 .   ? 31.609 -52.038 23.446  1.00 26.29 ? 597  HOH   B O   1 
HETATM 9235  O  O   . HOH   IA 5 .   ? 45.191 -56.514 22.744  1.00 40.17 ? 598  HOH   B O   1 
HETATM 9236  O  O   . HOH   IA 5 .   ? 21.846 -25.667 10.592  1.00 42.19 ? 599  HOH   B O   1 
HETATM 9237  O  O   . HOH   IA 5 .   ? 32.617 -31.420 33.042  1.00 54.37 ? 600  HOH   B O   1 
HETATM 9238  O  O   . HOH   IA 5 .   ? 45.081 -58.781 34.381  1.00 51.09 ? 601  HOH   B O   1 
HETATM 9239  O  O   . HOH   IA 5 .   ? 29.314 -28.781 12.652  1.00 43.85 ? 602  HOH   B O   1 
HETATM 9240  O  O   . HOH   IA 5 .   ? 33.999 -37.473 4.068   1.00 46.45 ? 603  HOH   B O   1 
HETATM 9241  O  O   . HOH   IA 5 .   ? 45.115 -54.685 19.243  1.00 36.29 ? 604  HOH   B O   1 
HETATM 9242  O  O   . HOH   IA 5 .   ? 31.234 -47.661 13.100  1.00 23.91 ? 605  HOH   B O   1 
HETATM 9243  O  O   . HOH   IA 5 .   ? 16.362 -36.794 18.248  1.00 24.88 ? 606  HOH   B O   1 
HETATM 9244  O  O   . HOH   IA 5 .   ? 8.743  -48.856 15.061  1.00 49.44 ? 607  HOH   B O   1 
HETATM 9245  O  O   . HOH   IA 5 .   ? 23.224 -59.218 5.432   1.00 33.48 ? 608  HOH   B O   1 
HETATM 9246  O  O   . HOH   IA 5 .   ? 29.313 -53.567 23.802  1.00 17.95 ? 609  HOH   B O   1 
HETATM 9247  O  O   . HOH   IA 5 .   ? 34.159 -67.106 20.390  1.00 48.96 ? 610  HOH   B O   1 
HETATM 9248  O  O   . HOH   IA 5 .   ? 34.719 -44.783 7.865   1.00 33.55 ? 611  HOH   B O   1 
HETATM 9249  O  O   . HOH   IA 5 .   ? 23.000 -43.161 5.874   1.00 37.81 ? 612  HOH   B O   1 
HETATM 9250  O  O   . HOH   IA 5 .   ? 32.094 -71.121 10.490  1.00 11.86 ? 613  HOH   B O   1 
HETATM 9251  O  O   . HOH   IA 5 .   ? 45.341 -33.249 23.561  1.00 46.52 ? 614  HOH   B O   1 
HETATM 9252  O  O   . HOH   IA 5 .   ? 9.475  -44.126 6.017   1.00 48.59 ? 615  HOH   B O   1 
HETATM 9253  O  O   . HOH   IA 5 .   ? 28.047 -24.021 13.503  1.00 44.77 ? 616  HOH   B O   1 
HETATM 9254  O  O   . HOH   IA 5 .   ? 15.943 -53.053 34.884  1.00 31.10 ? 617  HOH   B O   1 
HETATM 9255  O  O   . HOH   IA 5 .   ? 8.341  -55.645 24.270  1.00 44.92 ? 618  HOH   B O   1 
HETATM 9256  O  O   . HOH   IA 5 .   ? 19.799 -44.218 4.124   1.00 25.98 ? 619  HOH   B O   1 
HETATM 9257  O  O   . HOH   IA 5 .   ? 11.819 -43.281 42.300  1.00 45.46 ? 620  HOH   B O   1 
HETATM 9258  O  O   . HOH   IA 5 .   ? 13.391 -37.799 23.148  1.00 42.32 ? 621  HOH   B O   1 
HETATM 9259  O  O   . HOH   IA 5 .   ? 34.822 -30.564 31.302  1.00 51.45 ? 622  HOH   B O   1 
HETATM 9260  O  O   . HOH   IA 5 .   ? 35.513 -62.528 20.022  1.00 30.55 ? 623  HOH   B O   1 
HETATM 9261  O  O   . HOH   IA 5 .   ? 12.335 -51.732 18.720  1.00 30.00 ? 624  HOH   B O   1 
HETATM 9262  O  O   . HOH   IA 5 .   ? 32.649 -66.072 32.406  1.00 48.09 ? 625  HOH   B O   1 
HETATM 9263  O  O   . HOH   IA 5 .   ? 43.619 -53.277 38.186  1.00 44.37 ? 626  HOH   B O   1 
HETATM 9264  O  O   . HOH   IA 5 .   ? 18.185 -47.824 10.232  1.00 21.50 ? 627  HOH   B O   1 
HETATM 9265  O  O   . HOH   IA 5 .   ? 4.293  -45.145 26.402  1.00 51.04 ? 628  HOH   B O   1 
HETATM 9266  O  O   . HOH   IA 5 .   ? 10.836 -45.691 39.235  1.00 45.69 ? 629  HOH   B O   1 
HETATM 9267  O  O   . HOH   IA 5 .   ? 4.838  -39.014 27.164  1.00 51.74 ? 630  HOH   B O   1 
HETATM 9268  O  O   . HOH   IA 5 .   ? 32.341 -63.794 21.805  1.00 31.72 ? 631  HOH   B O   1 
HETATM 9269  O  O   . HOH   IA 5 .   ? 23.885 -27.753 24.366  1.00 44.12 ? 632  HOH   B O   1 
HETATM 9270  O  O   . HOH   IA 5 .   ? 10.161 -43.987 37.982  1.00 42.82 ? 633  HOH   B O   1 
HETATM 9271  O  O   . HOH   IA 5 .   ? 36.241 -64.755 16.345  1.00 32.61 ? 634  HOH   B O   1 
HETATM 9272  O  O   . HOH   IA 5 .   ? 47.399 -51.439 22.146  1.00 29.39 ? 635  HOH   B O   1 
HETATM 9273  O  O   . HOH   IA 5 .   ? 41.908 -52.129 10.734  1.00 32.16 ? 636  HOH   B O   1 
HETATM 9274  O  O   . HOH   IA 5 .   ? 25.070 -70.604 17.418  1.00 22.93 ? 637  HOH   B O   1 
HETATM 9275  O  O   . HOH   IA 5 .   ? 12.776 -37.786 7.916   1.00 58.08 ? 638  HOH   B O   1 
HETATM 9276  O  O   . HOH   IA 5 .   ? 39.464 -54.288 11.668  1.00 38.83 ? 639  HOH   B O   1 
HETATM 9277  O  O   . HOH   IA 5 .   ? 25.694 -63.507 16.956  1.00 22.89 ? 640  HOH   B O   1 
HETATM 9278  O  O   . HOH   IA 5 .   ? 49.034 -51.230 28.037  1.00 47.80 ? 641  HOH   B O   1 
HETATM 9279  O  O   . HOH   IA 5 .   ? 30.794 -30.127 30.727  1.00 42.88 ? 642  HOH   B O   1 
HETATM 9280  O  O   . HOH   IA 5 .   ? 25.544 -62.236 7.564   1.00 38.33 ? 643  HOH   B O   1 
HETATM 9281  O  O   . HOH   IA 5 .   ? 39.336 -35.005 33.124  1.00 38.22 ? 644  HOH   B O   1 
HETATM 9282  O  O   . HOH   IA 5 .   ? 24.079 -36.476 4.061   1.00 34.19 ? 645  HOH   B O   1 
HETATM 9283  O  O   . HOH   IA 5 .   ? 21.925 -71.174 12.236  1.00 30.24 ? 646  HOH   B O   1 
HETATM 9284  O  O   . HOH   IA 5 .   ? 13.292 -41.765 43.955  1.00 55.38 ? 647  HOH   B O   1 
HETATM 9285  O  O   . HOH   IA 5 .   ? 28.214 -68.628 23.598  1.00 21.50 ? 648  HOH   B O   1 
HETATM 9286  O  O   . HOH   IA 5 .   ? 27.342 -23.101 20.533  1.00 47.89 ? 649  HOH   B O   1 
HETATM 9287  O  O   . HOH   IA 5 .   ? 46.760 -50.207 37.759  1.00 48.43 ? 650  HOH   B O   1 
HETATM 9288  O  O   . HOH   IA 5 .   ? 50.887 -39.872 24.938  1.00 46.84 ? 651  HOH   B O   1 
HETATM 9289  O  O   . HOH   IA 5 .   ? 6.752  -48.624 33.558  1.00 36.74 ? 652  HOH   B O   1 
HETATM 9290  O  O   . HOH   IA 5 .   ? 14.291 -38.222 12.440  1.00 28.86 ? 653  HOH   B O   1 
HETATM 9291  O  O   . HOH   IA 5 .   ? 24.306 -28.896 32.097  1.00 39.82 ? 654  HOH   B O   1 
HETATM 9292  O  O   . HOH   IA 5 .   ? 40.964 -42.008 15.141  1.00 47.71 ? 655  HOH   B O   1 
HETATM 9293  O  O   . HOH   IA 5 .   ? 34.686 -69.351 31.582  1.00 49.31 ? 656  HOH   B O   1 
HETATM 9294  O  O   . HOH   IA 5 .   ? 41.147 -38.822 10.942  1.00 55.25 ? 657  HOH   B O   1 
HETATM 9295  O  O   . HOH   IA 5 .   ? 25.069 -27.592 8.474   1.00 56.65 ? 658  HOH   B O   1 
HETATM 9296  O  O   . HOH   IA 5 .   ? 36.335 -55.117 44.446  1.00 39.61 ? 659  HOH   B O   1 
HETATM 9297  O  O   . HOH   IA 5 .   ? 24.313 -54.936 39.755  1.00 44.22 ? 660  HOH   B O   1 
HETATM 9298  O  O   . HOH   IA 5 .   ? 38.564 -42.566 9.865   1.00 27.46 ? 661  HOH   B O   1 
HETATM 9299  O  O   . HOH   IA 5 .   ? 26.390 -53.640 33.853  1.00 24.10 ? 662  HOH   B O   1 
HETATM 9300  O  O   . HOH   IA 5 .   ? 31.913 -64.958 8.798   1.00 31.15 ? 663  HOH   B O   1 
HETATM 9301  O  O   . HOH   IA 5 .   ? 26.539 -29.774 11.977  1.00 35.34 ? 664  HOH   B O   1 
HETATM 9302  O  O   . HOH   IA 5 .   ? 49.798 -37.190 27.964  1.00 43.62 ? 665  HOH   B O   1 
HETATM 9303  O  O   . HOH   IA 5 .   ? 34.111 -60.816 40.101  1.00 30.85 ? 666  HOH   B O   1 
HETATM 9304  O  O   . HOH   IA 5 .   ? 26.005 -65.926 17.712  1.00 25.35 ? 667  HOH   B O   1 
HETATM 9305  O  O   . HOH   IA 5 .   ? 27.516 -54.404 25.952  1.00 18.92 ? 668  HOH   B O   1 
HETATM 9306  O  O   . HOH   IA 5 .   ? 23.657 -21.712 18.482  1.00 48.92 ? 669  HOH   B O   1 
HETATM 9307  O  O   . HOH   IA 5 .   ? 30.428 -62.731 25.717  1.00 29.15 ? 670  HOH   B O   1 
HETATM 9308  O  O   . HOH   IA 5 .   ? 22.962 -35.414 8.726   1.00 31.74 ? 671  HOH   B O   1 
HETATM 9309  O  O   . HOH   IA 5 .   ? 39.413 -33.370 26.909  1.00 31.49 ? 672  HOH   B O   1 
HETATM 9310  O  O   . HOH   IA 5 .   ? 11.028 -49.939 21.078  1.00 30.00 ? 673  HOH   B O   1 
HETATM 9311  O  O   . HOH   IA 5 .   ? 10.960 -41.515 19.959  1.00 48.73 ? 674  HOH   B O   1 
HETATM 9312  O  O   . HOH   IA 5 .   ? 44.956 -68.297 24.908  1.00 54.50 ? 675  HOH   B O   1 
HETATM 9313  O  O   . HOH   IA 5 .   ? 36.476 -39.374 6.599   1.00 53.37 ? 676  HOH   B O   1 
HETATM 9314  O  O   . HOH   IA 5 .   ? 24.624 -28.390 11.866  1.00 53.62 ? 677  HOH   B O   1 
HETATM 9315  O  O   . HOH   IA 5 .   ? 38.667 -42.285 44.727  1.00 41.24 ? 678  HOH   B O   1 
HETATM 9316  O  O   . HOH   IA 5 .   ? 23.040 -54.984 10.404  1.00 31.58 ? 679  HOH   B O   1 
HETATM 9317  O  O   . HOH   IA 5 .   ? 35.359 -35.033 41.804  1.00 48.04 ? 680  HOH   B O   1 
HETATM 9318  O  O   . HOH   IA 5 .   ? 23.420 -52.146 36.286  1.00 43.05 ? 681  HOH   B O   1 
HETATM 9319  O  O   . HOH   IA 5 .   ? 31.775 -48.002 10.619  1.00 29.21 ? 682  HOH   B O   1 
HETATM 9320  O  O   . HOH   IA 5 .   ? 24.065 -31.730 38.855  1.00 42.47 ? 683  HOH   B O   1 
HETATM 9321  O  O   . HOH   IA 5 .   ? 22.785 -64.500 21.869  1.00 15.25 ? 684  HOH   B O   1 
HETATM 9322  O  O   . HOH   IA 5 .   ? 29.051 -28.749 37.860  1.00 55.62 ? 685  HOH   B O   1 
HETATM 9323  O  O   . HOH   IA 5 .   ? 5.568  -45.401 24.096  1.00 51.15 ? 686  HOH   B O   1 
HETATM 9324  O  O   . HOH   IA 5 .   ? 22.212 -56.276 9.259   1.00 39.05 ? 687  HOH   B O   1 
HETATM 9325  O  O   . HOH   IA 5 .   ? 41.920 -61.674 10.673  1.00 66.41 ? 688  HOH   B O   1 
HETATM 9326  O  O   . HOH   IA 5 .   ? 40.600 -41.723 11.564  1.00 50.00 ? 689  HOH   B O   1 
HETATM 9327  O  O   . HOH   IA 5 .   ? 14.468 -58.430 16.366  1.00 15.83 ? 690  HOH   B O   1 
HETATM 9328  O  O   . HOH   IA 5 .   ? 25.224 -48.028 6.259   1.00 30.61 ? 691  HOH   B O   1 
HETATM 9329  O  O   . HOH   IA 5 .   ? 42.352 -62.157 35.836  1.00 51.09 ? 692  HOH   B O   1 
HETATM 9330  O  O   . HOH   IA 5 .   ? 10.388 -55.265 30.872  1.00 47.09 ? 693  HOH   B O   1 
HETATM 9331  O  O   . HOH   IA 5 .   ? 27.360 -30.138 33.168  1.00 48.63 ? 694  HOH   B O   1 
HETATM 9332  O  O   . HOH   IA 5 .   ? 10.362 -45.658 8.032   1.00 47.70 ? 695  HOH   B O   1 
HETATM 9333  O  O   . HOH   IA 5 .   ? 10.545 -31.797 23.060  1.00 51.06 ? 696  HOH   B O   1 
HETATM 9334  O  O   . HOH   IA 5 .   ? 31.247 -28.360 20.236  1.00 39.95 ? 697  HOH   B O   1 
HETATM 9335  O  O   . HOH   IA 5 .   ? 25.087 -68.978 9.743   1.00 43.93 ? 698  HOH   B O   1 
HETATM 9336  O  O   . HOH   IA 5 .   ? 37.882 -74.221 26.707  1.00 38.92 ? 699  HOH   B O   1 
HETATM 9337  O  O   . HOH   IA 5 .   ? 27.182 -51.752 24.948  1.00 39.78 ? 700  HOH   B O   1 
HETATM 9338  O  O   . HOH   IA 5 .   ? 47.371 -45.092 31.656  1.00 44.40 ? 701  HOH   B O   1 
HETATM 9339  O  O   . HOH   IA 5 .   ? 45.970 -59.382 26.024  1.00 48.86 ? 702  HOH   B O   1 
HETATM 9340  O  O   . HOH   IA 5 .   ? 30.328 -67.890 18.033  1.00 28.14 ? 703  HOH   B O   1 
HETATM 9341  O  O   . HOH   IA 5 .   ? 14.446 -36.233 14.115  1.00 39.29 ? 704  HOH   B O   1 
HETATM 9342  O  O   . HOH   IA 5 .   ? 9.054  -44.407 17.206  1.00 55.08 ? 705  HOH   B O   1 
HETATM 9343  O  O   . HOH   IA 5 .   ? 41.241 -40.311 17.219  1.00 42.23 ? 706  HOH   B O   1 
HETATM 9344  O  O   . HOH   IA 5 .   ? 17.505 -60.804 8.730   1.00 40.40 ? 707  HOH   B O   1 
HETATM 9345  O  O   . HOH   IA 5 .   ? 13.643 -55.042 10.375  1.00 42.37 ? 708  HOH   B O   1 
HETATM 9346  O  O   . HOH   IA 5 .   ? 15.920 -29.006 31.391  1.00 47.80 ? 709  HOH   B O   1 
HETATM 9347  O  O   . HOH   IA 5 .   ? 21.345 -62.343 24.165  1.00 17.31 ? 710  HOH   B O   1 
HETATM 9348  O  O   . HOH   IA 5 .   ? 28.931 -59.414 39.185  1.00 48.54 ? 711  HOH   B O   1 
HETATM 9349  O  O   . HOH   IA 5 .   ? 40.162 -47.091 42.047  1.00 54.93 ? 712  HOH   B O   1 
HETATM 9350  O  O   . HOH   IA 5 .   ? 33.010 -41.774 50.462  1.00 48.49 ? 713  HOH   B O   1 
HETATM 9351  O  O   . HOH   IA 5 .   ? 6.346  -48.998 36.173  1.00 55.57 ? 714  HOH   B O   1 
HETATM 9352  O  O   . HOH   IA 5 .   ? 23.915 -52.406 45.038  1.00 27.04 ? 715  HOH   B O   1 
HETATM 9353  O  O   . HOH   IA 5 .   ? 22.336 -64.899 19.757  1.00 26.40 ? 716  HOH   B O   1 
HETATM 9354  O  O   . HOH   IA 5 .   ? 28.075 -67.523 16.467  1.00 25.39 ? 717  HOH   B O   1 
HETATM 9355  O  O   . HOH   IA 5 .   ? 19.464 -24.573 23.693  1.00 42.84 ? 718  HOH   B O   1 
HETATM 9356  O  O   . HOH   IA 5 .   ? 12.001 -43.663 10.932  1.00 49.53 ? 719  HOH   B O   1 
HETATM 9357  O  O   . HOH   IA 5 .   ? 45.991 -43.985 13.918  1.00 50.99 ? 720  HOH   B O   1 
HETATM 9358  O  O   . HOH   IA 5 .   ? 12.525 -56.437 12.425  1.00 29.92 ? 721  HOH   B O   1 
HETATM 9359  O  O   . HOH   IA 5 .   ? 23.339 -69.159 11.493  1.00 40.67 ? 722  HOH   B O   1 
HETATM 9360  O  O   . HOH   IA 5 .   ? 29.665 -41.263 45.270  1.00 47.29 ? 723  HOH   B O   1 
HETATM 9361  O  O   . HOH   IA 5 .   ? 19.766 -52.153 6.154   1.00 43.95 ? 724  HOH   B O   1 
HETATM 9362  O  O   . HOH   IA 5 .   ? 37.983 -41.960 6.970   1.00 54.96 ? 725  HOH   B O   1 
HETATM 9363  O  O   . HOH   IA 5 .   ? 33.035 -28.697 2.980   1.00 55.69 ? 726  HOH   B O   1 
HETATM 9364  O  O   . HOH   IA 5 .   ? 20.936 -49.101 42.153  1.00 46.56 ? 727  HOH   B O   1 
HETATM 9365  O  O   . HOH   IA 5 .   ? 49.935 -39.927 20.691  1.00 50.93 ? 728  HOH   B O   1 
HETATM 9366  O  O   . HOH   IA 5 .   ? 20.234 -56.591 30.066  1.00 28.81 ? 729  HOH   B O   1 
HETATM 9367  O  O   . HOH   IA 5 .   ? 50.486 -46.913 23.840  1.00 41.32 ? 730  HOH   B O   1 
HETATM 9368  O  O   . HOH   IA 5 .   ? 15.723 -35.325 16.313  1.00 37.90 ? 731  HOH   B O   1 
HETATM 9369  O  O   . HOH   IA 5 .   ? 32.509 -24.396 25.465  1.00 49.47 ? 732  HOH   B O   1 
HETATM 9370  O  O   . HOH   IA 5 .   ? 30.151 -67.248 9.808   1.00 35.45 ? 733  HOH   B O   1 
HETATM 9371  O  O   . HOH   IA 5 .   ? 12.995 -30.575 30.822  1.00 42.47 ? 734  HOH   B O   1 
HETATM 9372  O  O   . HOH   IA 5 .   ? 34.090 -64.800 18.916  1.00 42.71 ? 735  HOH   B O   1 
HETATM 9373  O  O   . HOH   IA 5 .   ? 32.775 -62.783 39.911  1.00 52.48 ? 736  HOH   B O   1 
HETATM 9374  O  O   . HOH   IA 5 .   ? 12.210 -57.238 15.049  1.00 19.15 ? 737  HOH   B O   1 
HETATM 9375  O  O   . HOH   IA 5 .   ? 20.874 -58.209 34.544  1.00 50.28 ? 738  HOH   B O   1 
HETATM 9376  O  O   . HOH   IA 5 .   ? 15.040 -56.436 30.594  1.00 40.12 ? 739  HOH   B O   1 
HETATM 9377  O  O   . HOH   IA 5 .   ? 15.691 -49.330 39.290  1.00 44.74 ? 740  HOH   B O   1 
HETATM 9378  O  O   . HOH   IA 5 .   ? 46.166 -38.524 33.678  1.00 47.07 ? 741  HOH   B O   1 
HETATM 9379  O  O   . HOH   IA 5 .   ? 15.831 -33.655 38.534  1.00 47.34 ? 742  HOH   B O   1 
HETATM 9380  O  O   . HOH   IA 5 .   ? 14.872 -43.715 48.307  1.00 55.50 ? 743  HOH   B O   1 
HETATM 9381  O  O   . HOH   IA 5 .   ? 50.594 -54.631 27.986  1.00 58.64 ? 744  HOH   B O   1 
HETATM 9382  O  O   . HOH   IA 5 .   ? 48.298 -46.872 32.676  1.00 54.14 ? 745  HOH   B O   1 
HETATM 9383  O  O   . HOH   IA 5 .   ? 23.988 -63.699 5.884   1.00 58.40 ? 746  HOH   B O   1 
HETATM 9384  O  O   . HOH   IA 5 .   ? 38.721 -58.889 17.161  1.00 43.54 ? 747  HOH   B O   1 
HETATM 9385  O  O   . HOH   IA 5 .   ? 30.327 -44.862 47.870  1.00 43.66 ? 748  HOH   B O   1 
HETATM 9386  O  O   . HOH   IA 5 .   ? 49.603 -52.529 26.020  1.00 48.69 ? 749  HOH   B O   1 
HETATM 9387  O  O   . HOH   IA 5 .   ? 51.098 -52.764 33.888  1.00 47.08 ? 750  HOH   B O   1 
HETATM 9388  O  O   . HOH   IA 5 .   ? 42.454 -52.676 41.010  1.00 43.94 ? 751  HOH   B O   1 
HETATM 9389  O  O   . HOH   IA 5 .   ? 6.881  -35.029 29.621  1.00 48.73 ? 752  HOH   B O   1 
HETATM 9390  O  O   . HOH   IA 5 .   ? 36.332 -32.872 36.254  1.00 46.35 ? 753  HOH   B O   1 
HETATM 9391  O  O   . HOH   IA 5 .   ? 38.328 -32.734 29.000  1.00 38.68 ? 754  HOH   B O   1 
HETATM 9392  O  O   . HOH   IA 5 .   ? 24.590 -45.787 5.004   1.00 53.45 ? 755  HOH   B O   1 
HETATM 9393  O  O   . HOH   IA 5 .   ? 34.083 -64.627 37.162  1.00 43.61 ? 756  HOH   B O   1 
HETATM 9394  O  O   . HOH   IA 5 .   ? 36.585 -31.751 33.478  1.00 49.12 ? 757  HOH   B O   1 
HETATM 9395  O  O   . HOH   IA 5 .   ? 12.258 -39.851 12.619  1.00 35.16 ? 758  HOH   B O   1 
HETATM 9396  O  O   . HOH   IA 5 .   ? 9.996  -54.892 20.665  1.00 25.80 ? 759  HOH   B O   1 
HETATM 9397  O  O   . HOH   IA 5 .   ? 33.582 -32.390 14.494  1.00 39.64 ? 760  HOH   B O   1 
HETATM 9398  O  O   . HOH   IA 5 .   ? 31.709 -27.108 3.711   1.00 55.79 ? 761  HOH   B O   1 
HETATM 9399  O  O   . HOH   IA 5 .   ? 37.280 -60.837 18.496  1.00 46.38 ? 762  HOH   B O   1 
HETATM 9400  O  O   . HOH   IA 5 .   ? 10.953 -52.619 9.243   1.00 53.00 ? 763  HOH   B O   1 
HETATM 9401  O  O   . HOH   IA 5 .   ? 48.144 -46.539 15.315  1.00 49.25 ? 764  HOH   B O   1 
HETATM 9402  O  O   . HOH   IA 5 .   ? 16.176 -36.560 47.508  1.00 58.46 ? 765  HOH   B O   1 
HETATM 9403  O  O   . HOH   IA 5 .   ? 9.795  -48.992 11.748  1.00 42.62 ? 766  HOH   B O   1 
HETATM 9404  O  O   . HOH   IA 5 .   ? 13.953 -56.353 7.642   1.00 58.79 ? 767  HOH   B O   1 
HETATM 9405  O  O   . HOH   IA 5 .   ? 27.262 -39.115 3.154   1.00 48.77 ? 768  HOH   B O   1 
HETATM 9406  O  O   . HOH   IA 5 .   ? 25.125 -26.331 25.792  1.00 58.64 ? 769  HOH   B O   1 
HETATM 9407  O  O   . HOH   IA 5 .   ? 13.557 -33.235 19.079  1.00 42.60 ? 770  HOH   B O   1 
HETATM 9408  O  O   . HOH   IA 5 .   ? 42.877 -32.072 27.027  1.00 58.71 ? 771  HOH   B O   1 
HETATM 9409  O  O   . HOH   IA 5 .   ? 17.513 -54.859 33.040  1.00 46.27 ? 772  HOH   B O   1 
HETATM 9410  O  O   . HOH   IA 5 .   ? 35.345 -29.526 18.816  1.00 63.57 ? 773  HOH   B O   1 
HETATM 9411  O  O   . HOH   IA 5 .   ? 28.907 -31.106 34.389  1.00 47.18 ? 774  HOH   B O   1 
HETATM 9412  O  O   . HOH   IA 5 .   ? 35.971 -66.056 36.165  1.00 54.62 ? 775  HOH   B O   1 
HETATM 9413  O  O   . HOH   IA 5 .   ? 40.036 -62.798 19.223  1.00 38.46 ? 776  HOH   B O   1 
HETATM 9414  O  O   . HOH   IA 5 .   ? 32.009 -66.938 30.247  1.00 47.65 ? 777  HOH   B O   1 
HETATM 9415  O  O   . HOH   IA 5 .   ? 32.097 -46.929 49.456  1.00 30.00 ? 778  HOH   B O   1 
HETATM 9416  O  O   . HOH   IA 5 .   ? 17.186 -34.676 5.553   1.00 55.42 ? 779  HOH   B O   1 
HETATM 9417  O  O   . HOH   IA 5 .   ? 15.941 -36.980 44.906  1.00 54.47 ? 780  HOH   B O   1 
HETATM 9418  O  O   . HOH   IA 5 .   ? 11.794 -20.590 19.990  1.00 56.36 ? 781  HOH   B O   1 
HETATM 9419  O  O   . HOH   IA 5 .   ? 48.370 -49.292 18.243  1.00 45.49 ? 782  HOH   B O   1 
HETATM 9420  O  O   . HOH   IA 5 .   ? 12.549 -42.123 13.179  1.00 49.35 ? 783  HOH   B O   1 
HETATM 9421  O  O   . HOH   IA 5 .   ? 38.481 -34.194 35.928  1.00 50.12 ? 784  HOH   B O   1 
HETATM 9422  O  O   . HOH   IA 5 .   ? 13.940 -37.590 18.974  1.00 37.91 ? 785  HOH   B O   1 
HETATM 9423  O  O   . HOH   IA 5 .   ? 29.703 -66.399 24.442  1.00 43.41 ? 786  HOH   B O   1 
HETATM 9424  O  O   . HOH   IA 5 .   ? 7.104  -37.859 30.187  1.00 41.68 ? 787  HOH   B O   1 
HETATM 9425  O  O   . HOH   IA 5 .   ? 7.971  -38.002 33.005  1.00 37.69 ? 788  HOH   B O   1 
HETATM 9426  O  O   . HOH   IA 5 .   ? 41.259 -68.474 19.743  1.00 49.13 ? 789  HOH   B O   1 
HETATM 9427  O  O   . HOH   IA 5 .   ? 6.271  -50.032 31.098  1.00 37.79 ? 790  HOH   B O   1 
HETATM 9428  O  O   . HOH   IA 5 .   ? 30.573 -64.369 39.179  1.00 42.84 ? 791  HOH   B O   1 
HETATM 9429  O  O   . HOH   IA 5 .   ? 33.476 -28.021 19.314  1.00 44.12 ? 792  HOH   B O   1 
HETATM 9430  O  O   . HOH   IA 5 .   ? 15.839 -51.437 2.669   1.00 54.10 ? 793  HOH   B O   1 
HETATM 9431  O  O   . HOH   IA 5 .   ? 46.086 -39.021 36.263  1.00 53.84 ? 794  HOH   B O   1 
HETATM 9432  O  O   . HOH   IA 5 .   ? 49.812 -49.863 21.961  1.00 53.47 ? 795  HOH   B O   1 
HETATM 9433  O  O   . HOH   IA 5 .   ? 17.759 -52.179 36.250  1.00 48.43 ? 796  HOH   B O   1 
HETATM 9434  O  O   . HOH   IA 5 .   ? 37.647 -36.056 37.477  1.00 46.55 ? 797  HOH   B O   1 
HETATM 9435  O  O   . HOH   IA 5 .   ? 27.602 -25.927 11.704  1.00 47.83 ? 798  HOH   B O   1 
HETATM 9436  O  O   . HOH   IA 5 .   ? 6.062  -39.498 34.691  1.00 53.07 ? 799  HOH   B O   1 
HETATM 9437  O  O   . HOH   IA 5 .   ? 42.714 -57.951 16.083  1.00 46.90 ? 800  HOH   B O   1 
HETATM 9438  O  O   . HOH   IA 5 .   ? 7.362  -53.628 29.252  1.00 44.83 ? 801  HOH   B O   1 
HETATM 9439  O  O   . HOH   IA 5 .   ? 14.886 -25.904 3.007   1.00 51.27 ? 802  HOH   B O   1 
HETATM 9440  O  O   . HOH   IA 5 .   ? 10.050 -53.040 14.749  1.00 33.67 ? 803  HOH   B O   1 
HETATM 9441  O  O   . HOH   IA 5 .   ? 32.536 -31.160 12.501  1.00 45.07 ? 804  HOH   B O   1 
HETATM 9442  O  O   . HOH   IA 5 .   ? 37.087 -76.143 27.660  1.00 59.09 ? 805  HOH   B O   1 
HETATM 9443  O  O   . HOH   IA 5 .   ? 35.742 -31.023 9.659   1.00 54.09 ? 806  HOH   B O   1 
HETATM 9444  O  O   . HOH   IA 5 .   ? 17.087 -51.768 40.458  1.00 54.09 ? 807  HOH   B O   1 
HETATM 9445  O  O   . HOH   IA 5 .   ? 11.813 -58.494 10.521  1.00 31.82 ? 808  HOH   B O   1 
HETATM 9446  O  O   . HOH   IA 5 .   ? 44.864 -61.638 35.019  1.00 53.99 ? 809  HOH   B O   1 
HETATM 9447  O  O   . HOH   IA 5 .   ? 11.464 -53.158 12.153  1.00 33.17 ? 810  HOH   B O   1 
HETATM 9448  O  O   . HOH   IA 5 .   ? 13.903 -60.098 8.738   1.00 37.82 ? 811  HOH   B O   1 
HETATM 9449  O  O   . HOH   IA 5 .   ? 7.143  -43.927 18.288  1.00 49.67 ? 812  HOH   B O   1 
HETATM 9450  O  O   . HOH   IA 5 .   ? 12.571 -37.208 16.636  1.00 43.08 ? 813  HOH   B O   1 
HETATM 9451  O  O   . HOH   IA 5 .   ? 11.391 -54.276 18.400  1.00 33.66 ? 814  HOH   B O   1 
HETATM 9452  O  O   . HOH   IA 5 .   ? 8.425  -51.986 18.518  1.00 53.01 ? 815  HOH   B O   1 
HETATM 9453  O  O   . HOH   JA 5 .   ? 64.264 5.628   36.703  1.00 18.86 ? 401  HOH   C O   1 
HETATM 9454  O  O   . HOH   JA 5 .   ? 77.503 -16.852 49.715  1.00 33.47 ? 402  HOH   C O   1 
HETATM 9455  O  O   . HOH   JA 5 .   ? 69.862 -28.836 55.322  1.00 26.69 ? 403  HOH   C O   1 
HETATM 9456  O  O   . HOH   JA 5 .   ? 37.773 -7.426  43.663  1.00 45.34 ? 404  HOH   C O   1 
HETATM 9457  O  O   . HOH   JA 5 .   ? 71.563 -17.843 67.082  1.00 20.48 ? 405  HOH   C O   1 
HETATM 9458  O  O   . HOH   JA 5 .   ? 54.234 -0.385  47.976  1.00 42.81 ? 406  HOH   C O   1 
HETATM 9459  O  O   . HOH   JA 5 .   ? 50.337 1.650   33.414  1.00 45.71 ? 407  HOH   C O   1 
HETATM 9460  O  O   . HOH   JA 5 .   ? 31.626 -11.101 54.218  1.00 52.40 ? 408  HOH   C O   1 
HETATM 9461  O  O   . HOH   JA 5 .   ? 66.240 -20.684 61.243  1.00 33.27 ? 409  HOH   C O   1 
HETATM 9462  O  O   . HOH   JA 5 .   ? 62.617 2.184   41.955  1.00 34.79 ? 410  HOH   C O   1 
HETATM 9463  O  O   . HOH   JA 5 .   ? 53.447 -32.858 49.100  1.00 22.73 ? 411  HOH   C O   1 
HETATM 9464  O  O   . HOH   JA 5 .   ? 59.954 -14.116 42.335  1.00 27.02 ? 412  HOH   C O   1 
HETATM 9465  O  O   . HOH   JA 5 .   ? 71.987 -12.774 35.728  1.00 43.32 ? 413  HOH   C O   1 
HETATM 9466  O  O   . HOH   JA 5 .   ? 69.756 -20.886 62.761  1.00 28.52 ? 414  HOH   C O   1 
HETATM 9467  O  O   . HOH   JA 5 .   ? 57.263 -5.803  55.447  1.00 34.16 ? 415  HOH   C O   1 
HETATM 9468  O  O   . HOH   JA 5 .   ? 59.308 -20.744 51.070  1.00 16.16 ? 416  HOH   C O   1 
HETATM 9469  O  O   . HOH   JA 5 .   ? 47.007 2.059   41.585  1.00 43.78 ? 417  HOH   C O   1 
HETATM 9470  O  O   . HOH   JA 5 .   ? 52.328 5.357   42.660  1.00 24.98 ? 418  HOH   C O   1 
HETATM 9471  O  O   . HOH   JA 5 .   ? 47.276 -28.625 33.051  1.00 49.09 ? 419  HOH   C O   1 
HETATM 9472  O  O   . HOH   JA 5 .   ? 39.543 -1.540  61.217  1.00 53.17 ? 420  HOH   C O   1 
HETATM 9473  O  O   . HOH   JA 5 .   ? 37.878 -10.903 59.075  1.00 35.31 ? 421  HOH   C O   1 
HETATM 9474  O  O   . HOH   JA 5 .   ? 37.971 -1.715  35.600  1.00 51.21 ? 422  HOH   C O   1 
HETATM 9475  O  O   . HOH   JA 5 .   ? 61.241 -9.703  25.214  1.00 37.92 ? 423  HOH   C O   1 
HETATM 9476  O  O   . HOH   JA 5 .   ? 47.255 7.275   47.005  1.00 30.06 ? 424  HOH   C O   1 
HETATM 9477  O  O   . HOH   JA 5 .   ? 68.272 -1.590  45.948  1.00 25.94 ? 425  HOH   C O   1 
HETATM 9478  O  O   . HOH   JA 5 .   ? 53.203 -28.698 61.638  1.00 39.64 ? 426  HOH   C O   1 
HETATM 9479  O  O   . HOH   JA 5 .   ? 36.116 -2.563  48.780  1.00 43.33 ? 427  HOH   C O   1 
HETATM 9480  O  O   . HOH   JA 5 .   ? 48.292 -6.882  29.540  1.00 51.87 ? 428  HOH   C O   1 
HETATM 9481  O  O   . HOH   JA 5 .   ? 45.426 -11.065 66.976  1.00 52.08 ? 429  HOH   C O   1 
HETATM 9482  O  O   . HOH   JA 5 .   ? 34.782 -21.723 41.245  1.00 39.66 ? 430  HOH   C O   1 
HETATM 9483  O  O   . HOH   JA 5 .   ? 53.671 -18.257 23.594  1.00 44.10 ? 431  HOH   C O   1 
HETATM 9484  O  O   . HOH   JA 5 .   ? 63.851 -24.770 32.546  1.00 27.12 ? 432  HOH   C O   1 
HETATM 9485  O  O   . HOH   JA 5 .   ? 74.227 -11.831 51.561  1.00 53.20 ? 433  HOH   C O   1 
HETATM 9486  O  O   . HOH   JA 5 .   ? 47.847 -35.257 51.372  1.00 37.67 ? 434  HOH   C O   1 
HETATM 9487  O  O   . HOH   JA 5 .   ? 45.474 -8.443  30.797  1.00 42.58 ? 435  HOH   C O   1 
HETATM 9488  O  O   . HOH   JA 5 .   ? 35.219 -9.911  50.641  1.00 28.49 ? 436  HOH   C O   1 
HETATM 9489  O  O   . HOH   JA 5 .   ? 56.478 1.953   47.754  1.00 45.47 ? 437  HOH   C O   1 
HETATM 9490  O  O   . HOH   JA 5 .   ? 54.414 -12.026 65.967  1.00 21.57 ? 438  HOH   C O   1 
HETATM 9491  O  O   . HOH   JA 5 .   ? 35.320 -4.325  52.043  1.00 55.98 ? 439  HOH   C O   1 
HETATM 9492  O  O   . HOH   JA 5 .   ? 33.320 -13.645 50.858  1.00 31.47 ? 440  HOH   C O   1 
HETATM 9493  O  O   . HOH   JA 5 .   ? 41.761 -18.162 56.830  1.00 30.88 ? 441  HOH   C O   1 
HETATM 9494  O  O   . HOH   JA 5 .   ? 61.053 -29.796 31.230  1.00 40.82 ? 442  HOH   C O   1 
HETATM 9495  O  O   . HOH   JA 5 .   ? 49.058 1.937   59.356  1.00 48.77 ? 443  HOH   C O   1 
HETATM 9496  O  O   . HOH   JA 5 .   ? 66.322 -10.670 52.957  1.00 16.75 ? 444  HOH   C O   1 
HETATM 9497  O  O   . HOH   JA 5 .   ? 74.091 -7.268  45.695  1.00 27.21 ? 445  HOH   C O   1 
HETATM 9498  O  O   . HOH   JA 5 .   ? 50.510 -31.640 53.384  1.00 20.51 ? 446  HOH   C O   1 
HETATM 9499  O  O   . HOH   JA 5 .   ? 66.212 -31.980 59.750  1.00 40.21 ? 447  HOH   C O   1 
HETATM 9500  O  O   . HOH   JA 5 .   ? 38.714 -0.900  52.390  1.00 36.29 ? 448  HOH   C O   1 
HETATM 9501  O  O   . HOH   JA 5 .   ? 51.865 -27.176 67.094  1.00 51.18 ? 449  HOH   C O   1 
HETATM 9502  O  O   . HOH   JA 5 .   ? 68.641 -27.725 35.838  1.00 51.01 ? 450  HOH   C O   1 
HETATM 9503  O  O   . HOH   JA 5 .   ? 58.512 4.040   33.761  1.00 18.48 ? 451  HOH   C O   1 
HETATM 9504  O  O   . HOH   JA 5 .   ? 53.510 0.119   50.411  1.00 46.33 ? 452  HOH   C O   1 
HETATM 9505  O  O   . HOH   JA 5 .   ? 54.805 -27.786 60.110  1.00 23.33 ? 453  HOH   C O   1 
HETATM 9506  O  O   . HOH   JA 5 .   ? 53.247 1.494   37.020  1.00 26.93 ? 454  HOH   C O   1 
HETATM 9507  O  O   . HOH   JA 5 .   ? 59.093 -28.070 44.945  1.00 24.80 ? 455  HOH   C O   1 
HETATM 9508  O  O   . HOH   JA 5 .   ? 69.874 -17.532 65.063  1.00 19.04 ? 456  HOH   C O   1 
HETATM 9509  O  O   . HOH   JA 5 .   ? 67.106 0.053   48.437  1.00 48.37 ? 457  HOH   C O   1 
HETATM 9510  O  O   . HOH   JA 5 .   ? 41.685 7.712   41.220  1.00 47.48 ? 458  HOH   C O   1 
HETATM 9511  O  O   . HOH   JA 5 .   ? 60.562 -18.666 25.861  1.00 40.43 ? 459  HOH   C O   1 
HETATM 9512  O  O   . HOH   JA 5 .   ? 34.491 -30.157 44.612  1.00 39.50 ? 460  HOH   C O   1 
HETATM 9513  O  O   . HOH   JA 5 .   ? 48.530 2.562   37.154  1.00 61.39 ? 461  HOH   C O   1 
HETATM 9514  O  O   . HOH   JA 5 .   ? 58.926 -25.142 27.260  1.00 33.19 ? 462  HOH   C O   1 
HETATM 9515  O  O   . HOH   JA 5 .   ? 46.872 -31.123 65.796  1.00 45.60 ? 463  HOH   C O   1 
HETATM 9516  O  O   . HOH   JA 5 .   ? 41.010 -32.350 56.039  1.00 31.79 ? 464  HOH   C O   1 
HETATM 9517  O  O   . HOH   JA 5 .   ? 70.049 -15.530 53.918  1.00 26.13 ? 465  HOH   C O   1 
HETATM 9518  O  O   . HOH   JA 5 .   ? 61.343 -12.515 53.047  1.00 18.03 ? 466  HOH   C O   1 
HETATM 9519  O  O   . HOH   JA 5 .   ? 30.079 -30.176 49.754  1.00 40.88 ? 467  HOH   C O   1 
HETATM 9520  O  O   . HOH   JA 5 .   ? 36.406 -35.020 52.319  1.00 45.13 ? 468  HOH   C O   1 
HETATM 9521  O  O   . HOH   JA 5 .   ? 29.673 -24.785 54.342  1.00 57.88 ? 469  HOH   C O   1 
HETATM 9522  O  O   . HOH   JA 5 .   ? 30.296 -21.526 47.058  1.00 30.84 ? 470  HOH   C O   1 
HETATM 9523  O  O   . HOH   JA 5 .   ? 67.592 -17.188 50.764  1.00 16.64 ? 471  HOH   C O   1 
HETATM 9524  O  O   . HOH   JA 5 .   ? 49.532 -18.895 65.342  1.00 22.75 ? 472  HOH   C O   1 
HETATM 9525  O  O   . HOH   JA 5 .   ? 69.517 -26.850 45.067  1.00 30.79 ? 473  HOH   C O   1 
HETATM 9526  O  O   . HOH   JA 5 .   ? 71.751 -25.486 60.654  1.00 32.19 ? 474  HOH   C O   1 
HETATM 9527  O  O   . HOH   JA 5 .   ? 45.307 -34.183 59.223  1.00 37.63 ? 475  HOH   C O   1 
HETATM 9528  O  O   . HOH   JA 5 .   ? 49.770 -22.971 65.705  1.00 22.21 ? 476  HOH   C O   1 
HETATM 9529  O  O   . HOH   JA 5 .   ? 57.099 -6.123  48.830  1.00 27.71 ? 477  HOH   C O   1 
HETATM 9530  O  O   . HOH   JA 5 .   ? 58.778 -10.367 56.648  1.00 20.30 ? 478  HOH   C O   1 
HETATM 9531  O  O   . HOH   JA 5 .   ? 72.148 -22.664 45.166  1.00 31.86 ? 479  HOH   C O   1 
HETATM 9532  O  O   . HOH   JA 5 .   ? 41.568 -22.257 38.315  1.00 25.39 ? 480  HOH   C O   1 
HETATM 9533  O  O   . HOH   JA 5 .   ? 36.837 -17.890 55.417  1.00 44.59 ? 481  HOH   C O   1 
HETATM 9534  O  O   . HOH   JA 5 .   ? 67.024 -11.249 32.333  1.00 46.40 ? 482  HOH   C O   1 
HETATM 9535  O  O   . HOH   JA 5 .   ? 53.078 -33.055 53.126  1.00 29.81 ? 483  HOH   C O   1 
HETATM 9536  O  O   . HOH   JA 5 .   ? 61.805 -25.317 38.486  1.00 22.44 ? 484  HOH   C O   1 
HETATM 9537  O  O   . HOH   JA 5 .   ? 62.368 -33.572 42.009  1.00 28.92 ? 485  HOH   C O   1 
HETATM 9538  O  O   . HOH   JA 5 .   ? 47.539 -36.649 47.779  1.00 27.81 ? 486  HOH   C O   1 
HETATM 9539  O  O   . HOH   JA 5 .   ? 72.772 -17.471 56.523  1.00 29.35 ? 487  HOH   C O   1 
HETATM 9540  O  O   . HOH   JA 5 .   ? 48.348 -0.999  42.697  1.00 26.14 ? 488  HOH   C O   1 
HETATM 9541  O  O   . HOH   JA 5 .   ? 66.053 -6.975  28.906  1.00 45.61 ? 489  HOH   C O   1 
HETATM 9542  O  O   . HOH   JA 5 .   ? 34.379 -17.768 42.860  1.00 33.78 ? 490  HOH   C O   1 
HETATM 9543  O  O   . HOH   JA 5 .   ? 51.486 -9.522  32.218  1.00 32.24 ? 491  HOH   C O   1 
HETATM 9544  O  O   . HOH   JA 5 .   ? 68.389 -26.748 54.734  1.00 29.52 ? 492  HOH   C O   1 
HETATM 9545  O  O   . HOH   JA 5 .   ? 54.626 -6.892  61.540  1.00 22.12 ? 493  HOH   C O   1 
HETATM 9546  O  O   . HOH   JA 5 .   ? 69.364 -21.229 33.984  1.00 32.87 ? 494  HOH   C O   1 
HETATM 9547  O  O   . HOH   JA 5 .   ? 43.083 9.121   43.849  1.00 35.06 ? 495  HOH   C O   1 
HETATM 9548  O  O   . HOH   JA 5 .   ? 48.090 -5.843  63.962  1.00 28.32 ? 496  HOH   C O   1 
HETATM 9549  O  O   . HOH   JA 5 .   ? 50.716 6.748   46.317  1.00 26.27 ? 497  HOH   C O   1 
HETATM 9550  O  O   . HOH   JA 5 .   ? 47.961 -15.946 31.825  1.00 42.76 ? 498  HOH   C O   1 
HETATM 9551  O  O   . HOH   JA 5 .   ? 46.737 4.003   43.536  1.00 27.48 ? 499  HOH   C O   1 
HETATM 9552  O  O   . HOH   JA 5 .   ? 64.751 0.557   42.478  1.00 31.54 ? 500  HOH   C O   1 
HETATM 9553  O  O   . HOH   JA 5 .   ? 70.977 -18.301 62.631  1.00 23.55 ? 501  HOH   C O   1 
HETATM 9554  O  O   . HOH   JA 5 .   ? 44.007 -20.314 31.059  1.00 36.49 ? 502  HOH   C O   1 
HETATM 9555  O  O   . HOH   JA 5 .   ? 45.671 -27.842 63.133  1.00 28.20 ? 503  HOH   C O   1 
HETATM 9556  O  O   . HOH   JA 5 .   ? 54.639 -28.847 67.128  1.00 50.29 ? 504  HOH   C O   1 
HETATM 9557  O  O   . HOH   JA 5 .   ? 51.220 -1.801  53.327  1.00 24.03 ? 505  HOH   C O   1 
HETATM 9558  O  O   . HOH   JA 5 .   ? 72.106 -13.910 50.831  1.00 28.29 ? 506  HOH   C O   1 
HETATM 9559  O  O   . HOH   JA 5 .   ? 50.581 -12.201 65.804  1.00 54.24 ? 507  HOH   C O   1 
HETATM 9560  O  O   . HOH   JA 5 .   ? 38.690 -12.849 55.599  1.00 22.19 ? 508  HOH   C O   1 
HETATM 9561  O  O   . HOH   JA 5 .   ? 59.700 -0.366  51.413  1.00 39.98 ? 509  HOH   C O   1 
HETATM 9562  O  O   . HOH   JA 5 .   ? 37.864 -30.873 52.926  1.00 45.77 ? 510  HOH   C O   1 
HETATM 9563  O  O   . HOH   JA 5 .   ? 38.848 -5.011  54.647  1.00 27.91 ? 511  HOH   C O   1 
HETATM 9564  O  O   . HOH   JA 5 .   ? 55.805 -6.852  57.875  1.00 32.40 ? 512  HOH   C O   1 
HETATM 9565  O  O   . HOH   JA 5 .   ? 35.907 -21.986 35.371  1.00 44.37 ? 513  HOH   C O   1 
HETATM 9566  O  O   . HOH   JA 5 .   ? 38.911 -2.277  42.439  1.00 38.53 ? 514  HOH   C O   1 
HETATM 9567  O  O   . HOH   JA 5 .   ? 48.171 -33.751 40.294  1.00 34.91 ? 515  HOH   C O   1 
HETATM 9568  O  O   . HOH   JA 5 .   ? 46.314 -21.148 31.866  1.00 39.00 ? 516  HOH   C O   1 
HETATM 9569  O  O   . HOH   JA 5 .   ? 44.931 -32.417 51.171  1.00 28.19 ? 517  HOH   C O   1 
HETATM 9570  O  O   . HOH   JA 5 .   ? 61.259 -28.652 28.242  1.00 52.82 ? 518  HOH   C O   1 
HETATM 9571  O  O   . HOH   JA 5 .   ? 36.945 -27.406 38.090  1.00 53.40 ? 519  HOH   C O   1 
HETATM 9572  O  O   . HOH   JA 5 .   ? 43.621 -14.253 56.516  1.00 27.55 ? 520  HOH   C O   1 
HETATM 9573  O  O   . HOH   JA 5 .   ? 69.024 -2.746  38.724  1.00 40.97 ? 521  HOH   C O   1 
HETATM 9574  O  O   . HOH   JA 5 .   ? 51.636 -19.754 27.782  1.00 41.89 ? 522  HOH   C O   1 
HETATM 9575  O  O   . HOH   JA 5 .   ? 45.334 -34.218 40.313  1.00 48.13 ? 523  HOH   C O   1 
HETATM 9576  O  O   . HOH   JA 5 .   ? 37.972 -8.774  57.346  1.00 29.85 ? 524  HOH   C O   1 
HETATM 9577  O  O   . HOH   JA 5 .   ? 59.782 -3.644  49.000  1.00 28.32 ? 525  HOH   C O   1 
HETATM 9578  O  O   . HOH   JA 5 .   ? 50.295 2.235   51.275  1.00 39.75 ? 526  HOH   C O   1 
HETATM 9579  O  O   . HOH   JA 5 .   ? 51.095 -1.502  36.705  1.00 25.48 ? 527  HOH   C O   1 
HETATM 9580  O  O   . HOH   JA 5 .   ? 61.941 -26.170 60.177  1.00 19.61 ? 528  HOH   C O   1 
HETATM 9581  O  O   . HOH   JA 5 .   ? 59.649 -12.685 55.308  1.00 19.82 ? 529  HOH   C O   1 
HETATM 9582  O  O   . HOH   JA 5 .   ? 46.135 -28.113 39.800  1.00 29.05 ? 530  HOH   C O   1 
HETATM 9583  O  O   . HOH   JA 5 .   ? 41.890 -2.689  39.763  1.00 37.65 ? 531  HOH   C O   1 
HETATM 9584  O  O   . HOH   JA 5 .   ? 47.255 -22.581 39.404  1.00 22.32 ? 532  HOH   C O   1 
HETATM 9585  O  O   . HOH   JA 5 .   ? 32.272 -20.929 45.076  1.00 30.82 ? 533  HOH   C O   1 
HETATM 9586  O  O   . HOH   JA 5 .   ? 60.609 -2.903  46.627  1.00 35.81 ? 534  HOH   C O   1 
HETATM 9587  O  O   . HOH   JA 5 .   ? 73.266 -16.322 51.105  1.00 42.07 ? 535  HOH   C O   1 
HETATM 9588  O  O   . HOH   JA 5 .   ? 72.424 -7.624  38.082  1.00 27.78 ? 536  HOH   C O   1 
HETATM 9589  O  O   . HOH   JA 5 .   ? 73.864 -16.218 36.964  1.00 53.62 ? 537  HOH   C O   1 
HETATM 9590  O  O   . HOH   JA 5 .   ? 75.753 -8.139  41.290  1.00 36.35 ? 538  HOH   C O   1 
HETATM 9591  O  O   . HOH   JA 5 .   ? 31.668 -11.588 45.491  1.00 44.70 ? 539  HOH   C O   1 
HETATM 9592  O  O   . HOH   JA 5 .   ? 67.862 -13.986 34.302  1.00 34.22 ? 540  HOH   C O   1 
HETATM 9593  O  O   . HOH   JA 5 .   ? 55.253 -9.311  29.681  1.00 29.02 ? 541  HOH   C O   1 
HETATM 9594  O  O   . HOH   JA 5 .   ? 32.018 -27.963 52.712  1.00 38.51 ? 542  HOH   C O   1 
HETATM 9595  O  O   . HOH   JA 5 .   ? 73.167 -22.416 54.523  1.00 25.07 ? 543  HOH   C O   1 
HETATM 9596  O  O   . HOH   JA 5 .   ? 68.569 -9.698  55.358  1.00 20.55 ? 544  HOH   C O   1 
HETATM 9597  O  O   . HOH   JA 5 .   ? 58.787 -6.896  59.041  1.00 34.00 ? 545  HOH   C O   1 
HETATM 9598  O  O   . HOH   JA 5 .   ? 77.435 -13.486 42.452  1.00 33.84 ? 546  HOH   C O   1 
HETATM 9599  O  O   . HOH   JA 5 .   ? 52.753 -16.503 66.064  1.00 32.25 ? 547  HOH   C O   1 
HETATM 9600  O  O   . HOH   JA 5 .   ? 57.976 -16.814 64.122  1.00 16.62 ? 548  HOH   C O   1 
HETATM 9601  O  O   . HOH   JA 5 .   ? 45.910 -0.716  44.209  1.00 34.15 ? 549  HOH   C O   1 
HETATM 9602  O  O   . HOH   JA 5 .   ? 56.921 -30.827 59.321  1.00 37.12 ? 550  HOH   C O   1 
HETATM 9603  O  O   . HOH   JA 5 .   ? 57.483 -29.933 35.138  1.00 61.99 ? 551  HOH   C O   1 
HETATM 9604  O  O   . HOH   JA 5 .   ? 45.284 3.274   53.109  1.00 44.32 ? 552  HOH   C O   1 
HETATM 9605  O  O   . HOH   JA 5 .   ? 63.328 -1.724  46.144  1.00 30.84 ? 553  HOH   C O   1 
HETATM 9606  O  O   . HOH   JA 5 .   ? 77.996 -20.525 49.767  1.00 46.05 ? 554  HOH   C O   1 
HETATM 9607  O  O   . HOH   JA 5 .   ? 52.218 -5.928  31.495  1.00 33.85 ? 555  HOH   C O   1 
HETATM 9608  O  O   . HOH   JA 5 .   ? 59.565 -16.027 25.461  1.00 51.26 ? 556  HOH   C O   1 
HETATM 9609  O  O   . HOH   JA 5 .   ? 46.877 1.831   45.229  1.00 26.96 ? 557  HOH   C O   1 
HETATM 9610  O  O   . HOH   JA 5 .   ? 62.959 -30.281 60.307  1.00 25.93 ? 558  HOH   C O   1 
HETATM 9611  O  O   . HOH   JA 5 .   ? 59.669 -5.319  45.639  1.00 30.20 ? 559  HOH   C O   1 
HETATM 9612  O  O   . HOH   JA 5 .   ? 25.810 -21.929 47.472  1.00 55.15 ? 560  HOH   C O   1 
HETATM 9613  O  O   . HOH   JA 5 .   ? 43.569 -12.524 33.076  1.00 52.21 ? 561  HOH   C O   1 
HETATM 9614  O  O   . HOH   JA 5 .   ? 53.153 -1.621  60.302  1.00 31.85 ? 562  HOH   C O   1 
HETATM 9615  O  O   . HOH   JA 5 .   ? 69.224 -30.249 41.194  1.00 50.06 ? 563  HOH   C O   1 
HETATM 9616  O  O   . HOH   JA 5 .   ? 46.725 -2.519  46.007  1.00 26.18 ? 564  HOH   C O   1 
HETATM 9617  O  O   . HOH   JA 5 .   ? 61.770 -6.282  30.864  1.00 52.28 ? 565  HOH   C O   1 
HETATM 9618  O  O   . HOH   JA 5 .   ? 70.866 -29.926 62.630  1.00 50.26 ? 566  HOH   C O   1 
HETATM 9619  O  O   . HOH   JA 5 .   ? 41.012 -7.527  36.711  1.00 36.29 ? 567  HOH   C O   1 
HETATM 9620  O  O   . HOH   JA 5 .   ? 69.886 -25.347 38.464  1.00 35.85 ? 568  HOH   C O   1 
HETATM 9621  O  O   . HOH   JA 5 .   ? 43.379 4.095   52.471  1.00 46.44 ? 569  HOH   C O   1 
HETATM 9622  O  O   . HOH   JA 5 .   ? 32.912 -8.815  53.020  1.00 38.50 ? 570  HOH   C O   1 
HETATM 9623  O  O   . HOH   JA 5 .   ? 84.747 -9.956  48.222  1.00 40.55 ? 571  HOH   C O   1 
HETATM 9624  O  O   . HOH   JA 5 .   ? 44.755 -38.008 41.361  1.00 47.23 ? 572  HOH   C O   1 
HETATM 9625  O  O   . HOH   JA 5 .   ? 47.605 -31.849 53.347  1.00 46.43 ? 573  HOH   C O   1 
HETATM 9626  O  O   . HOH   JA 5 .   ? 36.342 -18.686 36.738  1.00 40.61 ? 574  HOH   C O   1 
HETATM 9627  O  O   . HOH   JA 5 .   ? 33.169 -27.861 57.014  1.00 51.93 ? 575  HOH   C O   1 
HETATM 9628  O  O   . HOH   JA 5 .   ? 48.149 -33.960 59.304  1.00 25.46 ? 576  HOH   C O   1 
HETATM 9629  O  O   . HOH   JA 5 .   ? 32.878 -19.086 53.179  1.00 52.47 ? 577  HOH   C O   1 
HETATM 9630  O  O   . HOH   JA 5 .   ? 64.698 -25.809 49.600  1.00 37.68 ? 578  HOH   C O   1 
HETATM 9631  O  O   . HOH   JA 5 .   ? 56.121 -34.654 46.082  1.00 34.52 ? 579  HOH   C O   1 
HETATM 9632  O  O   . HOH   JA 5 .   ? 60.809 -17.873 46.846  1.00 26.33 ? 580  HOH   C O   1 
HETATM 9633  O  O   . HOH   JA 5 .   ? 48.876 -33.591 55.819  1.00 38.51 ? 581  HOH   C O   1 
HETATM 9634  O  O   . HOH   JA 5 .   ? 44.799 -23.196 64.808  1.00 40.99 ? 582  HOH   C O   1 
HETATM 9635  O  O   . HOH   JA 5 .   ? 69.583 -19.165 50.677  1.00 18.44 ? 583  HOH   C O   1 
HETATM 9636  O  O   . HOH   JA 5 .   ? 72.586 -18.296 39.246  1.00 29.57 ? 584  HOH   C O   1 
HETATM 9637  O  O   . HOH   JA 5 .   ? 39.905 -22.471 31.661  1.00 40.72 ? 585  HOH   C O   1 
HETATM 9638  O  O   . HOH   JA 5 .   ? 72.605 -22.358 67.453  1.00 52.28 ? 586  HOH   C O   1 
HETATM 9639  O  O   . HOH   JA 5 .   ? 33.138 -31.654 46.766  1.00 43.90 ? 587  HOH   C O   1 
HETATM 9640  O  O   . HOH   JA 5 .   ? 68.548 -23.773 47.650  1.00 26.03 ? 588  HOH   C O   1 
HETATM 9641  O  O   . HOH   JA 5 .   ? 42.910 5.014   50.046  1.00 51.78 ? 589  HOH   C O   1 
HETATM 9642  O  O   . HOH   JA 5 .   ? 71.538 -21.733 38.037  1.00 34.97 ? 590  HOH   C O   1 
HETATM 9643  O  O   . HOH   JA 5 .   ? 55.312 -30.008 31.518  1.00 49.21 ? 591  HOH   C O   1 
HETATM 9644  O  O   . HOH   JA 5 .   ? 36.282 -8.798  61.399  1.00 53.70 ? 592  HOH   C O   1 
HETATM 9645  O  O   . HOH   JA 5 .   ? 49.399 -39.291 44.465  1.00 44.43 ? 593  HOH   C O   1 
HETATM 9646  O  O   . HOH   JA 5 .   ? 40.044 -20.934 53.825  1.00 24.73 ? 594  HOH   C O   1 
HETATM 9647  O  O   . HOH   JA 5 .   ? 61.045 -16.648 49.322  1.00 18.20 ? 595  HOH   C O   1 
HETATM 9648  O  O   . HOH   JA 5 .   ? 40.824 -31.370 53.531  1.00 27.82 ? 596  HOH   C O   1 
HETATM 9649  O  O   . HOH   JA 5 .   ? 36.402 -25.394 57.533  1.00 52.29 ? 597  HOH   C O   1 
HETATM 9650  O  O   . HOH   JA 5 .   ? 64.882 -28.846 33.903  1.00 37.58 ? 598  HOH   C O   1 
HETATM 9651  O  O   . HOH   JA 5 .   ? 39.746 -31.310 41.286  1.00 40.70 ? 599  HOH   C O   1 
HETATM 9652  O  O   . HOH   JA 5 .   ? 40.853 3.644   48.454  1.00 41.40 ? 600  HOH   C O   1 
HETATM 9653  O  O   . HOH   JA 5 .   ? 56.884 -28.277 48.522  1.00 24.76 ? 601  HOH   C O   1 
HETATM 9654  O  O   . HOH   JA 5 .   ? 36.064 -18.791 41.408  1.00 42.72 ? 602  HOH   C O   1 
HETATM 9655  O  O   . HOH   JA 5 .   ? 40.231 -36.066 41.457  1.00 44.99 ? 603  HOH   C O   1 
HETATM 9656  O  O   . HOH   JA 5 .   ? 50.015 -13.833 29.362  1.00 40.05 ? 604  HOH   C O   1 
HETATM 9657  O  O   . HOH   JA 5 .   ? 67.859 -20.415 59.196  1.00 22.46 ? 605  HOH   C O   1 
HETATM 9658  O  O   . HOH   JA 5 .   ? 53.873 -2.438  56.246  1.00 32.11 ? 606  HOH   C O   1 
HETATM 9659  O  O   . HOH   JA 5 .   ? 46.699 -19.908 66.879  1.00 48.56 ? 607  HOH   C O   1 
HETATM 9660  O  O   . HOH   JA 5 .   ? 68.239 -26.688 50.972  1.00 38.65 ? 608  HOH   C O   1 
HETATM 9661  O  O   . HOH   JA 5 .   ? 70.990 -6.431  50.989  1.00 48.86 ? 609  HOH   C O   1 
HETATM 9662  O  O   . HOH   JA 5 .   ? 48.045 -29.543 35.659  1.00 46.61 ? 610  HOH   C O   1 
HETATM 9663  O  O   . HOH   JA 5 .   ? 62.859 -31.301 63.092  1.00 33.07 ? 611  HOH   C O   1 
HETATM 9664  O  O   . HOH   JA 5 .   ? 43.653 -36.618 52.013  1.00 35.01 ? 612  HOH   C O   1 
HETATM 9665  O  O   . HOH   JA 5 .   ? 66.017 -32.819 42.705  1.00 32.76 ? 613  HOH   C O   1 
HETATM 9666  O  O   . HOH   JA 5 .   ? 58.539 -25.878 67.471  1.00 30.04 ? 614  HOH   C O   1 
HETATM 9667  O  O   . HOH   JA 5 .   ? 43.886 -15.089 31.433  1.00 51.69 ? 615  HOH   C O   1 
HETATM 9668  O  O   . HOH   JA 5 .   ? 27.823 -21.384 45.506  1.00 59.66 ? 616  HOH   C O   1 
HETATM 9669  O  O   . HOH   JA 5 .   ? 69.809 -12.549 36.688  1.00 48.30 ? 617  HOH   C O   1 
HETATM 9670  O  O   . HOH   JA 5 .   ? 35.992 -22.043 53.435  1.00 42.64 ? 618  HOH   C O   1 
HETATM 9671  O  O   . HOH   JA 5 .   ? 73.534 -7.379  49.598  1.00 47.37 ? 619  HOH   C O   1 
HETATM 9672  O  O   . HOH   JA 5 .   ? 26.126 -29.524 46.704  1.00 48.09 ? 620  HOH   C O   1 
HETATM 9673  O  O   . HOH   JA 5 .   ? 71.662 -21.214 64.608  1.00 32.26 ? 621  HOH   C O   1 
HETATM 9674  O  O   . HOH   JA 5 .   ? 41.514 -14.448 34.611  1.00 40.68 ? 622  HOH   C O   1 
HETATM 9675  O  O   . HOH   JA 5 .   ? 37.137 -11.515 39.099  1.00 38.32 ? 623  HOH   C O   1 
HETATM 9676  O  O   . HOH   JA 5 .   ? 66.652 -29.382 61.917  1.00 37.23 ? 624  HOH   C O   1 
HETATM 9677  O  O   . HOH   JA 5 .   ? 39.063 -30.945 44.437  1.00 35.44 ? 625  HOH   C O   1 
HETATM 9678  O  O   . HOH   JA 5 .   ? 74.201 -23.817 51.422  1.00 32.99 ? 626  HOH   C O   1 
HETATM 9679  O  O   . HOH   JA 5 .   ? 71.458 -17.690 52.335  1.00 31.45 ? 627  HOH   C O   1 
HETATM 9680  O  O   . HOH   JA 5 .   ? 56.927 -30.155 37.368  1.00 46.19 ? 628  HOH   C O   1 
HETATM 9681  O  O   . HOH   JA 5 .   ? 62.835 -12.112 57.650  1.00 16.37 ? 629  HOH   C O   1 
HETATM 9682  O  O   . HOH   JA 5 .   ? 40.054 -0.851  40.329  1.00 53.41 ? 630  HOH   C O   1 
HETATM 9683  O  O   . HOH   JA 5 .   ? 50.481 -27.212 60.206  1.00 21.96 ? 631  HOH   C O   1 
HETATM 9684  O  O   . HOH   JA 5 .   ? 40.281 -25.613 58.161  1.00 28.70 ? 632  HOH   C O   1 
HETATM 9685  O  O   . HOH   JA 5 .   ? 68.213 -23.713 34.085  1.00 28.81 ? 633  HOH   C O   1 
HETATM 9686  O  O   . HOH   JA 5 .   ? 46.853 -3.515  35.511  1.00 50.76 ? 634  HOH   C O   1 
HETATM 9687  O  O   . HOH   JA 5 .   ? 44.998 1.942   55.523  1.00 43.66 ? 635  HOH   C O   1 
HETATM 9688  O  O   . HOH   JA 5 .   ? 75.180 -18.849 52.935  1.00 49.05 ? 636  HOH   C O   1 
HETATM 9689  O  O   . HOH   JA 5 .   ? 71.903 -20.519 49.708  1.00 29.86 ? 637  HOH   C O   1 
HETATM 9690  O  O   . HOH   JA 5 .   ? 42.957 -29.274 67.020  1.00 47.89 ? 638  HOH   C O   1 
HETATM 9691  O  O   . HOH   JA 5 .   ? 59.635 -6.329  48.381  1.00 24.13 ? 639  HOH   C O   1 
HETATM 9692  O  O   . HOH   JA 5 .   ? 66.953 -9.023  28.877  1.00 47.42 ? 640  HOH   C O   1 
HETATM 9693  O  O   . HOH   JA 5 .   ? 34.910 -30.932 39.868  1.00 43.56 ? 641  HOH   C O   1 
HETATM 9694  O  O   . HOH   JA 5 .   ? 73.550 -14.066 57.344  1.00 22.60 ? 642  HOH   C O   1 
HETATM 9695  O  O   . HOH   JA 5 .   ? 56.128 -34.306 41.231  1.00 28.94 ? 643  HOH   C O   1 
HETATM 9696  O  O   . HOH   JA 5 .   ? 73.688 -18.631 62.943  1.00 22.38 ? 644  HOH   C O   1 
HETATM 9697  O  O   . HOH   JA 5 .   ? 35.036 -34.192 47.166  1.00 57.51 ? 645  HOH   C O   1 
HETATM 9698  O  O   . HOH   JA 5 .   ? 42.158 -32.103 51.009  1.00 31.02 ? 646  HOH   C O   1 
HETATM 9699  O  O   . HOH   JA 5 .   ? 39.401 -15.156 55.231  1.00 45.78 ? 647  HOH   C O   1 
HETATM 9700  O  O   . HOH   JA 5 .   ? 77.454 -8.435  49.846  1.00 51.91 ? 648  HOH   C O   1 
HETATM 9701  O  O   . HOH   JA 5 .   ? 36.428 -34.208 45.202  1.00 58.23 ? 649  HOH   C O   1 
HETATM 9702  O  O   . HOH   JA 5 .   ? 30.780 -25.417 40.592  1.00 53.70 ? 650  HOH   C O   1 
HETATM 9703  O  O   . HOH   JA 5 .   ? 67.974 -7.254  32.699  1.00 44.15 ? 651  HOH   C O   1 
HETATM 9704  O  O   . HOH   JA 5 .   ? 48.685 -20.074 30.434  1.00 33.31 ? 652  HOH   C O   1 
HETATM 9705  O  O   . HOH   JA 5 .   ? 66.780 -30.884 45.452  1.00 39.03 ? 653  HOH   C O   1 
HETATM 9706  O  O   . HOH   JA 5 .   ? 39.023 -29.554 60.596  1.00 62.53 ? 654  HOH   C O   1 
HETATM 9707  O  O   . HOH   JA 5 .   ? 52.082 -9.664  67.243  1.00 52.71 ? 655  HOH   C O   1 
HETATM 9708  O  O   . HOH   JA 5 .   ? 33.623 -24.111 37.632  1.00 52.77 ? 656  HOH   C O   1 
HETATM 9709  O  O   . HOH   JA 5 .   ? 38.719 -26.524 37.166  1.00 53.49 ? 657  HOH   C O   1 
HETATM 9710  O  O   . HOH   JA 5 .   ? 72.183 -29.648 57.566  1.00 30.01 ? 658  HOH   C O   1 
HETATM 9711  O  O   . HOH   JA 5 .   ? 51.335 -24.866 26.692  1.00 45.12 ? 659  HOH   C O   1 
HETATM 9712  O  O   . HOH   JA 5 .   ? 69.745 -1.500  43.320  1.00 30.84 ? 660  HOH   C O   1 
HETATM 9713  O  O   . HOH   JA 5 .   ? 45.500 -1.813  62.188  1.00 36.20 ? 661  HOH   C O   1 
HETATM 9714  O  O   . HOH   JA 5 .   ? 65.953 1.004   37.416  1.00 37.09 ? 662  HOH   C O   1 
HETATM 9715  O  O   . HOH   JA 5 .   ? 70.095 -19.361 59.907  1.00 26.36 ? 663  HOH   C O   1 
HETATM 9716  O  O   . HOH   JA 5 .   ? 42.911 7.643   48.461  1.00 43.72 ? 664  HOH   C O   1 
HETATM 9717  O  O   . HOH   JA 5 .   ? 73.414 -10.601 35.539  1.00 53.03 ? 665  HOH   C O   1 
HETATM 9718  O  O   . HOH   JA 5 .   ? 59.774 0.072   48.764  1.00 44.45 ? 666  HOH   C O   1 
HETATM 9719  O  O   . HOH   JA 5 .   ? 55.164 -10.437 25.583  1.00 47.36 ? 667  HOH   C O   1 
HETATM 9720  O  O   . HOH   JA 5 .   ? 56.471 -33.261 38.616  1.00 52.77 ? 668  HOH   C O   1 
HETATM 9721  O  O   . HOH   JA 5 .   ? 48.003 -4.537  29.701  1.00 51.81 ? 669  HOH   C O   1 
HETATM 9722  O  O   . HOH   JA 5 .   ? 41.414 -17.084 59.787  1.00 48.31 ? 670  HOH   C O   1 
HETATM 9723  O  O   . HOH   JA 5 .   ? 39.542 -4.595  38.216  1.00 39.83 ? 671  HOH   C O   1 
HETATM 9724  O  O   . HOH   JA 5 .   ? 69.508 -13.661 52.086  1.00 29.25 ? 672  HOH   C O   1 
HETATM 9725  O  O   . HOH   JA 5 .   ? 57.136 -21.363 23.410  1.00 43.60 ? 673  HOH   C O   1 
HETATM 9726  O  O   . HOH   JA 5 .   ? 43.266 0.696   55.548  1.00 43.46 ? 674  HOH   C O   1 
HETATM 9727  O  O   . HOH   JA 5 .   ? 37.698 -13.196 58.132  1.00 54.54 ? 675  HOH   C O   1 
HETATM 9728  O  O   . HOH   JA 5 .   ? 59.194 -27.209 59.554  1.00 29.35 ? 676  HOH   C O   1 
HETATM 9729  O  O   . HOH   JA 5 .   ? 57.834 -18.576 66.207  1.00 15.56 ? 677  HOH   C O   1 
HETATM 9730  O  O   . HOH   JA 5 .   ? 33.185 -9.764  45.886  1.00 52.36 ? 678  HOH   C O   1 
HETATM 9731  O  O   . HOH   JA 5 .   ? 67.254 -14.781 60.455  1.00 15.42 ? 679  HOH   C O   1 
HETATM 9732  O  O   . HOH   JA 5 .   ? 54.236 -32.938 55.864  1.00 31.06 ? 680  HOH   C O   1 
HETATM 9733  O  O   . HOH   JA 5 .   ? 57.472 -30.732 49.123  1.00 27.00 ? 681  HOH   C O   1 
HETATM 9734  O  O   . HOH   JA 5 .   ? 56.925 -3.425  49.357  1.00 43.63 ? 682  HOH   C O   1 
HETATM 9735  O  O   . HOH   JA 5 .   ? 61.476 -26.329 67.322  1.00 39.89 ? 683  HOH   C O   1 
HETATM 9736  O  O   . HOH   JA 5 .   ? 38.632 -24.363 56.351  1.00 41.10 ? 684  HOH   C O   1 
HETATM 9737  O  O   . HOH   JA 5 .   ? 83.282 -12.942 51.042  1.00 39.11 ? 685  HOH   C O   1 
HETATM 9738  O  O   . HOH   JA 5 .   ? 52.952 -4.511  63.461  1.00 51.32 ? 686  HOH   C O   1 
HETATM 9739  O  O   . HOH   JA 5 .   ? 72.356 -26.067 64.624  1.00 45.50 ? 687  HOH   C O   1 
HETATM 9740  O  O   . HOH   JA 5 .   ? 62.618 -15.914 27.995  1.00 46.63 ? 688  HOH   C O   1 
HETATM 9741  O  O   . HOH   JA 5 .   ? 40.198 -24.820 37.000  1.00 45.08 ? 689  HOH   C O   1 
HETATM 9742  O  O   . HOH   JA 5 .   ? 52.496 -37.282 42.370  1.00 51.15 ? 690  HOH   C O   1 
HETATM 9743  O  O   . HOH   JA 5 .   ? 54.564 -24.549 67.222  1.00 41.93 ? 691  HOH   C O   1 
HETATM 9744  O  O   . HOH   JA 5 .   ? 53.433 4.335   46.887  1.00 43.54 ? 692  HOH   C O   1 
HETATM 9745  O  O   . HOH   JA 5 .   ? 49.044 -10.397 67.464  1.00 58.54 ? 693  HOH   C O   1 
HETATM 9746  O  O   . HOH   JA 5 .   ? 44.545 -27.293 66.353  1.00 46.53 ? 694  HOH   C O   1 
HETATM 9747  O  O   . HOH   JA 5 .   ? 73.888 -20.007 57.182  1.00 27.92 ? 695  HOH   C O   1 
HETATM 9748  O  O   . HOH   JA 5 .   ? 75.036 -7.729  38.714  1.00 53.82 ? 696  HOH   C O   1 
HETATM 9749  O  O   . HOH   JA 5 .   ? 68.314 -21.978 28.750  1.00 54.61 ? 697  HOH   C O   1 
HETATM 9750  O  O   . HOH   JA 5 .   ? 49.226 -31.663 66.317  1.00 49.95 ? 698  HOH   C O   1 
HETATM 9751  O  O   . HOH   JA 5 .   ? 32.784 -15.655 54.573  1.00 50.96 ? 699  HOH   C O   1 
HETATM 9752  O  O   . HOH   JA 5 .   ? 64.659 -12.563 59.791  1.00 17.46 ? 700  HOH   C O   1 
HETATM 9753  O  O   . HOH   JA 5 .   ? 37.006 -2.131  45.978  1.00 48.14 ? 701  HOH   C O   1 
HETATM 9754  O  O   . HOH   JA 5 .   ? 57.354 4.751   46.085  1.00 28.94 ? 702  HOH   C O   1 
HETATM 9755  O  O   . HOH   JA 5 .   ? 52.711 5.479   31.893  1.00 48.76 ? 703  HOH   C O   1 
HETATM 9756  O  O   . HOH   JA 5 .   ? 55.581 -28.389 35.364  1.00 43.23 ? 704  HOH   C O   1 
HETATM 9757  O  O   . HOH   JA 5 .   ? 73.279 -27.784 59.782  1.00 34.17 ? 705  HOH   C O   1 
HETATM 9758  O  O   . HOH   JA 5 .   ? 30.892 -18.674 43.807  1.00 40.58 ? 706  HOH   C O   1 
HETATM 9759  O  O   . HOH   JA 5 .   ? 43.671 -25.722 63.516  1.00 52.97 ? 707  HOH   C O   1 
HETATM 9760  O  O   . HOH   JA 5 .   ? 72.504 -20.915 59.320  1.00 25.90 ? 708  HOH   C O   1 
HETATM 9761  O  O   . HOH   JA 5 .   ? 74.305 -18.523 37.606  1.00 47.20 ? 709  HOH   C O   1 
HETATM 9762  O  O   . HOH   JA 5 .   ? 67.352 -16.560 61.701  1.00 24.22 ? 710  HOH   C O   1 
HETATM 9763  O  O   . HOH   JA 5 .   ? 42.802 -8.997  31.518  1.00 54.30 ? 711  HOH   C O   1 
HETATM 9764  O  O   . HOH   JA 5 .   ? 64.471 -14.717 27.687  1.00 54.72 ? 712  HOH   C O   1 
HETATM 9765  O  O   . HOH   JA 5 .   ? 55.103 -22.011 68.166  1.00 29.17 ? 713  HOH   C O   1 
HETATM 9766  O  O   . HOH   JA 5 .   ? 60.944 -3.742  31.361  1.00 55.92 ? 714  HOH   C O   1 
HETATM 9767  O  O   . HOH   JA 5 .   ? 69.747 0.514   41.268  1.00 45.04 ? 715  HOH   C O   1 
HETATM 9768  O  O   . HOH   JA 5 .   ? 50.712 1.403   36.000  1.00 45.59 ? 716  HOH   C O   1 
HETATM 9769  O  O   . HOH   JA 5 .   ? 53.043 2.218   47.872  1.00 45.58 ? 717  HOH   C O   1 
HETATM 9770  O  O   . HOH   JA 5 .   ? 45.681 1.081   61.849  1.00 52.98 ? 718  HOH   C O   1 
HETATM 9771  O  O   . HOH   JA 5 .   ? 59.451 -27.742 26.985  1.00 48.75 ? 719  HOH   C O   1 
HETATM 9772  O  O   . HOH   JA 5 .   ? 61.162 -32.389 34.365  1.00 50.88 ? 720  HOH   C O   1 
HETATM 9773  O  O   . HOH   JA 5 .   ? 59.147 -7.573  56.118  1.00 28.97 ? 721  HOH   C O   1 
HETATM 9774  O  O   . HOH   JA 5 .   ? 55.295 -36.906 42.247  1.00 55.01 ? 722  HOH   C O   1 
HETATM 9775  O  O   . HOH   JA 5 .   ? 32.759 -6.685  54.630  1.00 61.41 ? 723  HOH   C O   1 
HETATM 9776  O  O   . HOH   JA 5 .   ? 73.177 -20.733 52.399  1.00 41.00 ? 724  HOH   C O   1 
HETATM 9777  O  O   . HOH   JA 5 .   ? 41.889 -21.335 61.460  1.00 53.48 ? 725  HOH   C O   1 
HETATM 9778  O  O   . HOH   JA 5 .   ? 70.722 -0.916  45.354  1.00 54.12 ? 726  HOH   C O   1 
HETATM 9779  O  O   . HOH   JA 5 .   ? 60.842 -3.199  54.790  1.00 49.98 ? 727  HOH   C O   1 
HETATM 9780  O  O   . HOH   JA 5 .   ? 55.667 -19.353 67.948  1.00 19.51 ? 728  HOH   C O   1 
HETATM 9781  O  O   . HOH   JA 5 .   ? 71.872 -7.651  52.874  1.00 47.62 ? 729  HOH   C O   1 
HETATM 9782  O  O   . HOH   JA 5 .   ? 65.952 -23.791 28.814  1.00 42.03 ? 730  HOH   C O   1 
HETATM 9783  O  O   . HOH   JA 5 .   ? 56.423 -14.643 25.195  1.00 46.48 ? 731  HOH   C O   1 
HETATM 9784  O  O   . HOH   JA 5 .   ? 38.452 -22.753 54.400  1.00 37.55 ? 732  HOH   C O   1 
HETATM 9785  O  O   . HOH   JA 5 .   ? 32.952 -9.061  49.492  1.00 47.40 ? 733  HOH   C O   1 
HETATM 9786  O  O   . HOH   JA 5 .   ? 45.247 8.951   48.260  1.00 55.45 ? 734  HOH   C O   1 
HETATM 9787  O  O   . HOH   JA 5 .   ? 71.670 -23.948 65.485  1.00 41.53 ? 735  HOH   C O   1 
HETATM 9788  O  O   . HOH   JA 5 .   ? 70.275 -24.761 46.330  1.00 44.20 ? 736  HOH   C O   1 
HETATM 9789  O  O   . HOH   JA 5 .   ? 56.428 -5.587  59.989  1.00 37.67 ? 737  HOH   C O   1 
HETATM 9790  O  O   . HOH   JA 5 .   ? 72.882 -3.652  46.181  1.00 44.50 ? 738  HOH   C O   1 
HETATM 9791  O  O   . HOH   JA 5 .   ? 66.927 -4.499  32.445  1.00 47.02 ? 739  HOH   C O   1 
HETATM 9792  O  O   . HOH   JA 5 .   ? 39.871 6.855   44.131  1.00 62.75 ? 740  HOH   C O   1 
HETATM 9793  O  O   . HOH   JA 5 .   ? 50.214 1.316   53.318  1.00 44.34 ? 741  HOH   C O   1 
HETATM 9794  O  O   . HOH   JA 5 .   ? 49.250 -11.224 28.445  1.00 48.08 ? 742  HOH   C O   1 
HETATM 9795  O  O   . HOH   JA 5 .   ? 54.165 4.258   36.315  1.00 41.09 ? 743  HOH   C O   1 
HETATM 9796  O  O   . HOH   JA 5 .   ? 70.325 -20.668 31.511  1.00 51.59 ? 744  HOH   C O   1 
HETATM 9797  O  O   . HOH   JA 5 .   ? 67.173 -30.439 64.388  1.00 54.78 ? 745  HOH   C O   1 
HETATM 9798  O  O   . HOH   JA 5 .   ? 47.280 -23.072 67.004  1.00 43.46 ? 746  HOH   C O   1 
HETATM 9799  O  O   . HOH   JA 5 .   ? 47.527 -17.853 30.459  1.00 38.79 ? 747  HOH   C O   1 
HETATM 9800  O  O   . HOH   JA 5 .   ? 33.804 -7.870  57.015  1.00 50.01 ? 748  HOH   C O   1 
HETATM 9801  O  O   . HOH   JA 5 .   ? 58.183 -30.594 33.442  1.00 62.45 ? 749  HOH   C O   1 
HETATM 9802  O  O   . HOH   JA 5 .   ? 71.263 -22.833 47.993  1.00 41.96 ? 750  HOH   C O   1 
HETATM 9803  O  O   . HOH   JA 5 .   ? 56.142 -4.408  56.815  1.00 54.18 ? 751  HOH   C O   1 
HETATM 9804  O  O   . HOH   JA 5 .   ? 71.146 -13.439 27.931  1.00 47.39 ? 752  HOH   C O   1 
HETATM 9805  O  O   . HOH   JA 5 .   ? 55.535 -26.913 68.529  1.00 57.34 ? 753  HOH   C O   1 
HETATM 9806  O  O   . HOH   JA 5 .   ? 40.580 -24.644 60.345  1.00 37.76 ? 754  HOH   C O   1 
HETATM 9807  O  O   . HOH   JA 5 .   ? 40.243 4.616   45.360  1.00 53.07 ? 755  HOH   C O   1 
HETATM 9808  O  O   . HOH   JA 5 .   ? 52.528 -13.821 66.745  1.00 25.43 ? 756  HOH   C O   1 
HETATM 9809  O  O   . HOH   JA 5 .   ? 64.380 -31.217 33.473  1.00 52.32 ? 757  HOH   C O   1 
HETATM 9810  O  O   . HOH   JA 5 .   ? 41.311 -10.156 35.567  1.00 48.08 ? 758  HOH   C O   1 
HETATM 9811  O  O   . HOH   JA 5 .   ? 46.876 -10.410 29.441  1.00 49.01 ? 759  HOH   C O   1 
HETATM 9812  O  O   . HOH   JA 5 .   ? 45.768 -13.266 29.791  1.00 46.01 ? 760  HOH   C O   1 
HETATM 9813  O  O   . HOH   JA 5 .   ? 39.289 6.251   41.160  1.00 55.84 ? 761  HOH   C O   1 
HETATM 9814  O  O   . HOH   JA 5 .   ? 40.326 -20.254 60.440  1.00 54.07 ? 762  HOH   C O   1 
HETATM 9815  O  O   . HOH   JA 5 .   ? 56.595 5.580   35.261  1.00 33.36 ? 763  HOH   C O   1 
HETATM 9816  O  O   . HOH   JA 5 .   ? 47.696 -38.014 51.039  1.00 47.47 ? 764  HOH   C O   1 
HETATM 9817  O  O   . HOH   JA 5 .   ? 66.002 -25.552 30.856  1.00 57.48 ? 765  HOH   C O   1 
HETATM 9818  O  O   . HOH   JA 5 .   ? 74.429 -22.522 46.386  1.00 38.78 ? 766  HOH   C O   1 
HETATM 9819  O  O   . HOH   JA 5 .   ? 44.713 -30.219 38.992  1.00 38.65 ? 767  HOH   C O   1 
HETATM 9820  O  O   . HOH   JA 5 .   ? 35.559 -19.933 54.246  1.00 41.64 ? 768  HOH   C O   1 
HETATM 9821  O  O   . HOH   JA 5 .   ? 72.366 -14.150 54.882  1.00 46.55 ? 769  HOH   C O   1 
HETATM 9822  O  O   . HOH   JA 5 .   ? 66.773 -28.047 33.662  1.00 45.32 ? 770  HOH   C O   1 
HETATM 9823  O  O   . HOH   JA 5 .   ? 73.874 -9.144  51.277  1.00 50.38 ? 771  HOH   C O   1 
HETATM 9824  O  O   . HOH   JA 5 .   ? 36.951 -4.390  56.370  1.00 39.41 ? 772  HOH   C O   1 
HETATM 9825  O  O   . HOH   JA 5 .   ? 70.986 -0.717  48.212  1.00 42.24 ? 773  HOH   C O   1 
HETATM 9826  O  O   . HOH   JA 5 .   ? 42.731 -23.780 61.276  1.00 51.51 ? 774  HOH   C O   1 
HETATM 9827  O  O   . HOH   JA 5 .   ? 48.553 -36.266 39.691  1.00 53.56 ? 775  HOH   C O   1 
HETATM 9828  O  O   . HOH   JA 5 .   ? 39.497 -19.484 55.971  1.00 34.98 ? 776  HOH   C O   1 
HETATM 9829  O  O   . HOH   JA 5 .   ? 79.848 -21.323 48.108  1.00 47.75 ? 777  HOH   C O   1 
HETATM 9830  O  O   . HOH   JA 5 .   ? 36.363 -6.771  57.913  1.00 41.81 ? 778  HOH   C O   1 
HETATM 9831  O  O   . HOH   JA 5 .   ? 46.532 -3.660  64.027  1.00 38.45 ? 779  HOH   C O   1 
HETATM 9832  O  O   . HOH   JA 5 .   ? 36.034 -5.499  60.953  1.00 51.17 ? 780  HOH   C O   1 
HETATM 9833  O  O   . HOH   JA 5 .   ? 56.725 -12.107 24.512  1.00 56.99 ? 781  HOH   C O   1 
HETATM 9834  O  O   . HOH   JA 5 .   ? 49.830 -30.731 34.204  1.00 56.67 ? 782  HOH   C O   1 
HETATM 9835  O  O   . HOH   JA 5 .   ? 43.083 -31.827 39.919  1.00 44.79 ? 783  HOH   C O   1 
HETATM 9836  O  O   . HOH   JA 5 .   ? 37.263 -2.092  58.068  1.00 50.59 ? 784  HOH   C O   1 
HETATM 9837  O  O   . HOH   JA 5 .   ? 71.493 -27.107 43.076  1.00 49.03 ? 785  HOH   C O   1 
HETATM 9838  O  O   . HOH   JA 5 .   ? 53.906 -1.558  53.627  1.00 49.64 ? 786  HOH   C O   1 
HETATM 9839  O  O   . HOH   JA 5 .   ? 68.234 -24.847 31.479  1.00 51.32 ? 787  HOH   C O   1 
HETATM 9840  O  O   . HOH   JA 5 .   ? 50.197 -5.177  65.389  1.00 44.94 ? 788  HOH   C O   1 
HETATM 9841  O  O   . HOH   JA 5 .   ? 50.145 -9.077  29.721  1.00 50.02 ? 789  HOH   C O   1 
HETATM 9842  O  O   . HOH   JA 5 .   ? 40.907 -26.318 35.190  1.00 41.78 ? 790  HOH   C O   1 
HETATM 9843  O  O   . HOH   JA 5 .   ? 50.932 -19.699 67.803  1.00 33.37 ? 791  HOH   C O   1 
HETATM 9844  O  O   . HOH   JA 5 .   ? 37.445 -3.087  61.593  1.00 51.45 ? 792  HOH   C O   1 
HETATM 9845  O  O   . HOH   JA 5 .   ? 78.019 -10.046 41.519  1.00 51.64 ? 793  HOH   C O   1 
HETATM 9846  O  O   . HOH   JA 5 .   ? 73.967 -2.829  43.153  1.00 56.70 ? 794  HOH   C O   1 
HETATM 9847  O  O   . HOH   JA 5 .   ? 53.333 2.287   52.922  1.00 55.73 ? 795  HOH   C O   1 
HETATM 9848  O  O   . HOH   JA 5 .   ? 29.904 -36.719 54.971  1.00 49.75 ? 796  HOH   C O   1 
HETATM 9849  O  O   . HOH   JA 5 .   ? 51.767 -22.528 67.568  1.00 32.77 ? 797  HOH   C O   1 
HETATM 9850  O  O   . HOH   JA 5 .   ? 56.564 -23.293 70.375  1.00 32.22 ? 798  HOH   C O   1 
HETATM 9851  O  O   . HOH   JA 5 .   ? 74.096 -21.159 61.524  1.00 57.65 ? 799  HOH   C O   1 
HETATM 9852  O  O   . HOH   JA 5 .   ? 41.846 -10.546 33.117  1.00 56.02 ? 800  HOH   C O   1 
HETATM 9853  O  O   . HOH   JA 5 .   ? 58.946 -25.275 70.017  1.00 41.44 ? 801  HOH   C O   1 
HETATM 9854  O  O   . HOH   JA 5 .   ? 75.867 -9.445  36.615  1.00 53.01 ? 802  HOH   C O   1 
HETATM 9855  O  O   . HOH   JA 5 .   ? 31.717 -18.578 41.464  1.00 48.60 ? 803  HOH   C O   1 
HETATM 9856  O  O   . HOH   JA 5 .   ? 53.167 -18.172 68.103  1.00 22.53 ? 804  HOH   C O   1 
HETATM 9857  O  O   . HOH   JA 5 .   ? 38.649 -21.171 57.768  1.00 41.57 ? 805  HOH   C O   1 
HETATM 9858  O  O   . HOH   JA 5 .   ? 52.028 -12.636 22.268  1.00 48.83 ? 806  HOH   C O   1 
HETATM 9859  O  O   . HOH   KA 5 .   ? 60.120 -25.997 56.921  1.00 18.10 ? 401  HOH   D O   1 
HETATM 9860  O  O   . HOH   KA 5 .   ? 71.536 -47.780 39.265  1.00 45.24 ? 402  HOH   D O   1 
HETATM 9861  O  O   . HOH   KA 5 .   ? 49.413 -47.066 74.048  1.00 39.46 ? 403  HOH   D O   1 
HETATM 9862  O  O   . HOH   KA 5 .   ? 52.123 -61.878 71.573  1.00 27.11 ? 404  HOH   D O   1 
HETATM 9863  O  O   . HOH   KA 5 .   ? 70.088 -72.650 44.831  1.00 48.53 ? 405  HOH   D O   1 
HETATM 9864  O  O   . HOH   KA 5 .   ? 70.875 -31.857 48.569  1.00 44.05 ? 406  HOH   D O   1 
HETATM 9865  O  O   . HOH   KA 5 .   ? 57.661 -39.247 47.859  1.00 43.18 ? 407  HOH   D O   1 
HETATM 9866  O  O   . HOH   KA 5 .   ? 68.013 -33.796 40.262  1.00 55.07 ? 408  HOH   D O   1 
HETATM 9867  O  O   . HOH   KA 5 .   ? 66.852 -57.638 32.331  1.00 47.47 ? 409  HOH   D O   1 
HETATM 9868  O  O   . HOH   KA 5 .   ? 65.817 -36.200 42.925  1.00 38.14 ? 410  HOH   D O   1 
HETATM 9869  O  O   . HOH   KA 5 .   ? 43.827 -58.807 65.199  1.00 29.80 ? 411  HOH   D O   1 
HETATM 9870  O  O   . HOH   KA 5 .   ? 49.743 -59.659 39.005  1.00 49.94 ? 412  HOH   D O   1 
HETATM 9871  O  O   . HOH   KA 5 .   ? 50.268 -44.212 38.798  1.00 49.36 ? 413  HOH   D O   1 
HETATM 9872  O  O   . HOH   KA 5 .   ? 56.035 -36.551 48.693  1.00 48.57 ? 414  HOH   D O   1 
HETATM 9873  O  O   . HOH   KA 5 .   ? 82.955 -42.913 64.076  1.00 49.54 ? 415  HOH   D O   1 
HETATM 9874  O  O   . HOH   KA 5 .   ? 66.715 -46.723 33.743  1.00 44.38 ? 416  HOH   D O   1 
HETATM 9875  O  O   . HOH   KA 5 .   ? 76.281 -39.168 39.322  1.00 48.81 ? 417  HOH   D O   1 
HETATM 9876  O  O   . HOH   KA 5 .   ? 69.581 -57.648 36.113  1.00 31.98 ? 418  HOH   D O   1 
HETATM 9877  O  O   . HOH   KA 5 .   ? 46.707 -58.836 62.717  1.00 35.18 ? 419  HOH   D O   1 
HETATM 9878  O  O   . HOH   KA 5 .   ? 57.592 -31.783 55.494  1.00 39.46 ? 420  HOH   D O   1 
HETATM 9879  O  O   . HOH   KA 5 .   ? 51.246 -67.643 68.635  1.00 38.38 ? 421  HOH   D O   1 
HETATM 9880  O  O   . HOH   KA 5 .   ? 78.242 -53.545 41.069  1.00 54.20 ? 422  HOH   D O   1 
HETATM 9881  O  O   . HOH   KA 5 .   ? 64.877 -49.865 32.992  1.00 53.26 ? 423  HOH   D O   1 
HETATM 9882  O  O   . HOH   KA 5 .   ? 59.769 -57.920 35.692  1.00 36.96 ? 424  HOH   D O   1 
HETATM 9883  O  O   . HOH   KA 5 .   ? 63.397 -46.374 60.869  1.00 28.76 ? 425  HOH   D O   1 
HETATM 9884  O  O   . HOH   KA 5 .   ? 76.437 -53.860 72.745  1.00 39.88 ? 426  HOH   D O   1 
HETATM 9885  O  O   . HOH   KA 5 .   ? 55.148 -69.601 55.839  1.00 43.96 ? 427  HOH   D O   1 
HETATM 9886  O  O   . HOH   KA 5 .   ? 50.049 -49.806 76.031  1.00 44.05 ? 428  HOH   D O   1 
HETATM 9887  O  O   . HOH   KA 5 .   ? 61.310 -32.488 45.357  1.00 25.94 ? 429  HOH   D O   1 
HETATM 9888  O  O   . HOH   KA 5 .   ? 52.627 -35.212 60.556  1.00 25.67 ? 430  HOH   D O   1 
HETATM 9889  O  O   . HOH   KA 5 .   ? 55.391 -67.636 57.227  1.00 23.53 ? 431  HOH   D O   1 
HETATM 9890  O  O   . HOH   KA 5 .   ? 61.870 -61.813 43.090  1.00 31.22 ? 432  HOH   D O   1 
HETATM 9891  O  O   . HOH   KA 5 .   ? 51.564 -46.449 50.355  1.00 33.86 ? 433  HOH   D O   1 
HETATM 9892  O  O   . HOH   KA 5 .   ? 58.451 -56.195 60.540  1.00 16.34 ? 434  HOH   D O   1 
HETATM 9893  O  O   . HOH   KA 5 .   ? 78.944 -59.429 44.155  1.00 40.88 ? 435  HOH   D O   1 
HETATM 9894  O  O   . HOH   KA 5 .   ? 75.423 -34.156 65.429  1.00 37.45 ? 436  HOH   D O   1 
HETATM 9895  O  O   . HOH   KA 5 .   ? 60.079 -55.449 73.708  1.00 33.74 ? 437  HOH   D O   1 
HETATM 9896  O  O   . HOH   KA 5 .   ? 62.684 -75.284 52.662  1.00 36.92 ? 438  HOH   D O   1 
HETATM 9897  O  O   . HOH   KA 5 .   ? 75.223 -59.151 40.903  1.00 27.93 ? 439  HOH   D O   1 
HETATM 9898  O  O   . HOH   KA 5 .   ? 78.416 -46.538 55.399  1.00 42.32 ? 440  HOH   D O   1 
HETATM 9899  O  O   . HOH   KA 5 .   ? 57.133 -43.606 52.572  1.00 28.26 ? 441  HOH   D O   1 
HETATM 9900  O  O   . HOH   KA 5 .   ? 72.491 -49.474 72.322  1.00 27.78 ? 442  HOH   D O   1 
HETATM 9901  O  O   . HOH   KA 5 .   ? 77.817 -42.283 69.042  1.00 41.68 ? 443  HOH   D O   1 
HETATM 9902  O  O   . HOH   KA 5 .   ? 62.276 -38.590 72.235  1.00 44.43 ? 444  HOH   D O   1 
HETATM 9903  O  O   . HOH   KA 5 .   ? 66.488 -67.057 62.106  1.00 23.34 ? 445  HOH   D O   1 
HETATM 9904  O  O   . HOH   KA 5 .   ? 67.758 -53.926 35.894  1.00 27.45 ? 446  HOH   D O   1 
HETATM 9905  O  O   . HOH   KA 5 .   ? 68.025 -71.731 58.037  1.00 38.24 ? 447  HOH   D O   1 
HETATM 9906  O  O   . HOH   KA 5 .   ? 61.943 -46.237 33.967  1.00 35.17 ? 448  HOH   D O   1 
HETATM 9907  O  O   . HOH   KA 5 .   ? 48.021 -44.726 68.313  1.00 47.03 ? 449  HOH   D O   1 
HETATM 9908  O  O   . HOH   KA 5 .   ? 66.022 -69.660 42.041  1.00 52.37 ? 450  HOH   D O   1 
HETATM 9909  O  O   . HOH   KA 5 .   ? 51.576 -38.126 68.024  1.00 26.96 ? 451  HOH   D O   1 
HETATM 9910  O  O   . HOH   KA 5 .   ? 64.137 -68.915 57.715  1.00 20.56 ? 452  HOH   D O   1 
HETATM 9911  O  O   . HOH   KA 5 .   ? 66.871 -73.487 49.423  1.00 29.80 ? 453  HOH   D O   1 
HETATM 9912  O  O   . HOH   KA 5 .   ? 66.529 -32.741 49.795  1.00 26.01 ? 454  HOH   D O   1 
HETATM 9913  O  O   . HOH   KA 5 .   ? 50.505 -46.660 60.848  1.00 16.08 ? 455  HOH   D O   1 
HETATM 9914  O  O   . HOH   KA 5 .   ? 53.484 -49.669 57.656  1.00 18.07 ? 456  HOH   D O   1 
HETATM 9915  O  O   . HOH   KA 5 .   ? 46.210 -57.394 47.479  1.00 21.44 ? 457  HOH   D O   1 
HETATM 9916  O  O   . HOH   KA 5 .   ? 56.540 -32.855 57.837  1.00 32.27 ? 458  HOH   D O   1 
HETATM 9917  O  O   . HOH   KA 5 .   ? 59.690 -34.354 38.809  1.00 27.48 ? 459  HOH   D O   1 
HETATM 9918  O  O   . HOH   KA 5 .   ? 54.515 -50.779 31.917  1.00 59.93 ? 460  HOH   D O   1 
HETATM 9919  O  O   . HOH   KA 5 .   ? 67.208 -37.581 68.756  1.00 45.78 ? 461  HOH   D O   1 
HETATM 9920  O  O   . HOH   KA 5 .   ? 67.036 -32.987 35.998  1.00 47.33 ? 462  HOH   D O   1 
HETATM 9921  O  O   . HOH   KA 5 .   ? 53.574 -50.689 65.733  1.00 16.51 ? 463  HOH   D O   1 
HETATM 9922  O  O   . HOH   KA 5 .   ? 49.290 -50.090 65.912  1.00 25.23 ? 464  HOH   D O   1 
HETATM 9923  O  O   . HOH   KA 5 .   ? 62.772 -57.647 38.466  1.00 23.11 ? 465  HOH   D O   1 
HETATM 9924  O  O   . HOH   KA 5 .   ? 60.030 -57.833 42.881  1.00 26.91 ? 466  HOH   D O   1 
HETATM 9925  O  O   . HOH   KA 5 .   ? 78.192 -56.539 51.021  1.00 26.70 ? 467  HOH   D O   1 
HETATM 9926  O  O   . HOH   KA 5 .   ? 76.892 -71.874 41.614  1.00 41.34 ? 468  HOH   D O   1 
HETATM 9927  O  O   . HOH   KA 5 .   ? 49.264 -53.084 40.098  1.00 29.68 ? 469  HOH   D O   1 
HETATM 9928  O  O   . HOH   KA 5 .   ? 67.343 -61.012 35.145  1.00 50.53 ? 470  HOH   D O   1 
HETATM 9929  O  O   . HOH   KA 5 .   ? 65.870 -27.578 53.976  1.00 19.20 ? 471  HOH   D O   1 
HETATM 9930  O  O   . HOH   KA 5 .   ? 68.813 -53.289 68.910  1.00 21.92 ? 472  HOH   D O   1 
HETATM 9931  O  O   . HOH   KA 5 .   ? 50.828 -35.385 57.982  1.00 45.21 ? 473  HOH   D O   1 
HETATM 9932  O  O   . HOH   KA 5 .   ? 48.266 -50.928 46.676  1.00 22.19 ? 474  HOH   D O   1 
HETATM 9933  O  O   . HOH   KA 5 .   ? 40.844 -57.041 63.000  1.00 19.01 ? 475  HOH   D O   1 
HETATM 9934  O  O   . HOH   KA 5 .   ? 78.886 -68.128 46.944  1.00 41.66 ? 476  HOH   D O   1 
HETATM 9935  O  O   . HOH   KA 5 .   ? 52.119 -39.201 51.203  1.00 36.95 ? 477  HOH   D O   1 
HETATM 9936  O  O   . HOH   KA 5 .   ? 51.170 -64.207 46.932  1.00 23.71 ? 478  HOH   D O   1 
HETATM 9937  O  O   . HOH   KA 5 .   ? 45.746 -61.009 69.810  1.00 34.10 ? 479  HOH   D O   1 
HETATM 9938  O  O   . HOH   KA 5 .   ? 55.728 -75.364 50.424  1.00 41.56 ? 480  HOH   D O   1 
HETATM 9939  O  O   . HOH   KA 5 .   ? 57.512 -71.700 48.696  1.00 27.34 ? 481  HOH   D O   1 
HETATM 9940  O  O   . HOH   KA 5 .   ? 46.360 -52.160 68.167  1.00 29.07 ? 482  HOH   D O   1 
HETATM 9941  O  O   . HOH   KA 5 .   ? 42.466 -56.237 65.031  1.00 23.87 ? 483  HOH   D O   1 
HETATM 9942  O  O   . HOH   KA 5 .   ? 51.942 -67.697 48.951  1.00 22.92 ? 484  HOH   D O   1 
HETATM 9943  O  O   . HOH   KA 5 .   ? 68.090 -61.693 72.114  1.00 30.31 ? 485  HOH   D O   1 
HETATM 9944  O  O   . HOH   KA 5 .   ? 68.462 -52.099 76.434  1.00 48.87 ? 486  HOH   D O   1 
HETATM 9945  O  O   . HOH   KA 5 .   ? 63.401 -69.231 60.549  1.00 29.44 ? 487  HOH   D O   1 
HETATM 9946  O  O   . HOH   KA 5 .   ? 78.437 -40.488 50.267  1.00 43.68 ? 488  HOH   D O   1 
HETATM 9947  O  O   . HOH   KA 5 .   ? 50.220 -48.491 69.932  1.00 38.25 ? 489  HOH   D O   1 
HETATM 9948  O  O   . HOH   KA 5 .   ? 50.887 -71.141 52.040  1.00 51.73 ? 490  HOH   D O   1 
HETATM 9949  O  O   . HOH   KA 5 .   ? 63.790 -35.628 41.125  1.00 26.87 ? 491  HOH   D O   1 
HETATM 9950  O  O   . HOH   KA 5 .   ? 64.337 -56.635 76.313  1.00 46.93 ? 492  HOH   D O   1 
HETATM 9951  O  O   . HOH   KA 5 .   ? 44.337 -41.622 71.020  1.00 53.93 ? 493  HOH   D O   1 
HETATM 9952  O  O   . HOH   KA 5 .   ? 55.876 -69.112 60.543  1.00 35.81 ? 494  HOH   D O   1 
HETATM 9953  O  O   . HOH   KA 5 .   ? 60.575 -55.325 35.399  1.00 29.51 ? 495  HOH   D O   1 
HETATM 9954  O  O   . HOH   KA 5 .   ? 50.281 -46.688 67.844  1.00 27.83 ? 496  HOH   D O   1 
HETATM 9955  O  O   . HOH   KA 5 .   ? 65.684 -59.505 65.866  1.00 23.79 ? 497  HOH   D O   1 
HETATM 9956  O  O   . HOH   KA 5 .   ? 71.608 -71.284 59.564  1.00 27.97 ? 498  HOH   D O   1 
HETATM 9957  O  O   . HOH   KA 5 .   ? 74.496 -40.275 55.164  1.00 30.97 ? 499  HOH   D O   1 
HETATM 9958  O  O   . HOH   KA 5 .   ? 70.391 -42.593 38.059  1.00 41.69 ? 500  HOH   D O   1 
HETATM 9959  O  O   . HOH   KA 5 .   ? 58.725 -33.491 42.138  1.00 27.94 ? 501  HOH   D O   1 
HETATM 9960  O  O   . HOH   KA 5 .   ? 79.394 -48.733 70.268  1.00 33.54 ? 502  HOH   D O   1 
HETATM 9961  O  O   . HOH   KA 5 .   ? 57.934 -48.511 56.594  1.00 19.73 ? 503  HOH   D O   1 
HETATM 9962  O  O   . HOH   KA 5 .   ? 69.413 -33.919 62.284  1.00 45.17 ? 504  HOH   D O   1 
HETATM 9963  O  O   . HOH   KA 5 .   ? 83.109 -54.303 57.573  1.00 57.56 ? 505  HOH   D O   1 
HETATM 9964  O  O   . HOH   KA 5 .   ? 57.437 -51.344 73.914  1.00 32.90 ? 506  HOH   D O   1 
HETATM 9965  O  O   . HOH   KA 5 .   ? 52.685 -60.327 69.556  1.00 27.19 ? 507  HOH   D O   1 
HETATM 9966  O  O   . HOH   KA 5 .   ? 54.569 -36.337 71.293  1.00 37.26 ? 508  HOH   D O   1 
HETATM 9967  O  O   . HOH   KA 5 .   ? 77.921 -40.094 66.984  1.00 54.00 ? 509  HOH   D O   1 
HETATM 9968  O  O   . HOH   KA 5 .   ? 56.180 -39.805 42.290  1.00 44.23 ? 510  HOH   D O   1 
HETATM 9969  O  O   . HOH   KA 5 .   ? 63.853 -32.542 35.664  1.00 33.53 ? 511  HOH   D O   1 
HETATM 9970  O  O   . HOH   KA 5 .   ? 55.200 -43.777 44.234  1.00 23.04 ? 512  HOH   D O   1 
HETATM 9971  O  O   . HOH   KA 5 .   ? 80.748 -51.237 56.491  1.00 38.43 ? 513  HOH   D O   1 
HETATM 9972  O  O   . HOH   KA 5 .   ? 65.130 -38.931 45.134  1.00 25.72 ? 514  HOH   D O   1 
HETATM 9973  O  O   . HOH   KA 5 .   ? 82.339 -50.767 54.527  1.00 35.80 ? 515  HOH   D O   1 
HETATM 9974  O  O   . HOH   KA 5 .   ? 52.515 -51.376 55.609  1.00 18.92 ? 516  HOH   D O   1 
HETATM 9975  O  O   . HOH   KA 5 .   ? 54.982 -40.823 53.576  1.00 29.40 ? 517  HOH   D O   1 
HETATM 9976  O  O   . HOH   KA 5 .   ? 83.343 -56.607 47.214  1.00 46.07 ? 518  HOH   D O   1 
HETATM 9977  O  O   . HOH   KA 5 .   ? 76.841 -56.967 41.572  1.00 32.38 ? 519  HOH   D O   1 
HETATM 9978  O  O   . HOH   KA 5 .   ? 74.260 -53.754 35.611  1.00 49.26 ? 520  HOH   D O   1 
HETATM 9979  O  O   . HOH   KA 5 .   ? 55.956 -40.582 46.420  1.00 47.12 ? 521  HOH   D O   1 
HETATM 9980  O  O   . HOH   KA 5 .   ? 61.231 -50.668 35.186  1.00 25.80 ? 522  HOH   D O   1 
HETATM 9981  O  O   . HOH   KA 5 .   ? 58.451 -32.538 64.115  1.00 43.28 ? 523  HOH   D O   1 
HETATM 9982  O  O   . HOH   KA 5 .   ? 51.305 -64.227 62.173  1.00 18.90 ? 524  HOH   D O   1 
HETATM 9983  O  O   . HOH   KA 5 .   ? 69.773 -62.783 69.027  1.00 27.77 ? 525  HOH   D O   1 
HETATM 9984  O  O   . HOH   KA 5 .   ? 76.553 -63.301 38.676  1.00 29.16 ? 526  HOH   D O   1 
HETATM 9985  O  O   . HOH   KA 5 .   ? 68.987 -70.157 54.310  1.00 28.56 ? 527  HOH   D O   1 
HETATM 9986  O  O   . HOH   KA 5 .   ? 51.879 -67.402 64.951  1.00 26.54 ? 528  HOH   D O   1 
HETATM 9987  O  O   . HOH   KA 5 .   ? 74.561 -55.704 55.482  1.00 22.19 ? 529  HOH   D O   1 
HETATM 9988  O  O   . HOH   KA 5 .   ? 58.736 -35.359 69.461  1.00 27.12 ? 530  HOH   D O   1 
HETATM 9989  O  O   . HOH   KA 5 .   ? 61.290 -41.545 75.002  1.00 52.78 ? 531  HOH   D O   1 
HETATM 9990  O  O   . HOH   KA 5 .   ? 68.775 -35.788 49.596  1.00 25.72 ? 532  HOH   D O   1 
HETATM 9991  O  O   . HOH   KA 5 .   ? 69.173 -32.305 67.097  1.00 46.16 ? 533  HOH   D O   1 
HETATM 9992  O  O   . HOH   KA 5 .   ? 52.601 -57.536 35.559  1.00 54.76 ? 534  HOH   D O   1 
HETATM 9993  O  O   . HOH   KA 5 .   ? 56.268 -38.798 54.752  1.00 36.88 ? 535  HOH   D O   1 
HETATM 9994  O  O   . HOH   KA 5 .   ? 81.080 -46.579 61.477  1.00 43.44 ? 536  HOH   D O   1 
HETATM 9995  O  O   . HOH   KA 5 .   ? 65.934 -40.169 69.921  1.00 33.82 ? 537  HOH   D O   1 
HETATM 9996  O  O   . HOH   KA 5 .   ? 52.012 -62.861 44.519  1.00 50.48 ? 538  HOH   D O   1 
HETATM 9997  O  O   . HOH   KA 5 .   ? 79.308 -55.869 67.956  1.00 51.64 ? 539  HOH   D O   1 
HETATM 9998  O  O   . HOH   KA 5 .   ? 47.357 -59.464 53.226  1.00 16.14 ? 540  HOH   D O   1 
HETATM 9999  O  O   . HOH   KA 5 .   ? 47.136 -46.324 61.441  1.00 21.14 ? 541  HOH   D O   1 
HETATM 10000 O  O   . HOH   KA 5 .   ? 64.990 -40.139 42.513  1.00 31.23 ? 542  HOH   D O   1 
HETATM 10001 O  O   . HOH   KA 5 .   ? 81.074 -54.403 45.676  1.00 40.82 ? 543  HOH   D O   1 
HETATM 10002 O  O   . HOH   KA 5 .   ? 78.532 -51.456 73.364  1.00 48.40 ? 544  HOH   D O   1 
HETATM 10003 O  O   . HOH   KA 5 .   ? 78.200 -66.408 59.086  1.00 43.81 ? 545  HOH   D O   1 
HETATM 10004 O  O   . HOH   KA 5 .   ? 51.684 -66.434 44.586  1.00 49.19 ? 546  HOH   D O   1 
HETATM 10005 O  O   . HOH   KA 5 .   ? 73.706 -36.683 54.320  1.00 33.48 ? 547  HOH   D O   1 
HETATM 10006 O  O   . HOH   KA 5 .   ? 76.898 -61.343 40.516  1.00 29.97 ? 548  HOH   D O   1 
HETATM 10007 O  O   . HOH   KA 5 .   ? 76.355 -60.849 56.993  1.00 28.55 ? 549  HOH   D O   1 
HETATM 10008 O  O   . HOH   KA 5 .   ? 74.651 -37.737 58.937  1.00 28.08 ? 550  HOH   D O   1 
HETATM 10009 O  O   . HOH   KA 5 .   ? 76.629 -65.165 61.127  1.00 35.71 ? 551  HOH   D O   1 
HETATM 10010 O  O   . HOH   KA 5 .   ? 79.214 -59.569 60.624  1.00 47.64 ? 552  HOH   D O   1 
HETATM 10011 O  O   . HOH   KA 5 .   ? 72.819 -70.821 41.104  1.00 41.39 ? 553  HOH   D O   1 
HETATM 10012 O  O   . HOH   KA 5 .   ? 67.537 -45.653 74.737  1.00 34.05 ? 554  HOH   D O   1 
HETATM 10013 O  O   . HOH   KA 5 .   ? 68.178 -66.351 66.144  1.00 36.96 ? 555  HOH   D O   1 
HETATM 10014 O  O   . HOH   KA 5 .   ? 66.579 -54.804 32.682  1.00 37.72 ? 556  HOH   D O   1 
HETATM 10015 O  O   . HOH   KA 5 .   ? 71.103 -39.998 38.897  1.00 47.18 ? 557  HOH   D O   1 
HETATM 10016 O  O   . HOH   KA 5 .   ? 71.207 -40.830 41.567  1.00 37.22 ? 558  HOH   D O   1 
HETATM 10017 O  O   . HOH   KA 5 .   ? 53.183 -51.714 68.300  1.00 18.79 ? 559  HOH   D O   1 
HETATM 10018 O  O   . HOH   KA 5 .   ? 49.147 -55.178 71.503  1.00 25.64 ? 560  HOH   D O   1 
HETATM 10019 O  O   . HOH   KA 5 .   ? 54.971 -36.790 56.499  1.00 30.50 ? 561  HOH   D O   1 
HETATM 10020 O  O   . HOH   KA 5 .   ? 49.914 -71.947 55.040  1.00 57.89 ? 562  HOH   D O   1 
HETATM 10021 O  O   . HOH   KA 5 .   ? 65.091 -62.252 39.717  1.00 41.23 ? 563  HOH   D O   1 
HETATM 10022 O  O   . HOH   KA 5 .   ? 48.773 -40.263 66.256  1.00 46.55 ? 564  HOH   D O   1 
HETATM 10023 O  O   . HOH   KA 5 .   ? 58.250 -40.684 55.361  1.00 30.07 ? 565  HOH   D O   1 
HETATM 10024 O  O   . HOH   KA 5 .   ? 80.257 -69.868 55.426  1.00 46.97 ? 566  HOH   D O   1 
HETATM 10025 O  O   . HOH   KA 5 .   ? 48.481 -46.390 43.400  1.00 31.26 ? 567  HOH   D O   1 
HETATM 10026 O  O   . HOH   KA 5 .   ? 54.298 -40.820 74.755  1.00 33.25 ? 568  HOH   D O   1 
HETATM 10027 O  O   . HOH   KA 5 .   ? 55.240 -68.863 45.296  1.00 38.78 ? 569  HOH   D O   1 
HETATM 10028 O  O   . HOH   KA 5 .   ? 60.782 -44.704 74.188  1.00 28.55 ? 570  HOH   D O   1 
HETATM 10029 O  O   . HOH   KA 5 .   ? 84.484 -54.155 51.959  1.00 40.43 ? 571  HOH   D O   1 
HETATM 10030 O  O   . HOH   KA 5 .   ? 55.814 -58.419 70.735  1.00 36.75 ? 572  HOH   D O   1 
HETATM 10031 O  O   . HOH   KA 5 .   ? 70.619 -71.790 47.131  1.00 46.34 ? 573  HOH   D O   1 
HETATM 10032 O  O   . HOH   KA 5 .   ? 62.864 -39.961 34.874  1.00 41.14 ? 574  HOH   D O   1 
HETATM 10033 O  O   . HOH   KA 5 .   ? 64.776 -51.038 75.589  1.00 36.58 ? 575  HOH   D O   1 
HETATM 10034 O  O   . HOH   KA 5 .   ? 72.090 -53.305 74.630  1.00 37.44 ? 576  HOH   D O   1 
HETATM 10035 O  O   . HOH   KA 5 .   ? 58.054 -40.762 35.393  1.00 49.29 ? 577  HOH   D O   1 
HETATM 10036 O  O   . HOH   KA 5 .   ? 78.657 -70.207 60.011  1.00 45.38 ? 578  HOH   D O   1 
HETATM 10037 O  O   . HOH   KA 5 .   ? 51.003 -61.467 47.678  1.00 25.11 ? 579  HOH   D O   1 
HETATM 10038 O  O   . HOH   KA 5 .   ? 53.061 -59.068 37.367  1.00 57.63 ? 580  HOH   D O   1 
HETATM 10039 O  O   . HOH   KA 5 .   ? 78.974 -48.353 48.550  1.00 42.08 ? 581  HOH   D O   1 
HETATM 10040 O  O   . HOH   KA 5 .   ? 60.353 -51.363 61.857  1.00 24.48 ? 582  HOH   D O   1 
HETATM 10041 O  O   . HOH   KA 5 .   ? 48.656 -46.547 72.287  1.00 45.66 ? 583  HOH   D O   1 
HETATM 10042 O  O   . HOH   KA 5 .   ? 63.662 -42.212 43.365  1.00 26.39 ? 584  HOH   D O   1 
HETATM 10043 O  O   . HOH   KA 5 .   ? 57.515 -54.444 70.692  1.00 25.14 ? 585  HOH   D O   1 
HETATM 10044 O  O   . HOH   KA 5 .   ? 78.072 -45.423 72.055  1.00 37.76 ? 586  HOH   D O   1 
HETATM 10045 O  O   . HOH   KA 5 .   ? 78.855 -42.884 57.001  1.00 36.65 ? 587  HOH   D O   1 
HETATM 10046 O  O   . HOH   KA 5 .   ? 48.529 -50.887 72.094  1.00 53.04 ? 588  HOH   D O   1 
HETATM 10047 O  O   . HOH   KA 5 .   ? 75.519 -43.743 44.169  1.00 36.38 ? 589  HOH   D O   1 
HETATM 10048 O  O   . HOH   KA 5 .   ? 44.952 -38.516 77.209  1.00 40.38 ? 590  HOH   D O   1 
HETATM 10049 O  O   . HOH   KA 5 .   ? 82.802 -66.416 49.068  1.00 48.32 ? 591  HOH   D O   1 
HETATM 10050 O  O   . HOH   KA 5 .   ? 68.819 -71.512 49.639  1.00 26.54 ? 592  HOH   D O   1 
HETATM 10051 O  O   . HOH   KA 5 .   ? 49.912 -69.552 64.438  1.00 32.16 ? 593  HOH   D O   1 
HETATM 10052 O  O   . HOH   KA 5 .   ? 63.938 -61.972 62.960  1.00 24.66 ? 594  HOH   D O   1 
HETATM 10053 O  O   . HOH   KA 5 .   ? 65.625 -69.885 55.553  1.00 42.42 ? 595  HOH   D O   1 
HETATM 10054 O  O   . HOH   KA 5 .   ? 45.924 -65.918 70.490  1.00 51.74 ? 596  HOH   D O   1 
HETATM 10055 O  O   . HOH   KA 5 .   ? 68.719 -72.559 40.644  1.00 51.33 ? 597  HOH   D O   1 
HETATM 10056 O  O   . HOH   KA 5 .   ? 78.659 -45.465 49.707  1.00 50.39 ? 598  HOH   D O   1 
HETATM 10057 O  O   . HOH   KA 5 .   ? 61.192 -74.291 54.939  1.00 25.97 ? 599  HOH   D O   1 
HETATM 10058 O  O   . HOH   KA 5 .   ? 46.923 -68.385 56.831  1.00 29.37 ? 600  HOH   D O   1 
HETATM 10059 O  O   . HOH   KA 5 .   ? 62.942 -38.182 41.651  1.00 25.59 ? 601  HOH   D O   1 
HETATM 10060 O  O   . HOH   KA 5 .   ? 62.583 -39.556 70.031  1.00 45.43 ? 602  HOH   D O   1 
HETATM 10061 O  O   . HOH   KA 5 .   ? 63.266 -47.328 75.343  1.00 36.11 ? 603  HOH   D O   1 
HETATM 10062 O  O   . HOH   KA 5 .   ? 57.844 -51.436 60.592  1.00 18.40 ? 604  HOH   D O   1 
HETATM 10063 O  O   . HOH   KA 5 .   ? 58.528 -58.240 67.859  1.00 30.00 ? 605  HOH   D O   1 
HETATM 10064 O  O   . HOH   KA 5 .   ? 69.694 -42.152 74.258  1.00 44.86 ? 606  HOH   D O   1 
HETATM 10065 O  O   . HOH   KA 5 .   ? 56.597 -45.214 35.626  1.00 41.97 ? 607  HOH   D O   1 
HETATM 10066 O  O   . HOH   KA 5 .   ? 78.241 -70.834 45.720  1.00 42.96 ? 608  HOH   D O   1 
HETATM 10067 O  O   . HOH   KA 5 .   ? 68.711 -48.095 74.880  1.00 29.69 ? 609  HOH   D O   1 
HETATM 10068 O  O   . HOH   KA 5 .   ? 56.769 -41.127 37.211  1.00 40.48 ? 610  HOH   D O   1 
HETATM 10069 O  O   . HOH   KA 5 .   ? 65.859 -63.217 43.972  1.00 26.12 ? 611  HOH   D O   1 
HETATM 10070 O  O   . HOH   KA 5 .   ? 65.311 -33.734 67.333  1.00 44.07 ? 612  HOH   D O   1 
HETATM 10071 O  O   . HOH   KA 5 .   ? 63.528 -72.112 56.603  1.00 38.81 ? 613  HOH   D O   1 
HETATM 10072 O  O   . HOH   KA 5 .   ? 47.454 -57.307 64.645  1.00 23.06 ? 614  HOH   D O   1 
HETATM 10073 O  O   . HOH   KA 5 .   ? 53.223 -51.713 71.140  1.00 30.20 ? 615  HOH   D O   1 
HETATM 10074 O  O   . HOH   KA 5 .   ? 48.850 -51.090 57.168  1.00 17.11 ? 616  HOH   D O   1 
HETATM 10075 O  O   . HOH   KA 5 .   ? 56.351 -42.815 54.954  1.00 25.09 ? 617  HOH   D O   1 
HETATM 10076 O  O   . HOH   KA 5 .   ? 68.579 -65.150 41.403  1.00 45.99 ? 618  HOH   D O   1 
HETATM 10077 O  O   . HOH   KA 5 .   ? 63.533 -59.237 40.352  1.00 42.76 ? 619  HOH   D O   1 
HETATM 10078 O  O   . HOH   KA 5 .   ? 77.487 -56.762 43.891  1.00 42.44 ? 620  HOH   D O   1 
HETATM 10079 O  O   . HOH   KA 5 .   ? 51.647 -44.944 45.772  1.00 31.73 ? 621  HOH   D O   1 
HETATM 10080 O  O   . HOH   KA 5 .   ? 55.620 -43.395 36.850  1.00 44.76 ? 622  HOH   D O   1 
HETATM 10081 O  O   . HOH   KA 5 .   ? 51.703 -54.640 74.065  1.00 31.42 ? 623  HOH   D O   1 
HETATM 10082 O  O   . HOH   KA 5 .   ? 57.265 -68.415 53.319  1.00 21.15 ? 624  HOH   D O   1 
HETATM 10083 O  O   . HOH   KA 5 .   ? 70.104 -74.385 54.943  1.00 33.81 ? 625  HOH   D O   1 
HETATM 10084 O  O   . HOH   KA 5 .   ? 56.090 -75.603 46.017  1.00 49.19 ? 626  HOH   D O   1 
HETATM 10085 O  O   . HOH   KA 5 .   ? 61.330 -59.540 36.721  1.00 50.42 ? 627  HOH   D O   1 
HETATM 10086 O  O   . HOH   KA 5 .   ? 69.476 -33.811 68.634  1.00 47.26 ? 628  HOH   D O   1 
HETATM 10087 O  O   . HOH   KA 5 .   ? 44.281 -49.447 66.894  1.00 21.02 ? 629  HOH   D O   1 
HETATM 10088 O  O   . HOH   KA 5 .   ? 78.618 -64.943 35.152  1.00 54.16 ? 630  HOH   D O   1 
HETATM 10089 O  O   . HOH   KA 5 .   ? 76.667 -49.116 42.067  1.00 38.98 ? 631  HOH   D O   1 
HETATM 10090 O  O   . HOH   KA 5 .   ? 63.607 -69.037 44.925  1.00 28.97 ? 632  HOH   D O   1 
HETATM 10091 O  O   . HOH   KA 5 .   ? 62.263 -59.856 73.278  1.00 38.88 ? 633  HOH   D O   1 
HETATM 10092 O  O   . HOH   KA 5 .   ? 61.167 -36.185 72.426  1.00 48.26 ? 634  HOH   D O   1 
HETATM 10093 O  O   . HOH   KA 5 .   ? 54.169 -37.594 51.907  1.00 45.77 ? 635  HOH   D O   1 
HETATM 10094 O  O   . HOH   KA 5 .   ? 83.479 -50.524 64.235  1.00 43.32 ? 636  HOH   D O   1 
HETATM 10095 O  O   . HOH   KA 5 .   ? 50.586 -50.774 68.625  1.00 32.82 ? 637  HOH   D O   1 
HETATM 10096 O  O   . HOH   KA 5 .   ? 48.450 -66.399 67.013  1.00 33.20 ? 638  HOH   D O   1 
HETATM 10097 O  O   . HOH   KA 5 .   ? 60.121 -39.001 35.267  1.00 54.50 ? 639  HOH   D O   1 
HETATM 10098 O  O   . HOH   KA 5 .   ? 80.629 -46.693 51.738  1.00 48.96 ? 640  HOH   D O   1 
HETATM 10099 O  O   . HOH   KA 5 .   ? 77.020 -67.398 50.910  1.00 38.17 ? 641  HOH   D O   1 
HETATM 10100 O  O   . HOH   KA 5 .   ? 80.370 -49.009 58.317  1.00 32.72 ? 642  HOH   D O   1 
HETATM 10101 O  O   . HOH   KA 5 .   ? 71.996 -63.736 67.620  1.00 27.70 ? 643  HOH   D O   1 
HETATM 10102 O  O   . HOH   KA 5 .   ? 51.968 -59.948 44.893  1.00 36.40 ? 644  HOH   D O   1 
HETATM 10103 O  O   . HOH   KA 5 .   ? 69.287 -63.376 37.408  1.00 57.25 ? 645  HOH   D O   1 
HETATM 10104 O  O   . HOH   KA 5 .   ? 49.320 -62.991 73.078  1.00 29.52 ? 646  HOH   D O   1 
HETATM 10105 O  O   . HOH   KA 5 .   ? 70.404 -70.532 51.994  1.00 30.86 ? 647  HOH   D O   1 
HETATM 10106 O  O   . HOH   KA 5 .   ? 54.014 -33.482 62.487  1.00 32.34 ? 648  HOH   D O   1 
HETATM 10107 O  O   . HOH   KA 5 .   ? 50.459 -47.777 65.172  1.00 27.90 ? 649  HOH   D O   1 
HETATM 10108 O  O   . HOH   KA 5 .   ? 79.269 -66.095 52.596  1.00 40.89 ? 650  HOH   D O   1 
HETATM 10109 O  O   . HOH   KA 5 .   ? 50.827 -49.632 36.663  1.00 36.01 ? 651  HOH   D O   1 
HETATM 10110 O  O   . HOH   KA 5 .   ? 76.938 -35.971 50.917  1.00 50.74 ? 652  HOH   D O   1 
HETATM 10111 O  O   . HOH   KA 5 .   ? 45.452 -56.128 65.735  1.00 27.29 ? 653  HOH   D O   1 
HETATM 10112 O  O   . HOH   KA 5 .   ? 48.534 -41.043 63.420  1.00 45.41 ? 654  HOH   D O   1 
HETATM 10113 O  O   . HOH   KA 5 .   ? 78.345 -36.787 60.816  1.00 50.36 ? 655  HOH   D O   1 
HETATM 10114 O  O   . HOH   KA 5 .   ? 65.603 -67.732 43.713  1.00 38.57 ? 656  HOH   D O   1 
HETATM 10115 O  O   . HOH   KA 5 .   ? 82.206 -44.332 68.320  1.00 45.31 ? 657  HOH   D O   1 
HETATM 10116 O  O   . HOH   KA 5 .   ? 73.811 -61.670 68.201  1.00 50.58 ? 658  HOH   D O   1 
HETATM 10117 O  O   . HOH   KA 5 .   ? 58.296 -57.738 32.646  1.00 56.70 ? 659  HOH   D O   1 
HETATM 10118 O  O   . HOH   KA 5 .   ? 54.851 -41.876 40.283  1.00 48.90 ? 660  HOH   D O   1 
HETATM 10119 O  O   . HOH   KA 5 .   ? 56.246 -49.829 58.824  1.00 18.93 ? 661  HOH   D O   1 
HETATM 10120 O  O   . HOH   KA 5 .   ? 60.492 -35.957 34.657  1.00 49.01 ? 662  HOH   D O   1 
HETATM 10121 O  O   . HOH   KA 5 .   ? 40.958 -55.882 67.338  1.00 22.13 ? 663  HOH   D O   1 
HETATM 10122 O  O   . HOH   KA 5 .   ? 60.050 -29.657 60.333  1.00 39.73 ? 664  HOH   D O   1 
HETATM 10123 O  O   . HOH   KA 5 .   ? 82.604 -63.348 42.751  1.00 46.69 ? 665  HOH   D O   1 
HETATM 10124 O  O   . HOH   KA 5 .   ? 52.790 -43.385 79.988  1.00 49.30 ? 666  HOH   D O   1 
HETATM 10125 O  O   . HOH   KA 5 .   ? 46.243 -61.941 53.265  1.00 15.85 ? 667  HOH   D O   1 
HETATM 10126 O  O   . HOH   KA 5 .   ? 53.451 -65.654 60.643  1.00 32.83 ? 668  HOH   D O   1 
HETATM 10127 O  O   . HOH   KA 5 .   ? 63.844 -64.113 64.410  1.00 28.46 ? 669  HOH   D O   1 
HETATM 10128 O  O   . HOH   KA 5 .   ? 45.961 -54.233 70.096  1.00 27.25 ? 670  HOH   D O   1 
HETATM 10129 O  O   . HOH   KA 5 .   ? 74.074 -42.365 40.961  1.00 40.79 ? 671  HOH   D O   1 
HETATM 10130 O  O   . HOH   KA 5 .   ? 45.097 -53.360 61.068  1.00 15.64 ? 672  HOH   D O   1 
HETATM 10131 O  O   . HOH   KA 5 .   ? 79.224 -42.473 44.125  1.00 55.54 ? 673  HOH   D O   1 
HETATM 10132 O  O   . HOH   KA 5 .   ? 58.391 -51.193 57.620  1.00 39.77 ? 674  HOH   D O   1 
HETATM 10133 O  O   . HOH   KA 5 .   ? 77.054 -47.054 45.007  1.00 50.93 ? 675  HOH   D O   1 
HETATM 10134 O  O   . HOH   KA 5 .   ? 60.615 -70.106 60.505  1.00 29.26 ? 676  HOH   D O   1 
HETATM 10135 O  O   . HOH   KA 5 .   ? 42.377 -63.408 69.108  1.00 43.85 ? 677  HOH   D O   1 
HETATM 10136 O  O   . HOH   KA 5 .   ? 56.076 -41.615 50.998  1.00 44.24 ? 678  HOH   D O   1 
HETATM 10137 O  O   . HOH   KA 5 .   ? 48.750 -68.339 53.166  1.00 46.86 ? 679  HOH   D O   1 
HETATM 10138 O  O   . HOH   KA 5 .   ? 55.206 -73.097 46.536  1.00 50.05 ? 680  HOH   D O   1 
HETATM 10139 O  O   . HOH   KA 5 .   ? 57.623 -71.159 45.675  1.00 49.95 ? 681  HOH   D O   1 
HETATM 10140 O  O   . HOH   KA 5 .   ? 45.709 -67.844 59.483  1.00 39.27 ? 682  HOH   D O   1 
HETATM 10141 O  O   . HOH   KA 5 .   ? 46.908 -50.089 43.498  1.00 46.88 ? 683  HOH   D O   1 
HETATM 10142 O  O   . HOH   KA 5 .   ? 55.597 -65.054 42.017  1.00 55.33 ? 684  HOH   D O   1 
HETATM 10143 O  O   . HOH   KA 5 .   ? 80.647 -58.486 51.505  1.00 37.16 ? 685  HOH   D O   1 
HETATM 10144 O  O   . HOH   KA 5 .   ? 57.050 -34.948 71.397  1.00 54.77 ? 686  HOH   D O   1 
HETATM 10145 O  O   . HOH   KA 5 .   ? 72.583 -37.874 47.660  1.00 50.17 ? 687  HOH   D O   1 
HETATM 10146 O  O   . HOH   KA 5 .   ? 73.905 -67.831 65.716  1.00 52.23 ? 688  HOH   D O   1 
HETATM 10147 O  O   . HOH   KA 5 .   ? 44.191 -42.815 76.387  1.00 41.16 ? 689  HOH   D O   1 
HETATM 10148 O  O   . HOH   KA 5 .   ? 57.556 -69.331 46.515  1.00 48.18 ? 690  HOH   D O   1 
HETATM 10149 O  O   . HOH   KA 5 .   ? 74.291 -40.347 68.855  1.00 47.02 ? 691  HOH   D O   1 
HETATM 10150 O  O   . HOH   KA 5 .   ? 49.048 -42.994 36.778  1.00 51.55 ? 692  HOH   D O   1 
HETATM 10151 O  O   . HOH   KA 5 .   ? 77.993 -59.252 38.866  1.00 44.45 ? 693  HOH   D O   1 
HETATM 10152 O  O   . HOH   KA 5 .   ? 46.298 -51.947 58.131  1.00 17.70 ? 694  HOH   D O   1 
HETATM 10153 O  O   . HOH   KA 5 .   ? 51.213 -62.459 74.268  1.00 41.24 ? 695  HOH   D O   1 
HETATM 10154 O  O   . HOH   KA 5 .   ? 56.117 -33.134 48.563  1.00 27.89 ? 696  HOH   D O   1 
HETATM 10155 O  O   . HOH   KA 5 .   ? 80.166 -69.412 36.146  1.00 55.57 ? 697  HOH   D O   1 
HETATM 10156 O  O   . HOH   KA 5 .   ? 75.383 -56.386 66.399  1.00 42.15 ? 698  HOH   D O   1 
HETATM 10157 O  O   . HOH   KA 5 .   ? 63.271 -71.891 43.496  1.00 55.03 ? 699  HOH   D O   1 
HETATM 10158 O  O   . HOH   KA 5 .   ? 44.555 -55.393 61.585  1.00 25.45 ? 700  HOH   D O   1 
HETATM 10159 O  O   . HOH   KA 5 .   ? 45.128 -56.384 68.605  1.00 25.54 ? 701  HOH   D O   1 
HETATM 10160 O  O   . HOH   KA 5 .   ? 58.521 -66.583 43.213  1.00 51.47 ? 702  HOH   D O   1 
HETATM 10161 O  O   . HOH   KA 5 .   ? 47.048 -66.489 51.996  1.00 27.59 ? 703  HOH   D O   1 
HETATM 10162 O  O   . HOH   KA 5 .   ? 46.543 -53.400 74.560  1.00 57.86 ? 704  HOH   D O   1 
HETATM 10163 O  O   . HOH   KA 5 .   ? 72.409 -30.494 55.463  1.00 44.82 ? 705  HOH   D O   1 
HETATM 10164 O  O   . HOH   KA 5 .   ? 44.782 -60.260 65.858  1.00 39.85 ? 706  HOH   D O   1 
HETATM 10165 O  O   . HOH   KA 5 .   ? 55.092 -30.769 62.181  1.00 46.41 ? 707  HOH   D O   1 
HETATM 10166 O  O   . HOH   KA 5 .   ? 46.845 -42.704 63.941  1.00 50.86 ? 708  HOH   D O   1 
HETATM 10167 O  O   . HOH   KA 5 .   ? 50.632 -47.636 52.524  1.00 29.99 ? 709  HOH   D O   1 
HETATM 10168 O  O   . HOH   KA 5 .   ? 68.552 -33.104 47.975  1.00 50.62 ? 710  HOH   D O   1 
HETATM 10169 O  O   . HOH   KA 5 .   ? 73.116 -38.774 69.934  1.00 52.26 ? 711  HOH   D O   1 
HETATM 10170 O  O   . HOH   KA 5 .   ? 57.527 -37.253 45.520  1.00 44.51 ? 712  HOH   D O   1 
HETATM 10171 O  O   . HOH   KA 5 .   ? 51.579 -33.753 62.328  1.00 54.63 ? 713  HOH   D O   1 
HETATM 10172 O  O   . HOH   KA 5 .   ? 68.837 -32.293 60.460  1.00 51.73 ? 714  HOH   D O   1 
HETATM 10173 O  O   . HOH   KA 5 .   ? 66.842 -65.552 43.517  1.00 39.21 ? 715  HOH   D O   1 
HETATM 10174 O  O   . HOH   KA 5 .   ? 70.129 -26.954 49.227  1.00 50.86 ? 716  HOH   D O   1 
HETATM 10175 O  O   . HOH   KA 5 .   ? 46.472 -62.127 72.370  1.00 32.54 ? 717  HOH   D O   1 
HETATM 10176 O  O   . HOH   KA 5 .   ? 79.535 -41.937 48.253  1.00 52.45 ? 718  HOH   D O   1 
HETATM 10177 O  O   . HOH   KA 5 .   ? 49.635 -42.886 52.275  1.00 48.82 ? 719  HOH   D O   1 
HETATM 10178 O  O   . HOH   KA 5 .   ? 68.379 -44.651 35.299  1.00 47.88 ? 720  HOH   D O   1 
HETATM 10179 O  O   . HOH   KA 5 .   ? 80.111 -50.699 71.901  1.00 52.51 ? 721  HOH   D O   1 
HETATM 10180 O  O   . HOH   KA 5 .   ? 69.181 -35.835 75.025  1.00 50.81 ? 722  HOH   D O   1 
HETATM 10181 O  O   . HOH   KA 5 .   ? 46.126 -64.009 51.280  1.00 20.38 ? 723  HOH   D O   1 
HETATM 10182 O  O   . HOH   KA 5 .   ? 50.491 -52.772 71.485  1.00 40.04 ? 724  HOH   D O   1 
HETATM 10183 O  O   . HOH   KA 5 .   ? 64.657 -53.808 30.963  1.00 61.35 ? 725  HOH   D O   1 
HETATM 10184 O  O   . HOH   KA 5 .   ? 79.315 -39.736 63.942  1.00 44.42 ? 726  HOH   D O   1 
HETATM 10185 O  O   . HOH   KA 5 .   ? 58.028 -54.154 72.976  1.00 46.89 ? 727  HOH   D O   1 
HETATM 10186 O  O   . HOH   KA 5 .   ? 54.629 -41.500 42.422  1.00 44.86 ? 728  HOH   D O   1 
HETATM 10187 O  O   . HOH   KA 5 .   ? 44.898 -46.901 63.704  1.00 49.64 ? 729  HOH   D O   1 
HETATM 10188 O  O   . HOH   KA 5 .   ? 69.450 -53.349 34.005  1.00 44.40 ? 730  HOH   D O   1 
HETATM 10189 O  O   . HOH   KA 5 .   ? 69.058 -43.774 76.052  1.00 51.27 ? 731  HOH   D O   1 
HETATM 10190 O  O   . HOH   KA 5 .   ? 79.262 -40.549 55.369  1.00 51.75 ? 732  HOH   D O   1 
HETATM 10191 O  O   . HOH   KA 5 .   ? 45.541 -55.160 42.898  1.00 51.02 ? 733  HOH   D O   1 
HETATM 10192 O  O   . HOH   KA 5 .   ? 47.959 -70.569 54.533  1.00 53.55 ? 734  HOH   D O   1 
HETATM 10193 O  O   . HOH   KA 5 .   ? 65.213 -31.660 65.171  1.00 43.82 ? 735  HOH   D O   1 
HETATM 10194 O  O   . HOH   KA 5 .   ? 54.005 -75.169 56.126  1.00 55.09 ? 736  HOH   D O   1 
HETATM 10195 O  O   . HOH   KA 5 .   ? 44.194 -69.211 63.140  1.00 51.84 ? 737  HOH   D O   1 
HETATM 10196 O  O   . HOH   KA 5 .   ? 47.398 -50.495 75.658  1.00 61.23 ? 738  HOH   D O   1 
HETATM 10197 O  O   . HOH   KA 5 .   ? 65.854 -29.945 49.388  1.00 43.24 ? 739  HOH   D O   1 
HETATM 10198 O  O   . HOH   KA 5 .   ? 50.648 -35.640 65.219  1.00 44.47 ? 740  HOH   D O   1 
HETATM 10199 O  O   . HOH   KA 5 .   ? 59.096 -33.948 35.916  1.00 54.31 ? 741  HOH   D O   1 
HETATM 10200 O  O   . HOH   KA 5 .   ? 61.243 -69.208 43.995  1.00 37.98 ? 742  HOH   D O   1 
HETATM 10201 O  O   . HOH   KA 5 .   ? 80.411 -47.370 56.448  1.00 40.74 ? 743  HOH   D O   1 
HETATM 10202 O  O   . HOH   KA 5 .   ? 70.902 -51.893 75.757  1.00 47.59 ? 744  HOH   D O   1 
HETATM 10203 O  O   . HOH   KA 5 .   ? 46.515 -68.263 67.192  1.00 57.79 ? 745  HOH   D O   1 
HETATM 10204 O  O   . HOH   KA 5 .   ? 52.174 -69.173 46.508  1.00 42.31 ? 746  HOH   D O   1 
HETATM 10205 O  O   . HOH   KA 5 .   ? 62.649 -55.566 31.593  1.00 47.58 ? 747  HOH   D O   1 
HETATM 10206 O  O   . HOH   KA 5 .   ? 55.481 -52.885 72.278  1.00 46.51 ? 748  HOH   D O   1 
HETATM 10207 O  O   . HOH   KA 5 .   ? 80.379 -43.865 53.051  1.00 49.99 ? 749  HOH   D O   1 
HETATM 10208 O  O   . HOH   KA 5 .   ? 65.219 -45.924 76.187  1.00 52.91 ? 750  HOH   D O   1 
HETATM 10209 O  O   . HOH   KA 5 .   ? 47.072 -59.762 46.531  1.00 25.20 ? 751  HOH   D O   1 
HETATM 10210 O  O   . HOH   KA 5 .   ? 79.288 -40.889 52.769  1.00 48.80 ? 752  HOH   D O   1 
HETATM 10211 O  O   . HOH   KA 5 .   ? 73.196 -55.259 75.611  1.00 49.79 ? 753  HOH   D O   1 
HETATM 10212 O  O   . HOH   KA 5 .   ? 78.302 -62.522 57.130  1.00 39.17 ? 754  HOH   D O   1 
HETATM 10213 O  O   . HOH   KA 5 .   ? 77.078 -45.202 46.063  1.00 48.75 ? 755  HOH   D O   1 
HETATM 10214 O  O   . HOH   KA 5 .   ? 65.271 -27.505 51.211  1.00 31.78 ? 756  HOH   D O   1 
HETATM 10215 O  O   . HOH   KA 5 .   ? 60.175 -65.710 41.723  1.00 57.11 ? 757  HOH   D O   1 
HETATM 10216 O  O   . HOH   KA 5 .   ? 47.626 -42.495 66.990  1.00 45.97 ? 758  HOH   D O   1 
HETATM 10217 O  O   . HOH   KA 5 .   ? 80.319 -46.407 71.330  1.00 54.49 ? 759  HOH   D O   1 
HETATM 10218 O  O   . HOH   KA 5 .   ? 46.938 -48.751 66.871  1.00 44.28 ? 760  HOH   D O   1 
HETATM 10219 O  O   . HOH   KA 5 .   ? 59.292 -68.120 45.086  1.00 44.12 ? 761  HOH   D O   1 
HETATM 10220 O  O   . HOH   KA 5 .   ? 55.228 -51.093 75.295  1.00 38.24 ? 762  HOH   D O   1 
HETATM 10221 O  O   . HOH   KA 5 .   ? 60.601 -51.503 32.841  1.00 41.40 ? 763  HOH   D O   1 
HETATM 10222 O  O   . HOH   KA 5 .   ? 63.957 -63.117 42.131  1.00 38.45 ? 764  HOH   D O   1 
HETATM 10223 O  O   . HOH   KA 5 .   ? 67.508 -63.823 39.650  1.00 43.14 ? 765  HOH   D O   1 
HETATM 10224 O  O   . HOH   KA 5 .   ? 44.414 -68.034 65.359  1.00 55.56 ? 766  HOH   D O   1 
HETATM 10225 O  O   . HOH   KA 5 .   ? 60.404 -54.360 32.953  1.00 41.76 ? 767  HOH   D O   1 
HETATM 10226 O  O   . HOH   KA 5 .   ? 69.273 -74.023 58.950  1.00 46.59 ? 768  HOH   D O   1 
HETATM 10227 O  O   . HOH   KA 5 .   ? 74.639 -79.822 42.715  1.00 48.92 ? 769  HOH   D O   1 
HETATM 10228 O  O   . HOH   KA 5 .   ? 50.482 -35.718 67.621  1.00 60.39 ? 770  HOH   D O   1 
HETATM 10229 O  O   . HOH   KA 5 .   ? 81.792 -58.286 55.880  1.00 58.09 ? 771  HOH   D O   1 
HETATM 10230 O  O   . HOH   KA 5 .   ? 49.145 -34.747 61.566  1.00 44.85 ? 772  HOH   D O   1 
HETATM 10231 O  O   . HOH   KA 5 .   ? 77.206 -39.178 54.512  1.00 51.86 ? 773  HOH   D O   1 
HETATM 10232 O  O   . HOH   KA 5 .   ? 53.442 -43.116 46.093  1.00 52.48 ? 774  HOH   D O   1 
HETATM 10233 O  O   . HOH   KA 5 .   ? 71.267 -47.984 76.230  1.00 48.42 ? 775  HOH   D O   1 
HETATM 10234 O  O   . HOH   KA 5 .   ? 78.878 -64.872 56.140  1.00 46.80 ? 776  HOH   D O   1 
HETATM 10235 O  O   . HOH   KA 5 .   ? 49.371 -51.740 37.717  1.00 39.34 ? 777  HOH   D O   1 
HETATM 10236 O  O   . HOH   KA 5 .   ? 55.226 -38.039 38.948  1.00 56.21 ? 778  HOH   D O   1 
HETATM 10237 O  O   . HOH   KA 5 .   ? 67.925 -72.402 55.259  1.00 55.51 ? 779  HOH   D O   1 
HETATM 10238 O  O   . HOH   KA 5 .   ? 58.663 -35.203 73.583  1.00 53.40 ? 780  HOH   D O   1 
HETATM 10239 O  O   . HOH   KA 5 .   ? 79.522 -55.424 43.510  1.00 56.68 ? 781  HOH   D O   1 
HETATM 10240 O  O   . HOH   KA 5 .   ? 58.354 -50.238 31.394  1.00 52.20 ? 782  HOH   D O   1 
HETATM 10241 O  O   . HOH   KA 5 .   ? 54.118 -37.556 73.986  1.00 46.99 ? 783  HOH   D O   1 
HETATM 10242 O  O   . HOH   KA 5 .   ? 46.789 -52.638 41.014  1.00 48.17 ? 784  HOH   D O   1 
HETATM 10243 O  O   . HOH   KA 5 .   ? 60.678 -54.063 76.179  1.00 48.29 ? 785  HOH   D O   1 
HETATM 10244 O  O   . HOH   KA 5 .   ? 82.279 -58.675 53.512  1.00 43.85 ? 786  HOH   D O   1 
HETATM 10245 O  O   . HOH   KA 5 .   ? 48.676 -65.647 47.615  1.00 33.17 ? 787  HOH   D O   1 
HETATM 10246 O  O   . HOH   KA 5 .   ? 42.254 -41.909 76.405  1.00 51.87 ? 788  HOH   D O   1 
HETATM 10247 O  O   . HOH   KA 5 .   ? 49.333 -67.610 49.685  1.00 32.82 ? 789  HOH   D O   1 
HETATM 10248 O  O   . HOH   KA 5 .   ? 80.545 -66.672 60.149  1.00 49.83 ? 790  HOH   D O   1 
HETATM 10249 O  O   . HOH   KA 5 .   ? 44.843 -68.178 53.030  1.00 30.85 ? 791  HOH   D O   1 
HETATM 10250 O  O   . HOH   KA 5 .   ? 78.960 -44.313 47.457  1.00 58.31 ? 792  HOH   D O   1 
HETATM 10251 O  O   . HOH   KA 5 .   ? 44.438 -69.003 56.057  1.00 37.75 ? 793  HOH   D O   1 
HETATM 10252 O  O   . HOH   KA 5 .   ? 63.383 -65.662 41.680  1.00 39.54 ? 794  HOH   D O   1 
HETATM 10253 O  O   . HOH   KA 5 .   ? 55.093 -64.659 39.858  1.00 50.79 ? 795  HOH   D O   1 
HETATM 10254 O  O   . HOH   KA 5 .   ? 62.467 -50.060 76.033  1.00 48.57 ? 796  HOH   D O   1 
HETATM 10255 O  O   . HOH   KA 5 .   ? 48.338 -61.551 48.466  1.00 35.52 ? 797  HOH   D O   1 
HETATM 10256 O  O   . HOH   KA 5 .   ? 78.403 -70.613 34.959  1.00 54.13 ? 798  HOH   D 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   . ALA A 2   ? 0.2516 0.2138 0.1756 0.0042  0.0337  0.0230  2   ALA A N   
2    C CA  . ALA A 2   ? 0.2534 0.2235 0.1801 0.0062  0.0412  0.0204  2   ALA A CA  
3    C C   . ALA A 2   ? 0.2534 0.2269 0.1851 0.0103  0.0377  0.0157  2   ALA A C   
4    O O   . ALA A 2   ? 0.2565 0.2223 0.1814 0.0114  0.0308  0.0147  2   ALA A O   
5    C CB  . ALA A 2   ? 0.2313 0.2120 0.1719 0.0021  0.0474  0.0219  2   ALA A CB  
6    N N   . HIS A 3   ? 0.2384 0.2230 0.1819 0.0122  0.0416  0.0131  3   HIS A N   
7    C CA  . HIS A 3   ? 0.2435 0.2285 0.1892 0.0166  0.0373  0.0091  3   HIS A CA  
8    C C   . HIS A 3   ? 0.2285 0.2131 0.1816 0.0139  0.0298  0.0092  3   HIS A C   
9    O O   . HIS A 3   ? 0.2381 0.2293 0.2026 0.0100  0.0299  0.0106  3   HIS A O   
10   C CB  . HIS A 3   ? 0.2364 0.2337 0.1929 0.0206  0.0426  0.0062  3   HIS A CB  
11   C CG  . HIS A 3   ? 0.2884 0.2859 0.2362 0.0251  0.0501  0.0047  3   HIS A CG  
12   N ND1 . HIS A 3   ? 0.3685 0.3659 0.3133 0.0330  0.0511  0.0002  3   HIS A ND1 
13   C CD2 . HIS A 3   ? 0.3183 0.3139 0.2569 0.0231  0.0568  0.0069  3   HIS A CD2 
14   C CE1 . HIS A 3   ? 0.3689 0.3661 0.3045 0.0360  0.0590  -0.0008 3   HIS A CE1 
15   N NE2 . HIS A 3   ? 0.3331 0.3294 0.2644 0.0296  0.0628  0.0034  3   HIS A NE2 
16   N N   . HIS A 4   ? 0.2252 0.2014 0.1707 0.0153  0.0236  0.0075  4   HIS A N   
17   C CA  . HIS A 4   ? 0.2272 0.2039 0.1788 0.0121  0.0174  0.0076  4   HIS A CA  
18   C C   . HIS A 4   ? 0.2121 0.1964 0.1746 0.0134  0.0173  0.0056  4   HIS A C   
19   O O   . HIS A 4   ? 0.2228 0.2091 0.1856 0.0183  0.0194  0.0034  4   HIS A O   
20   C CB  . HIS A 4   ? 0.2358 0.2012 0.1750 0.0120  0.0113  0.0067  4   HIS A CB  
21   C CG  . HIS A 4   ? 0.2227 0.1882 0.1659 0.0079  0.0054  0.0070  4   HIS A CG  
22   N ND1 . HIS A 4   ? 0.1907 0.1608 0.1408 0.0039  0.0040  0.0090  4   HIS A ND1 
23   C CD2 . HIS A 4   ? 0.2335 0.1942 0.1734 0.0069  0.0008  0.0055  4   HIS A CD2 
24   C CE1 . HIS A 4   ? 0.2085 0.1788 0.1605 0.0007  -0.0004 0.0084  4   HIS A CE1 
25   N NE2 . HIS A 4   ? 0.2154 0.1796 0.1608 0.0018  -0.0025 0.0066  4   HIS A NE2 
26   N N   . TRP A 5   ? 0.2011 0.1893 0.1721 0.0095  0.0145  0.0062  5   TRP A N   
27   C CA  . TRP A 5   ? 0.1890 0.1835 0.1690 0.0100  0.0132  0.0046  5   TRP A CA  
28   C C   . TRP A 5   ? 0.2236 0.2112 0.1965 0.0134  0.0087  0.0027  5   TRP A C   
29   O O   . TRP A 5   ? 0.2243 0.2013 0.1855 0.0136  0.0058  0.0025  5   TRP A O   
30   C CB  . TRP A 5   ? 0.1867 0.1845 0.1739 0.0048  0.0110  0.0053  5   TRP A CB  
31   C CG  . TRP A 5   ? 0.1793 0.1708 0.1606 0.0020  0.0063  0.0055  5   TRP A CG  
32   C CD1 . TRP A 5   ? 0.2058 0.1948 0.1843 -0.0003 0.0056  0.0068  5   TRP A CD1 
33   C CD2 . TRP A 5   ? 0.1836 0.1714 0.1612 0.0010  0.0020  0.0044  5   TRP A CD2 
34   N NE1 . TRP A 5   ? 0.1987 0.1849 0.1739 -0.0031 0.0014  0.0064  5   TRP A NE1 
35   C CE2 . TRP A 5   ? 0.1861 0.1705 0.1596 -0.0030 -0.0005 0.0051  5   TRP A CE2 
36   C CE3 . TRP A 5   ? 0.1941 0.1807 0.1710 0.0030  -0.0005 0.0031  5   TRP A CE3 
37   C CZ2 . TRP A 5   ? 0.1884 0.1689 0.1572 -0.0062 -0.0043 0.0047  5   TRP A CZ2 
38   C CZ3 . TRP A 5   ? 0.2147 0.1948 0.1850 0.0003  -0.0050 0.0030  5   TRP A CZ3 
39   C CH2 . TRP A 5   ? 0.2029 0.1798 0.1687 -0.0048 -0.0065 0.0039  5   TRP A CH2 
40   N N   . GLY A 6   ? 0.1962 0.1889 0.1756 0.0161  0.0077  0.0012  6   GLY A N   
41   C CA  . GLY A 6   ? 0.2088 0.1929 0.1807 0.0199  0.0027  -0.0003 6   GLY A CA  
42   C C   . GLY A 6   ? 0.1738 0.1649 0.1548 0.0212  0.0000  -0.0010 6   GLY A C   
43   O O   . GLY A 6   ? 0.1953 0.1942 0.1851 0.0166  -0.0001 -0.0002 6   GLY A O   
44   N N   . TYR A 7   ? 0.2119 0.1984 0.1892 0.0281  -0.0030 -0.0027 7   TYR A N   
45   C CA  . TYR A 7   ? 0.2012 0.1932 0.1858 0.0311  -0.0071 -0.0034 7   TYR A CA  
46   C C   . TYR A 7   ? 0.2224 0.2231 0.2148 0.0404  -0.0050 -0.0057 7   TYR A C   
47   O O   . TYR A 7   ? 0.2489 0.2524 0.2458 0.0456  -0.0098 -0.0066 7   TYR A O   
48   C CB  . TYR A 7   ? 0.2254 0.2020 0.1971 0.0307  -0.0149 -0.0029 7   TYR A CB  
49   C CG  . TYR A 7   ? 0.2189 0.1907 0.1855 0.0210  -0.0166 -0.0008 7   TYR A CG  
50   C CD1 . TYR A 7   ? 0.2110 0.1901 0.1845 0.0162  -0.0181 -0.0001 7   TYR A CD1 
51   C CD2 . TYR A 7   ? 0.2402 0.2008 0.1951 0.0166  -0.0168 0.0002  7   TYR A CD2 
52   C CE1 . TYR A 7   ? 0.2130 0.1885 0.1816 0.0081  -0.0186 0.0012  7   TYR A CE1 
53   C CE2 . TYR A 7   ? 0.2501 0.2091 0.2023 0.0081  -0.0177 0.0017  7   TYR A CE2 
54   C CZ  . TYR A 7   ? 0.2157 0.1821 0.1746 0.0044  -0.0181 0.0021  7   TYR A CZ  
55   O OH  . TYR A 7   ? 0.2421 0.2078 0.1982 -0.0033 -0.0181 0.0031  7   TYR A OH  
56   N N   . GLY A 8   ? 0.2242 0.2297 0.2181 0.0431  0.0021  -0.0066 8   GLY A N   
57   C CA  . GLY A 8   ? 0.2367 0.2524 0.2385 0.0523  0.0059  -0.0093 8   GLY A CA  
58   C C   . GLY A 8   ? 0.2172 0.2555 0.2394 0.0501  0.0102  -0.0090 8   GLY A C   
59   O O   . GLY A 8   ? 0.2001 0.2442 0.2293 0.0418  0.0091  -0.0070 8   GLY A O   
60   N N   . LYS A 9   ? 0.2239 0.2749 0.2553 0.0577  0.0153  -0.0115 9   LYS A N   
61   C CA  . LYS A 9   ? 0.2133 0.2883 0.2660 0.0560  0.0192  -0.0116 9   LYS A CA  
62   C C   . LYS A 9   ? 0.2109 0.2922 0.2673 0.0458  0.0263  -0.0090 9   LYS A C   
63   O O   . LYS A 9   ? 0.2082 0.3039 0.2792 0.0395  0.0269  -0.0079 9   LYS A O   
64   C CB  . LYS A 9   ? 0.2302 0.3189 0.2922 0.0668  0.0244  -0.0150 9   LYS A CB  
65   C CG  . LYS A 9   ? 0.2968 0.3777 0.3544 0.0789  0.0175  -0.0179 9   LYS A CG  
66   C CD  . LYS A 9   ? 0.2879 0.3750 0.3560 0.0779  0.0078  -0.0170 9   LYS A CD  
67   C CE  . LYS A 9   ? 0.4050 0.4881 0.4726 0.0921  0.0003  -0.0199 9   LYS A CE  
68   N NZ  . LYS A 9   ? 0.4679 0.5742 0.5544 0.1026  0.0057  -0.0236 9   LYS A NZ  
69   N N   . HIS A 10  ? 0.2191 0.2892 0.2617 0.0439  0.0315  -0.0080 10  HIS A N   
70   C CA  . HIS A 10  ? 0.1960 0.2699 0.2402 0.0350  0.0378  -0.0051 10  HIS A CA  
71   C C   . HIS A 10  ? 0.1998 0.2597 0.2345 0.0273  0.0338  -0.0023 10  HIS A C   
72   O O   . HIS A 10  ? 0.2253 0.2886 0.2645 0.0193  0.0363  0.0002  10  HIS A O   
73   C CB  . HIS A 10  ? 0.2360 0.3078 0.2712 0.0375  0.0468  -0.0053 10  HIS A CB  
74   C CG  . HIS A 10  ? 0.2769 0.3651 0.3223 0.0448  0.0535  -0.0083 10  HIS A CG  
75   N ND1 . HIS A 10  ? 0.3394 0.4218 0.3747 0.0549  0.0563  -0.0117 10  HIS A ND1 
76   C CD2 . HIS A 10  ? 0.2960 0.4071 0.3612 0.0433  0.0585  -0.0086 10  HIS A CD2 
77   C CE1 . HIS A 10  ? 0.3519 0.4541 0.4013 0.0604  0.0633  -0.0143 10  HIS A CE1 
78   N NE2 . HIS A 10  ? 0.2952 0.4163 0.3640 0.0533  0.0643  -0.0124 10  HIS A NE2 
79   N N   . ASN A 11  ? 0.1860 0.2302 0.2080 0.0293  0.0273  -0.0027 11  ASN A N   
80   C CA  . ASN A 11  ? 0.1789 0.2116 0.1925 0.0226  0.0242  -0.0004 11  ASN A CA  
81   C C   . ASN A 11  ? 0.1839 0.2132 0.1988 0.0200  0.0167  -0.0005 11  ASN A C   
82   O O   . ASN A 11  ? 0.1723 0.1928 0.1804 0.0155  0.0140  0.0008  11  ASN A O   
83   C CB  . ASN A 11  ? 0.2062 0.2239 0.2027 0.0246  0.0241  -0.0002 11  ASN A CB  
84   C CG  . ASN A 11  ? 0.2395 0.2468 0.2265 0.0307  0.0188  -0.0025 11  ASN A CG  
85   O OD1 . ASN A 11  ? 0.2399 0.2497 0.2321 0.0336  0.0145  -0.0038 11  ASN A OD1 
86   N ND2 . ASN A 11  ? 0.2649 0.2586 0.2363 0.0323  0.0183  -0.0029 11  ASN A ND2 
87   N N   . GLY A 12  ? 0.1696 0.2064 0.1931 0.0229  0.0131  -0.0020 12  GLY A N   
88   C CA  . GLY A 12  ? 0.1834 0.2143 0.2041 0.0210  0.0056  -0.0020 12  GLY A CA  
89   C C   . GLY A 12  ? 0.1750 0.2118 0.2036 0.0136  0.0043  -0.0013 12  GLY A C   
90   O O   . GLY A 12  ? 0.1723 0.2158 0.2079 0.0090  0.0089  -0.0004 12  GLY A O   
91   N N   . PRO A 13  ? 0.1640 0.1965 0.1896 0.0122  -0.0021 -0.0016 13  PRO A N   
92   C CA  . PRO A 13  ? 0.1764 0.2104 0.2049 0.0050  -0.0037 -0.0015 13  PRO A CA  
93   C C   . PRO A 13  ? 0.1477 0.1944 0.1899 0.0013  -0.0011 -0.0018 13  PRO A C   
94   O O   . PRO A 13  ? 0.1678 0.2128 0.2103 -0.0048 0.0010  -0.0015 13  PRO A O   
95   C CB  . PRO A 13  ? 0.1977 0.2269 0.2209 0.0062  -0.0113 -0.0021 13  PRO A CB  
96   C CG  . PRO A 13  ? 0.1910 0.2083 0.2019 0.0109  -0.0130 -0.0015 13  PRO A CG  
97   C CD  . PRO A 13  ? 0.1874 0.2088 0.2020 0.0164  -0.0079 -0.0019 13  PRO A CD  
98   N N   . GLU A 14  ? 0.1473 0.2070 0.2012 0.0046  -0.0013 -0.0027 14  GLU A N   
99   C CA  . GLU A 14  ? 0.1435 0.2161 0.2111 -0.0010 0.0006  -0.0029 14  GLU A CA  
100  C C   . GLU A 14  ? 0.1662 0.2395 0.2354 -0.0050 0.0086  -0.0013 14  GLU A C   
101  O O   . GLU A 14  ? 0.1747 0.2539 0.2517 -0.0118 0.0104  -0.0010 14  GLU A O   
102  C CB  . GLU A 14  ? 0.1401 0.2297 0.2224 0.0032  -0.0013 -0.0041 14  GLU A CB  
103  C CG  . GLU A 14  ? 0.1438 0.2413 0.2309 0.0096  0.0052  -0.0042 14  GLU A CG  
104  C CD  . GLU A 14  ? 0.2037 0.3225 0.3094 0.0126  0.0049  -0.0056 14  GLU A CD  
105  O OE1 . GLU A 14  ? 0.1972 0.3261 0.3139 0.0077  -0.0002 -0.0062 14  GLU A OE1 
106  O OE2 . GLU A 14  ? 0.2259 0.3528 0.3362 0.0196  0.0100  -0.0065 14  GLU A OE2 
107  N N   . HIS A 15  ? 0.1654 0.2316 0.2260 -0.0015 0.0128  -0.0002 15  HIS A N   
108  C CA  . HIS A 15  ? 0.1767 0.2414 0.2358 -0.0046 0.0200  0.0019  15  HIS A CA  
109  C C   . HIS A 15  ? 0.1518 0.2020 0.1994 -0.0074 0.0198  0.0033  15  HIS A C   
110  O O   . HIS A 15  ? 0.1691 0.2159 0.2142 -0.0102 0.0245  0.0054  15  HIS A O   
111  C CB  . HIS A 15  ? 0.1781 0.2453 0.2346 0.0016  0.0251  0.0021  15  HIS A CB  
112  C CG  . HIS A 15  ? 0.2111 0.2951 0.2808 0.0056  0.0268  0.0004  15  HIS A CG  
113  N ND1 . HIS A 15  ? 0.2477 0.3472 0.3326 0.0002  0.0292  0.0006  15  HIS A ND1 
114  C CD2 . HIS A 15  ? 0.2344 0.3229 0.3054 0.0146  0.0258  -0.0018 15  HIS A CD2 
115  C CE1 . HIS A 15  ? 0.2642 0.3795 0.3609 0.0058  0.0299  -0.0014 15  HIS A CE1 
116  N NE2 . HIS A 15  ? 0.2432 0.3515 0.3313 0.0153  0.0281  -0.0029 15  HIS A NE2 
117  N N   . TRP A 16  ? 0.1495 0.1912 0.1899 -0.0067 0.0146  0.0023  16  TRP A N   
118  C CA  . TRP A 16  ? 0.1478 0.1786 0.1792 -0.0082 0.0149  0.0034  16  TRP A CA  
119  C C   . TRP A 16  ? 0.1685 0.1973 0.2025 -0.0136 0.0170  0.0042  16  TRP A C   
120  O O   . TRP A 16  ? 0.1870 0.2086 0.2154 -0.0137 0.0189  0.0059  16  TRP A O   
121  C CB  . TRP A 16  ? 0.1577 0.1826 0.1830 -0.0079 0.0098  0.0020  16  TRP A CB  
122  C CG  . TRP A 16  ? 0.1724 0.1936 0.1906 -0.0031 0.0072  0.0018  16  TRP A CG  
123  C CD1 . TRP A 16  ? 0.1592 0.1797 0.1743 0.0016  0.0091  0.0023  16  TRP A CD1 
124  C CD2 . TRP A 16  ? 0.1699 0.1855 0.1815 -0.0030 0.0021  0.0010  16  TRP A CD2 
125  N NE1 . TRP A 16  ? 0.1706 0.1841 0.1774 0.0049  0.0050  0.0016  16  TRP A NE1 
126  C CE2 . TRP A 16  ? 0.1617 0.1722 0.1662 0.0018  0.0006  0.0011  16  TRP A CE2 
127  C CE3 . TRP A 16  ? 0.1743 0.1878 0.1838 -0.0067 -0.0010 0.0001  16  TRP A CE3 
128  C CZ2 . TRP A 16  ? 0.1849 0.1869 0.1800 0.0022  -0.0043 0.0009  16  TRP A CZ2 
129  C CZ3 . TRP A 16  ? 0.1714 0.1781 0.1718 -0.0065 -0.0053 0.0000  16  TRP A CZ3 
130  C CH2 . TRP A 16  ? 0.1858 0.1862 0.1789 -0.0023 -0.0071 0.0007  16  TRP A CH2 
131  N N   . HIS A 17  ? 0.1539 0.1876 0.1955 -0.0179 0.0160  0.0030  17  HIS A N   
132  C CA  . HIS A 17  ? 0.1556 0.1845 0.1982 -0.0233 0.0177  0.0035  17  HIS A CA  
133  C C   . HIS A 17  ? 0.1716 0.1983 0.2132 -0.0247 0.0230  0.0068  17  HIS A C   
134  O O   . HIS A 17  ? 0.1955 0.2132 0.2338 -0.0278 0.0240  0.0079  17  HIS A O   
135  C CB  . HIS A 17  ? 0.1951 0.2301 0.2460 -0.0287 0.0156  0.0017  17  HIS A CB  
136  C CG  . HIS A 17  ? 0.1822 0.2305 0.2435 -0.0301 0.0176  0.0025  17  HIS A CG  
137  N ND1 . HIS A 17  ? 0.2330 0.2839 0.2993 -0.0358 0.0221  0.0044  17  HIS A ND1 
138  C CD2 . HIS A 17  ? 0.1476 0.2075 0.2152 -0.0259 0.0164  0.0017  17  HIS A CD2 
139  C CE1 . HIS A 17  ? 0.2077 0.2740 0.2847 -0.0356 0.0240  0.0046  17  HIS A CE1 
140  N NE2 . HIS A 17  ? 0.1920 0.2641 0.2703 -0.0289 0.0204  0.0027  17  HIS A NE2 
141  N N   . LYS A 18  ? 0.1602 0.1938 0.2035 -0.0224 0.0266  0.0082  18  LYS A N   
142  C CA  . LYS A 18  ? 0.1462 0.1777 0.1869 -0.0246 0.0323  0.0115  18  LYS A CA  
143  C C   . LYS A 18  ? 0.1814 0.1995 0.2101 -0.0222 0.0322  0.0137  18  LYS A C   
144  O O   . LYS A 18  ? 0.1791 0.1901 0.2031 -0.0252 0.0352  0.0168  18  LYS A O   
145  C CB  . LYS A 18  ? 0.1817 0.2241 0.2257 -0.0217 0.0368  0.0119  18  LYS A CB  
146  C CG  . LYS A 18  ? 0.2631 0.3214 0.3217 -0.0244 0.0371  0.0101  18  LYS A CG  
147  C CD  . LYS A 18  ? 0.2774 0.3482 0.3404 -0.0193 0.0418  0.0096  18  LYS A CD  
148  C CE  . LYS A 18  ? 0.2933 0.3830 0.3735 -0.0203 0.0409  0.0074  18  LYS A CE  
149  N NZ  . LYS A 18  ? 0.3553 0.4575 0.4398 -0.0135 0.0465  0.0064  18  LYS A NZ  
150  N N   . ASP A 19  ? 0.1741 0.1887 0.1977 -0.0173 0.0284  0.0123  19  ASP A N   
151  C CA  . ASP A 19  ? 0.1866 0.1907 0.2008 -0.0149 0.0270  0.0140  19  ASP A CA  
152  C C   . ASP A 19  ? 0.1975 0.1971 0.2120 -0.0146 0.0227  0.0122  19  ASP A C   
153  O O   . ASP A 19  ? 0.1872 0.1791 0.1970 -0.0132 0.0216  0.0136  19  ASP A O   
154  C CB  . ASP A 19  ? 0.1720 0.1756 0.1790 -0.0100 0.0262  0.0140  19  ASP A CB  
155  C CG  . ASP A 19  ? 0.2041 0.2110 0.2086 -0.0091 0.0312  0.0154  19  ASP A CG  
156  O OD1 . ASP A 19  ? 0.2473 0.2492 0.2463 -0.0109 0.0346  0.0185  19  ASP A OD1 
157  O OD2 . ASP A 19  ? 0.2272 0.2415 0.2350 -0.0064 0.0319  0.0132  19  ASP A OD2 
158  N N   . PHE A 20  ? 0.1685 0.1730 0.1883 -0.0155 0.0204  0.0090  20  PHE A N   
159  C CA  . PHE A 20  ? 0.1857 0.1874 0.2052 -0.0152 0.0174  0.0066  20  PHE A CA  
160  C C   . PHE A 20  ? 0.1862 0.1886 0.2106 -0.0192 0.0171  0.0043  20  PHE A C   
161  O O   . PHE A 20  ? 0.2092 0.2169 0.2362 -0.0204 0.0151  0.0020  20  PHE A O   
162  C CB  . PHE A 20  ? 0.1768 0.1818 0.1941 -0.0130 0.0147  0.0051  20  PHE A CB  
163  C CG  . PHE A 20  ? 0.1629 0.1664 0.1744 -0.0098 0.0143  0.0070  20  PHE A CG  
164  C CD1 . PHE A 20  ? 0.1897 0.1894 0.1978 -0.0083 0.0129  0.0079  20  PHE A CD1 
165  C CD2 . PHE A 20  ? 0.1816 0.1873 0.1911 -0.0080 0.0149  0.0075  20  PHE A CD2 
166  C CE1 . PHE A 20  ? 0.1747 0.1721 0.1764 -0.0062 0.0117  0.0095  20  PHE A CE1 
167  C CE2 . PHE A 20  ? 0.1791 0.1810 0.1809 -0.0052 0.0144  0.0087  20  PHE A CE2 
168  C CZ  . PHE A 20  ? 0.1926 0.1900 0.1899 -0.0049 0.0125  0.0099  20  PHE A CZ  
169  N N   . PRO A 21  ? 0.1657 0.1615 0.1903 -0.0217 0.0185  0.0049  21  PRO A N   
170  C CA  . PRO A 21  ? 0.1954 0.1909 0.2238 -0.0268 0.0180  0.0027  21  PRO A CA  
171  C C   . PRO A 21  ? 0.1863 0.1810 0.2135 -0.0266 0.0152  -0.0016 21  PRO A C   
172  O O   . PRO A 21  ? 0.2048 0.2009 0.2344 -0.0309 0.0136  -0.0040 21  PRO A O   
173  C CB  . PRO A 21  ? 0.2388 0.2233 0.2646 -0.0294 0.0198  0.0046  21  PRO A CB  
174  C CG  . PRO A 21  ? 0.2512 0.2304 0.2716 -0.0245 0.0206  0.0076  21  PRO A CG  
175  C CD  . PRO A 21  ? 0.1775 0.1652 0.1977 -0.0208 0.0204  0.0084  21  PRO A CD  
176  N N   . ILE A 22  ? 0.1715 0.1649 0.1952 -0.0225 0.0147  -0.0027 22  ILE A N   
177  C CA  A ILE A 22  ? 0.1751 0.1689 0.1967 -0.0226 0.0132  -0.0067 22  ILE A CA  
178  C CA  B ILE A 22  ? 0.1765 0.1702 0.1982 -0.0227 0.0132  -0.0067 22  ILE A CA  
179  C C   . ILE A 22  ? 0.1902 0.1909 0.2122 -0.0246 0.0107  -0.0075 22  ILE A C   
180  O O   . ILE A 22  ? 0.1951 0.1952 0.2137 -0.0263 0.0090  -0.0106 22  ILE A O   
181  C CB  A ILE A 22  ? 0.1787 0.1726 0.1981 -0.0183 0.0139  -0.0072 22  ILE A CB  
182  C CB  B ILE A 22  ? 0.1791 0.1724 0.1985 -0.0183 0.0140  -0.0073 22  ILE A CB  
183  C CG1 A ILE A 22  ? 0.1750 0.1685 0.1916 -0.0188 0.0141  -0.0118 22  ILE A CG1 
184  C CG1 B ILE A 22  ? 0.1778 0.1699 0.1945 -0.0186 0.0144  -0.0120 22  ILE A CG1 
185  C CG2 A ILE A 22  ? 0.1858 0.1857 0.2046 -0.0167 0.0129  -0.0048 22  ILE A CG2 
186  C CG2 B ILE A 22  ? 0.1807 0.1804 0.1994 -0.0167 0.0130  -0.0053 22  ILE A CG2 
187  C CD1 A ILE A 22  ? 0.1845 0.1694 0.1998 -0.0195 0.0150  -0.0149 22  ILE A CD1 
188  C CD1 B ILE A 22  ? 0.1753 0.1711 0.1923 -0.0147 0.0158  -0.0127 22  ILE A CD1 
189  N N   . ALA A 23  ? 0.1777 0.1842 0.2027 -0.0240 0.0102  -0.0049 23  ALA A N   
190  C CA  . ALA A 23  ? 0.1788 0.1912 0.2048 -0.0249 0.0069  -0.0056 23  ALA A CA  
191  C C   . ALA A 23  ? 0.1724 0.1853 0.2003 -0.0295 0.0043  -0.0082 23  ALA A C   
192  O O   . ALA A 23  ? 0.1929 0.2085 0.2189 -0.0301 0.0003  -0.0095 23  ALA A O   
193  C CB  . ALA A 23  ? 0.1786 0.1980 0.2099 -0.0231 0.0075  -0.0030 23  ALA A CB  
194  N N   . LYS A 24  ? 0.1894 0.1986 0.2200 -0.0331 0.0058  -0.0088 24  LYS A N   
195  C CA  . LYS A 24  ? 0.1860 0.1943 0.2177 -0.0386 0.0029  -0.0116 24  LYS A CA  
196  C C   . LYS A 24  ? 0.2025 0.1998 0.2260 -0.0396 0.0032  -0.0154 24  LYS A C   
197  O O   . LYS A 24  ? 0.2340 0.2261 0.2564 -0.0445 0.0016  -0.0180 24  LYS A O   
198  C CB  . LYS A 24  ? 0.2238 0.2346 0.2633 -0.0431 0.0043  -0.0098 24  LYS A CB  
199  C CG  . LYS A 24  ? 0.2607 0.2853 0.3095 -0.0419 0.0045  -0.0071 24  LYS A CG  
200  C CD  . LYS A 24  ? 0.3583 0.3884 0.4162 -0.0480 0.0063  -0.0056 24  LYS A CD  
201  C CE  . LYS A 24  ? 0.4015 0.4471 0.4695 -0.0457 0.0079  -0.0033 24  LYS A CE  
202  N NZ  . LYS A 24  ? 0.4411 0.4991 0.5159 -0.0439 0.0022  -0.0051 24  LYS A NZ  
203  N N   . GLY A 25  ? 0.2175 0.2117 0.2354 -0.0353 0.0052  -0.0161 25  GLY A N   
204  C CA  . GLY A 25  ? 0.2289 0.2145 0.2400 -0.0344 0.0070  -0.0200 25  GLY A CA  
205  C C   . GLY A 25  ? 0.2468 0.2305 0.2503 -0.0374 0.0044  -0.0242 25  GLY A C   
206  O O   . GLY A 25  ? 0.2388 0.2269 0.2420 -0.0405 0.0000  -0.0239 25  GLY A O   
207  N N   . GLU A 26  ? 0.2197 0.1964 0.2164 -0.0359 0.0071  -0.0282 26  GLU A N   
208  C CA  . GLU A 26  ? 0.2666 0.2386 0.2532 -0.0388 0.0058  -0.0330 26  GLU A CA  
209  C C   . GLU A 26  ? 0.2553 0.2321 0.2354 -0.0379 0.0065  -0.0331 26  GLU A C   
210  O O   . GLU A 26  ? 0.3069 0.2801 0.2766 -0.0410 0.0050  -0.0364 26  GLU A O   
211  C CB  . GLU A 26  ? 0.2711 0.2318 0.2525 -0.0371 0.0092  -0.0381 26  GLU A CB  
212  C CG  . GLU A 26  ? 0.3150 0.2664 0.2993 -0.0394 0.0079  -0.0382 26  GLU A CG  
213  C CD  . GLU A 26  ? 0.4344 0.3851 0.4175 -0.0471 0.0021  -0.0389 26  GLU A CD  
214  O OE1 . GLU A 26  ? 0.4777 0.4251 0.4512 -0.0499 -0.0003 -0.0430 26  GLU A OE1 
215  O OE2 . GLU A 26  ? 0.4704 0.4250 0.4621 -0.0504 -0.0001 -0.0351 26  GLU A OE2 
216  N N   . ARG A 27  ? 0.2280 0.2119 0.2125 -0.0345 0.0088  -0.0296 27  ARG A N   
217  C CA  A ARG A 27  ? 0.2239 0.2115 0.2020 -0.0347 0.0103  -0.0294 27  ARG A CA  
218  C CA  B ARG A 27  ? 0.2234 0.2108 0.2009 -0.0350 0.0098  -0.0295 27  ARG A CA  
219  C C   . ARG A 27  ? 0.2122 0.2058 0.1938 -0.0342 0.0076  -0.0242 27  ARG A C   
220  O O   . ARG A 27  ? 0.2267 0.2244 0.2090 -0.0327 0.0101  -0.0224 27  ARG A O   
221  C CB  A ARG A 27  ? 0.2363 0.2256 0.2154 -0.0311 0.0167  -0.0319 27  ARG A CB  
222  C CB  B ARG A 27  ? 0.2304 0.2191 0.2064 -0.0323 0.0163  -0.0324 27  ARG A CB  
223  C CG  A ARG A 27  ? 0.2522 0.2461 0.2244 -0.0325 0.0202  -0.0329 27  ARG A CG  
224  C CG  B ARG A 27  ? 0.2257 0.2073 0.1982 -0.0310 0.0194  -0.0382 27  ARG A CG  
225  C CD  A ARG A 27  ? 0.2327 0.2322 0.2107 -0.0280 0.0268  -0.0353 27  ARG A CD  
226  C CD  B ARG A 27  ? 0.2276 0.2137 0.1983 -0.0280 0.0263  -0.0416 27  ARG A CD  
227  N NE  A ARG A 27  ? 0.1452 0.1546 0.1247 -0.0292 0.0292  -0.0329 27  ARG A NE  
228  N NE  B ARG A 27  ? 0.2095 0.2048 0.1915 -0.0232 0.0292  -0.0391 27  ARG A NE  
229  C CZ  A ARG A 27  ? 0.2505 0.2678 0.2327 -0.0276 0.0352  -0.0356 27  ARG A CZ  
230  C CZ  B ARG A 27  ? 0.2379 0.2321 0.2289 -0.0175 0.0300  -0.0389 27  ARG A CZ  
231  N NH1 A ARG A 27  ? 0.3069 0.3235 0.2906 -0.0231 0.0399  -0.0412 27  ARG A NH1 
232  N NH1 B ARG A 27  ? 0.1937 0.1971 0.1943 -0.0133 0.0317  -0.0367 27  ARG A NH1 
233  N NH2 A ARG A 27  ? 0.2849 0.3113 0.2686 -0.0305 0.0367  -0.0329 27  ARG A NH2 
234  N NH2 B ARG A 27  ? 0.2789 0.2619 0.2689 -0.0165 0.0282  -0.0407 27  ARG A NH2 
235  N N   . GLN A 28  ? 0.2171 0.2117 0.2015 -0.0352 0.0025  -0.0218 28  GLN A N   
236  C CA  . GLN A 28  ? 0.2033 0.2022 0.1911 -0.0333 0.0003  -0.0174 28  GLN A CA  
237  C C   . GLN A 28  ? 0.2039 0.2010 0.1818 -0.0351 -0.0037 -0.0161 28  GLN A C   
238  O O   . GLN A 28  ? 0.2332 0.2266 0.2027 -0.0382 -0.0067 -0.0180 28  GLN A O   
239  C CB  . GLN A 28  ? 0.2039 0.2063 0.2009 -0.0324 -0.0025 -0.0155 28  GLN A CB  
240  C CG  . GLN A 28  ? 0.1905 0.1930 0.1955 -0.0308 0.0016  -0.0152 28  GLN A CG  
241  C CD  . GLN A 28  ? 0.1787 0.1831 0.1855 -0.0271 0.0044  -0.0124 28  GLN A CD  
242  O OE1 . GLN A 28  ? 0.1823 0.1897 0.1908 -0.0251 0.0030  -0.0096 28  GLN A OE1 
243  N NE2 . GLN A 28  ? 0.1917 0.1942 0.1978 -0.0256 0.0080  -0.0136 28  GLN A NE2 
244  N N   . SER A 29  ? 0.1913 0.1895 0.1690 -0.0332 -0.0044 -0.0128 29  SER A N   
245  C CA  . SER A 29  ? 0.1896 0.1834 0.1568 -0.0345 -0.0084 -0.0108 29  SER A CA  
246  C C   . SER A 29  ? 0.2152 0.2096 0.1863 -0.0305 -0.0126 -0.0077 29  SER A C   
247  O O   . SER A 29  ? 0.2052 0.2040 0.1859 -0.0272 -0.0104 -0.0068 29  SER A O   
248  C CB  . SER A 29  ? 0.2130 0.2054 0.1735 -0.0369 -0.0045 -0.0100 29  SER A CB  
249  O OG  . SER A 29  ? 0.2122 0.2052 0.1688 -0.0400 0.0000  -0.0133 29  SER A OG  
250  N N   . PRO A 30  ? 0.2152 0.2044 0.1780 -0.0302 -0.0186 -0.0060 30  PRO A N   
251  C CA  . PRO A 30  ? 0.2129 0.1948 0.1614 -0.0343 -0.0220 -0.0061 30  PRO A CA  
252  C C   . PRO A 30  ? 0.2330 0.2165 0.1824 -0.0354 -0.0260 -0.0084 30  PRO A C   
253  O O   . PRO A 30  ? 0.2209 0.2118 0.1831 -0.0335 -0.0257 -0.0098 30  PRO A O   
254  C CB  . PRO A 30  ? 0.2345 0.2087 0.1750 -0.0317 -0.0280 -0.0027 30  PRO A CB  
255  C CG  . PRO A 30  ? 0.2276 0.2090 0.1824 -0.0247 -0.0301 -0.0024 30  PRO A CG  
256  C CD  . PRO A 30  ? 0.2284 0.2176 0.1947 -0.0248 -0.0226 -0.0037 30  PRO A CD  
257  N N   . VAL A 31  ? 0.2360 0.2122 0.1710 -0.0392 -0.0295 -0.0089 31  VAL A N   
258  C CA  . VAL A 31  ? 0.2337 0.2098 0.1667 -0.0411 -0.0348 -0.0111 31  VAL A CA  
259  C C   . VAL A 31  ? 0.2610 0.2282 0.1793 -0.0415 -0.0434 -0.0087 31  VAL A C   
260  O O   . VAL A 31  ? 0.2777 0.2364 0.1841 -0.0420 -0.0439 -0.0055 31  VAL A O   
261  C CB  . VAL A 31  ? 0.2406 0.2147 0.1674 -0.0461 -0.0296 -0.0154 31  VAL A CB  
262  C CG1 . VAL A 31  ? 0.2693 0.2501 0.2096 -0.0448 -0.0217 -0.0177 31  VAL A CG1 
263  C CG2 . VAL A 31  ? 0.2814 0.2472 0.1898 -0.0506 -0.0257 -0.0150 31  VAL A CG2 
264  N N   . ASP A 32  ? 0.2535 0.2220 0.1720 -0.0418 -0.0510 -0.0099 32  ASP A N   
265  C CA  . ASP A 32  ? 0.2653 0.2239 0.1670 -0.0430 -0.0600 -0.0081 32  ASP A CA  
266  C C   . ASP A 32  ? 0.3087 0.2574 0.1904 -0.0503 -0.0564 -0.0099 32  ASP A C   
267  O O   . ASP A 32  ? 0.3296 0.2810 0.2127 -0.0538 -0.0514 -0.0144 32  ASP A O   
268  C CB  . ASP A 32  ? 0.2625 0.2273 0.1720 -0.0410 -0.0701 -0.0090 32  ASP A CB  
269  C CG  . ASP A 32  ? 0.3227 0.2763 0.2137 -0.0417 -0.0810 -0.0068 32  ASP A CG  
270  O OD1 . ASP A 32  ? 0.3352 0.2800 0.2169 -0.0384 -0.0845 -0.0027 32  ASP A OD1 
271  O OD2 . ASP A 32  ? 0.3572 0.3096 0.2419 -0.0457 -0.0865 -0.0092 32  ASP A OD2 
272  N N   . ILE A 33  ? 0.3091 0.2453 0.1711 -0.0526 -0.0588 -0.0066 33  ILE A N   
273  C CA  . ILE A 33  ? 0.3242 0.2505 0.1644 -0.0600 -0.0558 -0.0079 33  ILE A CA  
274  C C   . ILE A 33  ? 0.3446 0.2625 0.1713 -0.0607 -0.0667 -0.0070 33  ILE A C   
275  O O   . ILE A 33  ? 0.3683 0.2788 0.1891 -0.0574 -0.0739 -0.0021 33  ILE A O   
276  C CB  . ILE A 33  ? 0.3160 0.2338 0.1425 -0.0635 -0.0504 -0.0043 33  ILE A CB  
277  C CG1 . ILE A 33  ? 0.3425 0.2706 0.1855 -0.0620 -0.0403 -0.0052 33  ILE A CG1 
278  C CG2 . ILE A 33  ? 0.3653 0.2749 0.1718 -0.0705 -0.0457 -0.0052 33  ILE A CG2 
279  C CD1 . ILE A 33  ? 0.3632 0.2856 0.1989 -0.0645 -0.0370 -0.0008 33  ILE A CD1 
280  N N   . ASP A 34  ? 0.3714 0.2915 0.1976 -0.0631 -0.0672 -0.0114 34  ASP A N   
281  C CA  . ASP A 34  ? 0.3740 0.2883 0.1914 -0.0629 -0.0760 -0.0105 34  ASP A CA  
282  C C   . ASP A 34  ? 0.4369 0.3391 0.2323 -0.0682 -0.0707 -0.0101 34  ASP A C   
283  O O   . ASP A 34  ? 0.4699 0.3723 0.2603 -0.0724 -0.0617 -0.0145 34  ASP A O   
284  C CB  . ASP A 34  ? 0.3774 0.2997 0.2053 -0.0633 -0.0805 -0.0154 34  ASP A CB  
285  C CG  . ASP A 34  ? 0.4188 0.3357 0.2372 -0.0634 -0.0900 -0.0144 34  ASP A CG  
286  O OD1 . ASP A 34  ? 0.4606 0.3673 0.2608 -0.0676 -0.0869 -0.0154 34  ASP A OD1 
287  O OD2 . ASP A 34  ? 0.4414 0.3644 0.2707 -0.0588 -0.1000 -0.0124 34  ASP A OD2 
288  N N   . THR A 35  ? 0.5189 0.2799 0.2560 -0.0997 -0.0771 0.0052  35  THR A N   
289  C CA  . THR A 35  ? 0.5498 0.3110 0.2660 -0.1106 -0.0736 0.0053  35  THR A CA  
290  C C   . THR A 35  ? 0.6341 0.3961 0.3388 -0.1134 -0.0725 -0.0034 35  THR A C   
291  O O   . THR A 35  ? 0.6844 0.4511 0.3722 -0.1216 -0.0668 -0.0062 35  THR A O   
292  C CB  . THR A 35  ? 0.5489 0.3020 0.2575 -0.1174 -0.0811 0.0167  35  THR A CB  
293  O OG1 . THR A 35  ? 0.5601 0.3037 0.2695 -0.1152 -0.0920 0.0199  35  THR A OG1 
294  C CG2 . THR A 35  ? 0.5234 0.2758 0.2439 -0.1148 -0.0818 0.0243  35  THR A CG2 
295  N N   . HIS A 36  ? 0.5737 0.3329 0.2878 -0.1070 -0.0775 -0.0078 36  HIS A N   
296  C CA  . HIS A 36  ? 0.6124 0.3721 0.3166 -0.1093 -0.0771 -0.0168 36  HIS A CA  
297  C C   . HIS A 36  ? 0.6091 0.3762 0.3167 -0.1064 -0.0663 -0.0299 36  HIS A C   
298  O O   . HIS A 36  ? 0.6400 0.4097 0.3353 -0.1101 -0.0627 -0.0387 36  HIS A O   
299  C CB  . HIS A 36  ? 0.6637 0.4181 0.3785 -0.1040 -0.0871 -0.0167 36  HIS A CB  
300  C CG  . HIS A 36  ? 0.8007 0.5475 0.5177 -0.1040 -0.0977 -0.0045 36  HIS A CG  
301  N ND1 . HIS A 36  ? 0.8140 0.5602 0.5511 -0.0956 -0.1040 -0.0018 36  HIS A ND1 
302  C CD2 . HIS A 36  ? 0.8505 0.5899 0.5529 -0.1115 -0.1029 0.0050  36  HIS A CD2 
303  C CE1 . HIS A 36  ? 0.8359 0.5743 0.5704 -0.0970 -0.1127 0.0085  36  HIS A CE1 
304  N NE2 . HIS A 36  ? 0.8424 0.5750 0.5562 -0.1069 -0.1126 0.0131  36  HIS A NE2 
305  N N   . THR A 37  ? 0.5490 0.3188 0.2740 -0.0995 -0.0614 -0.0319 37  THR A N   
306  C CA  . THR A 37  ? 0.5174 0.2914 0.2489 -0.0954 -0.0518 -0.0445 37  THR A CA  
307  C C   . THR A 37  ? 0.4926 0.2724 0.2192 -0.0976 -0.0415 -0.0467 37  THR A C   
308  O O   . THR A 37  ? 0.5620 0.3460 0.2878 -0.0962 -0.0323 -0.0588 37  THR A O   
309  C CB  . THR A 37  ? 0.5365 0.3087 0.2940 -0.0854 -0.0531 -0.0467 37  THR A CB  
310  O OG1 . THR A 37  ? 0.5764 0.3489 0.3464 -0.0819 -0.0558 -0.0367 37  THR A OG1 
311  C CG2 . THR A 37  ? 0.5438 0.3134 0.3066 -0.0837 -0.0611 -0.0484 37  THR A CG2 
312  N N   . ALA A 38  ? 0.4990 0.2799 0.2232 -0.1008 -0.0428 -0.0363 38  ALA A N   
313  C CA  . ALA A 38  ? 0.5210 0.3098 0.2394 -0.1042 -0.0332 -0.0383 38  ALA A CA  
314  C C   . ALA A 38  ? 0.5901 0.3878 0.2892 -0.1120 -0.0255 -0.0456 38  ALA A C   
315  O O   . ALA A 38  ? 0.6677 0.4642 0.3532 -0.1185 -0.0302 -0.0414 38  ALA A O   
316  C CB  . ALA A 38  ? 0.5185 0.3075 0.2365 -0.1079 -0.0375 -0.0249 38  ALA A CB  
317  N N   . LYS A 39  ? 0.5405 0.3474 0.2396 -0.1108 -0.0131 -0.0572 39  LYS A N   
318  C CA  . LYS A 39  ? 0.5511 0.3694 0.2357 -0.1165 -0.0034 -0.0669 39  LYS A CA  
319  C C   . LYS A 39  ? 0.5680 0.4027 0.2464 -0.1225 0.0078  -0.0670 39  LYS A C   
320  O O   . LYS A 39  ? 0.5298 0.3692 0.2192 -0.1182 0.0137  -0.0695 39  LYS A O   
321  C CB  . LYS A 39  ? 0.6146 0.4330 0.3075 -0.1089 0.0037  -0.0839 39  LYS A CB  
322  C CG  . LYS A 39  ? 0.7218 0.5293 0.4169 -0.1056 -0.0050 -0.0865 39  LYS A CG  
323  C CD  . LYS A 39  ? 0.7843 0.5938 0.4863 -0.0994 0.0032  -0.1040 39  LYS A CD  
324  C CE  . LYS A 39  ? 0.8603 0.6854 0.5480 -0.1052 0.0159  -0.1137 39  LYS A CE  
325  N NZ  . LYS A 39  ? 0.9024 0.7304 0.5962 -0.0992 0.0240  -0.1317 39  LYS A NZ  
326  N N   . TYR A 40  ? 0.5814 0.4257 0.2434 -0.1324 0.0114  -0.0655 40  TYR A N   
327  C CA  . TYR A 40  ? 0.5602 0.4236 0.2185 -0.1387 0.0237  -0.0670 40  TYR A CA  
328  C C   . TYR A 40  ? 0.5530 0.4297 0.2223 -0.1319 0.0387  -0.0846 40  TYR A C   
329  O O   . TYR A 40  ? 0.5662 0.4411 0.2374 -0.1268 0.0423  -0.0979 40  TYR A O   
330  C CB  . TYR A 40  ? 0.5813 0.4512 0.2208 -0.1506 0.0251  -0.0640 40  TYR A CB  
331  C CG  . TYR A 40  ? 0.6042 0.4964 0.2415 -0.1571 0.0399  -0.0692 40  TYR A CG  
332  C CD1 . TYR A 40  ? 0.5875 0.4892 0.2302 -0.1615 0.0422  -0.0603 40  TYR A CD1 
333  C CD2 . TYR A 40  ? 0.6295 0.5345 0.2616 -0.1586 0.0518  -0.0836 40  TYR A CD2 
334  C CE1 . TYR A 40  ? 0.6158 0.5405 0.2591 -0.1677 0.0562  -0.0655 40  TYR A CE1 
335  C CE2 . TYR A 40  ? 0.6731 0.6008 0.3056 -0.1645 0.0661  -0.0892 40  TYR A CE2 
336  C CZ  . TYR A 40  ? 0.6452 0.5832 0.2841 -0.1690 0.0684  -0.0803 40  TYR A CZ  
337  O OH  . TYR A 40  ? 0.6763 0.6388 0.3181 -0.1752 0.0827  -0.0862 40  TYR A OH  
338  N N   . ASP A 41  ? 0.5389 0.4289 0.2177 -0.1311 0.0471  -0.0850 41  ASP A N   
339  C CA  . ASP A 41  ? 0.5417 0.4494 0.2460 -0.1204 0.0605  -0.0985 41  ASP A CA  
340  C C   . ASP A 41  ? 0.5538 0.4867 0.2520 -0.1295 0.0745  -0.1030 41  ASP A C   
341  O O   . ASP A 41  ? 0.5344 0.4789 0.2400 -0.1326 0.0759  -0.0935 41  ASP A O   
342  C CB  . ASP A 41  ? 0.5160 0.4228 0.2530 -0.1066 0.0566  -0.0920 41  ASP A CB  
343  C CG  . ASP A 41  ? 0.5572 0.4790 0.3231 -0.0936 0.0675  -0.1049 41  ASP A CG  
344  O OD1 . ASP A 41  ? 0.5930 0.5295 0.3565 -0.0951 0.0799  -0.1197 41  ASP A OD1 
345  O OD2 . ASP A 41  ? 0.5763 0.4949 0.3677 -0.0818 0.0634  -0.1000 41  ASP A OD2 
346  N N   . PRO A 42  ? 0.5830 0.5266 0.2718 -0.1333 0.0852  -0.1171 42  PRO A N   
347  C CA  . PRO A 42  ? 0.5614 0.5314 0.2502 -0.1412 0.0984  -0.1204 42  PRO A CA  
348  C C   . PRO A 42  ? 0.5411 0.5337 0.2573 -0.1334 0.1108  -0.1284 42  PRO A C   
349  O O   . PRO A 42  ? 0.5770 0.5931 0.2944 -0.1412 0.1214  -0.1296 42  PRO A O   
350  C CB  . PRO A 42  ? 0.6040 0.5789 0.2852 -0.1424 0.1052  -0.1341 42  PRO A CB  
351  C CG  . PRO A 42  ? 0.6283 0.5844 0.3163 -0.1301 0.0995  -0.1431 42  PRO A CG  
352  C CD  . PRO A 42  ? 0.5881 0.5218 0.2749 -0.1277 0.0844  -0.1292 42  PRO A CD  
353  N N   . SER A 43  ? 0.5157 0.5030 0.2631 -0.1158 0.1068  -0.1304 43  SER A N   
354  C CA  . SER A 43  ? 0.5540 0.5616 0.3369 -0.1045 0.1138  -0.1341 43  SER A CA  
355  C C   . SER A 43  ? 0.5559 0.5678 0.3469 -0.1071 0.1075  -0.1167 43  SER A C   
356  O O   . SER A 43  ? 0.5735 0.6061 0.3906 -0.1011 0.1137  -0.1189 43  SER A O   
357  C CB  . SER A 43  ? 0.5593 0.5570 0.3712 -0.0850 0.1104  -0.1414 43  SER A CB  
358  O OG  . SER A 43  ? 0.5621 0.5390 0.3813 -0.0786 0.0956  -0.1265 43  SER A OG  
359  N N   . LEU A 44  ? 0.5131 0.5064 0.2841 -0.1154 0.0950  -0.1005 44  LEU A N   
360  C CA  . LEU A 44  ? 0.4966 0.4930 0.2733 -0.1189 0.0891  -0.0847 44  LEU A CA  
361  C C   . LEU A 44  ? 0.5445 0.5654 0.3137 -0.1326 0.0998  -0.0847 44  LEU A C   
362  O O   . LEU A 44  ? 0.5520 0.5760 0.2938 -0.1468 0.1056  -0.0878 44  LEU A O   
363  C CB  . LEU A 44  ? 0.4836 0.4540 0.2388 -0.1255 0.0737  -0.0690 44  LEU A CB  
364  C CG  . LEU A 44  ? 0.4658 0.4138 0.2319 -0.1124 0.0628  -0.0675 44  LEU A CG  
365  C CD1 . LEU A 44  ? 0.4949 0.4178 0.2383 -0.1193 0.0486  -0.0558 44  LEU A CD1 
366  C CD2 . LEU A 44  ? 0.4485 0.4004 0.2460 -0.0994 0.0600  -0.0626 44  LEU A CD2 
367  N N   . LYS A 45  ? 0.5216 0.5597 0.3144 -0.1291 0.1019  -0.0805 45  LYS A N   
368  C CA  . LYS A 45  ? 0.5014 0.5630 0.2889 -0.1431 0.1113  -0.0791 45  LYS A CA  
369  C C   . LYS A 45  ? 0.4827 0.5312 0.2502 -0.1560 0.1006  -0.0604 45  LYS A C   
370  O O   . LYS A 45  ? 0.4624 0.4879 0.2289 -0.1508 0.0864  -0.0493 45  LYS A O   
371  C CB  . LYS A 45  ? 0.5000 0.5887 0.3244 -0.1335 0.1188  -0.0848 45  LYS A CB  
372  C CG  . LYS A 45  ? 0.5506 0.6504 0.4012 -0.1174 0.1271  -0.1029 45  LYS A CG  
373  C CD  . LYS A 45  ? 0.6510 0.7631 0.4870 -0.1247 0.1416  -0.1192 45  LYS A CD  
374  C CE  . LYS A 45  ? 0.7142 0.8329 0.5756 -0.1075 0.1486  -0.1383 45  LYS A CE  
375  N NZ  . LYS A 45  ? 0.7796 0.9137 0.6288 -0.1145 0.1646  -0.1568 45  LYS A NZ  
376  N N   . PRO A 46  ? 0.4671 0.5299 0.2195 -0.1730 0.1071  -0.0566 46  PRO A N   
377  C CA  . PRO A 46  ? 0.4759 0.5245 0.2164 -0.1828 0.0943  -0.0384 46  PRO A CA  
378  C C   . PRO A 46  ? 0.4616 0.5081 0.2227 -0.1742 0.0868  -0.0297 46  PRO A C   
379  O O   . PRO A 46  ? 0.4628 0.5294 0.2545 -0.1641 0.0924  -0.0357 46  PRO A O   
380  C CB  . PRO A 46  ? 0.4802 0.5490 0.2212 -0.1953 0.1011  -0.0384 46  PRO A CB  
381  C CG  . PRO A 46  ? 0.5107 0.5952 0.2496 -0.1956 0.1155  -0.0553 46  PRO A CG  
382  C CD  . PRO A 46  ? 0.5061 0.5970 0.2617 -0.1804 0.1229  -0.0682 46  PRO A CD  
383  N N   . LEU A 47  ? 0.4356 0.4567 0.1842 -0.1761 0.0719  -0.0158 47  LEU A N   
384  C CA  . LEU A 47  ? 0.4157 0.4311 0.1838 -0.1676 0.0619  -0.0065 47  LEU A CA  
385  C C   . LEU A 47  ? 0.4401 0.4675 0.2092 -0.1793 0.0619  0.0023  47  LEU A C   
386  O O   . LEU A 47  ? 0.4986 0.5204 0.2563 -0.1888 0.0568  0.0065  47  LEU A O   
387  C CB  . LEU A 47  ? 0.4613 0.4451 0.2174 -0.1642 0.0464  0.0028  47  LEU A CB  
388  C CG  . LEU A 47  ? 0.4431 0.4199 0.2184 -0.1548 0.0367  0.0110  47  LEU A CG  
389  C CD1 . LEU A 47  ? 0.4268 0.4098 0.2303 -0.1368 0.0390  0.0031  47  LEU A CD1 
390  C CD2 . LEU A 47  ? 0.4925 0.4399 0.2526 -0.1558 0.0219  0.0208  47  LEU A CD2 
391  N N   . SER A 48  ? 0.4021 0.4453 0.1981 -0.1721 0.0632  0.0025  48  SER A N   
392  C CA  A SER A 48  ? 0.4339 0.4910 0.2346 -0.1825 0.0635  0.0100  48  SER A CA  
393  C CA  B SER A 48  ? 0.4329 0.4906 0.2345 -0.1821 0.0637  0.0098  48  SER A CA  
394  C C   . SER A 48  ? 0.4074 0.4497 0.2178 -0.1758 0.0499  0.0206  48  SER A C   
395  O O   . SER A 48  ? 0.4021 0.4472 0.2363 -0.1604 0.0473  0.0179  48  SER A O   
396  C CB  A SER A 48  ? 0.4406 0.5331 0.2673 -0.1802 0.0769  -0.0004 48  SER A CB  
397  C CB  B SER A 48  ? 0.4386 0.5310 0.2686 -0.1782 0.0761  -0.0003 48  SER A CB  
398  O OG  A SER A 48  ? 0.4476 0.5530 0.2829 -0.1884 0.0755  0.0070  48  SER A OG  
399  O OG  B SER A 48  ? 0.4784 0.5897 0.3004 -0.1876 0.0905  -0.0102 48  SER A OG  
400  N N   . VAL A 49  ? 0.4402 0.4656 0.2412 -0.1808 0.0374  0.0294  49  VAL A N   
401  C CA  . VAL A 49  ? 0.4369 0.4493 0.2466 -0.1752 0.0247  0.0377  49  VAL A CA  
402  C C   . VAL A 49  ? 0.4253 0.4530 0.2431 -0.1828 0.0246  0.0408  49  VAL A C   
403  O O   . VAL A 49  ? 0.5092 0.5313 0.3163 -0.1909 0.0201  0.0426  49  VAL A O   
404  C CB  . VAL A 49  ? 0.4673 0.4501 0.2657 -0.1717 0.0100  0.0417  49  VAL A CB  
405  C CG1 . VAL A 49  ? 0.4913 0.4642 0.3013 -0.1646 -0.0015 0.0474  49  VAL A CG1 
406  C CG2 . VAL A 49  ? 0.4821 0.4506 0.2717 -0.1657 0.0101  0.0381  49  VAL A CG2 
407  N N   A SER A 50  ? 0.4371 0.4850 0.2742 -0.1812 0.0294  0.0413  50  SER A N   
408  N N   B SER A 50  ? 0.4359 0.4828 0.2729 -0.1809 0.0288  0.0415  50  SER A N   
409  C CA  A SER A 50  ? 0.4473 0.5151 0.2946 -0.1892 0.0316  0.0425  50  SER A CA  
410  C CA  B SER A 50  ? 0.4472 0.5146 0.2944 -0.1890 0.0315  0.0425  50  SER A CA  
411  C C   A SER A 50  ? 0.4239 0.4827 0.2799 -0.1848 0.0195  0.0499  50  SER A C   
412  C C   B SER A 50  ? 0.4242 0.4832 0.2803 -0.1849 0.0196  0.0499  50  SER A C   
413  O O   A SER A 50  ? 0.4195 0.4905 0.2937 -0.1800 0.0206  0.0513  50  SER A O   
414  O O   B SER A 50  ? 0.4192 0.4910 0.2937 -0.1802 0.0208  0.0512  50  SER A O   
415  C CB  A SER A 50  ? 0.4583 0.5629 0.3261 -0.1914 0.0473  0.0351  50  SER A CB  
416  C CB  B SER A 50  ? 0.4583 0.5617 0.3253 -0.1909 0.0474  0.0349  50  SER A CB  
417  O OG  A SER A 50  ? 0.4934 0.6078 0.3541 -0.1941 0.0596  0.0258  50  SER A OG  
418  O OG  B SER A 50  ? 0.4862 0.6103 0.3631 -0.1992 0.0503  0.0347  50  SER A OG  
419  N N   . TYR A 51  ? 0.4185 0.4238 0.3452 -0.1694 0.1207  -0.0108 51  TYR A N   
420  C CA  . TYR A 51  ? 0.4009 0.4094 0.3396 -0.1614 0.1026  -0.0038 51  TYR A CA  
421  C C   . TYR A 51  ? 0.4394 0.4567 0.3857 -0.1689 0.0975  0.0018  51  TYR A C   
422  O O   . TYR A 51  ? 0.4333 0.4494 0.3832 -0.1659 0.0818  0.0073  51  TYR A O   
423  C CB  . TYR A 51  ? 0.4103 0.4010 0.3264 -0.1617 0.0869  0.0000  51  TYR A CB  
424  C CG  . TYR A 51  ? 0.3650 0.3481 0.2779 -0.1524 0.0865  -0.0042 51  TYR A CG  
425  C CD1 . TYR A 51  ? 0.3684 0.3580 0.2987 -0.1426 0.0991  -0.0105 51  TYR A CD1 
426  C CD2 . TYR A 51  ? 0.3532 0.3224 0.2468 -0.1536 0.0737  -0.0017 51  TYR A CD2 
427  C CE1 . TYR A 51  ? 0.3573 0.3377 0.2840 -0.1350 0.0992  -0.0142 51  TYR A CE1 
428  C CE2 . TYR A 51  ? 0.3433 0.3061 0.2345 -0.1465 0.0733  -0.0057 51  TYR A CE2 
429  C CZ  . TYR A 51  ? 0.3276 0.2951 0.2346 -0.1375 0.0861  -0.0121 51  TYR A CZ  
430  O OH  . TYR A 51  ? 0.3388 0.2980 0.2425 -0.1317 0.0856  -0.0158 51  TYR A OH  
431  N N   . ASP A 52  ? 0.4564 0.4817 0.4048 -0.1790 0.1110  -0.0003 52  ASP A N   
432  C CA  . ASP A 52  ? 0.4758 0.5077 0.4302 -0.1861 0.1058  0.0044  52  ASP A CA  
433  C C   . ASP A 52  ? 0.4449 0.4965 0.4312 -0.1794 0.0999  0.0063  52  ASP A C   
434  O O   . ASP A 52  ? 0.4907 0.5438 0.4796 -0.1856 0.0902  0.0110  52  ASP A O   
435  C CB  . ASP A 52  ? 0.5045 0.5422 0.4584 -0.1927 0.1203  0.0005  52  ASP A CB  
436  C CG  . ASP A 52  ? 0.5986 0.6167 0.5179 -0.2003 0.1221  -0.0006 52  ASP A CG  
437  O OD1 . ASP A 52  ? 0.6088 0.6094 0.5043 -0.2011 0.1110  0.0025  52  ASP A OD1 
438  O OD2 . ASP A 52  ? 0.6305 0.6518 0.5465 -0.2061 0.1347  -0.0047 52  ASP A OD2 
439  N N   . GLN A 53  ? 0.3850 0.4511 0.3957 -0.1650 0.1039  0.0027  53  GLN A N   
440  C CA  . GLN A 53  ? 0.3754 0.4631 0.4174 -0.1562 0.0972  0.0044  53  GLN A CA  
441  C C   . GLN A 53  ? 0.3795 0.4641 0.4260 -0.1410 0.0837  0.0065  53  GLN A C   
442  O O   . GLN A 53  ? 0.3759 0.4787 0.4484 -0.1292 0.0818  0.0068  53  GLN A O   
443  C CB  . GLN A 53  ? 0.3922 0.5044 0.4642 -0.1515 0.1130  0.0000  53  GLN A CB  
444  C CG  . GLN A 53  ? 0.4292 0.5489 0.5013 -0.1668 0.1274  -0.0024 53  GLN A CG  
445  C CD  . GLN A 53  ? 0.4919 0.6411 0.6009 -0.1613 0.1409  -0.0062 53  GLN A CD  
446  O OE1 . GLN A 53  ? 0.5009 0.6544 0.6212 -0.1511 0.1536  -0.0108 53  GLN A OE1 
447  N NE2 . GLN A 53  ? 0.5474 0.7173 0.6765 -0.1682 0.1384  -0.0044 53  GLN A NE2 
448  N N   . ALA A 54  ? 0.3554 0.4181 0.3773 -0.1411 0.0747  0.0081  54  ALA A N   
449  C CA  . ALA A 54  ? 0.3518 0.4104 0.3763 -0.1274 0.0639  0.0095  54  ALA A CA  
450  C C   . ALA A 54  ? 0.3380 0.4050 0.3736 -0.1249 0.0485  0.0134  54  ALA A C   
451  O O   . ALA A 54  ? 0.3372 0.4002 0.3654 -0.1356 0.0418  0.0156  54  ALA A O   
452  C CB  . ALA A 54  ? 0.3867 0.4214 0.3832 -0.1290 0.0588  0.0097  54  ALA A CB  
453  N N   . THR A 55  ? 0.2842 0.3621 0.3366 -0.1114 0.0433  0.0143  55  THR A N   
454  C CA  . THR A 55  ? 0.2685 0.3564 0.3313 -0.1091 0.0291  0.0170  55  THR A CA  
455  C C   . THR A 55  ? 0.2559 0.3309 0.3082 -0.0994 0.0187  0.0183  55  THR A C   
456  O O   . THR A 55  ? 0.2513 0.3325 0.3135 -0.0868 0.0198  0.0189  55  THR A O   
457  C CB  . THR A 55  ? 0.2891 0.4058 0.3826 -0.1024 0.0311  0.0175  55  THR A CB  
458  O OG1 . THR A 55  ? 0.3078 0.4377 0.4129 -0.1116 0.0423  0.0156  55  THR A OG1 
459  C CG2 . THR A 55  ? 0.2737 0.4020 0.3761 -0.1010 0.0155  0.0196  55  THR A CG2 
460  N N   . SER A 56  ? 0.2330 0.2903 0.2662 -0.1048 0.0091  0.0190  56  SER A N   
461  C CA  . SER A 56  ? 0.2254 0.2732 0.2514 -0.0959 -0.0006 0.0198  56  SER A CA  
462  C C   . SER A 56  ? 0.2274 0.2887 0.2661 -0.0914 -0.0111 0.0207  56  SER A C   
463  O O   . SER A 56  ? 0.2497 0.3230 0.2980 -0.0985 -0.0146 0.0206  56  SER A O   
464  C CB  . SER A 56  ? 0.2319 0.2572 0.2355 -0.1020 -0.0073 0.0202  56  SER A CB  
465  O OG  . SER A 56  ? 0.2684 0.2913 0.2699 -0.1112 -0.0151 0.0212  56  SER A OG  
466  N N   . LEU A 57  ? 0.2228 0.2830 0.2614 -0.0801 -0.0158 0.0215  57  LEU A N   
467  C CA  . LEU A 57  ? 0.2049 0.2783 0.2530 -0.0753 -0.0256 0.0224  57  LEU A CA  
468  C C   . LEU A 57  ? 0.2335 0.2927 0.2672 -0.0733 -0.0357 0.0213  57  LEU A C   
469  O O   . LEU A 57  ? 0.2299 0.2932 0.2643 -0.0772 -0.0449 0.0199  57  LEU A O   
470  C CB  . LEU A 57  ? 0.2692 0.3583 0.3327 -0.0625 -0.0218 0.0254  57  LEU A CB  
471  C CG  . LEU A 57  ? 0.3119 0.4202 0.3956 -0.0627 -0.0127 0.0263  57  LEU A CG  
472  C CD1 . LEU A 57  ? 0.3188 0.4377 0.4164 -0.0476 -0.0087 0.0303  57  LEU A CD1 
473  C CD2 . LEU A 57  ? 0.3118 0.4392 0.4085 -0.0716 -0.0188 0.0256  57  LEU A CD2 
474  N N   . ARG A 58  ? 0.2113 0.2562 0.2340 -0.0669 -0.0337 0.0214  58  ARG A N   
475  C CA  . ARG A 58  ? 0.2259 0.2614 0.2389 -0.0629 -0.0419 0.0203  58  ARG A CA  
476  C C   . ARG A 58  ? 0.2353 0.2527 0.2354 -0.0605 -0.0386 0.0195  58  ARG A C   
477  O O   . ARG A 58  ? 0.2427 0.2561 0.2413 -0.0605 -0.0298 0.0199  58  ARG A O   
478  C CB  . ARG A 58  ? 0.2977 0.3467 0.3182 -0.0533 -0.0455 0.0222  58  ARG A CB  
479  C CG  . ARG A 58  ? 0.3251 0.3788 0.3523 -0.0436 -0.0374 0.0257  58  ARG A CG  
480  C CD  . ARG A 58  ? 0.3674 0.4356 0.4019 -0.0346 -0.0424 0.0295  58  ARG A CD  
481  N NE  . ARG A 58  ? 0.4062 0.4942 0.4522 -0.0389 -0.0494 0.0299  58  ARG A NE  
482  C CZ  . ARG A 58  ? 0.4160 0.5238 0.4806 -0.0370 -0.0464 0.0331  58  ARG A CZ  
483  N NH1 . ARG A 58  ? 0.3773 0.5039 0.4521 -0.0426 -0.0540 0.0325  58  ARG A NH1 
484  N NH2 . ARG A 58  ? 0.3569 0.4660 0.4309 -0.0299 -0.0354 0.0362  58  ARG A NH2 
485  N N   . ILE A 59  ? 0.2176 0.2244 0.2085 -0.0592 -0.0454 0.0176  59  ILE A N   
486  C CA  . ILE A 59  ? 0.2238 0.2158 0.2045 -0.0569 -0.0438 0.0166  59  ILE A CA  
487  C C   . ILE A 59  ? 0.2325 0.2241 0.2116 -0.0484 -0.0464 0.0158  59  ILE A C   
488  O O   . ILE A 59  ? 0.2530 0.2486 0.2325 -0.0476 -0.0530 0.0145  59  ILE A O   
489  C CB  . ILE A 59  ? 0.2299 0.2083 0.2015 -0.0643 -0.0489 0.0155  59  ILE A CB  
490  C CG1 . ILE A 59  ? 0.2553 0.2220 0.2186 -0.0623 -0.0472 0.0150  59  ILE A CG1 
491  C CG2 . ILE A 59  ? 0.2473 0.2232 0.2184 -0.0658 -0.0580 0.0133  59  ILE A CG2 
492  C CD1 . ILE A 59  ? 0.2864 0.2402 0.2413 -0.0686 -0.0531 0.0157  59  ILE A CD1 
493  N N   . LEU A 60  ? 0.2433 0.2301 0.2198 -0.0430 -0.0406 0.0161  60  LEU A N   
494  C CA  . LEU A 60  ? 0.2541 0.2413 0.2293 -0.0350 -0.0405 0.0163  60  LEU A CA  
495  C C   . LEU A 60  ? 0.2425 0.2176 0.2107 -0.0342 -0.0387 0.0138  60  LEU A C   
496  O O   . LEU A 60  ? 0.2510 0.2208 0.2176 -0.0363 -0.0330 0.0134  60  LEU A O   
497  C CB  . LEU A 60  ? 0.2441 0.2392 0.2262 -0.0282 -0.0334 0.0203  60  LEU A CB  
498  C CG  . LEU A 60  ? 0.2467 0.2393 0.2256 -0.0201 -0.0309 0.0220  60  LEU A CG  
499  C CD1 . LEU A 60  ? 0.2450 0.2448 0.2215 -0.0172 -0.0388 0.0227  60  LEU A CD1 
500  C CD2 . LEU A 60  ? 0.2716 0.2680 0.2578 -0.0136 -0.0221 0.0267  60  LEU A CD2 
501  N N   . ASN A 61  ? 0.2367 0.2084 0.2011 -0.0315 -0.0428 0.0115  61  ASN A N   
502  C CA  . ASN A 61  ? 0.2203 0.1839 0.1810 -0.0294 -0.0398 0.0092  61  ASN A CA  
503  C C   . ASN A 61  ? 0.2231 0.1889 0.1842 -0.0229 -0.0325 0.0116  61  ASN A C   
504  O O   . ASN A 61  ? 0.2325 0.2030 0.1924 -0.0184 -0.0341 0.0131  61  ASN A O   
505  C CB  . ASN A 61  ? 0.2455 0.2049 0.2034 -0.0289 -0.0462 0.0053  61  ASN A CB  
506  C CG  . ASN A 61  ? 0.2453 0.1992 0.2021 -0.0265 -0.0431 0.0025  61  ASN A CG  
507  O OD1 . ASN A 61  ? 0.2504 0.2042 0.2072 -0.0244 -0.0359 0.0036  61  ASN A OD1 
508  N ND2 . ASN A 61  ? 0.2672 0.2164 0.2245 -0.0271 -0.0480 -0.0012 61  ASN A ND2 
509  N N   . ASN A 62  ? 0.2278 0.1897 0.1897 -0.0228 -0.0244 0.0123  62  ASN A N   
510  C CA  . ASN A 62  ? 0.2377 0.1990 0.2003 -0.0167 -0.0164 0.0153  62  ASN A CA  
511  C C   . ASN A 62  ? 0.2093 0.1635 0.1679 -0.0156 -0.0127 0.0128  62  ASN A C   
512  O O   . ASN A 62  ? 0.2463 0.1965 0.2044 -0.0119 -0.0045 0.0150  62  ASN A O   
513  C CB  . ASN A 62  ? 0.2115 0.1714 0.1784 -0.0167 -0.0074 0.0172  62  ASN A CB  
514  C CG  . ASN A 62  ? 0.2396 0.1909 0.2034 -0.0228 -0.0023 0.0125  62  ASN A CG  
515  O OD1 . ASN A 62  ? 0.2259 0.1743 0.1859 -0.0269 -0.0071 0.0089  62  ASN A OD1 
516  N ND2 . ASN A 62  ? 0.2250 0.1729 0.1909 -0.0234 0.0071  0.0125  62  ASN A ND2 
517  N N   . GLY A 63  ? 0.2261 0.1787 0.1827 -0.0183 -0.0183 0.0084  63  GLY A N   
518  C CA  . GLY A 63  ? 0.2280 0.1762 0.1832 -0.0178 -0.0148 0.0051  63  GLY A CA  
519  C C   . GLY A 63  ? 0.2451 0.1887 0.2019 -0.0225 -0.0100 0.0022  63  GLY A C   
520  O O   . GLY A 63  ? 0.2737 0.2151 0.2312 -0.0230 -0.0063 -0.0008 63  GLY A O   
521  N N   . HIS A 64  ? 0.2400 0.1828 0.1971 -0.0268 -0.0094 0.0025  64  HIS A N   
522  C CA  . HIS A 64  ? 0.2196 0.1585 0.1760 -0.0329 -0.0052 -0.0008 64  HIS A CA  
523  C C   . HIS A 64  ? 0.2535 0.1941 0.2081 -0.0388 -0.0129 -0.0017 64  HIS A C   
524  O O   . HIS A 64  ? 0.2675 0.2079 0.2214 -0.0436 -0.0164 -0.0047 64  HIS A O   
525  C CB  . HIS A 64  ? 0.2255 0.1595 0.1813 -0.0329 0.0060  0.0001  64  HIS A CB  
526  C CG  . HIS A 64  ? 0.2109 0.1415 0.1677 -0.0260 0.0136  0.0034  64  HIS A CG  
527  N ND1 . HIS A 64  ? 0.2246 0.1513 0.1808 -0.0256 0.0181  0.0017  64  HIS A ND1 
528  C CD2 . HIS A 64  ? 0.2334 0.1646 0.1920 -0.0194 0.0172  0.0091  64  HIS A CD2 
529  C CE1 . HIS A 64  ? 0.2579 0.1806 0.2135 -0.0192 0.0249  0.0067  64  HIS A CE1 
530  N NE2 . HIS A 64  ? 0.2404 0.1661 0.1978 -0.0148 0.0239  0.0116  64  HIS A NE2 
531  N N   . THR A 65  ? 0.2226 0.1654 0.1766 -0.0388 -0.0159 0.0013  65  THR A N   
532  C CA  . THR A 65  ? 0.2149 0.1581 0.1659 -0.0447 -0.0224 0.0020  65  THR A CA  
533  C C   . THR A 65  ? 0.2235 0.1706 0.1767 -0.0424 -0.0266 0.0053  65  THR A C   
534  O O   . THR A 65  ? 0.2246 0.1749 0.1811 -0.0365 -0.0271 0.0063  65  THR A O   
535  C CB  . THR A 65  ? 0.2345 0.1752 0.1806 -0.0511 -0.0160 0.0007  65  THR A CB  
536  O OG1 . THR A 65  ? 0.2658 0.2063 0.2066 -0.0576 -0.0228 0.0020  65  THR A OG1 
537  C CG2 . THR A 65  ? 0.2503 0.1919 0.1993 -0.0485 -0.0063 0.0021  65  THR A CG2 
538  N N   . PHE A 66  ? 0.2285 0.1758 0.1792 -0.0480 -0.0303 0.0068  66  PHE A N   
539  C CA  . PHE A 66  ? 0.2139 0.1662 0.1680 -0.0476 -0.0323 0.0094  66  PHE A CA  
540  C C   . PHE A 66  ? 0.2305 0.1856 0.1848 -0.0515 -0.0250 0.0105  66  PHE A C   
541  O O   . PHE A 66  ? 0.2405 0.1913 0.1884 -0.0577 -0.0223 0.0093  66  PHE A O   
542  C CB  . PHE A 66  ? 0.2565 0.2065 0.2092 -0.0509 -0.0425 0.0101  66  PHE A CB  
543  C CG  . PHE A 66  ? 0.2462 0.1900 0.1922 -0.0584 -0.0458 0.0114  66  PHE A CG  
544  C CD1 . PHE A 66  ? 0.2789 0.2236 0.2221 -0.0650 -0.0439 0.0137  66  PHE A CD1 
545  C CD2 . PHE A 66  ? 0.2637 0.2017 0.2063 -0.0589 -0.0509 0.0108  66  PHE A CD2 
546  C CE1 . PHE A 66  ? 0.2901 0.2284 0.2244 -0.0725 -0.0469 0.0158  66  PHE A CE1 
547  C CE2 . PHE A 66  ? 0.2923 0.2252 0.2275 -0.0656 -0.0551 0.0134  66  PHE A CE2 
548  C CZ  . PHE A 66  ? 0.2883 0.2204 0.2180 -0.0726 -0.0532 0.0162  66  PHE A CZ  
549  N N   . ASN A 67  ? 0.2333 0.1964 0.1953 -0.0476 -0.0214 0.0124  67  ASN A N   
550  C CA  . ASN A 67  ? 0.2276 0.1955 0.1936 -0.0498 -0.0132 0.0132  67  ASN A CA  
551  C C   . ASN A 67  ? 0.2488 0.2248 0.2196 -0.0536 -0.0178 0.0152  67  ASN A C   
552  O O   . ASN A 67  ? 0.2443 0.2272 0.2208 -0.0499 -0.0239 0.0167  67  ASN A O   
553  C CB  . ASN A 67  ? 0.2319 0.2049 0.2069 -0.0413 -0.0049 0.0147  67  ASN A CB  
554  C CG  . ASN A 67  ? 0.2523 0.2163 0.2236 -0.0381 0.0017  0.0127  67  ASN A CG  
555  O OD1 . ASN A 67  ? 0.2446 0.2002 0.2071 -0.0438 0.0023  0.0091  67  ASN A OD1 
556  N ND2 . ASN A 67  ? 0.2625 0.2282 0.2403 -0.0293 0.0067  0.0154  67  ASN A ND2 
557  N N   . VAL A 68  ? 0.2346 0.2104 0.2027 -0.0615 -0.0142 0.0150  68  VAL A N   
558  C CA  . VAL A 68  ? 0.2404 0.2253 0.2150 -0.0661 -0.0156 0.0167  68  VAL A CA  
559  C C   . VAL A 68  ? 0.2559 0.2516 0.2422 -0.0630 -0.0049 0.0169  68  VAL A C   
560  O O   . VAL A 68  ? 0.2452 0.2369 0.2281 -0.0656 0.0052  0.0148  68  VAL A O   
561  C CB  . VAL A 68  ? 0.2564 0.2337 0.2203 -0.0773 -0.0178 0.0170  68  VAL A CB  
562  C CG1 . VAL A 68  ? 0.2703 0.2574 0.2416 -0.0836 -0.0157 0.0183  68  VAL A CG1 
563  C CG2 . VAL A 68  ? 0.2611 0.2275 0.2161 -0.0788 -0.0293 0.0178  68  VAL A CG2 
564  N N   . GLU A 69  ? 0.2346 0.2447 0.2352 -0.0576 -0.0068 0.0191  69  GLU A N   
565  C CA  . GLU A 69  ? 0.2365 0.2589 0.2523 -0.0514 0.0024  0.0204  69  GLU A CA  
566  C C   . GLU A 69  ? 0.2282 0.2631 0.2538 -0.0585 0.0055  0.0204  69  GLU A C   
567  O O   . GLU A 69  ? 0.2618 0.3010 0.2870 -0.0653 -0.0028 0.0208  69  GLU A O   
568  C CB  . GLU A 69  ? 0.3133 0.3461 0.3396 -0.0406 -0.0029 0.0242  69  GLU A CB  
569  C CG  . GLU A 69  ? 0.4746 0.5203 0.5185 -0.0315 0.0052  0.0274  69  GLU A CG  
570  C CD  . GLU A 69  ? 0.5833 0.6453 0.6387 -0.0232 -0.0036 0.0327  69  GLU A CD  
571  O OE1 . GLU A 69  ? 0.6126 0.6885 0.6852 -0.0150 0.0009  0.0368  69  GLU A OE1 
572  O OE2 . GLU A 69  ? 0.6022 0.6637 0.6496 -0.0250 -0.0151 0.0327  69  GLU A OE2 
573  N N   . PHE A 70  ? 0.2152 0.2558 0.2501 -0.0571 0.0181  0.0194  70  PHE A N   
574  C CA  . PHE A 70  ? 0.2156 0.2703 0.2628 -0.0630 0.0242  0.0189  70  PHE A CA  
575  C C   . PHE A 70  ? 0.2608 0.3356 0.3329 -0.0529 0.0292  0.0214  70  PHE A C   
576  O O   . PHE A 70  ? 0.2379 0.3118 0.3160 -0.0412 0.0324  0.0234  70  PHE A O   
577  C CB  . PHE A 70  ? 0.2290 0.2738 0.2660 -0.0713 0.0369  0.0147  70  PHE A CB  
578  C CG  . PHE A 70  ? 0.2483 0.2771 0.2624 -0.0827 0.0311  0.0137  70  PHE A CG  
579  C CD1 . PHE A 70  ? 0.2634 0.2758 0.2610 -0.0812 0.0256  0.0131  70  PHE A CD1 
580  C CD2 . PHE A 70  ? 0.2536 0.2842 0.2634 -0.0948 0.0307  0.0139  70  PHE A CD2 
581  C CE1 . PHE A 70  ? 0.2597 0.2590 0.2383 -0.0908 0.0190  0.0134  70  PHE A CE1 
582  C CE2 . PHE A 70  ? 0.2741 0.2893 0.2629 -0.1047 0.0247  0.0147  70  PHE A CE2 
583  C CZ  . PHE A 70  ? 0.2857 0.2857 0.2595 -0.1018 0.0182  0.0147  70  PHE A CZ  
584  N N   . ASP A 71  ? 0.2786 0.3087 0.3143 -0.0936 -0.0132 -0.0179 71  ASP A N   
585  C CA  . ASP A 71  ? 0.2565 0.3027 0.3119 -0.0912 -0.0144 -0.0269 71  ASP A CA  
586  C C   . ASP A 71  ? 0.2563 0.3203 0.3185 -0.0907 -0.0065 -0.0321 71  ASP A C   
587  O O   . ASP A 71  ? 0.2966 0.3707 0.3579 -0.0997 0.0020  -0.0310 71  ASP A O   
588  C CB  . ASP A 71  ? 0.2782 0.3327 0.3462 -0.1007 -0.0149 -0.0284 71  ASP A CB  
589  C CG  . ASP A 71  ? 0.2713 0.3430 0.3627 -0.0978 -0.0177 -0.0386 71  ASP A CG  
590  O OD1 . ASP A 71  ? 0.2689 0.3538 0.3693 -0.0927 -0.0147 -0.0451 71  ASP A OD1 
591  O OD2 . ASP A 71  ? 0.3096 0.3819 0.4115 -0.1007 -0.0237 -0.0405 71  ASP A OD2 
592  N N   . ASP A 72  ? 0.2279 0.2934 0.2939 -0.0806 -0.0091 -0.0373 72  ASP A N   
593  C CA  . ASP A 72  ? 0.1937 0.2747 0.2662 -0.0789 -0.0025 -0.0433 72  ASP A CA  
594  C C   . ASP A 72  ? 0.2227 0.3214 0.3188 -0.0751 -0.0044 -0.0546 72  ASP A C   
595  O O   . ASP A 72  ? 0.2142 0.3203 0.3164 -0.0684 -0.0037 -0.0612 72  ASP A O   
596  C CB  . ASP A 72  ? 0.2071 0.2763 0.2664 -0.0704 -0.0041 -0.0411 72  ASP A CB  
597  C CG  . ASP A 72  ? 0.2306 0.2878 0.2907 -0.0602 -0.0142 -0.0429 72  ASP A CG  
598  O OD1 . ASP A 72  ? 0.2660 0.3207 0.3336 -0.0592 -0.0211 -0.0446 72  ASP A OD1 
599  O OD2 . ASP A 72  ? 0.2435 0.2928 0.2954 -0.0536 -0.0155 -0.0422 72  ASP A OD2 
600  N N   . SER A 73  ? 0.2151 0.3214 0.3258 -0.0794 -0.0072 -0.0576 73  SER A N   
601  C CA  . SER A 73  ? 0.1996 0.3230 0.3354 -0.0751 -0.0107 -0.0691 73  SER A CA  
602  C C   . SER A 73  ? 0.2434 0.3940 0.3962 -0.0816 0.0004  -0.0773 73  SER A C   
603  O O   . SER A 73  ? 0.2450 0.4132 0.4217 -0.0772 -0.0015 -0.0888 73  SER A O   
604  C CB  . SER A 73  ? 0.2374 0.3577 0.3833 -0.0764 -0.0197 -0.0697 73  SER A CB  
605  O OG  . SER A 73  ? 0.2446 0.3725 0.3936 -0.0894 -0.0137 -0.0668 73  SER A OG  
606  N N   . GLN A 74  ? 0.2082 0.3628 0.3497 -0.0924 0.0115  -0.0723 74  GLN A N   
607  C CA  . GLN A 74  ? 0.2082 0.3886 0.3630 -0.1009 0.0237  -0.0797 74  GLN A CA  
608  C C   . GLN A 74  ? 0.2034 0.3820 0.3383 -0.1051 0.0337  -0.0754 74  GLN A C   
609  O O   . GLN A 74  ? 0.2435 0.4012 0.3546 -0.1051 0.0317  -0.0646 74  GLN A O   
610  C CB  . GLN A 74  ? 0.2342 0.4245 0.3972 -0.1147 0.0281  -0.0783 74  GLN A CB  
611  C CG  . GLN A 74  ? 0.2081 0.4026 0.3930 -0.1112 0.0182  -0.0838 74  GLN A CG  
612  C CD  . GLN A 74  ? 0.2513 0.4570 0.4467 -0.1258 0.0225  -0.0830 74  GLN A CD  
613  O OE1 . GLN A 74  ? 0.2914 0.4833 0.4682 -0.1359 0.0247  -0.0720 74  GLN A OE1 
614  N NE2 . GLN A 74  ? 0.2794 0.5063 0.5018 -0.1249 0.0230  -0.0934 74  GLN A NE2 
615  N N   . ASP A 75  ? 0.2478 0.4497 0.3937 -0.1090 0.0445  -0.0847 75  ASP A N   
616  C CA  . ASP A 75  ? 0.2830 0.4867 0.4115 -0.1137 0.0547  -0.0829 75  ASP A CA  
617  C C   . ASP A 75  ? 0.3326 0.5328 0.4440 -0.1300 0.0625  -0.0730 75  ASP A C   
618  O O   . ASP A 75  ? 0.3855 0.6029 0.4976 -0.1410 0.0747  -0.0766 75  ASP A O   
619  C CB  . ASP A 75  ? 0.2960 0.5262 0.4422 -0.1121 0.0637  -0.0976 75  ASP A CB  
620  C CG  . ASP A 75  ? 0.3245 0.5534 0.4798 -0.0960 0.0566  -0.1060 75  ASP A CG  
621  O OD1 . ASP A 75  ? 0.3004 0.5075 0.4454 -0.0869 0.0457  -0.0996 75  ASP A OD1 
622  O OD2 . ASP A 75  ? 0.3594 0.6093 0.5315 -0.0928 0.0624  -0.1196 75  ASP A OD2 
623  N N   . LYS A 76  ? 0.3079 0.4857 0.4045 -0.1320 0.0551  -0.0608 76  LYS A N   
624  C CA  . LYS A 76  ? 0.3140 0.4846 0.3938 -0.1471 0.0600  -0.0506 76  LYS A CA  
625  C C   . LYS A 76  ? 0.3480 0.4972 0.3987 -0.1466 0.0587  -0.0400 76  LYS A C   
626  O O   . LYS A 76  ? 0.3771 0.5314 0.4148 -0.1536 0.0675  -0.0394 76  LYS A O   
627  C CB  . LYS A 76  ? 0.3303 0.4919 0.4157 -0.1513 0.0527  -0.0455 76  LYS A CB  
628  C CG  . LYS A 76  ? 0.3531 0.5389 0.4668 -0.1557 0.0562  -0.0557 76  LYS A CG  
629  C CD  . LYS A 76  ? 0.3719 0.5485 0.4915 -0.1600 0.0483  -0.0508 76  LYS A CD  
630  C CE  . LYS A 76  ? 0.3758 0.5737 0.5190 -0.1632 0.0525  -0.0590 76  LYS A CE  
631  N NZ  . LYS A 76  ? 0.3852 0.5771 0.5401 -0.1644 0.0429  -0.0573 76  LYS A NZ  
632  N N   . ALA A 77  ? 0.2896 0.4160 0.3304 -0.1379 0.0478  -0.0327 77  ALA A N   
633  C CA  . ALA A 77  ? 0.2730 0.3805 0.2895 -0.1365 0.0457  -0.0236 77  ALA A CA  
634  C C   . ALA A 77  ? 0.2849 0.3973 0.3023 -0.1258 0.0466  -0.0300 77  ALA A C   
635  O O   . ALA A 77  ? 0.2659 0.3730 0.2905 -0.1135 0.0393  -0.0329 77  ALA A O   
636  C CB  . ALA A 77  ? 0.3232 0.4066 0.3308 -0.1315 0.0347  -0.0148 77  ALA A CB  
637  N N   . VAL A 78  ? 0.2802 0.4018 0.2892 -0.1309 0.0552  -0.0324 78  VAL A N   
638  C CA  . VAL A 78  ? 0.2803 0.4089 0.2922 -0.1216 0.0568  -0.0402 78  VAL A CA  
639  C C   . VAL A 78  ? 0.2926 0.4140 0.2817 -0.1254 0.0602  -0.0353 78  VAL A C   
640  O O   . VAL A 78  ? 0.3285 0.4457 0.3012 -0.1373 0.0643  -0.0282 78  VAL A O   
641  C CB  . VAL A 78  ? 0.2572 0.4123 0.2901 -0.1215 0.0648  -0.0544 78  VAL A CB  
642  C CG1 . VAL A 78  ? 0.2600 0.4227 0.3176 -0.1167 0.0597  -0.0602 78  VAL A CG1 
643  C CG2 . VAL A 78  ? 0.2993 0.4691 0.3270 -0.1361 0.0772  -0.0559 78  VAL A CG2 
644  N N   . LEU A 79  ? 0.2770 0.3973 0.2655 -0.1154 0.0580  -0.0398 79  LEU A N   
645  C CA  . LEU A 79  ? 0.2715 0.3886 0.2420 -0.1172 0.0611  -0.0385 79  LEU A CA  
646  C C   . LEU A 79  ? 0.2975 0.4343 0.2791 -0.1139 0.0683  -0.0521 79  LEU A C   
647  O O   . LEU A 79  ? 0.3275 0.4706 0.3280 -0.1035 0.0649  -0.0605 79  LEU A O   
648  C CB  . LEU A 79  ? 0.3051 0.4025 0.2666 -0.1079 0.0512  -0.0321 79  LEU A CB  
649  C CG  . LEU A 79  ? 0.3738 0.4620 0.3162 -0.1082 0.0502  -0.0282 79  LEU A CG  
650  C CD1 . LEU A 79  ? 0.4184 0.4987 0.3410 -0.1207 0.0522  -0.0187 79  LEU A CD1 
651  C CD2 . LEU A 79  ? 0.2977 0.3700 0.2398 -0.0981 0.0403  -0.0235 79  LEU A CD2 
652  N N   . LYS A 80  ? 0.2975 0.4431 0.2668 -0.1227 0.0777  -0.0547 80  LYS A N   
653  C CA  . LYS A 80  ? 0.3154 0.4802 0.2934 -0.1202 0.0856  -0.0687 80  LYS A CA  
654  C C   . LYS A 80  ? 0.3295 0.4897 0.2825 -0.1258 0.0900  -0.0668 80  LYS A C   
655  O O   . LYS A 80  ? 0.3556 0.4998 0.2860 -0.1331 0.0875  -0.0547 80  LYS A O   
656  C CB  . LYS A 80  ? 0.3866 0.5765 0.3820 -0.1273 0.0966  -0.0788 80  LYS A CB  
657  C CG  . LYS A 80  ? 0.4114 0.6079 0.4338 -0.1216 0.0917  -0.0825 80  LYS A CG  
658  C CD  . LYS A 80  ? 0.4244 0.6497 0.4696 -0.1259 0.1022  -0.0963 80  LYS A CD  
659  C CE  . LYS A 80  ? 0.5298 0.7569 0.5607 -0.1398 0.1103  -0.0920 80  LYS A CE  
660  N NZ  . LYS A 80  ? 0.5803 0.7878 0.5936 -0.1483 0.1057  -0.0757 80  LYS A NZ  
661  N N   . GLY A 81  ? 0.3075 0.4808 0.2648 -0.1215 0.0954  -0.0793 81  GLY A N   
662  C CA  . GLY A 81  ? 0.3276 0.4979 0.2611 -0.1267 0.0998  -0.0793 81  GLY A CA  
663  C C   . GLY A 81  ? 0.3258 0.4741 0.2455 -0.1192 0.0883  -0.0715 81  GLY A C   
664  O O   . GLY A 81  ? 0.3107 0.4503 0.2424 -0.1080 0.0787  -0.0703 81  GLY A O   
665  N N   . GLY A 82  ? 0.3611 0.5007 0.2546 -0.1262 0.0895  -0.0665 82  GLY A N   
666  C CA  . GLY A 82  ? 0.3567 0.4785 0.2377 -0.1198 0.0794  -0.0611 82  GLY A CA  
667  C C   . GLY A 82  ? 0.3361 0.4629 0.2321 -0.1070 0.0766  -0.0724 82  GLY A C   
668  O O   . GLY A 82  ? 0.3671 0.5092 0.2682 -0.1062 0.0842  -0.0854 82  GLY A O   
669  N N   . PRO A 83  ? 0.3209 0.4344 0.2239 -0.0971 0.0655  -0.0680 83  PRO A N   
670  C CA  . PRO A 83  ? 0.3096 0.4253 0.2270 -0.0853 0.0616  -0.0777 83  PRO A CA  
671  C C   . PRO A 83  ? 0.3480 0.4744 0.2915 -0.0781 0.0621  -0.0857 83  PRO A C   
672  O O   . PRO A 83  ? 0.3757 0.5021 0.3311 -0.0683 0.0577  -0.0935 83  PRO A O   
673  C CB  . PRO A 83  ? 0.2768 0.3729 0.1896 -0.0797 0.0499  -0.0679 83  PRO A CB  
674  C CG  . PRO A 83  ? 0.2885 0.3772 0.2002 -0.0840 0.0475  -0.0561 83  PRO A CG  
675  C CD  . PRO A 83  ? 0.3175 0.4135 0.2157 -0.0966 0.0564  -0.0544 83  PRO A CD  
676  N N   . LEU A 84  ? 0.2925 0.4265 0.2450 -0.0828 0.0659  -0.0836 84  LEU A N   
677  C CA  . LEU A 84  ? 0.2719 0.4124 0.2487 -0.0756 0.0633  -0.0888 84  LEU A CA  
678  C C   . LEU A 84  ? 0.2618 0.4246 0.2553 -0.0747 0.0716  -0.1043 84  LEU A C   
679  O O   . LEU A 84  ? 0.2855 0.4624 0.2737 -0.0841 0.0825  -0.1083 84  LEU A O   
680  C CB  . LEU A 84  ? 0.2480 0.3853 0.2273 -0.0809 0.0624  -0.0794 84  LEU A CB  
681  C CG  . LEU A 84  ? 0.2659 0.3820 0.2289 -0.0823 0.0549  -0.0647 84  LEU A CG  
682  C CD1 . LEU A 84  ? 0.3054 0.4185 0.2696 -0.0885 0.0546  -0.0563 84  LEU A CD1 
683  C CD2 . LEU A 84  ? 0.2489 0.3517 0.2175 -0.0710 0.0447  -0.0633 84  LEU A CD2 
684  N N   . ASP A 85  ? 0.2882 0.4542 0.3023 -0.0636 0.0662  -0.1131 85  ASP A N   
685  C CA  . ASP A 85  ? 0.2956 0.4830 0.3327 -0.0606 0.0715  -0.1280 85  ASP A CA  
686  C C   . ASP A 85  ? 0.2704 0.4608 0.3248 -0.0600 0.0680  -0.1253 85  ASP A C   
687  O O   . ASP A 85  ? 0.2819 0.4566 0.3388 -0.0535 0.0573  -0.1184 85  ASP A O   
688  C CB  . ASP A 85  ? 0.3212 0.5088 0.3707 -0.0481 0.0659  -0.1400 85  ASP A CB  
689  C CG  . ASP A 85  ? 0.4330 0.6189 0.4664 -0.0489 0.0694  -0.1443 85  ASP A CG  
690  O OD1 . ASP A 85  ? 0.4586 0.6578 0.4826 -0.0578 0.0811  -0.1484 85  ASP A OD1 
691  O OD2 . ASP A 85  ? 0.4784 0.6489 0.5068 -0.0415 0.0607  -0.1430 85  ASP A OD2 
692  N N   . GLY A 86  ? 0.2974 0.5076 0.3629 -0.0673 0.0772  -0.1308 86  GLY A N   
693  C CA  . GLY A 86  ? 0.2949 0.5092 0.3785 -0.0669 0.0735  -0.1293 86  GLY A CA  
694  C C   . GLY A 86  ? 0.3067 0.5091 0.3754 -0.0767 0.0730  -0.1137 86  GLY A C   
695  O O   . GLY A 86  ? 0.3177 0.5138 0.3640 -0.0864 0.0782  -0.1050 86  GLY A O   
696  N N   . THR A 87  ? 0.2362 0.4339 0.3173 -0.0737 0.0654  -0.1101 87  THR A N   
697  C CA  . THR A 87  ? 0.2333 0.4227 0.3057 -0.0826 0.0649  -0.0978 87  THR A CA  
698  C C   . THR A 87  ? 0.2449 0.4106 0.3104 -0.0756 0.0525  -0.0876 87  THR A C   
699  O O   . THR A 87  ? 0.2542 0.4162 0.3329 -0.0651 0.0439  -0.0919 87  THR A O   
700  C CB  . THR A 87  ? 0.2414 0.4488 0.3356 -0.0872 0.0683  -0.1037 87  THR A CB  
701  O OG1 . THR A 87  ? 0.2547 0.4859 0.3546 -0.0957 0.0819  -0.1132 87  THR A OG1 
702  C CG2 . THR A 87  ? 0.2533 0.4492 0.3397 -0.0954 0.0654  -0.0910 87  THR A CG2 
703  N N   . TYR A 88  ? 0.2380 0.3871 0.2828 -0.0814 0.0512  -0.0743 88  TYR A N   
704  C CA  . TYR A 88  ? 0.2174 0.3449 0.2550 -0.0754 0.0407  -0.0650 88  TYR A CA  
705  C C   . TYR A 88  ? 0.2300 0.3504 0.2643 -0.0822 0.0390  -0.0561 88  TYR A C   
706  O O   . TYR A 88  ? 0.2390 0.3570 0.2599 -0.0922 0.0436  -0.0492 88  TYR A O   
707  C CB  . TYR A 88  ? 0.2188 0.3317 0.2365 -0.0740 0.0391  -0.0583 88  TYR A CB  
708  C CG  . TYR A 88  ? 0.1839 0.2982 0.2041 -0.0656 0.0377  -0.0658 88  TYR A CG  
709  C CD1 . TYR A 88  ? 0.2076 0.3380 0.2316 -0.0671 0.0452  -0.0759 88  TYR A CD1 
710  C CD2 . TYR A 88  ? 0.1915 0.2902 0.2088 -0.0570 0.0292  -0.0628 88  TYR A CD2 
711  C CE1 . TYR A 88  ? 0.2148 0.3450 0.2405 -0.0592 0.0433  -0.0833 88  TYR A CE1 
712  C CE2 . TYR A 88  ? 0.1878 0.2862 0.2069 -0.0501 0.0273  -0.0692 88  TYR A CE2 
713  C CZ  . TYR A 88  ? 0.2120 0.3255 0.2353 -0.0508 0.0338  -0.0795 88  TYR A CZ  
714  O OH  . TYR A 88  ? 0.2416 0.3534 0.2661 -0.0438 0.0312  -0.0864 88  TYR A OH  
715  N N   . ARG A 89  ? 0.2187 0.3337 0.2637 -0.0768 0.0313  -0.0560 89  ARG A N   
716  C CA  . ARG A 89  ? 0.2140 0.3224 0.2580 -0.0825 0.0286  -0.0492 89  ARG A CA  
717  C C   . ARG A 89  ? 0.2146 0.3005 0.2410 -0.0810 0.0227  -0.0380 89  ARG A C   
718  O O   . ARG A 89  ? 0.2121 0.2869 0.2352 -0.0722 0.0169  -0.0372 89  ARG A O   
719  C CB  . ARG A 89  ? 0.2067 0.3191 0.2697 -0.0774 0.0223  -0.0548 89  ARG A CB  
720  C CG  . ARG A 89  ? 0.2303 0.3669 0.3152 -0.0804 0.0276  -0.0659 89  ARG A CG  
721  C CD  . ARG A 89  ? 0.2036 0.3411 0.3062 -0.0755 0.0189  -0.0699 89  ARG A CD  
722  N NE  . ARG A 89  ? 0.2162 0.3778 0.3441 -0.0748 0.0220  -0.0830 89  ARG A NE  
723  C CZ  . ARG A 89  ? 0.1927 0.3590 0.3404 -0.0679 0.0136  -0.0903 89  ARG A CZ  
724  N NH1 . ARG A 89  ? 0.2144 0.3623 0.3578 -0.0619 0.0019  -0.0854 89  ARG A NH1 
725  N NH2 . ARG A 89  ? 0.2376 0.4276 0.4100 -0.0668 0.0168  -0.1033 89  ARG A NH2 
726  N N   . LEU A 90  ? 0.2241 0.3031 0.2395 -0.0898 0.0241  -0.0298 90  LEU A N   
727  C CA  . LEU A 90  ? 0.2155 0.2737 0.2172 -0.0882 0.0179  -0.0203 90  LEU A CA  
728  C C   . LEU A 90  ? 0.2160 0.2660 0.2251 -0.0817 0.0101  -0.0208 90  LEU A C   
729  O O   . LEU A 90  ? 0.2343 0.2900 0.2544 -0.0848 0.0090  -0.0233 90  LEU A O   
730  C CB  . LEU A 90  ? 0.2501 0.3030 0.2411 -0.0995 0.0200  -0.0124 90  LEU A CB  
731  C CG  . LEU A 90  ? 0.2632 0.2947 0.2419 -0.0977 0.0128  -0.0035 90  LEU A CG  
732  C CD1 . LEU A 90  ? 0.2706 0.2933 0.2379 -0.0920 0.0112  -0.0006 90  LEU A CD1 
733  C CD2 . LEU A 90  ? 0.2973 0.3223 0.2671 -0.1092 0.0134  0.0038  90  LEU A CD2 
734  N N   . ILE A 91  ? 0.2123 0.2490 0.2152 -0.0734 0.0048  -0.0187 91  ILE A N   
735  C CA  . ILE A 91  ? 0.2206 0.2469 0.2259 -0.0680 -0.0024 -0.0183 91  ILE A CA  
736  C C   . ILE A 91  ? 0.2263 0.2355 0.2190 -0.0685 -0.0058 -0.0106 91  ILE A C   
737  O O   . ILE A 91  ? 0.2291 0.2308 0.2227 -0.0686 -0.0103 -0.0095 91  ILE A O   
738  C CB  . ILE A 91  ? 0.2147 0.2391 0.2237 -0.0585 -0.0062 -0.0230 91  ILE A CB  
739  C CG1 . ILE A 91  ? 0.2426 0.2541 0.2501 -0.0542 -0.0135 -0.0220 91  ILE A CG1 
740  C CG2 . ILE A 91  ? 0.2392 0.2575 0.2382 -0.0545 -0.0049 -0.0209 91  ILE A CG2 
741  C CD1 . ILE A 91  ? 0.2467 0.2566 0.2586 -0.0464 -0.0183 -0.0270 91  ILE A CD1 
742  N N   . GLN A 92  ? 0.2262 0.2290 0.2079 -0.0685 -0.0043 -0.0059 92  GLN A N   
743  C CA  . GLN A 92  ? 0.2335 0.2207 0.2054 -0.0675 -0.0081 0.0000  92  GLN A CA  
744  C C   . GLN A 92  ? 0.2373 0.2215 0.1996 -0.0694 -0.0063 0.0047  92  GLN A C   
745  O O   . GLN A 92  ? 0.2349 0.2274 0.1967 -0.0698 -0.0026 0.0029  92  GLN A O   
746  C CB  . GLN A 92  ? 0.2223 0.2000 0.1929 -0.0591 -0.0120 -0.0012 92  GLN A CB  
747  C CG  . GLN A 92  ? 0.2247 0.2054 0.1951 -0.0535 -0.0104 -0.0038 92  GLN A CG  
748  C CD  . GLN A 92  ? 0.2430 0.2148 0.2056 -0.0503 -0.0109 -0.0005 92  GLN A CD  
749  O OE1 . GLN A 92  ? 0.2501 0.2190 0.2079 -0.0531 -0.0107 0.0036  92  GLN A OE1 
750  N NE2 . GLN A 92  ? 0.2854 0.2528 0.2469 -0.0447 -0.0117 -0.0023 92  GLN A NE2 
751  N N   . PHE A 93  ? 0.2424 0.2138 0.1972 -0.0704 -0.0099 0.0102  93  PHE A N   
752  C CA  . PHE A 93  ? 0.2439 0.2095 0.1904 -0.0692 -0.0109 0.0140  93  PHE A CA  
753  C C   . PHE A 93  ? 0.2506 0.2040 0.1956 -0.0625 -0.0155 0.0151  93  PHE A C   
754  O O   . PHE A 93  ? 0.2486 0.1953 0.1953 -0.0608 -0.0182 0.0145  93  PHE A O   
755  C CB  . PHE A 93  ? 0.2709 0.2333 0.2085 -0.0778 -0.0111 0.0199  93  PHE A CB  
756  C CG  . PHE A 93  ? 0.2636 0.2133 0.1972 -0.0817 -0.0159 0.0247  93  PHE A CG  
757  C CD1 . PHE A 93  ? 0.2784 0.2133 0.2079 -0.0771 -0.0224 0.0278  93  PHE A CD1 
758  C CD2 . PHE A 93  ? 0.2791 0.2321 0.2137 -0.0905 -0.0141 0.0256  93  PHE A CD2 
759  C CE1 . PHE A 93  ? 0.2921 0.2141 0.2179 -0.0806 -0.0276 0.0318  93  PHE A CE1 
760  C CE2 . PHE A 93  ? 0.2866 0.2268 0.2173 -0.0950 -0.0190 0.0303  93  PHE A CE2 
761  C CZ  . PHE A 93  ? 0.3072 0.2310 0.2328 -0.0899 -0.0262 0.0334  93  PHE A CZ  
762  N N   . HIS A 94  ? 0.2354 0.1865 0.1774 -0.0590 -0.0164 0.0163  94  HIS A N   
763  C CA  . HIS A 94  ? 0.2474 0.1894 0.1897 -0.0527 -0.0199 0.0164  94  HIS A CA  
764  C C   . HIS A 94  ? 0.2526 0.1927 0.1915 -0.0520 -0.0221 0.0192  94  HIS A C   
765  O O   . HIS A 94  ? 0.2498 0.1950 0.1846 -0.0563 -0.0208 0.0209  94  HIS A O   
766  C CB  . HIS A 94  ? 0.2297 0.1748 0.1769 -0.0464 -0.0173 0.0114  94  HIS A CB  
767  C CG  . HIS A 94  ? 0.2031 0.1576 0.1520 -0.0456 -0.0139 0.0095  94  HIS A CG  
768  N ND1 . HIS A 94  ? 0.2220 0.1853 0.1731 -0.0477 -0.0110 0.0069  94  HIS A ND1 
769  C CD2 . HIS A 94  ? 0.2205 0.1767 0.1699 -0.0430 -0.0137 0.0093  94  HIS A CD2 
770  C CE1 . HIS A 94  ? 0.2198 0.1887 0.1717 -0.0462 -0.0091 0.0052  94  HIS A CE1 
771  N NE2 . HIS A 94  ? 0.1972 0.1621 0.1478 -0.0438 -0.0107 0.0070  94  HIS A NE2 
772  N N   . PHE A 95  ? 0.2553 0.1886 0.1963 -0.0464 -0.0256 0.0189  95  PHE A N   
773  C CA  . PHE A 95  ? 0.2341 0.1653 0.1743 -0.0447 -0.0295 0.0209  95  PHE A CA  
774  C C   . PHE A 95  ? 0.2543 0.1899 0.2026 -0.0377 -0.0279 0.0164  95  PHE A C   
775  O O   . PHE A 95  ? 0.2532 0.1900 0.2060 -0.0342 -0.0245 0.0124  95  PHE A O   
776  C CB  . PHE A 95  ? 0.2612 0.1789 0.1981 -0.0446 -0.0374 0.0248  95  PHE A CB  
777  C CG  . PHE A 95  ? 0.2781 0.1889 0.2058 -0.0527 -0.0396 0.0303  95  PHE A CG  
778  C CD1 . PHE A 95  ? 0.2899 0.1985 0.2181 -0.0553 -0.0380 0.0296  95  PHE A CD1 
779  C CD2 . PHE A 95  ? 0.2975 0.2033 0.2152 -0.0584 -0.0437 0.0361  95  PHE A CD2 
780  C CE1 . PHE A 95  ? 0.2833 0.1858 0.2041 -0.0636 -0.0399 0.0346  95  PHE A CE1 
781  C CE2 . PHE A 95  ? 0.3199 0.2185 0.2277 -0.0674 -0.0453 0.0416  95  PHE A CE2 
782  C CZ  . PHE A 95  ? 0.3310 0.2288 0.2413 -0.0703 -0.0429 0.0407  95  PHE A CZ  
783  N N   . HIS A 96  ? 0.2368 0.1740 0.1862 -0.0365 -0.0308 0.0173  96  HIS A N   
784  C CA  . HIS A 96  ? 0.2271 0.1682 0.1859 -0.0306 -0.0307 0.0134  96  HIS A CA  
785  C C   . HIS A 96  ? 0.2406 0.1746 0.2014 -0.0279 -0.0392 0.0154  96  HIS A C   
786  O O   . HIS A 96  ? 0.2579 0.1865 0.2105 -0.0317 -0.0446 0.0204  96  HIS A O   
787  C CB  . HIS A 96  ? 0.2285 0.1795 0.1887 -0.0315 -0.0273 0.0119  96  HIS A CB  
788  C CG  . HIS A 96  ? 0.2182 0.1747 0.1762 -0.0339 -0.0208 0.0100  96  HIS A CG  
789  N ND1 . HIS A 96  ? 0.2490 0.2092 0.2118 -0.0314 -0.0160 0.0060  96  HIS A ND1 
790  C CD2 . HIS A 96  ? 0.2150 0.1732 0.1667 -0.0385 -0.0188 0.0113  96  HIS A CD2 
791  C CE1 . HIS A 96  ? 0.2246 0.1874 0.1840 -0.0337 -0.0127 0.0052  96  HIS A CE1 
792  N NE2 . HIS A 96  ? 0.2232 0.1863 0.1773 -0.0377 -0.0140 0.0078  96  HIS A NE2 
793  N N   . TRP A 97  ? 0.2415 0.1750 0.2127 -0.0215 -0.0406 0.0112  97  TRP A N   
794  C CA  . TRP A 97  ? 0.2331 0.1593 0.2087 -0.0176 -0.0501 0.0120  97  TRP A CA  
795  C C   . TRP A 97  ? 0.2616 0.1951 0.2533 -0.0104 -0.0495 0.0053  97  TRP A C   
796  O O   . TRP A 97  ? 0.2401 0.1830 0.2378 -0.0094 -0.0410 0.0004  97  TRP A O   
797  C CB  . TRP A 97  ? 0.2454 0.1577 0.2164 -0.0173 -0.0557 0.0144  97  TRP A CB  
798  C CG  . TRP A 97  ? 0.2559 0.1677 0.2320 -0.0136 -0.0508 0.0090  97  TRP A CG  
799  C CD1 . TRP A 97  ? 0.2627 0.1740 0.2500 -0.0062 -0.0518 0.0027  97  TRP A CD1 
800  C CD2 . TRP A 97  ? 0.2554 0.1674 0.2249 -0.0173 -0.0442 0.0090  97  TRP A CD2 
801  N NE1 . TRP A 97  ? 0.2689 0.1792 0.2548 -0.0055 -0.0459 -0.0011 97  TRP A NE1 
802  C CE2 . TRP A 97  ? 0.2722 0.1823 0.2472 -0.0121 -0.0419 0.0030  97  TRP A CE2 
803  C CE3 . TRP A 97  ? 0.2417 0.1560 0.2019 -0.0242 -0.0403 0.0127  97  TRP A CE3 
804  C CZ2 . TRP A 97  ? 0.2602 0.1685 0.2297 -0.0140 -0.0369 0.0014  97  TRP A CZ2 
805  C CZ3 . TRP A 97  ? 0.2533 0.1670 0.2110 -0.0255 -0.0358 0.0108  97  TRP A CZ3 
806  C CH2 . TRP A 97  ? 0.2558 0.1655 0.2171 -0.0205 -0.0347 0.0057  97  TRP A CH2 
807  N N   . GLY A 98  ? 0.2619 0.1909 0.2610 -0.0057 -0.0589 0.0047  98  GLY A N   
808  C CA  . GLY A 98  ? 0.2536 0.1916 0.2707 0.0009  -0.0593 -0.0022 98  GLY A CA  
809  C C   . GLY A 98  ? 0.2717 0.2060 0.2996 0.0081  -0.0613 -0.0082 98  GLY A C   
810  O O   . GLY A 98  ? 0.2755 0.1980 0.2963 0.0083  -0.0637 -0.0067 98  GLY A O   
811  N N   . SER A 99  ? 0.2571 0.2027 0.3039 0.0141  -0.0599 -0.0161 99  SER A N   
812  C CA  . SER A 99  ? 0.2703 0.2141 0.3309 0.0223  -0.0631 -0.0236 99  SER A CA  
813  C C   . SER A 99  ? 0.2779 0.2105 0.3435 0.0276  -0.0791 -0.0219 99  SER A C   
814  O O   . SER A 99  ? 0.3086 0.2361 0.3843 0.0349  -0.0840 -0.0277 99  SER A O   
815  C CB  . SER A 99  ? 0.2925 0.2542 0.3729 0.0264  -0.0544 -0.0339 99  SER A CB  
816  O OG  . SER A 99  ? 0.3043 0.2772 0.3946 0.0255  -0.0563 -0.0340 99  SER A OG  
817  N N   . HIS A 100 ? 0.3041 0.2317 0.3619 0.0240  -0.0877 -0.0145 100 HIS A N   
818  C CA  . HIS A 100 ? 0.3189 0.2317 0.3757 0.0274  -0.1044 -0.0107 100 HIS A CA  
819  C C   . HIS A 100 ? 0.3161 0.2203 0.3515 0.0185  -0.1087 0.0004  100 HIS A C   
820  O O   . HIS A 100 ? 0.3307 0.2434 0.3575 0.0117  -0.0989 0.0029  100 HIS A O   
821  C CB  . HIS A 100 ? 0.3084 0.2302 0.3890 0.0360  -0.1122 -0.0181 100 HIS A CB  
822  C CG  . HIS A 100 ? 0.3047 0.2426 0.3920 0.0332  -0.1081 -0.0191 100 HIS A CG  
823  N ND1 . HIS A 100 ? 0.3335 0.2661 0.4110 0.0294  -0.1175 -0.0120 100 HIS A ND1 
824  C CD2 . HIS A 100 ? 0.3148 0.2727 0.4155 0.0327  -0.0956 -0.0259 100 HIS A CD2 
825  C CE1 . HIS A 100 ? 0.3343 0.2833 0.4204 0.0273  -0.1114 -0.0149 100 HIS A CE1 
826  N NE2 . HIS A 100 ? 0.2905 0.2548 0.3906 0.0290  -0.0980 -0.0230 100 HIS A NE2 
827  N N   . ASP A 101 ? 0.3348 0.2211 0.3608 0.0184  -0.1236 0.0068  101 ASP A N   
828  C CA  . ASP A 101 ? 0.3385 0.2144 0.3403 0.0086  -0.1267 0.0177  101 ASP A CA  
829  C C   . ASP A 101 ? 0.3492 0.2355 0.3495 0.0054  -0.1262 0.0189  101 ASP A C   
830  O O   . ASP A 101 ? 0.3762 0.2575 0.3562 -0.0033 -0.1255 0.0264  101 ASP A O   
831  C CB  . ASP A 101 ? 0.3892 0.2417 0.3795 0.0085  -0.1438 0.0247  101 ASP A CB  
832  C CG  . ASP A 101 ? 0.3917 0.2291 0.3765 0.0086  -0.1455 0.0262  101 ASP A CG  
833  O OD1 . ASP A 101 ? 0.4063 0.2512 0.3938 0.0078  -0.1330 0.0224  101 ASP A OD1 
834  O OD2 . ASP A 101 ? 0.4417 0.2580 0.4180 0.0089  -0.1604 0.0317  101 ASP A OD2 
835  N N   . GLY A 102 ? 0.3320 0.2320 0.3531 0.0120  -0.1269 0.0114  102 GLY A N   
836  C CA  . GLY A 102 ? 0.3308 0.2397 0.3520 0.0095  -0.1282 0.0119  102 GLY A CA  
837  C C   . GLY A 102 ? 0.3259 0.2507 0.3456 0.0040  -0.1128 0.0101  102 GLY A C   
838  O O   . GLY A 102 ? 0.3364 0.2683 0.3555 0.0015  -0.1133 0.0102  102 GLY A O   
839  N N   . GLN A 103 ? 0.2916 0.2209 0.3101 0.0023  -0.1000 0.0083  103 GLN A N   
840  C CA  . GLN A 103 ? 0.2864 0.2275 0.3009 -0.0031 -0.0865 0.0074  103 GLN A CA  
841  C C   . GLN A 103 ? 0.2885 0.2247 0.2911 -0.0070 -0.0781 0.0099  103 GLN A C   
842  O O   . GLN A 103 ? 0.2960 0.2217 0.2964 -0.0050 -0.0817 0.0111  103 GLN A O   
843  C CB  . GLN A 103 ? 0.2732 0.2317 0.3083 0.0006  -0.0787 -0.0011 103 GLN A CB  
844  C CG  . GLN A 103 ? 0.2866 0.2493 0.3361 0.0062  -0.0731 -0.0078 103 GLN A CG  
845  C CD  . GLN A 103 ? 0.2889 0.2689 0.3597 0.0092  -0.0667 -0.0164 103 GLN A CD  
846  O OE1 . GLN A 103 ? 0.3151 0.3024 0.3957 0.0098  -0.0715 -0.0179 103 GLN A OE1 
847  N NE2 . GLN A 103 ? 0.2643 0.2509 0.3420 0.0106  -0.0559 -0.0220 103 GLN A NE2 
848  N N   . GLY A 104 ? 0.2760 0.2197 0.2719 -0.0122 -0.0677 0.0102  104 GLY A N   
849  C CA  . GLY A 104 ? 0.2552 0.1956 0.2415 -0.0158 -0.0602 0.0119  104 GLY A CA  
850  C C   . GLY A 104 ? 0.2565 0.1999 0.2297 -0.0228 -0.0543 0.0150  104 GLY A C   
851  O O   . GLY A 104 ? 0.2601 0.2080 0.2322 -0.0246 -0.0456 0.0132  104 GLY A O   
852  N N   . SER A 105 ? 0.2521 0.1927 0.2150 -0.0269 -0.0594 0.0191  105 SER A N   
853  C CA  . SER A 105 ? 0.2520 0.1970 0.2037 -0.0332 -0.0529 0.0205  105 SER A CA  
854  C C   . SER A 105 ? 0.2460 0.2033 0.2063 -0.0319 -0.0460 0.0151  105 SER A C   
855  O O   . SER A 105 ? 0.2423 0.2051 0.2155 -0.0276 -0.0471 0.0113  105 SER A O   
856  C CB  . SER A 105 ? 0.2748 0.2139 0.2113 -0.0386 -0.0590 0.0256  105 SER A CB  
857  O OG  . SER A 105 ? 0.2835 0.2249 0.2239 -0.0362 -0.0654 0.0243  105 SER A OG  
858  N N   . GLU A 106 ? 0.2501 0.2117 0.2035 -0.0360 -0.0390 0.0146  106 GLU A N   
859  C CA  . GLU A 106 ? 0.2123 0.1829 0.1712 -0.0355 -0.0332 0.0102  106 GLU A CA  
860  C C   . GLU A 106 ? 0.2264 0.1997 0.1794 -0.0382 -0.0358 0.0100  106 GLU A C   
861  O O   . GLU A 106 ? 0.2348 0.2121 0.1952 -0.0362 -0.0382 0.0075  106 GLU A O   
862  C CB  . GLU A 106 ? 0.2394 0.2122 0.1957 -0.0372 -0.0256 0.0087  106 GLU A CB  
863  C CG  . GLU A 106 ? 0.2391 0.2085 0.2007 -0.0344 -0.0237 0.0083  106 GLU A CG  
864  C CD  . GLU A 106 ? 0.2205 0.1931 0.1839 -0.0341 -0.0172 0.0052  106 GLU A CD  
865  O OE1 . GLU A 106 ? 0.2233 0.1974 0.1812 -0.0369 -0.0148 0.0052  106 GLU A OE1 
866  O OE2 . GLU A 106 ? 0.2537 0.2274 0.2239 -0.0313 -0.0148 0.0026  106 GLU A OE2 
867  N N   . HIS A 107 ? 0.2399 0.2112 0.1794 -0.0431 -0.0355 0.0124  107 HIS A N   
868  C CA  . HIS A 107 ? 0.2660 0.2378 0.1969 -0.0459 -0.0390 0.0125  107 HIS A CA  
869  C C   . HIS A 107 ? 0.2690 0.2337 0.1984 -0.0447 -0.0494 0.0160  107 HIS A C   
870  O O   . HIS A 107 ? 0.2715 0.2291 0.2024 -0.0430 -0.0539 0.0194  107 HIS A O   
871  C CB  . HIS A 107 ? 0.2441 0.2158 0.1597 -0.0522 -0.0352 0.0138  107 HIS A CB  
872  C CG  . HIS A 107 ? 0.2468 0.2268 0.1661 -0.0524 -0.0265 0.0089  107 HIS A CG  
873  N ND1 . HIS A 107 ? 0.2544 0.2354 0.1781 -0.0520 -0.0217 0.0087  107 HIS A ND1 
874  C CD2 . HIS A 107 ? 0.2505 0.2372 0.1714 -0.0519 -0.0231 0.0034  107 HIS A CD2 
875  C CE1 . HIS A 107 ? 0.2431 0.2311 0.1707 -0.0514 -0.0160 0.0036  107 HIS A CE1 
876  N NE2 . HIS A 107 ? 0.2480 0.2393 0.1741 -0.0512 -0.0167 0.0002  107 HIS A NE2 
877  N N   . THR A 108 ? 0.2582 0.2243 0.1855 -0.0450 -0.0542 0.0147  108 THR A N   
878  C CA  . THR A 108 ? 0.2666 0.2250 0.1895 -0.0445 -0.0659 0.0181  108 THR A CA  
879  C C   . THR A 108 ? 0.2893 0.2439 0.1922 -0.0505 -0.0684 0.0199  108 THR A C   
880  O O   . THR A 108 ? 0.3062 0.2671 0.2036 -0.0536 -0.0610 0.0166  108 THR A O   
881  C CB  . THR A 108 ? 0.2526 0.2161 0.1936 -0.0389 -0.0714 0.0142  108 THR A CB  
882  O OG1 . THR A 108 ? 0.2711 0.2432 0.2155 -0.0399 -0.0669 0.0093  108 THR A OG1 
883  C CG2 . THR A 108 ? 0.2632 0.2309 0.2230 -0.0336 -0.0681 0.0118  108 THR A CG2 
884  N N   . VAL A 109 ? 0.2895 0.2329 0.1805 -0.0523 -0.0791 0.0251  109 VAL A N   
885  C CA  . VAL A 109 ? 0.3189 0.2565 0.1875 -0.0587 -0.0827 0.0275  109 VAL A CA  
886  C C   . VAL A 109 ? 0.3341 0.2674 0.2056 -0.0554 -0.0960 0.0274  109 VAL A C   
887  O O   . VAL A 109 ? 0.3425 0.2669 0.2178 -0.0522 -0.1069 0.0311  109 VAL A O   
888  C CB  . VAL A 109 ? 0.3575 0.2835 0.2043 -0.0660 -0.0834 0.0348  109 VAL A CB  
889  C CG1 . VAL A 109 ? 0.3940 0.3144 0.2150 -0.0738 -0.0856 0.0367  109 VAL A CG1 
890  C CG2 . VAL A 109 ? 0.3636 0.2963 0.2118 -0.0689 -0.0702 0.0337  109 VAL A CG2 
891  N N   . ASP A 110 ? 0.3349 0.2743 0.2058 -0.0559 -0.0960 0.0226  110 ASP A N   
892  C CA  . ASP A 110 ? 0.3400 0.2770 0.2163 -0.0526 -0.1088 0.0214  110 ASP A CA  
893  C C   . ASP A 110 ? 0.3431 0.2841 0.2463 -0.0447 -0.1137 0.0198  110 ASP A C   
894  O O   . ASP A 110 ? 0.3730 0.3076 0.2811 -0.0413 -0.1272 0.0216  110 ASP A O   
895  C CB  . ASP A 110 ? 0.3926 0.3139 0.2441 -0.0572 -0.1213 0.0276  110 ASP A CB  
896  C CG  . ASP A 110 ? 0.4685 0.3876 0.2930 -0.0657 -0.1151 0.0278  110 ASP A CG  
897  O OD1 . ASP A 110 ? 0.4200 0.3503 0.2477 -0.0663 -0.1055 0.0212  110 ASP A OD1 
898  O OD2 . ASP A 110 ? 0.5076 0.4129 0.3069 -0.0719 -0.1206 0.0344  110 ASP A OD2 
899  N N   . LYS A 111 ? 0.3273 0.2791 0.2483 -0.0418 -0.1028 0.0159  111 LYS A N   
900  C CA  . LYS A 111 ? 0.3207 0.2800 0.2681 -0.0351 -0.1025 0.0125  111 LYS A CA  
901  C C   . LYS A 111 ? 0.3561 0.3078 0.3066 -0.0318 -0.1064 0.0163  111 LYS A C   
902  O O   . LYS A 111 ? 0.3800 0.3381 0.3520 -0.0261 -0.1053 0.0128  111 LYS A O   
903  C CB  . LYS A 111 ? 0.3555 0.3205 0.3198 -0.0313 -0.1119 0.0083  111 LYS A CB  
904  C CG  . LYS A 111 ? 0.4424 0.4140 0.4052 -0.0344 -0.1096 0.0040  111 LYS A CG  
905  C CD  . LYS A 111 ? 0.5245 0.5056 0.4943 -0.0355 -0.0948 0.0002  111 LYS A CD  
906  C CE  . LYS A 111 ? 0.5602 0.5501 0.5550 -0.0309 -0.0906 -0.0029 111 LYS A CE  
907  N NZ  . LYS A 111 ? 0.5012 0.4981 0.5014 -0.0322 -0.0774 -0.0057 111 LYS A NZ  
908  N N   . LYS A 112 ? 0.3272 0.2656 0.2570 -0.0357 -0.1101 0.0230  112 LYS A N   
909  C CA  . LYS A 112 ? 0.3627 0.2910 0.2937 -0.0330 -0.1156 0.0270  112 LYS A CA  
910  C C   . LYS A 112 ? 0.3341 0.2659 0.2677 -0.0337 -0.1031 0.0267  112 LYS A C   
911  O O   . LYS A 112 ? 0.3316 0.2665 0.2537 -0.0392 -0.0929 0.0273  112 LYS A O   
912  C CB  . LYS A 112 ? 0.4383 0.3487 0.3435 -0.0385 -0.1255 0.0353  112 LYS A CB  
913  C CG  . LYS A 112 ? 0.5951 0.4910 0.4970 -0.0371 -0.1321 0.0408  112 LYS A CG  
914  C CD  . LYS A 112 ? 0.6549 0.5452 0.5375 -0.0453 -0.1226 0.0459  112 LYS A CD  
915  C CE  . LYS A 112 ? 0.6958 0.5663 0.5657 -0.0474 -0.1323 0.0537  112 LYS A CE  
916  N NZ  . LYS A 112 ? 0.7148 0.5822 0.6055 -0.0380 -0.1393 0.0514  112 LYS A NZ  
917  N N   . LYS A 113 ? 0.3205 0.2518 0.2698 -0.0276 -0.1045 0.0252  113 LYS A N   
918  C CA  . LYS A 113 ? 0.3066 0.2385 0.2575 -0.0278 -0.0948 0.0251  113 LYS A CA  
919  C C   . LYS A 113 ? 0.3252 0.2410 0.2637 -0.0296 -0.1011 0.0316  113 LYS A C   
920  O O   . LYS A 113 ? 0.3756 0.2793 0.3113 -0.0275 -0.1145 0.0349  113 LYS A O   
921  C CB  . LYS A 113 ? 0.2743 0.2164 0.2498 -0.0204 -0.0906 0.0182  113 LYS A CB  
922  C CG  . LYS A 113 ? 0.2888 0.2460 0.2753 -0.0203 -0.0820 0.0125  113 LYS A CG  
923  C CD  . LYS A 113 ? 0.3164 0.2832 0.3244 -0.0147 -0.0765 0.0060  113 LYS A CD  
924  C CE  . LYS A 113 ? 0.3070 0.2863 0.3214 -0.0169 -0.0663 0.0017  113 LYS A CE  
925  N NZ  . LYS A 113 ? 0.3238 0.3106 0.3517 -0.0142 -0.0568 -0.0033 113 LYS A NZ  
926  N N   . TYR A 114 ? 0.3111 0.2258 0.2415 -0.0339 -0.0921 0.0335  114 TYR A N   
927  C CA  . TYR A 114 ? 0.3336 0.2340 0.2550 -0.0359 -0.0962 0.0389  114 TYR A CA  
928  C C   . TYR A 114 ? 0.3139 0.2167 0.2522 -0.0293 -0.0928 0.0343  114 TYR A C   
929  O O   . TYR A 114 ? 0.3027 0.2188 0.2562 -0.0251 -0.0849 0.0277  114 TYR A O   
930  C CB  . TYR A 114 ? 0.3594 0.2574 0.2615 -0.0458 -0.0886 0.0436  114 TYR A CB  
931  C CG  . TYR A 114 ? 0.3622 0.2558 0.2440 -0.0534 -0.0919 0.0482  114 TYR A CG  
932  C CD1 . TYR A 114 ? 0.3766 0.2825 0.2569 -0.0553 -0.0852 0.0444  114 TYR A CD1 
933  C CD2 . TYR A 114 ? 0.4413 0.3169 0.3034 -0.0593 -0.1016 0.0565  114 TYR A CD2 
934  C CE1 . TYR A 114 ? 0.4389 0.3406 0.2991 -0.0624 -0.0876 0.0479  114 TYR A CE1 
935  C CE2 . TYR A 114 ? 0.4483 0.3192 0.2889 -0.0671 -0.1042 0.0607  114 TYR A CE2 
936  C CZ  . TYR A 114 ? 0.4705 0.3553 0.3109 -0.0683 -0.0967 0.0558  114 TYR A CZ  
937  O OH  . TYR A 114 ? 0.5417 0.4224 0.3597 -0.0761 -0.0982 0.0590  114 TYR A OH  
938  N N   . ALA A 115 ? 0.3336 0.2223 0.2673 -0.0293 -0.0987 0.0381  115 ALA A N   
939  C CA  . ALA A 115 ? 0.3135 0.2025 0.2613 -0.0230 -0.0964 0.0334  115 ALA A CA  
940  C C   . ALA A 115 ? 0.2904 0.1883 0.2383 -0.0259 -0.0827 0.0309  115 ALA A C   
941  O O   . ALA A 115 ? 0.3091 0.2125 0.2702 -0.0204 -0.0777 0.0250  115 ALA A O   
942  C CB  . ALA A 115 ? 0.3472 0.2164 0.2881 -0.0228 -0.1075 0.0384  115 ALA A CB  
943  N N   . ALA A 116 ? 0.2649 0.2092 0.2441 -0.0209 -0.0726 0.0119  116 ALA A N   
944  C CA  . ALA A 116 ? 0.2487 0.1983 0.2255 -0.0248 -0.0607 0.0086  116 ALA A CA  
945  C C   . ALA A 116 ? 0.2633 0.2164 0.2242 -0.0326 -0.0560 0.0129  116 ALA A C   
946  O O   . ALA A 116 ? 0.2669 0.2168 0.2168 -0.0360 -0.0614 0.0185  116 ALA A O   
947  C CB  . ALA A 116 ? 0.2654 0.2038 0.2417 -0.0254 -0.0595 0.0094  116 ALA A CB  
948  N N   . GLU A 117 ? 0.2541 0.2139 0.2142 -0.0356 -0.0460 0.0099  117 GLU A N   
949  C CA  . GLU A 117 ? 0.2709 0.2353 0.2194 -0.0423 -0.0400 0.0124  117 GLU A CA  
950  C C   . GLU A 117 ? 0.2527 0.2173 0.2002 -0.0454 -0.0330 0.0119  117 GLU A C   
951  O O   . GLU A 117 ? 0.2486 0.2165 0.2051 -0.0423 -0.0293 0.0070  117 GLU A O   
952  C CB  . GLU A 117 ? 0.2510 0.2277 0.2027 -0.0416 -0.0354 0.0076  117 GLU A CB  
953  C CG  . GLU A 117 ? 0.2503 0.2314 0.1913 -0.0478 -0.0297 0.0092  117 GLU A CG  
954  C CD  . GLU A 117 ? 0.2441 0.2350 0.1879 -0.0471 -0.0262 0.0043  117 GLU A CD  
955  O OE1 . GLU A 117 ? 0.2409 0.2339 0.1900 -0.0438 -0.0313 0.0023  117 GLU A OE1 
956  O OE2 . GLU A 117 ? 0.2507 0.2472 0.1920 -0.0499 -0.0186 0.0024  117 GLU A OE2 
957  N N   . LEU A 118 ? 0.2512 0.2127 0.1874 -0.0521 -0.0314 0.0167  118 LEU A N   
958  C CA  . LEU A 118 ? 0.2552 0.2184 0.1903 -0.0563 -0.0253 0.0167  118 LEU A CA  
959  C C   . LEU A 118 ? 0.2385 0.2137 0.1733 -0.0588 -0.0175 0.0142  118 LEU A C   
960  O O   . LEU A 118 ? 0.2545 0.2325 0.1823 -0.0618 -0.0164 0.0153  118 LEU A O   
961  C CB  . LEU A 118 ? 0.2643 0.2168 0.1879 -0.0630 -0.0282 0.0232  118 LEU A CB  
962  C CG  . LEU A 118 ? 0.2542 0.2106 0.1752 -0.0697 -0.0216 0.0236  118 LEU A CG  
963  C CD1 . LEU A 118 ? 0.2554 0.2138 0.1862 -0.0673 -0.0195 0.0199  118 LEU A CD1 
964  C CD2 . LEU A 118 ? 0.2887 0.2333 0.1965 -0.0778 -0.0245 0.0303  118 LEU A CD2 
965  N N   . HIS A 119 ? 0.2254 0.2072 0.1676 -0.0574 -0.0123 0.0106  119 HIS A N   
966  C CA  . HIS A 119 ? 0.2367 0.2290 0.1809 -0.0588 -0.0054 0.0082  119 HIS A CA  
967  C C   . HIS A 119 ? 0.2253 0.2203 0.1707 -0.0629 -0.0023 0.0090  119 HIS A C   
968  O O   . HIS A 119 ? 0.2293 0.2234 0.1798 -0.0613 -0.0030 0.0080  119 HIS A O   
969  C CB  . HIS A 119 ? 0.2181 0.2158 0.1706 -0.0532 -0.0031 0.0034  119 HIS A CB  
970  C CG  . HIS A 119 ? 0.2024 0.2005 0.1552 -0.0503 -0.0047 0.0015  119 HIS A CG  
971  N ND1 . HIS A 119 ? 0.1947 0.1951 0.1540 -0.0459 -0.0037 -0.0028 119 HIS A ND1 
972  C CD2 . HIS A 119 ? 0.2191 0.2158 0.1658 -0.0519 -0.0074 0.0031  119 HIS A CD2 
973  C CE1 . HIS A 119 ? 0.2218 0.2233 0.1808 -0.0447 -0.0057 -0.0041 119 HIS A CE1 
974  N NE2 . HIS A 119 ? 0.2202 0.2192 0.1716 -0.0480 -0.0087 -0.0004 119 HIS A NE2 
975  N N   . LEU A 120 ? 0.2383 0.2379 0.1797 -0.0683 0.0017  0.0100  120 LEU A N   
976  C CA  . LEU A 120 ? 0.2288 0.2349 0.1742 -0.0725 0.0058  0.0095  120 LEU A CA  
977  C C   . LEU A 120 ? 0.2330 0.2507 0.1873 -0.0694 0.0111  0.0051  120 LEU A C   
978  O O   . LEU A 120 ? 0.2238 0.2455 0.1762 -0.0699 0.0148  0.0033  120 LEU A O   
979  C CB  . LEU A 120 ? 0.2532 0.2571 0.1892 -0.0813 0.0076  0.0126  120 LEU A CB  
980  C CG  . LEU A 120 ? 0.2644 0.2543 0.1916 -0.0844 0.0015  0.0177  120 LEU A CG  
981  C CD1 . LEU A 120 ? 0.3295 0.3115 0.2419 -0.0894 -0.0005 0.0219  120 LEU A CD1 
982  C CD2 . LEU A 120 ? 0.2984 0.2879 0.2268 -0.0906 0.0027  0.0189  120 LEU A CD2 
983  N N   . VAL A 121 ? 0.2355 0.2575 0.1990 -0.0660 0.0109  0.0034  121 VAL A N   
984  C CA  . VAL A 121 ? 0.2131 0.2428 0.1853 -0.0613 0.0137  0.0000  121 VAL A CA  
985  C C   . VAL A 121 ? 0.2283 0.2688 0.2095 -0.0635 0.0174  -0.0017 121 VAL A C   
986  O O   . VAL A 121 ? 0.2240 0.2668 0.2087 -0.0663 0.0157  -0.0007 121 VAL A O   
987  C CB  . VAL A 121 ? 0.2108 0.2371 0.1860 -0.0563 0.0100  -0.0003 121 VAL A CB  
988  C CG1 . VAL A 121 ? 0.2130 0.2443 0.1953 -0.0515 0.0119  -0.0027 121 VAL A CG1 
989  C CG2 . VAL A 121 ? 0.2357 0.2528 0.2045 -0.0542 0.0070  0.0002  121 VAL A CG2 
990  N N   . HIS A 122 ? 0.2092 0.2569 0.1955 -0.0623 0.0225  -0.0051 122 HIS A N   
991  C CA  . HIS A 122 ? 0.2048 0.2648 0.2027 -0.0638 0.0268  -0.0082 122 HIS A CA  
992  C C   . HIS A 122 ? 0.2129 0.2782 0.2222 -0.0569 0.0284  -0.0118 122 HIS A C   
993  O O   . HIS A 122 ? 0.2109 0.2711 0.2163 -0.0533 0.0292  -0.0128 122 HIS A O   
994  C CB  . HIS A 122 ? 0.2080 0.2726 0.2018 -0.0711 0.0336  -0.0102 122 HIS A CB  
995  C CG  . HIS A 122 ? 0.2133 0.2692 0.1922 -0.0784 0.0320  -0.0059 122 HIS A CG  
996  N ND1 . HIS A 122 ? 0.2243 0.2687 0.1901 -0.0778 0.0284  -0.0029 122 HIS A ND1 
997  C CD2 . HIS A 122 ? 0.2394 0.2958 0.2144 -0.0866 0.0331  -0.0040 122 HIS A CD2 
998  C CE1 . HIS A 122 ? 0.2413 0.2785 0.1957 -0.0847 0.0266  0.0013  122 HIS A CE1 
999  N NE2 . HIS A 122 ? 0.2565 0.3000 0.2152 -0.0906 0.0297  0.0008  122 HIS A NE2 
1000 N N   . TRP A 123 ? 0.1995 0.2752 0.2236 -0.0552 0.0285  -0.0138 123 TRP A N   
1001 C CA  . TRP A 123 ? 0.2055 0.2854 0.2419 -0.0479 0.0289  -0.0168 123 TRP A CA  
1002 C C   . TRP A 123 ? 0.1821 0.2761 0.2341 -0.0484 0.0350  -0.0226 123 TRP A C   
1003 O O   . TRP A 123 ? 0.2076 0.3114 0.2653 -0.0540 0.0375  -0.0241 123 TRP A O   
1004 C CB  . TRP A 123 ? 0.1801 0.2573 0.2212 -0.0426 0.0208  -0.0137 123 TRP A CB  
1005 C CG  . TRP A 123 ? 0.1944 0.2790 0.2424 -0.0456 0.0168  -0.0123 123 TRP A CG  
1006 C CD1 . TRP A 123 ? 0.1956 0.2758 0.2345 -0.0507 0.0133  -0.0089 123 TRP A CD1 
1007 C CD2 . TRP A 123 ? 0.1925 0.2910 0.2593 -0.0438 0.0157  -0.0149 123 TRP A CD2 
1008 N NE1 . TRP A 123 ? 0.1966 0.2865 0.2461 -0.0529 0.0101  -0.0091 123 TRP A NE1 
1009 C CE2 . TRP A 123 ? 0.1998 0.3021 0.2671 -0.0488 0.0115  -0.0128 123 TRP A CE2 
1010 C CE3 . TRP A 123 ? 0.1863 0.2946 0.2708 -0.0383 0.0178  -0.0193 123 TRP A CE3 
1011 C CZ2 . TRP A 123 ? 0.1822 0.2989 0.2673 -0.0487 0.0089  -0.0149 123 TRP A CZ2 
1012 C CZ3 . TRP A 123 ? 0.1841 0.3073 0.2880 -0.0374 0.0153  -0.0216 123 TRP A CZ3 
1013 C CH2 . TRP A 123 ? 0.2241 0.3518 0.3281 -0.0428 0.0106  -0.0192 123 TRP A CH2 
1014 N N   . ASN A 124 ? 0.2087 0.3036 0.2681 -0.0427 0.0381  -0.0267 124 ASN A N   
1015 C CA  . ASN A 124 ? 0.1920 0.2997 0.2672 -0.0422 0.0455  -0.0341 124 ASN A CA  
1016 C C   . ASN A 124 ? 0.2074 0.3272 0.3041 -0.0380 0.0418  -0.0356 124 ASN A C   
1017 O O   . ASN A 124 ? 0.1992 0.3151 0.3027 -0.0301 0.0346  -0.0331 124 ASN A O   
1018 C CB  . ASN A 124 ? 0.1993 0.3011 0.2750 -0.0367 0.0490  -0.0379 124 ASN A CB  
1019 C CG  . ASN A 124 ? 0.2346 0.3478 0.3247 -0.0366 0.0583  -0.0470 124 ASN A CG  
1020 O OD1 . ASN A 124 ? 0.2285 0.3562 0.3334 -0.0387 0.0617  -0.0511 124 ASN A OD1 
1021 N ND2 . ASN A 124 ? 0.2207 0.3277 0.3065 -0.0348 0.0634  -0.0512 124 ASN A ND2 
1022 N N   . THR A 125 ? 0.1732 0.3080 0.2810 -0.0434 0.0468  -0.0398 125 THR A N   
1023 C CA  . THR A 125 ? 0.1822 0.3308 0.3128 -0.0395 0.0424  -0.0416 125 THR A CA  
1024 C C   . THR A 125 ? 0.2102 0.3653 0.3624 -0.0298 0.0434  -0.0476 125 THR A C   
1025 O O   . THR A 125 ? 0.2459 0.4131 0.4201 -0.0248 0.0387  -0.0495 125 THR A O   
1026 C CB  . THR A 125 ? 0.1957 0.3601 0.3344 -0.0485 0.0481  -0.0455 125 THR A CB  
1027 O OG1 . THR A 125 ? 0.2403 0.4128 0.3833 -0.0525 0.0607  -0.0539 125 THR A OG1 
1028 C CG2 . THR A 125 ? 0.2148 0.3707 0.3327 -0.0578 0.0464  -0.0393 125 THR A CG2 
1029 N N   . LYS A 126 ? 0.2048 0.3527 0.3522 -0.0271 0.0493  -0.0511 126 LYS A N   
1030 C CA  . LYS A 126 ? 0.2389 0.3866 0.4032 -0.0165 0.0483  -0.0551 126 LYS A CA  
1031 C C   . LYS A 126 ? 0.2211 0.3598 0.3877 -0.0081 0.0349  -0.0476 126 LYS A C   
1032 O O   . LYS A 126 ? 0.2450 0.3874 0.4315 0.0010  0.0303  -0.0497 126 LYS A O   
1033 C CB  . LYS A 126 ? 0.2880 0.4241 0.4391 -0.0167 0.0557  -0.0583 126 LYS A CB  
1034 C CG  . LYS A 126 ? 0.2961 0.4250 0.4577 -0.0066 0.0547  -0.0613 126 LYS A CG  
1035 C CD  . LYS A 126 ? 0.3059 0.4240 0.4521 -0.0093 0.0631  -0.0651 126 LYS A CD  
1036 C CE  . LYS A 126 ? 0.3469 0.4564 0.5044 0.0008  0.0623  -0.0686 126 LYS A CE  
1037 N NZ  . LYS A 126 ? 0.3519 0.4490 0.4942 -0.0015 0.0688  -0.0718 126 LYS A NZ  
1038 N N   . TYR A 127 ? 0.2012 0.3275 0.3471 -0.0112 0.0282  -0.0390 127 TYR A N   
1039 C CA  . TYR A 127 ? 0.2167 0.3321 0.3588 -0.0055 0.0162  -0.0315 127 TYR A CA  
1040 C C   . TYR A 127 ? 0.2604 0.3834 0.4045 -0.0091 0.0089  -0.0275 127 TYR A C   
1041 O O   . TYR A 127 ? 0.2798 0.4138 0.4254 -0.0165 0.0135  -0.0298 127 TYR A O   
1042 C CB  . TYR A 127 ? 0.2142 0.3100 0.3314 -0.0070 0.0157  -0.0265 127 TYR A CB  
1043 C CG  . TYR A 127 ? 0.2122 0.3022 0.3278 -0.0050 0.0239  -0.0316 127 TYR A CG  
1044 C CD1 . TYR A 127 ? 0.2255 0.3129 0.3552 0.0035  0.0229  -0.0345 127 TYR A CD1 
1045 C CD2 . TYR A 127 ? 0.2072 0.2938 0.3075 -0.0117 0.0320  -0.0337 127 TYR A CD2 
1046 C CE1 . TYR A 127 ? 0.2258 0.3074 0.3545 0.0051  0.0305  -0.0399 127 TYR A CE1 
1047 C CE2 . TYR A 127 ? 0.2128 0.2944 0.3113 -0.0105 0.0393  -0.0390 127 TYR A CE2 
1048 C CZ  . TYR A 127 ? 0.2423 0.3212 0.3549 -0.0023 0.0390  -0.0425 127 TYR A CZ  
1049 O OH  . TYR A 127 ? 0.2587 0.3322 0.3705 -0.0012 0.0463  -0.0485 127 TYR A OH  
1050 N N   . GLY A 128 ? 0.2886 0.4055 0.4321 -0.0047 -0.0027 -0.0213 128 GLY A N   
1051 C CA  . GLY A 128 ? 0.2854 0.4126 0.4353 -0.0077 -0.0100 -0.0191 128 GLY A CA  
1052 C C   . GLY A 128 ? 0.2435 0.3654 0.3732 -0.0170 -0.0097 -0.0153 128 GLY A C   
1053 O O   . GLY A 128 ? 0.2819 0.4143 0.4164 -0.0225 -0.0115 -0.0156 128 GLY A O   
1054 N N   . ASP A 129 ? 0.2123 0.3180 0.3203 -0.0189 -0.0079 -0.0120 129 ASP A N   
1055 C CA  . ASP A 129 ? 0.2153 0.3135 0.3045 -0.0260 -0.0090 -0.0083 129 ASP A CA  
1056 C C   . ASP A 129 ? 0.2019 0.2850 0.2729 -0.0264 -0.0046 -0.0070 129 ASP A C   
1057 O O   . ASP A 129 ? 0.2121 0.2904 0.2842 -0.0217 -0.0015 -0.0086 129 ASP A O   
1058 C CB  . ASP A 129 ? 0.2562 0.3507 0.3409 -0.0262 -0.0200 -0.0032 129 ASP A CB  
1059 C CG  . ASP A 129 ? 0.3072 0.3913 0.3894 -0.0191 -0.0272 0.0006  129 ASP A CG  
1060 O OD1 . ASP A 129 ? 0.2818 0.3537 0.3536 -0.0170 -0.0237 0.0013  129 ASP A OD1 
1061 O OD2 . ASP A 129 ? 0.3482 0.4357 0.4384 -0.0161 -0.0368 0.0032  129 ASP A OD2 
1062 N N   . PHE A 130 ? 0.1946 0.2699 0.2494 -0.0319 -0.0049 -0.0044 130 PHE A N   
1063 C CA  . PHE A 130 ? 0.2116 0.2747 0.2511 -0.0327 -0.0010 -0.0039 130 PHE A CA  
1064 C C   . PHE A 130 ? 0.2144 0.2668 0.2488 -0.0275 -0.0040 -0.0019 130 PHE A C   
1065 O O   . PHE A 130 ? 0.2173 0.2640 0.2477 -0.0258 0.0007  -0.0035 130 PHE A O   
1066 C CB  . PHE A 130 ? 0.2265 0.2832 0.2523 -0.0384 -0.0022 -0.0018 130 PHE A CB  
1067 C CG  . PHE A 130 ? 0.2032 0.2488 0.2158 -0.0386 0.0007  -0.0017 130 PHE A CG  
1068 C CD1 . PHE A 130 ? 0.2177 0.2533 0.2216 -0.0367 -0.0019 0.0000  130 PHE A CD1 
1069 C CD2 . PHE A 130 ? 0.2173 0.2627 0.2261 -0.0411 0.0062  -0.0034 130 PHE A CD2 
1070 C CE1 . PHE A 130 ? 0.2362 0.2636 0.2304 -0.0370 0.0013  -0.0009 130 PHE A CE1 
1071 C CE2 . PHE A 130 ? 0.2275 0.2642 0.2262 -0.0410 0.0080  -0.0036 130 PHE A CE2 
1072 C CZ  . PHE A 130 ? 0.2291 0.2576 0.2217 -0.0388 0.0059  -0.0028 130 PHE A CZ  
1073 N N   . GLY A 131 ? 0.2222 0.2712 0.2555 -0.0259 -0.0119 0.0017  131 GLY A N   
1074 C CA  . GLY A 131 ? 0.2169 0.2534 0.2420 -0.0225 -0.0149 0.0045  131 GLY A CA  
1075 C C   . GLY A 131 ? 0.2284 0.2643 0.2636 -0.0162 -0.0131 0.0029  131 GLY A C   
1076 O O   . GLY A 131 ? 0.2322 0.2567 0.2592 -0.0147 -0.0113 0.0034  131 GLY A O   
1077 N N   . LYS A 132 ? 0.2056 0.2537 0.2596 -0.0125 -0.0134 0.0002  132 LYS A N   
1078 C CA  . LYS A 132 ? 0.2032 0.2511 0.2686 -0.0062 -0.0105 -0.0028 132 LYS A CA  
1079 C C   . LYS A 132 ? 0.2457 0.2943 0.3084 -0.0085 0.0003  -0.0081 132 LYS A C   
1080 O O   . LYS A 132 ? 0.2155 0.2557 0.2761 -0.0056 0.0037  -0.0098 132 LYS A O   
1081 C CB  . LYS A 132 ? 0.1990 0.2615 0.2878 -0.0015 -0.0136 -0.0053 132 LYS A CB  
1082 C CG  . LYS A 132 ? 0.2386 0.2987 0.3302 0.0019  -0.0261 0.0004  132 LYS A CG  
1083 C CD  . LYS A 132 ? 0.2762 0.3543 0.3934 0.0059  -0.0301 -0.0026 132 LYS A CD  
1084 C CE  . LYS A 132 ? 0.3481 0.4234 0.4682 0.0098  -0.0442 0.0036  132 LYS A CE  
1085 N NZ  . LYS A 132 ? 0.4425 0.5152 0.5457 0.0022  -0.0494 0.0083  132 LYS A NZ  
1086 N N   . ALA A 133 ? 0.2117 0.2691 0.2731 -0.0142 0.0054  -0.0105 133 ALA A N   
1087 C CA  . ALA A 133 ? 0.1924 0.2511 0.2504 -0.0171 0.0146  -0.0152 133 ALA A CA  
1088 C C   . ALA A 133 ? 0.2220 0.2674 0.2631 -0.0188 0.0162  -0.0138 133 ALA A C   
1089 O O   . ALA A 133 ? 0.2076 0.2506 0.2470 -0.0186 0.0222  -0.0175 133 ALA A O   
1090 C CB  . ALA A 133 ? 0.1867 0.2550 0.2434 -0.0240 0.0183  -0.0166 133 ALA A CB  
1091 N N   . VAL A 134 ? 0.1970 0.2346 0.2259 -0.0209 0.0115  -0.0092 134 VAL A N   
1092 C CA  . VAL A 134 ? 0.2229 0.2507 0.2378 -0.0233 0.0138  -0.0090 134 VAL A CA  
1093 C C   . VAL A 134 ? 0.2352 0.2533 0.2483 -0.0198 0.0145  -0.0095 134 VAL A C   
1094 O O   . VAL A 134 ? 0.2180 0.2296 0.2220 -0.0218 0.0176  -0.0107 134 VAL A O   
1095 C CB  . VAL A 134 ? 0.2242 0.2472 0.2283 -0.0266 0.0095  -0.0054 134 VAL A CB  
1096 C CG1 . VAL A 134 ? 0.2055 0.2222 0.2078 -0.0245 0.0032  -0.0016 134 VAL A CG1 
1097 C CG2 . VAL A 134 ? 0.2134 0.2293 0.2059 -0.0294 0.0125  -0.0065 134 VAL A CG2 
1098 N N   . GLN A 135 ? 0.2178 0.2348 0.2402 -0.0146 0.0114  -0.0086 135 GLN A N   
1099 C CA  . GLN A 135 ? 0.2219 0.2276 0.2431 -0.0111 0.0117  -0.0088 135 GLN A CA  
1100 C C   . GLN A 135 ? 0.2448 0.2538 0.2754 -0.0087 0.0185  -0.0150 135 GLN A C   
1101 O O   . GLN A 135 ? 0.3097 0.3087 0.3405 -0.0056 0.0194  -0.0159 135 GLN A O   
1102 C CB  . GLN A 135 ? 0.2349 0.2350 0.2605 -0.0062 0.0035  -0.0040 135 GLN A CB  
1103 C CG  . GLN A 135 ? 0.2351 0.2302 0.2484 -0.0097 -0.0033 0.0019  135 GLN A CG  
1104 C CD  . GLN A 135 ? 0.2340 0.2169 0.2290 -0.0147 -0.0009 0.0031  135 GLN A CD  
1105 O OE1 . GLN A 135 ? 0.2955 0.2695 0.2867 -0.0144 0.0031  0.0015  135 GLN A OE1 
1106 N NE2 . GLN A 135 ? 0.2250 0.2078 0.2096 -0.0196 -0.0028 0.0051  135 GLN A NE2 
1107 N N   . GLN A 136 ? 0.2254 0.2469 0.2622 -0.0108 0.0238  -0.0194 136 GLN A N   
1108 C CA  . GLN A 136 ? 0.2361 0.2618 0.2821 -0.0092 0.0309  -0.0264 136 GLN A CA  
1109 C C   . GLN A 136 ? 0.2311 0.2590 0.2673 -0.0154 0.0378  -0.0302 136 GLN A C   
1110 O O   . GLN A 136 ? 0.2276 0.2598 0.2561 -0.0204 0.0372  -0.0281 136 GLN A O   
1111 C CB  . GLN A 136 ? 0.2362 0.2764 0.3006 -0.0066 0.0319  -0.0297 136 GLN A CB  
1112 C CG  . GLN A 136 ? 0.2661 0.3062 0.3431 0.0002  0.0236  -0.0262 136 GLN A CG  
1113 C CD  . GLN A 136 ? 0.3345 0.3628 0.4167 0.0072  0.0218  -0.0266 136 GLN A CD  
1114 O OE1 . GLN A 136 ? 0.3745 0.3983 0.4568 0.0077  0.0287  -0.0321 136 GLN A OE1 
1115 N NE2 . GLN A 136 ? 0.3530 0.3746 0.4379 0.0121  0.0120  -0.0205 136 GLN A NE2 
1116 N N   . PRO A 137 ? 0.2413 0.2660 0.2774 -0.0154 0.0439  -0.0358 137 PRO A N   
1117 C CA  . PRO A 137 ? 0.2463 0.2727 0.2712 -0.0220 0.0492  -0.0391 137 PRO A CA  
1118 C C   . PRO A 137 ? 0.2585 0.2970 0.2840 -0.0267 0.0523  -0.0407 137 PRO A C   
1119 O O   . PRO A 137 ? 0.2769 0.3160 0.2903 -0.0326 0.0526  -0.0395 137 PRO A O   
1120 C CB  . PRO A 137 ? 0.2794 0.3007 0.3066 -0.0208 0.0555  -0.0460 137 PRO A CB  
1121 C CG  . PRO A 137 ? 0.3516 0.3624 0.3848 -0.0142 0.0516  -0.0437 137 PRO A CG  
1122 C CD  . PRO A 137 ? 0.2984 0.3147 0.3420 -0.0098 0.0452  -0.0389 137 PRO A CD  
1123 N N   . ASP A 138 ? 0.2174 0.2657 0.2570 -0.0246 0.0547  -0.0437 138 ASP A N   
1124 C CA  . ASP A 138 ? 0.2208 0.2808 0.2610 -0.0302 0.0583  -0.0453 138 ASP A CA  
1125 C C   . ASP A 138 ? 0.2086 0.2734 0.2520 -0.0304 0.0521  -0.0394 138 ASP A C   
1126 O O   . ASP A 138 ? 0.2257 0.3016 0.2754 -0.0339 0.0550  -0.0412 138 ASP A O   
1127 C CB  . ASP A 138 ? 0.2194 0.2894 0.2741 -0.0295 0.0666  -0.0539 138 ASP A CB  
1128 C CG  . ASP A 138 ? 0.2732 0.3468 0.3489 -0.0207 0.0639  -0.0552 138 ASP A CG  
1129 O OD1 . ASP A 138 ? 0.2635 0.3298 0.3403 -0.0155 0.0556  -0.0491 138 ASP A OD1 
1130 O OD2 . ASP A 138 ? 0.2877 0.3717 0.3797 -0.0191 0.0701  -0.0628 138 ASP A OD2 
1131 N N   . GLY A 139 ? 0.2092 0.2661 0.2482 -0.0276 0.0444  -0.0331 139 GLY A N   
1132 C CA  . GLY A 139 ? 0.2037 0.2647 0.2469 -0.0273 0.0382  -0.0283 139 GLY A CA  
1133 C C   . GLY A 139 ? 0.1994 0.2624 0.2324 -0.0343 0.0373  -0.0251 139 GLY A C   
1134 O O   . GLY A 139 ? 0.2120 0.2828 0.2513 -0.0362 0.0356  -0.0239 139 GLY A O   
1135 N N   . LEU A 140 ? 0.2105 0.2663 0.2286 -0.0379 0.0375  -0.0236 140 LEU A N   
1136 C CA  . LEU A 140 ? 0.1980 0.2524 0.2063 -0.0432 0.0347  -0.0196 140 LEU A CA  
1137 C C   . LEU A 140 ? 0.2168 0.2711 0.2148 -0.0493 0.0389  -0.0211 140 LEU A C   
1138 O O   . LEU A 140 ? 0.2216 0.2745 0.2165 -0.0493 0.0429  -0.0247 140 LEU A O   
1139 C CB  . LEU A 140 ? 0.2003 0.2450 0.2002 -0.0416 0.0287  -0.0154 140 LEU A CB  
1140 C CG  . LEU A 140 ? 0.2140 0.2561 0.2193 -0.0369 0.0239  -0.0132 140 LEU A CG  
1141 C CD1 . LEU A 140 ? 0.2100 0.2432 0.2053 -0.0374 0.0199  -0.0104 140 LEU A CD1 
1142 C CD2 . LEU A 140 ? 0.2095 0.2589 0.2233 -0.0375 0.0211  -0.0117 140 LEU A CD2 
1143 N N   . ALA A 141 ? 0.2092 0.2639 0.2007 -0.0548 0.0374  -0.0179 141 ALA A N   
1144 C CA  . ALA A 141 ? 0.2151 0.2668 0.1933 -0.0613 0.0389  -0.0172 141 ALA A CA  
1145 C C   . ALA A 141 ? 0.2330 0.2769 0.2029 -0.0628 0.0320  -0.0114 141 ALA A C   
1146 O O   . ALA A 141 ? 0.2337 0.2786 0.2069 -0.0640 0.0296  -0.0089 141 ALA A O   
1147 C CB  . ALA A 141 ? 0.2455 0.3050 0.2234 -0.0684 0.0454  -0.0198 141 ALA A CB  
1148 N N   . VAL A 142 ? 0.2175 0.2540 0.1778 -0.0627 0.0285  -0.0097 142 VAL A N   
1149 C CA  . VAL A 142 ? 0.2274 0.2560 0.1816 -0.0632 0.0218  -0.0049 142 VAL A CA  
1150 C C   . VAL A 142 ? 0.2410 0.2650 0.1820 -0.0692 0.0204  -0.0024 142 VAL A C   
1151 O O   . VAL A 142 ? 0.2674 0.2911 0.2024 -0.0703 0.0214  -0.0041 142 VAL A O   
1152 C CB  . VAL A 142 ? 0.2143 0.2381 0.1707 -0.0573 0.0174  -0.0051 142 VAL A CB  
1153 C CG1 . VAL A 142 ? 0.2427 0.2588 0.1952 -0.0575 0.0109  -0.0011 142 VAL A CG1 
1154 C CG2 . VAL A 142 ? 0.2278 0.2542 0.1939 -0.0526 0.0184  -0.0067 142 VAL A CG2 
1155 N N   . LEU A 143 ? 0.2460 0.2657 0.1817 -0.0738 0.0178  0.0019  143 LEU A N   
1156 C CA  . LEU A 143 ? 0.2685 0.2807 0.1895 -0.0801 0.0147  0.0061  143 LEU A CA  
1157 C C   . LEU A 143 ? 0.2798 0.2820 0.1986 -0.0759 0.0056  0.0098  143 LEU A C   
1158 O O   . LEU A 143 ? 0.2757 0.2739 0.1997 -0.0733 0.0022  0.0115  143 LEU A O   
1159 C CB  . LEU A 143 ? 0.2712 0.2830 0.1877 -0.0880 0.0172  0.0087  143 LEU A CB  
1160 C CG  . LEU A 143 ? 0.3147 0.3167 0.2133 -0.0964 0.0143  0.0141  143 LEU A CG  
1161 C CD1 . LEU A 143 ? 0.3405 0.3450 0.2283 -0.1011 0.0182  0.0120  143 LEU A CD1 
1162 C CD2 . LEU A 143 ? 0.3193 0.3218 0.2149 -0.1051 0.0184  0.0159  143 LEU A CD2 
1163 N N   . GLY A 144 ? 0.2550 0.2544 0.1681 -0.0748 0.0019  0.0100  144 GLY A N   
1164 C CA  . GLY A 144 ? 0.2821 0.2742 0.1964 -0.0699 -0.0068 0.0122  144 GLY A CA  
1165 C C   . GLY A 144 ? 0.2839 0.2654 0.1845 -0.0745 -0.0140 0.0185  144 GLY A C   
1166 O O   . GLY A 144 ? 0.2892 0.2703 0.1772 -0.0810 -0.0129 0.0200  144 GLY A O   
1167 N N   . ILE A 145 ? 0.2676 0.2397 0.1701 -0.0717 -0.0212 0.0221  145 ILE A N   
1168 C CA  . ILE A 145 ? 0.3023 0.2610 0.1923 -0.0753 -0.0298 0.0293  145 ILE A CA  
1169 C C   . ILE A 145 ? 0.3012 0.2537 0.1991 -0.0672 -0.0397 0.0299  145 ILE A C   
1170 O O   . ILE A 145 ? 0.3059 0.2590 0.2170 -0.0611 -0.0394 0.0267  145 ILE A O   
1171 C CB  . ILE A 145 ? 0.3154 0.2661 0.1994 -0.0812 -0.0285 0.0335  145 ILE A CB  
1172 C CG1 . ILE A 145 ? 0.3304 0.2903 0.2100 -0.0891 -0.0179 0.0314  145 ILE A CG1 
1173 C CG2 . ILE A 145 ? 0.3273 0.2607 0.1965 -0.0853 -0.0384 0.0420  145 ILE A CG2 
1174 C CD1 . ILE A 145 ? 0.3558 0.3113 0.2309 -0.0966 -0.0147 0.0343  145 ILE A CD1 
1175 N N   . PHE A 146 ? 0.3096 0.2566 0.1999 -0.0673 -0.0483 0.0335  146 PHE A N   
1176 C CA  . PHE A 146 ? 0.3038 0.2460 0.2038 -0.0592 -0.0587 0.0338  146 PHE A CA  
1177 C C   . PHE A 146 ? 0.3425 0.2682 0.2397 -0.0586 -0.0667 0.0399  146 PHE A C   
1178 O O   . PHE A 146 ? 0.3439 0.2587 0.2246 -0.0664 -0.0681 0.0469  146 PHE A O   
1179 C CB  . PHE A 146 ? 0.3003 0.2433 0.1940 -0.0595 -0.0665 0.0356  146 PHE A CB  
1180 C CG  . PHE A 146 ? 0.2881 0.2459 0.1853 -0.0597 -0.0598 0.0290  146 PHE A CG  
1181 C CD1 . PHE A 146 ? 0.2863 0.2548 0.2019 -0.0527 -0.0557 0.0212  146 PHE A CD1 
1182 C CD2 . PHE A 146 ? 0.3067 0.2668 0.1881 -0.0677 -0.0571 0.0302  146 PHE A CD2 
1183 C CE1 . PHE A 146 ? 0.3047 0.2850 0.2232 -0.0532 -0.0497 0.0153  146 PHE A CE1 
1184 C CE2 . PHE A 146 ? 0.3035 0.2760 0.1881 -0.0681 -0.0507 0.0236  146 PHE A CE2 
1185 C CZ  . PHE A 146 ? 0.3002 0.2825 0.2039 -0.0606 -0.0473 0.0163  146 PHE A CZ  
1186 N N   . LEU A 147 ? 0.3195 0.2428 0.2327 -0.0497 -0.0716 0.0370  147 LEU A N   
1187 C CA  . LEU A 147 ? 0.3345 0.2411 0.2482 -0.0471 -0.0803 0.0417  147 LEU A CA  
1188 C C   . LEU A 147 ? 0.3375 0.2392 0.2571 -0.0402 -0.0937 0.0435  147 LEU A C   
1189 O O   . LEU A 147 ? 0.3463 0.2588 0.2841 -0.0321 -0.0945 0.0364  147 LEU A O   
1190 C CB  . LEU A 147 ? 0.3320 0.2387 0.2606 -0.0422 -0.0757 0.0358  147 LEU A CB  
1191 C CG  . LEU A 147 ? 0.3197 0.2256 0.2419 -0.0491 -0.0663 0.0360  147 LEU A CG  
1192 C CD1 . LEU A 147 ? 0.3330 0.2554 0.2537 -0.0532 -0.0554 0.0322  147 LEU A CD1 
1193 C CD2 . LEU A 147 ? 0.3302 0.2331 0.2654 -0.0444 -0.0641 0.0307  147 LEU A CD2 
1194 N N   . LYS A 148 ? 0.3680 0.2533 0.2731 -0.0434 -0.1044 0.0530  148 LYS A N   
1195 C CA  . LYS A 148 ? 0.3972 0.2756 0.3072 -0.0367 -0.1195 0.0563  148 LYS A CA  
1196 C C   . LYS A 148 ? 0.4364 0.2959 0.3518 -0.0315 -0.1281 0.0599  148 LYS A C   
1197 O O   . LYS A 148 ? 0.4900 0.3350 0.3919 -0.0381 -0.1263 0.0655  148 LYS A O   
1198 C CB  . LYS A 148 ? 0.4691 0.3408 0.3557 -0.0447 -0.1271 0.0655  148 LYS A CB  
1199 C CG  . LYS A 148 ? 0.5809 0.4442 0.4689 -0.0391 -0.1449 0.0708  148 LYS A CG  
1200 C CD  . LYS A 148 ? 0.6629 0.5173 0.5212 -0.0503 -0.1506 0.0808  148 LYS A CD  
1201 C CE  . LYS A 148 ? 0.7497 0.5881 0.5854 -0.0615 -0.1452 0.0881  148 LYS A CE  
1202 N NZ  . LYS A 148 ? 0.8229 0.6415 0.6636 -0.0570 -0.1521 0.0926  148 LYS A NZ  
1203 N N   . VAL A 149 ? 0.4038 0.2635 0.3397 -0.0201 -0.1374 0.0562  149 VAL A N   
1204 C CA  . VAL A 149 ? 0.4595 0.3009 0.4038 -0.0135 -0.1461 0.0583  149 VAL A CA  
1205 C C   . VAL A 149 ? 0.4773 0.2952 0.4015 -0.0174 -0.1609 0.0720  149 VAL A C   
1206 O O   . VAL A 149 ? 0.5224 0.3400 0.4394 -0.0174 -0.1720 0.0776  149 VAL A O   
1207 C CB  . VAL A 149 ? 0.4930 0.3433 0.4676 0.0002  -0.1514 0.0491  149 VAL A CB  
1208 C CG1 . VAL A 149 ? 0.5189 0.3487 0.5029 0.0079  -0.1624 0.0515  149 VAL A CG1 
1209 C CG2 . VAL A 149 ? 0.4700 0.3393 0.4614 0.0025  -0.1361 0.0361  149 VAL A CG2 
1210 N N   . GLY A 150 ? 0.4765 0.2739 0.3906 -0.0213 -0.1615 0.0775  150 GLY A N   
1211 C CA  . GLY A 150 ? 0.5191 0.2904 0.4117 -0.0263 -0.1747 0.0911  150 GLY A CA  
1212 C C   . GLY A 150 ? 0.5221 0.2739 0.4092 -0.0301 -0.1714 0.0936  150 GLY A C   
1213 O O   . GLY A 150 ? 0.5197 0.2705 0.4280 -0.0214 -0.1695 0.0858  150 GLY A O   
1214 N N   . SER A 151 ? 0.5601 0.2963 0.4188 -0.0437 -0.1702 0.1037  151 SER A N   
1215 C CA  A SER A 151 ? 0.5578 0.2749 0.4090 -0.0494 -0.1667 0.1065  151 SER A CA  
1216 C CA  B SER A 151 ? 0.5555 0.2726 0.4072 -0.0491 -0.1668 0.1063  151 SER A CA  
1217 C C   . SER A 151 ? 0.5299 0.2649 0.3919 -0.0517 -0.1487 0.0955  151 SER A C   
1218 O O   . SER A 151 ? 0.5338 0.2925 0.3983 -0.0541 -0.1379 0.0895  151 SER A O   
1219 C CB  A SER A 151 ? 0.5991 0.2974 0.4162 -0.0651 -0.1688 0.1196  151 SER A CB  
1220 C CB  B SER A 151 ? 0.6009 0.2981 0.4188 -0.0645 -0.1694 0.1197  151 SER A CB  
1221 O OG  A SER A 151 ? 0.6016 0.3186 0.4055 -0.0764 -0.1555 0.1179  151 SER A OG  
1222 O OG  B SER A 151 ? 0.6356 0.3188 0.4452 -0.0621 -0.1849 0.1278  151 SER A OG  
1223 N N   . ALA A 152 ? 0.5612 0.2836 0.4288 -0.0513 -0.1462 0.0931  152 ALA A N   
1224 C CA  . ALA A 152 ? 0.5277 0.2643 0.4036 -0.0545 -0.1307 0.0836  152 ALA A CA  
1225 C C   . ALA A 152 ? 0.5536 0.2968 0.4089 -0.0698 -0.1201 0.0874  152 ALA A C   
1226 O O   . ALA A 152 ? 0.6001 0.3272 0.4323 -0.0803 -0.1241 0.0979  152 ALA A O   
1227 C CB  . ALA A 152 ? 0.5371 0.2555 0.4205 -0.0521 -0.1317 0.0810  152 ALA A CB  
1228 N N   . LEU A 153 ? 0.4988 0.2656 0.3626 -0.0713 -0.1067 0.0786  153 LEU A N   
1229 C CA  . LEU A 153 ? 0.4726 0.2497 0.3224 -0.0843 -0.0957 0.0799  153 LEU A CA  
1230 C C   . LEU A 153 ? 0.4551 0.2281 0.3058 -0.0906 -0.0883 0.0770  153 LEU A C   
1231 O O   . LEU A 153 ? 0.4454 0.2298 0.3133 -0.0849 -0.0826 0.0677  153 LEU A O   
1232 C CB  . LEU A 153 ? 0.4610 0.2661 0.3201 -0.0818 -0.0866 0.0724  153 LEU A CB  
1233 C CG  . LEU A 153 ? 0.4759 0.2939 0.3228 -0.0939 -0.0756 0.0730  153 LEU A CG  
1234 C CD1 . LEU A 153 ? 0.5230 0.3306 0.3458 -0.1037 -0.0798 0.0828  153 LEU A CD1 
1235 C CD2 . LEU A 153 ? 0.4505 0.2940 0.3099 -0.0894 -0.0672 0.0647  153 LEU A CD2 
1236 N N   . PRO A 154 ? 0.4754 0.2754 0.2790 -0.1244 -0.0933 0.0976  154 PRO A N   
1237 C CA  . PRO A 154 ? 0.5100 0.2716 0.2795 -0.1423 -0.0935 0.0882  154 PRO A CA  
1238 C C   . PRO A 154 ? 0.4965 0.3056 0.2948 -0.1528 -0.0904 0.0755  154 PRO A C   
1239 O O   . PRO A 154 ? 0.5278 0.3147 0.3090 -0.1553 -0.0893 0.0684  154 PRO A O   
1240 C CB  . PRO A 154 ? 0.5793 0.3305 0.3241 -0.1683 -0.0992 0.0867  154 PRO A CB  
1241 C CG  . PRO A 154 ? 0.6038 0.3555 0.3557 -0.1557 -0.1014 0.0989  154 PRO A CG  
1242 C CD  . PRO A 154 ? 0.5215 0.3237 0.3175 -0.1407 -0.0986 0.1046  154 PRO A CD  
1243 N N   . GLY A 155 ? 0.4620 0.3322 0.3004 -0.1563 -0.0884 0.0732  155 GLY A N   
1244 C CA  . GLY A 155 ? 0.4426 0.3588 0.3089 -0.1609 -0.0846 0.0636  155 GLY A CA  
1245 C C   . GLY A 155 ? 0.3893 0.3093 0.2721 -0.1371 -0.0814 0.0582  155 GLY A C   
1246 O O   . GLY A 155 ? 0.3980 0.3450 0.2963 -0.1408 -0.0799 0.0512  155 GLY A O   
1247 N N   . LEU A 156 ? 0.3726 0.2711 0.2531 -0.1128 -0.0803 0.0632  156 LEU A N   
1248 C CA  . LEU A 156 ? 0.3627 0.2661 0.2561 -0.0910 -0.0766 0.0594  156 LEU A CA  
1249 C C   . LEU A 156 ? 0.4201 0.2713 0.2779 -0.0858 -0.0745 0.0560  156 LEU A C   
1250 O O   . LEU A 156 ? 0.3949 0.2490 0.2586 -0.0727 -0.0706 0.0506  156 LEU A O   
1251 C CB  . LEU A 156 ? 0.3582 0.2787 0.2700 -0.0678 -0.0756 0.0696  156 LEU A CB  
1252 C CG  . LEU A 156 ? 0.3580 0.2982 0.2883 -0.0467 -0.0720 0.0689  156 LEU A CG  
1253 C CD1 . LEU A 156 ? 0.3122 0.2856 0.2641 -0.0563 -0.0725 0.0586  156 LEU A CD1 
1254 C CD2 . LEU A 156 ? 0.3324 0.2983 0.2786 -0.0305 -0.0732 0.0845  156 LEU A CD2 
1255 N N   . GLN A 157 ? 0.4696 0.2670 0.2838 -0.0977 -0.0767 0.0586  157 GLN A N   
1256 C CA  . GLN A 157 ? 0.5068 0.2370 0.2742 -0.0866 -0.0723 0.0562  157 GLN A CA  
1257 C C   . GLN A 157 ? 0.5199 0.2467 0.2762 -0.1028 -0.0723 0.0447  157 GLN A C   
1258 O O   . GLN A 157 ? 0.5157 0.2114 0.2527 -0.0852 -0.0655 0.0399  157 GLN A O   
1259 C CB  . GLN A 157 ? 0.6084 0.2679 0.3190 -0.0987 -0.0757 0.0619  157 GLN A CB  
1260 C CG  . GLN A 157 ? 0.7208 0.2977 0.3768 -0.0721 -0.0672 0.0622  157 GLN A CG  
1261 C CD  . GLN A 157 ? 0.7331 0.3308 0.4185 -0.0219 -0.0567 0.0704  157 GLN A CD  
1262 O OE1 . GLN A 157 ? 0.6975 0.3424 0.4223 -0.0083 -0.0590 0.0828  157 GLN A OE1 
1263 N NE2 . GLN A 157 ? 0.7112 0.2734 0.3723 0.0035  -0.0452 0.0651  157 GLN A NE2 
1264 N N   . LYS A 158 ? 0.4764 0.2417 0.2472 -0.1347 -0.0792 0.0417  158 LYS A N   
1265 C CA  . LYS A 158 ? 0.5002 0.2691 0.2617 -0.1525 -0.0814 0.0346  158 LYS A CA  
1266 C C   . LYS A 158 ? 0.4330 0.2363 0.2307 -0.1276 -0.0762 0.0297  158 LYS A C   
1267 O O   . LYS A 158 ? 0.4709 0.2538 0.2490 -0.1295 -0.0748 0.0237  158 LYS A O   
1268 C CB  . LYS A 158 ? 0.4919 0.3188 0.2741 -0.1808 -0.0868 0.0379  158 LYS A CB  
1269 C CG  . LYS A 158 ? 0.5263 0.3666 0.2987 -0.1941 -0.0865 0.0375  158 LYS A CG  
1270 C CD  . LYS A 158 ? 0.5232 0.4394 0.3344 -0.2032 -0.0853 0.0451  158 LYS A CD  
1271 C CE  . LYS A 158 ? 0.5138 0.4503 0.3218 -0.2153 -0.0861 0.0487  158 LYS A CE  
1272 N NZ  . LYS A 158 ? 0.5400 0.4501 0.2971 -0.2449 -0.0900 0.0569  158 LYS A NZ  
1273 N N   . VAL A 159 ? 0.3673 0.2209 0.2131 -0.1080 -0.0742 0.0324  159 VAL A N   
1274 C CA  . VAL A 159 ? 0.3251 0.2076 0.1998 -0.0873 -0.0705 0.0294  159 VAL A CA  
1275 C C   . VAL A 159 ? 0.3862 0.2285 0.2377 -0.0615 -0.0623 0.0293  159 VAL A C   
1276 O O   . VAL A 159 ? 0.4061 0.2391 0.2482 -0.0561 -0.0587 0.0235  159 VAL A O   
1277 C CB  . VAL A 159 ? 0.3070 0.2400 0.2247 -0.0766 -0.0709 0.0336  159 VAL A CB  
1278 C CG1 . VAL A 159 ? 0.3096 0.2662 0.2491 -0.0576 -0.0685 0.0327  159 VAL A CG1 
1279 C CG2 . VAL A 159 ? 0.3373 0.3111 0.2769 -0.0947 -0.0748 0.0328  159 VAL A CG2 
1280 N N   . VAL A 160 ? 0.4267 0.2485 0.2695 -0.0428 -0.0583 0.0374  160 VAL A N   
1281 C CA  A VAL A 160 ? 0.4763 0.2697 0.3019 -0.0098 -0.0477 0.0411  160 VAL A CA  
1282 C CA  B VAL A 160 ? 0.4696 0.2675 0.2982 -0.0103 -0.0478 0.0403  160 VAL A CA  
1283 C C   . VAL A 160 ? 0.5412 0.2662 0.3109 -0.0118 -0.0413 0.0317  160 VAL A C   
1284 O O   . VAL A 160 ? 0.5620 0.2741 0.3203 0.0105  -0.0308 0.0287  160 VAL A O   
1285 C CB  A VAL A 160 ? 0.5330 0.3122 0.3532 0.0092  -0.0458 0.0549  160 VAL A CB  
1286 C CB  B VAL A 160 ? 0.5176 0.3164 0.3520 0.0142  -0.0449 0.0552  160 VAL A CB  
1287 C CG1 A VAL A 160 ? 0.5970 0.3228 0.3791 0.0442  -0.0326 0.0591  160 VAL A CG1 
1288 C CG1 B VAL A 160 ? 0.4637 0.3354 0.3509 0.0134  -0.0509 0.0635  160 VAL A CG1 
1289 C CG2 A VAL A 160 ? 0.4937 0.3422 0.3652 0.0174  -0.0496 0.0661  160 VAL A CG2 
1290 C CG2 B VAL A 160 ? 0.5587 0.3086 0.3582 0.0007  -0.0491 0.0583  160 VAL A CG2 
1291 N N   . ASP A 161 ? 0.5548 0.2334 0.2833 -0.0417 -0.0474 0.0275  161 ASP A N   
1292 C CA  . ASP A 161 ? 0.6475 0.2435 0.3054 -0.0501 -0.0426 0.0196  161 ASP A CA  
1293 C C   . ASP A 161 ? 0.6439 0.2496 0.2986 -0.0632 -0.0423 0.0094  161 ASP A C   
1294 O O   . ASP A 161 ? 0.7807 0.3178 0.3763 -0.0603 -0.0338 0.0020  161 ASP A O   
1295 C CB  . ASP A 161 ? 0.7109 0.2595 0.3217 -0.0892 -0.0527 0.0199  161 ASP A CB  
1296 C CG  . ASP A 161 ? 0.7608 0.2621 0.3443 -0.0755 -0.0510 0.0291  161 ASP A CG  
1297 O OD1 . ASP A 161 ? 0.7738 0.2693 0.3666 -0.0316 -0.0403 0.0357  161 ASP A OD1 
1298 O OD2 . ASP A 161 ? 0.8185 0.3100 0.3799 -0.1063 -0.0601 0.0296  161 ASP A OD2 
1299 N N   . VAL A 162 ? 0.5256 0.2088 0.2365 -0.0773 -0.0509 0.0091  162 VAL A N   
1300 C CA  . VAL A 162 ? 0.5328 0.2315 0.2440 -0.0931 -0.0537 0.0021  162 VAL A CA  
1301 C C   . VAL A 162 ? 0.4773 0.2084 0.2192 -0.0625 -0.0451 0.0004  162 VAL A C   
1302 O O   . VAL A 162 ? 0.5011 0.2341 0.2347 -0.0710 -0.0451 -0.0056 162 VAL A O   
1303 C CB  . VAL A 162 ? 0.4756 0.2399 0.2274 -0.1239 -0.0681 0.0055  162 VAL A CB  
1304 C CG1 . VAL A 162 ? 0.4366 0.2745 0.2560 -0.1049 -0.0692 0.0095  162 VAL A CG1 
1305 C CG2 . VAL A 162 ? 0.5316 0.2947 0.2628 -0.1533 -0.0750 0.0018  162 VAL A CG2 
1306 N N   . LEU A 163 ? 0.4546 0.2110 0.2271 -0.0299 -0.0382 0.0073  163 LEU A N   
1307 C CA  . LEU A 163 ? 0.4444 0.2482 0.2521 -0.0089 -0.0333 0.0088  163 LEU A CA  
1308 C C   . LEU A 163 ? 0.5030 0.2677 0.2720 0.0075  -0.0194 0.0022  163 LEU A C   
1309 O O   . LEU A 163 ? 0.4438 0.2430 0.2314 0.0098  -0.0182 0.0000  163 LEU A O   
1310 C CB  . LEU A 163 ? 0.4083 0.2529 0.2534 0.0168  -0.0306 0.0212  163 LEU A CB  
1311 C CG  . LEU A 163 ? 0.3652 0.2502 0.2469 0.0002  -0.0430 0.0267  163 LEU A CG  
1312 C CD1 . LEU A 163 ? 0.3570 0.2814 0.2690 0.0220  -0.0412 0.0407  163 LEU A CD1 
1313 C CD2 . LEU A 163 ? 0.3399 0.2656 0.2495 -0.0204 -0.0528 0.0219  163 LEU A CD2 
1314 N N   . ASP A 164 ? 0.5926 0.2811 0.3026 0.0203  -0.0075 -0.0009 164 ASP A N   
1315 C CA  . ASP A 164 ? 0.6365 0.2824 0.3029 0.0394  0.0093  -0.0084 164 ASP A CA  
1316 C C   . ASP A 164 ? 0.6211 0.2495 0.2604 0.0048  0.0032  -0.0204 164 ASP A C   
1317 O O   . ASP A 164 ? 0.6660 0.2747 0.2780 0.0165  0.0159  -0.0272 164 ASP A O   
1318 C CB  . ASP A 164 ? 0.8375 0.3894 0.4335 0.0633  0.0254  -0.0099 164 ASP A CB  
1319 C CG  . ASP A 164 ? 0.9572 0.5317 0.5766 0.1157  0.0399  0.0045  164 ASP A CG  
1320 O OD1 . ASP A 164 ? 0.9308 0.5909 0.6117 0.1336  0.0410  0.0142  164 ASP A OD1 
1321 O OD2 . ASP A 164 ? 1.0568 0.5653 0.6319 0.1376  0.0489  0.0086  164 ASP A OD2 
1322 N N   . SER A 165 ? 0.5914 0.2341 0.2397 -0.0366 -0.0155 -0.0212 165 SER A N   
1323 C CA  . SER A 165 ? 0.6006 0.2414 0.2310 -0.0717 -0.0245 -0.0278 165 SER A CA  
1324 C C   . SER A 165 ? 0.5140 0.2381 0.2076 -0.0746 -0.0336 -0.0243 165 SER A C   
1325 O O   . SER A 165 ? 0.5541 0.2838 0.2373 -0.1008 -0.0415 -0.0275 165 SER A O   
1326 C CB  . SER A 165 ? 0.6913 0.3121 0.2968 -0.1165 -0.0405 -0.0264 165 SER A CB  
1327 O OG  . SER A 165 ? 0.6427 0.3389 0.3132 -0.1263 -0.0546 -0.0172 165 SER A OG  
1328 N N   . ILE A 166 ? 0.3433 0.2134 0.2562 -0.0316 -0.0349 -0.0093 166 ILE A N   
1329 C CA  . ILE A 166 ? 0.3263 0.2074 0.2412 -0.0317 -0.0303 -0.0114 166 ILE A CA  
1330 C C   . ILE A 166 ? 0.3191 0.2072 0.2386 -0.0267 -0.0280 -0.0120 166 ILE A C   
1331 O O   . ILE A 166 ? 0.2884 0.1864 0.2107 -0.0283 -0.0260 -0.0108 166 ILE A O   
1332 C CB  . ILE A 166 ? 0.3069 0.1956 0.2222 -0.0384 -0.0295 -0.0092 166 ILE A CB  
1333 C CG1 . ILE A 166 ? 0.2913 0.1823 0.2074 -0.0413 -0.0313 -0.0043 166 ILE A CG1 
1334 C CG2 . ILE A 166 ? 0.3202 0.2040 0.2328 -0.0434 -0.0309 -0.0103 166 ILE A CG2 
1335 C CD1 . ILE A 166 ? 0.2904 0.1928 0.2079 -0.0461 -0.0288 -0.0035 166 ILE A CD1 
1336 N N   . LYS A 167 ? 0.3422 0.2257 0.2630 -0.0206 -0.0282 -0.0145 167 LYS A N   
1337 C CA  . LYS A 167 ? 0.3352 0.2258 0.2625 -0.0158 -0.0268 -0.0150 167 LYS A CA  
1338 C C   . LYS A 167 ? 0.3175 0.2186 0.2465 -0.0159 -0.0211 -0.0174 167 LYS A C   
1339 O O   . LYS A 167 ? 0.3185 0.2288 0.2533 -0.0150 -0.0198 -0.0165 167 LYS A O   
1340 C CB  . LYS A 167 ? 0.3521 0.2358 0.2814 -0.0089 -0.0282 -0.0183 167 LYS A CB  
1341 C CG  . LYS A 167 ? 0.4344 0.3268 0.3729 -0.0034 -0.0268 -0.0199 167 LYS A CG  
1342 C CD  . LYS A 167 ? 0.5028 0.3887 0.4445 0.0043  -0.0284 -0.0242 167 LYS A CD  
1343 C CE  . LYS A 167 ? 0.5836 0.4797 0.5365 0.0099  -0.0272 -0.0266 167 LYS A CE  
1344 N NZ  . LYS A 167 ? 0.6719 0.5632 0.6288 0.0177  -0.0277 -0.0323 167 LYS A NZ  
1345 N N   . THR A 168 ? 0.3045 0.2035 0.2281 -0.0168 -0.0182 -0.0205 168 THR A N   
1346 C CA  . THR A 168 ? 0.2954 0.2018 0.2187 -0.0169 -0.0130 -0.0227 168 THR A CA  
1347 C C   . THR A 168 ? 0.3068 0.2151 0.2257 -0.0221 -0.0127 -0.0219 168 THR A C   
1348 O O   . THR A 168 ? 0.2865 0.1902 0.2025 -0.0253 -0.0157 -0.0208 168 THR A O   
1349 C CB  . THR A 168 ? 0.3241 0.2257 0.2436 -0.0130 -0.0097 -0.0277 168 THR A CB  
1350 O OG1 . THR A 168 ? 0.3526 0.2429 0.2651 -0.0135 -0.0124 -0.0289 168 THR A OG1 
1351 C CG2 . THR A 168 ? 0.3488 0.2517 0.2751 -0.0070 -0.0092 -0.0297 168 THR A CG2 
1352 N N   . LYS A 169 ? 0.3142 0.2295 0.2332 -0.0231 -0.0090 -0.0227 169 LYS A N   
1353 C CA  . LYS A 169 ? 0.3099 0.2271 0.2253 -0.0273 -0.0091 -0.0221 169 LYS A CA  
1354 C C   . LYS A 169 ? 0.3097 0.2179 0.2179 -0.0285 -0.0112 -0.0242 169 LYS A C   
1355 O O   . LYS A 169 ? 0.3116 0.2127 0.2141 -0.0263 -0.0101 -0.0271 169 LYS A O   
1356 C CB  . LYS A 169 ? 0.2976 0.2203 0.2118 -0.0279 -0.0050 -0.0232 169 LYS A CB  
1357 C CG  . LYS A 169 ? 0.2867 0.2102 0.1973 -0.0318 -0.0062 -0.0228 169 LYS A CG  
1358 C CD  . LYS A 169 ? 0.3026 0.2303 0.2112 -0.0332 -0.0026 -0.0233 169 LYS A CD  
1359 C CE  . LYS A 169 ? 0.3367 0.2633 0.2410 -0.0365 -0.0050 -0.0232 169 LYS A CE  
1360 N NZ  . LYS A 169 ? 0.3956 0.3255 0.2977 -0.0386 -0.0023 -0.0230 169 LYS A NZ  
1361 N N   . GLY A 170 ? 0.3036 0.2130 0.2124 -0.0321 -0.0140 -0.0231 170 GLY A N   
1362 C CA  . GLY A 170 ? 0.3114 0.2141 0.2154 -0.0335 -0.0167 -0.0254 170 GLY A CA  
1363 C C   . GLY A 170 ? 0.3161 0.2129 0.2209 -0.0340 -0.0199 -0.0252 170 GLY A C   
1364 O O   . GLY A 170 ? 0.3456 0.2388 0.2488 -0.0360 -0.0227 -0.0269 170 GLY A O   
1365 N N   . LYS A 171 ? 0.2964 0.1917 0.2038 -0.0324 -0.0200 -0.0233 171 LYS A N   
1366 C CA  . LYS A 171 ? 0.3026 0.1907 0.2097 -0.0334 -0.0233 -0.0228 171 LYS A CA  
1367 C C   . LYS A 171 ? 0.3038 0.1970 0.2147 -0.0388 -0.0250 -0.0203 171 LYS A C   
1368 O O   . LYS A 171 ? 0.3062 0.2077 0.2205 -0.0404 -0.0236 -0.0180 171 LYS A O   
1369 C CB  . LYS A 171 ? 0.3307 0.2139 0.2388 -0.0299 -0.0239 -0.0216 171 LYS A CB  
1370 C CG  . LYS A 171 ? 0.3446 0.2227 0.2493 -0.0245 -0.0218 -0.0251 171 LYS A CG  
1371 C CD  . LYS A 171 ? 0.4265 0.2974 0.3323 -0.0207 -0.0239 -0.0251 171 LYS A CD  
1372 C CE  . LYS A 171 ? 0.4461 0.3057 0.3481 -0.0224 -0.0283 -0.0254 171 LYS A CE  
1373 N NZ  . LYS A 171 ? 0.5102 0.3605 0.4123 -0.0182 -0.0310 -0.0257 171 LYS A NZ  
1374 N N   . SER A 172 ? 0.3173 0.2057 0.2276 -0.0419 -0.0277 -0.0212 172 SER A N   
1375 C CA  A SER A 172 ? 0.2908 0.1843 0.2047 -0.0478 -0.0285 -0.0195 172 SER A CA  
1376 C CA  B SER A 172 ? 0.2882 0.1817 0.2021 -0.0478 -0.0286 -0.0199 172 SER A CA  
1377 C C   . SER A 172 ? 0.3470 0.2322 0.2597 -0.0506 -0.0315 -0.0187 172 SER A C   
1378 O O   . SER A 172 ? 0.4169 0.2920 0.3261 -0.0477 -0.0334 -0.0202 172 SER A O   
1379 C CB  A SER A 172 ? 0.3084 0.2088 0.2249 -0.0502 -0.0284 -0.0227 172 SER A CB  
1380 C CB  B SER A 172 ? 0.3093 0.2081 0.2253 -0.0498 -0.0289 -0.0236 172 SER A CB  
1381 O OG  A SER A 172 ? 0.3236 0.2172 0.2380 -0.0492 -0.0309 -0.0263 172 SER A OG  
1382 O OG  B SER A 172 ? 0.2815 0.1873 0.2024 -0.0556 -0.0290 -0.0234 172 SER A OG  
1383 N N   . ALA A 173 ? 0.3132 0.2019 0.2281 -0.0566 -0.0316 -0.0162 173 ALA A N   
1384 C CA  . ALA A 173 ? 0.3211 0.2019 0.2346 -0.0609 -0.0343 -0.0150 173 ALA A CA  
1385 C C   . ALA A 173 ? 0.2850 0.1740 0.2023 -0.0689 -0.0331 -0.0149 173 ALA A C   
1386 O O   . ALA A 173 ? 0.3048 0.2038 0.2244 -0.0710 -0.0304 -0.0140 173 ALA A O   
1387 C CB  . ALA A 173 ? 0.3569 0.2291 0.2664 -0.0601 -0.0361 -0.0103 173 ALA A CB  
1388 N N   . ASP A 174 ? 0.3083 0.1930 0.2264 -0.0737 -0.0350 -0.0161 174 ASP A N   
1389 C CA  . ASP A 174 ? 0.3107 0.2033 0.2326 -0.0823 -0.0332 -0.0158 174 ASP A CA  
1390 C C   . ASP A 174 ? 0.3372 0.2294 0.2546 -0.0865 -0.0318 -0.0100 174 ASP A C   
1391 O O   . ASP A 174 ? 0.3394 0.2206 0.2506 -0.0845 -0.0343 -0.0058 174 ASP A O   
1392 C CB  . ASP A 174 ? 0.3261 0.2127 0.2489 -0.0877 -0.0357 -0.0171 174 ASP A CB  
1393 C CG  . ASP A 174 ? 0.3826 0.2676 0.3090 -0.0842 -0.0384 -0.0228 174 ASP A CG  
1394 O OD1 . ASP A 174 ? 0.3724 0.2647 0.3024 -0.0801 -0.0377 -0.0264 174 ASP A OD1 
1395 O OD2 . ASP A 174 ? 0.4606 0.3365 0.3858 -0.0863 -0.0416 -0.0234 174 ASP A OD2 
1396 N N   . PHE A 175 ? 0.2978 0.2014 0.2179 -0.0923 -0.0282 -0.0100 175 PHE A N   
1397 C CA  . PHE A 175 ? 0.3003 0.2035 0.2145 -0.0965 -0.0269 -0.0045 175 PHE A CA  
1398 C C   . PHE A 175 ? 0.2856 0.1991 0.2025 -0.1062 -0.0229 -0.0058 175 PHE A C   
1399 O O   . PHE A 175 ? 0.3163 0.2428 0.2372 -0.1068 -0.0192 -0.0083 175 PHE A O   
1400 C CB  . PHE A 175 ? 0.3019 0.2093 0.2152 -0.0905 -0.0260 -0.0032 175 PHE A CB  
1401 C CG  . PHE A 175 ? 0.3189 0.2220 0.2248 -0.0932 -0.0267 0.0030  175 PHE A CG  
1402 C CD1 . PHE A 175 ? 0.3584 0.2474 0.2582 -0.0906 -0.0312 0.0073  175 PHE A CD1 
1403 C CD2 . PHE A 175 ? 0.3076 0.2198 0.2120 -0.0982 -0.0235 0.0041  175 PHE A CD2 
1404 C CE1 . PHE A 175 ? 0.3872 0.2707 0.2796 -0.0925 -0.0332 0.0132  175 PHE A CE1 
1405 C CE2 . PHE A 175 ? 0.3225 0.2289 0.2183 -0.1007 -0.0250 0.0102  175 PHE A CE2 
1406 C CZ  . PHE A 175 ? 0.3638 0.2560 0.2539 -0.0979 -0.0301 0.0147  175 PHE A CZ  
1407 N N   . THR A 176 ? 0.3013 0.2091 0.2157 -0.1139 -0.0234 -0.0041 176 THR A N   
1408 C CA  . THR A 176 ? 0.3032 0.2215 0.2220 -0.1237 -0.0191 -0.0067 176 THR A CA  
1409 C C   . THR A 176 ? 0.3617 0.2760 0.2707 -0.1333 -0.0172 -0.0007 176 THR A C   
1410 O O   . THR A 176 ? 0.3769 0.2771 0.2754 -0.1328 -0.0208 0.0057  176 THR A O   
1411 C CB  . THR A 176 ? 0.3120 0.2289 0.2371 -0.1267 -0.0207 -0.0106 176 THR A CB  
1412 O OG1 . THR A 176 ? 0.3541 0.2536 0.2714 -0.1276 -0.0252 -0.0060 176 THR A OG1 
1413 C CG2 . THR A 176 ? 0.3372 0.2580 0.2708 -0.1176 -0.0229 -0.0168 176 THR A CG2 
1414 N N   . ASN A 177 ? 0.3583 0.2855 0.2704 -0.1418 -0.0115 -0.0033 177 ASN A N   
1415 C CA  . ASN A 177 ? 0.3859 0.3103 0.2879 -0.1530 -0.0086 0.0018  177 ASN A CA  
1416 C C   . ASN A 177 ? 0.4059 0.3237 0.2959 -0.1510 -0.0099 0.0081  177 ASN A C   
1417 O O   . ASN A 177 ? 0.4555 0.3626 0.3327 -0.1584 -0.0108 0.0146  177 ASN A O   
1418 C CB  . ASN A 177 ? 0.4326 0.3425 0.3286 -0.1601 -0.0116 0.0056  177 ASN A CB  
1419 C CG  . ASN A 177 ? 0.4531 0.3691 0.3617 -0.1620 -0.0113 -0.0008 177 ASN A CG  
1420 O OD1 . ASN A 177 ? 0.4787 0.3833 0.3882 -0.1584 -0.0166 -0.0007 177 ASN A OD1 
1421 N ND2 . ASN A 177 ? 0.4146 0.3485 0.3331 -0.1676 -0.0052 -0.0070 177 ASN A ND2 
1422 N N   . PHE A 178 ? 0.3653 0.2891 0.2588 -0.1418 -0.0103 0.0064  178 PHE A N   
1423 C CA  . PHE A 178 ? 0.3505 0.2694 0.2342 -0.1397 -0.0119 0.0117  178 PHE A CA  
1424 C C   . PHE A 178 ? 0.3875 0.3189 0.2688 -0.1464 -0.0058 0.0105  178 PHE A C   
1425 O O   . PHE A 178 ? 0.3874 0.3344 0.2787 -0.1453 -0.0013 0.0037  178 PHE A O   
1426 C CB  . PHE A 178 ? 0.3505 0.2697 0.2388 -0.1271 -0.0151 0.0107  178 PHE A CB  
1427 C CG  . PHE A 178 ? 0.3478 0.2622 0.2273 -0.1249 -0.0175 0.0160  178 PHE A CG  
1428 C CD1 . PHE A 178 ? 0.4077 0.3057 0.2770 -0.1253 -0.0231 0.0229  178 PHE A CD1 
1429 C CD2 . PHE A 178 ? 0.3256 0.2511 0.2067 -0.1232 -0.0147 0.0141  178 PHE A CD2 
1430 C CE1 . PHE A 178 ? 0.4147 0.3083 0.2761 -0.1234 -0.0261 0.0277  178 PHE A CE1 
1431 C CE2 . PHE A 178 ? 0.3534 0.2747 0.2266 -0.1217 -0.0173 0.0189  178 PHE A CE2 
1432 C CZ  . PHE A 178 ? 0.3571 0.2627 0.2208 -0.1217 -0.0232 0.0256  178 PHE A CZ  
1433 N N   . ASP A 179 ? 0.3999 0.3233 0.2671 -0.1530 -0.0062 0.0169  179 ASP A N   
1434 C CA  . ASP A 179 ? 0.3820 0.3149 0.2436 -0.1603 -0.0006 0.0164  179 ASP A CA  
1435 C C   . ASP A 179 ? 0.3925 0.3265 0.2507 -0.1532 -0.0028 0.0180  179 ASP A C   
1436 O O   . ASP A 179 ? 0.3959 0.3166 0.2425 -0.1525 -0.0081 0.0249  179 ASP A O   
1437 C CB  . ASP A 179 ? 0.3766 0.2981 0.2221 -0.1727 -0.0001 0.0229  179 ASP A CB  
1438 C CG  . ASP A 179 ? 0.4301 0.3597 0.2671 -0.1816 0.0061  0.0227  179 ASP A CG  
1439 O OD1 . ASP A 179 ? 0.4015 0.3469 0.2466 -0.1778 0.0102  0.0166  179 ASP A OD1 
1440 O OD2 . ASP A 179 ? 0.5129 0.4321 0.3341 -0.1925 0.0064  0.0287  179 ASP A OD2 
1441 N N   . PRO A 180 ? 0.3500 0.2988 0.2178 -0.1481 0.0004  0.0117  180 PRO A N   
1442 C CA  . PRO A 180 ? 0.3633 0.3125 0.2277 -0.1419 -0.0021 0.0135  180 PRO A CA  
1443 C C   . PRO A 180 ? 0.3643 0.3116 0.2142 -0.1498 -0.0005 0.0175  180 PRO A C   
1444 O O   . PRO A 180 ? 0.3694 0.3136 0.2142 -0.1455 -0.0041 0.0205  180 PRO A O   
1445 C CB  . PRO A 180 ? 0.3386 0.3036 0.2167 -0.1358 0.0011  0.0054  180 PRO A CB  
1446 C CG  . PRO A 180 ? 0.3693 0.3450 0.2545 -0.1426 0.0073  -0.0008 180 PRO A CG  
1447 C CD  . PRO A 180 ? 0.3591 0.3240 0.2413 -0.1474 0.0055  0.0028  180 PRO A CD  
1448 N N   . ARG A 181 ? 0.3800 0.3282 0.2224 -0.1616 0.0045  0.0180  181 ARG A N   
1449 C CA  . ARG A 181 ? 0.4078 0.3514 0.2332 -0.1697 0.0055  0.0226  181 ARG A CA  
1450 C C   . ARG A 181 ? 0.3902 0.3138 0.2019 -0.1684 -0.0032 0.0321  181 ARG A C   
1451 O O   . ARG A 181 ? 0.4201 0.3382 0.2182 -0.1712 -0.0053 0.0364  181 ARG A O   
1452 C CB  . ARG A 181 ? 0.4515 0.3992 0.2706 -0.1835 0.0130  0.0214  181 ARG A CB  
1453 C CG  . ARG A 181 ? 0.4311 0.4001 0.2640 -0.1850 0.0216  0.0112  181 ARG A CG  
1454 C CD  . ARG A 181 ? 0.4382 0.4119 0.2677 -0.1986 0.0291  0.0095  181 ARG A CD  
1455 N NE  . ARG A 181 ? 0.4880 0.4505 0.3183 -0.2010 0.0258  0.0133  181 ARG A NE  
1456 C CZ  . ARG A 181 ? 0.5504 0.5121 0.3767 -0.2099 0.0293  0.0133  181 ARG A CZ  
1457 N NH1 . ARG A 181 ? 0.6137 0.5860 0.4356 -0.2169 0.0365  0.0092  181 ARG A NH1 
1458 N NH2 . ARG A 181 ? 0.5567 0.5074 0.3837 -0.2106 0.0253  0.0166  181 ARG A NH2 
1459 N N   . GLY A 182 ? 0.4331 0.3451 0.2475 -0.1644 -0.0087 0.0351  182 GLY A N   
1460 C CA  . GLY A 182 ? 0.4385 0.3314 0.2414 -0.1621 -0.0177 0.0434  182 GLY A CA  
1461 C C   . GLY A 182 ? 0.4298 0.3226 0.2364 -0.1509 -0.0236 0.0441  182 GLY A C   
1462 O O   . GLY A 182 ? 0.4607 0.3387 0.2583 -0.1485 -0.0317 0.0505  182 GLY A O   
1463 N N   . LEU A 183 ? 0.4141 0.3227 0.2337 -0.1443 -0.0200 0.0377  183 LEU A N   
1464 C CA  . LEU A 183 ? 0.3651 0.2758 0.1892 -0.1346 -0.0245 0.0377  183 LEU A CA  
1465 C C   . LEU A 183 ? 0.3848 0.3030 0.2025 -0.1377 -0.0222 0.0370  183 LEU A C   
1466 O O   . LEU A 183 ? 0.3880 0.3101 0.2104 -0.1305 -0.0252 0.0362  183 LEU A O   
1467 C CB  . LEU A 183 ? 0.3490 0.2701 0.1910 -0.1249 -0.0230 0.0315  183 LEU A CB  
1468 C CG  . LEU A 183 ? 0.3622 0.2756 0.2105 -0.1206 -0.0256 0.0316  183 LEU A CG  
1469 C CD1 . LEU A 183 ? 0.3505 0.2742 0.2141 -0.1122 -0.0235 0.0253  183 LEU A CD1 
1470 C CD2 . LEU A 183 ? 0.3931 0.2906 0.2357 -0.1164 -0.0342 0.0379  183 LEU A CD2 
1471 N N   . LEU A 184 ? 0.3997 0.3199 0.2065 -0.1486 -0.0169 0.0371  184 LEU A N   
1472 C CA  . LEU A 184 ? 0.4060 0.3330 0.2049 -0.1526 -0.0140 0.0358  184 LEU A CA  
1473 C C   . LEU A 184 ? 0.4131 0.3248 0.1919 -0.1583 -0.0197 0.0439  184 LEU A C   
1474 O O   . LEU A 184 ? 0.4552 0.3533 0.2223 -0.1651 -0.0217 0.0495  184 LEU A O   
1475 C CB  . LEU A 184 ? 0.4184 0.3584 0.2176 -0.1614 -0.0039 0.0298  184 LEU A CB  
1476 C CG  . LEU A 184 ? 0.4410 0.3961 0.2595 -0.1570 0.0017  0.0212  184 LEU A CG  
1477 C CD1 . LEU A 184 ? 0.4390 0.4064 0.2569 -0.1667 0.0113  0.0154  184 LEU A CD1 
1478 C CD2 . LEU A 184 ? 0.4237 0.3877 0.2536 -0.1466 0.0000  0.0169  184 LEU A CD2 
1479 N N   . PRO A 185 ? 0.4177 0.3306 0.1909 -0.1563 -0.0225 0.0447  185 PRO A N   
1480 C CA  . PRO A 185 ? 0.4522 0.3510 0.2041 -0.1629 -0.0277 0.0518  185 PRO A CA  
1481 C C   . PRO A 185 ? 0.4721 0.3733 0.2090 -0.1764 -0.0196 0.0510  185 PRO A C   
1482 O O   . PRO A 185 ? 0.4869 0.4032 0.2318 -0.1797 -0.0098 0.0439  185 PRO A O   
1483 C CB  . PRO A 185 ? 0.4267 0.3294 0.1805 -0.1559 -0.0325 0.0511  185 PRO A CB  
1484 C CG  . PRO A 185 ? 0.4176 0.3405 0.1878 -0.1518 -0.0246 0.0419  185 PRO A CG  
1485 C CD  . PRO A 185 ? 0.3935 0.3212 0.1789 -0.1491 -0.0206 0.0384  185 PRO A CD  
1486 N N   . GLU A 186 ? 0.4834 0.3717 0.2045 -0.1815 -0.0241 0.0558  186 GLU A N   
1487 C CA  . GLU A 186 ? 0.5441 0.4361 0.2567 -0.1918 -0.0168 0.0527  186 GLU A CA  
1488 C C   . GLU A 186 ? 0.5411 0.4488 0.2561 -0.1923 -0.0102 0.0458  186 GLU A C   
1489 O O   . GLU A 186 ? 0.5430 0.4626 0.2598 -0.1987 -0.0005 0.0395  186 GLU A O   
1490 C CB  . GLU A 186 ? 0.6309 0.5039 0.3257 -0.1969 -0.0240 0.0594  186 GLU A CB  
1491 C CG  . GLU A 186 ? 0.7820 0.6570 0.4655 -0.2084 -0.0168 0.0568  186 GLU A CG  
1492 C CD  . GLU A 186 ? 0.9209 0.7751 0.5858 -0.2147 -0.0238 0.0638  186 GLU A CD  
1493 O OE1 . GLU A 186 ? 0.9740 0.8282 0.6295 -0.2251 -0.0178 0.0622  186 GLU A OE1 
1494 O OE2 . GLU A 186 ? 0.9601 0.7982 0.6199 -0.2094 -0.0353 0.0705  186 GLU A OE2 
1495 N N   . SER A 187 ? 0.4813 0.3890 0.1962 -0.1855 -0.0157 0.0466  187 SER A N   
1496 C CA  . SER A 187 ? 0.4966 0.4179 0.2136 -0.1852 -0.0106 0.0401  187 SER A CA  
1497 C C   . SER A 187 ? 0.4769 0.4144 0.2105 -0.1784 -0.0063 0.0336  187 SER A C   
1498 O O   . SER A 187 ? 0.4446 0.3800 0.1855 -0.1707 -0.0118 0.0360  187 SER A O   
1499 C CB  . SER A 187 ? 0.4962 0.4095 0.2052 -0.1814 -0.0191 0.0437  187 SER A CB  
1500 O OG  . SER A 187 ? 0.5200 0.4463 0.2318 -0.1806 -0.0142 0.0370  187 SER A OG  
1501 N N   . LEU A 188 ? 0.4819 0.4352 0.2210 -0.1810 0.0029  0.0250  188 LEU A N   
1502 C CA  . LEU A 188 ? 0.4505 0.4189 0.2045 -0.1744 0.0065  0.0179  188 LEU A CA  
1503 C C   . LEU A 188 ? 0.4452 0.4199 0.1999 -0.1699 0.0051  0.0138  188 LEU A C   
1504 O O   . LEU A 188 ? 0.4671 0.4552 0.2352 -0.1648 0.0087  0.0060  188 LEU A O   
1505 C CB  . LEU A 188 ? 0.4597 0.4426 0.2237 -0.1787 0.0172  0.0098  188 LEU A CB  
1506 C CG  . LEU A 188 ? 0.4833 0.4622 0.2513 -0.1822 0.0189  0.0123  188 LEU A CG  
1507 C CD1 . LEU A 188 ? 0.4953 0.4910 0.2761 -0.1855 0.0290  0.0029  188 LEU A CD1 
1508 C CD2 . LEU A 188 ? 0.4414 0.4138 0.2220 -0.1718 0.0110  0.0159  188 LEU A CD2 
1509 N N   . ASP A 189 ? 0.4167 0.3810 0.1599 -0.1704 -0.0012 0.0188  189 ASP A N   
1510 C CA  . ASP A 189 ? 0.4259 0.3936 0.1703 -0.1650 -0.0048 0.0164  189 ASP A CA  
1511 C C   . ASP A 189 ? 0.3968 0.3692 0.1542 -0.1555 -0.0093 0.0152  189 ASP A C   
1512 O O   . ASP A 189 ? 0.3859 0.3521 0.1511 -0.1505 -0.0143 0.0198  189 ASP A O   
1513 C CB  . ASP A 189 ? 0.4397 0.3928 0.1706 -0.1658 -0.0134 0.0239  189 ASP A CB  
1514 C CG  . ASP A 189 ? 0.5056 0.4543 0.2220 -0.1750 -0.0094 0.0240  189 ASP A CG  
1515 O OD1 . ASP A 189 ? 0.5499 0.5081 0.2674 -0.1808 0.0004  0.0180  189 ASP A OD1 
1516 O OD2 . ASP A 189 ? 0.5430 0.4784 0.2466 -0.1766 -0.0164 0.0300  189 ASP A OD2 
1517 N N   . TYR A 190 ? 0.3423 0.3157 0.1522 -0.1312 -0.0033 0.0303  190 TYR A N   
1518 C CA  . TYR A 190 ? 0.3231 0.3030 0.1544 -0.1193 -0.0059 0.0262  190 TYR A CA  
1519 C C   . TYR A 190 ? 0.3403 0.3264 0.1737 -0.1146 -0.0059 0.0207  190 TYR A C   
1520 O O   . TYR A 190 ? 0.3589 0.3468 0.1793 -0.1201 -0.0023 0.0182  190 TYR A O   
1521 C CB  . TYR A 190 ? 0.3112 0.3025 0.1601 -0.1166 0.0020  0.0205  190 TYR A CB  
1522 C CG  . TYR A 190 ? 0.3265 0.3314 0.1765 -0.1202 0.0133  0.0125  190 TYR A CG  
1523 C CD1 . TYR A 190 ? 0.3397 0.3540 0.1988 -0.1137 0.0162  0.0050  190 TYR A CD1 
1524 C CD2 . TYR A 190 ? 0.3265 0.3348 0.1686 -0.1303 0.0213  0.0120  190 TYR A CD2 
1525 C CE1 . TYR A 190 ? 0.3526 0.3790 0.2133 -0.1161 0.0264  -0.0031 190 TYR A CE1 
1526 C CE2 . TYR A 190 ? 0.3463 0.3686 0.1908 -0.1330 0.0322  0.0036  190 TYR A CE2 
1527 C CZ  . TYR A 190 ? 0.3359 0.3671 0.1902 -0.1254 0.0345  -0.0042 190 TYR A CZ  
1528 O OH  . TYR A 190 ? 0.3652 0.4095 0.2214 -0.1277 0.0450  -0.0131 190 TYR A OH  
1529 N N   . TRP A 191 ? 0.3328 0.3213 0.1821 -0.1048 -0.0104 0.0190  191 TRP A N   
1530 C CA  . TRP A 191 ? 0.3107 0.3067 0.1676 -0.0993 -0.0092 0.0127  191 TRP A CA  
1531 C C   . TRP A 191 ? 0.3050 0.3117 0.1800 -0.0934 -0.0023 0.0062  191 TRP A C   
1532 O O   . TRP A 191 ? 0.2865 0.2936 0.1717 -0.0904 -0.0023 0.0076  191 TRP A O   
1533 C CB  . TRP A 191 ? 0.3269 0.3177 0.1883 -0.0930 -0.0194 0.0157  191 TRP A CB  
1534 C CG  . TRP A 191 ? 0.3252 0.3056 0.1706 -0.0973 -0.0281 0.0220  191 TRP A CG  
1535 C CD1 . TRP A 191 ? 0.3439 0.3225 0.1745 -0.1020 -0.0295 0.0212  191 TRP A CD1 
1536 C CD2 . TRP A 191 ? 0.3392 0.3084 0.1814 -0.0964 -0.0378 0.0299  191 TRP A CD2 
1537 N NE1 . TRP A 191 ? 0.4086 0.3759 0.2262 -0.1046 -0.0398 0.0286  191 TRP A NE1 
1538 C CE2 . TRP A 191 ? 0.3785 0.3398 0.2038 -0.1006 -0.0453 0.0340  191 TRP A CE2 
1539 C CE3 . TRP A 191 ? 0.3786 0.3434 0.2307 -0.0920 -0.0414 0.0336  191 TRP A CE3 
1540 C CZ2 . TRP A 191 ? 0.3793 0.3277 0.1969 -0.1006 -0.0567 0.0422  191 TRP A CZ2 
1541 C CZ3 . TRP A 191 ? 0.3842 0.3364 0.2295 -0.0918 -0.0521 0.0411  191 TRP A CZ3 
1542 C CH2 . TRP A 191 ? 0.3929 0.3370 0.2216 -0.0958 -0.0598 0.0455  191 TRP A CH2 
1543 N N   . THR A 192 ? 0.2894 0.3040 0.1684 -0.0913 0.0029  -0.0010 192 THR A N   
1544 C CA  . THR A 192 ? 0.2589 0.2824 0.1543 -0.0852 0.0084  -0.0069 192 THR A CA  
1545 C C   . THR A 192 ? 0.2690 0.2950 0.1711 -0.0794 0.0079  -0.0117 192 THR A C   
1546 O O   . THR A 192 ? 0.3102 0.3346 0.2032 -0.0819 0.0072  -0.0136 192 THR A O   
1547 C CB  . THR A 192 ? 0.2596 0.2917 0.1551 -0.0894 0.0181  -0.0121 192 THR A CB  
1548 O OG1 . THR A 192 ? 0.2631 0.3033 0.1757 -0.0825 0.0218  -0.0173 192 THR A OG1 
1549 C CG2 . THR A 192 ? 0.2960 0.3310 0.1801 -0.0944 0.0232  -0.0171 192 THR A CG2 
1550 N N   . TYR A 193 ? 0.2550 0.2843 0.1721 -0.0720 0.0083  -0.0137 193 TYR A N   
1551 C CA  . TYR A 193 ? 0.2573 0.2882 0.1813 -0.0667 0.0084  -0.0181 193 TYR A CA  
1552 C C   . TYR A 193 ? 0.2394 0.2747 0.1779 -0.0600 0.0112  -0.0208 193 TYR A C   
1553 O O   . TYR A 193 ? 0.2427 0.2787 0.1863 -0.0586 0.0109  -0.0182 193 TYR A O   
1554 C CB  . TYR A 193 ? 0.2523 0.2775 0.1760 -0.0650 0.0006  -0.0143 193 TYR A CB  
1555 C CG  . TYR A 193 ? 0.2404 0.2639 0.1743 -0.0599 -0.0035 -0.0099 193 TYR A CG  
1556 C CD1 . TYR A 193 ? 0.2503 0.2697 0.1808 -0.0617 -0.0076 -0.0042 193 TYR A CD1 
1557 C CD2 . TYR A 193 ? 0.2165 0.2418 0.1622 -0.0536 -0.0034 -0.0117 193 TYR A CD2 
1558 C CE1 . TYR A 193 ? 0.2503 0.2679 0.1899 -0.0567 -0.0111 -0.0011 193 TYR A CE1 
1559 C CE2 . TYR A 193 ? 0.2113 0.2355 0.1656 -0.0490 -0.0064 -0.0084 193 TYR A CE2 
1560 C CZ  . TYR A 193 ? 0.2165 0.2371 0.1678 -0.0505 -0.0103 -0.0034 193 TYR A CZ  
1561 O OH  . TYR A 193 ? 0.2217 0.2412 0.1814 -0.0457 -0.0129 -0.0011 193 TYR A OH  
1562 N N   . PRO A 194 ? 0.2181 0.2554 0.1625 -0.0558 0.0137  -0.0260 194 PRO A N   
1563 C CA  . PRO A 194 ? 0.2324 0.2723 0.1892 -0.0490 0.0153  -0.0280 194 PRO A CA  
1564 C C   . PRO A 194 ? 0.2163 0.2518 0.1787 -0.0447 0.0104  -0.0238 194 PRO A C   
1565 O O   . PRO A 194 ? 0.2199 0.2519 0.1809 -0.0447 0.0075  -0.0232 194 PRO A O   
1566 C CB  . PRO A 194 ? 0.2241 0.2654 0.1826 -0.0467 0.0191  -0.0349 194 PRO A CB  
1567 C CG  . PRO A 194 ? 0.2832 0.3209 0.2317 -0.0513 0.0175  -0.0354 194 PRO A CG  
1568 C CD  . PRO A 194 ? 0.2392 0.2759 0.1776 -0.0576 0.0153  -0.0308 194 PRO A CD  
1569 N N   . GLY A 195 ? 0.1973 0.2334 0.1663 -0.0412 0.0096  -0.0217 195 GLY A N   
1570 C CA  . GLY A 195 ? 0.1799 0.2127 0.1541 -0.0372 0.0058  -0.0182 195 GLY A CA  
1571 C C   . GLY A 195 ? 0.1760 0.2098 0.1578 -0.0319 0.0068  -0.0185 195 GLY A C   
1572 O O   . GLY A 195 ? 0.1989 0.2354 0.1839 -0.0295 0.0100  -0.0224 195 GLY A O   
1573 N N   . SER A 196 ? 0.1792 0.2108 0.1636 -0.0299 0.0037  -0.0148 196 SER A N   
1574 C CA  . SER A 196 ? 0.1806 0.2120 0.1708 -0.0247 0.0041  -0.0149 196 SER A CA  
1575 C C   . SER A 196 ? 0.1848 0.2153 0.1760 -0.0243 0.0017  -0.0122 196 SER A C   
1576 O O   . SER A 196 ? 0.1901 0.2189 0.1780 -0.0277 -0.0008 -0.0095 196 SER A O   
1577 C CB  . SER A 196 ? 0.1826 0.2111 0.1755 -0.0217 0.0034  -0.0141 196 SER A CB  
1578 O OG  . SER A 196 ? 0.1989 0.2262 0.1925 -0.0224 0.0002  -0.0108 196 SER A OG  
1579 N N   . LEU A 197 ? 0.1777 0.2083 0.1728 -0.0200 0.0019  -0.0128 197 LEU A N   
1580 C CA  . LEU A 197 ? 0.1658 0.1940 0.1620 -0.0187 -0.0007 -0.0106 197 LEU A CA  
1581 C C   . LEU A 197 ? 0.1773 0.2027 0.1740 -0.0180 -0.0030 -0.0081 197 LEU A C   
1582 O O   . LEU A 197 ? 0.1788 0.2045 0.1769 -0.0168 -0.0019 -0.0084 197 LEU A O   
1583 C CB  . LEU A 197 ? 0.1707 0.1988 0.1697 -0.0139 -0.0002 -0.0120 197 LEU A CB  
1584 C CG  . LEU A 197 ? 0.1677 0.1997 0.1685 -0.0134 0.0012  -0.0150 197 LEU A CG  
1585 C CD1 . LEU A 197 ? 0.1760 0.2064 0.1780 -0.0081 0.0004  -0.0158 197 LEU A CD1 
1586 C CD2 . LEU A 197 ? 0.1855 0.2199 0.1864 -0.0175 0.0004  -0.0151 197 LEU A CD2 
1587 N N   . THR A 198 ? 0.1746 0.1974 0.1711 -0.0185 -0.0062 -0.0058 198 THR A N   
1588 C CA  . THR A 198 ? 0.1709 0.1923 0.1701 -0.0168 -0.0088 -0.0041 198 THR A CA  
1589 C C   . THR A 198 ? 0.1632 0.1840 0.1667 -0.0118 -0.0083 -0.0049 198 THR A C   
1590 O O   . THR A 198 ? 0.1735 0.1944 0.1810 -0.0099 -0.0099 -0.0042 198 THR A O   
1591 C CB  . THR A 198 ? 0.1779 0.1957 0.1748 -0.0193 -0.0136 -0.0011 198 THR A CB  
1592 O OG1 . THR A 198 ? 0.1746 0.1887 0.1709 -0.0186 -0.0150 -0.0007 198 THR A OG1 
1593 C CG2 . THR A 198 ? 0.1905 0.2081 0.1807 -0.0250 -0.0139 -0.0001 198 THR A CG2 
1594 N N   . THR A 199 ? 0.1773 0.1982 0.1802 -0.0097 -0.0060 -0.0067 199 THR A N   
1595 C CA  . THR A 199 ? 0.1548 0.1750 0.1596 -0.0053 -0.0047 -0.0078 199 THR A CA  
1596 C C   . THR A 199 ? 0.1636 0.1848 0.1666 -0.0040 -0.0013 -0.0091 199 THR A C   
1597 O O   . THR A 199 ? 0.1716 0.1939 0.1731 -0.0056 -0.0006 -0.0097 199 THR A O   
1598 C CB  . THR A 199 ? 0.1761 0.1935 0.1800 -0.0036 -0.0065 -0.0086 199 THR A CB  
1599 O OG1 . THR A 199 ? 0.1928 0.2110 0.1943 -0.0049 -0.0061 -0.0098 199 THR A OG1 
1600 C CG2 . THR A 199 ? 0.1876 0.2018 0.1921 -0.0052 -0.0105 -0.0071 199 THR A CG2 
1601 N N   . PRO A 200 ? 0.1744 0.1949 0.1774 -0.0010 0.0008  -0.0095 200 PRO A N   
1602 C CA  . PRO A 200 ? 0.1510 0.1699 0.1503 0.0007  0.0030  -0.0102 200 PRO A CA  
1603 C C   . PRO A 200 ? 0.1609 0.1795 0.1583 0.0013  0.0011  -0.0115 200 PRO A C   
1604 O O   . PRO A 200 ? 0.1740 0.1926 0.1719 0.0015  -0.0011 -0.0121 200 PRO A O   
1605 C CB  . PRO A 200 ? 0.1800 0.1974 0.1777 0.0036  0.0051  -0.0104 200 PRO A CB  
1606 C CG  . PRO A 200 ? 0.1914 0.2118 0.1950 0.0027  0.0055  -0.0100 200 PRO A CG  
1607 C CD  . PRO A 200 ? 0.1704 0.1912 0.1764 0.0012  0.0012  -0.0097 200 PRO A CD  
1608 N N   . PRO A 201 ? 0.1666 0.1852 0.1626 0.0018  0.0017  -0.0122 201 PRO A N   
1609 C CA  . PRO A 201 ? 0.1736 0.1901 0.1682 0.0020  0.0040  -0.0116 201 PRO A CA  
1610 C C   . PRO A 201 ? 0.1624 0.1807 0.1593 -0.0014 0.0048  -0.0117 201 PRO A C   
1611 O O   . PRO A 201 ? 0.1793 0.1951 0.1750 -0.0014 0.0063  -0.0118 201 PRO A O   
1612 C CB  . PRO A 201 ? 0.1705 0.1852 0.1628 0.0050  0.0030  -0.0129 201 PRO A CB  
1613 C CG  . PRO A 201 ? 0.1661 0.1856 0.1618 0.0043  0.0008  -0.0150 201 PRO A CG  
1614 C CD  . PRO A 201 ? 0.1717 0.1919 0.1681 0.0028  -0.0002 -0.0142 201 PRO A CD  
1615 N N   . LEU A 202 ? 0.1692 0.1907 0.1683 -0.0044 0.0036  -0.0115 202 LEU A N   
1616 C CA  . LEU A 202 ? 0.1561 0.1789 0.1559 -0.0080 0.0039  -0.0114 202 LEU A CA  
1617 C C   . LEU A 202 ? 0.1680 0.1911 0.1667 -0.0088 0.0052  -0.0137 202 LEU A C   
1618 O O   . LEU A 202 ? 0.1827 0.2052 0.1808 -0.0111 0.0060  -0.0143 202 LEU A O   
1619 C CB  . LEU A 202 ? 0.1771 0.1989 0.1784 -0.0086 0.0049  -0.0100 202 LEU A CB  
1620 C CG  . LEU A 202 ? 0.1688 0.1918 0.1730 -0.0076 0.0038  -0.0087 202 LEU A CG  
1621 C CD1 . LEU A 202 ? 0.1764 0.2003 0.1837 -0.0079 0.0058  -0.0081 202 LEU A CD1 
1622 C CD2 . LEU A 202 ? 0.1682 0.1930 0.1739 -0.0096 0.0003  -0.0078 202 LEU A CD2 
1623 N N   . LEU A 203 ? 0.1733 0.1978 0.1724 -0.0067 0.0051  -0.0156 203 LEU A N   
1624 C CA  . LEU A 203 ? 0.1757 0.2013 0.1754 -0.0063 0.0065  -0.0188 203 LEU A CA  
1625 C C   . LEU A 203 ? 0.1759 0.2051 0.1749 -0.0110 0.0075  -0.0203 203 LEU A C   
1626 O O   . LEU A 203 ? 0.1731 0.2051 0.1714 -0.0143 0.0067  -0.0192 203 LEU A O   
1627 C CB  . LEU A 203 ? 0.1809 0.2089 0.1830 -0.0029 0.0056  -0.0209 203 LEU A CB  
1628 C CG  . LEU A 203 ? 0.1854 0.2082 0.1857 0.0018  0.0042  -0.0194 203 LEU A CG  
1629 C CD1 . LEU A 203 ? 0.2101 0.2363 0.2132 0.0050  0.0019  -0.0216 203 LEU A CD1 
1630 C CD2 . LEU A 203 ? 0.2143 0.2307 0.2122 0.0038  0.0051  -0.0194 203 LEU A CD2 
1631 N N   . GLU A 204 ? 0.1869 0.2155 0.1854 -0.0114 0.0092  -0.0230 204 GLU A N   
1632 C CA  . GLU A 204 ? 0.1774 0.2086 0.1732 -0.0161 0.0105  -0.0248 204 GLU A CA  
1633 C C   . GLU A 204 ? 0.2007 0.2382 0.1985 -0.0166 0.0127  -0.0289 204 GLU A C   
1634 O O   . GLU A 204 ? 0.2187 0.2577 0.2169 -0.0163 0.0151  -0.0334 204 GLU A O   
1635 C CB  . GLU A 204 ? 0.2089 0.2357 0.2028 -0.0167 0.0112  -0.0262 204 GLU A CB  
1636 C CG  . GLU A 204 ? 0.1911 0.2141 0.1845 -0.0176 0.0093  -0.0221 204 GLU A CG  
1637 C CD  . GLU A 204 ? 0.2027 0.2213 0.1949 -0.0191 0.0097  -0.0232 204 GLU A CD  
1638 O OE1 . GLU A 204 ? 0.2285 0.2441 0.2202 -0.0176 0.0113  -0.0267 204 GLU A OE1 
1639 O OE2 . GLU A 204 ? 0.2109 0.2291 0.2034 -0.0215 0.0081  -0.0207 204 GLU A OE2 
1640 N N   . SER A 205 ? 0.1893 0.2305 0.1888 -0.0174 0.0120  -0.0276 205 SER A N   
1641 C CA  A SER A 205 ? 0.1860 0.2348 0.1895 -0.0180 0.0141  -0.0314 205 SER A CA  
1642 C CA  B SER A 205 ? 0.1848 0.2335 0.1883 -0.0180 0.0141  -0.0313 205 SER A CA  
1643 C C   . SER A 205 ? 0.1763 0.2288 0.1765 -0.0247 0.0152  -0.0301 205 SER A C   
1644 O O   . SER A 205 ? 0.2030 0.2624 0.2071 -0.0264 0.0171  -0.0326 205 SER A O   
1645 C CB  A SER A 205 ? 0.1957 0.2460 0.2051 -0.0132 0.0121  -0.0317 205 SER A CB  
1646 C CB  B SER A 205 ? 0.1917 0.2416 0.2009 -0.0131 0.0120  -0.0314 205 SER A CB  
1647 O OG  A SER A 205 ? 0.2055 0.2519 0.2127 -0.0136 0.0093  -0.0271 205 SER A OG  
1648 O OG  B SER A 205 ? 0.1874 0.2314 0.1969 -0.0075 0.0106  -0.0312 205 SER A OG  
1649 N N   . VAL A 206 ? 0.1919 0.2400 0.1851 -0.0290 0.0138  -0.0263 206 VAL A N   
1650 C CA  . VAL A 206 ? 0.1969 0.2457 0.1853 -0.0353 0.0136  -0.0237 206 VAL A CA  
1651 C C   . VAL A 206 ? 0.2103 0.2598 0.1908 -0.0412 0.0160  -0.0246 206 VAL A C   
1652 O O   . VAL A 206 ? 0.2226 0.2679 0.1986 -0.0412 0.0146  -0.0239 206 VAL A O   
1653 C CB  . VAL A 206 ? 0.1825 0.2245 0.1685 -0.0353 0.0088  -0.0180 206 VAL A CB  
1654 C CG1 . VAL A 206 ? 0.1969 0.2371 0.1763 -0.0423 0.0078  -0.0146 206 VAL A CG1 
1655 C CG2 . VAL A 206 ? 0.1808 0.2218 0.1731 -0.0299 0.0067  -0.0173 206 VAL A CG2 
1656 N N   . THR A 207 ? 0.2066 0.2610 0.1845 -0.0468 0.0194  -0.0260 207 THR A N   
1657 C CA  . THR A 207 ? 0.2202 0.2734 0.1869 -0.0541 0.0209  -0.0251 207 THR A CA  
1658 C C   . THR A 207 ? 0.2284 0.2748 0.1883 -0.0585 0.0166  -0.0182 207 THR A C   
1659 O O   . THR A 207 ? 0.2294 0.2769 0.1916 -0.0606 0.0167  -0.0166 207 THR A O   
1660 C CB  . THR A 207 ? 0.2108 0.2730 0.1774 -0.0586 0.0278  -0.0303 207 THR A CB  
1661 O OG1 . THR A 207 ? 0.2483 0.3161 0.2221 -0.0534 0.0312  -0.0372 207 THR A OG1 
1662 C CG2 . THR A 207 ? 0.2413 0.3012 0.1937 -0.0669 0.0296  -0.0289 207 THR A CG2 
1663 N N   . TRP A 208 ? 0.2247 0.2637 0.1777 -0.0590 0.0119  -0.0142 208 TRP A N   
1664 C CA  . TRP A 208 ? 0.2391 0.2702 0.1856 -0.0621 0.0064  -0.0075 208 TRP A CA  
1665 C C   . TRP A 208 ? 0.2562 0.2851 0.1893 -0.0711 0.0077  -0.0054 208 TRP A C   
1666 O O   . TRP A 208 ? 0.2589 0.2889 0.1841 -0.0742 0.0098  -0.0075 208 TRP A O   
1667 C CB  . TRP A 208 ? 0.2291 0.2543 0.1754 -0.0583 0.0002  -0.0045 208 TRP A CB  
1668 C CG  . TRP A 208 ? 0.2259 0.2512 0.1836 -0.0509 -0.0016 -0.0046 208 TRP A CG  
1669 C CD1 . TRP A 208 ? 0.2067 0.2353 0.1723 -0.0452 0.0000  -0.0080 208 TRP A CD1 
1670 C CD2 . TRP A 208 ? 0.2101 0.2315 0.1712 -0.0490 -0.0051 -0.0013 208 TRP A CD2 
1671 N NE1 . TRP A 208 ? 0.1985 0.2260 0.1717 -0.0400 -0.0018 -0.0069 208 TRP A NE1 
1672 C CE2 . TRP A 208 ? 0.1964 0.2197 0.1672 -0.0421 -0.0049 -0.0032 208 TRP A CE2 
1673 C CE3 . TRP A 208 ? 0.2264 0.2416 0.1823 -0.0527 -0.0085 0.0032  208 TRP A CE3 
1674 C CZ2 . TRP A 208 ? 0.2029 0.2233 0.1786 -0.0385 -0.0076 -0.0015 208 TRP A CZ2 
1675 C CZ3 . TRP A 208 ? 0.2332 0.2448 0.1951 -0.0487 -0.0116 0.0047  208 TRP A CZ3 
1676 C CH2 . TRP A 208 ? 0.2233 0.2379 0.1948 -0.0417 -0.0110 0.0021  208 TRP A CH2 
1677 N N   . ILE A 209 ? 0.2449 0.2693 0.1741 -0.0754 0.0061  -0.0009 209 ILE A N   
1678 C CA  . ILE A 209 ? 0.2496 0.2692 0.1642 -0.0847 0.0065  0.0027  209 ILE A CA  
1679 C C   . ILE A 209 ? 0.2724 0.2798 0.1823 -0.0847 -0.0019 0.0102  209 ILE A C   
1680 O O   . ILE A 209 ? 0.2788 0.2834 0.1943 -0.0837 -0.0035 0.0122  209 ILE A O   
1681 C CB  . ILE A 209 ? 0.2744 0.3007 0.1898 -0.0909 0.0137  0.0004  209 ILE A CB  
1682 C CG1 . ILE A 209 ? 0.2918 0.3313 0.2141 -0.0894 0.0217  -0.0081 209 ILE A CG1 
1683 C CG2 . ILE A 209 ? 0.2879 0.3075 0.1864 -0.1016 0.0141  0.0054  209 ILE A CG2 
1684 C CD1 . ILE A 209 ? 0.2842 0.3337 0.2130 -0.0936 0.0288  -0.0120 209 ILE A CD1 
1685 N N   . VAL A 210 ? 0.2733 0.2735 0.1743 -0.0850 -0.0079 0.0140  210 VAL A N   
1686 C CA  . VAL A 210 ? 0.2787 0.2673 0.1768 -0.0832 -0.0171 0.0206  210 VAL A CA  
1687 C C   . VAL A 210 ? 0.3186 0.2971 0.1984 -0.0922 -0.0199 0.0267  210 VAL A C   
1688 O O   . VAL A 210 ? 0.3079 0.2855 0.1754 -0.0965 -0.0200 0.0271  210 VAL A O   
1689 C CB  . VAL A 210 ? 0.2774 0.2655 0.1808 -0.0762 -0.0232 0.0205  210 VAL A CB  
1690 C CG1 . VAL A 210 ? 0.2883 0.2654 0.1905 -0.0736 -0.0331 0.0268  210 VAL A CG1 
1691 C CG2 . VAL A 210 ? 0.2502 0.2474 0.1701 -0.0683 -0.0197 0.0149  210 VAL A CG2 
1692 N N   . LEU A 211 ? 0.3149 0.2848 0.1915 -0.0955 -0.0222 0.0315  211 LEU A N   
1693 C CA  . LEU A 211 ? 0.3151 0.2737 0.1725 -0.1050 -0.0247 0.0381  211 LEU A CA  
1694 C C   . LEU A 211 ? 0.3353 0.2821 0.1836 -0.1028 -0.0357 0.0440  211 LEU A C   
1695 O O   . LEU A 211 ? 0.3565 0.3002 0.2150 -0.0943 -0.0431 0.0449  211 LEU A O   
1696 C CB  . LEU A 211 ? 0.3215 0.2725 0.1779 -0.1094 -0.0247 0.0418  211 LEU A CB  
1697 C CG  . LEU A 211 ? 0.3357 0.2985 0.2011 -0.1126 -0.0145 0.0362  211 LEU A CG  
1698 C CD1 . LEU A 211 ? 0.3396 0.2921 0.2009 -0.1191 -0.0159 0.0411  211 LEU A CD1 
1699 C CD2 . LEU A 211 ? 0.3644 0.3367 0.2215 -0.1204 -0.0053 0.0326  211 LEU A CD2 
1700 N N   . LYS A 212 ? 0.3662 0.3070 0.1953 -0.1106 -0.0370 0.0477  212 LYS A N   
1701 C CA  . LYS A 212 ? 0.3696 0.2990 0.1886 -0.1091 -0.0484 0.0535  212 LYS A CA  
1702 C C   . LYS A 212 ? 0.4041 0.3166 0.2183 -0.1090 -0.0579 0.0617  212 LYS A C   
1703 O O   . LYS A 212 ? 0.4224 0.3280 0.2402 -0.1021 -0.0686 0.0647  212 LYS A O   
1704 C CB  . LYS A 212 ? 0.4238 0.3508 0.2213 -0.1181 -0.0471 0.0551  212 LYS A CB  
1705 C CG  . LYS A 212 ? 0.4703 0.3837 0.2543 -0.1178 -0.0600 0.0621  212 LYS A CG  
1706 C CD  . LYS A 212 ? 0.5601 0.4740 0.3251 -0.1248 -0.0589 0.0617  212 LYS A CD  
1707 C CE  . LYS A 212 ? 0.6297 0.5288 0.3801 -0.1247 -0.0733 0.0695  212 LYS A CE  
1708 N NZ  . LYS A 212 ? 0.6807 0.5781 0.4087 -0.1327 -0.0729 0.0697  212 LYS A NZ  
1709 N N   . GLU A 213 ? 0.3849 0.2905 0.1917 -0.1165 -0.0543 0.0650  213 GLU A N   
1710 C CA  . GLU A 213 ? 0.4053 0.2922 0.2053 -0.1174 -0.0634 0.0731  213 GLU A CA  
1711 C C   . GLU A 213 ? 0.3938 0.2816 0.2141 -0.1083 -0.0652 0.0705  213 GLU A C   
1712 O O   . GLU A 213 ? 0.3927 0.2901 0.2238 -0.1089 -0.0566 0.0654  213 GLU A O   
1713 C CB  . GLU A 213 ? 0.4326 0.3097 0.2144 -0.1308 -0.0590 0.0784  213 GLU A CB  
1714 C CG  . GLU A 213 ? 0.4959 0.3508 0.2684 -0.1325 -0.0690 0.0874  213 GLU A CG  
1715 C CD  . GLU A 213 ? 0.5685 0.4116 0.3200 -0.1473 -0.0651 0.0938  213 GLU A CD  
1716 O OE1 . GLU A 213 ? 0.5855 0.4398 0.3336 -0.1563 -0.0527 0.0902  213 GLU A OE1 
1717 O OE2 . GLU A 213 ? 0.6530 0.4752 0.3915 -0.1497 -0.0747 0.1024  213 GLU A OE2 
1718 N N   . PRO A 214 ? 0.3918 0.2699 0.2177 -0.1000 -0.0763 0.0735  214 PRO A N   
1719 C CA  . PRO A 214 ? 0.3984 0.2762 0.2420 -0.0919 -0.0776 0.0707  214 PRO A CA  
1720 C C   . PRO A 214 ? 0.4061 0.2694 0.2422 -0.0984 -0.0782 0.0754  214 PRO A C   
1721 O O   . PRO A 214 ? 0.4669 0.3161 0.2835 -0.1078 -0.0809 0.0827  214 PRO A O   
1722 C CB  . PRO A 214 ? 0.4039 0.2756 0.2544 -0.0814 -0.0897 0.0724  214 PRO A CB  
1723 C CG  . PRO A 214 ? 0.5061 0.3765 0.3430 -0.0842 -0.0948 0.0759  214 PRO A CG  
1724 C CD  . PRO A 214 ? 0.4530 0.3194 0.2692 -0.0975 -0.0888 0.0794  214 PRO A CD  
1725 N N   . ILE A 215 ? 0.3981 0.2637 0.2494 -0.0932 -0.0763 0.0712  215 ILE A N   
1726 C CA  . ILE A 215 ? 0.4085 0.2579 0.2560 -0.0964 -0.0799 0.0752  215 ILE A CA  
1727 C C   . ILE A 215 ? 0.4152 0.2516 0.2686 -0.0861 -0.0920 0.0774  215 ILE A C   
1728 O O   . ILE A 215 ? 0.4316 0.2771 0.2989 -0.0751 -0.0946 0.0730  215 ILE A O   
1729 C CB  . ILE A 215 ? 0.4035 0.2622 0.2626 -0.0981 -0.0710 0.0692  215 ILE A CB  
1730 C CG1 . ILE A 215 ? 0.3795 0.2513 0.2596 -0.0856 -0.0697 0.0612  215 ILE A CG1 
1731 C CG2 . ILE A 215 ? 0.4084 0.2802 0.2622 -0.1085 -0.0594 0.0670  215 ILE A CG2 
1732 C CD1 . ILE A 215 ? 0.3799 0.2599 0.2715 -0.0861 -0.0625 0.0550  215 ILE A CD1 
1733 N N   . SER A 216 ? 0.4531 0.2681 0.2961 -0.0896 -0.0993 0.0840  216 SER A N   
1734 C CA  A SER A 216 ? 0.4852 0.2857 0.3328 -0.0797 -0.1117 0.0864  216 SER A CA  
1735 C CA  B SER A 216 ? 0.4873 0.2873 0.3345 -0.0800 -0.1118 0.0866  216 SER A CA  
1736 C C   . SER A 216 ? 0.5094 0.3060 0.3699 -0.0749 -0.1112 0.0819  216 SER A C   
1737 O O   . SER A 216 ? 0.5572 0.3461 0.4117 -0.0834 -0.1075 0.0833  216 SER A O   
1738 C CB  A SER A 216 ? 0.5413 0.3176 0.3683 -0.0854 -0.1223 0.0970  216 SER A CB  
1739 C CB  B SER A 216 ? 0.5380 0.3134 0.3641 -0.0865 -0.1218 0.0972  216 SER A CB  
1740 O OG  A SER A 216 ? 0.5402 0.3190 0.3562 -0.0870 -0.1258 0.1007  216 SER A OG  
1741 O OG  B SER A 216 ? 0.5467 0.3051 0.3775 -0.0776 -0.1337 0.0993  216 SER A OG  
1742 N N   . VAL A 217 ? 0.4627 0.2647 0.3405 -0.0616 -0.1149 0.0763  217 VAL A N   
1743 C CA  . VAL A 217 ? 0.4788 0.2760 0.3687 -0.0552 -0.1157 0.0714  217 VAL A CA  
1744 C C   . VAL A 217 ? 0.4660 0.2500 0.3616 -0.0440 -0.1280 0.0725  217 VAL A C   
1745 O O   . VAL A 217 ? 0.4765 0.2619 0.3727 -0.0386 -0.1346 0.0746  217 VAL A O   
1746 C CB  . VAL A 217 ? 0.4818 0.3008 0.3889 -0.0494 -0.1062 0.0616  217 VAL A CB  
1747 C CG1 . VAL A 217 ? 0.5014 0.3327 0.4040 -0.0598 -0.0951 0.0603  217 VAL A CG1 
1748 C CG2 . VAL A 217 ? 0.4278 0.2611 0.3465 -0.0394 -0.1075 0.0580  217 VAL A CG2 
1749 N N   . SER A 218 ? 0.4741 0.2452 0.3746 -0.0400 -0.1315 0.0703  218 SER A N   
1750 C CA  . SER A 218 ? 0.4822 0.2414 0.3898 -0.0282 -0.1430 0.0703  218 SER A CA  
1751 C C   . SER A 218 ? 0.4510 0.2291 0.3804 -0.0149 -0.1403 0.0606  218 SER A C   
1752 O O   . SER A 218 ? 0.4012 0.1960 0.3395 -0.0145 -0.1301 0.0536  218 SER A O   
1753 C CB  . SER A 218 ? 0.5227 0.2581 0.4263 -0.0286 -0.1491 0.0718  218 SER A CB  
1754 O OG  . SER A 218 ? 0.4867 0.2297 0.4021 -0.0256 -0.1419 0.0630  218 SER A OG  
1755 N N   . SER A 219 ? 0.4745 0.2841 0.3931 0.0207  -0.0966 0.0531  219 SER A N   
1756 C CA  A SER A 219 ? 0.4481 0.2783 0.3861 0.0320  -0.0928 0.0444  219 SER A CA  
1757 C CA  B SER A 219 ? 0.4473 0.2775 0.3853 0.0320  -0.0927 0.0444  219 SER A CA  
1758 C C   . SER A 219 ? 0.4316 0.2382 0.3640 0.0330  -0.0850 0.0353  219 SER A C   
1759 O O   . SER A 219 ? 0.4156 0.2390 0.3587 0.0315  -0.0787 0.0260  219 SER A O   
1760 C CB  A SER A 219 ? 0.4781 0.3202 0.4270 0.0530  -0.0989 0.0511  219 SER A CB  
1761 C CB  B SER A 219 ? 0.4794 0.3213 0.4285 0.0532  -0.0986 0.0508  219 SER A CB  
1762 O OG  A SER A 219 ? 0.4734 0.3427 0.4442 0.0640  -0.0939 0.0443  219 SER A OG  
1763 O OG  B SER A 219 ? 0.4711 0.3460 0.4293 0.0500  -0.1069 0.0570  219 SER A OG  
1764 N N   . GLU A 220 ? 0.4744 0.2394 0.3865 0.0337  -0.0859 0.0379  220 GLU A N   
1765 C CA  . GLU A 220 ? 0.5079 0.2449 0.4079 0.0314  -0.0802 0.0283  220 GLU A CA  
1766 C C   . GLU A 220 ? 0.4914 0.2403 0.3923 0.0102  -0.0770 0.0227  220 GLU A C   
1767 O O   . GLU A 220 ? 0.4802 0.2315 0.3820 0.0094  -0.0718 0.0127  220 GLU A O   
1768 C CB  . GLU A 220 ? 0.5853 0.2695 0.4587 0.0319  -0.0830 0.0329  220 GLU A CB  
1769 C CG  . GLU A 220 ? 0.7322 0.3991 0.6032 0.0588  -0.0847 0.0389  220 GLU A CG  
1770 C CD  . GLU A 220 ? 0.7787 0.4539 0.6518 0.0631  -0.0936 0.0552  220 GLU A CD  
1771 O OE1 . GLU A 220 ? 0.7160 0.4232 0.5982 0.0497  -0.0975 0.0599  220 GLU A OE1 
1772 O OE2 . GLU A 220 ? 0.8350 0.4810 0.6970 0.0814  -0.0964 0.0636  220 GLU A OE2 
1773 N N   . GLN A 221 ? 0.4523 0.2116 0.3532 -0.0057 -0.0793 0.0298  221 GLN A N   
1774 C CA  . GLN A 221 ? 0.4212 0.1969 0.3265 -0.0225 -0.0757 0.0269  221 GLN A CA  
1775 C C   . GLN A 221 ? 0.4044 0.2138 0.3279 -0.0180 -0.0707 0.0201  221 GLN A C   
1776 O O   . GLN A 221 ? 0.3828 0.1983 0.3082 -0.0232 -0.0670 0.0139  221 GLN A O   
1777 C CB  . GLN A 221 ? 0.4293 0.2130 0.3328 -0.0363 -0.0764 0.0369  221 GLN A CB  
1778 C CG  . GLN A 221 ? 0.4668 0.2191 0.3522 -0.0487 -0.0799 0.0444  221 GLN A CG  
1779 C CD  . GLN A 221 ? 0.4584 0.2229 0.3429 -0.0614 -0.0784 0.0557  221 GLN A CD  
1780 O OE1 . GLN A 221 ? 0.4506 0.2304 0.3378 -0.0554 -0.0775 0.0597  221 GLN A OE1 
1781 N NE2 . GLN A 221 ? 0.4533 0.2125 0.3329 -0.0799 -0.0780 0.0611  221 GLN A NE2 
1782 N N   . VAL A 222 ? 0.3696 0.2010 0.3050 -0.0100 -0.0712 0.0218  222 VAL A N   
1783 C CA  . VAL A 222 ? 0.3481 0.2079 0.2988 -0.0086 -0.0664 0.0161  222 VAL A CA  
1784 C C   . VAL A 222 ? 0.3665 0.2266 0.3217 0.0015  -0.0624 0.0082  222 VAL A C   
1785 O O   . VAL A 222 ? 0.3416 0.2169 0.3034 -0.0014 -0.0568 0.0030  222 VAL A O   
1786 C CB  . VAL A 222 ? 0.3824 0.2637 0.3422 -0.0057 -0.0694 0.0192  222 VAL A CB  
1787 C CG1 . VAL A 222 ? 0.3559 0.2620 0.3283 -0.0094 -0.0639 0.0138  222 VAL A CG1 
1788 C CG2 . VAL A 222 ? 0.4524 0.3289 0.4015 -0.0143 -0.0723 0.0262  222 VAL A CG2 
1789 N N   . SER A 223 ? 0.3752 0.2180 0.3256 0.0153  -0.0641 0.0077  223 SER A N   
1790 C CA  . SER A 223 ? 0.3935 0.2359 0.3461 0.0276  -0.0576 -0.0004 223 SER A CA  
1791 C C   . SER A 223 ? 0.3974 0.2232 0.3348 0.0176  -0.0536 -0.0080 223 SER A C   
1792 O O   . SER A 223 ? 0.3865 0.2203 0.3250 0.0223  -0.0466 -0.0154 223 SER A O   
1793 C CB  . SER A 223 ? 0.4446 0.2647 0.3909 0.0472  -0.0584 0.0008  223 SER A CB  
1794 O OG  . SER A 223 ? 0.5325 0.3065 0.4524 0.0428  -0.0602 -0.0008 223 SER A OG  
1795 N N   . LYS A 224 ? 0.3843 0.1884 0.3067 0.0031  -0.0583 -0.0055 224 LYS A N   
1796 C CA  . LYS A 224 ? 0.3973 0.1912 0.3061 -0.0096 -0.0574 -0.0112 224 LYS A CA  
1797 C C   . LYS A 224 ? 0.3507 0.1780 0.2731 -0.0167 -0.0538 -0.0110 224 LYS A C   
1798 O O   . LYS A 224 ? 0.3660 0.1934 0.2804 -0.0204 -0.0512 -0.0169 224 LYS A O   
1799 C CB  . LYS A 224 ? 0.4128 0.1846 0.3073 -0.0267 -0.0643 -0.0061 224 LYS A CB  
1800 C CG  . LYS A 224 ? 0.4865 0.2147 0.3610 -0.0226 -0.0679 -0.0054 224 LYS A CG  
1801 C CD  . LYS A 224 ? 0.5839 0.2803 0.4383 -0.0123 -0.0641 -0.0171 224 LYS A CD  
1802 C CE  . LYS A 224 ? 0.7293 0.3743 0.5604 -0.0060 -0.0666 -0.0157 224 LYS A CE  
1803 N NZ  . LYS A 224 ? 0.8200 0.4310 0.6314 0.0129  -0.0595 -0.0273 224 LYS A NZ  
1804 N N   . PHE A 225 ? 0.3163 0.1684 0.2554 -0.0185 -0.0535 -0.0045 225 PHE A N   
1805 C CA  . PHE A 225 ? 0.3280 0.2058 0.2780 -0.0223 -0.0487 -0.0040 225 PHE A CA  
1806 C C   . PHE A 225 ? 0.2981 0.1859 0.2520 -0.0132 -0.0422 -0.0107 225 PHE A C   
1807 O O   . PHE A 225 ? 0.3039 0.2019 0.2570 -0.0171 -0.0381 -0.0121 225 PHE A O   
1808 C CB  . PHE A 225 ? 0.3230 0.2181 0.2855 -0.0233 -0.0478 0.0018  225 PHE A CB  
1809 C CG  . PHE A 225 ? 0.3189 0.2109 0.2784 -0.0317 -0.0504 0.0093  225 PHE A CG  
1810 C CD1 . PHE A 225 ? 0.3707 0.2509 0.3216 -0.0402 -0.0541 0.0126  225 PHE A CD1 
1811 C CD2 . PHE A 225 ? 0.3450 0.2463 0.3089 -0.0320 -0.0487 0.0129  225 PHE A CD2 
1812 C CE1 . PHE A 225 ? 0.3739 0.2566 0.3246 -0.0478 -0.0546 0.0212  225 PHE A CE1 
1813 C CE2 . PHE A 225 ? 0.3866 0.2862 0.3462 -0.0379 -0.0483 0.0198  225 PHE A CE2 
1814 C CZ  . PHE A 225 ? 0.3504 0.2434 0.3055 -0.0452 -0.0506 0.0247  225 PHE A CZ  
1815 N N   . ARG A 226 ? 0.3064 0.1947 0.2659 -0.0005 -0.0408 -0.0132 226 ARG A N   
1816 C CA  . ARG A 226 ? 0.2843 0.1905 0.2530 0.0087  -0.0329 -0.0175 226 ARG A CA  
1817 C C   . ARG A 226 ? 0.3144 0.2046 0.2660 0.0138  -0.0274 -0.0258 226 ARG A C   
1818 O O   . ARG A 226 ? 0.3331 0.2394 0.2896 0.0203  -0.0186 -0.0293 226 ARG A O   
1819 C CB  . ARG A 226 ? 0.2852 0.2049 0.2697 0.0218  -0.0335 -0.0152 226 ARG A CB  
1820 C CG  . ARG A 226 ? 0.3039 0.2376 0.3001 0.0155  -0.0405 -0.0079 226 ARG A CG  
1821 C CD  . ARG A 226 ? 0.2861 0.2451 0.3018 0.0264  -0.0421 -0.0046 226 ARG A CD  
1822 N NE  . ARG A 226 ? 0.3016 0.2693 0.3216 0.0183  -0.0510 0.0017  226 ARG A NE  
1823 C CZ  . ARG A 226 ? 0.3092 0.2665 0.3245 0.0230  -0.0596 0.0073  226 ARG A CZ  
1824 N NH1 . ARG A 226 ? 0.3536 0.2892 0.3612 0.0374  -0.0606 0.0082  226 ARG A NH1 
1825 N NH2 . ARG A 226 ? 0.3107 0.2752 0.3251 0.0137  -0.0670 0.0121  226 ARG A NH2 
1826 N N   . LYS A 227 ? 0.3318 0.1907 0.2611 0.0085  -0.0321 -0.0291 227 LYS A N   
1827 C CA  . LYS A 227 ? 0.3652 0.2039 0.2710 0.0102  -0.0276 -0.0387 227 LYS A CA  
1828 C C   . LYS A 227 ? 0.3536 0.2028 0.2517 -0.0039 -0.0279 -0.0386 227 LYS A C   
1829 O O   . LYS A 227 ? 0.3925 0.2286 0.2685 -0.0041 -0.0243 -0.0467 227 LYS A O   
1830 C CB  . LYS A 227 ? 0.4027 0.1980 0.2830 0.0081  -0.0333 -0.0431 227 LYS A CB  
1831 C CG  . LYS A 227 ? 0.4436 0.2222 0.3268 0.0262  -0.0320 -0.0425 227 LYS A CG  
1832 C CD  . LYS A 227 ? 0.6106 0.3392 0.4652 0.0206  -0.0384 -0.0452 227 LYS A CD  
1833 C CE  . LYS A 227 ? 0.7348 0.4276 0.5548 0.0200  -0.0338 -0.0587 227 LYS A CE  
1834 N NZ  . LYS A 227 ? 0.8211 0.4576 0.6083 0.0116  -0.0402 -0.0623 227 LYS A NZ  
1835 N N   . LEU A 228 ? 0.3243 0.1944 0.2371 -0.0146 -0.0321 -0.0295 228 LEU A N   
1836 C CA  . LEU A 228 ? 0.3155 0.2012 0.2256 -0.0235 -0.0312 -0.0265 228 LEU A CA  
1837 C C   . LEU A 228 ? 0.3090 0.2131 0.2256 -0.0157 -0.0205 -0.0280 228 LEU A C   
1838 O O   . LEU A 228 ? 0.3007 0.2150 0.2324 -0.0057 -0.0146 -0.0288 228 LEU A O   
1839 C CB  . LEU A 228 ? 0.3129 0.2158 0.2387 -0.0318 -0.0354 -0.0153 228 LEU A CB  
1840 C CG  . LEU A 228 ? 0.3261 0.2179 0.2483 -0.0415 -0.0448 -0.0113 228 LEU A CG  
1841 C CD1 . LEU A 228 ? 0.3373 0.2471 0.2779 -0.0441 -0.0449 -0.0005 228 LEU A CD1 
1842 C CD2 . LEU A 228 ? 0.3685 0.2561 0.2739 -0.0536 -0.0512 -0.0117 228 LEU A CD2 
1843 N N   . ASN A 229 ? 0.3118 0.2237 0.2183 -0.0217 -0.0186 -0.0263 229 ASN A N   
1844 C CA  . ASN A 229 ? 0.3117 0.2402 0.2206 -0.0173 -0.0077 -0.0260 229 ASN A CA  
1845 C C   . ASN A 229 ? 0.2968 0.2414 0.2127 -0.0250 -0.0080 -0.0148 229 ASN A C   
1846 O O   . ASN A 229 ? 0.2976 0.2409 0.2073 -0.0325 -0.0159 -0.0090 229 ASN A O   
1847 C CB  . ASN A 229 ? 0.3488 0.2654 0.2298 -0.0150 -0.0027 -0.0350 229 ASN A CB  
1848 C CG  . ASN A 229 ? 0.4266 0.3266 0.2997 -0.0016 0.0037  -0.0465 229 ASN A CG  
1849 O OD1 . ASN A 229 ? 0.4171 0.3192 0.3086 0.0072  0.0043  -0.0462 229 ASN A OD1 
1850 N ND2 . ASN A 229 ? 0.5122 0.3948 0.3551 0.0013  0.0091  -0.0563 229 ASN A ND2 
1851 N N   . PHE A 230 ? 0.2820 0.2418 0.2106 -0.0229 0.0011  -0.0109 230 PHE A N   
1852 C CA  . PHE A 230 ? 0.2755 0.2433 0.2055 -0.0286 0.0031  -0.0002 230 PHE A CA  
1853 C C   . PHE A 230 ? 0.3007 0.2692 0.2094 -0.0309 0.0049  0.0018  230 PHE A C   
1854 O O   . PHE A 230 ? 0.2982 0.2694 0.2026 -0.0347 0.0018  0.0122  230 PHE A O   
1855 C CB  . PHE A 230 ? 0.2709 0.2499 0.2156 -0.0293 0.0124  0.0032  230 PHE A CB  
1856 C CG  . PHE A 230 ? 0.2512 0.2311 0.2143 -0.0302 0.0099  0.0032  230 PHE A CG  
1857 C CD1 . PHE A 230 ? 0.2426 0.2135 0.2085 -0.0329 0.0044  0.0085  230 PHE A CD1 
1858 C CD2 . PHE A 230 ? 0.2477 0.2406 0.2252 -0.0285 0.0139  -0.0009 230 PHE A CD2 
1859 C CE1 . PHE A 230 ? 0.2429 0.2124 0.2201 -0.0351 0.0030  0.0079  230 PHE A CE1 
1860 C CE2 . PHE A 230 ? 0.2367 0.2326 0.2289 -0.0319 0.0101  -0.0001 230 PHE A CE2 
1861 C CZ  . PHE A 230 ? 0.2433 0.2248 0.2327 -0.0358 0.0046  0.0034  230 PHE A CZ  
1862 N N   . ASN A 231 ? 0.3143 0.2809 0.2083 -0.0273 0.0110  -0.0070 231 ASN A N   
1863 C CA  . ASN A 231 ? 0.3376 0.3051 0.2072 -0.0298 0.0148  -0.0055 231 ASN A CA  
1864 C C   . ASN A 231 ? 0.3559 0.3128 0.2019 -0.0362 0.0023  -0.0066 231 ASN A C   
1865 O O   . ASN A 231 ? 0.3550 0.3013 0.2014 -0.0388 -0.0078 -0.0112 231 ASN A O   
1866 C CB  . ASN A 231 ? 0.3745 0.3431 0.2340 -0.0226 0.0278  -0.0156 231 ASN A CB  
1867 C CG  . ASN A 231 ? 0.3701 0.3215 0.2228 -0.0150 0.0256  -0.0298 231 ASN A CG  
1868 O OD1 . ASN A 231 ? 0.3539 0.3067 0.2282 -0.0092 0.0249  -0.0317 231 ASN A OD1 
1869 N ND2 . ASN A 231 ? 0.4112 0.3431 0.2299 -0.0156 0.0242  -0.0393 231 ASN A ND2 
1870 N N   . GLY A 232 ? 0.3782 0.3395 0.2029 -0.0406 0.0024  -0.0007 232 GLY A N   
1871 C CA  . GLY A 232 ? 0.4180 0.3714 0.2144 -0.0488 -0.0095 -0.0035 232 GLY A CA  
1872 C C   . GLY A 232 ? 0.4532 0.3870 0.2184 -0.0473 -0.0044 -0.0207 232 GLY A C   
1873 O O   . GLY A 232 ? 0.4623 0.3945 0.2261 -0.0376 0.0112  -0.0279 232 GLY A O   
1874 N N   . GLU A 233 ? 0.4952 0.4137 0.2335 -0.0574 -0.0171 -0.0271 233 GLU A N   
1875 C CA  . GLU A 233 ? 0.6101 0.5009 0.3090 -0.0571 -0.0126 -0.0451 233 GLU A CA  
1876 C C   . GLU A 233 ? 0.5880 0.4837 0.2620 -0.0524 0.0014  -0.0462 233 GLU A C   
1877 O O   . GLU A 233 ? 0.6135 0.5275 0.2816 -0.0586 -0.0019 -0.0330 233 GLU A O   
1878 C CB  . GLU A 233 ? 0.7104 0.5847 0.3806 -0.0748 -0.0316 -0.0495 233 GLU A CB  
1879 C CG  . GLU A 233 ? 0.8523 0.6847 0.4853 -0.0765 -0.0306 -0.0704 233 GLU A CG  
1880 C CD  . GLU A 233 ? 0.9863 0.8041 0.5962 -0.0996 -0.0524 -0.0725 233 GLU A CD  
1881 O OE1 . GLU A 233 ? 0.9953 0.8037 0.6220 -0.1055 -0.0613 -0.0725 233 GLU A OE1 
1882 O OE2 . GLU A 233 ? 1.0599 0.8782 0.6348 -0.1138 -0.0616 -0.0727 233 GLU A OE2 
1883 N N   . GLY A 234 ? 0.5864 0.4669 0.2456 -0.0400 0.0185  -0.0605 234 GLY A N   
1884 C CA  . GLY A 234 ? 0.6068 0.4938 0.2425 -0.0347 0.0350  -0.0616 234 GLY A CA  
1885 C C   . GLY A 234 ? 0.6002 0.5180 0.2704 -0.0256 0.0511  -0.0499 234 GLY A C   
1886 O O   . GLY A 234 ? 0.6140 0.5406 0.2675 -0.0218 0.0670  -0.0491 234 GLY A O   
1887 N N   . GLU A 235 ? 0.5809 0.5141 0.2961 -0.0235 0.0480  -0.0412 235 GLU A N   
1888 C CA  . GLU A 235 ? 0.5355 0.4948 0.2846 -0.0178 0.0617  -0.0320 235 GLU A CA  
1889 C C   . GLU A 235 ? 0.5355 0.4976 0.3103 -0.0045 0.0703  -0.0410 235 GLU A C   
1890 O O   . GLU A 235 ? 0.5101 0.4513 0.2813 0.0001  0.0628  -0.0514 235 GLU A O   
1891 C CB  . GLU A 235 ? 0.5199 0.4921 0.2970 -0.0262 0.0515  -0.0154 235 GLU A CB  
1892 C CG  . GLU A 235 ? 0.5553 0.5258 0.3109 -0.0364 0.0402  -0.0042 235 GLU A CG  
1893 C CD  . GLU A 235 ? 0.5864 0.5665 0.3698 -0.0402 0.0331  0.0125  235 GLU A CD  
1894 O OE1 . GLU A 235 ? 0.6276 0.6134 0.4022 -0.0441 0.0332  0.0272  235 GLU A OE1 
1895 O OE2 . GLU A 235 ? 0.5052 0.4846 0.3161 -0.0381 0.0283  0.0109  235 GLU A OE2 
1896 N N   . PRO A 236 ? 0.5417 0.5304 0.3424 0.0017  0.0856  -0.0362 236 PRO A N   
1897 C CA  . PRO A 236 ? 0.5502 0.5477 0.3773 0.0161  0.0929  -0.0429 236 PRO A CA  
1898 C C   . PRO A 236 ? 0.4593 0.4499 0.3113 0.0140  0.0766  -0.0415 236 PRO A C   
1899 O O   . PRO A 236 ? 0.4335 0.4283 0.2992 0.0019  0.0658  -0.0313 236 PRO A O   
1900 C CB  . PRO A 236 ? 0.5765 0.6124 0.4314 0.0164  0.1087  -0.0333 236 PRO A CB  
1901 C CG  . PRO A 236 ? 0.5873 0.6248 0.4129 0.0077  0.1172  -0.0275 236 PRO A CG  
1902 C CD  . PRO A 236 ? 0.5640 0.5759 0.3671 -0.0043 0.0981  -0.0243 236 PRO A CD  
1903 N N   . GLU A 237 ? 0.5049 0.4827 0.3601 0.0273  0.0761  -0.0514 237 GLU A N   
1904 C CA  . GLU A 237 ? 0.5111 0.4773 0.3827 0.0255  0.0606  -0.0507 237 GLU A CA  
1905 C C   . GLU A 237 ? 0.4563 0.4520 0.3687 0.0221  0.0586  -0.0398 237 GLU A C   
1906 O O   . GLU A 237 ? 0.4402 0.4640 0.3759 0.0297  0.0693  -0.0374 237 GLU A O   
1907 C CB  . GLU A 237 ? 0.6036 0.5461 0.4669 0.0418  0.0618  -0.0622 237 GLU A CB  
1908 C CG  . GLU A 237 ? 0.6899 0.6272 0.5758 0.0418  0.0484  -0.0588 237 GLU A CG  
1909 C CD  . GLU A 237 ? 0.8161 0.7152 0.6829 0.0529  0.0450  -0.0689 237 GLU A CD  
1910 O OE1 . GLU A 237 ? 0.8768 0.7402 0.7070 0.0463  0.0403  -0.0775 237 GLU A OE1 
1911 O OE2 . GLU A 237 ? 0.8302 0.7344 0.7179 0.0676  0.0464  -0.0676 237 GLU A OE2 
1912 N N   . GLU A 238 ? 0.3742 0.2803 0.3428 -0.0166 0.0385  -0.0581 238 GLU A N   
1913 C CA  . GLU A 238 ? 0.3443 0.2647 0.3333 -0.0108 0.0314  -0.0509 238 GLU A CA  
1914 C C   . GLU A 238 ? 0.3360 0.2622 0.3294 -0.0108 0.0176  -0.0451 238 GLU A C   
1915 O O   . GLU A 238 ? 0.3421 0.2738 0.3195 -0.0142 0.0090  -0.0404 238 GLU A O   
1916 C CB  . GLU A 238 ? 0.3825 0.3129 0.3620 -0.0111 0.0298  -0.0463 238 GLU A CB  
1917 C CG  . GLU A 238 ? 0.4978 0.4230 0.4687 -0.0123 0.0429  -0.0511 238 GLU A CG  
1918 C CD  . GLU A 238 ? 0.6074 0.5417 0.5648 -0.0144 0.0402  -0.0457 238 GLU A CD  
1919 O OE1 . GLU A 238 ? 0.6218 0.5658 0.5776 -0.0145 0.0291  -0.0388 238 GLU A OE1 
1920 O OE2 . GLU A 238 ? 0.6516 0.5833 0.6002 -0.0161 0.0496  -0.0482 238 GLU A OE2 
1921 N N   . PRO A 239 ? 0.3096 0.2358 0.3259 -0.0072 0.0151  -0.0442 239 PRO A N   
1922 C CA  . PRO A 239 ? 0.2999 0.2322 0.3210 -0.0074 0.0018  -0.0381 239 PRO A CA  
1923 C C   . PRO A 239 ? 0.2675 0.2134 0.2842 -0.0071 -0.0077 -0.0306 239 PRO A C   
1924 O O   . PRO A 239 ? 0.2798 0.2327 0.3046 -0.0043 -0.0061 -0.0288 239 PRO A O   
1925 C CB  . PRO A 239 ? 0.3111 0.2432 0.3621 -0.0030 0.0020  -0.0371 239 PRO A CB  
1926 C CG  . PRO A 239 ? 0.3720 0.2918 0.4297 -0.0017 0.0175  -0.0454 239 PRO A CG  
1927 C CD  . PRO A 239 ? 0.3507 0.2701 0.3898 -0.0032 0.0251  -0.0486 239 PRO A CD  
1928 N N   . MET A 240 ? 0.2506 0.1998 0.2555 -0.0101 -0.0174 -0.0263 240 MET A N   
1929 C CA  . MET A 240 ? 0.2376 0.1985 0.2377 -0.0101 -0.0255 -0.0193 240 MET A CA  
1930 C C   . MET A 240 ? 0.2487 0.2166 0.2682 -0.0073 -0.0328 -0.0148 240 MET A C   
1931 O O   . MET A 240 ? 0.2255 0.1946 0.2475 -0.0085 -0.0409 -0.0113 240 MET A O   
1932 C CB  . MET A 240 ? 0.2403 0.2019 0.2221 -0.0145 -0.0322 -0.0158 240 MET A CB  
1933 C CG  . MET A 240 ? 0.2410 0.2141 0.2182 -0.0142 -0.0380 -0.0088 240 MET A CG  
1934 S SD  . MET A 240 ? 0.2467 0.2213 0.2059 -0.0191 -0.0454 -0.0030 240 MET A SD  
1935 C CE  . MET A 240 ? 0.2683 0.2390 0.2102 -0.0227 -0.0382 -0.0052 240 MET A CE  
1936 N N   . VAL A 241 ? 0.2288 0.2014 0.2617 -0.0043 -0.0304 -0.0144 241 VAL A N   
1937 C CA  . VAL A 241 ? 0.2141 0.1935 0.2648 -0.0029 -0.0376 -0.0097 241 VAL A CA  
1938 C C   . VAL A 241 ? 0.2195 0.2060 0.2709 -0.0018 -0.0367 -0.0083 241 VAL A C   
1939 O O   . VAL A 241 ? 0.2265 0.2115 0.2726 -0.0007 -0.0286 -0.0117 241 VAL A O   
1940 C CB  . VAL A 241 ? 0.2552 0.2307 0.3298 -0.0006 -0.0355 -0.0107 241 VAL A CB  
1941 C CG1 . VAL A 241 ? 0.2365 0.2040 0.3114 -0.0018 -0.0361 -0.0123 241 VAL A CG1 
1942 C CG2 . VAL A 241 ? 0.2416 0.2129 0.3252 0.0022  -0.0239 -0.0156 241 VAL A CG2 
1943 N N   . ASP A 242 ? 0.2131 0.2069 0.2708 -0.0026 -0.0451 -0.0033 242 ASP A N   
1944 C CA  . ASP A 242 ? 0.2069 0.2065 0.2661 -0.0023 -0.0447 -0.0024 242 ASP A CA  
1945 C C   . ASP A 242 ? 0.2101 0.2107 0.2511 -0.0026 -0.0402 -0.0036 242 ASP A C   
1946 O O   . ASP A 242 ? 0.2156 0.2174 0.2572 -0.0012 -0.0342 -0.0054 242 ASP A O   
1947 C CB  . ASP A 242 ? 0.2083 0.2068 0.2861 0.0003  -0.0392 -0.0043 242 ASP A CB  
1948 C CG  . ASP A 242 ? 0.2357 0.2358 0.3354 0.0000  -0.0456 -0.0005 242 ASP A CG  
1949 O OD1 . ASP A 242 ? 0.2032 0.2081 0.3027 -0.0030 -0.0559 0.0045  242 ASP A OD1 
1950 O OD2 . ASP A 242 ? 0.2612 0.2577 0.3783 0.0026  -0.0398 -0.0021 242 ASP A OD2 
1951 N N   . ASN A 243 ? 0.1811 0.1821 0.2077 -0.0045 -0.0437 -0.0015 243 ASN A N   
1952 C CA  . ASN A 243 ? 0.1820 0.1853 0.1935 -0.0053 -0.0409 -0.0004 243 ASN A CA  
1953 C C   . ASN A 243 ? 0.1871 0.1964 0.1959 -0.0065 -0.0454 0.0032  243 ASN A C   
1954 O O   . ASN A 243 ? 0.2093 0.2207 0.2075 -0.0079 -0.0475 0.0065  243 ASN A O   
1955 C CB  . ASN A 243 ? 0.1995 0.1998 0.1976 -0.0072 -0.0415 0.0007  243 ASN A CB  
1956 C CG  . ASN A 243 ? 0.1913 0.1915 0.1887 -0.0090 -0.0499 0.0038  243 ASN A CG  
1957 O OD1 . ASN A 243 ? 0.2199 0.2226 0.2267 -0.0090 -0.0554 0.0055  243 ASN A OD1 
1958 N ND2 . ASN A 243 ? 0.2258 0.2236 0.2119 -0.0112 -0.0514 0.0053  243 ASN A ND2 
1959 N N   . TRP A 244 ? 0.1903 0.2016 0.2089 -0.0062 -0.0461 0.0025  244 TRP A N   
1960 C CA  . TRP A 244 ? 0.1964 0.2117 0.2120 -0.0081 -0.0492 0.0044  244 TRP A CA  
1961 C C   . TRP A 244 ? 0.2158 0.2318 0.2354 -0.0070 -0.0434 0.0019  244 TRP A C   
1962 O O   . TRP A 244 ? 0.2268 0.2415 0.2565 -0.0050 -0.0395 -0.0006 244 TRP A O   
1963 C CB  . TRP A 244 ? 0.2137 0.2305 0.2363 -0.0109 -0.0582 0.0066  244 TRP A CB  
1964 C CG  . TRP A 244 ? 0.2311 0.2471 0.2712 -0.0101 -0.0599 0.0060  244 TRP A CG  
1965 C CD1 . TRP A 244 ? 0.2252 0.2387 0.2749 -0.0090 -0.0616 0.0065  244 TRP A CD1 
1966 C CD2 . TRP A 244 ? 0.2522 0.2694 0.3042 -0.0104 -0.0596 0.0051  244 TRP A CD2 
1967 N NE1 . TRP A 244 ? 0.2130 0.2267 0.2816 -0.0082 -0.0621 0.0066  244 TRP A NE1 
1968 C CE2 . TRP A 244 ? 0.2559 0.2722 0.3261 -0.0092 -0.0612 0.0061  244 TRP A CE2 
1969 C CE3 . TRP A 244 ? 0.2645 0.2833 0.3146 -0.0118 -0.0577 0.0038  244 TRP A CE3 
1970 C CZ2 . TRP A 244 ? 0.3105 0.3281 0.3982 -0.0091 -0.0615 0.0066  244 TRP A CZ2 
1971 C CZ3 . TRP A 244 ? 0.2827 0.3024 0.3481 -0.0122 -0.0585 0.0038  244 TRP A CZ3 
1972 C CH2 . TRP A 244 ? 0.2929 0.3126 0.3776 -0.0110 -0.0609 0.0058  244 TRP A CH2 
1973 N N   . ARG A 245 ? 0.1875 0.2055 0.1996 -0.0084 -0.0422 0.0026  245 ARG A N   
1974 C CA  . ARG A 245 ? 0.1832 0.2016 0.1991 -0.0081 -0.0374 0.0003  245 ARG A CA  
1975 C C   . ARG A 245 ? 0.1904 0.2091 0.2103 -0.0119 -0.0435 -0.0001 245 ARG A C   
1976 O O   . ARG A 245 ? 0.2252 0.2443 0.2380 -0.0153 -0.0493 0.0018  245 ARG A O   
1977 C CB  . ARG A 245 ? 0.1807 0.1999 0.1871 -0.0079 -0.0318 0.0013  245 ARG A CB  
1978 C CG  . ARG A 245 ? 0.1599 0.1789 0.1714 -0.0071 -0.0255 -0.0012 245 ARG A CG  
1979 C CD  . ARG A 245 ? 0.1943 0.2137 0.1996 -0.0070 -0.0194 0.0001  245 ARG A CD  
1980 N NE  . ARG A 245 ? 0.1764 0.1955 0.1887 -0.0057 -0.0130 -0.0021 245 ARG A NE  
1981 C CZ  . ARG A 245 ? 0.1795 0.1980 0.1908 -0.0058 -0.0067 -0.0021 245 ARG A CZ  
1982 N NH1 . ARG A 245 ? 0.1759 0.1937 0.1795 -0.0071 -0.0052 -0.0003 245 ARG A NH1 
1983 N NH2 . ARG A 245 ? 0.1869 0.2052 0.2065 -0.0044 -0.0011 -0.0038 245 ARG A NH2 
1984 N N   . PRO A 246 ? 0.1941 0.2127 0.2249 -0.0118 -0.0424 -0.0021 246 PRO A N   
1985 C CA  . PRO A 246 ? 0.2088 0.2277 0.2423 -0.0168 -0.0488 -0.0020 246 PRO A CA  
1986 C C   . PRO A 246 ? 0.2071 0.2244 0.2260 -0.0205 -0.0475 -0.0033 246 PRO A C   
1987 O O   . PRO A 246 ? 0.2103 0.2267 0.2227 -0.0181 -0.0396 -0.0045 246 PRO A O   
1988 C CB  . PRO A 246 ? 0.2595 0.2784 0.3069 -0.0155 -0.0457 -0.0038 246 PRO A CB  
1989 C CG  . PRO A 246 ? 0.2262 0.2451 0.2817 -0.0097 -0.0394 -0.0042 246 PRO A CG  
1990 C CD  . PRO A 246 ? 0.2245 0.2427 0.2655 -0.0079 -0.0356 -0.0039 246 PRO A CD  
1991 N N   . THR A 247 ? 0.2219 0.2386 0.2361 -0.0268 -0.0550 -0.0026 247 THR A N   
1992 C CA  . THR A 247 ? 0.2184 0.2319 0.2179 -0.0310 -0.0523 -0.0051 247 THR A CA  
1993 C C   . THR A 247 ? 0.2116 0.2223 0.2138 -0.0307 -0.0449 -0.0093 247 THR A C   
1994 O O   . THR A 247 ? 0.2331 0.2445 0.2479 -0.0300 -0.0457 -0.0100 247 THR A O   
1995 C CB  . THR A 247 ? 0.2332 0.2457 0.2243 -0.0394 -0.0618 -0.0039 247 THR A CB  
1996 O OG1 . THR A 247 ? 0.2463 0.2600 0.2493 -0.0428 -0.0693 -0.0027 247 THR A OG1 
1997 C CG2 . THR A 247 ? 0.2336 0.2488 0.2208 -0.0400 -0.0683 0.0008  247 THR A CG2 
1998 N N   . GLN A 248 ? 0.1966 0.2040 0.1883 -0.0309 -0.0371 -0.0119 248 GLN A N   
1999 C CA  . GLN A 248 ? 0.1871 0.1914 0.1812 -0.0300 -0.0284 -0.0157 248 GLN A CA  
2000 C C   . GLN A 248 ? 0.2102 0.2080 0.1921 -0.0374 -0.0277 -0.0200 248 GLN A C   
2001 O O   . GLN A 248 ? 0.2361 0.2319 0.2048 -0.0426 -0.0320 -0.0199 248 GLN A O   
2002 C CB  . GLN A 248 ? 0.1993 0.2046 0.1935 -0.0239 -0.0181 -0.0144 248 GLN A CB  
2003 C CG  . GLN A 248 ? 0.1929 0.2034 0.1956 -0.0178 -0.0184 -0.0104 248 GLN A CG  
2004 C CD  . GLN A 248 ? 0.1855 0.1975 0.2018 -0.0157 -0.0185 -0.0114 248 GLN A CD  
2005 O OE1 . GLN A 248 ? 0.2194 0.2300 0.2413 -0.0154 -0.0133 -0.0137 248 GLN A OE1 
2006 N NE2 . GLN A 248 ? 0.1832 0.1977 0.2058 -0.0144 -0.0242 -0.0096 248 GLN A NE2 
2007 N N   . PRO A 249 ? 0.2163 0.2101 0.2016 -0.0384 -0.0221 -0.0242 249 PRO A N   
2008 C CA  . PRO A 249 ? 0.2460 0.2319 0.2187 -0.0466 -0.0213 -0.0295 249 PRO A CA  
2009 C C   . PRO A 249 ? 0.2464 0.2276 0.2045 -0.0474 -0.0131 -0.0313 249 PRO A C   
2010 O O   . PRO A 249 ? 0.2449 0.2274 0.2075 -0.0409 -0.0036 -0.0299 249 PRO A O   
2011 C CB  . PRO A 249 ? 0.2646 0.2475 0.2472 -0.0453 -0.0146 -0.0331 249 PRO A CB  
2012 C CG  . PRO A 249 ? 0.2491 0.2397 0.2505 -0.0388 -0.0173 -0.0289 249 PRO A CG  
2013 C CD  . PRO A 249 ? 0.2286 0.2249 0.2298 -0.0328 -0.0172 -0.0241 249 PRO A CD  
2014 N N   . LEU A 250 ? 0.2603 0.2358 0.2012 -0.0561 -0.0166 -0.0341 250 LEU A N   
2015 C CA  . LEU A 250 ? 0.2695 0.2390 0.1956 -0.0578 -0.0074 -0.0366 250 LEU A CA  
2016 C C   . LEU A 250 ? 0.2701 0.2318 0.1975 -0.0568 0.0068  -0.0425 250 LEU A C   
2017 O O   . LEU A 250 ? 0.2971 0.2563 0.2226 -0.0534 0.0182  -0.0426 250 LEU A O   
2018 C CB  . LEU A 250 ? 0.3272 0.2917 0.2327 -0.0688 -0.0148 -0.0387 250 LEU A CB  
2019 C CG  . LEU A 250 ? 0.3563 0.3157 0.2449 -0.0712 -0.0070 -0.0400 250 LEU A CG  
2020 C CD1 . LEU A 250 ? 0.3103 0.2776 0.2066 -0.0623 -0.0048 -0.0331 250 LEU A CD1 
2021 C CD2 . LEU A 250 ? 0.4025 0.3578 0.2699 -0.0833 -0.0164 -0.0413 250 LEU A CD2 
2022 N N   . LYS A 251 ? 0.2677 0.2255 0.2001 -0.0596 0.0068  -0.0469 251 LYS A N   
2023 C CA  . LYS A 251 ? 0.2892 0.2386 0.2235 -0.0593 0.0201  -0.0528 251 LYS A CA  
2024 C C   . LYS A 251 ? 0.3350 0.2735 0.2499 -0.0655 0.0289  -0.0585 251 LYS A C   
2025 O O   . LYS A 251 ? 0.3606 0.2943 0.2564 -0.0751 0.0219  -0.0614 251 LYS A O   
2026 C CB  . LYS A 251 ? 0.3064 0.2619 0.2605 -0.0483 0.0290  -0.0484 251 LYS A CB  
2027 C CG  . LYS A 251 ? 0.3501 0.3150 0.3209 -0.0437 0.0203  -0.0437 251 LYS A CG  
2028 C CD  . LYS A 251 ? 0.3437 0.3137 0.3331 -0.0347 0.0286  -0.0401 251 LYS A CD  
2029 C CE  . LYS A 251 ? 0.3884 0.3665 0.3912 -0.0312 0.0206  -0.0362 251 LYS A CE  
2030 N NZ  . LYS A 251 ? 0.3964 0.3797 0.4153 -0.0235 0.0282  -0.0321 251 LYS A NZ  
2031 N N   . ASN A 252 ? 0.3223 0.2564 0.2422 -0.0607 0.0445  -0.0601 252 ASN A N   
2032 C CA  . ASN A 252 ? 0.3644 0.2857 0.2677 -0.0666 0.0562  -0.0672 252 ASN A CA  
2033 C C   . ASN A 252 ? 0.4017 0.3262 0.2996 -0.0636 0.0599  -0.0624 252 ASN A C   
2034 O O   . ASN A 252 ? 0.4517 0.3740 0.3567 -0.0582 0.0742  -0.0613 252 ASN A O   
2035 C CB  . ASN A 252 ? 0.4163 0.3297 0.3307 -0.0635 0.0724  -0.0719 252 ASN A CB  
2036 C CG  . ASN A 252 ? 0.5053 0.4028 0.4018 -0.0711 0.0850  -0.0813 252 ASN A CG  
2037 O OD1 . ASN A 252 ? 0.5100 0.4016 0.3828 -0.0803 0.0806  -0.0850 252 ASN A OD1 
2038 N ND2 . ASN A 252 ? 0.5592 0.4489 0.4666 -0.0678 0.1015  -0.0849 252 ASN A ND2 
2039 N N   . ARG A 253 ? 0.3350 0.2654 0.2226 -0.0669 0.0464  -0.0584 253 ARG A N   
2040 C CA  . ARG A 253 ? 0.3408 0.2752 0.2218 -0.0652 0.0468  -0.0533 253 ARG A CA  
2041 C C   . ARG A 253 ? 0.3771 0.3076 0.2341 -0.0761 0.0373  -0.0555 253 ARG A C   
2042 O O   . ARG A 253 ? 0.4195 0.3484 0.2689 -0.0838 0.0262  -0.0583 253 ARG A O   
2043 C CB  . ARG A 253 ? 0.3152 0.2641 0.2127 -0.0560 0.0386  -0.0430 253 ARG A CB  
2044 C CG  . ARG A 253 ? 0.2939 0.2473 0.2131 -0.0460 0.0479  -0.0390 253 ARG A CG  
2045 C CD  . ARG A 253 ? 0.2785 0.2450 0.2109 -0.0387 0.0391  -0.0297 253 ARG A CD  
2046 N NE  . ARG A 253 ? 0.2631 0.2341 0.1996 -0.0395 0.0266  -0.0298 253 ARG A NE  
2047 C CZ  . ARG A 253 ? 0.2362 0.2167 0.1816 -0.0349 0.0178  -0.0236 253 ARG A CZ  
2048 N NH1 . ARG A 253 ? 0.2375 0.2238 0.1862 -0.0302 0.0184  -0.0169 253 ARG A NH1 
2049 N NH2 . ARG A 253 ? 0.2290 0.2125 0.1802 -0.0354 0.0088  -0.0241 253 ARG A NH2 
2050 N N   . GLN A 254 ? 0.3710 0.3008 0.2174 -0.0768 0.0416  -0.0533 254 GLN A N   
2051 C CA  . GLN A 254 ? 0.4424 0.3691 0.2652 -0.0871 0.0338  -0.0543 254 GLN A CA  
2052 C C   . GLN A 254 ? 0.4238 0.3620 0.2515 -0.0822 0.0262  -0.0445 254 GLN A C   
2053 O O   . GLN A 254 ? 0.4533 0.3956 0.2925 -0.0736 0.0349  -0.0398 254 GLN A O   
2054 C CB  . GLN A 254 ? 0.5316 0.4439 0.3333 -0.0945 0.0487  -0.0623 254 GLN A CB  
2055 C CG  . GLN A 254 ? 0.6519 0.5513 0.4508 -0.0982 0.0595  -0.0725 254 GLN A CG  
2056 C CD  . GLN A 254 ? 0.7666 0.6506 0.5479 -0.1035 0.0781  -0.0808 254 GLN A CD  
2057 O OE1 . GLN A 254 ? 0.8435 0.7139 0.6033 -0.1152 0.0805  -0.0905 254 GLN A OE1 
2058 N NE2 . GLN A 254 ? 0.7873 0.6728 0.5780 -0.0955 0.0916  -0.0769 254 GLN A NE2 
2059 N N   . ILE A 255 ? 0.3817 0.3255 0.2027 -0.0876 0.0096  -0.0406 255 ILE A N   
2060 C CA  . ILE A 255 ? 0.3675 0.3209 0.1910 -0.0845 0.0019  -0.0318 255 ILE A CA  
2061 C C   . ILE A 255 ? 0.3893 0.3364 0.1893 -0.0929 0.0054  -0.0333 255 ILE A C   
2062 O O   . ILE A 255 ? 0.4288 0.3685 0.2084 -0.1047 0.0015  -0.0382 255 ILE A O   
2063 C CB  . ILE A 255 ? 0.3532 0.3161 0.1849 -0.0852 -0.0168 -0.0261 255 ILE A CB  
2064 C CG1 . ILE A 255 ? 0.3696 0.3377 0.2239 -0.0768 -0.0180 -0.0254 255 ILE A CG1 
2065 C CG2 . ILE A 255 ? 0.3573 0.3295 0.1927 -0.0817 -0.0241 -0.0171 255 ILE A CG2 
2066 C CD1 . ILE A 255 ? 0.3546 0.3316 0.2205 -0.0764 -0.0345 -0.0199 255 ILE A CD1 
2067 N N   . LYS A 256 ? 0.3795 0.3289 0.1816 -0.0876 0.0137  -0.0290 256 LYS A N   
2068 C CA  . LYS A 256 ? 0.3896 0.3332 0.1705 -0.0948 0.0190  -0.0298 256 LYS A CA  
2069 C C   . LYS A 256 ? 0.3877 0.3415 0.1677 -0.0953 0.0054  -0.0203 256 LYS A C   
2070 O O   . LYS A 256 ? 0.3894 0.3539 0.1884 -0.0871 -0.0022 -0.0130 256 LYS A O   
2071 C CB  . LYS A 256 ? 0.4065 0.3449 0.1907 -0.0890 0.0392  -0.0310 256 LYS A CB  
2072 C CG  . LYS A 256 ? 0.4392 0.3663 0.2251 -0.0884 0.0554  -0.0403 256 LYS A CG  
2073 C CD  . LYS A 256 ? 0.5202 0.4340 0.2800 -0.1020 0.0554  -0.0508 256 LYS A CD  
2074 C CE  . LYS A 256 ? 0.5986 0.4985 0.3574 -0.1024 0.0742  -0.0610 256 LYS A CE  
2075 N NZ  . LYS A 256 ? 0.6494 0.5357 0.3806 -0.1171 0.0725  -0.0716 256 LYS A NZ  
2076 N N   . ALA A 257 ? 0.4199 0.3698 0.1772 -0.1058 0.0023  -0.0207 257 ALA A N   
2077 C CA  . ALA A 257 ? 0.4261 0.3848 0.1812 -0.1073 -0.0093 -0.0114 257 ALA A CA  
2078 C C   . ALA A 257 ? 0.4303 0.3865 0.1768 -0.1065 0.0032  -0.0094 257 ALA A C   
2079 O O   . ALA A 257 ? 0.4505 0.3953 0.1807 -0.1113 0.0183  -0.0165 257 ALA A O   
2080 C CB  . ALA A 257 ? 0.4389 0.3973 0.1770 -0.1201 -0.0243 -0.0107 257 ALA A CB  
2081 N N   . SER A 258 ? 0.4092 0.3758 0.1673 -0.1006 -0.0026 0.0005  258 SER A N   
2082 C CA  . SER A 258 ? 0.4083 0.3746 0.1604 -0.1000 0.0069  0.0045  258 SER A CA  
2083 C C   . SER A 258 ? 0.4711 0.4345 0.1976 -0.1123 0.0019  0.0053  258 SER A C   
2084 O O   . SER A 258 ? 0.5074 0.4684 0.2256 -0.1133 0.0118  0.0072  258 SER A O   
2085 C CB  . SER A 258 ? 0.3841 0.3630 0.1584 -0.0899 0.0006  0.0154  258 SER A CB  
2086 O OG  . SER A 258 ? 0.4014 0.3883 0.1749 -0.0937 -0.0181 0.0220  258 SER A OG  
2087 N N   . PHE A 259 ? 0.4580 0.4230 0.1835 -0.1185 -0.0131 0.0046  259 PHE A N   
2088 C CA  . PHE A 259 ? 0.4958 0.4615 0.2130 -0.1264 -0.0204 0.0075  259 PHE A CA  
2089 C C   . PHE A 259 ? 0.5329 0.4879 0.2334 -0.1369 -0.0186 -0.0011 259 PHE A C   
2090 O O   . PHE A 259 ? 0.5389 0.4906 0.2417 -0.1375 -0.0200 -0.0064 259 PHE A O   
2091 C CB  . PHE A 259 ? 0.4875 0.4660 0.2246 -0.1236 -0.0394 0.0172  259 PHE A CB  
2092 C CG  . PHE A 259 ? 0.4712 0.4534 0.2242 -0.1207 -0.0496 0.0169  259 PHE A CG  
2093 C CD1 . PHE A 259 ? 0.4554 0.4429 0.2253 -0.1107 -0.0504 0.0184  259 PHE A CD1 
2094 C CD2 . PHE A 259 ? 0.5166 0.4964 0.2670 -0.1283 -0.0575 0.0150  259 PHE A CD2 
2095 C CE1 . PHE A 259 ? 0.4609 0.4515 0.2459 -0.1079 -0.0589 0.0178  259 PHE A CE1 
2096 C CE2 . PHE A 259 ? 0.4783 0.4613 0.2444 -0.1251 -0.0657 0.0150  259 PHE A CE2 
2097 C CZ  . PHE A 259 ? 0.4830 0.4712 0.2665 -0.1147 -0.0660 0.0160  259 PHE A CZ  
2108 N N   . ALA B 2   ? 0.2287 0.1640 0.2627 -0.0042 -0.0128 -0.0148 2   ALA B N   
2109 C CA  . ALA B 2   ? 0.2329 0.1647 0.2690 0.0027  -0.0107 -0.0184 2   ALA B CA  
2110 C C   . ALA B 2   ? 0.2358 0.1767 0.2749 0.0058  -0.0083 -0.0142 2   ALA B C   
2111 O O   . ALA B 2   ? 0.2125 0.1566 0.2530 0.0026  -0.0102 -0.0078 2   ALA B O   
2112 C CB  . ALA B 2   ? 0.2243 0.1544 0.2534 0.0048  -0.0090 -0.0267 2   ALA B CB  
2113 N N   . HIS B 3   ? 0.2177 0.1629 0.2572 0.0114  -0.0043 -0.0171 3   HIS B N   
2114 C CA  . HIS B 3   ? 0.2157 0.1701 0.2601 0.0131  -0.0029 -0.0117 3   HIS B CA  
2115 C C   . HIS B 3   ? 0.2073 0.1690 0.2453 0.0088  -0.0033 -0.0094 3   HIS B C   
2116 O O   . HIS B 3   ? 0.2226 0.1861 0.2532 0.0080  -0.0019 -0.0135 3   HIS B O   
2117 C CB  . HIS B 3   ? 0.2158 0.1743 0.2636 0.0201  0.0024  -0.0147 3   HIS B CB  
2118 C CG  . HIS B 3   ? 0.2753 0.2273 0.3315 0.0259  0.0033  -0.0156 3   HIS B CG  
2119 N ND1 . HIS B 3   ? 0.3222 0.2806 0.3903 0.0313  0.0057  -0.0114 3   HIS B ND1 
2120 C CD2 . HIS B 3   ? 0.2961 0.2352 0.3518 0.0268  0.0014  -0.0192 3   HIS B CD2 
2121 C CE1 . HIS B 3   ? 0.3306 0.2803 0.4051 0.0366  0.0060  -0.0131 3   HIS B CE1 
2122 N NE2 . HIS B 3   ? 0.3063 0.2430 0.3724 0.0338  0.0032  -0.0180 3   HIS B NE2 
2123 N N   . HIS B 4   ? 0.1873 0.1523 0.2274 0.0062  -0.0058 -0.0028 4   HIS B N   
2124 C CA  . HIS B 4   ? 0.1954 0.1646 0.2281 0.0026  -0.0062 -0.0009 4   HIS B CA  
2125 C C   . HIS B 4   ? 0.1880 0.1645 0.2203 0.0051  -0.0033 -0.0016 4   HIS B C   
2126 O O   . HIS B 4   ? 0.1916 0.1722 0.2316 0.0088  -0.0012 -0.0005 4   HIS B O   
2127 C CB  . HIS B 4   ? 0.1959 0.1633 0.2288 -0.0013 -0.0103 0.0060  4   HIS B CB  
2128 C CG  . HIS B 4   ? 0.1885 0.1567 0.2120 -0.0050 -0.0113 0.0080  4   HIS B CG  
2129 N ND1 . HIS B 4   ? 0.1722 0.1384 0.1871 -0.0070 -0.0101 0.0055  4   HIS B ND1 
2130 C CD2 . HIS B 4   ? 0.2020 0.1715 0.2231 -0.0071 -0.0138 0.0126  4   HIS B CD2 
2131 C CE1 . HIS B 4   ? 0.1957 0.1610 0.2025 -0.0092 -0.0111 0.0079  4   HIS B CE1 
2132 N NE2 . HIS B 4   ? 0.1907 0.1570 0.2002 -0.0098 -0.0138 0.0120  4   HIS B NE2 
2133 N N   . TRP B 5   ? 0.1882 0.1666 0.2118 0.0030  -0.0029 -0.0026 5   TRP B N   
2134 C CA  . TRP B 5   ? 0.1956 0.1801 0.2174 0.0044  -0.0004 -0.0025 5   TRP B CA  
2135 C C   . TRP B 5   ? 0.1935 0.1826 0.2210 0.0031  -0.0019 0.0041  5   TRP B C   
2136 O O   . TRP B 5   ? 0.1889 0.1756 0.2189 0.0004  -0.0059 0.0087  5   TRP B O   
2137 C CB  . TRP B 5   ? 0.1931 0.1772 0.2048 0.0026  -0.0007 -0.0042 5   TRP B CB  
2138 C CG  . TRP B 5   ? 0.1825 0.1634 0.1891 -0.0012 -0.0038 -0.0005 5   TRP B CG  
2139 C CD1 . TRP B 5   ? 0.1948 0.1711 0.1980 -0.0031 -0.0052 -0.0007 5   TRP B CD1 
2140 C CD2 . TRP B 5   ? 0.1870 0.1681 0.1906 -0.0034 -0.0057 0.0039  5   TRP B CD2 
2141 N NE1 . TRP B 5   ? 0.2027 0.1755 0.1991 -0.0057 -0.0071 0.0026  5   TRP B NE1 
2142 C CE2 . TRP B 5   ? 0.1865 0.1612 0.1829 -0.0062 -0.0082 0.0054  5   TRP B CE2 
2143 C CE3 . TRP B 5   ? 0.1753 0.1611 0.1814 -0.0038 -0.0054 0.0071  5   TRP B CE3 
2144 C CZ2 . TRP B 5   ? 0.1915 0.1621 0.1810 -0.0091 -0.0110 0.0089  5   TRP B CZ2 
2145 C CZ3 . TRP B 5   ? 0.1918 0.1747 0.1930 -0.0076 -0.0089 0.0115  5   TRP B CZ3 
2146 C CH2 . TRP B 5   ? 0.1998 0.1740 0.1920 -0.0102 -0.0121 0.0120  5   TRP B CH2 
2147 N N   . GLY B 6   ? 0.1872 0.1831 0.2169 0.0048  0.0011  0.0050  6   GLY B N   
2148 C CA  . GLY B 6   ? 0.1805 0.1825 0.2174 0.0027  -0.0006 0.0120  6   GLY B CA  
2149 C C   . GLY B 6   ? 0.1551 0.1644 0.1908 0.0031  0.0031  0.0129  6   GLY B C   
2150 O O   . GLY B 6   ? 0.1736 0.1806 0.1986 0.0028  0.0046  0.0094  6   GLY B O   
2151 N N   . TYR B 7   ? 0.1727 0.1913 0.2202 0.0033  0.0042  0.0186  7   TYR B N   
2152 C CA  . TYR B 7   ? 0.1656 0.1931 0.2143 0.0030  0.0083  0.0213  7   TYR B CA  
2153 C C   . TYR B 7   ? 0.1822 0.2203 0.2437 0.0088  0.0154  0.0218  7   TYR B C   
2154 O O   . TYR B 7   ? 0.2136 0.2624 0.2808 0.0084  0.0193  0.0264  7   TYR B O   
2155 C CB  . TYR B 7   ? 0.1780 0.2081 0.2289 -0.0040 0.0027  0.0296  7   TYR B CB  
2156 C CG  . TYR B 7   ? 0.1688 0.1871 0.2042 -0.0089 -0.0028 0.0284  7   TYR B CG  
2157 C CD1 . TYR B 7   ? 0.1870 0.2027 0.2109 -0.0097 -0.0012 0.0265  7   TYR B CD1 
2158 C CD2 . TYR B 7   ? 0.1930 0.2024 0.2247 -0.0123 -0.0095 0.0295  7   TYR B CD2 
2159 C CE1 . TYR B 7   ? 0.1908 0.1952 0.2013 -0.0129 -0.0058 0.0254  7   TYR B CE1 
2160 C CE2 . TYR B 7   ? 0.2060 0.2042 0.2230 -0.0158 -0.0135 0.0282  7   TYR B CE2 
2161 C CZ  . TYR B 7   ? 0.1869 0.1828 0.1944 -0.0156 -0.0115 0.0261  7   TYR B CZ  
2162 O OH  . TYR B 7   ? 0.2293 0.2136 0.2231 -0.0179 -0.0150 0.0247  7   TYR B OH  
2163 N N   . GLY B 8   ? 0.1850 0.2204 0.2519 0.0144  0.0174  0.0178  8   GLY B N   
2164 C CA  . GLY B 8   ? 0.1806 0.2245 0.2596 0.0215  0.0247  0.0175  8   GLY B CA  
2165 C C   . GLY B 8   ? 0.2144 0.2562 0.2826 0.0266  0.0329  0.0096  8   GLY B C   
2166 O O   . GLY B 8   ? 0.1984 0.2339 0.2506 0.0240  0.0322  0.0054  8   GLY B O   
2167 N N   . LYS B 9   ? 0.2094 0.2559 0.2861 0.0343  0.0404  0.0077  9   LYS B N   
2168 C CA  . LYS B 9   ? 0.2273 0.2719 0.2927 0.0398  0.0492  0.0004  9   LYS B CA  
2169 C C   . LYS B 9   ? 0.2336 0.2620 0.2827 0.0405  0.0468  -0.0094 9   LYS B C   
2170 O O   . LYS B 9   ? 0.2388 0.2630 0.2722 0.0410  0.0502  -0.0151 9   LYS B O   
2171 C CB  . LYS B 9   ? 0.2323 0.2843 0.3107 0.0492  0.0585  0.0000  9   LYS B CB  
2172 C CG  . LYS B 9   ? 0.2759 0.3469 0.3752 0.0492  0.0613  0.0107  9   LYS B CG  
2173 C CD  . LYS B 9   ? 0.3016 0.3811 0.3932 0.0442  0.0647  0.0142  9   LYS B CD  
2174 C CE  . LYS B 9   ? 0.4056 0.5066 0.5185 0.0448  0.0702  0.0249  9   LYS B CE  
2175 N NZ  . LYS B 9   ? 0.4650 0.5749 0.5861 0.0558  0.0838  0.0225  9   LYS B NZ  
2176 N N   . HIS B 10  ? 0.2328 0.2518 0.2852 0.0401  0.0407  -0.0111 10  HIS B N   
2177 C CA  . HIS B 10  ? 0.2301 0.2344 0.2691 0.0401  0.0381  -0.0197 10  HIS B CA  
2178 C C   . HIS B 10  ? 0.2212 0.2208 0.2529 0.0323  0.0299  -0.0188 10  HIS B C   
2179 O O   . HIS B 10  ? 0.2573 0.2486 0.2762 0.0307  0.0279  -0.0248 10  HIS B O   
2180 C CB  . HIS B 10  ? 0.2462 0.2418 0.2929 0.0447  0.0371  -0.0225 10  HIS B CB  
2181 C CG  . HIS B 10  ? 0.2903 0.2880 0.3439 0.0541  0.0457  -0.0248 10  HIS B CG  
2182 N ND1 . HIS B 10  ? 0.3395 0.3425 0.4120 0.0589  0.0467  -0.0196 10  HIS B ND1 
2183 C CD2 . HIS B 10  ? 0.3254 0.3195 0.3685 0.0601  0.0538  -0.0321 10  HIS B CD2 
2184 C CE1 . HIS B 10  ? 0.3616 0.3658 0.4369 0.0684  0.0561  -0.0234 10  HIS B CE1 
2185 N NE2 . HIS B 10  ? 0.3241 0.3228 0.3806 0.0691  0.0610  -0.0312 10  HIS B NE2 
2186 N N   . ASN B 11  ? 0.1974 0.2022 0.2362 0.0275  0.0251  -0.0113 11  ASN B N   
2187 C CA  . ASN B 11  ? 0.1843 0.1838 0.2162 0.0213  0.0182  -0.0107 11  ASN B CA  
2188 C C   . ASN B 11  ? 0.1898 0.1942 0.2162 0.0167  0.0167  -0.0066 11  ASN B C   
2189 O O   . ASN B 11  ? 0.1720 0.1726 0.1937 0.0122  0.0116  -0.0053 11  ASN B O   
2190 C CB  . ASN B 11  ? 0.1938 0.1900 0.2345 0.0192  0.0129  -0.0066 11  ASN B CB  
2191 C CG  . ASN B 11  ? 0.2255 0.2299 0.2774 0.0179  0.0114  0.0017  11  ASN B CG  
2192 O OD1 . ASN B 11  ? 0.2172 0.2304 0.2712 0.0176  0.0140  0.0050  11  ASN B OD1 
2193 N ND2 . ASN B 11  ? 0.2422 0.2436 0.3011 0.0163  0.0065  0.0058  11  ASN B ND2 
2194 N N   . GLY B 12  ? 0.1791 0.1915 0.2056 0.0177  0.0212  -0.0044 12  GLY B N   
2195 C CA  . GLY B 12  ? 0.1941 0.2104 0.2169 0.0128  0.0191  0.0009  12  GLY B CA  
2196 C C   . GLY B 12  ? 0.1962 0.2086 0.2041 0.0113  0.0186  -0.0025 12  GLY B C   
2197 O O   . GLY B 12  ? 0.1955 0.2023 0.1956 0.0132  0.0189  -0.0089 12  GLY B O   
2198 N N   . PRO B 13  ? 0.1786 0.1934 0.1827 0.0075  0.0171  0.0024  13  PRO B N   
2199 C CA  . PRO B 13  ? 0.1805 0.1907 0.1715 0.0058  0.0149  0.0008  13  PRO B CA  
2200 C C   . PRO B 13  ? 0.1816 0.1906 0.1628 0.0088  0.0183  -0.0051 13  PRO B C   
2201 O O   . PRO B 13  ? 0.2004 0.2036 0.1736 0.0083  0.0145  -0.0087 13  PRO B O   
2202 C CB  . PRO B 13  ? 0.2046 0.2188 0.1954 0.0019  0.0145  0.0080  13  PRO B CB  
2203 C CG  . PRO B 13  ? 0.1957 0.2123 0.1983 -0.0006 0.0118  0.0132  13  PRO B CG  
2204 C CD  . PRO B 13  ? 0.1892 0.2091 0.2020 0.0038  0.0150  0.0104  13  PRO B CD  
2205 N N   . GLU B 14  ? 0.1785 0.1924 0.1596 0.0120  0.0249  -0.0063 14  GLU B N   
2206 C CA  . GLU B 14  ? 0.2036 0.2143 0.1712 0.0142  0.0275  -0.0121 14  GLU B CA  
2207 C C   . GLU B 14  ? 0.2200 0.2227 0.1850 0.0162  0.0250  -0.0197 14  GLU B C   
2208 O O   . GLU B 14  ? 0.2458 0.2434 0.1984 0.0167  0.0241  -0.0248 14  GLU B O   
2209 C CB  . GLU B 14  ? 0.2044 0.2215 0.1709 0.0177  0.0364  -0.0119 14  GLU B CB  
2210 C CG  . GLU B 14  ? 0.2157 0.2341 0.1919 0.0231  0.0416  -0.0152 14  GLU B CG  
2211 C CD  . GLU B 14  ? 0.2728 0.2954 0.2440 0.0280  0.0516  -0.0174 14  GLU B CD  
2212 O OE1 . GLU B 14  ? 0.2809 0.3037 0.2375 0.0270  0.0544  -0.0177 14  GLU B OE1 
2213 O OE2 . GLU B 14  ? 0.2973 0.3223 0.2784 0.0335  0.0571  -0.0190 14  GLU B OE2 
2214 N N   . HIS B 15  ? 0.2029 0.2038 0.1789 0.0168  0.0232  -0.0202 15  HIS B N   
2215 C CA  . HIS B 15  ? 0.2127 0.2056 0.1876 0.0178  0.0204  -0.0264 15  HIS B CA  
2216 C C   . HIS B 15  ? 0.2072 0.1970 0.1842 0.0140  0.0136  -0.0254 15  HIS B C   
2217 O O   . HIS B 15  ? 0.2217 0.2058 0.1982 0.0135  0.0107  -0.0297 15  HIS B O   
2218 C CB  . HIS B 15  ? 0.2221 0.2141 0.2079 0.0215  0.0235  -0.0274 15  HIS B CB  
2219 C CG  . HIS B 15  ? 0.2800 0.2750 0.2651 0.0268  0.0316  -0.0292 15  HIS B CG  
2220 N ND1 . HIS B 15  ? 0.3319 0.3224 0.3026 0.0292  0.0351  -0.0355 15  HIS B ND1 
2221 C CD2 . HIS B 15  ? 0.2930 0.2960 0.2898 0.0304  0.0372  -0.0252 15  HIS B CD2 
2222 C CE1 . HIS B 15  ? 0.3470 0.3420 0.3196 0.0346  0.0437  -0.0358 15  HIS B CE1 
2223 N NE2 . HIS B 15  ? 0.3046 0.3081 0.2945 0.0356  0.0452  -0.0293 15  HIS B NE2 
2224 N N   . TRP B 16  ? 0.1885 0.1816 0.1676 0.0111  0.0111  -0.0198 16  TRP B N   
2225 C CA  . TRP B 16  ? 0.1777 0.1680 0.1591 0.0086  0.0062  -0.0189 16  TRP B CA  
2226 C C   . TRP B 16  ? 0.2001 0.1878 0.1756 0.0078  0.0029  -0.0230 16  TRP B C   
2227 O O   . TRP B 16  ? 0.2064 0.1921 0.1861 0.0064  0.0001  -0.0238 16  TRP B O   
2228 C CB  . TRP B 16  ? 0.1746 0.1665 0.1557 0.0063  0.0045  -0.0133 16  TRP B CB  
2229 C CG  . TRP B 16  ? 0.1922 0.1860 0.1807 0.0054  0.0053  -0.0084 16  TRP B CG  
2230 C CD1 . TRP B 16  ? 0.1871 0.1820 0.1846 0.0065  0.0068  -0.0080 16  TRP B CD1 
2231 C CD2 . TRP B 16  ? 0.1857 0.1799 0.1736 0.0026  0.0035  -0.0027 16  TRP B CD2 
2232 N NE1 . TRP B 16  ? 0.1737 0.1711 0.1769 0.0044  0.0056  -0.0019 16  TRP B NE1 
2233 C CE2 . TRP B 16  ? 0.1770 0.1736 0.1739 0.0016  0.0036  0.0011  16  TRP B CE2 
2234 C CE3 . TRP B 16  ? 0.1868 0.1786 0.1671 0.0009  0.0015  -0.0004 16  TRP B CE3 
2235 C CZ2 . TRP B 16  ? 0.1796 0.1762 0.1776 -0.0020 0.0008  0.0072  16  TRP B CZ2 
2236 C CZ3 . TRP B 16  ? 0.1986 0.1888 0.1790 -0.0024 -0.0007 0.0050  16  TRP B CZ3 
2237 C CH2 . TRP B 16  ? 0.1948 0.1876 0.1839 -0.0043 -0.0013 0.0088  16  TRP B CH2 
2238 N N   . HIS B 17  ? 0.1977 0.1857 0.1637 0.0083  0.0028  -0.0248 17  HIS B N   
2239 C CA  . HIS B 17  ? 0.1913 0.1776 0.1522 0.0071  -0.0018 -0.0279 17  HIS B CA  
2240 C C   . HIS B 17  ? 0.2065 0.1883 0.1696 0.0065  -0.0035 -0.0330 17  HIS B C   
2241 O O   . HIS B 17  ? 0.2304 0.2120 0.1939 0.0042  -0.0084 -0.0343 17  HIS B O   
2242 C CB  . HIS B 17  ? 0.2385 0.2246 0.1870 0.0076  -0.0020 -0.0291 17  HIS B CB  
2243 C CG  . HIS B 17  ? 0.2468 0.2301 0.1882 0.0096  0.0025  -0.0333 17  HIS B CG  
2244 N ND1 . HIS B 17  ? 0.3052 0.2823 0.2388 0.0096  0.0007  -0.0397 17  HIS B ND1 
2245 C CD2 . HIS B 17  ? 0.2202 0.2056 0.1622 0.0120  0.0093  -0.0322 17  HIS B CD2 
2246 C CE1 . HIS B 17  ? 0.2967 0.2710 0.2242 0.0126  0.0069  -0.0430 17  HIS B CE1 
2247 N NE2 . HIS B 17  ? 0.2796 0.2603 0.2136 0.0144  0.0125  -0.0382 17  HIS B NE2 
2248 N N   . LYS B 18  ? 0.2068 0.1850 0.1720 0.0084  0.0002  -0.0356 18  LYS B N   
2249 C CA  . LYS B 18  ? 0.1798 0.1509 0.1455 0.0076  -0.0020 -0.0408 18  LYS B CA  
2250 C C   . LYS B 18  ? 0.2136 0.1852 0.1895 0.0044  -0.0056 -0.0385 18  LYS B C   
2251 O O   . LYS B 18  ? 0.2182 0.1851 0.1945 0.0018  -0.0096 -0.0416 18  LYS B O   
2252 C CB  . LYS B 18  ? 0.2232 0.1895 0.1898 0.0116  0.0032  -0.0437 18  LYS B CB  
2253 C CG  . LYS B 18  ? 0.3254 0.2914 0.2808 0.0149  0.0079  -0.0465 18  LYS B CG  
2254 C CD  . LYS B 18  ? 0.3507 0.3140 0.3097 0.0203  0.0145  -0.0486 18  LYS B CD  
2255 C CE  . LYS B 18  ? 0.3819 0.3470 0.3305 0.0242  0.0214  -0.0505 18  LYS B CE  
2256 N NZ  . LYS B 18  ? 0.4461 0.4097 0.4011 0.0307  0.0287  -0.0523 18  LYS B NZ  
2257 N N   . ASP B 19  ? 0.1888 0.1652 0.1719 0.0042  -0.0044 -0.0331 19  ASP B N   
2258 C CA  . ASP B 19  ? 0.1890 0.1663 0.1801 0.0013  -0.0067 -0.0303 19  ASP B CA  
2259 C C   . ASP B 19  ? 0.2129 0.1963 0.2047 0.0003  -0.0079 -0.0266 19  ASP B C   
2260 O O   . ASP B 19  ? 0.2000 0.1856 0.1974 -0.0021 -0.0096 -0.0251 19  ASP B O   
2261 C CB  . ASP B 19  ? 0.1956 0.1712 0.1933 0.0018  -0.0044 -0.0270 19  ASP B CB  
2262 C CG  . ASP B 19  ? 0.2245 0.1937 0.2240 0.0036  -0.0033 -0.0300 19  ASP B CG  
2263 O OD1 . ASP B 19  ? 0.2578 0.2211 0.2583 0.0018  -0.0058 -0.0331 19  ASP B OD1 
2264 O OD2 . ASP B 19  ? 0.2464 0.2163 0.2465 0.0071  0.0002  -0.0294 19  ASP B OD2 
2265 N N   . PHE B 20  ? 0.1879 0.1739 0.1743 0.0022  -0.0068 -0.0250 20  PHE B N   
2266 C CA  . PHE B 20  ? 0.2022 0.1920 0.1884 0.0025  -0.0076 -0.0216 20  PHE B CA  
2267 C C   . PHE B 20  ? 0.2135 0.2050 0.1929 0.0035  -0.0097 -0.0225 20  PHE B C   
2268 O O   . PHE B 20  ? 0.2289 0.2200 0.2022 0.0049  -0.0084 -0.0209 20  PHE B O   
2269 C CB  . PHE B 20  ? 0.2055 0.1940 0.1909 0.0032  -0.0051 -0.0177 20  PHE B CB  
2270 C CG  . PHE B 20  ? 0.1829 0.1689 0.1736 0.0019  -0.0039 -0.0162 20  PHE B CG  
2271 C CD1 . PHE B 20  ? 0.2085 0.1944 0.2024 0.0005  -0.0039 -0.0145 20  PHE B CD1 
2272 C CD2 . PHE B 20  ? 0.1861 0.1703 0.1786 0.0022  -0.0024 -0.0162 20  PHE B CD2 
2273 C CE1 . PHE B 20  ? 0.1713 0.1541 0.1684 -0.0012 -0.0033 -0.0126 20  PHE B CE1 
2274 C CE2 . PHE B 20  ? 0.1782 0.1599 0.1759 0.0010  -0.0023 -0.0141 20  PHE B CE2 
2275 C CZ  . PHE B 20  ? 0.1900 0.1702 0.1891 -0.0011 -0.0031 -0.0122 20  PHE B CZ  
2276 N N   . PRO B 21  ? 0.1831 0.1766 0.1631 0.0023  -0.0136 -0.0245 21  PRO B N   
2277 C CA  . PRO B 21  ? 0.2050 0.1991 0.1766 0.0028  -0.0167 -0.0255 21  PRO B CA  
2278 C C   . PRO B 21  ? 0.2084 0.2050 0.1779 0.0050  -0.0172 -0.0212 21  PRO B C   
2279 O O   . PRO B 21  ? 0.2205 0.2162 0.1812 0.0055  -0.0191 -0.0209 21  PRO B O   
2280 C CB  . PRO B 21  ? 0.2387 0.2348 0.2134 0.0001  -0.0223 -0.0278 21  PRO B CB  
2281 C CG  . PRO B 21  ? 0.2543 0.2523 0.2408 -0.0017 -0.0215 -0.0270 21  PRO B CG  
2282 C CD  . PRO B 21  ? 0.1968 0.1912 0.1844 -0.0005 -0.0160 -0.0262 21  PRO B CD  
2283 N N   A ILE B 22  ? 0.1890 0.1871 0.1647 0.0063  -0.0157 -0.0181 22  ILE B N   
2284 N N   B ILE B 22  ? 0.1888 0.1869 0.1645 0.0063  -0.0157 -0.0181 22  ILE B N   
2285 C CA  A ILE B 22  ? 0.1863 0.1838 0.1589 0.0089  -0.0160 -0.0144 22  ILE B CA  
2286 C CA  B ILE B 22  ? 0.1868 0.1844 0.1595 0.0089  -0.0160 -0.0144 22  ILE B CA  
2287 C C   A ILE B 22  ? 0.2050 0.1977 0.1689 0.0089  -0.0140 -0.0130 22  ILE B C   
2288 C C   B ILE B 22  ? 0.2049 0.1975 0.1688 0.0089  -0.0140 -0.0130 22  ILE B C   
2289 O O   A ILE B 22  ? 0.2164 0.2067 0.1752 0.0103  -0.0152 -0.0099 22  ILE B O   
2290 O O   B ILE B 22  ? 0.2158 0.2061 0.1748 0.0103  -0.0151 -0.0099 22  ILE B O   
2291 C CB  A ILE B 22  ? 0.1901 0.1881 0.1692 0.0108  -0.0138 -0.0123 22  ILE B CB  
2292 C CB  B ILE B 22  ? 0.1902 0.1884 0.1695 0.0108  -0.0139 -0.0123 22  ILE B CB  
2293 C CG1 A ILE B 22  ? 0.1974 0.1936 0.1736 0.0146  -0.0148 -0.0093 22  ILE B CG1 
2294 C CG1 B ILE B 22  ? 0.1970 0.1943 0.1743 0.0146  -0.0152 -0.0094 22  ILE B CG1 
2295 C CG2 A ILE B 22  ? 0.1921 0.1853 0.1701 0.0095  -0.0099 -0.0121 22  ILE B CG2 
2296 C CG2 B ILE B 22  ? 0.1931 0.1862 0.1709 0.0097  -0.0099 -0.0119 22  ILE B CG2 
2297 C CD1 A ILE B 22  ? 0.2101 0.2119 0.1889 0.0162  -0.0196 -0.0084 22  ILE B CD1 
2298 C CD1 B ILE B 22  ? 0.1955 0.1917 0.1768 0.0174  -0.0119 -0.0081 22  ILE B CD1 
2299 N N   . ALA B 23  ? 0.1956 0.1869 0.1583 0.0073  -0.0110 -0.0146 23  ALA B N   
2300 C CA  . ALA B 23  ? 0.2112 0.2007 0.1674 0.0069  -0.0087 -0.0126 23  ALA B CA  
2301 C C   . ALA B 23  ? 0.2137 0.2031 0.1604 0.0071  -0.0108 -0.0116 23  ALA B C   
2302 O O   . ALA B 23  ? 0.2238 0.2116 0.1652 0.0065  -0.0095 -0.0080 23  ALA B O   
2303 C CB  . ALA B 23  ? 0.2180 0.2082 0.1757 0.0063  -0.0049 -0.0151 23  ALA B CB  
2304 N N   . LYS B 24  ? 0.2153 0.2062 0.1596 0.0073  -0.0144 -0.0142 24  LYS B N   
2305 C CA  . LYS B 24  ? 0.2117 0.2019 0.1454 0.0071  -0.0175 -0.0131 24  LYS B CA  
2306 C C   . LYS B 24  ? 0.2166 0.2075 0.1521 0.0087  -0.0231 -0.0098 24  LYS B C   
2307 O O   . LYS B 24  ? 0.2571 0.2482 0.1859 0.0085  -0.0278 -0.0090 24  LYS B O   
2308 C CB  . LYS B 24  ? 0.2733 0.2633 0.2009 0.0059  -0.0188 -0.0182 24  LYS B CB  
2309 C CG  . LYS B 24  ? 0.3143 0.3027 0.2384 0.0059  -0.0122 -0.0212 24  LYS B CG  
2310 C CD  . LYS B 24  ? 0.4012 0.3862 0.3149 0.0053  -0.0128 -0.0270 24  LYS B CD  
2311 C CE  . LYS B 24  ? 0.4675 0.4507 0.3791 0.0069  -0.0052 -0.0304 24  LYS B CE  
2312 N NZ  . LYS B 24  ? 0.5045 0.4898 0.4090 0.0078  0.0011  -0.0269 24  LYS B NZ  
2313 N N   . GLY B 25  ? 0.2359 0.2266 0.1797 0.0106  -0.0224 -0.0078 25  GLY B N   
2314 C CA  . GLY B 25  ? 0.2325 0.2243 0.1810 0.0136  -0.0263 -0.0052 25  GLY B CA  
2315 C C   . GLY B 25  ? 0.2664 0.2530 0.2068 0.0151  -0.0287 -0.0005 25  GLY B C   
2316 O O   . GLY B 25  ? 0.2603 0.2430 0.1909 0.0129  -0.0276 0.0013  25  GLY B O   
2317 N N   . GLU B 26  ? 0.2246 0.2112 0.1700 0.0190  -0.0317 0.0020  26  GLU B N   
2318 C CA  . GLU B 26  ? 0.2717 0.2523 0.2105 0.0212  -0.0354 0.0069  26  GLU B CA  
2319 C C   . GLU B 26  ? 0.2742 0.2447 0.2095 0.0225  -0.0326 0.0091  26  GLU B C   
2320 O O   . GLU B 26  ? 0.3248 0.2876 0.2529 0.0235  -0.0356 0.0135  26  GLU B O   
2321 C CB  . GLU B 26  ? 0.2937 0.2794 0.2410 0.0259  -0.0405 0.0087  26  GLU B CB  
2322 C CG  . GLU B 26  ? 0.3094 0.3040 0.2592 0.0236  -0.0457 0.0074  26  GLU B CG  
2323 C CD  . GLU B 26  ? 0.4223 0.4129 0.3568 0.0198  -0.0491 0.0087  26  GLU B CD  
2324 O OE1 . GLU B 26  ? 0.4567 0.4411 0.3835 0.0211  -0.0519 0.0136  26  GLU B OE1 
2325 O OE2 . GLU B 26  ? 0.4787 0.4714 0.4080 0.0156  -0.0485 0.0049  26  GLU B OE2 
2326 N N   . ARG B 27  ? 0.2469 0.2160 0.1864 0.0223  -0.0278 0.0066  27  ARG B N   
2327 C CA  A ARG B 27  ? 0.2506 0.2088 0.1861 0.0234  -0.0261 0.0082  27  ARG B CA  
2328 C CA  B ARG B 27  ? 0.2475 0.2052 0.1821 0.0231  -0.0263 0.0085  27  ARG B CA  
2329 C C   . ARG B 27  ? 0.2276 0.1840 0.1613 0.0185  -0.0222 0.0069  27  ARG B C   
2330 O O   . ARG B 27  ? 0.2600 0.2118 0.1948 0.0191  -0.0198 0.0055  27  ARG B O   
2331 C CB  A ARG B 27  ? 0.2677 0.2250 0.2100 0.0296  -0.0247 0.0067  27  ARG B CB  
2332 C CB  B ARG B 27  ? 0.2695 0.2235 0.2088 0.0294  -0.0255 0.0078  27  ARG B CB  
2333 C CG  A ARG B 27  ? 0.3020 0.2447 0.2375 0.0325  -0.0238 0.0077  27  ARG B CG  
2334 C CG  B ARG B 27  ? 0.2587 0.2168 0.2033 0.0350  -0.0293 0.0096  27  ARG B CG  
2335 C CD  A ARG B 27  ? 0.2704 0.2135 0.2127 0.0398  -0.0206 0.0056  27  ARG B CD  
2336 C CD  B ARG B 27  ? 0.2537 0.2057 0.2017 0.0426  -0.0272 0.0094  27  ARG B CD  
2337 N NE  A ARG B 27  ? 0.1873 0.1190 0.1227 0.0399  -0.0166 0.0035  27  ARG B NE  
2338 N NE  B ARG B 27  ? 0.2592 0.2146 0.2134 0.0441  -0.0210 0.0057  27  ARG B NE  
2339 C CZ  A ARG B 27  ? 0.2793 0.2046 0.2139 0.0465  -0.0132 0.0019  27  ARG B CZ  
2340 C CZ  B ARG B 27  ? 0.2701 0.2394 0.2373 0.0455  -0.0189 0.0041  27  ARG B CZ  
2341 N NH1 A ARG B 27  ? 0.3170 0.2476 0.2601 0.0544  -0.0127 0.0025  27  ARG B NH1 
2342 N NH1 B ARG B 27  ? 0.2346 0.2061 0.2059 0.0465  -0.0128 0.0015  27  ARG B NH1 
2343 N NH2 A ARG B 27  ? 0.3186 0.2322 0.2438 0.0454  -0.0103 -0.0003 27  ARG B NH2 
2344 N NH2 B ARG B 27  ? 0.2840 0.2653 0.2595 0.0450  -0.0234 0.0056  27  ARG B NH2 
2345 N N   . GLN B 28  ? 0.2352 0.1959 0.1664 0.0140  -0.0215 0.0073  28  GLN B N   
2346 C CA  . GLN B 28  ? 0.2226 0.1843 0.1554 0.0100  -0.0179 0.0066  28  GLN B CA  
2347 C C   . GLN B 28  ? 0.2443 0.1980 0.1709 0.0063  -0.0186 0.0111  28  GLN B C   
2348 O O   . GLN B 28  ? 0.2601 0.2087 0.1799 0.0054  -0.0212 0.0151  28  GLN B O   
2349 C CB  . GLN B 28  ? 0.2286 0.1993 0.1631 0.0078  -0.0158 0.0046  28  GLN B CB  
2350 C CG  . GLN B 28  ? 0.2181 0.1953 0.1593 0.0099  -0.0157 -0.0002 28  GLN B CG  
2351 C CD  . GLN B 28  ? 0.2054 0.1827 0.1540 0.0099  -0.0131 -0.0023 28  GLN B CD  
2352 O OE1 . GLN B 28  ? 0.2032 0.1815 0.1538 0.0074  -0.0105 -0.0027 28  GLN B OE1 
2353 N NE2 . GLN B 28  ? 0.2114 0.1883 0.1643 0.0127  -0.0136 -0.0032 28  GLN B NE2 
2354 N N   . SER B 29  ? 0.2259 0.1786 0.1553 0.0034  -0.0168 0.0110  29  SER B N   
2355 C CA  . SER B 29  ? 0.2149 0.1609 0.1406 -0.0014 -0.0182 0.0155  29  SER B CA  
2356 C C   . SER B 29  ? 0.2421 0.1970 0.1747 -0.0053 -0.0153 0.0165  29  SER B C   
2357 O O   . SER B 29  ? 0.2267 0.1891 0.1662 -0.0037 -0.0124 0.0127  29  SER B O   
2358 C CB  . SER B 29  ? 0.2472 0.1811 0.1691 -0.0009 -0.0201 0.0147  29  SER B CB  
2359 O OG  . SER B 29  ? 0.2554 0.1805 0.1715 0.0040  -0.0220 0.0139  29  SER B OG  
2360 N N   . PRO B 30  ? 0.2230 0.1773 0.1550 -0.0106 -0.0162 0.0220  30  PRO B N   
2361 C CA  . PRO B 30  ? 0.2308 0.1753 0.1549 -0.0141 -0.0202 0.0274  30  PRO B CA  
2362 C C   . PRO B 30  ? 0.2430 0.1908 0.1625 -0.0136 -0.0195 0.0298  30  PRO B C   
2363 O O   . PRO B 30  ? 0.2530 0.2101 0.1744 -0.0105 -0.0160 0.0267  30  PRO B O   
2364 C CB  . PRO B 30  ? 0.2468 0.1944 0.1763 -0.0208 -0.0207 0.0327  30  PRO B CB  
2365 C CG  . PRO B 30  ? 0.2358 0.2000 0.1759 -0.0196 -0.0147 0.0313  30  PRO B CG  
2366 C CD  . PRO B 30  ? 0.2444 0.2092 0.1857 -0.0136 -0.0131 0.0238  30  PRO B CD  
2367 N N   . VAL B 31  ? 0.2388 0.1771 0.1506 -0.0166 -0.0233 0.0352  31  VAL B N   
2368 C CA  . VAL B 31  ? 0.2501 0.1896 0.1555 -0.0173 -0.0236 0.0392  31  VAL B CA  
2369 C C   . VAL B 31  ? 0.2831 0.2196 0.1861 -0.0250 -0.0253 0.0476  31  VAL B C   
2370 O O   . VAL B 31  ? 0.2969 0.2267 0.2017 -0.0296 -0.0284 0.0503  31  VAL B O   
2371 C CB  . VAL B 31  ? 0.2759 0.2046 0.1733 -0.0122 -0.0279 0.0380  31  VAL B CB  
2372 C CG1 . VAL B 31  ? 0.2896 0.2233 0.1915 -0.0052 -0.0265 0.0306  31  VAL B CG1 
2373 C CG2 . VAL B 31  ? 0.3037 0.2143 0.1956 -0.0129 -0.0333 0.0398  31  VAL B CG2 
2374 N N   . ASP B 32  ? 0.2798 0.2209 0.1781 -0.0271 -0.0237 0.0524  32  ASP B N   
2375 C CA  . ASP B 32  ? 0.2867 0.2231 0.1812 -0.0345 -0.0261 0.0615  32  ASP B CA  
2376 C C   . ASP B 32  ? 0.3197 0.2364 0.2036 -0.0340 -0.0339 0.0636  32  ASP B C   
2377 O O   . ASP B 32  ? 0.3473 0.2588 0.2250 -0.0279 -0.0358 0.0607  32  ASP B O   
2378 C CB  . ASP B 32  ? 0.2699 0.2177 0.1612 -0.0368 -0.0211 0.0663  32  ASP B CB  
2379 C CG  . ASP B 32  ? 0.3070 0.2507 0.1946 -0.0455 -0.0233 0.0772  32  ASP B CG  
2380 O OD1 . ASP B 32  ? 0.3153 0.2607 0.2112 -0.0518 -0.0242 0.0815  32  ASP B OD1 
2381 O OD2 . ASP B 32  ? 0.3607 0.3001 0.2376 -0.0467 -0.0248 0.0819  32  ASP B OD2 
2382 N N   . ILE B 33  ? 0.3094 0.2145 0.1915 -0.0405 -0.0388 0.0688  33  ILE B N   
2383 C CA  . ILE B 33  ? 0.3318 0.2180 0.2057 -0.0398 -0.0454 0.0698  33  ILE B CA  
2384 C C   . ILE B 33  ? 0.3389 0.2275 0.2118 -0.0458 -0.0457 0.0772  33  ILE B C   
2385 O O   . ILE B 33  ? 0.3581 0.2518 0.2368 -0.0538 -0.0454 0.0823  33  ILE B O   
2386 C CB  . ILE B 33  ? 0.3125 0.1856 0.1872 -0.0420 -0.0498 0.0670  33  ILE B CB  
2387 C CG1 . ILE B 33  ? 0.3518 0.2233 0.2266 -0.0359 -0.0485 0.0600  33  ILE B CG1 
2388 C CG2 . ILE B 33  ? 0.3675 0.2221 0.2344 -0.0413 -0.0556 0.0670  33  ILE B CG2 
2389 C CD1 . ILE B 33  ? 0.3811 0.2448 0.2572 -0.0392 -0.0513 0.0572  33  ILE B CD1 
2390 N N   . ASP B 34  ? 0.3659 0.2524 0.2318 -0.0421 -0.0463 0.0785  34  ASP B N   
2391 C CA  . ASP B 34  ? 0.3800 0.2672 0.2432 -0.0474 -0.0467 0.0857  34  ASP B CA  
2392 C C   . ASP B 34  ? 0.4384 0.3065 0.2972 -0.0481 -0.0539 0.0865  34  ASP B C   
2393 O O   . ASP B 34  ? 0.4586 0.3148 0.3121 -0.0409 -0.0575 0.0827  34  ASP B O   
2394 C CB  . ASP B 34  ? 0.3870 0.2817 0.2437 -0.0439 -0.0440 0.0872  34  ASP B CB  
2395 C CG  . ASP B 34  ? 0.4174 0.3122 0.2702 -0.0496 -0.0442 0.0950  34  ASP B CG  
2396 O OD1 . ASP B 34  ? 0.4449 0.3255 0.2934 -0.0494 -0.0501 0.0968  34  ASP B OD1 
2397 O OD2 . ASP B 34  ? 0.4411 0.3500 0.2962 -0.0543 -0.0380 0.0990  34  ASP B OD2 
2398 N N   . THR B 35  ? 0.4222 0.3085 0.3451 -0.1028 -0.1372 0.0864  35  THR B N   
2399 C CA  . THR B 35  ? 0.4627 0.3160 0.3655 -0.0999 -0.1398 0.0858  35  THR B CA  
2400 C C   . THR B 35  ? 0.5474 0.3905 0.4409 -0.0911 -0.1441 0.0900  35  THR B C   
2401 O O   . THR B 35  ? 0.6206 0.4338 0.4962 -0.0847 -0.1463 0.0891  35  THR B O   
2402 C CB  . THR B 35  ? 0.4525 0.3025 0.3467 -0.1112 -0.1401 0.0850  35  THR B CB  
2403 O OG1 . THR B 35  ? 0.4535 0.3199 0.3520 -0.1201 -0.1422 0.0906  35  THR B OG1 
2404 C CG2 . THR B 35  ? 0.4236 0.2887 0.3245 -0.1133 -0.1351 0.0809  35  THR B CG2 
2405 N N   . HIS B 36  ? 0.4717 0.3395 0.3763 -0.0899 -0.1444 0.0935  36  HIS B N   
2406 C CA  . HIS B 36  ? 0.5134 0.3748 0.4096 -0.0804 -0.1481 0.0974  36  HIS B CA  
2407 C C   . HIS B 36  ? 0.5188 0.3826 0.4174 -0.0618 -0.1510 0.0940  36  HIS B C   
2408 O O   . HIS B 36  ? 0.5501 0.3986 0.4368 -0.0502 -0.1545 0.0964  36  HIS B O   
2409 C CB  . HIS B 36  ? 0.5546 0.4435 0.4615 -0.0859 -0.1463 0.1016  36  HIS B CB  
2410 C CG  . HIS B 36  ? 0.6774 0.5729 0.5875 -0.1032 -0.1434 0.1042  36  HIS B CG  
2411 N ND1 . HIS B 36  ? 0.6805 0.6067 0.6075 -0.1090 -0.1378 0.1045  36  HIS B ND1 
2412 C CD2 . HIS B 36  ? 0.7294 0.6072 0.6283 -0.1145 -0.1455 0.1056  36  HIS B CD2 
2413 C CE1 . HIS B 36  ? 0.7050 0.6323 0.6320 -0.1232 -0.1368 0.1073  36  HIS B CE1 
2414 N NE2 . HIS B 36  ? 0.7114 0.6123 0.6222 -0.1271 -0.1426 0.1072  36  HIS B NE2 
2415 N N   . THR B 37  ? 0.4338 0.3218 0.3521 -0.0579 -0.1460 0.0849  37  THR B N   
2416 C CA  . THR B 37  ? 0.3968 0.2994 0.3269 -0.0408 -0.1432 0.0763  37  THR B CA  
2417 C C   . THR B 37  ? 0.3853 0.2745 0.3149 -0.0331 -0.1379 0.0678  37  THR B C   
2418 O O   . THR B 37  ? 0.4425 0.3363 0.3756 -0.0169 -0.1368 0.0627  37  THR B O   
2419 C CB  . THR B 37  ? 0.3976 0.3432 0.3535 -0.0410 -0.1395 0.0701  37  THR B CB  
2420 O OG1 . THR B 37  ? 0.4193 0.3755 0.3863 -0.0528 -0.1339 0.0659  37  THR B OG1 
2421 C CG2 . THR B 37  ? 0.4178 0.3774 0.3722 -0.0442 -0.1451 0.0780  37  THR B CG2 
2422 N N   . ALA B 38  ? 0.4046 0.2799 0.3301 -0.0437 -0.1346 0.0662  38  ALA B N   
2423 C CA  . ALA B 38  ? 0.4237 0.2828 0.3446 -0.0363 -0.1298 0.0590  38  ALA B CA  
2424 C C   . ALA B 38  ? 0.5113 0.3355 0.4081 -0.0234 -0.1346 0.0619  38  ALA B C   
2425 O O   . ALA B 38  ? 0.6056 0.4026 0.4815 -0.0289 -0.1419 0.0711  38  ALA B O   
2426 C CB  . ALA B 38  ? 0.3984 0.2442 0.3141 -0.0511 -0.1272 0.0590  38  ALA B CB  
2427 N N   . LYS B 39  ? 0.4567 0.2821 0.3559 -0.0059 -0.1306 0.0544  39  LYS B N   
2428 C CA  . LYS B 39  ? 0.4895 0.2849 0.3669 0.0110  -0.1347 0.0561  39  LYS B CA  
2429 C C   . LYS B 39  ? 0.5156 0.2827 0.3776 0.0183  -0.1306 0.0500  39  LYS B C   
2430 O O   . LYS B 39  ? 0.4639 0.2507 0.3411 0.0214  -0.1224 0.0415  39  LYS B O   
2431 C CB  . LYS B 39  ? 0.5236 0.3476 0.4159 0.0300  -0.1341 0.0532  39  LYS B CB  
2432 C CG  . LYS B 39  ? 0.6248 0.4660 0.5226 0.0276  -0.1406 0.0606  39  LYS B CG  
2433 C CD  . LYS B 39  ? 0.6767 0.5403 0.5838 0.0484  -0.1416 0.0585  39  LYS B CD  
2434 C CE  . LYS B 39  ? 0.7768 0.6055 0.6601 0.0684  -0.1437 0.0591  39  LYS B CE  
2435 N NZ  . LYS B 39  ? 0.8195 0.6681 0.7089 0.0908  -0.1459 0.0588  39  LYS B NZ  
2436 N N   . TYR B 40  ? 0.5451 0.2653 0.3752 0.0224  -0.1365 0.0543  40  TYR B N   
2437 C CA  . TYR B 40  ? 0.5629 0.2523 0.3739 0.0328  -0.1334 0.0481  40  TYR B CA  
2438 C C   . TYR B 40  ? 0.5325 0.2445 0.3563 0.0570  -0.1266 0.0395  40  TYR B C   
2439 O O   . TYR B 40  ? 0.5547 0.2832 0.3858 0.0720  -0.1286 0.0411  40  TYR B O   
2440 C CB  . TYR B 40  ? 0.6071 0.2407 0.3799 0.0350  -0.1422 0.0545  40  TYR B CB  
2441 C CG  . TYR B 40  ? 0.6548 0.2532 0.4037 0.0512  -0.1399 0.0476  40  TYR B CG  
2442 C CD1 . TYR B 40  ? 0.6593 0.2439 0.4005 0.0428  -0.1354 0.0415  40  TYR B CD1 
2443 C CD2 . TYR B 40  ? 0.7013 0.2838 0.4361 0.0754  -0.1412 0.0464  40  TYR B CD2 
2444 C CE1 . TYR B 40  ? 0.7198 0.2764 0.4393 0.0577  -0.1318 0.0337  40  TYR B CE1 
2445 C CE2 . TYR B 40  ? 0.7701 0.3249 0.4837 0.0907  -0.1372 0.0386  40  TYR B CE2 
2446 C CZ  . TYR B 40  ? 0.7609 0.3030 0.4669 0.0820  -0.1326 0.0322  40  TYR B CZ  
2447 O OH  . TYR B 40  ? 0.8181 0.3340 0.5020 0.0979  -0.1286 0.0242  40  TYR B OH  
2448 N N   . ASP B 41  ? 0.5272 0.2430 0.3545 0.0605  -0.1183 0.0309  41  ASP B N   
2449 C CA  . ASP B 41  ? 0.5382 0.2786 0.3784 0.0822  -0.1105 0.0228  41  ASP B CA  
2450 C C   . ASP B 41  ? 0.5911 0.2904 0.4014 0.0974  -0.1091 0.0184  41  ASP B C   
2451 O O   . ASP B 41  ? 0.5789 0.2649 0.3814 0.0904  -0.1043 0.0136  41  ASP B O   
2452 C CB  . ASP B 41  ? 0.5118 0.2960 0.3829 0.0736  -0.1009 0.0164  41  ASP B CB  
2453 C CG  . ASP B 41  ? 0.5549 0.3724 0.4434 0.0933  -0.0927 0.0089  41  ASP B CG  
2454 O OD1 . ASP B 41  ? 0.5777 0.3836 0.4531 0.1161  -0.0934 0.0077  41  ASP B OD1 
2455 O OD2 . ASP B 41  ? 0.5394 0.3970 0.4557 0.0855  -0.0854 0.0046  41  ASP B OD2 
2456 N N   . PRO B 42  ? 0.6201 0.2980 0.4119 0.1193  -0.1130 0.0195  42  PRO B N   
2457 C CA  . PRO B 42  ? 0.6374 0.2722 0.3974 0.1355  -0.1117 0.0147  42  PRO B CA  
2458 C C   . PRO B 42  ? 0.6436 0.3029 0.4155 0.1485  -0.0998 0.0044  42  PRO B C   
2459 O O   . PRO B 42  ? 0.7182 0.3423 0.4631 0.1598  -0.0976 -0.0008 42  PRO B O   
2460 C CB  . PRO B 42  ? 0.6846 0.2988 0.4267 0.1589  -0.1182 0.0186  42  PRO B CB  
2461 C CG  . PRO B 42  ? 0.6753 0.3411 0.4505 0.1605  -0.1189 0.0224  42  PRO B CG  
2462 C CD  . PRO B 42  ? 0.6202 0.3141 0.4196 0.1319  -0.1183 0.0248  42  PRO B CD  
2463 N N   . SER B 43  ? 0.5856 0.3024 0.3947 0.1478  -0.0923 0.0012  43  SER B N   
2464 C CA  . SER B 43  ? 0.6346 0.3792 0.4571 0.1579  -0.0804 -0.0075 43  SER B CA  
2465 C C   . SER B 43  ? 0.6432 0.3807 0.4642 0.1384  -0.0750 -0.0109 43  SER B C   
2466 O O   . SER B 43  ? 0.6469 0.3955 0.4699 0.1467  -0.0654 -0.0179 43  SER B O   
2467 C CB  . SER B 43  ? 0.6099 0.4195 0.4731 0.1618  -0.0749 -0.0090 43  SER B CB  
2468 O OG  . SER B 43  ? 0.5943 0.4334 0.4835 0.1366  -0.0733 -0.0077 43  SER B OG  
2469 N N   . LEU B 44  ? 0.6076 0.3285 0.4246 0.1136  -0.0808 -0.0058 44  LEU B N   
2470 C CA  . LEU B 44  ? 0.5783 0.2908 0.3918 0.0957  -0.0767 -0.0082 44  LEU B CA  
2471 C C   . LEU B 44  ? 0.6489 0.3133 0.4256 0.1044  -0.0765 -0.0126 44  LEU B C   
2472 O O   . LEU B 44  ? 0.6714 0.2905 0.4173 0.1109  -0.0847 -0.0102 44  LEU B O   
2473 C CB  . LEU B 44  ? 0.5572 0.2615 0.3723 0.0692  -0.0840 -0.0010 44  LEU B CB  
2474 C CG  . LEU B 44  ? 0.5044 0.2555 0.3547 0.0584  -0.0833 0.0021  44  LEU B CG  
2475 C CD1 . LEU B 44  ? 0.5014 0.2429 0.3503 0.0365  -0.0917 0.0103  44  LEU B CD1 
2476 C CD2 . LEU B 44  ? 0.4694 0.2579 0.3450 0.0524  -0.0724 -0.0034 44  LEU B CD2 
2477 N N   . LYS B 45  ? 0.6538 0.3261 0.4317 0.1041  -0.0672 -0.0191 45  LYS B N   
2478 C CA  . LYS B 45  ? 0.6746 0.3013 0.4164 0.1105  -0.0669 -0.0240 45  LYS B CA  
2479 C C   . LYS B 45  ? 0.6464 0.2460 0.3741 0.0847  -0.0726 -0.0207 45  LYS B C   
2480 O O   . LYS B 45  ? 0.5914 0.2155 0.3416 0.0640  -0.0737 -0.0158 45  LYS B O   
2481 C CB  . LYS B 45  ? 0.6839 0.3333 0.4319 0.1246  -0.0538 -0.0324 45  LYS B CB  
2482 C CG  . LYS B 45  ? 0.7469 0.4370 0.5169 0.1479  -0.0469 -0.0351 45  LYS B CG  
2483 C CD  . LYS B 45  ? 0.8803 0.5413 0.6277 0.1711  -0.0532 -0.0348 45  LYS B CD  
2484 C CE  . LYS B 45  ? 0.9415 0.6485 0.7140 0.1938  -0.0477 -0.0361 45  LYS B CE  
2485 N NZ  . LYS B 45  ? 0.9955 0.7207 0.7678 0.2144  -0.0354 -0.0442 45  LYS B NZ  
2486 N N   . PRO B 46  ? 0.6745 0.2243 0.3646 0.0855  -0.0763 -0.0236 46  PRO B N   
2487 C CA  . PRO B 46  ? 0.6783 0.2043 0.3544 0.0605  -0.0820 -0.0207 46  PRO B CA  
2488 C C   . PRO B 46  ? 0.6443 0.2087 0.3460 0.0474  -0.0734 -0.0219 46  PRO B C   
2489 O O   . PRO B 46  ? 0.6274 0.2159 0.3398 0.0593  -0.0623 -0.0282 46  PRO B O   
2490 C CB  . PRO B 46  ? 0.7286 0.2100 0.3654 0.0680  -0.0835 -0.0262 46  PRO B CB  
2491 C CG  . PRO B 46  ? 0.7851 0.2516 0.4089 0.0952  -0.0838 -0.0288 46  PRO B CG  
2492 C CD  . PRO B 46  ? 0.7675 0.2811 0.4254 0.1101  -0.0754 -0.0303 46  PRO B CD  
2493 N N   . LEU B 47  ? 0.6019 0.1722 0.3128 0.0231  -0.0785 -0.0154 47  LEU B N   
2494 C CA  . LEU B 47  ? 0.5662 0.1687 0.2991 0.0094  -0.0716 -0.0155 47  LEU B CA  
2495 C C   . LEU B 47  ? 0.6152 0.1898 0.3221 0.0026  -0.0712 -0.0190 47  LEU B C   
2496 O O   . LEU B 47  ? 0.6739 0.2217 0.3582 -0.0055 -0.0792 -0.0162 47  LEU B O   
2497 C CB  . LEU B 47  ? 0.5891 0.2118 0.3430 -0.0113 -0.0769 -0.0071 47  LEU B CB  
2498 C CG  . LEU B 47  ? 0.5458 0.2028 0.3238 -0.0233 -0.0696 -0.0067 47  LEU B CG  
2499 C CD1 . LEU B 47  ? 0.5170 0.2181 0.3265 -0.0136 -0.0589 -0.0101 47  LEU B CD1 
2500 C CD2 . LEU B 47  ? 0.5757 0.2398 0.3636 -0.0439 -0.0771 0.0017  47  LEU B CD2 
2501 N N   . SER B 48  ? 0.5872 0.1839 0.3040 0.0061  -0.0602 -0.0238 48  SER B N   
2502 C CA  A SER B 48  ? 0.6230 0.1990 0.3172 0.0012  -0.0583 -0.0277 48  SER B CA  
2503 C CA  B SER B 48  ? 0.6227 0.1992 0.3171 0.0014  -0.0580 -0.0278 48  SER B CA  
2504 C C   . SER B 48  ? 0.5796 0.1845 0.2949 -0.0167 -0.0546 -0.0237 48  SER B C   
2505 O O   . SER B 48  ? 0.5616 0.2050 0.3045 -0.0140 -0.0448 -0.0243 48  SER B O   
2506 C CB  A SER B 48  ? 0.6528 0.2272 0.3357 0.0229  -0.0478 -0.0368 48  SER B CB  
2507 C CB  B SER B 48  ? 0.6507 0.2293 0.3365 0.0228  -0.0468 -0.0367 48  SER B CB  
2508 O OG  A SER B 48  ? 0.6857 0.2449 0.3490 0.0172  -0.0451 -0.0402 48  SER B OG  
2509 O OG  B SER B 48  ? 0.7273 0.2720 0.3864 0.0409  -0.0503 -0.0413 48  SER B OG  
2510 N N   . VAL B 49  ? 0.6219 0.2115 0.3252 -0.0346 -0.0623 -0.0191 49  VAL B N   
2511 C CA  . VAL B 49  ? 0.5999 0.2157 0.3204 -0.0501 -0.0595 -0.0146 49  VAL B CA  
2512 C C   . VAL B 49  ? 0.6294 0.2289 0.3263 -0.0511 -0.0575 -0.0178 49  VAL B C   
2513 O O   . VAL B 49  ? 0.6855 0.2745 0.3671 -0.0566 -0.0646 -0.0145 49  VAL B O   
2514 C CB  . VAL B 49  ? 0.6041 0.2456 0.3432 -0.0644 -0.0666 -0.0043 49  VAL B CB  
2515 C CG1 . VAL B 49  ? 0.6089 0.2783 0.3649 -0.0758 -0.0629 -0.0002 49  VAL B CG1 
2516 C CG2 . VAL B 49  ? 0.5867 0.2412 0.3450 -0.0625 -0.0693 -0.0013 49  VAL B CG2 
2517 N N   . SER B 50  ? 0.6233 0.2263 0.3186 -0.0455 -0.0471 -0.0238 50  SER B N   
2518 C CA  . SER B 50  ? 0.6612 0.2418 0.3278 -0.0436 -0.0446 -0.0290 50  SER B CA  
2519 C C   . SER B 50  ? 0.6085 0.2095 0.2862 -0.0576 -0.0411 -0.0245 50  SER B C   
2520 O O   . SER B 50  ? 0.6202 0.2491 0.3152 -0.0532 -0.0294 -0.0253 50  SER B O   
2521 C CB  . SER B 50  ? 0.7339 0.3156 0.3928 -0.0221 -0.0333 -0.0376 50  SER B CB  
2522 O OG  . SER B 50  ? 0.8270 0.3929 0.4780 -0.0070 -0.0361 -0.0412 50  SER B OG  
2523 N N   . TYR B 51  ? 0.5505 0.2704 0.2982 0.0020  -0.0654 -0.0683 51  TYR B N   
2524 C CA  . TYR B 51  ? 0.5365 0.2726 0.2882 -0.0060 -0.0647 -0.0658 51  TYR B CA  
2525 C C   . TYR B 51  ? 0.6046 0.3386 0.3475 -0.0091 -0.0694 -0.0699 51  TYR B C   
2526 O O   . TYR B 51  ? 0.6041 0.3497 0.3505 -0.0175 -0.0709 -0.0669 51  TYR B O   
2527 C CB  . TYR B 51  ? 0.5304 0.2728 0.2962 -0.0194 -0.0667 -0.0568 51  TYR B CB  
2528 C CG  . TYR B 51  ? 0.4762 0.2347 0.2589 -0.0175 -0.0597 -0.0496 51  TYR B CG  
2529 C CD1 . TYR B 51  ? 0.4789 0.2465 0.2645 -0.0054 -0.0522 -0.0510 51  TYR B CD1 
2530 C CD2 . TYR B 51  ? 0.4374 0.2026 0.2331 -0.0279 -0.0608 -0.0415 51  TYR B CD2 
2531 C CE1 . TYR B 51  ? 0.4352 0.2173 0.2361 -0.0044 -0.0468 -0.0448 51  TYR B CE1 
2532 C CE2 . TYR B 51  ? 0.4131 0.1926 0.2228 -0.0261 -0.0550 -0.0357 51  TYR B CE2 
2533 C CZ  . TYR B 51  ? 0.4023 0.1896 0.2147 -0.0147 -0.0483 -0.0374 51  TYR B CZ  
2534 O OH  . TYR B 51  ? 0.4101 0.2111 0.2363 -0.0140 -0.0437 -0.0319 51  TYR B OH  
2535 N N   . ASP B 52  ? 0.6219 0.3416 0.3537 -0.0022 -0.0722 -0.0766 52  ASP B N   
2536 C CA  . ASP B 52  ? 0.6477 0.3637 0.3704 -0.0053 -0.0776 -0.0811 52  ASP B CA  
2537 C C   . ASP B 52  ? 0.6175 0.3524 0.3363 -0.0016 -0.0731 -0.0833 52  ASP B C   
2538 O O   . ASP B 52  ? 0.6677 0.4055 0.3825 -0.0076 -0.0775 -0.0844 52  ASP B O   
2539 C CB  . ASP B 52  ? 0.6915 0.3878 0.4019 0.0030  -0.0811 -0.0888 52  ASP B CB  
2540 C CG  . ASP B 52  ? 0.7819 0.4572 0.4938 -0.0029 -0.0876 -0.0860 52  ASP B CG  
2541 O OD1 . ASP B 52  ? 0.7706 0.4473 0.4932 -0.0144 -0.0896 -0.0780 52  ASP B OD1 
2542 O OD2 . ASP B 52  ? 0.8145 0.4717 0.5164 0.0042  -0.0910 -0.0917 52  ASP B OD2 
2543 N N   . GLN B 53  ? 0.5690 0.3174 0.2885 0.0083  -0.0646 -0.0836 53  GLN B N   
2544 C CA  . GLN B 53  ? 0.5578 0.3243 0.2722 0.0125  -0.0598 -0.0848 53  GLN B CA  
2545 C C   . GLN B 53  ? 0.5684 0.3533 0.2922 0.0086  -0.0548 -0.0772 53  GLN B C   
2546 O O   . GLN B 53  ? 0.5940 0.3982 0.3196 0.0148  -0.0473 -0.0754 53  GLN B O   
2547 C CB  . GLN B 53  ? 0.6044 0.3744 0.3100 0.0280  -0.0535 -0.0912 53  GLN B CB  
2548 C CG  . GLN B 53  ? 0.6347 0.3873 0.3289 0.0327  -0.0587 -0.0994 53  GLN B CG  
2549 C CD  . GLN B 53  ? 0.7170 0.4774 0.4019 0.0478  -0.0524 -0.1059 53  GLN B CD  
2550 O OE1 . GLN B 53  ? 0.7504 0.5150 0.4385 0.0579  -0.0464 -0.1063 53  GLN B OE1 
2551 N NE2 . GLN B 53  ? 0.7841 0.5483 0.4577 0.0495  -0.0536 -0.1107 53  GLN B NE2 
2552 N N   . ALA B 54  ? 0.5357 0.3227 0.2750 -0.0019 -0.0569 -0.0697 54  ALA B N   
2553 C CA  . ALA B 54  ? 0.5083 0.3190 0.2671 -0.0049 -0.0504 -0.0600 54  ALA B CA  
2554 C C   . ALA B 54  ? 0.4904 0.3166 0.2499 -0.0095 -0.0508 -0.0565 54  ALA B C   
2555 O O   . ALA B 54  ? 0.5196 0.3390 0.2711 -0.0162 -0.0583 -0.0586 54  ALA B O   
2556 C CB  . ALA B 54  ? 0.5147 0.3237 0.2885 -0.0140 -0.0527 -0.0536 54  ALA B CB  
2557 N N   . THR B 55  ? 0.4529 0.2996 0.2217 -0.0063 -0.0432 -0.0508 55  THR B N   
2558 C CA  . THR B 55  ? 0.4298 0.2908 0.1984 -0.0095 -0.0434 -0.0466 55  THR B CA  
2559 C C   . THR B 55  ? 0.4127 0.2885 0.2019 -0.0151 -0.0408 -0.0368 55  THR B C   
2560 O O   . THR B 55  ? 0.4000 0.2881 0.1987 -0.0111 -0.0337 -0.0324 55  THR B O   
2561 C CB  . THR B 55  ? 0.4749 0.3465 0.2338 -0.0006 -0.0372 -0.0480 55  THR B CB  
2562 O OG1 . THR B 55  ? 0.5253 0.3827 0.2642 0.0061  -0.0395 -0.0583 55  THR B OG1 
2563 C CG2 . THR B 55  ? 0.4675 0.3534 0.2255 -0.0043 -0.0377 -0.0425 55  THR B CG2 
2564 N N   . SER B 56  ? 0.3702 0.2458 0.1663 -0.0242 -0.0468 -0.0336 56  SER B N   
2565 C CA  . SER B 56  ? 0.3595 0.2499 0.1737 -0.0279 -0.0445 -0.0250 56  SER B CA  
2566 C C   . SER B 56  ? 0.3533 0.2575 0.1673 -0.0274 -0.0432 -0.0203 56  SER B C   
2567 O O   . SER B 56  ? 0.3912 0.2945 0.1916 -0.0271 -0.0464 -0.0228 56  SER B O   
2568 C CB  . SER B 56  ? 0.3344 0.2232 0.1573 -0.0369 -0.0506 -0.0227 56  SER B CB  
2569 O OG  . SER B 56  ? 0.3796 0.2685 0.1953 -0.0424 -0.0577 -0.0234 56  SER B OG  
2570 N N   . LEU B 57  ? 0.3573 0.2736 0.1857 -0.0267 -0.0386 -0.0132 57  LEU B N   
2571 C CA  . LEU B 57  ? 0.3594 0.2876 0.1886 -0.0261 -0.0372 -0.0073 57  LEU B CA  
2572 C C   . LEU B 57  ? 0.3366 0.2731 0.1795 -0.0307 -0.0401 -0.0005 57  LEU B C   
2573 O O   . LEU B 57  ? 0.3347 0.2767 0.1740 -0.0324 -0.0438 0.0027  57  LEU B O   
2574 C CB  . LEU B 57  ? 0.4071 0.3424 0.2395 -0.0206 -0.0291 -0.0043 57  LEU B CB  
2575 C CG  . LEU B 57  ? 0.4628 0.3952 0.2802 -0.0143 -0.0254 -0.0100 57  LEU B CG  
2576 C CD1 . LEU B 57  ? 0.4704 0.4130 0.2953 -0.0099 -0.0171 -0.0060 57  LEU B CD1 
2577 C CD2 . LEU B 57  ? 0.4858 0.4191 0.2858 -0.0136 -0.0283 -0.0118 57  LEU B CD2 
2578 N N   . ARG B 58  ? 0.2976 0.2360 0.1555 -0.0315 -0.0383 0.0018  58  ARG B N   
2579 C CA  . ARG B 58  ? 0.3028 0.2500 0.1737 -0.0333 -0.0399 0.0082  58  ARG B CA  
2580 C C   . ARG B 58  ? 0.2913 0.2383 0.1752 -0.0346 -0.0396 0.0078  58  ARG B C   
2581 O O   . ARG B 58  ? 0.3120 0.2525 0.1956 -0.0337 -0.0371 0.0039  58  ARG B O   
2582 C CB  . ARG B 58  ? 0.3746 0.3281 0.2492 -0.0301 -0.0359 0.0143  58  ARG B CB  
2583 C CG  . ARG B 58  ? 0.4034 0.3560 0.2826 -0.0270 -0.0296 0.0140  58  ARG B CG  
2584 C CD  . ARG B 58  ? 0.4754 0.4344 0.3575 -0.0256 -0.0264 0.0211  58  ARG B CD  
2585 N NE  . ARG B 58  ? 0.5199 0.4817 0.3888 -0.0253 -0.0271 0.0231  58  ARG B NE  
2586 C CZ  . ARG B 58  ? 0.5125 0.4760 0.3707 -0.0227 -0.0226 0.0216  58  ARG B CZ  
2587 N NH1 . ARG B 58  ? 0.4770 0.4397 0.3371 -0.0199 -0.0174 0.0180  58  ARG B NH1 
2588 N NH2 . ARG B 58  ? 0.4829 0.4499 0.3282 -0.0223 -0.0236 0.0236  58  ARG B NH2 
2589 N N   . ILE B 59  ? 0.2704 0.2250 0.1649 -0.0361 -0.0423 0.0118  59  ILE B N   
2590 C CA  . ILE B 59  ? 0.2563 0.2138 0.1634 -0.0366 -0.0418 0.0119  59  ILE B CA  
2591 C C   . ILE B 59  ? 0.2457 0.2097 0.1641 -0.0331 -0.0404 0.0165  59  ILE B C   
2592 O O   . ILE B 59  ? 0.2671 0.2357 0.1858 -0.0323 -0.0429 0.0206  59  ILE B O   
2593 C CB  . ILE B 59  ? 0.2502 0.2111 0.1588 -0.0419 -0.0471 0.0112  59  ILE B CB  
2594 C CG1 . ILE B 59  ? 0.2776 0.2424 0.1976 -0.0425 -0.0456 0.0113  59  ILE B CG1 
2595 C CG2 . ILE B 59  ? 0.2689 0.2394 0.1793 -0.0432 -0.0522 0.0151  59  ILE B CG2 
2596 C CD1 . ILE B 59  ? 0.2932 0.2632 0.2156 -0.0489 -0.0503 0.0115  59  ILE B CD1 
2597 N N   . LEU B 60  ? 0.2574 0.2206 0.1839 -0.0308 -0.0370 0.0157  60  LEU B N   
2598 C CA  . LEU B 60  ? 0.2590 0.2248 0.1947 -0.0272 -0.0358 0.0189  60  LEU B CA  
2599 C C   . LEU B 60  ? 0.2515 0.2213 0.1977 -0.0257 -0.0358 0.0175  60  LEU B C   
2600 O O   . LEU B 60  ? 0.2572 0.2250 0.2036 -0.0265 -0.0338 0.0141  60  LEU B O   
2601 C CB  . LEU B 60  ? 0.2596 0.2204 0.1941 -0.0254 -0.0313 0.0190  60  LEU B CB  
2602 C CG  . LEU B 60  ? 0.2671 0.2278 0.2115 -0.0227 -0.0303 0.0214  60  LEU B CG  
2603 C CD1 . LEU B 60  ? 0.2673 0.2287 0.2130 -0.0219 -0.0330 0.0273  60  LEU B CD1 
2604 C CD2 . LEU B 60  ? 0.2877 0.2453 0.2317 -0.0224 -0.0259 0.0207  60  LEU B CD2 
2605 N N   . ASN B 61  ? 0.2388 0.2141 0.1929 -0.0228 -0.0381 0.0200  61  ASN B N   
2606 C CA  . ASN B 61  ? 0.2010 0.1802 0.1647 -0.0194 -0.0375 0.0181  61  ASN B CA  
2607 C C   . ASN B 61  ? 0.2106 0.1828 0.1775 -0.0162 -0.0352 0.0178  61  ASN B C   
2608 O O   . ASN B 61  ? 0.2379 0.2066 0.2060 -0.0144 -0.0367 0.0211  61  ASN B O   
2609 C CB  . ASN B 61  ? 0.2214 0.2101 0.1919 -0.0164 -0.0413 0.0204  61  ASN B CB  
2610 C CG  . ASN B 61  ? 0.2166 0.2104 0.1963 -0.0111 -0.0406 0.0180  61  ASN B CG  
2611 O OD1 . ASN B 61  ? 0.2232 0.2112 0.2045 -0.0091 -0.0380 0.0153  61  ASN B OD1 
2612 N ND2 . ASN B 61  ? 0.2265 0.2327 0.2122 -0.0087 -0.0429 0.0187  61  ASN B ND2 
2613 N N   . ASN B 62  ? 0.2266 0.1960 0.1941 -0.0163 -0.0321 0.0143  62  ASN B N   
2614 C CA  . ASN B 62  ? 0.2477 0.2112 0.2185 -0.0143 -0.0305 0.0138  62  ASN B CA  
2615 C C   . ASN B 62  ? 0.2192 0.1837 0.1979 -0.0097 -0.0318 0.0113  62  ASN B C   
2616 O O   . ASN B 62  ? 0.2417 0.2012 0.2235 -0.0085 -0.0311 0.0097  62  ASN B O   
2617 C CB  . ASN B 62  ? 0.2184 0.1785 0.1853 -0.0162 -0.0269 0.0114  62  ASN B CB  
2618 C CG  . ASN B 62  ? 0.2442 0.2065 0.2122 -0.0155 -0.0257 0.0074  62  ASN B CG  
2619 O OD1 . ASN B 62  ? 0.2238 0.1915 0.1947 -0.0144 -0.0270 0.0066  62  ASN B OD1 
2620 N ND2 . ASN B 62  ? 0.2267 0.1859 0.1921 -0.0159 -0.0230 0.0053  62  ASN B ND2 
2621 N N   . GLY B 63  ? 0.2162 0.1877 0.1984 -0.0068 -0.0339 0.0109  63  GLY B N   
2622 C CA  . GLY B 63  ? 0.2001 0.1738 0.1888 -0.0010 -0.0349 0.0077  63  GLY B CA  
2623 C C   . GLY B 63  ? 0.2146 0.1929 0.2038 -0.0004 -0.0323 0.0034  63  GLY B C   
2624 O O   . GLY B 63  ? 0.2394 0.2201 0.2327 0.0051  -0.0329 -0.0001 63  GLY B O   
2625 N N   . HIS B 64  ? 0.2201 0.1988 0.2044 -0.0052 -0.0297 0.0035  64  HIS B N   
2626 C CA  . HIS B 64  ? 0.1854 0.1673 0.1686 -0.0055 -0.0273 0.0007  64  HIS B CA  
2627 C C   . HIS B 64  ? 0.2274 0.2151 0.2070 -0.0102 -0.0267 0.0027  64  HIS B C   
2628 O O   . HIS B 64  ? 0.2427 0.2390 0.2239 -0.0099 -0.0257 0.0023  64  HIS B O   
2629 C CB  . HIS B 64  ? 0.1974 0.1711 0.1778 -0.0067 -0.0255 -0.0010 64  HIS B CB  
2630 C CG  . HIS B 64  ? 0.1978 0.1651 0.1819 -0.0043 -0.0267 -0.0021 64  HIS B CG  
2631 N ND1 . HIS B 64  ? 0.2048 0.1720 0.1936 0.0005  -0.0284 -0.0055 64  HIS B ND1 
2632 C CD2 . HIS B 64  ? 0.2119 0.1727 0.1955 -0.0067 -0.0267 0.0000  64  HIS B CD2 
2633 C CE1 . HIS B 64  ? 0.2371 0.1964 0.2285 0.0002  -0.0300 -0.0055 64  HIS B CE1 
2634 N NE2 . HIS B 64  ? 0.2168 0.1732 0.2056 -0.0044 -0.0287 -0.0016 64  HIS B NE2 
2635 N N   . THR B 65  ? 0.2084 0.1916 0.1828 -0.0148 -0.0273 0.0050  65  THR B N   
2636 C CA  . THR B 65  ? 0.2059 0.1913 0.1758 -0.0204 -0.0280 0.0067  65  THR B CA  
2637 C C   . THR B 65  ? 0.2124 0.1942 0.1780 -0.0230 -0.0302 0.0087  65  THR B C   
2638 O O   . THR B 65  ? 0.2248 0.2054 0.1924 -0.0202 -0.0312 0.0099  65  THR B O   
2639 C CB  . THR B 65  ? 0.2101 0.1887 0.1742 -0.0229 -0.0260 0.0052  65  THR B CB  
2640 O OG1 . THR B 65  ? 0.2406 0.2195 0.2002 -0.0290 -0.0276 0.0070  65  THR B OG1 
2641 C CG2 . THR B 65  ? 0.2315 0.1991 0.1901 -0.0222 -0.0247 0.0038  65  THR B CG2 
2642 N N   . PHE B 66  ? 0.2251 0.2046 0.1840 -0.0286 -0.0317 0.0094  66  PHE B N   
2643 C CA  . PHE B 66  ? 0.2152 0.1893 0.1671 -0.0306 -0.0335 0.0102  66  PHE B CA  
2644 C C   . PHE B 66  ? 0.2258 0.1884 0.1678 -0.0324 -0.0320 0.0077  66  PHE B C   
2645 O O   . PHE B 66  ? 0.2378 0.1966 0.1772 -0.0347 -0.0317 0.0063  66  PHE B O   
2646 C CB  . PHE B 66  ? 0.2424 0.2236 0.1938 -0.0350 -0.0380 0.0125  66  PHE B CB  
2647 C CG  . PHE B 66  ? 0.2339 0.2164 0.1833 -0.0413 -0.0397 0.0123  66  PHE B CG  
2648 C CD1 . PHE B 66  ? 0.2517 0.2463 0.2097 -0.0426 -0.0396 0.0140  66  PHE B CD1 
2649 C CD2 . PHE B 66  ? 0.2539 0.2255 0.1926 -0.0461 -0.0415 0.0106  66  PHE B CD2 
2650 C CE1 . PHE B 66  ? 0.2481 0.2441 0.2047 -0.0498 -0.0413 0.0152  66  PHE B CE1 
2651 C CE2 . PHE B 66  ? 0.2654 0.2357 0.2019 -0.0531 -0.0440 0.0109  66  PHE B CE2 
2652 C CZ  . PHE B 66  ? 0.2713 0.2541 0.2171 -0.0557 -0.0440 0.0138  66  PHE B CZ  
2653 N N   . ASN B 67  ? 0.2361 0.1935 0.1729 -0.0305 -0.0309 0.0075  67  ASN B N   
2654 C CA  . ASN B 67  ? 0.2445 0.1924 0.1717 -0.0303 -0.0291 0.0047  67  ASN B CA  
2655 C C   . ASN B 67  ? 0.2751 0.2196 0.1920 -0.0327 -0.0317 0.0043  67  ASN B C   
2656 O O   . ASN B 67  ? 0.2807 0.2296 0.1974 -0.0322 -0.0327 0.0069  67  ASN B O   
2657 C CB  . ASN B 67  ? 0.2553 0.2024 0.1841 -0.0259 -0.0251 0.0046  67  ASN B CB  
2658 C CG  . ASN B 67  ? 0.2672 0.2164 0.2049 -0.0234 -0.0230 0.0040  67  ASN B CG  
2659 O OD1 . ASN B 67  ? 0.2519 0.2018 0.1922 -0.0241 -0.0235 0.0030  67  ASN B OD1 
2660 N ND2 . ASN B 67  ? 0.2866 0.2374 0.2287 -0.0209 -0.0209 0.0051  67  ASN B ND2 
2661 N N   . VAL B 68  ? 0.2663 0.2019 0.1736 -0.0349 -0.0332 0.0009  68  VAL B N   
2662 C CA  . VAL B 68  ? 0.2766 0.2066 0.1714 -0.0361 -0.0358 -0.0011 68  VAL B CA  
2663 C C   . VAL B 68  ? 0.3015 0.2251 0.1884 -0.0308 -0.0317 -0.0044 68  VAL B C   
2664 O O   . VAL B 68  ? 0.3027 0.2188 0.1874 -0.0288 -0.0302 -0.0074 68  VAL B O   
2665 C CB  . VAL B 68  ? 0.3009 0.2235 0.1892 -0.0421 -0.0411 -0.0034 68  VAL B CB  
2666 C CG1 . VAL B 68  ? 0.3383 0.2518 0.2110 -0.0422 -0.0438 -0.0075 68  VAL B CG1 
2667 C CG2 . VAL B 68  ? 0.2962 0.2293 0.1934 -0.0479 -0.0452 0.0005  68  VAL B CG2 
2668 N N   . GLU B 69  ? 0.2965 0.2241 0.1793 -0.0281 -0.0298 -0.0032 69  GLU B N   
2669 C CA  . GLU B 69  ? 0.3248 0.2516 0.2024 -0.0226 -0.0248 -0.0050 69  GLU B CA  
2670 C C   . GLU B 69  ? 0.3229 0.2420 0.1838 -0.0209 -0.0263 -0.0101 69  GLU B C   
2671 O O   . GLU B 69  ? 0.3615 0.2797 0.2150 -0.0241 -0.0307 -0.0103 69  GLU B O   
2672 C CB  . GLU B 69  ? 0.4094 0.3468 0.2929 -0.0212 -0.0216 0.0005  69  GLU B CB  
2673 C CG  . GLU B 69  ? 0.5679 0.5092 0.4491 -0.0164 -0.0158 0.0004  69  GLU B CG  
2674 C CD  . GLU B 69  ? 0.6861 0.6370 0.5684 -0.0169 -0.0136 0.0067  69  GLU B CD  
2675 O OE1 . GLU B 69  ? 0.7028 0.6558 0.5880 -0.0202 -0.0170 0.0111  69  GLU B OE1 
2676 O OE2 . GLU B 69  ? 0.7206 0.6775 0.6007 -0.0137 -0.0087 0.0077  69  GLU B OE2 
2677 N N   . PHE B 70  ? 0.3155 0.2297 0.1703 -0.0152 -0.0229 -0.0144 70  PHE B N   
2678 C CA  . PHE B 70  ? 0.3253 0.2312 0.1632 -0.0112 -0.0236 -0.0206 70  PHE B CA  
2679 C C   . PHE B 70  ? 0.3816 0.2967 0.2157 -0.0042 -0.0172 -0.0206 70  PHE B C   
2680 O O   . PHE B 70  ? 0.3678 0.2929 0.2130 -0.0023 -0.0121 -0.0167 70  PHE B O   
2681 C CB  . PHE B 70  ? 0.3464 0.2372 0.1790 -0.0091 -0.0256 -0.0265 70  PHE B CB  
2682 C CG  . PHE B 70  ? 0.3549 0.2358 0.1879 -0.0167 -0.0324 -0.0267 70  PHE B CG  
2683 C CD1 . PHE B 70  ? 0.3615 0.2474 0.2090 -0.0218 -0.0328 -0.0217 70  PHE B CD1 
2684 C CD2 . PHE B 70  ? 0.3717 0.2393 0.1906 -0.0192 -0.0385 -0.0318 70  PHE B CD2 
2685 C CE1 . PHE B 70  ? 0.3523 0.2320 0.2007 -0.0294 -0.0387 -0.0210 70  PHE B CE1 
2686 C CE2 . PHE B 70  ? 0.3883 0.2480 0.2083 -0.0278 -0.0452 -0.0312 70  PHE B CE2 
2687 C CZ  . PHE B 70  ? 0.3780 0.2453 0.2136 -0.0331 -0.0449 -0.0252 70  PHE B CZ  
2688 N N   . ASP B 71  ? 0.3805 0.2927 0.1985 -0.0006 -0.0176 -0.0251 71  ASP B N   
2689 C CA  . ASP B 71  ? 0.3692 0.2908 0.1814 0.0072  -0.0110 -0.0260 71  ASP B CA  
2690 C C   . ASP B 71  ? 0.3966 0.3125 0.2087 0.0145  -0.0084 -0.0315 71  ASP B C   
2691 O O   . ASP B 71  ? 0.4336 0.3332 0.2349 0.0170  -0.0124 -0.0387 71  ASP B O   
2692 C CB  . ASP B 71  ? 0.4052 0.3245 0.1982 0.0098  -0.0128 -0.0304 71  ASP B CB  
2693 C CG  . ASP B 71  ? 0.4343 0.3666 0.2206 0.0181  -0.0054 -0.0308 71  ASP B CG  
2694 O OD1 . ASP B 71  ? 0.4234 0.3598 0.2148 0.0242  -0.0003 -0.0322 71  ASP B OD1 
2695 O OD2 . ASP B 71  ? 0.4588 0.3985 0.2341 0.0189  -0.0045 -0.0297 71  ASP B OD2 
2696 N N   . ASP B 72  ? 0.3693 0.2971 0.1942 0.0170  -0.0026 -0.0276 72  ASP B N   
2697 C CA  . ASP B 72  ? 0.3347 0.2595 0.1612 0.0244  -0.0001 -0.0319 72  ASP B CA  
2698 C C   . ASP B 72  ? 0.3646 0.3033 0.1871 0.0336  0.0069  -0.0333 72  ASP B C   
2699 O O   . ASP B 72  ? 0.3666 0.3127 0.1973 0.0390  0.0109  -0.0334 72  ASP B O   
2700 C CB  . ASP B 72  ? 0.3261 0.2548 0.1708 0.0208  0.0004  -0.0271 72  ASP B CB  
2701 C CG  . ASP B 72  ? 0.3322 0.2798 0.1907 0.0176  0.0051  -0.0192 72  ASP B CG  
2702 O OD1 . ASP B 72  ? 0.3660 0.3236 0.2209 0.0166  0.0077  -0.0158 72  ASP B OD1 
2703 O OD2 . ASP B 72  ? 0.3344 0.2865 0.2071 0.0157  0.0059  -0.0161 72  ASP B OD2 
2704 N N   . SER B 73  ? 0.3635 0.3070 0.1730 0.0361  0.0084  -0.0347 73  SER B N   
2705 C CA  . SER B 73  ? 0.3765 0.3367 0.1820 0.0448  0.0159  -0.0354 73  SER B CA  
2706 C C   . SER B 73  ? 0.4246 0.3757 0.2160 0.0572  0.0162  -0.0460 73  SER B C   
2707 O O   . SER B 73  ? 0.4322 0.3987 0.2212 0.0665  0.0230  -0.0474 73  SER B O   
2708 C CB  . SER B 73  ? 0.4018 0.3731 0.1988 0.0425  0.0180  -0.0315 73  SER B CB  
2709 O OG  . SER B 73  ? 0.4208 0.3778 0.1979 0.0444  0.0129  -0.0388 73  SER B OG  
2710 N N   . GLN B 74  ? 0.3955 0.3223 0.1769 0.0577  0.0090  -0.0533 74  GLN B N   
2711 C CA  . GLN B 74  ? 0.4222 0.3356 0.1876 0.0696  0.0078  -0.0641 74  GLN B CA  
2712 C C   . GLN B 74  ? 0.4435 0.3348 0.2110 0.0692  0.0016  -0.0675 74  GLN B C   
2713 O O   . GLN B 74  ? 0.4534 0.3368 0.2301 0.0585  -0.0030 -0.0628 74  GLN B O   
2714 C CB  . GLN B 74  ? 0.4641 0.3661 0.2073 0.0716  0.0037  -0.0713 74  GLN B CB  
2715 C CG  . GLN B 74  ? 0.4372 0.3613 0.1756 0.0734  0.0100  -0.0680 74  GLN B CG  
2716 C CD  . GLN B 74  ? 0.5235 0.4366 0.2382 0.0765  0.0057  -0.0762 74  GLN B CD  
2717 O OE1 . GLN B 74  ? 0.5516 0.4471 0.2599 0.0683  -0.0028 -0.0780 74  GLN B OE1 
2718 N NE2 . GLN B 74  ? 0.5654 0.4902 0.2698 0.0876  0.0113  -0.0807 74  GLN B NE2 
2719 N N   . ASP B 75  ? 0.4851 0.3667 0.2432 0.0818  0.0017  -0.0758 75  ASP B N   
2720 C CA  . ASP B 75  ? 0.5207 0.3797 0.2785 0.0833  -0.0041 -0.0791 75  ASP B CA  
2721 C C   . ASP B 75  ? 0.5686 0.3988 0.3104 0.0781  -0.0138 -0.0849 75  ASP B C   
2722 O O   . ASP B 75  ? 0.6333 0.4446 0.3637 0.0849  -0.0182 -0.0923 75  ASP B O   
2723 C CB  . ASP B 75  ? 0.5635 0.4219 0.3165 0.0995  -0.0012 -0.0856 75  ASP B CB  
2724 C CG  . ASP B 75  ? 0.5656 0.4490 0.3377 0.1029  0.0062  -0.0794 75  ASP B CG  
2725 O OD1 . ASP B 75  ? 0.5033 0.4007 0.2922 0.0923  0.0081  -0.0703 75  ASP B OD1 
2726 O OD2 . ASP B 75  ? 0.6123 0.5012 0.3827 0.1169  0.0096  -0.0839 75  ASP B OD2 
2727 N N   . LYS B 76  ? 0.5307 0.3613 0.2761 0.0647  -0.0172 -0.0798 76  LYS B N   
2728 C CA  . LYS B 76  ? 0.5514 0.3578 0.2834 0.0579  -0.0267 -0.0844 76  LYS B CA  
2729 C C   . LYS B 76  ? 0.5789 0.3736 0.3219 0.0467  -0.0321 -0.0789 76  LYS B C   
2730 O O   . LYS B 76  ? 0.6111 0.3840 0.3483 0.0492  -0.0370 -0.0827 76  LYS B O   
2731 C CB  . LYS B 76  ? 0.5757 0.3904 0.3012 0.0518  -0.0277 -0.0837 76  LYS B CB  
2732 C CG  . LYS B 76  ? 0.6127 0.4350 0.3242 0.0634  -0.0236 -0.0905 76  LYS B CG  
2733 C CD  . LYS B 76  ? 0.6062 0.4371 0.3094 0.0582  -0.0249 -0.0899 76  LYS B CD  
2734 C CE  . LYS B 76  ? 0.6251 0.4625 0.3170 0.0692  -0.0215 -0.0966 76  LYS B CE  
2735 N NZ  . LYS B 76  ? 0.6505 0.5028 0.3348 0.0666  -0.0199 -0.0948 76  LYS B NZ  
2736 N N   . ALA B 77  ? 0.4956 0.3046 0.2544 0.0356  -0.0310 -0.0698 77  ALA B N   
2737 C CA  . ALA B 77  ? 0.4727 0.2737 0.2420 0.0256  -0.0354 -0.0644 77  ALA B CA  
2738 C C   . ALA B 77  ? 0.4594 0.2675 0.2413 0.0307  -0.0305 -0.0608 77  ALA B C   
2739 O O   . ALA B 77  ? 0.4269 0.2565 0.2232 0.0304  -0.0243 -0.0551 77  ALA B O   
2740 C CB  . ALA B 77  ? 0.4982 0.3121 0.2786 0.0133  -0.0362 -0.0570 77  ALA B CB  
2741 N N   . VAL B 78  ? 0.4723 0.2618 0.2485 0.0356  -0.0337 -0.0643 78  VAL B N   
2742 C CA  . VAL B 78  ? 0.4669 0.2627 0.2527 0.0426  -0.0295 -0.0620 78  VAL B CA  
2743 C C   . VAL B 78  ? 0.4576 0.2343 0.2436 0.0388  -0.0352 -0.0599 78  VAL B C   
2744 O O   . VAL B 78  ? 0.4999 0.2538 0.2747 0.0340  -0.0425 -0.0624 78  VAL B O   
2745 C CB  . VAL B 78  ? 0.4637 0.2604 0.2414 0.0585  -0.0257 -0.0688 78  VAL B CB  
2746 C CG1 . VAL B 78  ? 0.4741 0.2921 0.2511 0.0627  -0.0192 -0.0701 78  VAL B CG1 
2747 C CG2 . VAL B 78  ? 0.5174 0.2861 0.2763 0.0645  -0.0321 -0.0771 78  VAL B CG2 
2748 N N   . LEU B 79  ? 0.4491 0.2353 0.2471 0.0417  -0.0318 -0.0555 79  LEU B N   
2749 C CA  . LEU B 79  ? 0.4513 0.2224 0.2496 0.0412  -0.0357 -0.0530 79  LEU B CA  
2750 C C   . LEU B 79  ? 0.4804 0.2502 0.2761 0.0561  -0.0334 -0.0568 79  LEU B C   
2751 O O   . LEU B 79  ? 0.4836 0.2755 0.2883 0.0630  -0.0268 -0.0567 79  LEU B O   
2752 C CB  . LEU B 79  ? 0.4707 0.2572 0.2857 0.0319  -0.0338 -0.0443 79  LEU B CB  
2753 C CG  . LEU B 79  ? 0.5115 0.2883 0.3294 0.0276  -0.0373 -0.0390 79  LEU B CG  
2754 C CD1 . LEU B 79  ? 0.5718 0.3254 0.3785 0.0190  -0.0448 -0.0392 79  LEU B CD1 
2755 C CD2 . LEU B 79  ? 0.4172 0.2149 0.2512 0.0197  -0.0340 -0.0320 79  LEU B CD2 
2756 N N   . LYS B 80  ? 0.4773 0.2217 0.2614 0.0612  -0.0391 -0.0598 80  LYS B N   
2757 C CA  . LYS B 80  ? 0.5203 0.2608 0.3006 0.0767  -0.0380 -0.0638 80  LYS B CA  
2758 C C   . LYS B 80  ? 0.5522 0.2692 0.3280 0.0758  -0.0445 -0.0606 80  LYS B C   
2759 O O   . LYS B 80  ? 0.5632 0.2644 0.3357 0.0635  -0.0502 -0.0568 80  LYS B O   
2760 C CB  . LYS B 80  ? 0.6095 0.3420 0.3760 0.0878  -0.0384 -0.0730 80  LYS B CB  
2761 C CG  . LYS B 80  ? 0.6411 0.3938 0.4073 0.0907  -0.0320 -0.0771 80  LYS B CG  
2762 C CD  . LYS B 80  ? 0.6670 0.4178 0.4230 0.1013  -0.0319 -0.0843 80  LYS B CD  
2763 C CE  . LYS B 80  ? 0.7702 0.5239 0.5275 0.1166  -0.0302 -0.0865 80  LYS B CE  
2764 N NZ  . LYS B 80  ? 0.8015 0.5839 0.5714 0.1242  -0.0216 -0.0848 80  LYS B NZ  
2765 N N   . GLY B 81  ? 0.5238 0.2407 0.3006 0.0885  -0.0438 -0.0613 81  GLY B N   
2766 C CA  . GLY B 81  ? 0.5067 0.2049 0.2805 0.0878  -0.0498 -0.0567 81  GLY B CA  
2767 C C   . GLY B 81  ? 0.5105 0.2137 0.2941 0.0784  -0.0498 -0.0478 81  GLY B C   
2768 O O   . GLY B 81  ? 0.4893 0.2201 0.2879 0.0745  -0.0439 -0.0442 81  GLY B O   
2769 N N   . GLY B 82  ? 0.5291 0.2109 0.3070 0.0731  -0.0562 -0.0426 82  GLY B N   
2770 C CA  . GLY B 82  ? 0.5170 0.2062 0.3042 0.0653  -0.0561 -0.0332 82  GLY B CA  
2771 C C   . GLY B 82  ? 0.5089 0.2198 0.3070 0.0759  -0.0513 -0.0321 82  GLY B C   
2772 O O   . GLY B 82  ? 0.5375 0.2417 0.3306 0.0901  -0.0523 -0.0356 82  GLY B O   
2773 N N   . PRO B 83  ? 0.4780 0.2153 0.2911 0.0693  -0.0464 -0.0272 83  PRO B N   
2774 C CA  . PRO B 83  ? 0.4779 0.2379 0.3026 0.0778  -0.0423 -0.0263 83  PRO B CA  
2775 C C   . PRO B 83  ? 0.4915 0.2731 0.3236 0.0856  -0.0363 -0.0325 83  PRO B C   
2776 O O   . PRO B 83  ? 0.5125 0.3151 0.3556 0.0918  -0.0331 -0.0318 83  PRO B O   
2777 C CB  . PRO B 83  ? 0.4228 0.1996 0.2590 0.0658  -0.0404 -0.0193 83  PRO B CB  
2778 C CG  . PRO B 83  ? 0.4174 0.1940 0.2535 0.0537  -0.0396 -0.0197 83  PRO B CG  
2779 C CD  . PRO B 83  ? 0.4525 0.1994 0.2724 0.0538  -0.0451 -0.0226 83  PRO B CD  
2780 N N   . LEU B 84  ? 0.4471 0.2254 0.2737 0.0845  -0.0349 -0.0378 84  LEU B N   
2781 C CA  . LEU B 84  ? 0.4483 0.2501 0.2828 0.0883  -0.0285 -0.0417 84  LEU B CA  
2782 C C   . LEU B 84  ? 0.4347 0.2363 0.2635 0.1048  -0.0271 -0.0484 84  LEU B C   
2783 O O   . LEU B 84  ? 0.4804 0.2578 0.2940 0.1118  -0.0314 -0.0531 84  LEU B O   
2784 C CB  . LEU B 84  ? 0.4055 0.2058 0.2364 0.0791  -0.0275 -0.0435 84  LEU B CB  
2785 C CG  . LEU B 84  ? 0.4127 0.2123 0.2482 0.0634  -0.0293 -0.0374 84  LEU B CG  
2786 C CD1 . LEU B 84  ? 0.4489 0.2454 0.2794 0.0553  -0.0295 -0.0397 84  LEU B CD1 
2787 C CD2 . LEU B 84  ? 0.4042 0.2292 0.2568 0.0594  -0.0252 -0.0324 84  LEU B CD2 
2788 N N   . ASP B 85  ? 0.4611 0.2903 0.3021 0.1108  -0.0213 -0.0489 85  ASP B N   
2789 C CA  . ASP B 85  ? 0.4737 0.3111 0.3116 0.1255  -0.0178 -0.0554 85  ASP B CA  
2790 C C   . ASP B 85  ? 0.4591 0.3107 0.2979 0.1218  -0.0124 -0.0579 85  ASP B C   
2791 O O   . ASP B 85  ? 0.4503 0.3223 0.3021 0.1120  -0.0087 -0.0533 85  ASP B O   
2792 C CB  . ASP B 85  ? 0.4994 0.3611 0.3512 0.1343  -0.0148 -0.0535 85  ASP B CB  
2793 C CG  . ASP B 85  ? 0.6065 0.4542 0.4559 0.1398  -0.0205 -0.0511 85  ASP B CG  
2794 O OD1 . ASP B 85  ? 0.6424 0.4627 0.4764 0.1473  -0.0256 -0.0545 85  ASP B OD1 
2795 O OD2 . ASP B 85  ? 0.6250 0.4876 0.4871 0.1361  -0.0205 -0.0457 85  ASP B OD2 
2796 N N   . GLY B 86  ? 0.5030 0.3433 0.3273 0.1296  -0.0124 -0.0651 86  GLY B N   
2797 C CA  . GLY B 86  ? 0.5172 0.3719 0.3410 0.1267  -0.0072 -0.0672 86  GLY B CA  
2798 C C   . GLY B 86  ? 0.5201 0.3596 0.3365 0.1128  -0.0105 -0.0664 86  GLY B C   
2799 O O   . GLY B 86  ? 0.5305 0.3443 0.3383 0.1072  -0.0173 -0.0661 86  GLY B O   
2800 N N   . THR B 87  ? 0.4437 0.3006 0.2642 0.1068  -0.0057 -0.0651 87  THR B N   
2801 C CA  . THR B 87  ? 0.4135 0.2589 0.2257 0.0961  -0.0085 -0.0654 87  THR B CA  
2802 C C   . THR B 87  ? 0.4078 0.2704 0.2351 0.0825  -0.0061 -0.0575 87  THR B C   
2803 O O   . THR B 87  ? 0.3962 0.2841 0.2362 0.0830  -0.0001 -0.0540 87  THR B O   
2804 C CB  . THR B 87  ? 0.4344 0.2824 0.2337 0.1028  -0.0057 -0.0721 87  THR B CB  
2805 O OG1 . THR B 87  ? 0.5027 0.3314 0.2858 0.1166  -0.0088 -0.0809 87  THR B OG1 
2806 C CG2 . THR B 87  ? 0.4530 0.2922 0.2448 0.0911  -0.0088 -0.0719 87  THR B CG2 
2807 N N   . TYR B 88  ? 0.4110 0.2605 0.2372 0.0705  -0.0110 -0.0545 88  TYR B N   
2808 C CA  . TYR B 88  ? 0.3591 0.2230 0.1989 0.0584  -0.0094 -0.0474 88  TYR B CA  
2809 C C   . TYR B 88  ? 0.3869 0.2460 0.2199 0.0499  -0.0114 -0.0476 88  TYR B C   
2810 O O   . TYR B 88  ? 0.3989 0.2376 0.2212 0.0457  -0.0173 -0.0498 88  TYR B O   
2811 C CB  . TYR B 88  ? 0.3708 0.2289 0.2185 0.0519  -0.0129 -0.0425 88  TYR B CB  
2812 C CG  . TYR B 88  ? 0.3292 0.1971 0.1868 0.0583  -0.0109 -0.0407 88  TYR B CG  
2813 C CD1 . TYR B 88  ? 0.3619 0.2208 0.2126 0.0701  -0.0120 -0.0448 88  TYR B CD1 
2814 C CD2 . TYR B 88  ? 0.3174 0.2026 0.1907 0.0527  -0.0088 -0.0353 88  TYR B CD2 
2815 C CE1 . TYR B 88  ? 0.3529 0.2215 0.2130 0.0759  -0.0110 -0.0428 88  TYR B CE1 
2816 C CE2 . TYR B 88  ? 0.2997 0.1939 0.1817 0.0579  -0.0079 -0.0339 88  TYR B CE2 
2817 C CZ  . TYR B 88  ? 0.3381 0.2253 0.2140 0.0694  -0.0089 -0.0374 88  TYR B CZ  
2818 O OH  . TYR B 88  ? 0.3578 0.2551 0.2429 0.0747  -0.0087 -0.0356 88  TYR B OH  
2819 N N   . ARG B 89  ? 0.3621 0.2397 0.2012 0.0469  -0.0070 -0.0448 89  ARG B N   
2820 C CA  . ARG B 89  ? 0.3545 0.2302 0.1868 0.0401  -0.0086 -0.0448 89  ARG B CA  
2821 C C   . ARG B 89  ? 0.3338 0.2105 0.1755 0.0280  -0.0115 -0.0387 89  ARG B C   
2822 O O   . ARG B 89  ? 0.3360 0.2259 0.1922 0.0248  -0.0090 -0.0334 89  ARG B O   
2823 C CB  . ARG B 89  ? 0.3430 0.2384 0.1766 0.0429  -0.0026 -0.0436 89  ARG B CB  
2824 C CG  . ARG B 89  ? 0.3904 0.2863 0.2112 0.0550  0.0005  -0.0505 89  ARG B CG  
2825 C CD  . ARG B 89  ? 0.3713 0.2881 0.1929 0.0553  0.0064  -0.0476 89  ARG B CD  
2826 N NE  . ARG B 89  ? 0.4016 0.3266 0.2149 0.0681  0.0114  -0.0529 89  ARG B NE  
2827 C CZ  . ARG B 89  ? 0.3723 0.3203 0.1886 0.0711  0.0184  -0.0500 89  ARG B CZ  
2828 N NH1 . ARG B 89  ? 0.3657 0.3289 0.1922 0.0617  0.0209  -0.0414 89  ARG B NH1 
2829 N NH2 . ARG B 89  ? 0.4382 0.3942 0.2474 0.0840  0.0230  -0.0553 89  ARG B NH2 
2830 N N   . LEU B 90  ? 0.3624 0.2259 0.1957 0.0214  -0.0169 -0.0399 90  LEU B N   
2831 C CA  . LEU B 90  ? 0.3415 0.2088 0.1832 0.0105  -0.0195 -0.0343 90  LEU B CA  
2832 C C   . LEU B 90  ? 0.3303 0.2159 0.1795 0.0081  -0.0157 -0.0301 90  LEU B C   
2833 O O   . LEU B 90  ? 0.3508 0.2391 0.1912 0.0103  -0.0147 -0.0321 90  LEU B O   
2834 C CB  . LEU B 90  ? 0.3667 0.2179 0.1970 0.0044  -0.0263 -0.0369 90  LEU B CB  
2835 C CG  . LEU B 90  ? 0.3547 0.2116 0.1934 -0.0065 -0.0293 -0.0314 90  LEU B CG  
2836 C CD1 . LEU B 90  ? 0.3590 0.2181 0.2099 -0.0103 -0.0294 -0.0267 90  LEU B CD1 
2837 C CD2 . LEU B 90  ? 0.3839 0.2268 0.2108 -0.0128 -0.0365 -0.0342 90  LEU B CD2 
2838 N N   . ILE B 91  ? 0.3089 0.2060 0.1731 0.0040  -0.0140 -0.0244 91  ILE B N   
2839 C CA  . ILE B 91  ? 0.3070 0.2181 0.1780 0.0008  -0.0118 -0.0197 91  ILE B CA  
2840 C C   . ILE B 91  ? 0.2772 0.1882 0.1526 -0.0073 -0.0159 -0.0162 91  ILE B C   
2841 O O   . ILE B 91  ? 0.2931 0.2097 0.1674 -0.0100 -0.0164 -0.0137 91  ILE B O   
2842 C CB  . ILE B 91  ? 0.2839 0.2091 0.1682 0.0030  -0.0069 -0.0161 91  ILE B CB  
2843 C CG1 . ILE B 91  ? 0.3024 0.2393 0.1933 -0.0011 -0.0054 -0.0104 91  ILE B CG1 
2844 C CG2 . ILE B 91  ? 0.3009 0.2255 0.1959 0.0018  -0.0078 -0.0149 91  ILE B CG2 
2845 C CD1 . ILE B 91  ? 0.3115 0.2614 0.2131 0.0007  -0.0008 -0.0071 91  ILE B CD1 
2846 N N   . GLN B 92  ? 0.2732 0.1794 0.1538 -0.0110 -0.0188 -0.0154 92  GLN B N   
2847 C CA  . GLN B 92  ? 0.2853 0.1949 0.1716 -0.0179 -0.0221 -0.0118 92  GLN B CA  
2848 C C   . GLN B 92  ? 0.2958 0.1986 0.1839 -0.0214 -0.0251 -0.0118 92  GLN B C   
2849 O O   . GLN B 92  ? 0.3005 0.1971 0.1876 -0.0183 -0.0242 -0.0135 92  GLN B O   
2850 C CB  . GLN B 92  ? 0.2534 0.1759 0.1529 -0.0184 -0.0198 -0.0071 92  GLN B CB  
2851 C CG  . GLN B 92  ? 0.2773 0.2034 0.1863 -0.0154 -0.0169 -0.0068 92  GLN B CG  
2852 C CD  . GLN B 92  ? 0.2450 0.1746 0.1633 -0.0184 -0.0186 -0.0046 92  GLN B CD  
2853 O OE1 . GLN B 92  ? 0.2671 0.1931 0.1834 -0.0220 -0.0216 -0.0046 92  GLN B OE1 
2854 N NE2 . GLN B 92  ? 0.2839 0.2211 0.2124 -0.0170 -0.0169 -0.0029 92  GLN B NE2 
2855 N N   . PHE B 93  ? 0.2825 0.1872 0.1729 -0.0280 -0.0290 -0.0095 93  PHE B N   
2856 C CA  . PHE B 93  ? 0.2794 0.1843 0.1757 -0.0320 -0.0306 -0.0072 93  PHE B CA  
2857 C C   . PHE B 93  ? 0.2814 0.2005 0.1895 -0.0349 -0.0307 -0.0031 93  PHE B C   
2858 O O   . PHE B 93  ? 0.2622 0.1883 0.1724 -0.0352 -0.0313 -0.0017 93  PHE B O   
2859 C CB  . PHE B 93  ? 0.3092 0.2018 0.1968 -0.0380 -0.0358 -0.0082 93  PHE B CB  
2860 C CG  . PHE B 93  ? 0.3042 0.1990 0.1893 -0.0444 -0.0404 -0.0075 93  PHE B CG  
2861 C CD1 . PHE B 93  ? 0.2905 0.1981 0.1856 -0.0500 -0.0421 -0.0030 93  PHE B CD1 
2862 C CD2 . PHE B 93  ? 0.3285 0.2125 0.2005 -0.0445 -0.0436 -0.0117 93  PHE B CD2 
2863 C CE1 . PHE B 93  ? 0.2834 0.1941 0.1767 -0.0560 -0.0470 -0.0022 93  PHE B CE1 
2864 C CE2 . PHE B 93  ? 0.3405 0.2263 0.2095 -0.0508 -0.0489 -0.0113 93  PHE B CE2 
2865 C CZ  . PHE B 93  ? 0.3239 0.2234 0.2040 -0.0568 -0.0507 -0.0063 93  PHE B CZ  
2866 N N   . HIS B 94  ? 0.2591 0.1827 0.1742 -0.0362 -0.0302 -0.0010 94  HIS B N   
2867 C CA  . HIS B 94  ? 0.2565 0.1940 0.1825 -0.0375 -0.0301 0.0022  94  HIS B CA  
2868 C C   . HIS B 94  ? 0.2474 0.1870 0.1760 -0.0411 -0.0307 0.0043  94  HIS B C   
2869 O O   . HIS B 94  ? 0.2564 0.1856 0.1787 -0.0422 -0.0311 0.0038  94  HIS B O   
2870 C CB  . HIS B 94  ? 0.2378 0.1822 0.1717 -0.0314 -0.0267 0.0020  94  HIS B CB  
2871 C CG  . HIS B 94  ? 0.2143 0.1552 0.1487 -0.0276 -0.0239 0.0004  94  HIS B CG  
2872 N ND1 . HIS B 94  ? 0.2391 0.1723 0.1682 -0.0241 -0.0222 -0.0021 94  HIS B ND1 
2873 C CD2 . HIS B 94  ? 0.2402 0.1851 0.1790 -0.0267 -0.0229 0.0009  94  HIS B CD2 
2874 C CE1 . HIS B 94  ? 0.2322 0.1646 0.1631 -0.0212 -0.0206 -0.0029 94  HIS B CE1 
2875 N NE2 . HIS B 94  ? 0.2199 0.1587 0.1560 -0.0229 -0.0211 -0.0011 94  HIS B NE2 
2876 N N   . PHE B 95  ? 0.2447 0.1984 0.1826 -0.0420 -0.0305 0.0071  95  PHE B N   
2877 C CA  . PHE B 95  ? 0.2445 0.2046 0.1857 -0.0455 -0.0303 0.0101  95  PHE B CA  
2878 C C   . PHE B 95  ? 0.2520 0.2244 0.2019 -0.0397 -0.0270 0.0101  95  PHE B C   
2879 O O   . PHE B 95  ? 0.2447 0.2216 0.1995 -0.0343 -0.0259 0.0082  95  PHE B O   
2880 C CB  . PHE B 95  ? 0.2447 0.2140 0.1890 -0.0532 -0.0337 0.0138  95  PHE B CB  
2881 C CG  . PHE B 95  ? 0.2620 0.2197 0.1978 -0.0600 -0.0382 0.0135  95  PHE B CG  
2882 C CD1 . PHE B 95  ? 0.2670 0.2212 0.1991 -0.0587 -0.0403 0.0110  95  PHE B CD1 
2883 C CD2 . PHE B 95  ? 0.2757 0.2251 0.2062 -0.0677 -0.0410 0.0158  95  PHE B CD2 
2884 C CE1 . PHE B 95  ? 0.2793 0.2228 0.2024 -0.0646 -0.0451 0.0098  95  PHE B CE1 
2885 C CE2 . PHE B 95  ? 0.2922 0.2290 0.2141 -0.0744 -0.0464 0.0147  95  PHE B CE2 
2886 C CZ  . PHE B 95  ? 0.3122 0.2463 0.2301 -0.0725 -0.0485 0.0112  95  PHE B CZ  
2887 N N   . HIS B 96  ? 0.2239 0.2010 0.1748 -0.0412 -0.0257 0.0124  96  HIS B N   
2888 C CA  . HIS B 96  ? 0.2135 0.2047 0.1715 -0.0366 -0.0230 0.0126  96  HIS B CA  
2889 C C   . HIS B 96  ? 0.2172 0.2225 0.1790 -0.0424 -0.0233 0.0175  96  HIS B C   
2890 O O   . HIS B 96  ? 0.2336 0.2334 0.1907 -0.0501 -0.0249 0.0212  96  HIS B O   
2891 C CB  . HIS B 96  ? 0.2139 0.1995 0.1685 -0.0324 -0.0207 0.0110  96  HIS B CB  
2892 C CG  . HIS B 96  ? 0.2101 0.1836 0.1617 -0.0276 -0.0204 0.0068  96  HIS B CG  
2893 N ND1 . HIS B 96  ? 0.2444 0.2211 0.2009 -0.0211 -0.0193 0.0033  96  HIS B ND1 
2894 C CD2 . HIS B 96  ? 0.2412 0.2005 0.1859 -0.0286 -0.0214 0.0056  96  HIS B CD2 
2895 C CE1 . HIS B 96  ? 0.2178 0.1843 0.1714 -0.0192 -0.0192 0.0010  96  HIS B CE1 
2896 N NE2 . HIS B 96  ? 0.2378 0.1944 0.1841 -0.0229 -0.0202 0.0021  96  HIS B NE2 
2897 N N   . TRP B 97  ? 0.2025 0.2258 0.1728 -0.0389 -0.0219 0.0179  97  TRP B N   
2898 C CA  . TRP B 97  ? 0.1950 0.2361 0.1704 -0.0443 -0.0217 0.0232  97  TRP B CA  
2899 C C   . TRP B 97  ? 0.2169 0.2775 0.1996 -0.0367 -0.0184 0.0222  97  TRP B C   
2900 O O   . TRP B 97  ? 0.1982 0.2566 0.1818 -0.0276 -0.0172 0.0170  97  TRP B O   
2901 C CB  . TRP B 97  ? 0.2136 0.2595 0.1926 -0.0503 -0.0255 0.0254  97  TRP B CB  
2902 C CG  . TRP B 97  ? 0.2016 0.2526 0.1861 -0.0434 -0.0264 0.0222  97  TRP B CG  
2903 C CD1 . TRP B 97  ? 0.2091 0.2796 0.2031 -0.0382 -0.0257 0.0225  97  TRP B CD1 
2904 C CD2 . TRP B 97  ? 0.2022 0.2383 0.1827 -0.0407 -0.0285 0.0187  97  TRP B CD2 
2905 N NE1 . TRP B 97  ? 0.1991 0.2660 0.1950 -0.0324 -0.0277 0.0196  97  TRP B NE1 
2906 C CE2 . TRP B 97  ? 0.2054 0.2517 0.1931 -0.0344 -0.0292 0.0176  97  TRP B CE2 
2907 C CE3 . TRP B 97  ? 0.1982 0.2144 0.1695 -0.0427 -0.0296 0.0166  97  TRP B CE3 
2908 C CZ2 . TRP B 97  ? 0.2156 0.2518 0.2011 -0.0313 -0.0313 0.0156  97  TRP B CZ2 
2909 C CZ3 . TRP B 97  ? 0.2219 0.2305 0.1915 -0.0390 -0.0308 0.0141  97  TRP B CZ3 
2910 C CH2 . TRP B 97  ? 0.2097 0.2282 0.1863 -0.0342 -0.0318 0.0142  97  TRP B CH2 
2911 N N   . GLY B 98  ? 0.2099 0.2902 0.1978 -0.0406 -0.0170 0.0273  98  GLY B N   
2912 C CA  . GLY B 98  ? 0.2045 0.3055 0.1980 -0.0330 -0.0132 0.0266  98  GLY B CA  
2913 C C   . GLY B 98  ? 0.2081 0.3296 0.2120 -0.0297 -0.0137 0.0268  98  GLY B C   
2914 O O   . GLY B 98  ? 0.2138 0.3347 0.2211 -0.0336 -0.0173 0.0281  98  GLY B O   
2915 N N   . SER B 99  ? 0.2077 0.3479 0.2161 -0.0207 -0.0102 0.0249  99  SER B N   
2916 C CA  . SER B 99  ? 0.2069 0.3711 0.2258 -0.0162 -0.0100 0.0257  99  SER B CA  
2917 C C   . SER B 99  ? 0.2157 0.4035 0.2407 -0.0258 -0.0086 0.0342  99  SER B C   
2918 O O   . SER B 99  ? 0.2243 0.4344 0.2593 -0.0240 -0.0089 0.0361  99  SER B O   
2919 C CB  . SER B 99  ? 0.2271 0.4016 0.2477 -0.0015 -0.0069 0.0194  99  SER B CB  
2920 O OG  . SER B 99  ? 0.2569 0.4362 0.2721 -0.0003 -0.0027 0.0196  99  SER B OG  
2921 N N   . HIS B 100 ? 0.2333 0.4169 0.2528 -0.0361 -0.0075 0.0398  100 HIS B N   
2922 C CA  . HIS B 100 ? 0.2276 0.4299 0.2525 -0.0482 -0.0072 0.0492  100 HIS B CA  
2923 C C   . HIS B 100 ? 0.2372 0.4175 0.2526 -0.0607 -0.0092 0.0537  100 HIS B C   
2924 O O   . HIS B 100 ? 0.2461 0.4019 0.2516 -0.0576 -0.0097 0.0493  100 HIS B O   
2925 C CB  . HIS B 100 ? 0.2025 0.4356 0.2325 -0.0437 -0.0010 0.0524  100 HIS B CB  
2926 C CG  . HIS B 100 ? 0.2298 0.4566 0.2504 -0.0388 0.0031  0.0506  100 HIS B CG  
2927 N ND1 . HIS B 100 ? 0.2673 0.4895 0.2813 -0.0491 0.0044  0.0580  100 HIS B ND1 
2928 C CD2 . HIS B 100 ? 0.2428 0.4662 0.2589 -0.0248 0.0057  0.0425  100 HIS B CD2 
2929 C CE1 . HIS B 100 ? 0.2787 0.4965 0.2845 -0.0413 0.0078  0.0546  100 HIS B CE1 
2930 N NE2 . HIS B 100 ? 0.2509 0.4691 0.2577 -0.0268 0.0084  0.0449  100 HIS B NE2 
2931 N N   . ASP B 101 ? 0.2213 0.4101 0.2398 -0.0748 -0.0110 0.0625  101 ASP B N   
2932 C CA  . ASP B 101 ? 0.2429 0.4067 0.2519 -0.0869 -0.0147 0.0663  101 ASP B CA  
2933 C C   . ASP B 101 ? 0.2574 0.4118 0.2568 -0.0863 -0.0112 0.0685  101 ASP B C   
2934 O O   . ASP B 101 ? 0.2898 0.4188 0.2796 -0.0930 -0.0144 0.0700  101 ASP B O   
2935 C CB  . ASP B 101 ? 0.2809 0.4553 0.2954 -0.1032 -0.0181 0.0757  101 ASP B CB  
2936 C CG  . ASP B 101 ? 0.2648 0.4418 0.2862 -0.1069 -0.0238 0.0739  101 ASP B CG  
2937 O OD1 . ASP B 101 ? 0.2816 0.4479 0.3015 -0.0975 -0.0254 0.0659  101 ASP B OD1 
2938 O OD2 . ASP B 101 ? 0.2858 0.4763 0.3139 -0.1202 -0.0270 0.0815  101 ASP B OD2 
2939 N N   . GLY B 102 ? 0.2552 0.4292 0.2565 -0.0781 -0.0053 0.0686  102 GLY B N   
2940 C CA  . GLY B 102 ? 0.2511 0.4182 0.2429 -0.0777 -0.0023 0.0715  102 GLY B CA  
2941 C C   . GLY B 102 ? 0.2754 0.4193 0.2576 -0.0671 -0.0023 0.0629  102 GLY B C   
2942 O O   . GLY B 102 ? 0.2968 0.4353 0.2708 -0.0654 -0.0002 0.0646  102 GLY B O   
2943 N N   . GLN B 103 ? 0.2358 0.3676 0.2191 -0.0597 -0.0046 0.0541  103 GLN B N   
2944 C CA  . GLN B 103 ? 0.2370 0.3464 0.2123 -0.0515 -0.0053 0.0465  103 GLN B CA  
2945 C C   . GLN B 103 ? 0.2587 0.3501 0.2345 -0.0514 -0.0097 0.0413  103 GLN B C   
2946 O O   . GLN B 103 ? 0.2452 0.3432 0.2275 -0.0557 -0.0119 0.0426  103 GLN B O   
2947 C CB  . GLN B 103 ? 0.2506 0.3709 0.2265 -0.0377 -0.0016 0.0398  103 GLN B CB  
2948 C CG  . GLN B 103 ? 0.2707 0.4054 0.2559 -0.0295 -0.0011 0.0344  103 GLN B CG  
2949 C CD  . GLN B 103 ? 0.2675 0.4152 0.2528 -0.0166 0.0024  0.0284  103 GLN B CD  
2950 O OE1 . GLN B 103 ? 0.2801 0.4369 0.2606 -0.0154 0.0057  0.0308  103 GLN B OE1 
2951 N NE2 . GLN B 103 ? 0.2258 0.3734 0.2155 -0.0067 0.0012  0.0206  103 GLN B NE2 
2952 N N   . GLY B 104 ? 0.2394 0.3096 0.2085 -0.0463 -0.0108 0.0356  104 GLY B N   
2953 C CA  . GLY B 104 ? 0.2297 0.2838 0.1984 -0.0456 -0.0142 0.0309  104 GLY B CA  
2954 C C   . GLY B 104 ? 0.2329 0.2623 0.1923 -0.0458 -0.0161 0.0287  104 GLY B C   
2955 O O   . GLY B 104 ? 0.2465 0.2652 0.2051 -0.0405 -0.0170 0.0230  104 GLY B O   
2956 N N   . SER B 105 ? 0.2263 0.2467 0.1787 -0.0520 -0.0168 0.0337  105 SER B N   
2957 C CA  . SER B 105 ? 0.2421 0.2394 0.1857 -0.0506 -0.0186 0.0311  105 SER B CA  
2958 C C   . SER B 105 ? 0.2290 0.2257 0.1714 -0.0404 -0.0163 0.0262  105 SER B C   
2959 O O   . SER B 105 ? 0.2338 0.2458 0.1795 -0.0358 -0.0134 0.0259  105 SER B O   
2960 C CB  . SER B 105 ? 0.2551 0.2402 0.1907 -0.0589 -0.0209 0.0376  105 SER B CB  
2961 O OG  . SER B 105 ? 0.2668 0.2612 0.2008 -0.0590 -0.0183 0.0428  105 SER B OG  
2962 N N   . GLU B 106 ? 0.2408 0.2202 0.1781 -0.0370 -0.0177 0.0222  106 GLU B N   
2963 C CA  . GLU B 106 ? 0.2194 0.1973 0.1560 -0.0284 -0.0164 0.0177  106 GLU B CA  
2964 C C   . GLU B 106 ? 0.2473 0.2179 0.1761 -0.0284 -0.0167 0.0212  106 GLU B C   
2965 O O   . GLU B 106 ? 0.2425 0.2227 0.1707 -0.0251 -0.0149 0.0222  106 GLU B O   
2966 C CB  . GLU B 106 ? 0.2527 0.2198 0.1899 -0.0243 -0.0174 0.0119  106 GLU B CB  
2967 C CG  . GLU B 106 ? 0.2405 0.2152 0.1850 -0.0238 -0.0173 0.0094  106 GLU B CG  
2968 C CD  . GLU B 106 ? 0.2333 0.2040 0.1806 -0.0180 -0.0172 0.0040  106 GLU B CD  
2969 O OE1 . GLU B 106 ? 0.2480 0.2069 0.1911 -0.0178 -0.0180 0.0028  106 GLU B OE1 
2970 O OE2 . GLU B 106 ? 0.2416 0.2211 0.1948 -0.0137 -0.0165 0.0013  106 GLU B OE2 
2971 N N   . HIS B 107 ? 0.2468 0.2001 0.1685 -0.0319 -0.0192 0.0233  107 HIS B N   
2972 C CA  . HIS B 107 ? 0.2691 0.2143 0.1828 -0.0331 -0.0203 0.0283  107 HIS B CA  
2973 C C   . HIS B 107 ? 0.2728 0.2281 0.1863 -0.0410 -0.0195 0.0364  107 HIS B C   
2974 O O   . HIS B 107 ? 0.2771 0.2413 0.1957 -0.0474 -0.0193 0.0385  107 HIS B O   
2975 C CB  . HIS B 107 ? 0.2558 0.1779 0.1615 -0.0345 -0.0238 0.0283  107 HIS B CB  
2976 C CG  . HIS B 107 ? 0.2637 0.1789 0.1693 -0.0259 -0.0238 0.0213  107 HIS B CG  
2977 N ND1 . HIS B 107 ? 0.2682 0.1829 0.1778 -0.0246 -0.0236 0.0160  107 HIS B ND1 
2978 C CD2 . HIS B 107 ? 0.2850 0.1969 0.1883 -0.0182 -0.0238 0.0191  107 HIS B CD2 
2979 C CE1 . HIS B 107 ? 0.2845 0.1957 0.1942 -0.0170 -0.0231 0.0112  107 HIS B CE1 
2980 N NE2 . HIS B 107 ? 0.2804 0.1902 0.1869 -0.0129 -0.0234 0.0127  107 HIS B NE2 
2981 N N   . THR B 108 ? 0.2602 0.2163 0.1681 -0.0404 -0.0190 0.0414  108 THR B N   
2982 C CA  . THR B 108 ? 0.2634 0.2272 0.1692 -0.0488 -0.0184 0.0510  108 THR B CA  
2983 C C   . THR B 108 ? 0.2759 0.2191 0.1710 -0.0525 -0.0219 0.0573  108 THR B C   
2984 O O   . THR B 108 ? 0.3087 0.2368 0.1983 -0.0457 -0.0238 0.0537  108 THR B O   
2985 C CB  . THR B 108 ? 0.2566 0.2439 0.1648 -0.0447 -0.0140 0.0525  108 THR B CB  
2986 O OG1 . THR B 108 ? 0.2835 0.2674 0.1866 -0.0356 -0.0139 0.0492  108 THR B OG1 
2987 C CG2 . THR B 108 ? 0.2741 0.2805 0.1925 -0.0407 -0.0110 0.0465  108 THR B CG2 
2988 N N   . VAL B 109 ? 0.2897 0.2327 0.1823 -0.0634 -0.0230 0.0671  109 VAL B N   
2989 C CA  . VAL B 109 ? 0.3181 0.2403 0.1998 -0.0685 -0.0270 0.0749  109 VAL B CA  
2990 C C   . VAL B 109 ? 0.3405 0.2788 0.2205 -0.0727 -0.0242 0.0852  109 VAL B C   
2991 O O   . VAL B 109 ? 0.3299 0.2860 0.2155 -0.0815 -0.0220 0.0913  109 VAL B O   
2992 C CB  . VAL B 109 ? 0.3417 0.2440 0.2207 -0.0791 -0.0324 0.0776  109 VAL B CB  
2993 C CG1 . VAL B 109 ? 0.3911 0.2677 0.2577 -0.0833 -0.0375 0.0852  109 VAL B CG1 
2994 C CG2 . VAL B 109 ? 0.3494 0.2390 0.2296 -0.0733 -0.0344 0.0666  109 VAL B CG2 
2995 N N   . ASP B 110 ? 0.3295 0.2641 0.2018 -0.0661 -0.0240 0.0872  110 ASP B N   
2996 C CA  . ASP B 110 ? 0.3352 0.2867 0.2042 -0.0686 -0.0209 0.0969  110 ASP B CA  
2997 C C   . ASP B 110 ? 0.3530 0.3372 0.2320 -0.0678 -0.0148 0.0948  110 ASP B C   
2998 O O   . ASP B 110 ? 0.3858 0.3884 0.2665 -0.0754 -0.0118 0.1038  110 ASP B O   
2999 C CB  . ASP B 110 ? 0.3684 0.3086 0.2310 -0.0824 -0.0239 0.1109  110 ASP B CB  
3000 C CG  . ASP B 110 ? 0.4580 0.3641 0.3094 -0.0814 -0.0305 0.1127  110 ASP B CG  
3001 O OD1 . ASP B 110 ? 0.4178 0.3153 0.2644 -0.0692 -0.0314 0.1066  110 ASP B OD1 
3002 O OD2 . ASP B 110 ? 0.4920 0.3799 0.3392 -0.0929 -0.0352 0.1204  110 ASP B OD2 
3003 N N   . LYS B 111 ? 0.3271 0.3185 0.2127 -0.0579 -0.0130 0.0828  111 LYS B N   
3004 C CA  . LYS B 111 ? 0.3081 0.3267 0.2025 -0.0531 -0.0080 0.0775  111 LYS B CA  
3005 C C   . LYS B 111 ? 0.3499 0.3802 0.2543 -0.0609 -0.0070 0.0786  111 LYS B C   
3006 O O   . LYS B 111 ? 0.3947 0.4467 0.3071 -0.0563 -0.0033 0.0739  111 LYS B O   
3007 C CB  . LYS B 111 ? 0.3523 0.3937 0.2431 -0.0499 -0.0035 0.0821  111 LYS B CB  
3008 C CG  . LYS B 111 ? 0.4372 0.4707 0.3179 -0.0419 -0.0048 0.0813  111 LYS B CG  
3009 C CD  . LYS B 111 ? 0.5371 0.5630 0.4203 -0.0305 -0.0065 0.0680  111 LYS B CD  
3010 C CE  . LYS B 111 ? 0.5824 0.6294 0.4743 -0.0239 -0.0029 0.0589  111 LYS B CE  
3011 N NZ  . LYS B 111 ? 0.5475 0.5875 0.4426 -0.0145 -0.0049 0.0468  111 LYS B NZ  
3012 N N   . LYS B 112 ? 0.3282 0.3439 0.2324 -0.0718 -0.0107 0.0838  112 LYS B N   
3013 C CA  . LYS B 112 ? 0.3532 0.3809 0.2671 -0.0802 -0.0106 0.0855  112 LYS B CA  
3014 C C   . LYS B 112 ? 0.3071 0.3273 0.2267 -0.0753 -0.0124 0.0748  112 LYS B C   
3015 O O   . LYS B 112 ? 0.2983 0.2948 0.2127 -0.0719 -0.0160 0.0694  112 LYS B O   
3016 C CB  . LYS B 112 ? 0.4258 0.4406 0.3367 -0.0953 -0.0148 0.0959  112 LYS B CB  
3017 C CG  . LYS B 112 ? 0.5566 0.5820 0.4775 -0.1057 -0.0161 0.0980  112 LYS B CG  
3018 C CD  . LYS B 112 ? 0.6243 0.6228 0.5431 -0.1094 -0.0227 0.0928  112 LYS B CD  
3019 C CE  . LYS B 112 ? 0.6597 0.6645 0.5854 -0.1236 -0.0260 0.0982  112 LYS B CE  
3020 N NZ  . LYS B 112 ? 0.6869 0.7259 0.6262 -0.1227 -0.0215 0.0977  112 LYS B NZ  
3021 N N   . LYS B 113 ? 0.2809 0.3219 0.2110 -0.0746 -0.0100 0.0721  113 LYS B N   
3022 C CA  . LYS B 113 ? 0.2669 0.3029 0.2028 -0.0714 -0.0119 0.0636  113 LYS B CA  
3023 C C   . LYS B 113 ? 0.2823 0.3166 0.2226 -0.0830 -0.0155 0.0674  113 LYS B C   
3024 O O   . LYS B 113 ? 0.3404 0.3886 0.2843 -0.0931 -0.0152 0.0762  113 LYS B O   
3025 C CB  . LYS B 113 ? 0.2546 0.3131 0.1991 -0.0617 -0.0079 0.0573  113 LYS B CB  
3026 C CG  . LYS B 113 ? 0.2835 0.3398 0.2238 -0.0497 -0.0059 0.0507  113 LYS B CG  
3027 C CD  . LYS B 113 ? 0.3216 0.3964 0.2695 -0.0398 -0.0030 0.0435  113 LYS B CD  
3028 C CE  . LYS B 113 ? 0.3202 0.3882 0.2638 -0.0287 -0.0026 0.0356  113 LYS B CE  
3029 N NZ  . LYS B 113 ? 0.3301 0.4056 0.2805 -0.0192 -0.0021 0.0265  113 LYS B NZ  
3030 N N   . TYR B 114 ? 0.2882 0.3060 0.2279 -0.0818 -0.0192 0.0609  114 TYR B N   
3031 C CA  . TYR B 114 ? 0.2993 0.3162 0.2432 -0.0911 -0.0231 0.0623  114 TYR B CA  
3032 C C   . TYR B 114 ? 0.2571 0.2919 0.2113 -0.0852 -0.0215 0.0567  114 TYR B C   
3033 O O   . TYR B 114 ? 0.2490 0.2898 0.2053 -0.0737 -0.0181 0.0506  114 TYR B O   
3034 C CB  . TYR B 114 ? 0.3144 0.3008 0.2492 -0.0935 -0.0287 0.0587  114 TYR B CB  
3035 C CG  . TYR B 114 ? 0.3424 0.3087 0.2669 -0.1001 -0.0318 0.0646  114 TYR B CG  
3036 C CD1 . TYR B 114 ? 0.3513 0.3041 0.2676 -0.0924 -0.0306 0.0631  114 TYR B CD1 
3037 C CD2 . TYR B 114 ? 0.3877 0.3469 0.3105 -0.1143 -0.0368 0.0717  114 TYR B CD2 
3038 C CE1 . TYR B 114 ? 0.4118 0.3443 0.3179 -0.0978 -0.0340 0.0689  114 TYR B CE1 
3039 C CE2 . TYR B 114 ? 0.3972 0.3345 0.3096 -0.1206 -0.0405 0.0776  114 TYR B CE2 
3040 C CZ  . TYR B 114 ? 0.4296 0.3536 0.3336 -0.1115 -0.0389 0.0760  114 TYR B CZ  
3041 O OH  . TYR B 114 ? 0.5014 0.4023 0.3946 -0.1165 -0.0430 0.0819  114 TYR B OH  
3042 N N   . ALA B 115 ? 0.2640 0.3044 0.2238 -0.0929 -0.0248 0.0584  115 ALA B N   
3043 C CA  . ALA B 115 ? 0.2455 0.3029 0.2150 -0.0874 -0.0239 0.0541  115 ALA B CA  
3044 C C   . ALA B 115 ? 0.2580 0.2998 0.2244 -0.0786 -0.0251 0.0451  115 ALA B C   
3045 O O   . ALA B 115 ? 0.2464 0.3000 0.2195 -0.0705 -0.0234 0.0408  115 ALA B O   
3046 C CB  . ALA B 115 ? 0.2664 0.3345 0.2427 -0.0988 -0.0280 0.0588  115 ALA B CB  
3047 N N   . ALA B 116 ? 0.2473 0.2632 0.2035 -0.0796 -0.0280 0.0424  116 ALA B N   
3048 C CA  . ALA B 116 ? 0.2429 0.2464 0.1964 -0.0713 -0.0284 0.0347  116 ALA B CA  
3049 C C   . ALA B 116 ? 0.2683 0.2464 0.2103 -0.0708 -0.0300 0.0325  116 ALA B C   
3050 O O   . ALA B 116 ? 0.2719 0.2404 0.2079 -0.0772 -0.0317 0.0370  116 ALA B O   
3051 C CB  . ALA B 116 ? 0.2507 0.2563 0.2074 -0.0740 -0.0320 0.0329  116 ALA B CB  
3052 N N   . GLU B 117 ? 0.2536 0.2215 0.1926 -0.0630 -0.0295 0.0261  117 GLU B N   
3053 C CA  . GLU B 117 ? 0.2715 0.2176 0.2004 -0.0605 -0.0306 0.0232  117 GLU B CA  
3054 C C   . GLU B 117 ? 0.2716 0.2098 0.1982 -0.0568 -0.0318 0.0175  117 GLU B C   
3055 O O   . GLU B 117 ? 0.2644 0.2125 0.1972 -0.0515 -0.0298 0.0149  117 GLU B O   
3056 C CB  . GLU B 117 ? 0.2606 0.2068 0.1888 -0.0527 -0.0270 0.0220  117 GLU B CB  
3057 C CG  . GLU B 117 ? 0.2745 0.2001 0.1929 -0.0494 -0.0283 0.0197  117 GLU B CG  
3058 C CD  . GLU B 117 ? 0.2829 0.2105 0.2010 -0.0427 -0.0256 0.0196  117 GLU B CD  
3059 O OE1 . GLU B 117 ? 0.2694 0.2095 0.1908 -0.0438 -0.0238 0.0236  117 GLU B OE1 
3060 O OE2 . GLU B 117 ? 0.2916 0.2094 0.2060 -0.0361 -0.0254 0.0157  117 GLU B OE2 
3061 N N   . LEU B 118 ? 0.2760 0.1955 0.1927 -0.0594 -0.0353 0.0157  118 LEU B N   
3062 C CA  . LEU B 118 ? 0.2768 0.1875 0.1885 -0.0560 -0.0364 0.0105  118 LEU B CA  
3063 C C   . LEU B 118 ? 0.2729 0.1723 0.1790 -0.0475 -0.0342 0.0064  118 LEU B C   
3064 O O   . LEU B 118 ? 0.3032 0.1911 0.2033 -0.0469 -0.0349 0.0072  118 LEU B O   
3065 C CB  . LEU B 118 ? 0.2862 0.1836 0.1894 -0.0639 -0.0422 0.0103  118 LEU B CB  
3066 C CG  . LEU B 118 ? 0.2984 0.1819 0.1917 -0.0598 -0.0438 0.0042  118 LEU B CG  
3067 C CD1 . LEU B 118 ? 0.2892 0.1852 0.1875 -0.0562 -0.0420 0.0022  118 LEU B CD1 
3068 C CD2 . LEU B 118 ? 0.3404 0.2084 0.2238 -0.0680 -0.0506 0.0035  118 LEU B CD2 
3069 N N   . HIS B 119 ? 0.2616 0.1654 0.1701 -0.0410 -0.0315 0.0027  119 HIS B N   
3070 C CA  . HIS B 119 ? 0.2685 0.1653 0.1732 -0.0329 -0.0291 -0.0010 119 HIS B CA  
3071 C C   . HIS B 119 ? 0.2805 0.1706 0.1784 -0.0307 -0.0298 -0.0050 119 HIS B C   
3072 O O   . HIS B 119 ? 0.2812 0.1803 0.1831 -0.0306 -0.0288 -0.0053 119 HIS B O   
3073 C CB  . HIS B 119 ? 0.2618 0.1718 0.1763 -0.0273 -0.0251 -0.0013 119 HIS B CB  
3074 C CG  . HIS B 119 ? 0.2522 0.1680 0.1712 -0.0273 -0.0242 0.0014  119 HIS B CG  
3075 N ND1 . HIS B 119 ? 0.2405 0.1689 0.1682 -0.0240 -0.0218 0.0013  119 HIS B ND1 
3076 C CD2 . HIS B 119 ? 0.2484 0.1585 0.1632 -0.0303 -0.0256 0.0044  119 HIS B CD2 
3077 C CE1 . HIS B 119 ? 0.2360 0.1676 0.1643 -0.0244 -0.0215 0.0037  119 HIS B CE1 
3078 N NE2 . HIS B 119 ? 0.2580 0.1793 0.1789 -0.0287 -0.0236 0.0063  119 HIS B NE2 
3079 N N   . LEU B 120 ? 0.3107 0.1851 0.1978 -0.0280 -0.0313 -0.0082 120 LEU B N   
3080 C CA  . LEU B 120 ? 0.3033 0.1713 0.1820 -0.0236 -0.0312 -0.0130 120 LEU B CA  
3081 C C   . LEU B 120 ? 0.3186 0.1902 0.1993 -0.0143 -0.0266 -0.0152 120 LEU B C   
3082 O O   . LEU B 120 ? 0.2996 0.1640 0.1780 -0.0100 -0.0266 -0.0159 120 LEU B O   
3083 C CB  . LEU B 120 ? 0.3281 0.1762 0.1930 -0.0258 -0.0363 -0.0159 120 LEU B CB  
3084 C CG  . LEU B 120 ? 0.3346 0.1806 0.1980 -0.0361 -0.0414 -0.0138 120 LEU B CG  
3085 C CD1 . LEU B 120 ? 0.4036 0.2328 0.2608 -0.0420 -0.0465 -0.0121 120 LEU B CD1 
3086 C CD2 . LEU B 120 ? 0.3797 0.2220 0.2344 -0.0365 -0.0439 -0.0181 120 LEU B CD2 
3087 N N   . VAL B 121 ? 0.3049 0.1885 0.1906 -0.0114 -0.0231 -0.0157 121 VAL B N   
3088 C CA  . VAL B 121 ? 0.2948 0.1871 0.1866 -0.0045 -0.0187 -0.0162 121 VAL B CA  
3089 C C   . VAL B 121 ? 0.3053 0.1946 0.1888 0.0023  -0.0167 -0.0204 121 VAL B C   
3090 O O   . VAL B 121 ? 0.3031 0.1931 0.1809 0.0014  -0.0167 -0.0216 121 VAL B O   
3091 C CB  . VAL B 121 ? 0.2751 0.1828 0.1786 -0.0066 -0.0163 -0.0131 121 VAL B CB  
3092 C CG1 . VAL B 121 ? 0.2720 0.1894 0.1829 -0.0011 -0.0124 -0.0133 121 VAL B CG1 
3093 C CG2 . VAL B 121 ? 0.2969 0.2090 0.2081 -0.0119 -0.0181 -0.0098 121 VAL B CG2 
3094 N N   . HIS B 122 ? 0.2959 0.1832 0.1782 0.0096  -0.0151 -0.0226 122 HIS B N   
3095 C CA  . HIS B 122 ? 0.3028 0.1885 0.1771 0.0178  -0.0129 -0.0270 122 HIS B CA  
3096 C C   . HIS B 122 ? 0.3015 0.2019 0.1852 0.0243  -0.0082 -0.0265 122 HIS B C   
3097 O O   . HIS B 122 ? 0.2974 0.2019 0.1898 0.0242  -0.0084 -0.0243 122 HIS B O   
3098 C CB  . HIS B 122 ? 0.3396 0.2053 0.2004 0.0224  -0.0165 -0.0316 122 HIS B CB  
3099 C CG  . HIS B 122 ? 0.3252 0.1746 0.1780 0.0147  -0.0223 -0.0315 122 HIS B CG  
3100 N ND1 . HIS B 122 ? 0.3253 0.1717 0.1834 0.0072  -0.0252 -0.0269 122 HIS B ND1 
3101 C CD2 . HIS B 122 ? 0.3495 0.1851 0.1891 0.0131  -0.0262 -0.0354 122 HIS B CD2 
3102 C CE1 . HIS B 122 ? 0.3222 0.1548 0.1719 0.0005  -0.0304 -0.0274 122 HIS B CE1 
3103 N NE2 . HIS B 122 ? 0.3716 0.1965 0.2099 0.0038  -0.0315 -0.0327 122 HIS B NE2 
3104 N N   . TRP B 123 ? 0.3120 0.2210 0.1932 0.0301  -0.0043 -0.0286 123 TRP B N   
3105 C CA  . TRP B 123 ? 0.2976 0.2233 0.1887 0.0357  0.0002  -0.0276 123 TRP B CA  
3106 C C   . TRP B 123 ? 0.3063 0.2316 0.1891 0.0471  0.0025  -0.0326 123 TRP B C   
3107 O O   . TRP B 123 ? 0.3342 0.2512 0.2036 0.0509  0.0023  -0.0369 123 TRP B O   
3108 C CB  . TRP B 123 ? 0.2682 0.2123 0.1699 0.0309  0.0040  -0.0229 123 TRP B CB  
3109 C CG  . TRP B 123 ? 0.2804 0.2262 0.1732 0.0302  0.0058  -0.0233 123 TRP B CG  
3110 C CD1 . TRP B 123 ? 0.2810 0.2199 0.1684 0.0236  0.0032  -0.0221 123 TRP B CD1 
3111 C CD2 . TRP B 123 ? 0.2929 0.2495 0.1810 0.0370  0.0107  -0.0249 123 TRP B CD2 
3112 N NE1 . TRP B 123 ? 0.2951 0.2393 0.1743 0.0255  0.0059  -0.0227 123 TRP B NE1 
3113 C CE2 . TRP B 123 ? 0.2937 0.2488 0.1727 0.0339  0.0108  -0.0245 123 TRP B CE2 
3114 C CE3 . TRP B 123 ? 0.2895 0.2590 0.1806 0.0458  0.0152  -0.0264 123 TRP B CE3 
3115 C CZ2 . TRP B 123 ? 0.3001 0.2656 0.1718 0.0391  0.0154  -0.0256 123 TRP B CZ2 
3116 C CZ3 . TRP B 123 ? 0.3000 0.2807 0.1847 0.0513  0.0201  -0.0276 123 TRP B CZ3 
3117 C CH2 . TRP B 123 ? 0.3201 0.2988 0.1947 0.0479  0.0204  -0.0271 123 TRP B CH2 
3118 N N   . ASN B 124 ? 0.3057 0.2409 0.1967 0.0532  0.0044  -0.0324 124 ASN B N   
3119 C CA  . ASN B 124 ? 0.3130 0.2492 0.1982 0.0658  0.0062  -0.0372 124 ASN B CA  
3120 C C   . ASN B 124 ? 0.3263 0.2804 0.2112 0.0705  0.0122  -0.0380 124 ASN B C   
3121 O O   . ASN B 124 ? 0.3189 0.2943 0.2171 0.0669  0.0162  -0.0331 124 ASN B O   
3122 C CB  . ASN B 124 ? 0.3117 0.2562 0.2083 0.0697  0.0059  -0.0355 124 ASN B CB  
3123 C CG  . ASN B 124 ? 0.3572 0.3014 0.2485 0.0840  0.0066  -0.0403 124 ASN B CG  
3124 O OD1 . ASN B 124 ? 0.3659 0.3091 0.2471 0.0921  0.0090  -0.0450 124 ASN B OD1 
3125 N ND2 . ASN B 124 ? 0.3523 0.2971 0.2498 0.0879  0.0043  -0.0393 124 ASN B ND2 
3126 N N   . THR B 125 ? 0.3178 0.2633 0.1870 0.0788  0.0128  -0.0441 125 THR B N   
3127 C CA  . THR B 125 ? 0.3144 0.2787 0.1819 0.0838  0.0192  -0.0447 125 THR B CA  
3128 C C   . THR B 125 ? 0.3447 0.3321 0.2226 0.0931  0.0245  -0.0442 125 THR B C   
3129 O O   . THR B 125 ? 0.4075 0.4147 0.2856 0.0977  0.0307  -0.0440 125 THR B O   
3130 C CB  . THR B 125 ? 0.3708 0.3205 0.2176 0.0912  0.0183  -0.0524 125 THR B CB  
3131 O OG1 . THR B 125 ? 0.4295 0.3644 0.2678 0.1033  0.0156  -0.0592 125 THR B OG1 
3132 C CG2 . THR B 125 ? 0.3776 0.3076 0.2153 0.0810  0.0129  -0.0524 125 THR B CG2 
3133 N N   . LYS B 126 ? 0.3643 0.3505 0.2502 0.0965  0.0221  -0.0441 126 LYS B N   
3134 C CA  . LYS B 126 ? 0.4014 0.4130 0.3019 0.1023  0.0262  -0.0418 126 LYS B CA  
3135 C C   . LYS B 126 ? 0.3491 0.3853 0.2655 0.0917  0.0305  -0.0340 126 LYS B C   
3136 O O   . LYS B 126 ? 0.3747 0.4370 0.3009 0.0954  0.0359  -0.0316 126 LYS B O   
3137 C CB  . LYS B 126 ? 0.4313 0.4346 0.3378 0.1043  0.0212  -0.0418 126 LYS B CB  
3138 C CG  . LYS B 126 ? 0.4172 0.4453 0.3411 0.1074  0.0234  -0.0385 126 LYS B CG  
3139 C CD  . LYS B 126 ? 0.4226 0.4387 0.3488 0.1100  0.0174  -0.0390 126 LYS B CD  
3140 C CE  . LYS B 126 ? 0.4606 0.5038 0.4048 0.1131  0.0189  -0.0360 126 LYS B CE  
3141 N NZ  . LYS B 126 ? 0.4439 0.4797 0.3919 0.1147  0.0132  -0.0354 126 LYS B NZ  
3142 N N   . TYR B 127 ? 0.3224 0.3504 0.2412 0.0785  0.0279  -0.0297 127 TYR B N   
3143 C CA  . TYR B 127 ? 0.3155 0.3611 0.2487 0.0675  0.0302  -0.0221 127 TYR B CA  
3144 C C   . TYR B 127 ? 0.3624 0.4077 0.2869 0.0627  0.0328  -0.0202 127 TYR B C   
3145 O O   . TYR B 127 ? 0.3800 0.4100 0.2880 0.0667  0.0318  -0.0251 127 TYR B O   
3146 C CB  . TYR B 127 ? 0.2708 0.3072 0.2133 0.0576  0.0247  -0.0190 127 TYR B CB  
3147 C CG  . TYR B 127 ? 0.2843 0.3200 0.2325 0.0633  0.0217  -0.0213 127 TYR B CG  
3148 C CD1 . TYR B 127 ? 0.2824 0.3406 0.2434 0.0675  0.0244  -0.0197 127 TYR B CD1 
3149 C CD2 . TYR B 127 ? 0.2738 0.2877 0.2148 0.0644  0.0162  -0.0243 127 TYR B CD2 
3150 C CE1 . TYR B 127 ? 0.2826 0.3417 0.2484 0.0735  0.0214  -0.0216 127 TYR B CE1 
3151 C CE2 . TYR B 127 ? 0.2774 0.2909 0.2224 0.0702  0.0135  -0.0257 127 TYR B CE2 
3152 C CZ  . TYR B 127 ? 0.3276 0.3638 0.2850 0.0751  0.0159  -0.0246 127 TYR B CZ  
3153 O OH  . TYR B 127 ? 0.4048 0.4423 0.3664 0.0814  0.0128  -0.0258 127 TYR B OH  
3154 N N   . GLY B 128 ? 0.3665 0.4284 0.3014 0.0540  0.0357  -0.0128 128 GLY B N   
3155 C CA  . GLY B 128 ? 0.3693 0.4353 0.2953 0.0518  0.0393  -0.0105 128 GLY B CA  
3156 C C   . GLY B 128 ? 0.3413 0.3861 0.2577 0.0446  0.0345  -0.0106 128 GLY B C   
3157 O O   . GLY B 128 ? 0.3977 0.4388 0.3007 0.0456  0.0357  -0.0117 128 GLY B O   
3158 N N   . ASP B 129 ? 0.3032 0.3360 0.2265 0.0375  0.0292  -0.0093 129 ASP B N   
3159 C CA  . ASP B 129 ? 0.3033 0.3202 0.2214 0.0298  0.0248  -0.0080 129 ASP B CA  
3160 C C   . ASP B 129 ? 0.2874 0.2936 0.2139 0.0255  0.0195  -0.0082 129 ASP B C   
3161 O O   . ASP B 129 ? 0.2815 0.2929 0.2171 0.0280  0.0193  -0.0090 129 ASP B O   
3162 C CB  . ASP B 129 ? 0.3120 0.3388 0.2342 0.0216  0.0266  -0.0002 129 ASP B CB  
3163 C CG  . ASP B 129 ? 0.3629 0.4062 0.3030 0.0161  0.0285  0.0066  129 ASP B CG  
3164 O OD1 . ASP B 129 ? 0.3172 0.3568 0.2674 0.0139  0.0252  0.0060  129 ASP B OD1 
3165 O OD2 . ASP B 129 ? 0.4031 0.4632 0.3467 0.0139  0.0331  0.0126  129 ASP B OD2 
3166 N N   . PHE B 130 ? 0.2784 0.2718 0.2021 0.0190  0.0153  -0.0072 130 PHE B N   
3167 C CA  . PHE B 130 ? 0.2739 0.2575 0.2035 0.0153  0.0106  -0.0077 130 PHE B CA  
3168 C C   . PHE B 130 ? 0.2603 0.2551 0.2061 0.0116  0.0108  -0.0038 130 PHE B C   
3169 O O   . PHE B 130 ? 0.2459 0.2388 0.1972 0.0131  0.0087  -0.0057 130 PHE B O   
3170 C CB  . PHE B 130 ? 0.2801 0.2525 0.2058 0.0089  0.0067  -0.0064 130 PHE B CB  
3171 C CG  . PHE B 130 ? 0.2584 0.2240 0.1909 0.0056  0.0026  -0.0065 130 PHE B CG  
3172 C CD1 . PHE B 130 ? 0.2565 0.2276 0.2010 0.0009  0.0016  -0.0029 130 PHE B CD1 
3173 C CD2 . PHE B 130 ? 0.2653 0.2186 0.1914 0.0072  -0.0003 -0.0102 130 PHE B CD2 
3174 C CE1 . PHE B 130 ? 0.2618 0.2278 0.2113 -0.0009 -0.0018 -0.0038 130 PHE B CE1 
3175 C CE2 . PHE B 130 ? 0.2740 0.2233 0.2055 0.0044  -0.0034 -0.0099 130 PHE B CE2 
3176 C CZ  . PHE B 130 ? 0.2666 0.2229 0.2096 0.0009  -0.0040 -0.0071 130 PHE B CZ  
3177 N N   . GLY B 131 ? 0.2593 0.2648 0.2119 0.0066  0.0128  0.0018  131 GLY B N   
3178 C CA  . GLY B 131 ? 0.2306 0.2444 0.1983 0.0017  0.0118  0.0055  131 GLY B CA  
3179 C C   . GLY B 131 ? 0.2505 0.2764 0.2260 0.0061  0.0135  0.0040  131 GLY B C   
3180 O O   . GLY B 131 ? 0.2419 0.2697 0.2276 0.0039  0.0107  0.0038  131 GLY B O   
3181 N N   . LYS B 132 ? 0.2386 0.2738 0.2094 0.0128  0.0180  0.0025  132 LYS B N   
3182 C CA  . LYS B 132 ? 0.2411 0.2888 0.2192 0.0186  0.0195  0.0007  132 LYS B CA  
3183 C C   . LYS B 132 ? 0.2628 0.2976 0.2358 0.0248  0.0160  -0.0053 132 LYS B C   
3184 O O   . LYS B 132 ? 0.2455 0.2852 0.2271 0.0262  0.0139  -0.0062 132 LYS B O   
3185 C CB  . LYS B 132 ? 0.2526 0.3157 0.2270 0.0254  0.0258  0.0008  132 LYS B CB  
3186 C CG  . LYS B 132 ? 0.2738 0.3542 0.2558 0.0184  0.0297  0.0085  132 LYS B CG  
3187 C CD  . LYS B 132 ? 0.3476 0.4442 0.3231 0.0257  0.0368  0.0086  132 LYS B CD  
3188 C CE  . LYS B 132 ? 0.4082 0.5233 0.3919 0.0177  0.0408  0.0177  132 LYS B CE  
3189 N NZ  . LYS B 132 ? 0.5063 0.6070 0.4825 0.0100  0.0386  0.0213  132 LYS B NZ  
3190 N N   . ALA B 133 ? 0.2493 0.2672 0.2079 0.0281  0.0148  -0.0092 133 ALA B N   
3191 C CA  . ALA B 133 ? 0.2382 0.2428 0.1906 0.0338  0.0115  -0.0139 133 ALA B CA  
3192 C C   . ALA B 133 ? 0.2669 0.2653 0.2259 0.0285  0.0069  -0.0131 133 ALA B C   
3193 O O   . ALA B 133 ? 0.2412 0.2371 0.2011 0.0328  0.0046  -0.0152 133 ALA B O   
3194 C CB  . ALA B 133 ? 0.2506 0.2369 0.1863 0.0360  0.0103  -0.0175 133 ALA B CB  
3195 N N   . VAL B 134 ? 0.2341 0.2297 0.1966 0.0201  0.0052  -0.0102 134 VAL B N   
3196 C CA  . VAL B 134 ? 0.2321 0.2207 0.1984 0.0162  0.0009  -0.0103 134 VAL B CA  
3197 C C   . VAL B 134 ? 0.2419 0.2416 0.2204 0.0160  -0.0005 -0.0099 134 VAL B C   
3198 O O   . VAL B 134 ? 0.2345 0.2298 0.2150 0.0150  -0.0040 -0.0111 134 VAL B O   
3199 C CB  . VAL B 134 ? 0.2384 0.2217 0.2051 0.0088  -0.0006 -0.0079 134 VAL B CB  
3200 C CG1 . VAL B 134 ? 0.2319 0.2261 0.2088 0.0038  0.0006  -0.0038 134 VAL B CG1 
3201 C CG2 . VAL B 134 ? 0.2292 0.2049 0.1973 0.0065  -0.0047 -0.0090 134 VAL B CG2 
3202 N N   . GLN B 135 ? 0.2386 0.2535 0.2249 0.0170  0.0022  -0.0083 135 GLN B N   
3203 C CA  . GLN B 135 ? 0.2218 0.2494 0.2206 0.0167  0.0005  -0.0079 135 GLN B CA  
3204 C C   . GLN B 135 ? 0.2606 0.2921 0.2579 0.0256  0.0004  -0.0109 135 GLN B C   
3205 O O   . GLN B 135 ? 0.3032 0.3474 0.3110 0.0261  -0.0013 -0.0107 135 GLN B O   
3206 C CB  . GLN B 135 ? 0.2228 0.2672 0.2325 0.0120  0.0032  -0.0036 135 GLN B CB  
3207 C CG  . GLN B 135 ? 0.2310 0.2708 0.2431 0.0028  0.0024  0.0004  135 GLN B CG  
3208 C CD  . GLN B 135 ? 0.2249 0.2555 0.2413 -0.0024 -0.0033 -0.0007 135 GLN B CD  
3209 O OE1 . GLN B 135 ? 0.2682 0.3017 0.2903 -0.0014 -0.0068 -0.0033 135 GLN B OE1 
3210 N NE2 . GLN B 135 ? 0.2039 0.2236 0.2169 -0.0070 -0.0046 0.0008  135 GLN B NE2 
3211 N N   . GLN B 136 ? 0.2544 0.2754 0.2393 0.0328  0.0014  -0.0135 136 GLN B N   
3212 C CA  . GLN B 136 ? 0.2489 0.2726 0.2317 0.0426  0.0012  -0.0161 136 GLN B CA  
3213 C C   . GLN B 136 ? 0.2598 0.2650 0.2321 0.0456  -0.0026 -0.0182 136 GLN B C   
3214 O O   . GLN B 136 ? 0.2642 0.2539 0.2270 0.0423  -0.0033 -0.0185 136 GLN B O   
3215 C CB  . GLN B 136 ? 0.2641 0.2918 0.2406 0.0503  0.0059  -0.0175 136 GLN B CB  
3216 C CG  . GLN B 136 ? 0.2920 0.3399 0.2779 0.0473  0.0105  -0.0143 136 GLN B CG  
3217 C CD  . GLN B 136 ? 0.3584 0.4285 0.3605 0.0474  0.0103  -0.0124 136 GLN B CD  
3218 O OE1 . GLN B 136 ? 0.4520 0.5236 0.4564 0.0532  0.0074  -0.0144 136 GLN B OE1 
3219 N NE2 . GLN B 136 ? 0.3579 0.4455 0.3714 0.0405  0.0130  -0.0078 136 GLN B NE2 
3220 N N   . PRO B 137 ? 0.2617 0.2689 0.2355 0.0515  -0.0053 -0.0193 137 PRO B N   
3221 C CA  . PRO B 137 ? 0.2830 0.2727 0.2465 0.0535  -0.0090 -0.0199 137 PRO B CA  
3222 C C   . PRO B 137 ? 0.3115 0.2832 0.2603 0.0574  -0.0084 -0.0214 137 PRO B C   
3223 O O   . PRO B 137 ? 0.3394 0.2948 0.2795 0.0540  -0.0109 -0.0207 137 PRO B O   
3224 C CB  . PRO B 137 ? 0.3004 0.2984 0.2682 0.0608  -0.0116 -0.0204 137 PRO B CB  
3225 C CG  . PRO B 137 ? 0.3516 0.3715 0.3349 0.0580  -0.0108 -0.0196 137 PRO B CG  
3226 C CD  . PRO B 137 ? 0.3088 0.3355 0.2946 0.0553  -0.0057 -0.0190 137 PRO B CD  
3227 N N   . ASP B 138 ? 0.2764 0.2507 0.2219 0.0644  -0.0054 -0.0236 138 ASP B N   
3228 C CA  . ASP B 138 ? 0.2899 0.2458 0.2204 0.0686  -0.0054 -0.0262 138 ASP B CA  
3229 C C   . ASP B 138 ? 0.2756 0.2300 0.2025 0.0629  -0.0025 -0.0266 138 ASP B C   
3230 O O   . ASP B 138 ? 0.3095 0.2538 0.2250 0.0675  -0.0016 -0.0297 138 ASP B O   
3231 C CB  . ASP B 138 ? 0.3074 0.2651 0.2338 0.0821  -0.0044 -0.0296 138 ASP B CB  
3232 C CG  . ASP B 138 ? 0.3453 0.3271 0.2815 0.0859  0.0008  -0.0301 138 ASP B CG  
3233 O OD1 . ASP B 138 ? 0.3371 0.3344 0.2845 0.0777  0.0031  -0.0272 138 ASP B OD1 
3234 O OD2 . ASP B 138 ? 0.3802 0.3658 0.3128 0.0978  0.0026  -0.0334 138 ASP B OD2 
3235 N N   . GLY B 139 ? 0.2809 0.2445 0.2166 0.0534  -0.0014 -0.0236 139 GLY B N   
3236 C CA  . GLY B 139 ? 0.2667 0.2326 0.2006 0.0487  0.0015  -0.0231 139 GLY B CA  
3237 C C   . GLY B 139 ? 0.2810 0.2284 0.2032 0.0439  -0.0007 -0.0238 139 GLY B C   
3238 O O   . GLY B 139 ? 0.2802 0.2254 0.1952 0.0441  0.0012  -0.0252 139 GLY B O   
3239 N N   . LEU B 140 ? 0.2828 0.2193 0.2036 0.0389  -0.0045 -0.0224 140 LEU B N   
3240 C CA  . LEU B 140 ? 0.2599 0.1829 0.1727 0.0323  -0.0068 -0.0219 140 LEU B CA  
3241 C C   . LEU B 140 ? 0.2927 0.1973 0.1956 0.0333  -0.0109 -0.0226 140 LEU B C   
3242 O O   . LEU B 140 ? 0.3014 0.2044 0.2055 0.0371  -0.0124 -0.0221 140 LEU B O   
3243 C CB  . LEU B 140 ? 0.2699 0.1989 0.1914 0.0234  -0.0074 -0.0184 140 LEU B CB  
3244 C CG  . LEU B 140 ? 0.2707 0.2153 0.2026 0.0206  -0.0045 -0.0165 140 LEU B CG  
3245 C CD1 . LEU B 140 ? 0.2710 0.2168 0.2090 0.0131  -0.0064 -0.0139 140 LEU B CD1 
3246 C CD2 . LEU B 140 ? 0.2830 0.2295 0.2095 0.0211  -0.0017 -0.0170 140 LEU B CD2 
3247 N N   . ALA B 141 ? 0.2938 0.1847 0.1869 0.0290  -0.0131 -0.0233 141 ALA B N   
3248 C CA  . ALA B 141 ? 0.3153 0.1880 0.1995 0.0265  -0.0177 -0.0226 141 ALA B CA  
3249 C C   . ALA B 141 ? 0.3180 0.1887 0.2022 0.0161  -0.0194 -0.0200 141 ALA B C   
3250 O O   . ALA B 141 ? 0.3280 0.1994 0.2093 0.0137  -0.0189 -0.0216 141 ALA B O   
3251 C CB  . ALA B 141 ? 0.3448 0.1996 0.2149 0.0330  -0.0199 -0.0270 141 ALA B CB  
3252 N N   . VAL B 142 ? 0.3019 0.1721 0.1895 0.0103  -0.0213 -0.0160 142 VAL B N   
3253 C CA  . VAL B 142 ? 0.2979 0.1690 0.1869 0.0009  -0.0229 -0.0132 142 VAL B CA  
3254 C C   . VAL B 142 ? 0.3137 0.1686 0.1940 -0.0038 -0.0274 -0.0110 142 VAL B C   
3255 O O   . VAL B 142 ? 0.3296 0.1798 0.2088 -0.0024 -0.0285 -0.0085 142 VAL B O   
3256 C CB  . VAL B 142 ? 0.2771 0.1645 0.1782 -0.0026 -0.0211 -0.0101 142 VAL B CB  
3257 C CG1 . VAL B 142 ? 0.2945 0.1837 0.1967 -0.0113 -0.0228 -0.0074 142 VAL B CG1 
3258 C CG2 . VAL B 142 ? 0.2828 0.1840 0.1924 0.0007  -0.0176 -0.0116 142 VAL B CG2 
3259 N N   . LEU B 143 ? 0.3419 0.1875 0.2154 -0.0094 -0.0304 -0.0118 143 LEU B N   
3260 C CA  . LEU B 143 ? 0.3553 0.1852 0.2211 -0.0163 -0.0355 -0.0093 143 LEU B CA  
3261 C C   . LEU B 143 ? 0.3463 0.1888 0.2207 -0.0259 -0.0356 -0.0038 143 LEU B C   
3262 O O   . LEU B 143 ? 0.3307 0.1835 0.2098 -0.0295 -0.0350 -0.0042 143 LEU B O   
3263 C CB  . LEU B 143 ? 0.3662 0.1798 0.2200 -0.0172 -0.0394 -0.0139 143 LEU B CB  
3264 C CG  . LEU B 143 ? 0.3937 0.1878 0.2384 -0.0252 -0.0460 -0.0118 143 LEU B CG  
3265 C CD1 . LEU B 143 ? 0.4171 0.1950 0.2557 -0.0218 -0.0482 -0.0099 143 LEU B CD1 
3266 C CD2 . LEU B 143 ? 0.4088 0.1880 0.2413 -0.0251 -0.0500 -0.0182 143 LEU B CD2 
3267 N N   . GLY B 144 ? 0.3252 0.1692 0.2021 -0.0289 -0.0360 0.0014  144 GLY B N   
3268 C CA  . GLY B 144 ? 0.3362 0.1951 0.2216 -0.0366 -0.0352 0.0068  144 GLY B CA  
3269 C C   . GLY B 144 ? 0.3461 0.1950 0.2263 -0.0469 -0.0399 0.0116  144 GLY B C   
3270 O O   . GLY B 144 ? 0.3570 0.1884 0.2286 -0.0476 -0.0431 0.0134  144 GLY B O   
3271 N N   . ILE B 145 ? 0.3145 0.1740 0.2002 -0.0550 -0.0409 0.0139  145 ILE B N   
3272 C CA  . ILE B 145 ? 0.3441 0.1970 0.2268 -0.0668 -0.0459 0.0188  145 ILE B CA  
3273 C C   . ILE B 145 ? 0.3309 0.2071 0.2252 -0.0734 -0.0438 0.0249  145 ILE B C   
3274 O O   . ILE B 145 ? 0.3311 0.2249 0.2341 -0.0711 -0.0410 0.0231  145 ILE B O   
3275 C CB  . ILE B 145 ? 0.3640 0.2057 0.2403 -0.0707 -0.0507 0.0144  145 ILE B CB  
3276 C CG1 . ILE B 145 ? 0.3990 0.2191 0.2631 -0.0622 -0.0521 0.0075  145 ILE B CG1 
3277 C CG2 . ILE B 145 ? 0.3714 0.2069 0.2457 -0.0845 -0.0567 0.0198  145 ILE B CG2 
3278 C CD1 . ILE B 145 ? 0.4232 0.2307 0.2783 -0.0640 -0.0568 0.0017  145 ILE B CD1 
3279 N N   . PHE B 146 ? 0.3201 0.1968 0.2143 -0.0810 -0.0450 0.0324  146 PHE B N   
3280 C CA  . PHE B 146 ? 0.3131 0.2142 0.2181 -0.0869 -0.0425 0.0387  146 PHE B CA  
3281 C C   . PHE B 146 ? 0.3471 0.2543 0.2560 -0.0979 -0.0465 0.0411  146 PHE B C   
3282 O O   . PHE B 146 ? 0.3543 0.2428 0.2555 -0.1052 -0.0526 0.0410  146 PHE B O   
3283 C CB  . PHE B 146 ? 0.3073 0.2093 0.2106 -0.0912 -0.0417 0.0470  146 PHE B CB  
3284 C CG  . PHE B 146 ? 0.3119 0.2118 0.2123 -0.0807 -0.0380 0.0455  146 PHE B CG  
3285 C CD1 . PHE B 146 ? 0.3037 0.2221 0.2115 -0.0716 -0.0326 0.0420  146 PHE B CD1 
3286 C CD2 . PHE B 146 ? 0.3336 0.2121 0.2234 -0.0799 -0.0406 0.0475  146 PHE B CD2 
3287 C CE1 . PHE B 146 ? 0.3234 0.2405 0.2286 -0.0624 -0.0299 0.0403  146 PHE B CE1 
3288 C CE2 . PHE B 146 ? 0.3448 0.2219 0.2318 -0.0700 -0.0378 0.0463  146 PHE B CE2 
3289 C CZ  . PHE B 146 ? 0.3408 0.2385 0.2358 -0.0615 -0.0324 0.0427  146 PHE B CZ  
3290 N N   . LEU B 147 ? 0.3138 0.2471 0.2347 -0.0987 -0.0436 0.0429  147 LEU B N   
3291 C CA  . LEU B 147 ? 0.3245 0.2699 0.2519 -0.1090 -0.0471 0.0462  147 LEU B CA  
3292 C C   . LEU B 147 ? 0.3124 0.2783 0.2478 -0.1167 -0.0451 0.0556  147 LEU B C   
3293 O O   . LEU B 147 ? 0.3239 0.3108 0.2669 -0.1102 -0.0391 0.0568  147 LEU B O   
3294 C CB  . LEU B 147 ? 0.3195 0.2811 0.2550 -0.1033 -0.0457 0.0415  147 LEU B CB  
3295 C CG  . LEU B 147 ? 0.3111 0.2568 0.2396 -0.0997 -0.0489 0.0340  147 LEU B CG  
3296 C CD1 . LEU B 147 ? 0.3203 0.2483 0.2402 -0.0892 -0.0465 0.0280  147 LEU B CD1 
3297 C CD2 . LEU B 147 ? 0.3061 0.2695 0.2431 -0.0963 -0.0485 0.0317  147 LEU B CD2 
3298 N N   . LYS B 148 ? 0.3332 0.2938 0.2670 -0.1305 -0.0502 0.0621  148 LYS B N   
3299 C CA  . LYS B 148 ? 0.3656 0.3465 0.3072 -0.1403 -0.0488 0.0725  148 LYS B CA  
3300 C C   . LYS B 148 ? 0.3940 0.3947 0.3464 -0.1499 -0.0520 0.0753  148 LYS B C   
3301 O O   . LYS B 148 ? 0.4405 0.4274 0.3892 -0.1560 -0.0588 0.0723  148 LYS B O   
3302 C CB  . LYS B 148 ? 0.4469 0.4061 0.3789 -0.1506 -0.0529 0.0795  148 LYS B CB  
3303 C CG  . LYS B 148 ? 0.5255 0.5033 0.4640 -0.1625 -0.0518 0.0918  148 LYS B CG  
3304 C CD  . LYS B 148 ? 0.6028 0.5526 0.5300 -0.1733 -0.0575 0.0985  148 LYS B CD  
3305 C CE  . LYS B 148 ? 0.6490 0.6194 0.5827 -0.1817 -0.0555 0.1100  148 LYS B CE  
3306 N NZ  . LYS B 148 ? 0.7148 0.6593 0.6377 -0.1854 -0.0601 0.1140  148 LYS B NZ  
3307 N N   . VAL B 149 ? 0.3605 0.3942 0.3258 -0.1510 -0.0473 0.0811  149 VAL B N   
3308 C CA  . VAL B 149 ? 0.3952 0.4527 0.3727 -0.1593 -0.0500 0.0844  149 VAL B CA  
3309 C C   . VAL B 149 ? 0.3904 0.4420 0.3674 -0.1785 -0.0569 0.0932  149 VAL B C   
3310 O O   . VAL B 149 ? 0.4311 0.4808 0.4058 -0.1863 -0.0559 0.1018  149 VAL B O   
3311 C CB  . VAL B 149 ? 0.4303 0.5264 0.4219 -0.1535 -0.0427 0.0879  149 VAL B CB  
3312 C CG1 . VAL B 149 ? 0.4197 0.5431 0.4251 -0.1638 -0.0457 0.0934  149 VAL B CG1 
3313 C CG2 . VAL B 149 ? 0.4241 0.5246 0.4171 -0.1357 -0.0381 0.0785  149 VAL B CG2 
3314 N N   . GLY B 150 ? 0.3847 0.4325 0.3632 -0.1866 -0.0643 0.0912  150 GLY B N   
3315 C CA  . GLY B 150 ? 0.3992 0.4381 0.3748 -0.1975 -0.0711 0.0954  150 GLY B CA  
3316 C C   . GLY B 150 ? 0.3997 0.4370 0.3764 -0.1999 -0.0779 0.0900  150 GLY B C   
3317 O O   . GLY B 150 ? 0.3920 0.4553 0.3803 -0.1966 -0.0761 0.0888  150 GLY B O   
3318 N N   . SER B 151 ? 0.4266 0.4344 0.3911 -0.2047 -0.0856 0.0867  151 SER B N   
3319 C CA  . SER B 151 ? 0.4094 0.4130 0.3724 -0.2065 -0.0924 0.0810  151 SER B CA  
3320 C C   . SER B 151 ? 0.3989 0.3954 0.3575 -0.1956 -0.0915 0.0710  151 SER B C   
3321 O O   . SER B 151 ? 0.4383 0.4201 0.3896 -0.1877 -0.0878 0.0670  151 SER B O   
3322 C CB  . SER B 151 ? 0.4758 0.4480 0.4254 -0.2131 -0.1005 0.0791  151 SER B CB  
3323 O OG  . SER B 151 ? 0.5725 0.5530 0.5272 -0.2246 -0.1027 0.0886  151 SER B OG  
3324 N N   . ALA B 152 ? 0.4372 0.4449 0.4001 -0.1953 -0.0950 0.0676  152 ALA B N   
3325 C CA  . ALA B 152 ? 0.4333 0.4351 0.3915 -0.1854 -0.0951 0.0586  152 ALA B CA  
3326 C C   . ALA B 152 ? 0.4655 0.4290 0.4042 -0.1819 -0.0987 0.0505  152 ALA B C   
3327 O O   . ALA B 152 ? 0.4934 0.4374 0.4234 -0.1880 -0.1042 0.0503  152 ALA B O   
3328 C CB  . ALA B 152 ? 0.4054 0.4265 0.3713 -0.1863 -0.0991 0.0574  152 ALA B CB  
3329 N N   . LEU B 153 ? 0.4220 0.3756 0.3541 -0.1714 -0.0957 0.0435  153 LEU B N   
3330 C CA  . LEU B 153 ? 0.4077 0.3282 0.3216 -0.1656 -0.0980 0.0352  153 LEU B CA  
3331 C C   . LEU B 153 ? 0.3905 0.3089 0.2987 -0.1616 -0.1020 0.0280  153 LEU B C   
3332 O O   . LEU B 153 ? 0.3869 0.3199 0.2997 -0.1548 -0.0993 0.0258  153 LEU B O   
3333 C CB  . LEU B 153 ? 0.4153 0.3272 0.3249 -0.1540 -0.0908 0.0322  153 LEU B CB  
3334 C CG  . LEU B 153 ? 0.4598 0.3382 0.3511 -0.1475 -0.0924 0.0243  153 LEU B CG  
3335 C CD1 . LEU B 153 ? 0.4848 0.3407 0.3676 -0.1538 -0.0968 0.0265  153 LEU B CD1 
3336 C CD2 . LEU B 153 ? 0.4355 0.3126 0.3259 -0.1327 -0.0834 0.0217  153 LEU B CD2 
3337 N N   . PRO B 154 ? 0.4353 0.3125 0.3167 -0.1657 -0.1105 0.0594  154 PRO B N   
3338 C CA  . PRO B 154 ? 0.4595 0.3268 0.3344 -0.1642 -0.1308 0.0617  154 PRO B CA  
3339 C C   . PRO B 154 ? 0.4644 0.3170 0.3061 -0.1511 -0.1262 0.0559  154 PRO B C   
3340 O O   . PRO B 154 ? 0.4980 0.3504 0.3415 -0.1486 -0.1367 0.0576  154 PRO B O   
3341 C CB  . PRO B 154 ? 0.5090 0.3502 0.3578 -0.1749 -0.1467 0.0643  154 PRO B CB  
3342 C CG  . PRO B 154 ? 0.5257 0.3771 0.3915 -0.1842 -0.1378 0.0656  154 PRO B CG  
3343 C CD  . PRO B 154 ? 0.4925 0.3514 0.3561 -0.1786 -0.1156 0.0609  154 PRO B CD  
3344 N N   . GLY B 155 ? 0.4748 0.3142 0.2884 -0.1438 -0.1121 0.0491  155 GLY B N   
3345 C CA  . GLY B 155 ? 0.4842 0.3110 0.2713 -0.1318 -0.1049 0.0414  155 GLY B CA  
3346 C C   . GLY B 155 ? 0.4499 0.3006 0.2569 -0.1211 -0.0939 0.0411  155 GLY B C   
3347 O O   . GLY B 155 ? 0.4782 0.3199 0.2652 -0.1127 -0.0894 0.0351  155 GLY B O   
3348 N N   . LEU B 156 ? 0.4067 0.2863 0.2526 -0.1223 -0.0869 0.0459  156 LEU B N   
3349 C CA  . LEU B 156 ? 0.3793 0.2821 0.2484 -0.1131 -0.0753 0.0452  156 LEU B CA  
3350 C C   . LEU B 156 ? 0.3736 0.2885 0.2729 -0.1143 -0.0901 0.0504  156 LEU B C   
3351 O O   . LEU B 156 ? 0.3533 0.2818 0.2684 -0.1057 -0.0848 0.0498  156 LEU B O   
3352 C CB  . LEU B 156 ? 0.3662 0.2897 0.2599 -0.1160 -0.0558 0.0452  156 LEU B CB  
3353 C CG  . LEU B 156 ? 0.3626 0.3080 0.2779 -0.1082 -0.0379 0.0428  156 LEU B CG  
3354 C CD1 . LEU B 156 ? 0.3468 0.2811 0.2295 -0.0956 -0.0319 0.0384  156 LEU B CD1 
3355 C CD2 . LEU B 156 ? 0.3654 0.3238 0.2982 -0.1180 -0.0174 0.0417  156 LEU B CD2 
3356 N N   . GLN B 157 ? 0.3734 0.2811 0.2808 -0.1252 -0.1114 0.0563  157 GLN B N   
3357 C CA  . GLN B 157 ? 0.3574 0.2798 0.3076 -0.1277 -0.1291 0.0634  157 GLN B CA  
3358 C C   . GLN B 157 ? 0.3916 0.2987 0.3191 -0.1221 -0.1414 0.0645  157 GLN B C   
3359 O O   . GLN B 157 ? 0.3604 0.2848 0.3258 -0.1170 -0.1462 0.0680  157 GLN B O   
3360 C CB  . GLN B 157 ? 0.4076 0.3234 0.3719 -0.1426 -0.1532 0.0708  157 GLN B CB  
3361 C CG  . GLN B 157 ? 0.4282 0.3696 0.4622 -0.1453 -0.1696 0.0782  157 GLN B CG  
3362 C CD  . GLN B 157 ? 0.4445 0.4264 0.5420 -0.1391 -0.1429 0.0730  157 GLN B CD  
3363 O OE1 . GLN B 157 ? 0.4346 0.4264 0.5334 -0.1425 -0.1182 0.0669  157 GLN B OE1 
3364 N NE2 . GLN B 157 ? 0.3989 0.4003 0.5485 -0.1325 -0.1487 0.0751  157 GLN B NE2 
3365 N N   . LYS B 158 ? 0.4145 0.2883 0.2811 -0.1233 -0.1435 0.0599  158 LYS B N   
3366 C CA  . LYS B 158 ? 0.4428 0.2979 0.2809 -0.1218 -0.1527 0.0597  158 LYS B CA  
3367 C C   . LYS B 158 ? 0.3945 0.2708 0.2483 -0.1067 -0.1329 0.0555  158 LYS B C   
3368 O O   . LYS B 158 ? 0.4205 0.2957 0.2799 -0.1043 -0.1430 0.0591  158 LYS B O   
3369 C CB  . LYS B 158 ? 0.5042 0.3240 0.2915 -0.1216 -0.1386 0.0511  158 LYS B CB  
3370 C CG  . LYS B 158 ? 0.5524 0.3503 0.3182 -0.1217 -0.1388 0.0498  158 LYS B CG  
3371 C CD  . LYS B 158 ? 0.5845 0.3570 0.3125 -0.1215 -0.1186 0.0381  158 LYS B CD  
3372 C CE  . LYS B 158 ? 0.5928 0.3448 0.2994 -0.1242 -0.1157 0.0363  158 LYS B CE  
3373 N NZ  . LYS B 158 ? 0.6359 0.3546 0.3199 -0.1411 -0.1339 0.0455  158 LYS B NZ  
3374 N N   . VAL B 159 ? 0.3559 0.2485 0.2145 -0.0978 -0.1064 0.0485  159 VAL B N   
3375 C CA  . VAL B 159 ? 0.3267 0.2390 0.1997 -0.0853 -0.0871 0.0448  159 VAL B CA  
3376 C C   . VAL B 159 ? 0.3386 0.2802 0.2718 -0.0833 -0.0891 0.0506  159 VAL B C   
3377 O O   . VAL B 159 ? 0.3426 0.2902 0.2898 -0.0768 -0.0915 0.0519  159 VAL B O   
3378 C CB  . VAL B 159 ? 0.3368 0.2561 0.2015 -0.0801 -0.0629 0.0383  159 VAL B CB  
3379 C CG1 . VAL B 159 ? 0.3278 0.2677 0.2092 -0.0701 -0.0432 0.0357  159 VAL B CG1 
3380 C CG2 . VAL B 159 ? 0.3869 0.2786 0.2027 -0.0791 -0.0595 0.0305  159 VAL B CG2 
3381 N N   . VAL B 160 ? 0.3346 0.2949 0.3080 -0.0892 -0.0860 0.0527  160 VAL B N   
3382 C CA  A VAL B 160 ? 0.3313 0.3224 0.3728 -0.0881 -0.0816 0.0545  160 VAL B CA  
3383 C CA  B VAL B 160 ? 0.3311 0.3218 0.3700 -0.0868 -0.0804 0.0541  160 VAL B CA  
3384 C C   . VAL B 160 ? 0.3361 0.3254 0.4061 -0.0874 -0.1102 0.0623  160 VAL B C   
3385 O O   . VAL B 160 ? 0.3416 0.3495 0.4576 -0.0802 -0.1074 0.0624  160 VAL B O   
3386 C CB  A VAL B 160 ? 0.3609 0.3671 0.4373 -0.0989 -0.0758 0.0544  160 VAL B CB  
3387 C CB  B VAL B 160 ? 0.3549 0.3656 0.4325 -0.0956 -0.0665 0.0521  160 VAL B CB  
3388 C CG1 A VAL B 160 ? 0.3407 0.3739 0.4965 -0.1011 -0.0824 0.0569  160 VAL B CG1 
3389 C CG1 B VAL B 160 ? 0.3678 0.3780 0.4155 -0.0955 -0.0368 0.0449  160 VAL B CG1 
3390 C CG2 A VAL B 160 ? 0.3722 0.3853 0.4358 -0.1003 -0.0436 0.0469  160 VAL B CG2 
3391 C CG2 B VAL B 160 ? 0.3649 0.3627 0.4354 -0.1073 -0.0880 0.0576  160 VAL B CG2 
3392 N N   . ASP B 161 ? 0.3483 0.3111 0.3897 -0.0965 -0.1399 0.0694  161 ASP B N   
3393 C CA  . ASP B 161 ? 0.3897 0.3436 0.4546 -0.1008 -0.1752 0.0800  161 ASP B CA  
3394 C C   . ASP B 161 ? 0.3887 0.3289 0.4318 -0.0936 -0.1814 0.0811  161 ASP B C   
3395 O O   . ASP B 161 ? 0.4858 0.4248 0.5647 -0.0944 -0.2084 0.0901  161 ASP B O   
3396 C CB  . ASP B 161 ? 0.4418 0.3614 0.4645 -0.1166 -0.2056 0.0873  161 ASP B CB  
3397 C CG  . ASP B 161 ? 0.4483 0.3815 0.5081 -0.1264 -0.2117 0.0904  161 ASP B CG  
3398 O OD1 . ASP B 161 ? 0.4331 0.4033 0.5605 -0.1222 -0.1960 0.0875  161 ASP B OD1 
3399 O OD2 . ASP B 161 ? 0.5116 0.4150 0.5284 -0.1350 -0.2234 0.0943  161 ASP B OD2 
3400 N N   . VAL B 162 ? 0.3532 0.2808 0.3398 -0.0876 -0.1595 0.0726  162 VAL B N   
3401 C CA  . VAL B 162 ? 0.3755 0.2862 0.3322 -0.0831 -0.1640 0.0727  162 VAL B CA  
3402 C C   . VAL B 162 ? 0.3362 0.2764 0.3317 -0.0680 -0.1399 0.0677  162 VAL B C   
3403 O O   . VAL B 162 ? 0.3576 0.2886 0.3440 -0.0635 -0.1460 0.0693  162 VAL B O   
3404 C CB  . VAL B 162 ? 0.4043 0.2826 0.2788 -0.0869 -0.1532 0.0645  162 VAL B CB  
3405 C CG1 . VAL B 162 ? 0.4092 0.3052 0.2760 -0.0752 -0.1168 0.0530  162 VAL B CG1 
3406 C CG2 . VAL B 162 ? 0.4690 0.3171 0.3102 -0.0894 -0.1580 0.0633  162 VAL B CG2 
3407 N N   . LEU B 163 ? 0.2946 0.2672 0.3329 -0.0626 -0.1138 0.0620  163 LEU B N   
3408 C CA  . LEU B 163 ? 0.2714 0.2654 0.3307 -0.0511 -0.0858 0.0550  163 LEU B CA  
3409 C C   . LEU B 163 ? 0.3042 0.3104 0.4209 -0.0449 -0.0977 0.0593  163 LEU B C   
3410 O O   . LEU B 163 ? 0.2735 0.2840 0.3886 -0.0358 -0.0829 0.0552  163 LEU B O   
3411 C CB  . LEU B 163 ? 0.2514 0.2699 0.3354 -0.0519 -0.0552 0.0477  163 LEU B CB  
3412 C CG  . LEU B 163 ? 0.3031 0.3053 0.3281 -0.0564 -0.0460 0.0442  163 LEU B CG  
3413 C CD1 . LEU B 163 ? 0.3783 0.3980 0.4208 -0.0604 -0.0196 0.0389  163 LEU B CD1 
3414 C CD2 . LEU B 163 ? 0.2811 0.2679 0.2522 -0.0495 -0.0356 0.0394  163 LEU B CD2 
3415 N N   . ASP B 164 ? 0.3249 0.3369 0.4974 -0.0496 -0.1250 0.0675  164 ASP B N   
3416 C CA  . ASP B 164 ? 0.3194 0.3423 0.5559 -0.0425 -0.1390 0.0715  164 ASP B CA  
3417 C C   . ASP B 164 ? 0.3336 0.3248 0.5237 -0.0410 -0.1626 0.0785  164 ASP B C   
3418 O O   . ASP B 164 ? 0.3415 0.3380 0.5727 -0.0330 -0.1698 0.0806  164 ASP B O   
3419 C CB  . ASP B 164 ? 0.4437 0.4777 0.7557 -0.0483 -0.1690 0.0799  164 ASP B CB  
3420 C CG  . ASP B 164 ? 0.5388 0.6138 0.9308 -0.0472 -0.1394 0.0698  164 ASP B CG  
3421 O OD1 . ASP B 164 ? 0.5470 0.6406 0.9451 -0.0412 -0.0979 0.0572  164 ASP B OD1 
3422 O OD2 . ASP B 164 ? 0.5772 0.6635 1.0225 -0.0547 -0.1566 0.0739  164 ASP B OD2 
3423 N N   . SER B 165 ? 0.3301 0.2866 0.4350 -0.0495 -0.1723 0.0806  165 SER B N   
3424 C CA  . SER B 165 ? 0.3460 0.2678 0.3957 -0.0521 -0.1899 0.0850  165 SER B CA  
3425 C C   . SER B 165 ? 0.3273 0.2512 0.3365 -0.0428 -0.1560 0.0740  165 SER B C   
3426 O O   . SER B 165 ? 0.3996 0.2969 0.3661 -0.0447 -0.1663 0.0761  165 SER B O   
3427 C CB  . SER B 165 ? 0.4727 0.3506 0.4496 -0.0696 -0.2108 0.0888  165 SER B CB  
3428 O OG  . SER B 165 ? 0.5023 0.3740 0.4205 -0.0718 -0.1852 0.0784  165 SER B OG  
3429 N N   . ILE B 166 ? 0.2901 0.2419 0.3094 -0.0348 -0.1178 0.0631  166 ILE B N   
3430 C CA  . ILE B 166 ? 0.2812 0.2344 0.2643 -0.0271 -0.0886 0.0538  166 ILE B CA  
3431 C C   . ILE B 166 ? 0.2504 0.2386 0.2871 -0.0168 -0.0583 0.0472  166 ILE B C   
3432 O O   . ILE B 166 ? 0.2262 0.2240 0.2421 -0.0145 -0.0286 0.0388  166 ILE B O   
3433 C CB  . ILE B 166 ? 0.2741 0.2140 0.1933 -0.0315 -0.0729 0.0463  166 ILE B CB  
3434 C CG1 . ILE B 166 ? 0.2550 0.2108 0.1921 -0.0344 -0.0626 0.0441  166 ILE B CG1 
3435 C CG2 . ILE B 166 ? 0.3494 0.2488 0.2084 -0.0438 -0.0971 0.0494  166 ILE B CG2 
3436 C CD1 . ILE B 166 ? 0.2854 0.2372 0.1780 -0.0332 -0.0392 0.0350  166 ILE B CD1 
3437 N N   . LYS B 167 ? 0.2655 0.2748 0.2605 -0.0241 -0.0592 0.0329  167 LYS B N   
3438 C CA  . LYS B 167 ? 0.2641 0.2795 0.2661 -0.0203 -0.0552 0.0317  167 LYS B CA  
3439 C C   . LYS B 167 ? 0.2674 0.2777 0.2684 -0.0134 -0.0531 0.0289  167 LYS B C   
3440 O O   . LYS B 167 ? 0.2702 0.2808 0.2705 -0.0105 -0.0488 0.0267  167 LYS B O   
3441 C CB  . LYS B 167 ? 0.2758 0.3049 0.2919 -0.0192 -0.0571 0.0341  167 LYS B CB  
3442 C CG  . LYS B 167 ? 0.3482 0.3861 0.3722 -0.0139 -0.0526 0.0327  167 LYS B CG  
3443 C CD  . LYS B 167 ? 0.3857 0.4383 0.4242 -0.0122 -0.0549 0.0353  167 LYS B CD  
3444 C CE  . LYS B 167 ? 0.4905 0.5533 0.5370 -0.0053 -0.0503 0.0336  167 LYS B CE  
3445 N NZ  . LYS B 167 ? 0.6116 0.6796 0.6556 -0.0084 -0.0449 0.0341  167 LYS B NZ  
3446 N N   . THR B 168 ? 0.2585 0.2648 0.2598 -0.0109 -0.0566 0.0295  168 THR B N   
3447 C CA  . THR B 168 ? 0.2392 0.2409 0.2411 -0.0048 -0.0562 0.0274  168 THR B CA  
3448 C C   . THR B 168 ? 0.2552 0.2470 0.2476 -0.0055 -0.0565 0.0273  168 THR B C   
3449 O O   . THR B 168 ? 0.2537 0.2429 0.2396 -0.0096 -0.0577 0.0290  168 THR B O   
3450 C CB  . THR B 168 ? 0.2596 0.2654 0.2723 -0.0007 -0.0607 0.0286  168 THR B CB  
3451 O OG1 . THR B 168 ? 0.2840 0.2909 0.2978 -0.0045 -0.0656 0.0325  168 THR B OG1 
3452 C CG2 . THR B 168 ? 0.2937 0.3101 0.3163 0.0021  -0.0594 0.0280  168 THR B CG2 
3453 N N   . LYS B 169 ? 0.2525 0.2394 0.2440 -0.0009 -0.0556 0.0252  169 LYS B N   
3454 C CA  . LYS B 169 ? 0.2596 0.2387 0.2431 -0.0011 -0.0556 0.0255  169 LYS B CA  
3455 C C   . LYS B 169 ? 0.2624 0.2414 0.2455 -0.0037 -0.0599 0.0295  169 LYS B C   
3456 O O   . LYS B 169 ? 0.2720 0.2537 0.2627 -0.0028 -0.0645 0.0319  169 LYS B O   
3457 C CB  . LYS B 169 ? 0.2501 0.2246 0.2349 0.0039  -0.0559 0.0234  169 LYS B CB  
3458 C CG  . LYS B 169 ? 0.2477 0.2156 0.2253 0.0034  -0.0560 0.0244  169 LYS B CG  
3459 C CD  . LYS B 169 ? 0.2508 0.2135 0.2293 0.0077  -0.0571 0.0223  169 LYS B CD  
3460 C CE  . LYS B 169 ? 0.2983 0.2561 0.2710 0.0066  -0.0576 0.0243  169 LYS B CE  
3461 N NZ  . LYS B 169 ? 0.3482 0.3002 0.3207 0.0103  -0.0589 0.0221  169 LYS B NZ  
3462 N N   . GLY B 170 ? 0.2583 0.2341 0.2323 -0.0062 -0.0584 0.0302  170 GLY B N   
3463 C CA  . GLY B 170 ? 0.2668 0.2434 0.2387 -0.0081 -0.0615 0.0340  170 GLY B CA  
3464 C C   . GLY B 170 ? 0.2780 0.2584 0.2474 -0.0122 -0.0630 0.0355  170 GLY B C   
3465 O O   . GLY B 170 ? 0.3003 0.2816 0.2649 -0.0139 -0.0646 0.0383  170 GLY B O   
3466 N N   . LYS B 171 ? 0.2471 0.2305 0.2197 -0.0139 -0.0626 0.0341  171 LYS B N   
3467 C CA  . LYS B 171 ? 0.2550 0.2414 0.2252 -0.0183 -0.0649 0.0355  171 LYS B CA  
3468 C C   . LYS B 171 ? 0.2592 0.2397 0.2164 -0.0204 -0.0623 0.0333  171 LYS B C   
3469 O O   . LYS B 171 ? 0.2687 0.2440 0.2214 -0.0194 -0.0584 0.0303  171 LYS B O   
3470 C CB  . LYS B 171 ? 0.2842 0.2765 0.2626 -0.0200 -0.0657 0.0353  171 LYS B CB  
3471 C CG  . LYS B 171 ? 0.2999 0.2985 0.2912 -0.0171 -0.0689 0.0374  171 LYS B CG  
3472 C CD  . LYS B 171 ? 0.3541 0.3611 0.3537 -0.0194 -0.0707 0.0385  171 LYS B CD  
3473 C CE  . LYS B 171 ? 0.3695 0.3792 0.3666 -0.0247 -0.0752 0.0417  171 LYS B CE  
3474 N NZ  . LYS B 171 ? 0.4160 0.4353 0.4228 -0.0271 -0.0778 0.0435  171 LYS B NZ  
3475 N N   . SER B 172 ? 0.2775 0.2582 0.2281 -0.0231 -0.0647 0.0347  172 SER B N   
3476 C CA  A SER B 172 ? 0.2753 0.2493 0.2125 -0.0245 -0.0631 0.0320  172 SER B CA  
3477 C CA  B SER B 172 ? 0.2725 0.2467 0.2093 -0.0243 -0.0632 0.0322  172 SER B CA  
3478 C C   . SER B 172 ? 0.2975 0.2728 0.2307 -0.0290 -0.0670 0.0326  172 SER B C   
3479 O O   . SER B 172 ? 0.3181 0.3005 0.2588 -0.0310 -0.0710 0.0358  172 SER B O   
3480 C CB  A SER B 172 ? 0.2906 0.2624 0.2200 -0.0212 -0.0613 0.0323  172 SER B CB  
3481 C CB  B SER B 172 ? 0.2935 0.2666 0.2232 -0.0212 -0.0619 0.0332  172 SER B CB  
3482 O OG  A SER B 172 ? 0.2810 0.2592 0.2119 -0.0218 -0.0646 0.0364  172 SER B OG  
3483 O OG  B SER B 172 ? 0.2802 0.2473 0.1959 -0.0209 -0.0603 0.0304  172 SER B OG  
3484 N N   . ALA B 173 ? 0.2768 0.2445 0.1980 -0.0308 -0.0665 0.0293  173 ALA B N   
3485 C CA  . ALA B 173 ? 0.2861 0.2528 0.2012 -0.0353 -0.0709 0.0290  173 ALA B CA  
3486 C C   . ALA B 173 ? 0.2678 0.2244 0.1658 -0.0343 -0.0701 0.0250  173 ALA B C   
3487 O O   . ALA B 173 ? 0.2939 0.2428 0.1864 -0.0316 -0.0664 0.0220  173 ALA B O   
3488 C CB  . ALA B 173 ? 0.3089 0.2765 0.2302 -0.0406 -0.0732 0.0290  173 ALA B CB  
3489 N N   . ASP B 174 ? 0.2773 0.2334 0.1664 -0.0362 -0.0740 0.0247  174 ASP B N   
3490 C CA  . ASP B 174 ? 0.3164 0.2615 0.1882 -0.0350 -0.0740 0.0199  174 ASP B CA  
3491 C C   . ASP B 174 ? 0.3401 0.2743 0.2087 -0.0385 -0.0748 0.0165  174 ASP B C   
3492 O O   . ASP B 174 ? 0.3340 0.2708 0.2114 -0.0440 -0.0777 0.0183  174 ASP B O   
3493 C CB  . ASP B 174 ? 0.3170 0.2628 0.1792 -0.0373 -0.0790 0.0197  174 ASP B CB  
3494 C CG  . ASP B 174 ? 0.3575 0.3148 0.2220 -0.0349 -0.0789 0.0240  174 ASP B CG  
3495 O OD1 . ASP B 174 ? 0.3748 0.3366 0.2425 -0.0303 -0.0747 0.0259  174 ASP B OD1 
3496 O OD2 . ASP B 174 ? 0.4516 0.4125 0.3130 -0.0381 -0.0838 0.0256  174 ASP B OD2 
3497 N N   . PHE B 175 ? 0.3072 0.2298 0.1635 -0.0352 -0.0728 0.0120  175 PHE B N   
3498 C CA  . PHE B 175 ? 0.3200 0.2310 0.1732 -0.0385 -0.0737 0.0093  175 PHE B CA  
3499 C C   . PHE B 175 ? 0.3241 0.2205 0.1585 -0.0349 -0.0742 0.0036  175 PHE B C   
3500 O O   . PHE B 175 ? 0.3620 0.2529 0.1916 -0.0291 -0.0699 0.0014  175 PHE B O   
3501 C CB  . PHE B 175 ? 0.3095 0.2226 0.1728 -0.0370 -0.0688 0.0109  175 PHE B CB  
3502 C CG  . PHE B 175 ? 0.3383 0.2435 0.2023 -0.0422 -0.0702 0.0103  175 PHE B CG  
3503 C CD1 . PHE B 175 ? 0.3650 0.2764 0.2389 -0.0493 -0.0736 0.0135  175 PHE B CD1 
3504 C CD2 . PHE B 175 ? 0.3256 0.2177 0.1801 -0.0401 -0.0686 0.0071  175 PHE B CD2 
3505 C CE1 . PHE B 175 ? 0.3941 0.2998 0.2695 -0.0550 -0.0750 0.0142  175 PHE B CE1 
3506 C CE2 . PHE B 175 ? 0.3554 0.2403 0.2110 -0.0458 -0.0703 0.0077  175 PHE B CE2 
3507 C CZ  . PHE B 175 ? 0.3712 0.2631 0.2368 -0.0534 -0.0735 0.0114  175 PHE B CZ  
3508 N N   . THR B 176 ? 0.3441 0.2336 0.1679 -0.0382 -0.0800 0.0010  176 THR B N   
3509 C CA  . THR B 176 ? 0.3667 0.2432 0.1711 -0.0337 -0.0813 -0.0051 176 THR B CA  
3510 C C   . THR B 176 ? 0.4342 0.2926 0.2292 -0.0383 -0.0867 -0.0090 176 THR B C   
3511 O O   . THR B 176 ? 0.4372 0.2949 0.2401 -0.0466 -0.0906 -0.0064 176 THR B O   
3512 C CB  . THR B 176 ? 0.3729 0.2548 0.1693 -0.0327 -0.0842 -0.0056 176 THR B CB  
3513 O OG1 . THR B 176 ? 0.4006 0.2851 0.2018 -0.0412 -0.0907 -0.0033 176 THR B OG1 
3514 C CG2 . THR B 176 ? 0.4034 0.3030 0.2093 -0.0282 -0.0790 -0.0008 176 THR B CG2 
3515 N N   . ASN B 177 ? 0.4273 0.2710 0.2055 -0.0325 -0.0868 -0.0152 177 ASN B N   
3516 C CA  . ASN B 177 ? 0.4596 0.2828 0.2254 -0.0361 -0.0932 -0.0198 177 ASN B CA  
3517 C C   . ASN B 177 ? 0.4734 0.2913 0.2488 -0.0419 -0.0933 -0.0169 177 ASN B C   
3518 O O   . ASN B 177 ? 0.5276 0.3322 0.2986 -0.0490 -0.1001 -0.0177 177 ASN B O   
3519 C CB  . ASN B 177 ? 0.5122 0.3322 0.2722 -0.0433 -0.1017 -0.0207 177 ASN B CB  
3520 C CG  . ASN B 177 ? 0.5179 0.3447 0.2681 -0.0380 -0.1016 -0.0230 177 ASN B CG  
3521 O OD1 . ASN B 177 ? 0.5452 0.3852 0.3019 -0.0421 -0.1036 -0.0192 177 ASN B OD1 
3522 N ND2 . ASN B 177 ? 0.5033 0.3216 0.2375 -0.0286 -0.0992 -0.0290 177 ASN B ND2 
3523 N N   . PHE B 178 ? 0.4414 0.2682 0.2285 -0.0389 -0.0864 -0.0134 178 PHE B N   
3524 C CA  . PHE B 178 ? 0.4313 0.2540 0.2264 -0.0437 -0.0860 -0.0105 178 PHE B CA  
3525 C C   . PHE B 178 ? 0.4735 0.2783 0.2564 -0.0385 -0.0853 -0.0148 178 PHE B C   
3526 O O   . PHE B 178 ? 0.4767 0.2816 0.2543 -0.0291 -0.0804 -0.0175 178 PHE B O   
3527 C CB  . PHE B 178 ? 0.4090 0.2494 0.2220 -0.0431 -0.0793 -0.0049 178 PHE B CB  
3528 C CG  . PHE B 178 ? 0.4024 0.2406 0.2233 -0.0481 -0.0786 -0.0016 178 PHE B CG  
3529 C CD1 . PHE B 178 ? 0.4183 0.2578 0.2460 -0.0579 -0.0833 0.0020  178 PHE B CD1 
3530 C CD2 . PHE B 178 ? 0.3635 0.1979 0.1840 -0.0432 -0.0737 -0.0018 178 PHE B CD2 
3531 C CE1 . PHE B 178 ? 0.4400 0.2782 0.2744 -0.0628 -0.0824 0.0058  178 PHE B CE1 
3532 C CE2 . PHE B 178 ? 0.4089 0.2410 0.2353 -0.0478 -0.0731 0.0015  178 PHE B CE2 
3533 C CZ  . PHE B 178 ? 0.4037 0.2383 0.2371 -0.0576 -0.0772 0.0055  178 PHE B CZ  
3534 N N   . ASP B 179 ? 0.4607 0.2509 0.2403 -0.0451 -0.0906 -0.0147 179 ASP B N   
3535 C CA  . ASP B 179 ? 0.4680 0.2389 0.2361 -0.0413 -0.0915 -0.0183 179 ASP B CA  
3536 C C   . ASP B 179 ? 0.4649 0.2399 0.2441 -0.0424 -0.0868 -0.0134 179 ASP B C   
3537 O O   . ASP B 179 ? 0.4503 0.2253 0.2373 -0.0517 -0.0895 -0.0086 179 ASP B O   
3538 C CB  . ASP B 179 ? 0.4871 0.2378 0.2441 -0.0486 -0.1016 -0.0208 179 ASP B CB  
3539 C CG  . ASP B 179 ? 0.5454 0.2734 0.2899 -0.0454 -0.1042 -0.0245 179 ASP B CG  
3540 O OD1 . ASP B 179 ? 0.5026 0.2311 0.2463 -0.0366 -0.0979 -0.0255 179 ASP B OD1 
3541 O OD2 . ASP B 179 ? 0.6116 0.3212 0.3474 -0.0521 -0.1132 -0.0260 179 ASP B OD2 
3542 N N   . PRO B 180 ? 0.4310 0.2102 0.2113 -0.0337 -0.0799 -0.0140 180 PRO B N   
3543 C CA  . PRO B 180 ? 0.4363 0.2195 0.2265 -0.0351 -0.0757 -0.0093 180 PRO B CA  
3544 C C   . PRO B 180 ? 0.4496 0.2130 0.2321 -0.0384 -0.0802 -0.0094 180 PRO B C   
3545 O O   . PRO B 180 ? 0.4341 0.2004 0.2245 -0.0417 -0.0779 -0.0047 180 PRO B O   
3546 C CB  . PRO B 180 ? 0.4223 0.2140 0.2140 -0.0246 -0.0683 -0.0103 180 PRO B CB  
3547 C CG  . PRO B 180 ? 0.4601 0.2432 0.2369 -0.0166 -0.0697 -0.0169 180 PRO B CG  
3548 C CD  . PRO B 180 ? 0.4581 0.2397 0.2309 -0.0224 -0.0757 -0.0184 180 PRO B CD  
3549 N N   . ARG B 181 ? 0.4760 0.2190 0.2430 -0.0377 -0.0868 -0.0147 181 ARG B N   
3550 C CA  . ARG B 181 ? 0.5008 0.2238 0.2612 -0.0422 -0.0924 -0.0140 181 ARG B CA  
3551 C C   . ARG B 181 ? 0.4723 0.1994 0.2431 -0.0557 -0.0962 -0.0070 181 ARG B C   
3552 O O   . ARG B 181 ? 0.5055 0.2226 0.2764 -0.0609 -0.0989 -0.0033 181 ARG B O   
3553 C CB  . ARG B 181 ? 0.5427 0.2419 0.2841 -0.0391 -0.0999 -0.0214 181 ARG B CB  
3554 C CG  . ARG B 181 ? 0.5544 0.2486 0.2843 -0.0248 -0.0961 -0.0283 181 ARG B CG  
3555 C CD  . ARG B 181 ? 0.5862 0.2591 0.2969 -0.0213 -0.1036 -0.0364 181 ARG B CD  
3556 N NE  . ARG B 181 ? 0.6283 0.3069 0.3385 -0.0273 -0.1076 -0.0373 181 ARG B NE  
3557 C CZ  . ARG B 181 ? 0.6804 0.3412 0.3748 -0.0276 -0.1159 -0.0436 181 ARG B CZ  
3558 N NH1 . ARG B 181 ? 0.7592 0.4022 0.4431 -0.0206 -0.1182 -0.0476 181 ARG B NH1 
3559 N NH2 . ARG B 181 ? 0.6840 0.3518 0.3793 -0.0334 -0.1195 -0.0435 181 ARG B NH2 
3560 N N   . GLY B 182 ? 0.5006 0.2426 0.2803 -0.0615 -0.0969 -0.0046 182 GLY B N   
3561 C CA  . GLY B 182 ? 0.4625 0.2112 0.2535 -0.0740 -0.1002 0.0026  182 GLY B CA  
3562 C C   . GLY B 182 ? 0.4523 0.2179 0.2583 -0.0756 -0.0931 0.0094  182 GLY B C   
3563 O O   . GLY B 182 ? 0.4685 0.2405 0.2838 -0.0856 -0.0951 0.0161  182 GLY B O   
3564 N N   . LEU B 183 ? 0.4408 0.2136 0.2486 -0.0661 -0.0852 0.0079  183 LEU B N   
3565 C CA  . LEU B 183 ? 0.4016 0.1886 0.2213 -0.0661 -0.0784 0.0133  183 LEU B CA  
3566 C C   . LEU B 183 ? 0.4433 0.2173 0.2566 -0.0635 -0.0775 0.0139  183 LEU B C   
3567 O O   . LEU B 183 ? 0.4314 0.2159 0.2523 -0.0623 -0.0718 0.0176  183 LEU B O   
3568 C CB  . LEU B 183 ? 0.3954 0.2003 0.2227 -0.0579 -0.0708 0.0119  183 LEU B CB  
3569 C CG  . LEU B 183 ? 0.3940 0.2138 0.2296 -0.0605 -0.0713 0.0123  183 LEU B CG  
3570 C CD1 . LEU B 183 ? 0.3946 0.2295 0.2369 -0.0523 -0.0647 0.0111  183 LEU B CD1 
3571 C CD2 . LEU B 183 ? 0.4123 0.2444 0.2606 -0.0703 -0.0725 0.0188  183 LEU B CD2 
3572 N N   . LEU B 184 ? 0.4601 0.2110 0.2592 -0.0627 -0.0836 0.0103  184 LEU B N   
3573 C CA  . LEU B 184 ? 0.4599 0.1960 0.2519 -0.0600 -0.0839 0.0109  184 LEU B CA  
3574 C C   . LEU B 184 ? 0.4660 0.1916 0.2579 -0.0714 -0.0904 0.0168  184 LEU B C   
3575 O O   . LEU B 184 ? 0.4999 0.2177 0.2892 -0.0794 -0.0979 0.0172  184 LEU B O   
3576 C CB  . LEU B 184 ? 0.5046 0.2204 0.2805 -0.0506 -0.0868 0.0030  184 LEU B CB  
3577 C CG  . LEU B 184 ? 0.5429 0.2679 0.3171 -0.0390 -0.0811 -0.0028 184 LEU B CG  
3578 C CD1 . LEU B 184 ? 0.5651 0.2699 0.3225 -0.0303 -0.0847 -0.0104 184 LEU B CD1 
3579 C CD2 . LEU B 184 ? 0.4992 0.2390 0.2822 -0.0333 -0.0727 -0.0001 184 LEU B CD2 
3580 N N   . PRO B 185 ? 0.4707 0.1945 0.2644 -0.0726 -0.0884 0.0217  185 PRO B N   
3581 C CA  . PRO B 185 ? 0.5090 0.2201 0.3008 -0.0832 -0.0953 0.0278  185 PRO B CA  
3582 C C   . PRO B 185 ? 0.5085 0.1892 0.2837 -0.0809 -0.1037 0.0230  185 PRO B C   
3583 O O   . PRO B 185 ? 0.5684 0.2394 0.3337 -0.0697 -0.1029 0.0150  185 PRO B O   
3584 C CB  . PRO B 185 ? 0.4942 0.2150 0.2926 -0.0830 -0.0892 0.0341  185 PRO B CB  
3585 C CG  . PRO B 185 ? 0.4833 0.2066 0.2784 -0.0691 -0.0823 0.0281  185 PRO B CG  
3586 C CD  . PRO B 185 ? 0.4462 0.1786 0.2425 -0.0637 -0.0803 0.0216  185 PRO B CD  
3587 N N   . GLU B 186 ? 0.5270 0.1925 0.2991 -0.0914 -0.1121 0.0282  186 GLU B N   
3588 C CA  . GLU B 186 ? 0.6054 0.2417 0.3620 -0.0890 -0.1209 0.0236  186 GLU B CA  
3589 C C   . GLU B 186 ? 0.6298 0.2566 0.3798 -0.0783 -0.1178 0.0213  186 GLU B C   
3590 O O   . GLU B 186 ? 0.6558 0.2680 0.3942 -0.0679 -0.1200 0.0134  186 GLU B O   
3591 C CB  . GLU B 186 ? 0.6831 0.3161 0.4430 -0.1013 -0.1291 0.0305  186 GLU B CB  
3592 C CG  . GLU B 186 ? 0.8551 0.4656 0.6028 -0.0982 -0.1379 0.0267  186 GLU B CG  
3593 C CD  . GLU B 186 ? 0.9897 0.5974 0.7409 -0.1115 -0.1471 0.0336  186 GLU B CD  
3594 O OE1 . GLU B 186 ? 1.0152 0.6403 0.7797 -0.1229 -0.1457 0.0429  186 GLU B OE1 
3595 O OE2 . GLU B 186 ? 1.0439 0.6327 0.7848 -0.1102 -0.1557 0.0301  186 GLU B OE2 
3596 N N   . SER B 187 ? 0.5569 0.1928 0.3142 -0.0802 -0.1125 0.0285  187 SER B N   
3597 C CA  . SER B 187 ? 0.5680 0.1966 0.3203 -0.0708 -0.1097 0.0275  187 SER B CA  
3598 C C   . SER B 187 ? 0.5470 0.1902 0.3020 -0.0589 -0.0999 0.0230  187 SER B C   
3599 O O   . SER B 187 ? 0.5201 0.1879 0.2870 -0.0604 -0.0928 0.0253  187 SER B O   
3600 C CB  . SER B 187 ? 0.5773 0.2128 0.3370 -0.0782 -0.1086 0.0375  187 SER B CB  
3601 O OG  . SER B 187 ? 0.6214 0.2506 0.3764 -0.0687 -0.1060 0.0362  187 SER B OG  
3602 N N   . LEU B 188 ? 0.5764 0.2071 0.3219 -0.0467 -0.0994 0.0169  188 LEU B N   
3603 C CA  . LEU B 188 ? 0.5444 0.1918 0.2941 -0.0353 -0.0901 0.0136  188 LEU B CA  
3604 C C   . LEU B 188 ? 0.5597 0.2081 0.3109 -0.0313 -0.0866 0.0178  188 LEU B C   
3605 O O   . LEU B 188 ? 0.5720 0.2280 0.3237 -0.0206 -0.0808 0.0147  188 LEU B O   
3606 C CB  . LEU B 188 ? 0.5910 0.2305 0.3310 -0.0232 -0.0903 0.0038  188 LEU B CB  
3607 C CG  . LEU B 188 ? 0.6150 0.2545 0.3520 -0.0254 -0.0933 -0.0012 188 LEU B CG  
3608 C CD1 . LEU B 188 ? 0.6530 0.2873 0.3800 -0.0117 -0.0920 -0.0104 188 LEU B CD1 
3609 C CD2 . LEU B 188 ? 0.5815 0.2472 0.3326 -0.0313 -0.0877 0.0022  188 LEU B CD2 
3610 N N   . ASP B 189 ? 0.5253 0.1674 0.2776 -0.0403 -0.0901 0.0256  189 ASP B N   
3611 C CA  . ASP B 189 ? 0.5145 0.1620 0.2700 -0.0386 -0.0861 0.0312  189 ASP B CA  
3612 C C   . ASP B 189 ? 0.4743 0.1497 0.2411 -0.0358 -0.0763 0.0320  189 ASP B C   
3613 O O   . ASP B 189 ? 0.4701 0.1624 0.2455 -0.0412 -0.0733 0.0330  189 ASP B O   
3614 C CB  . ASP B 189 ? 0.5145 0.1586 0.2725 -0.0513 -0.0904 0.0406  189 ASP B CB  
3615 C CG  . ASP B 189 ? 0.5910 0.2167 0.3427 -0.0523 -0.0989 0.0395  189 ASP B CG  
3616 O OD1 . ASP B 189 ? 0.6529 0.2646 0.3959 -0.0430 -0.1020 0.0315  189 ASP B OD1 
3617 O OD2 . ASP B 189 ? 0.6281 0.2539 0.3834 -0.0624 -0.1026 0.0467  189 ASP B OD2 
3618 N N   . TYR B 190 ? 0.4405 0.1500 0.2239 -0.0500 -0.0641 0.0154  190 TYR B N   
3619 C CA  . TYR B 190 ? 0.4041 0.1417 0.2019 -0.0453 -0.0564 0.0153  190 TYR B CA  
3620 C C   . TYR B 190 ? 0.4343 0.1760 0.2355 -0.0396 -0.0544 0.0189  190 TYR B C   
3621 O O   . TYR B 190 ? 0.4583 0.1811 0.2509 -0.0361 -0.0585 0.0204  190 TYR B O   
3622 C CB  . TYR B 190 ? 0.4061 0.1515 0.2079 -0.0347 -0.0524 0.0076  190 TYR B CB  
3623 C CG  . TYR B 190 ? 0.4237 0.1544 0.2192 -0.0214 -0.0531 0.0027  190 TYR B CG  
3624 C CD1 . TYR B 190 ? 0.4515 0.1913 0.2539 -0.0120 -0.0495 0.0034  190 TYR B CD1 
3625 C CD2 . TYR B 190 ? 0.4452 0.1527 0.2274 -0.0179 -0.0576 -0.0026 190 TYR B CD2 
3626 C CE1 . TYR B 190 ? 0.4707 0.1987 0.2685 0.0009  -0.0501 -0.0006 190 TYR B CE1 
3627 C CE2 . TYR B 190 ? 0.4710 0.1656 0.2477 -0.0041 -0.0577 -0.0073 190 TYR B CE2 
3628 C CZ  . TYR B 190 ? 0.4582 0.1644 0.2435 0.0053  -0.0538 -0.0060 190 TYR B CZ  
3629 O OH  . TYR B 190 ? 0.5073 0.2022 0.2881 0.0192  -0.0541 -0.0101 190 TYR B OH  
3630 N N   . TRP B 191 ? 0.4074 0.1738 0.2209 -0.0387 -0.0485 0.0202  191 TRP B N   
3631 C CA  . TRP B 191 ? 0.3919 0.1672 0.2106 -0.0317 -0.0458 0.0218  191 TRP B CA  
3632 C C   . TRP B 191 ? 0.3943 0.1822 0.2217 -0.0208 -0.0411 0.0159  191 TRP B C   
3633 O O   . TRP B 191 ? 0.3773 0.1761 0.2103 -0.0213 -0.0381 0.0125  191 TRP B O   
3634 C CB  . TRP B 191 ? 0.3975 0.1906 0.2227 -0.0391 -0.0428 0.0276  191 TRP B CB  
3635 C CG  . TRP B 191 ? 0.4022 0.1870 0.2204 -0.0504 -0.0465 0.0345  191 TRP B CG  
3636 C CD1 . TRP B 191 ? 0.4357 0.2053 0.2450 -0.0515 -0.0506 0.0396  191 TRP B CD1 
3637 C CD2 . TRP B 191 ? 0.4080 0.2007 0.2280 -0.0627 -0.0463 0.0382  191 TRP B CD2 
3638 N NE1 . TRP B 191 ? 0.4779 0.2446 0.2828 -0.0643 -0.0529 0.0464  191 TRP B NE1 
3639 C CE2 . TRP B 191 ? 0.4490 0.2313 0.2611 -0.0714 -0.0501 0.0459  191 TRP B CE2 
3640 C CE3 . TRP B 191 ? 0.4337 0.2427 0.2620 -0.0672 -0.0433 0.0365  191 TRP B CE3 
3641 C CZ2 . TRP B 191 ? 0.4447 0.2323 0.2570 -0.0852 -0.0510 0.0519  191 TRP B CZ2 
3642 C CZ3 . TRP B 191 ? 0.4376 0.2528 0.2667 -0.0801 -0.0443 0.0420  191 TRP B CZ3 
3643 C CH2 . TRP B 191 ? 0.4462 0.2513 0.2677 -0.0891 -0.0479 0.0497  191 TRP B CH2 
3644 N N   . THR B 192 ? 0.3869 0.1745 0.2160 -0.0112 -0.0406 0.0152  192 THR B N   
3645 C CA  . THR B 192 ? 0.3720 0.1728 0.2102 -0.0016 -0.0362 0.0104  192 THR B CA  
3646 C C   . THR B 192 ? 0.3497 0.1624 0.1953 0.0030  -0.0345 0.0125  192 THR B C   
3647 O O   . THR B 192 ? 0.3896 0.1943 0.2304 0.0035  -0.0378 0.0163  192 THR B O   
3648 C CB  . THR B 192 ? 0.3659 0.1532 0.1986 0.0081  -0.0374 0.0052  192 THR B CB  
3649 O OG1 . THR B 192 ? 0.3664 0.1695 0.2090 0.0163  -0.0325 0.0013  192 THR B OG1 
3650 C CG2 . THR B 192 ? 0.4035 0.1723 0.2279 0.0141  -0.0421 0.0065  192 THR B CG2 
3651 N N   . TYR B 193 ? 0.3423 0.1735 0.1991 0.0063  -0.0299 0.0101  193 TYR B N   
3652 C CA  . TYR B 193 ? 0.3316 0.1745 0.1959 0.0107  -0.0288 0.0113  193 TYR B CA  
3653 C C   . TYR B 193 ? 0.3329 0.1917 0.2086 0.0158  -0.0244 0.0075  193 TYR B C   
3654 O O   . TYR B 193 ? 0.3244 0.1877 0.2025 0.0139  -0.0217 0.0051  193 TYR B O   
3655 C CB  . TYR B 193 ? 0.3204 0.1718 0.1856 0.0030  -0.0284 0.0154  193 TYR B CB  
3656 C CG  . TYR B 193 ? 0.3045 0.1715 0.1773 -0.0020 -0.0242 0.0142  193 TYR B CG  
3657 C CD1 . TYR B 193 ? 0.3156 0.1807 0.1855 -0.0093 -0.0238 0.0148  193 TYR B CD1 
3658 C CD2 . TYR B 193 ? 0.2986 0.1815 0.1812 0.0005  -0.0211 0.0127  193 TYR B CD2 
3659 C CE1 . TYR B 193 ? 0.3054 0.1852 0.1827 -0.0131 -0.0201 0.0139  193 TYR B CE1 
3660 C CE2 . TYR B 193 ? 0.2772 0.1731 0.1666 -0.0032 -0.0175 0.0114  193 TYR B CE2 
3661 C CZ  . TYR B 193 ? 0.2778 0.1723 0.1646 -0.0096 -0.0169 0.0122  193 TYR B CZ  
3662 O OH  . TYR B 193 ? 0.2846 0.1925 0.1788 -0.0123 -0.0135 0.0111  193 TYR B OH  
3663 N N   . PRO B 194 ? 0.2950 0.1622 0.1778 0.0220  -0.0240 0.0073  194 PRO B N   
3664 C CA  . PRO B 194 ? 0.3052 0.1881 0.1996 0.0258  -0.0201 0.0047  194 PRO B CA  
3665 C C   . PRO B 194 ? 0.2781 0.1745 0.1793 0.0199  -0.0179 0.0054  194 PRO B C   
3666 O O   . PRO B 194 ? 0.2743 0.1733 0.1751 0.0172  -0.0194 0.0076  194 PRO B O   
3667 C CB  . PRO B 194 ? 0.2885 0.1748 0.1878 0.0337  -0.0216 0.0051  194 PRO B CB  
3668 C CG  . PRO B 194 ? 0.3379 0.2144 0.2293 0.0319  -0.0262 0.0087  194 PRO B CG  
3669 C CD  . PRO B 194 ? 0.3135 0.1751 0.1935 0.0261  -0.0278 0.0099  194 PRO B CD  
3670 N N   . GLY B 195 ? 0.2601 0.1647 0.1669 0.0182  -0.0145 0.0035  195 GLY B N   
3671 C CA  . GLY B 195 ? 0.2466 0.1630 0.1598 0.0135  -0.0124 0.0037  195 GLY B CA  
3672 C C   . GLY B 195 ? 0.2355 0.1625 0.1580 0.0150  -0.0091 0.0019  195 GLY B C   
3673 O O   . GLY B 195 ? 0.2481 0.1784 0.1755 0.0204  -0.0083 0.0010  195 GLY B O   
3674 N N   . SER B 196 ? 0.2348 0.1678 0.1600 0.0104  -0.0072 0.0018  196 SER B N   
3675 C CA  . SER B 196 ? 0.2286 0.1719 0.1632 0.0112  -0.0046 0.0008  196 SER B CA  
3676 C C   . SER B 196 ? 0.2373 0.1822 0.1714 0.0077  -0.0028 0.0007  196 SER B C   
3677 O O   . SER B 196 ? 0.2283 0.1682 0.1558 0.0036  -0.0037 0.0014  196 SER B O   
3678 C CB  . SER B 196 ? 0.2331 0.1841 0.1738 0.0100  -0.0047 0.0006  196 SER B CB  
3679 O OG  . SER B 196 ? 0.2364 0.1885 0.1742 0.0054  -0.0042 0.0009  196 SER B OG  
3680 N N   . LEU B 197 ? 0.2174 0.1700 0.1589 0.0088  -0.0007 0.0003  197 LEU B N   
3681 C CA  . LEU B 197 ? 0.2083 0.1648 0.1512 0.0053  0.0006  0.0007  197 LEU B CA  
3682 C C   . LEU B 197 ? 0.2263 0.1860 0.1698 0.0018  0.0003  0.0011  197 LEU B C   
3683 O O   . LEU B 197 ? 0.2107 0.1727 0.1568 0.0027  -0.0001 0.0005  197 LEU B O   
3684 C CB  . LEU B 197 ? 0.2058 0.1700 0.1572 0.0071  0.0025  0.0010  197 LEU B CB  
3685 C CG  . LEU B 197 ? 0.2025 0.1668 0.1543 0.0107  0.0038  0.0011  197 LEU B CG  
3686 C CD1 . LEU B 197 ? 0.2234 0.1960 0.1843 0.0111  0.0055  0.0025  197 LEU B CD1 
3687 C CD2 . LEU B 197 ? 0.2300 0.1887 0.1734 0.0104  0.0038  0.0006  197 LEU B CD2 
3688 N N   . THR B 198 ? 0.2165 0.1777 0.1581 -0.0021 0.0006  0.0019  198 THR B N   
3689 C CA  . THR B 198 ? 0.2069 0.1737 0.1499 -0.0048 0.0012  0.0023  198 THR B CA  
3690 C C   . THR B 198 ? 0.2107 0.1864 0.1620 -0.0036 0.0030  0.0018  198 THR B C   
3691 O O   . THR B 198 ? 0.1847 0.1662 0.1375 -0.0048 0.0040  0.0017  198 THR B O   
3692 C CB  . THR B 198 ? 0.2062 0.1720 0.1437 -0.0101 0.0005  0.0043  198 THR B CB  
3693 O OG1 . THR B 198 ? 0.2169 0.1853 0.1561 -0.0117 0.0005  0.0048  198 THR B OG1 
3694 C CG2 . THR B 198 ? 0.2318 0.1862 0.1599 -0.0118 -0.0020 0.0052  198 THR B CG2 
3695 N N   . THR B 199 ? 0.2047 0.1813 0.1608 -0.0010 0.0034  0.0015  199 THR B N   
3696 C CA  . THR B 199 ? 0.1782 0.1609 0.1421 0.0007  0.0045  0.0012  199 THR B CA  
3697 C C   . THR B 199 ? 0.1863 0.1675 0.1546 0.0036  0.0042  0.0005  199 THR B C   
3698 O O   . THR B 199 ? 0.2094 0.1872 0.1758 0.0046  0.0037  0.0007  199 THR B O   
3699 C CB  . THR B 199 ? 0.1911 0.1771 0.1574 0.0001  0.0049  0.0029  199 THR B CB  
3700 O OG1 . THR B 199 ? 0.2208 0.2035 0.1857 0.0013  0.0048  0.0037  199 THR B OG1 
3701 C CG2 . THR B 199 ? 0.2148 0.2030 0.1773 -0.0036 0.0045  0.0041  199 THR B CG2 
3702 N N   . PRO B 200 ? 0.1970 0.1809 0.1715 0.0050  0.0043  -0.0003 200 PRO B N   
3703 C CA  . PRO B 200 ? 0.1689 0.1521 0.1491 0.0065  0.0036  0.0000  200 PRO B CA  
3704 C C   . PRO B 200 ? 0.1845 0.1683 0.1652 0.0067  0.0046  0.0026  200 PRO B C   
3705 O O   . PRO B 200 ? 0.1944 0.1795 0.1733 0.0060  0.0054  0.0040  200 PRO B O   
3706 C CB  . PRO B 200 ? 0.1930 0.1777 0.1792 0.0074  0.0034  -0.0006 200 PRO B CB  
3707 C CG  . PRO B 200 ? 0.1947 0.1808 0.1773 0.0075  0.0039  -0.0031 200 PRO B CG  
3708 C CD  . PRO B 200 ? 0.1807 0.1686 0.1579 0.0054  0.0049  -0.0013 200 PRO B CD  
3709 N N   . PRO B 201 ? 0.1897 0.1734 0.1726 0.0078  0.0044  0.0033  201 PRO B N   
3710 C CA  . PRO B 201 ? 0.1905 0.1741 0.1770 0.0083  0.0027  0.0021  201 PRO B CA  
3711 C C   . PRO B 201 ? 0.1787 0.1594 0.1595 0.0089  0.0014  0.0004  201 PRO B C   
3712 O O   . PRO B 201 ? 0.1936 0.1748 0.1772 0.0094  -0.0005 -0.0002 201 PRO B O   
3713 C CB  . PRO B 201 ? 0.1797 0.1671 0.1722 0.0090  0.0033  0.0048  201 PRO B CB  
3714 C CG  . PRO B 201 ? 0.1824 0.1701 0.1699 0.0103  0.0057  0.0062  201 PRO B CG  
3715 C CD  . PRO B 201 ? 0.1963 0.1820 0.1795 0.0088  0.0060  0.0057  201 PRO B CD  
3716 N N   . LEU B 202 ? 0.1875 0.1649 0.1605 0.0083  0.0018  0.0000  202 LEU B N   
3717 C CA  . LEU B 202 ? 0.1782 0.1516 0.1446 0.0083  0.0003  -0.0010 202 LEU B CA  
3718 C C   . LEU B 202 ? 0.1897 0.1617 0.1562 0.0110  -0.0009 -0.0004 202 LEU B C   
3719 O O   . LEU B 202 ? 0.2089 0.1786 0.1724 0.0116  -0.0031 -0.0009 202 LEU B O   
3720 C CB  . LEU B 202 ? 0.1850 0.1591 0.1513 0.0073  -0.0010 -0.0028 202 LEU B CB  
3721 C CG  . LEU B 202 ? 0.1877 0.1643 0.1539 0.0058  0.0005  -0.0036 202 LEU B CG  
3722 C CD1 . LEU B 202 ? 0.2060 0.1836 0.1723 0.0061  -0.0004 -0.0063 202 LEU B CD1 
3723 C CD2 . LEU B 202 ? 0.2028 0.1783 0.1622 0.0035  0.0015  -0.0025 202 LEU B CD2 
3724 N N   . LEU B 203 ? 0.2020 0.1763 0.1718 0.0131  0.0006  0.0008  203 LEU B N   
3725 C CA  . LEU B 203 ? 0.1989 0.1741 0.1702 0.0167  0.0000  0.0013  203 LEU B CA  
3726 C C   . LEU B 203 ? 0.2043 0.1715 0.1662 0.0185  -0.0012 0.0007  203 LEU B C   
3727 O O   . LEU B 203 ? 0.2018 0.1628 0.1561 0.0172  -0.0007 0.0004  203 LEU B O   
3728 C CB  . LEU B 203 ? 0.1897 0.1700 0.1653 0.0189  0.0028  0.0028  203 LEU B CB  
3729 C CG  . LEU B 203 ? 0.1925 0.1802 0.1780 0.0167  0.0035  0.0045  203 LEU B CG  
3730 C CD1 . LEU B 203 ? 0.2308 0.2238 0.2190 0.0181  0.0068  0.0068  203 LEU B CD1 
3731 C CD2 . LEU B 203 ? 0.2364 0.2284 0.2296 0.0164  0.0008  0.0048  203 LEU B CD2 
3732 N N   . GLU B 204 ? 0.2075 0.1748 0.1704 0.0217  -0.0032 0.0010  204 GLU B N   
3733 C CA  . GLU B 204 ? 0.2064 0.1647 0.1605 0.0237  -0.0053 0.0009  204 GLU B CA  
3734 C C   . GLU B 204 ? 0.2343 0.1896 0.1859 0.0291  -0.0039 0.0006  204 GLU B C   
3735 O O   . GLU B 204 ? 0.2605 0.2156 0.2129 0.0344  -0.0052 0.0009  204 GLU B O   
3736 C CB  . GLU B 204 ? 0.2269 0.1863 0.1824 0.0245  -0.0087 0.0014  204 GLU B CB  
3737 C CG  . GLU B 204 ? 0.2175 0.1780 0.1722 0.0193  -0.0097 0.0008  204 GLU B CG  
3738 C CD  . GLU B 204 ? 0.2339 0.1955 0.1884 0.0194  -0.0135 0.0009  204 GLU B CD  
3739 O OE1 . GLU B 204 ? 0.2637 0.2292 0.2235 0.0229  -0.0155 0.0017  204 GLU B OE1 
3740 O OE2 . GLU B 204 ? 0.2482 0.2078 0.1974 0.0161  -0.0143 0.0003  204 GLU B OE2 
3741 N N   . SER B 205 ? 0.2268 0.1797 0.1747 0.0281  -0.0015 -0.0002 205 SER B N   
3742 C CA  A SER B 205 ? 0.2228 0.1736 0.1675 0.0333  0.0005  -0.0012 205 SER B CA  
3743 C CA  B SER B 205 ? 0.2234 0.1743 0.1681 0.0332  0.0005  -0.0012 205 SER B CA  
3744 C C   . SER B 205 ? 0.2355 0.1728 0.1675 0.0324  -0.0005 -0.0028 205 SER B C   
3745 O O   . SER B 205 ? 0.2678 0.2019 0.1950 0.0360  0.0012  -0.0045 205 SER B O   
3746 C CB  A SER B 205 ? 0.2336 0.1947 0.1851 0.0334  0.0042  -0.0005 205 SER B CB  
3747 C CB  B SER B 205 ? 0.2294 0.1906 0.1809 0.0329  0.0042  -0.0005 205 SER B CB  
3748 O OG  A SER B 205 ? 0.2386 0.2002 0.1900 0.0275  0.0045  -0.0001 205 SER B OG  
3749 O OG  B SER B 205 ? 0.2229 0.1947 0.1859 0.0316  0.0042  0.0014  205 SER B OG  
3750 N N   . VAL B 206 ? 0.2508 0.1800 0.1767 0.0275  -0.0033 -0.0024 206 VAL B N   
3751 C CA  . VAL B 206 ? 0.2590 0.1762 0.1738 0.0244  -0.0047 -0.0034 206 VAL B CA  
3752 C C   . VAL B 206 ? 0.2913 0.1944 0.1971 0.0257  -0.0084 -0.0032 206 VAL B C   
3753 O O   . VAL B 206 ? 0.2935 0.1960 0.1999 0.0238  -0.0105 -0.0012 206 VAL B O   
3754 C CB  . VAL B 206 ? 0.2496 0.1695 0.1647 0.0164  -0.0048 -0.0022 206 VAL B CB  
3755 C CG1 . VAL B 206 ? 0.2760 0.1839 0.1801 0.0121  -0.0071 -0.0027 206 VAL B CG1 
3756 C CG2 . VAL B 206 ? 0.2338 0.1662 0.1575 0.0152  -0.0017 -0.0019 206 VAL B CG2 
3757 N N   . THR B 207 ? 0.2907 0.1812 0.1868 0.0286  -0.0095 -0.0054 207 THR B N   
3758 C CA  . THR B 207 ? 0.3154 0.1886 0.2005 0.0276  -0.0139 -0.0050 207 THR B CA  
3759 C C   . THR B 207 ? 0.3127 0.1800 0.1915 0.0184  -0.0155 -0.0042 207 THR B C   
3760 O O   . THR B 207 ? 0.3099 0.1757 0.1852 0.0171  -0.0148 -0.0065 207 THR B O   
3761 C CB  . THR B 207 ? 0.3205 0.1814 0.1977 0.0359  -0.0147 -0.0082 207 THR B CB  
3762 O OG1 . THR B 207 ? 0.3397 0.2088 0.2244 0.0446  -0.0130 -0.0083 207 THR B OG1 
3763 C CG2 . THR B 207 ? 0.3486 0.1890 0.2137 0.0345  -0.0200 -0.0075 207 THR B CG2 
3764 N N   . TRP B 208 ? 0.3026 0.1692 0.1808 0.0117  -0.0175 -0.0008 208 TRP B N   
3765 C CA  . TRP B 208 ? 0.3043 0.1679 0.1782 0.0022  -0.0191 0.0009  208 TRP B CA  
3766 C C   . TRP B 208 ? 0.3366 0.1798 0.1975 -0.0003 -0.0239 0.0011  208 TRP B C   
3767 O O   . TRP B 208 ? 0.3427 0.1749 0.1984 0.0023  -0.0266 0.0026  208 TRP B O   
3768 C CB  . TRP B 208 ? 0.2919 0.1651 0.1706 -0.0037 -0.0185 0.0048  208 TRP B CB  
3769 C CG  . TRP B 208 ? 0.2757 0.1670 0.1657 -0.0037 -0.0144 0.0041  208 TRP B CG  
3770 C CD1 . TRP B 208 ? 0.2707 0.1729 0.1695 0.0010  -0.0120 0.0035  208 TRP B CD1 
3771 C CD2 . TRP B 208 ? 0.2747 0.1741 0.1682 -0.0085 -0.0128 0.0040  208 TRP B CD2 
3772 N NE1 . TRP B 208 ? 0.2696 0.1846 0.1766 -0.0004 -0.0090 0.0028  208 TRP B NE1 
3773 C CE2 . TRP B 208 ? 0.2659 0.1795 0.1697 -0.0057 -0.0094 0.0032  208 TRP B CE2 
3774 C CE3 . TRP B 208 ? 0.2876 0.1831 0.1763 -0.0149 -0.0146 0.0046  208 TRP B CE3 
3775 C CZ2 . TRP B 208 ? 0.2492 0.1732 0.1589 -0.0084 -0.0074 0.0032  208 TRP B CZ2 
3776 C CZ3 . TRP B 208 ? 0.2793 0.1870 0.1745 -0.0178 -0.0126 0.0045  208 TRP B CZ3 
3777 C CH2 . TRP B 208 ? 0.2680 0.1894 0.1734 -0.0141 -0.0089 0.0039  208 TRP B CH2 
3778 N N   . ILE B 209 ? 0.3282 0.1660 0.1837 -0.0058 -0.0254 0.0000  209 ILE B N   
3779 C CA  . ILE B 209 ? 0.3384 0.1563 0.1815 -0.0104 -0.0307 0.0003  209 ILE B CA  
3780 C C   . ILE B 209 ? 0.3551 0.1791 0.1996 -0.0223 -0.0317 0.0037  209 ILE B C   
3781 O O   . ILE B 209 ? 0.3610 0.1925 0.2080 -0.0249 -0.0307 0.0020  209 ILE B O   
3782 C CB  . ILE B 209 ? 0.3679 0.1731 0.2023 -0.0049 -0.0320 -0.0053 209 ILE B CB  
3783 C CG1 . ILE B 209 ? 0.3977 0.2007 0.2326 0.0079  -0.0300 -0.0084 209 ILE B CG1 
3784 C CG2 . ILE B 209 ? 0.3885 0.1709 0.2089 -0.0108 -0.0384 -0.0055 209 ILE B CG2 
3785 C CD1 . ILE B 209 ? 0.4171 0.2128 0.2451 0.0156  -0.0293 -0.0145 209 ILE B CD1 
3786 N N   . VAL B 210 ? 0.3466 0.1691 0.1900 -0.0293 -0.0336 0.0089  210 VAL B N   
3787 C CA  . VAL B 210 ? 0.3437 0.1759 0.1905 -0.0405 -0.0338 0.0130  210 VAL B CA  
3788 C C   . VAL B 210 ? 0.3886 0.2026 0.2244 -0.0493 -0.0399 0.0155  210 VAL B C   
3789 O O   . VAL B 210 ? 0.3820 0.1814 0.2103 -0.0502 -0.0432 0.0184  210 VAL B O   
3790 C CB  . VAL B 210 ? 0.3447 0.1919 0.1990 -0.0426 -0.0306 0.0175  210 VAL B CB  
3791 C CG1 . VAL B 210 ? 0.3310 0.1901 0.1894 -0.0536 -0.0302 0.0219  210 VAL B CG1 
3792 C CG2 . VAL B 210 ? 0.3314 0.1949 0.1962 -0.0343 -0.0253 0.0146  210 VAL B CG2 
3793 N N   . LEU B 211 ? 0.3789 0.1922 0.2130 -0.0557 -0.0423 0.0144  211 LEU B N   
3794 C CA  . LEU B 211 ? 0.3941 0.1883 0.2172 -0.0647 -0.0491 0.0163  211 LEU B CA  
3795 C C   . LEU B 211 ? 0.4065 0.2065 0.2321 -0.0763 -0.0501 0.0243  211 LEU B C   
3796 O O   . LEU B 211 ? 0.4099 0.2324 0.2464 -0.0801 -0.0459 0.0276  211 LEU B O   
3797 C CB  . LEU B 211 ? 0.3931 0.1858 0.2136 -0.0690 -0.0519 0.0129  211 LEU B CB  
3798 C CG  . LEU B 211 ? 0.4167 0.2025 0.2323 -0.0589 -0.0513 0.0050  211 LEU B CG  
3799 C CD1 . LEU B 211 ? 0.4313 0.2135 0.2418 -0.0663 -0.0559 0.0028  211 LEU B CD1 
3800 C CD2 . LEU B 211 ? 0.4660 0.2264 0.2690 -0.0516 -0.0545 0.0019  211 LEU B CD2 
3801 N N   . LYS B 212 ? 0.4251 0.2044 0.2399 -0.0818 -0.0557 0.0278  212 LYS B N   
3802 C CA  . LYS B 212 ? 0.4297 0.2139 0.2458 -0.0933 -0.0567 0.0364  212 LYS B CA  
3803 C C   . LYS B 212 ? 0.4484 0.2419 0.2683 -0.1065 -0.0589 0.0396  212 LYS B C   
3804 O O   . LYS B 212 ? 0.4579 0.2703 0.2859 -0.1144 -0.0562 0.0459  212 LYS B O   
3805 C CB  . LYS B 212 ? 0.4689 0.2268 0.2720 -0.0954 -0.0625 0.0397  212 LYS B CB  
3806 C CG  . LYS B 212 ? 0.4937 0.2532 0.2958 -0.1094 -0.0647 0.0495  212 LYS B CG  
3807 C CD  . LYS B 212 ? 0.5978 0.3332 0.3880 -0.1093 -0.0695 0.0536  212 LYS B CD  
3808 C CE  . LYS B 212 ? 0.6888 0.4286 0.4790 -0.1234 -0.0714 0.0635  212 LYS B CE  
3809 N NZ  . LYS B 212 ? 0.7410 0.4617 0.5221 -0.1212 -0.0761 0.0657  212 LYS B NZ  
3810 N N   . GLU B 213 ? 0.4277 0.2090 0.2417 -0.1092 -0.0640 0.0353  213 GLU B N   
3811 C CA  . GLU B 213 ? 0.4322 0.2213 0.2495 -0.1226 -0.0675 0.0387  213 GLU B CA  
3812 C C   . GLU B 213 ? 0.4134 0.2296 0.2440 -0.1201 -0.0623 0.0364  213 GLU B C   
3813 O O   . GLU B 213 ? 0.4105 0.2257 0.2404 -0.1108 -0.0610 0.0294  213 GLU B O   
3814 C CB  . GLU B 213 ? 0.4527 0.2157 0.2567 -0.1276 -0.0763 0.0351  213 GLU B CB  
3815 C CG  . GLU B 213 ? 0.4846 0.2551 0.2918 -0.1429 -0.0812 0.0391  213 GLU B CG  
3816 C CD  . GLU B 213 ? 0.5717 0.3171 0.3654 -0.1476 -0.0905 0.0356  213 GLU B CD  
3817 O OE1 . GLU B 213 ? 0.6001 0.3233 0.3818 -0.1378 -0.0927 0.0283  213 GLU B OE1 
3818 O OE2 . GLU B 213 ? 0.6341 0.3867 0.4310 -0.1591 -0.0946 0.0403  213 GLU B OE2 
3819 N N   . PRO B 214 ? 0.4074 0.2479 0.2499 -0.1280 -0.0595 0.0424  214 PRO B N   
3820 C CA  . PRO B 214 ? 0.3908 0.2557 0.2457 -0.1253 -0.0555 0.0403  214 PRO B CA  
3821 C C   . PRO B 214 ? 0.3996 0.2601 0.2517 -0.1321 -0.0619 0.0381  214 PRO B C   
3822 O O   . PRO B 214 ? 0.4506 0.2937 0.2934 -0.1422 -0.0694 0.0399  214 PRO B O   
3823 C CB  . PRO B 214 ? 0.3978 0.2887 0.2654 -0.1319 -0.0511 0.0478  214 PRO B CB  
3824 C CG  . PRO B 214 ? 0.5051 0.3850 0.3659 -0.1379 -0.0523 0.0539  214 PRO B CG  
3825 C CD  . PRO B 214 ? 0.4475 0.2951 0.2928 -0.1400 -0.0601 0.0516  214 PRO B CD  
3826 N N   . ILE B 215 ? 0.3857 0.2627 0.2459 -0.1268 -0.0591 0.0347  215 ILE B N   
3827 C CA  . ILE B 215 ? 0.3767 0.2589 0.2385 -0.1342 -0.0643 0.0343  215 ILE B CA  
3828 C C   . ILE B 215 ? 0.3900 0.3014 0.2676 -0.1420 -0.0620 0.0412  215 ILE B C   
3829 O O   . ILE B 215 ? 0.3895 0.3200 0.2779 -0.1373 -0.0546 0.0439  215 ILE B O   
3830 C CB  . ILE B 215 ? 0.3877 0.2691 0.2473 -0.1243 -0.0637 0.0268  215 ILE B CB  
3831 C CG1 . ILE B 215 ? 0.3593 0.2629 0.2319 -0.1138 -0.0552 0.0262  215 ILE B CG1 
3832 C CG2 . ILE B 215 ? 0.4139 0.2667 0.2572 -0.1171 -0.0661 0.0201  215 ILE B CG2 
3833 C CD1 . ILE B 215 ? 0.3769 0.2818 0.2483 -0.1048 -0.0543 0.0202  215 ILE B CD1 
3834 N N   . SER B 216 ? 0.4118 0.3265 0.2905 -0.1541 -0.0685 0.0442  216 SER B N   
3835 C CA  A SER B 216 ? 0.4086 0.3517 0.3027 -0.1628 -0.0673 0.0514  216 SER B CA  
3836 C CA  B SER B 216 ? 0.4079 0.3512 0.3022 -0.1626 -0.0671 0.0514  216 SER B CA  
3837 C C   . SER B 216 ? 0.4359 0.3978 0.3395 -0.1586 -0.0668 0.0490  216 SER B C   
3838 O O   . SER B 216 ? 0.4952 0.4460 0.3912 -0.1602 -0.0732 0.0448  216 SER B O   
3839 C CB  A SER B 216 ? 0.4443 0.3815 0.3353 -0.1800 -0.0755 0.0572  216 SER B CB  
3840 C CB  B SER B 216 ? 0.4462 0.3846 0.3379 -0.1800 -0.0749 0.0577  216 SER B CB  
3841 O OG  A SER B 216 ? 0.4307 0.3972 0.3374 -0.1879 -0.0754 0.0631  216 SER B OG  
3842 O OG  B SER B 216 ? 0.4434 0.3716 0.3303 -0.1849 -0.0741 0.0627  216 SER B OG  
3843 N N   . VAL B 217 ? 0.3727 0.3622 0.2918 -0.1535 -0.0597 0.0517  217 VAL B N   
3844 C CA  . VAL B 217 ? 0.3833 0.3942 0.3140 -0.1501 -0.0591 0.0511  217 VAL B CA  
3845 C C   . VAL B 217 ? 0.3586 0.4001 0.3064 -0.1569 -0.0569 0.0589  217 VAL B C   
3846 O O   . VAL B 217 ? 0.3839 0.4331 0.3358 -0.1606 -0.0530 0.0639  217 VAL B O   
3847 C CB  . VAL B 217 ? 0.3923 0.4066 0.3257 -0.1342 -0.0521 0.0460  217 VAL B CB  
3848 C CG1 . VAL B 217 ? 0.4481 0.4350 0.3656 -0.1276 -0.0540 0.0389  217 VAL B CG1 
3849 C CG2 . VAL B 217 ? 0.3613 0.3876 0.3025 -0.1286 -0.0435 0.0483  217 VAL B CG2 
3850 N N   . SER B 218 ? 0.3617 0.4223 0.3199 -0.1579 -0.0593 0.0600  218 SER B N   
3851 C CA  . SER B 218 ? 0.3424 0.4344 0.3182 -0.1633 -0.0568 0.0674  218 SER B CA  
3852 C C   . SER B 218 ? 0.3092 0.4216 0.2972 -0.1500 -0.0469 0.0669  218 SER B C   
3853 O O   . SER B 218 ? 0.2861 0.3923 0.2718 -0.1375 -0.0437 0.0612  218 SER B O   
3854 C CB  . SER B 218 ? 0.3570 0.4633 0.3403 -0.1708 -0.0641 0.0699  218 SER B CB  
3855 O OG  . SER B 218 ? 0.3285 0.4410 0.3154 -0.1598 -0.0634 0.0657  218 SER B OG  
3856 N N   . SER B 219 ? 0.3155 0.4390 0.3930 -0.1263 -0.0326 0.0621  219 SER B N   
3857 C CA  . SER B 219 ? 0.2852 0.4239 0.3717 -0.1123 -0.0230 0.0602  219 SER B CA  
3858 C C   . SER B 219 ? 0.2382 0.3885 0.3405 -0.1021 -0.0362 0.0574  219 SER B C   
3859 O O   . SER B 219 ? 0.2642 0.4088 0.3566 -0.0886 -0.0347 0.0545  219 SER B O   
3860 C CB  . SER B 219 ? 0.3317 0.4957 0.4447 -0.1164 -0.0053 0.0626  219 SER B CB  
3861 O OG  . SER B 219 ? 0.4210 0.5687 0.5093 -0.1240 0.0090  0.0659  219 SER B OG  
3862 N N   . GLU B 220 ? 0.2712 0.4343 0.3950 -0.1095 -0.0511 0.0589  220 GLU B N   
3863 C CA  . GLU B 220 ? 0.2715 0.4410 0.4050 -0.1008 -0.0673 0.0583  220 GLU B CA  
3864 C C   . GLU B 220 ? 0.2790 0.4172 0.3730 -0.0949 -0.0747 0.0552  220 GLU B C   
3865 O O   . GLU B 220 ? 0.2755 0.4120 0.3670 -0.0827 -0.0783 0.0546  220 GLU B O   
3866 C CB  . GLU B 220 ? 0.3443 0.5290 0.5025 -0.1122 -0.0867 0.0610  220 GLU B CB  
3867 C CG  . GLU B 220 ? 0.5182 0.7414 0.7291 -0.1174 -0.0814 0.0643  220 GLU B CG  
3868 C CD  . GLU B 220 ? 0.6635 0.8877 0.8783 -0.1358 -0.0722 0.0657  220 GLU B CD  
3869 O OE1 . GLU B 220 ? 0.7343 0.9273 0.9098 -0.1428 -0.0706 0.0643  220 GLU B OE1 
3870 O OE2 . GLU B 220 ? 0.7005 0.9561 0.9594 -0.1430 -0.0649 0.0685  220 GLU B OE2 
3871 N N   . GLN B 221 ? 0.2753 0.3877 0.3398 -0.1033 -0.0753 0.0531  221 GLN B N   
3872 C CA  . GLN B 221 ? 0.2773 0.3615 0.3086 -0.0979 -0.0784 0.0493  221 GLN B CA  
3873 C C   . GLN B 221 ? 0.2744 0.3539 0.2978 -0.0847 -0.0663 0.0478  221 GLN B C   
3874 O O   . GLN B 221 ? 0.2695 0.3408 0.2830 -0.0758 -0.0691 0.0463  221 GLN B O   
3875 C CB  . GLN B 221 ? 0.2962 0.3546 0.3039 -0.1080 -0.0785 0.0463  221 GLN B CB  
3876 C CG  . GLN B 221 ? 0.3078 0.3594 0.3105 -0.1211 -0.0932 0.0450  221 GLN B CG  
3877 C CD  . GLN B 221 ? 0.3418 0.3648 0.3219 -0.1307 -0.0906 0.0405  221 GLN B CD  
3878 O OE1 . GLN B 221 ? 0.3250 0.3435 0.3078 -0.1326 -0.0806 0.0419  221 GLN B OE1 
3879 N NE2 . GLN B 221 ? 0.3454 0.3457 0.3007 -0.1366 -0.0994 0.0351  221 GLN B NE2 
3880 N N   . VAL B 222 ? 0.2553 0.3374 0.2801 -0.0846 -0.0534 0.0485  222 VAL B N   
3881 C CA  . VAL B 222 ? 0.2488 0.3248 0.2636 -0.0737 -0.0446 0.0465  222 VAL B CA  
3882 C C   . VAL B 222 ? 0.2605 0.3524 0.2916 -0.0628 -0.0428 0.0457  222 VAL B C   
3883 O O   . VAL B 222 ? 0.2518 0.3337 0.2724 -0.0534 -0.0410 0.0428  222 VAL B O   
3884 C CB  . VAL B 222 ? 0.3042 0.3773 0.3118 -0.0770 -0.0332 0.0482  222 VAL B CB  
3885 C CG1 . VAL B 222 ? 0.2943 0.3558 0.2858 -0.0674 -0.0283 0.0451  222 VAL B CG1 
3886 C CG2 . VAL B 222 ? 0.3888 0.4454 0.3844 -0.0869 -0.0362 0.0503  222 VAL B CG2 
3887 N N   . SER B 223 ? 0.2509 0.3678 0.3114 -0.0637 -0.0429 0.0481  223 SER B N   
3888 C CA  . SER B 223 ? 0.2408 0.3720 0.3215 -0.0512 -0.0404 0.0472  223 SER B CA  
3889 C C   . SER B 223 ? 0.2415 0.3607 0.3138 -0.0441 -0.0545 0.0476  223 SER B C   
3890 O O   . SER B 223 ? 0.2375 0.3551 0.3137 -0.0320 -0.0523 0.0462  223 SER B O   
3891 C CB  . SER B 223 ? 0.2471 0.4103 0.3697 -0.0528 -0.0389 0.0499  223 SER B CB  
3892 O OG  . SER B 223 ? 0.3044 0.4746 0.4406 -0.0575 -0.0592 0.0539  223 SER B OG  
3893 N N   . LYS B 224 ? 0.2304 0.3382 0.2889 -0.0522 -0.0683 0.0495  224 LYS B N   
3894 C CA  . LYS B 224 ? 0.2459 0.3370 0.2881 -0.0475 -0.0800 0.0506  224 LYS B CA  
3895 C C   . LYS B 224 ? 0.2428 0.3111 0.2597 -0.0416 -0.0711 0.0467  224 LYS B C   
3896 O O   . LYS B 224 ? 0.2599 0.3172 0.2692 -0.0343 -0.0752 0.0478  224 LYS B O   
3897 C CB  . LYS B 224 ? 0.2585 0.3367 0.2825 -0.0594 -0.0942 0.0520  224 LYS B CB  
3898 C CG  . LYS B 224 ? 0.3119 0.4119 0.3618 -0.0675 -0.1082 0.0561  224 LYS B CG  
3899 C CD  . LYS B 224 ? 0.3727 0.4911 0.4511 -0.0578 -0.1198 0.0614  224 LYS B CD  
3900 C CE  . LYS B 224 ? 0.4621 0.6060 0.5741 -0.0663 -0.1365 0.0659  224 LYS B CE  
3901 N NZ  . LYS B 224 ? 0.5088 0.6786 0.6643 -0.0538 -0.1452 0.0713  224 LYS B NZ  
3902 N N   . PHE B 225 ? 0.2292 0.2891 0.2338 -0.0454 -0.0606 0.0430  225 PHE B N   
3903 C CA  . PHE B 225 ? 0.2621 0.3047 0.2505 -0.0401 -0.0536 0.0393  225 PHE B CA  
3904 C C   . PHE B 225 ? 0.2385 0.2865 0.2368 -0.0290 -0.0485 0.0379  225 PHE B C   
3905 O O   . PHE B 225 ? 0.2509 0.2843 0.2392 -0.0236 -0.0477 0.0361  225 PHE B O   
3906 C CB  . PHE B 225 ? 0.2595 0.2964 0.2402 -0.0446 -0.0460 0.0367  225 PHE B CB  
3907 C CG  . PHE B 225 ? 0.2638 0.2888 0.2342 -0.0537 -0.0486 0.0365  225 PHE B CG  
3908 C CD1 . PHE B 225 ? 0.3133 0.3305 0.2758 -0.0590 -0.0554 0.0367  225 PHE B CD1 
3909 C CD2 . PHE B 225 ? 0.2950 0.3142 0.2619 -0.0569 -0.0445 0.0360  225 PHE B CD2 
3910 C CE1 . PHE B 225 ? 0.3324 0.3356 0.2842 -0.0671 -0.0553 0.0345  225 PHE B CE1 
3911 C CE2 . PHE B 225 ? 0.3513 0.3575 0.3120 -0.0637 -0.0458 0.0352  225 PHE B CE2 
3912 C CZ  . PHE B 225 ? 0.3187 0.3166 0.2722 -0.0686 -0.0497 0.0335  225 PHE B CZ  
3913 N N   . ARG B 226 ? 0.2285 0.2961 0.2466 -0.0261 -0.0429 0.0380  226 ARG B N   
3914 C CA  . ARG B 226 ? 0.2224 0.2925 0.2479 -0.0156 -0.0338 0.0343  226 ARG B CA  
3915 C C   . ARG B 226 ? 0.2360 0.3080 0.2764 -0.0053 -0.0404 0.0366  226 ARG B C   
3916 O O   . ARG B 226 ? 0.2636 0.3323 0.3092 0.0048  -0.0330 0.0326  226 ARG B O   
3917 C CB  . ARG B 226 ? 0.2094 0.2979 0.2496 -0.0165 -0.0212 0.0327  226 ARG B CB  
3918 C CG  . ARG B 226 ? 0.2218 0.3056 0.2443 -0.0275 -0.0158 0.0328  226 ARG B CG  
3919 C CD  . ARG B 226 ? 0.2347 0.3299 0.2625 -0.0282 0.0010  0.0305  226 ARG B CD  
3920 N NE  . ARG B 226 ? 0.2549 0.3428 0.2635 -0.0400 0.0036  0.0333  226 ARG B NE  
3921 C CZ  . ARG B 226 ? 0.2597 0.3592 0.2787 -0.0501 0.0051  0.0384  226 ARG B CZ  
3922 N NH1 . ARG B 226 ? 0.2518 0.3758 0.3047 -0.0509 0.0045  0.0406  226 ARG B NH1 
3923 N NH2 . ARG B 226 ? 0.2819 0.3685 0.2798 -0.0599 0.0059  0.0418  226 ARG B NH2 
3924 N N   . LYS B 227 ? 0.2198 0.2928 0.2638 -0.0077 -0.0554 0.0428  227 LYS B N   
3925 C CA  . LYS B 227 ? 0.2337 0.3035 0.2877 0.0020  -0.0656 0.0472  227 LYS B CA  
3926 C C   . LYS B 227 ? 0.2394 0.2793 0.2646 0.0034  -0.0684 0.0476  227 LYS B C   
3927 O O   . LYS B 227 ? 0.2739 0.3045 0.3021 0.0118  -0.0764 0.0522  227 LYS B O   
3928 C CB  . LYS B 227 ? 0.2550 0.3373 0.3228 -0.0023 -0.0835 0.0548  227 LYS B CB  
3929 C CG  . LYS B 227 ? 0.2635 0.3791 0.3695 -0.0038 -0.0813 0.0552  227 LYS B CG  
3930 C CD  . LYS B 227 ? 0.3871 0.5123 0.5038 -0.0112 -0.1034 0.0626  227 LYS B CD  
3931 C CE  . LYS B 227 ? 0.4812 0.6050 0.6117 -0.0006 -0.1220 0.0702  227 LYS B CE  
3932 N NZ  . LYS B 227 ? 0.5284 0.6600 0.6663 -0.0093 -0.1477 0.0778  227 LYS B NZ  
3933 N N   . LEU B 228 ? 0.2459 0.2703 0.2459 -0.0049 -0.0626 0.0439  228 LEU B N   
3934 C CA  . LEU B 228 ? 0.2541 0.2528 0.2330 -0.0041 -0.0602 0.0428  228 LEU B CA  
3935 C C   . LEU B 228 ? 0.2590 0.2538 0.2449 0.0051  -0.0513 0.0375  228 LEU B C   
3936 O O   . LEU B 228 ? 0.2480 0.2575 0.2477 0.0088  -0.0434 0.0327  228 LEU B O   
3937 C CB  . LEU B 228 ? 0.2766 0.2647 0.2370 -0.0144 -0.0543 0.0390  228 LEU B CB  
3938 C CG  . LEU B 228 ? 0.2809 0.2665 0.2291 -0.0241 -0.0607 0.0419  228 LEU B CG  
3939 C CD1 . LEU B 228 ? 0.2993 0.2803 0.2402 -0.0318 -0.0525 0.0368  228 LEU B CD1 
3940 C CD2 . LEU B 228 ? 0.3439 0.3077 0.2703 -0.0261 -0.0666 0.0466  228 LEU B CD2 
3941 N N   . ASN B 229 ? 0.2587 0.2305 0.2313 0.0071  -0.0510 0.0378  229 ASN B N   
3942 C CA  . ASN B 229 ? 0.2658 0.2267 0.2407 0.0144  -0.0438 0.0321  229 ASN B CA  
3943 C C   . ASN B 229 ? 0.2847 0.2270 0.2426 0.0065  -0.0387 0.0277  229 ASN B C   
3944 O O   . ASN B 229 ? 0.2970 0.2276 0.2420 -0.0010 -0.0404 0.0314  229 ASN B O   
3945 C CB  . ASN B 229 ? 0.3067 0.2552 0.2876 0.0251  -0.0497 0.0373  229 ASN B CB  
3946 C CG  . ASN B 229 ? 0.3621 0.3316 0.3716 0.0363  -0.0531 0.0396  229 ASN B CG  
3947 O OD1 . ASN B 229 ? 0.3547 0.3481 0.3792 0.0354  -0.0482 0.0363  229 ASN B OD1 
3948 N ND2 . ASN B 229 ? 0.4411 0.4011 0.4608 0.0471  -0.0612 0.0458  229 ASN B ND2 
3949 N N   . PHE B 230 ? 0.2686 0.2076 0.2269 0.0077  -0.0322 0.0193  230 PHE B N   
3950 C CA  . PHE B 230 ? 0.2723 0.1944 0.2213 0.0007  -0.0299 0.0151  230 PHE B CA  
3951 C C   . PHE B 230 ? 0.3111 0.2096 0.2547 0.0026  -0.0301 0.0176  230 PHE B C   
3952 O O   . PHE B 230 ? 0.3243 0.2093 0.2619 -0.0057 -0.0282 0.0177  230 PHE B O   
3953 C CB  . PHE B 230 ? 0.2753 0.1960 0.2223 0.0004  -0.0265 0.0054  230 PHE B CB  
3954 C CG  . PHE B 230 ? 0.2626 0.1996 0.2085 -0.0042 -0.0265 0.0033  230 PHE B CG  
3955 C CD1 . PHE B 230 ? 0.2497 0.1922 0.1966 -0.0130 -0.0301 0.0055  230 PHE B CD1 
3956 C CD2 . PHE B 230 ? 0.2791 0.2224 0.2217 0.0002  -0.0218 -0.0016 230 PHE B CD2 
3957 C CE1 . PHE B 230 ? 0.2556 0.2084 0.2000 -0.0168 -0.0318 0.0046  230 PHE B CE1 
3958 C CE2 . PHE B 230 ? 0.2651 0.2178 0.2006 -0.0054 -0.0217 -0.0027 230 PHE B CE2 
3959 C CZ  . PHE B 230 ? 0.2654 0.2222 0.2015 -0.0137 -0.0283 0.0012  230 PHE B CZ  
3960 N N   . ASN B 231 ? 0.3063 0.1986 0.2546 0.0137  -0.0314 0.0192  231 ASN B N   
3961 C CA  . ASN B 231 ? 0.3422 0.2073 0.2847 0.0166  -0.0318 0.0215  231 ASN B CA  
3962 C C   . ASN B 231 ? 0.3615 0.2132 0.2921 0.0130  -0.0374 0.0335  231 ASN B C   
3963 O O   . ASN B 231 ? 0.3506 0.2143 0.2780 0.0106  -0.0426 0.0400  231 ASN B O   
3964 C CB  . ASN B 231 ? 0.3556 0.2172 0.3097 0.0315  -0.0314 0.0193  231 ASN B CB  
3965 C CG  . ASN B 231 ? 0.3379 0.2208 0.3081 0.0406  -0.0376 0.0266  231 ASN B CG  
3966 O OD1 . ASN B 231 ? 0.3356 0.2439 0.3161 0.0405  -0.0349 0.0234  231 ASN B OD1 
3967 N ND2 . ASN B 231 ? 0.3658 0.2373 0.3390 0.0478  -0.0470 0.0371  231 ASN B ND2 
3968 N N   . GLY B 232 ? 0.3857 0.2087 0.3059 0.0108  -0.0359 0.0363  232 GLY B N   
3969 C CA  . GLY B 232 ? 0.4433 0.2455 0.3460 0.0088  -0.0413 0.0491  232 GLY B CA  
3970 C C   . GLY B 232 ? 0.4392 0.2353 0.3481 0.0236  -0.0524 0.0571  232 GLY B C   
3971 O O   . GLY B 232 ? 0.4594 0.2619 0.3884 0.0361  -0.0521 0.0514  232 GLY B O   
3972 N N   . GLU B 233 ? 0.4793 0.2609 0.3702 0.0221  -0.0625 0.0706  233 GLU B N   
3973 C CA  . GLU B 233 ? 0.5706 0.3438 0.4688 0.0363  -0.0775 0.0811  233 GLU B CA  
3974 C C   . GLU B 233 ? 0.5340 0.2811 0.4394 0.0459  -0.0746 0.0798  233 GLU B C   
3975 O O   . GLU B 233 ? 0.5839 0.3038 0.4720 0.0370  -0.0658 0.0785  233 GLU B O   
3976 C CB  . GLU B 233 ? 0.6647 0.4176 0.5309 0.0290  -0.0902 0.0968  233 GLU B CB  
3977 C CG  . GLU B 233 ? 0.7698 0.5276 0.6457 0.0409  -0.1127 0.1091  233 GLU B CG  
3978 C CD  . GLU B 233 ? 0.8977 0.6331 0.7321 0.0302  -0.1273 0.1239  233 GLU B CD  
3979 O OE1 . GLU B 233 ? 0.8974 0.6467 0.7172 0.0189  -0.1276 0.1218  233 GLU B OE1 
3980 O OE2 . GLU B 233 ? 0.9839 0.6858 0.7980 0.0326  -0.1377 0.1369  233 GLU B OE2 
3981 N N   . GLY B 234 ? 0.5320 0.2873 0.4665 0.0641  -0.0801 0.0788  234 GLY B N   
3982 C CA  . GLY B 234 ? 0.5623 0.2900 0.5046 0.0748  -0.0763 0.0760  234 GLY B CA  
3983 C C   . GLY B 234 ? 0.5544 0.2871 0.5081 0.0754  -0.0593 0.0569  234 GLY B C   
3984 O O   . GLY B 234 ? 0.5738 0.2817 0.5332 0.0842  -0.0548 0.0518  234 GLY B O   
3985 N N   . GLU B 235 ? 0.5388 0.3002 0.4942 0.0668  -0.0509 0.0464  235 GLU B N   
3986 C CA  . GLU B 235 ? 0.5182 0.2860 0.4801 0.0667  -0.0377 0.0290  235 GLU B CA  
3987 C C   . GLU B 235 ? 0.5172 0.3182 0.5033 0.0776  -0.0338 0.0225  235 GLU B C   
3988 O O   . GLU B 235 ? 0.4834 0.3093 0.4824 0.0805  -0.0417 0.0311  235 GLU B O   
3989 C CB  . GLU B 235 ? 0.5249 0.2977 0.4699 0.0480  -0.0322 0.0228  235 GLU B CB  
3990 C CG  . GLU B 235 ? 0.5607 0.3061 0.4863 0.0350  -0.0332 0.0299  235 GLU B CG  
3991 C CD  . GLU B 235 ? 0.6011 0.3555 0.5203 0.0177  -0.0272 0.0230  235 GLU B CD  
3992 O OE1 . GLU B 235 ? 0.6588 0.3913 0.5714 0.0073  -0.0231 0.0201  235 GLU B OE1 
3993 O OE2 . GLU B 235 ? 0.4969 0.2805 0.4210 0.0147  -0.0271 0.0205  235 GLU B OE2 
3994 N N   . PRO B 236 ? 0.5163 0.3174 0.5078 0.0826  -0.0210 0.0072  236 PRO B N   
3995 C CA  . PRO B 236 ? 0.5085 0.3401 0.5227 0.0922  -0.0132 0.0010  236 PRO B CA  
3996 C C   . PRO B 236 ? 0.4389 0.3027 0.4506 0.0808  -0.0157 0.0042  236 PRO B C   
3997 O O   . PRO B 236 ? 0.4182 0.2799 0.4080 0.0657  -0.0165 0.0027  236 PRO B O   
3998 C CB  . PRO B 236 ? 0.5562 0.3736 0.5609 0.0936  0.0029  -0.0175 236 PRO B CB  
3999 C CG  . PRO B 236 ? 0.5877 0.3627 0.5783 0.0936  0.0005  -0.0191 236 PRO B CG  
4000 C CD  . PRO B 236 ? 0.5544 0.3241 0.5308 0.0799  -0.0128 -0.0053 236 PRO B CD  
4001 N N   . GLU B 237 ? 0.4709 0.3645 0.5088 0.0882  -0.0170 0.0087  237 GLU B N   
4002 C CA  . GLU B 237 ? 0.4819 0.4039 0.5191 0.0775  -0.0212 0.0134  237 GLU B CA  
4003 C C   . GLU B 237 ? 0.4297 0.3601 0.4519 0.0679  -0.0086 0.0020  237 GLU B C   
4004 O O   . GLU B 237 ? 0.4441 0.3763 0.4703 0.0735  0.0057  -0.0089 237 GLU B O   
4005 C CB  . GLU B 237 ? 0.5409 0.4934 0.6136 0.0866  -0.0258 0.0202  237 GLU B CB  
4006 C CG  . GLU B 237 ? 0.6131 0.5945 0.6864 0.0750  -0.0261 0.0217  237 GLU B CG  
4007 C CD  . GLU B 237 ? 0.7013 0.7098 0.8060 0.0787  -0.0386 0.0322  237 GLU B CD  
4008 O OE1 . GLU B 237 ? 0.7295 0.7289 0.8328 0.0799  -0.0570 0.0437  237 GLU B OE1 
4009 O OE2 . GLU B 237 ? 0.7217 0.7595 0.8512 0.0791  -0.0303 0.0290  237 GLU B OE2 
4010 N N   . GLU B 238 ? 0.3151 0.3437 0.3520 0.0431  -0.0578 -0.0065 238 GLU B N   
4011 C CA  . GLU B 238 ? 0.2903 0.3324 0.3284 0.0366  -0.0474 -0.0091 238 GLU B CA  
4012 C C   . GLU B 238 ? 0.2806 0.3271 0.3067 0.0272  -0.0411 -0.0034 238 GLU B C   
4013 O O   . GLU B 238 ? 0.2950 0.3241 0.3084 0.0209  -0.0370 0.0059  238 GLU B O   
4014 C CB  . GLU B 238 ? 0.3195 0.3462 0.3550 0.0340  -0.0422 -0.0056 238 GLU B CB  
4015 C CG  . GLU B 238 ? 0.3986 0.4171 0.4448 0.0423  -0.0480 -0.0105 238 GLU B CG  
4016 C CD  . GLU B 238 ? 0.5182 0.5177 0.5594 0.0387  -0.0430 -0.0058 238 GLU B CD  
4017 O OE1 . GLU B 238 ? 0.5421 0.5358 0.5725 0.0303  -0.0355 0.0005  238 GLU B OE1 
4018 O OE2 . GLU B 238 ? 0.5663 0.5566 0.6150 0.0441  -0.0466 -0.0093 238 GLU B OE2 
4019 N N   . PRO B 239 ? 0.2688 0.3381 0.2986 0.0252  -0.0393 -0.0094 239 PRO B N   
4020 C CA  . PRO B 239 ? 0.2626 0.3353 0.2808 0.0157  -0.0330 -0.0042 239 PRO B CA  
4021 C C   . PRO B 239 ? 0.2295 0.2915 0.2382 0.0078  -0.0241 0.0022  239 PRO B C   
4022 O O   . PRO B 239 ? 0.2418 0.3072 0.2549 0.0080  -0.0205 -0.0009 239 PRO B O   
4023 C CB  . PRO B 239 ? 0.2715 0.3721 0.2974 0.0144  -0.0315 -0.0141 239 PRO B CB  
4024 C CG  . PRO B 239 ? 0.3027 0.4141 0.3450 0.0256  -0.0408 -0.0243 239 PRO B CG  
4025 C CD  . PRO B 239 ? 0.2835 0.3767 0.3288 0.0313  -0.0434 -0.0220 239 PRO B CD  
4026 N N   . MET B 240 ? 0.2255 0.2759 0.2217 0.0011  -0.0208 0.0105  240 MET B N   
4027 C CA  . MET B 240 ? 0.2096 0.2494 0.1974 -0.0058 -0.0131 0.0161  240 MET B CA  
4028 C C   . MET B 240 ? 0.2314 0.2866 0.2169 -0.0120 -0.0072 0.0135  240 MET B C   
4029 O O   . MET B 240 ? 0.2131 0.2713 0.1913 -0.0180 -0.0047 0.0161  240 MET B O   
4030 C CB  . MET B 240 ? 0.2134 0.2357 0.1894 -0.0108 -0.0120 0.0246  240 MET B CB  
4031 C CG  . MET B 240 ? 0.2353 0.2465 0.2050 -0.0170 -0.0046 0.0287  240 MET B CG  
4032 S SD  . MET B 240 ? 0.2461 0.2396 0.2033 -0.0240 -0.0023 0.0367  240 MET B SD  
4033 C CE  . MET B 240 ? 0.2471 0.2230 0.2054 -0.0195 -0.0067 0.0384  240 MET B CE  
4034 N N   . VAL B 241 ? 0.2147 0.2793 0.2058 -0.0108 -0.0052 0.0084  241 VAL B N   
4035 C CA  . VAL B 241 ? 0.2011 0.2784 0.1883 -0.0172 0.0002  0.0062  241 VAL B CA  
4036 C C   . VAL B 241 ? 0.2020 0.2752 0.1894 -0.0168 0.0029  0.0060  241 VAL B C   
4037 O O   . VAL B 241 ? 0.2085 0.2769 0.2034 -0.0106 0.0003  0.0040  241 VAL B O   
4038 C CB  . VAL B 241 ? 0.2215 0.3225 0.2159 -0.0165 -0.0012 -0.0029 241 VAL B CB  
4039 C CG1 . VAL B 241 ? 0.2131 0.3200 0.2076 -0.0168 -0.0044 -0.0035 241 VAL B CG1 
4040 C CG2 . VAL B 241 ? 0.2046 0.3148 0.2129 -0.0082 -0.0055 -0.0111 241 VAL B CG2 
4041 N N   . ASP B 242 ? 0.2041 0.2790 0.1827 -0.0237 0.0079  0.0079  242 ASP B N   
4042 C CA  . ASP B 242 ? 0.2066 0.2787 0.1839 -0.0235 0.0098  0.0076  242 ASP B CA  
4043 C C   . ASP B 242 ? 0.1933 0.2474 0.1721 -0.0197 0.0091  0.0114  242 ASP B C   
4044 O O   . ASP B 242 ? 0.2117 0.2651 0.1970 -0.0151 0.0080  0.0082  242 ASP B O   
4045 C CB  . ASP B 242 ? 0.2185 0.3079 0.2048 -0.0199 0.0084  -0.0011 242 ASP B CB  
4046 C CG  . ASP B 242 ? 0.2289 0.3369 0.2115 -0.0263 0.0109  -0.0055 242 ASP B CG  
4047 O OD1 . ASP B 242 ? 0.2152 0.3193 0.1848 -0.0345 0.0148  -0.0006 242 ASP B OD1 
4048 O OD2 . ASP B 242 ? 0.2530 0.3789 0.2458 -0.0234 0.0090  -0.0143 242 ASP B OD2 
4049 N N   . ASN B 243 ? 0.1875 0.2279 0.1602 -0.0226 0.0102  0.0175  243 ASN B N   
4050 C CA  . ASN B 243 ? 0.1940 0.2180 0.1669 -0.0213 0.0108  0.0205  243 ASN B CA  
4051 C C   . ASN B 243 ? 0.2201 0.2370 0.1859 -0.0251 0.0140  0.0232  243 ASN B C   
4052 O O   . ASN B 243 ? 0.2233 0.2282 0.1847 -0.0281 0.0159  0.0270  243 ASN B O   
4053 C CB  . ASN B 243 ? 0.2144 0.2277 0.1851 -0.0225 0.0101  0.0245  243 ASN B CB  
4054 C CG  . ASN B 243 ? 0.2088 0.2228 0.1707 -0.0288 0.0120  0.0284  243 ASN B CG  
4055 O OD1 . ASN B 243 ? 0.2313 0.2532 0.1887 -0.0327 0.0141  0.0281  243 ASN B OD1 
4056 N ND2 . ASN B 243 ? 0.2292 0.2340 0.1879 -0.0306 0.0116  0.0321  243 ASN B ND2 
4057 N N   . TRP B 244 ? 0.2157 0.2404 0.1804 -0.0249 0.0141  0.0208  244 TRP B N   
4058 C CA  . TRP B 244 ? 0.2182 0.2360 0.1756 -0.0273 0.0154  0.0231  244 TRP B CA  
4059 C C   . TRP B 244 ? 0.2289 0.2492 0.1917 -0.0222 0.0137  0.0190  244 TRP B C   
4060 O O   . TRP B 244 ? 0.2359 0.2674 0.2060 -0.0186 0.0123  0.0141  244 TRP B O   
4061 C CB  . TRP B 244 ? 0.2358 0.2588 0.1820 -0.0337 0.0169  0.0254  244 TRP B CB  
4062 C CG  . TRP B 244 ? 0.2459 0.2866 0.1936 -0.0344 0.0167  0.0209  244 TRP B CG  
4063 C CD1 . TRP B 244 ? 0.2473 0.2997 0.1974 -0.0363 0.0172  0.0185  244 TRP B CD1 
4064 C CD2 . TRP B 244 ? 0.2806 0.3309 0.2277 -0.0336 0.0160  0.0170  244 TRP B CD2 
4065 N NE1 . TRP B 244 ? 0.2260 0.2955 0.1782 -0.0369 0.0171  0.0127  244 TRP B NE1 
4066 C CE2 . TRP B 244 ? 0.2821 0.3505 0.2321 -0.0356 0.0167  0.0118  244 TRP B CE2 
4067 C CE3 . TRP B 244 ? 0.2830 0.3295 0.2282 -0.0311 0.0145  0.0166  244 TRP B CE3 
4068 C CZ2 . TRP B 244 ? 0.3289 0.4121 0.2794 -0.0362 0.0167  0.0061  244 TRP B CZ2 
4069 C CZ3 . TRP B 244 ? 0.3158 0.3758 0.2603 -0.0314 0.0141  0.0119  244 TRP B CZ3 
4070 C CH2 . TRP B 244 ? 0.3140 0.3924 0.2607 -0.0345 0.0156  0.0068  244 TRP B CH2 
4071 N N   . ARG B 245 ? 0.2227 0.2327 0.1830 -0.0217 0.0135  0.0204  245 ARG B N   
4072 C CA  . ARG B 245 ? 0.2023 0.2144 0.1661 -0.0171 0.0115  0.0165  245 ARG B CA  
4073 C C   . ARG B 245 ? 0.2180 0.2331 0.1704 -0.0200 0.0103  0.0185  245 ARG B C   
4074 O O   . ARG B 245 ? 0.2453 0.2522 0.1869 -0.0247 0.0109  0.0236  245 ARG B O   
4075 C CB  . ARG B 245 ? 0.1960 0.1961 0.1638 -0.0146 0.0112  0.0158  245 ARG B CB  
4076 C CG  . ARG B 245 ? 0.1826 0.1866 0.1569 -0.0090 0.0088  0.0103  245 ARG B CG  
4077 C CD  . ARG B 245 ? 0.2071 0.2012 0.1856 -0.0066 0.0083  0.0081  245 ARG B CD  
4078 N NE  . ARG B 245 ? 0.1915 0.1919 0.1781 -0.0011 0.0063  0.0016  245 ARG B NE  
4079 C CZ  . ARG B 245 ? 0.1779 0.1744 0.1695 0.0024  0.0047  -0.0026 245 ARG B CZ  
4080 N NH1 . ARG B 245 ? 0.1855 0.1718 0.1750 0.0014  0.0044  -0.0015 245 ARG B NH1 
4081 N NH2 . ARG B 245 ? 0.1850 0.1892 0.1851 0.0072  0.0030  -0.0094 245 ARG B NH2 
4082 N N   . PRO B 246 ? 0.2317 0.2575 0.1854 -0.0177 0.0087  0.0144  246 PRO B N   
4083 C CA  . PRO B 246 ? 0.2503 0.2770 0.1905 -0.0211 0.0071  0.0166  246 PRO B CA  
4084 C C   . PRO B 246 ? 0.2334 0.2444 0.1672 -0.0195 0.0042  0.0201  246 PRO B C   
4085 O O   . PRO B 246 ? 0.2284 0.2327 0.1716 -0.0145 0.0033  0.0180  246 PRO B O   
4086 C CB  . PRO B 246 ? 0.2828 0.3239 0.2287 -0.0176 0.0058  0.0102  246 PRO B CB  
4087 C CG  . PRO B 246 ? 0.2430 0.2940 0.2047 -0.0141 0.0073  0.0045  246 PRO B CG  
4088 C CD  . PRO B 246 ? 0.2549 0.2920 0.2218 -0.0125 0.0081  0.0074  246 PRO B CD  
4089 N N   . THR B 247 ? 0.2660 0.2707 0.1838 -0.0242 0.0026  0.0253  247 THR B N   
4090 C CA  . THR B 247 ? 0.2567 0.2458 0.1683 -0.0216 -0.0018 0.0282  247 THR B CA  
4091 C C   . THR B 247 ? 0.2457 0.2385 0.1631 -0.0143 -0.0062 0.0232  247 THR B C   
4092 O O   . THR B 247 ? 0.2660 0.2723 0.1853 -0.0135 -0.0063 0.0193  247 THR B O   
4093 C CB  . THR B 247 ? 0.2790 0.2577 0.1698 -0.0282 -0.0036 0.0353  247 THR B CB  
4094 O OG1 . THR B 247 ? 0.2906 0.2800 0.1714 -0.0325 -0.0034 0.0353  247 THR B OG1 
4095 C CG2 . THR B 247 ? 0.2947 0.2683 0.1805 -0.0354 0.0008  0.0397  247 THR B CG2 
4096 N N   . GLN B 248 ? 0.2455 0.2274 0.1676 -0.0088 -0.0097 0.0220  248 GLN B N   
4097 C CA  . GLN B 248 ? 0.2116 0.1965 0.1425 -0.0010 -0.0140 0.0159  248 GLN B CA  
4098 C C   . GLN B 248 ? 0.2449 0.2181 0.1634 0.0016  -0.0215 0.0189  248 GLN B C   
4099 O O   . GLN B 248 ? 0.2670 0.2261 0.1727 -0.0019 -0.0233 0.0255  248 GLN B O   
4100 C CB  . GLN B 248 ? 0.2124 0.1958 0.1611 0.0036  -0.0120 0.0099  248 GLN B CB  
4101 C CG  . GLN B 248 ? 0.2174 0.2091 0.1768 0.0013  -0.0055 0.0076  248 GLN B CG  
4102 C CD  . GLN B 248 ? 0.2076 0.2145 0.1720 0.0029  -0.0049 0.0033  248 GLN B CD  
4103 O OE1 . GLN B 248 ? 0.2412 0.2539 0.2110 0.0078  -0.0078 -0.0022 248 GLN B OE1 
4104 N NE2 . GLN B 248 ? 0.2082 0.2226 0.1708 -0.0014 -0.0016 0.0051  248 GLN B NE2 
4105 N N   . PRO B 249 ? 0.2409 0.2187 0.1625 0.0079  -0.0266 0.0141  249 PRO B N   
4106 C CA  . PRO B 249 ? 0.2657 0.2320 0.1741 0.0111  -0.0355 0.0172  249 PRO B CA  
4107 C C   . PRO B 249 ? 0.2742 0.2246 0.1862 0.0152  -0.0392 0.0173  249 PRO B C   
4108 O O   . PRO B 249 ? 0.2675 0.2206 0.1974 0.0193  -0.0370 0.0103  249 PRO B O   
4109 C CB  . PRO B 249 ? 0.2839 0.2620 0.2008 0.0182  -0.0394 0.0095  249 PRO B CB  
4110 C CG  . PRO B 249 ? 0.2743 0.2710 0.2016 0.0154  -0.0320 0.0049  249 PRO B CG  
4111 C CD  . PRO B 249 ? 0.2486 0.2431 0.1848 0.0120  -0.0249 0.0057  249 PRO B CD  
4112 N N   . LEU B 250 ? 0.2883 0.2218 0.1828 0.0137  -0.0450 0.0246  250 LEU B N   
4113 C CA  . LEU B 250 ? 0.2983 0.2159 0.1960 0.0184  -0.0500 0.0240  250 LEU B CA  
4114 C C   . LEU B 250 ? 0.2939 0.2135 0.2040 0.0296  -0.0576 0.0152  250 LEU B C   
4115 O O   . LEU B 250 ? 0.3172 0.2320 0.2406 0.0347  -0.0592 0.0092  250 LEU B O   
4116 C CB  . LEU B 250 ? 0.3595 0.2565 0.2337 0.0143  -0.0555 0.0343  250 LEU B CB  
4117 C CG  . LEU B 250 ? 0.3968 0.2750 0.2719 0.0171  -0.0598 0.0351  250 LEU B CG  
4118 C CD1 . LEU B 250 ? 0.3627 0.2456 0.2533 0.0138  -0.0506 0.0314  250 LEU B CD1 
4119 C CD2 . LEU B 250 ? 0.4237 0.2806 0.2725 0.0112  -0.0645 0.0465  250 LEU B CD2 
4120 N N   . LYS B 251 ? 0.2860 0.2135 0.1923 0.0335  -0.0627 0.0133  251 LYS B N   
4121 C CA  . LYS B 251 ? 0.2993 0.2300 0.2168 0.0442  -0.0707 0.0044  251 LYS B CA  
4122 C C   . LYS B 251 ? 0.3447 0.2560 0.2582 0.0504  -0.0805 0.0054  251 LYS B C   
4123 O O   . LYS B 251 ? 0.3711 0.2647 0.2632 0.0473  -0.0858 0.0156  251 LYS B O   
4124 C CB  . LYS B 251 ? 0.2898 0.2375 0.2332 0.0472  -0.0638 -0.0075 251 LYS B CB  
4125 C CG  . LYS B 251 ? 0.3541 0.3192 0.3003 0.0418  -0.0555 -0.0082 251 LYS B CG  
4126 C CD  . LYS B 251 ? 0.3699 0.3507 0.3393 0.0450  -0.0503 -0.0200 251 LYS B CD  
4127 C CE  . LYS B 251 ? 0.4251 0.4203 0.3958 0.0401  -0.0433 -0.0199 251 LYS B CE  
4128 N NZ  . LYS B 251 ? 0.4270 0.4355 0.4184 0.0424  -0.0381 -0.0307 251 LYS B NZ  
4129 N N   . ASN B 252 ? 0.3241 0.2383 0.2573 0.0590  -0.0837 -0.0057 252 ASN B N   
4130 C CA  . ASN B 252 ? 0.3720 0.2701 0.3038 0.0673  -0.0953 -0.0073 252 ASN B CA  
4131 C C   . ASN B 252 ? 0.4131 0.3012 0.3513 0.0642  -0.0908 -0.0074 252 ASN B C   
4132 O O   . ASN B 252 ? 0.4496 0.3410 0.4078 0.0698  -0.0913 -0.0186 252 ASN B O   
4133 C CB  . ASN B 252 ? 0.4307 0.3398 0.3813 0.0789  -0.1021 -0.0211 252 ASN B CB  
4134 C CG  . ASN B 252 ? 0.5084 0.4016 0.4556 0.0890  -0.1167 -0.0227 252 ASN B CG  
4135 O OD1 . ASN B 252 ? 0.5024 0.3738 0.4302 0.0874  -0.1228 -0.0120 252 ASN B OD1 
4136 N ND2 . ASN B 252 ? 0.5468 0.4500 0.5132 0.0998  -0.1230 -0.0367 252 ASN B ND2 
4137 N N   . ARG B 253 ? 0.3603 0.2380 0.2820 0.0543  -0.0856 0.0042  253 ARG B N   
4138 C CA  . ARG B 253 ? 0.3520 0.2196 0.2764 0.0497  -0.0808 0.0058  253 ARG B CA  
4139 C C   . ARG B 253 ? 0.3831 0.2282 0.2824 0.0448  -0.0855 0.0187  253 ARG B C   
4140 O O   . ARG B 253 ? 0.4155 0.2558 0.2941 0.0414  -0.0888 0.0278  253 ARG B O   
4141 C CB  . ARG B 253 ? 0.3148 0.1961 0.2481 0.0402  -0.0661 0.0053  253 ARG B CB  
4142 C CG  . ARG B 253 ? 0.3009 0.2004 0.2582 0.0438  -0.0611 -0.0074 253 ARG B CG  
4143 C CD  . ARG B 253 ? 0.2740 0.1844 0.2373 0.0347  -0.0480 -0.0067 253 ARG B CD  
4144 N NE  . ARG B 253 ? 0.2769 0.1948 0.2294 0.0299  -0.0446 0.0002  253 ARG B NE  
4145 C CZ  . ARG B 253 ? 0.2587 0.1850 0.2125 0.0225  -0.0352 0.0027  253 ARG B CZ  
4146 N NH1 . ARG B 253 ? 0.2697 0.1961 0.2322 0.0182  -0.0281 0.0006  253 ARG B NH1 
4147 N NH2 . ARG B 253 ? 0.2487 0.1837 0.1951 0.0193  -0.0330 0.0068  253 ARG B NH2 
4148 N N   . GLN B 254 ? 0.3802 0.2118 0.2815 0.0436  -0.0854 0.0190  254 GLN B N   
4149 C CA  . GLN B 254 ? 0.4476 0.2557 0.3267 0.0383  -0.0892 0.0304  254 GLN B CA  
4150 C C   . GLN B 254 ? 0.4340 0.2433 0.3159 0.0282  -0.0776 0.0324  254 GLN B C   
4151 O O   . GLN B 254 ? 0.4648 0.2828 0.3671 0.0295  -0.0721 0.0234  254 GLN B O   
4152 C CB  . GLN B 254 ? 0.5206 0.3073 0.3984 0.0481  -0.1030 0.0283  254 GLN B CB  
4153 C CG  . GLN B 254 ? 0.6136 0.4006 0.4912 0.0595  -0.1154 0.0246  254 GLN B CG  
4154 C CD  . GLN B 254 ? 0.7318 0.5011 0.6140 0.0716  -0.1299 0.0193  254 GLN B CD  
4155 O OE1 . GLN B 254 ? 0.7409 0.5114 0.6430 0.0754  -0.1286 0.0094  254 GLN B OE1 
4156 N NE2 . GLN B 254 ? 0.7956 0.5484 0.6593 0.0778  -0.1442 0.0254  254 GLN B NE2 
4157 N N   . ILE B 255 ? 0.4132 0.2153 0.2747 0.0176  -0.0733 0.0436  255 ILE B N   
4158 C CA  . ILE B 255 ? 0.3983 0.1997 0.2600 0.0079  -0.0635 0.0462  255 ILE B CA  
4159 C C   . ILE B 255 ? 0.4297 0.2055 0.2815 0.0080  -0.0701 0.0500  255 ILE B C   
4160 O O   . ILE B 255 ? 0.4575 0.2141 0.2881 0.0077  -0.0785 0.0582  255 ILE B O   
4161 C CB  . ILE B 255 ? 0.3923 0.2025 0.2400 -0.0039 -0.0547 0.0542  255 ILE B CB  
4162 C CG1 . ILE B 255 ? 0.4091 0.2440 0.2687 -0.0023 -0.0495 0.0492  255 ILE B CG1 
4163 C CG2 . ILE B 255 ? 0.4142 0.2252 0.2634 -0.0134 -0.0449 0.0559  255 ILE B CG2 
4164 C CD1 . ILE B 255 ? 0.4062 0.2530 0.2551 -0.0128 -0.0412 0.0549  255 ILE B CD1 
4165 N N   . LYS B 256 ? 0.4210 0.1958 0.2881 0.0087  -0.0669 0.0435  256 LYS B N   
4166 C CA  . LYS B 256 ? 0.4399 0.1911 0.3010 0.0093  -0.0727 0.0452  256 LYS B CA  
4167 C C   . LYS B 256 ? 0.4187 0.1667 0.2714 -0.0037 -0.0628 0.0511  256 LYS B C   
4168 O O   . LYS B 256 ? 0.4295 0.1963 0.2901 -0.0103 -0.0516 0.0495  256 LYS B O   
4169 C CB  . LYS B 256 ? 0.4331 0.1855 0.3184 0.0192  -0.0766 0.0319  256 LYS B CB  
4170 C CG  . LYS B 256 ? 0.4618 0.2183 0.3584 0.0329  -0.0871 0.0237  256 LYS B CG  
4171 C CD  . LYS B 256 ? 0.5497 0.2837 0.4249 0.0384  -0.1014 0.0320  256 LYS B CD  
4172 C CE  . LYS B 256 ? 0.6131 0.3492 0.5011 0.0535  -0.1138 0.0224  256 LYS B CE  
4173 N NZ  . LYS B 256 ? 0.6724 0.3840 0.5356 0.0581  -0.1285 0.0324  256 LYS B NZ  
4174 N N   . ALA B 257 ? 0.4648 0.1884 0.3005 -0.0073 -0.0675 0.0582  257 ALA B N   
4175 C CA  . ALA B 257 ? 0.4821 0.2001 0.3097 -0.0194 -0.0591 0.0629  257 ALA B CA  
4176 C C   . ALA B 257 ? 0.4904 0.1961 0.3297 -0.0164 -0.0612 0.0564  257 ALA B C   
4177 O O   . ALA B 257 ? 0.5101 0.2016 0.3536 -0.0064 -0.0722 0.0524  257 ALA B O   
4178 C CB  . ALA B 257 ? 0.4894 0.2026 0.2960 -0.0272 -0.0588 0.0717  257 ALA B CB  
4179 N N   . SER B 258 ? 0.4741 0.1888 0.3205 -0.0250 -0.0504 0.0541  258 SER B N   
4180 C CA  . SER B 258 ? 0.4642 0.1700 0.3215 -0.0246 -0.0501 0.0475  258 SER B CA  
4181 C C   . SER B 258 ? 0.5260 0.2179 0.3706 -0.0286 -0.0522 0.0529  258 SER B C   
4182 O O   . SER B 258 ? 0.5467 0.2287 0.3997 -0.0268 -0.0540 0.0475  258 SER B O   
4183 C CB  . SER B 258 ? 0.4370 0.1636 0.3064 -0.0332 -0.0364 0.0431  258 SER B CB  
4184 O OG  . SER B 258 ? 0.4541 0.1856 0.3094 -0.0451 -0.0284 0.0511  258 SER B OG  
4185 N N   . PHE B 259 ? 0.5141 0.2062 0.3398 -0.0345 -0.0514 0.0622  259 PHE B N   
4186 C CA  . PHE B 259 ? 0.5338 0.2140 0.3460 -0.0408 -0.0515 0.0672  259 PHE B CA  
4187 C C   . PHE B 259 ? 0.5926 0.2565 0.3890 -0.0359 -0.0627 0.0728  259 PHE B C   
4188 O O   . PHE B 259 ? 0.6038 0.2721 0.3957 -0.0319 -0.0667 0.0749  259 PHE B O   
4189 C CB  . PHE B 259 ? 0.5473 0.2444 0.3524 -0.0540 -0.0392 0.0710  259 PHE B CB  
4190 C CG  . PHE B 259 ? 0.5482 0.2634 0.3481 -0.0567 -0.0353 0.0741  259 PHE B CG  
4191 C CD1 . PHE B 259 ? 0.5146 0.2498 0.3271 -0.0560 -0.0293 0.0705  259 PHE B CD1 
4192 C CD2 . PHE B 259 ? 0.5812 0.2928 0.3637 -0.0599 -0.0380 0.0802  259 PHE B CD2 
4193 C CE1 . PHE B 259 ? 0.5286 0.2806 0.3369 -0.0581 -0.0261 0.0729  259 PHE B CE1 
4194 C CE2 . PHE B 259 ? 0.5696 0.2984 0.3486 -0.0623 -0.0346 0.0819  259 PHE B CE2 
4195 C CZ  . PHE B 259 ? 0.5702 0.3194 0.3627 -0.0610 -0.0289 0.0782  259 PHE B CZ  
4206 N N   . ALA C 2   ? 0.1876 0.2722 0.2065 -0.0079 -0.0331 -0.0083 2   ALA C N   
4207 C CA  . ALA C 2   ? 0.1711 0.2680 0.2024 -0.0035 -0.0323 -0.0070 2   ALA C CA  
4208 C C   . ALA C 2   ? 0.1830 0.2758 0.2174 -0.0039 -0.0266 -0.0086 2   ALA C C   
4209 O O   . ALA C 2   ? 0.1770 0.2636 0.2063 -0.0104 -0.0249 -0.0106 2   ALA C O   
4210 C CB  . ALA C 2   ? 0.1641 0.2613 0.1971 0.0049  -0.0344 -0.0026 2   ALA C CB  
4211 N N   . HIS C 3   ? 0.1640 0.2591 0.2058 0.0023  -0.0237 -0.0079 3   HIS C N   
4212 C CA  . HIS C 3   ? 0.1585 0.2499 0.2011 0.0005  -0.0180 -0.0104 3   HIS C CA  
4213 C C   . HIS C 3   ? 0.1654 0.2400 0.1975 -0.0009 -0.0164 -0.0096 3   HIS C C   
4214 O O   . HIS C 3   ? 0.1834 0.2496 0.2118 0.0036  -0.0174 -0.0071 3   HIS C O   
4215 C CB  . HIS C 3   ? 0.1779 0.2751 0.2309 0.0077  -0.0148 -0.0111 3   HIS C CB  
4216 C CG  . HIS C 3   ? 0.2179 0.3340 0.2841 0.0084  -0.0150 -0.0127 3   HIS C CG  
4217 N ND1 . HIS C 3   ? 0.2650 0.3902 0.3397 0.0079  -0.0093 -0.0168 3   HIS C ND1 
4218 C CD2 . HIS C 3   ? 0.2353 0.3642 0.3075 0.0083  -0.0203 -0.0110 3   HIS C CD2 
4219 C CE1 . HIS C 3   ? 0.2616 0.4055 0.3491 0.0085  -0.0107 -0.0173 3   HIS C CE1 
4220 N NE2 . HIS C 3   ? 0.2232 0.3696 0.3094 0.0086  -0.0179 -0.0135 3   HIS C NE2 
4221 N N   . HIS C 4   ? 0.1577 0.2279 0.1854 -0.0076 -0.0142 -0.0112 4   HIS C N   
4222 C CA  . HIS C 4   ? 0.1799 0.2357 0.1994 -0.0089 -0.0135 -0.0098 4   HIS C CA  
4223 C C   . HIS C 4   ? 0.1629 0.2144 0.1834 -0.0049 -0.0101 -0.0099 4   HIS C C   
4224 O O   . HIS C 4   ? 0.1761 0.2345 0.2022 -0.0034 -0.0067 -0.0125 4   HIS C O   
4225 C CB  . HIS C 4   ? 0.1713 0.2242 0.1862 -0.0177 -0.0133 -0.0104 4   HIS C CB  
4226 C CG  . HIS C 4   ? 0.1664 0.2058 0.1743 -0.0200 -0.0139 -0.0083 4   HIS C CG  
4227 N ND1 . HIS C 4   ? 0.1420 0.1725 0.1467 -0.0179 -0.0164 -0.0066 4   HIS C ND1 
4228 C CD2 . HIS C 4   ? 0.1874 0.2220 0.1914 -0.0248 -0.0126 -0.0074 4   HIS C CD2 
4229 C CE1 . HIS C 4   ? 0.1591 0.1802 0.1602 -0.0205 -0.0167 -0.0046 4   HIS C CE1 
4230 N NE2 . HIS C 4   ? 0.1761 0.1992 0.1761 -0.0250 -0.0150 -0.0046 4   HIS C NE2 
4231 N N   . TRP C 5   ? 0.1637 0.2036 0.1788 -0.0035 -0.0106 -0.0076 5   TRP C N   
4232 C CA  . TRP C 5   ? 0.1518 0.1859 0.1667 -0.0008 -0.0079 -0.0077 5   TRP C CA  
4233 C C   . TRP C 5   ? 0.1925 0.2264 0.2050 -0.0063 -0.0046 -0.0104 5   TRP C C   
4234 O O   . TRP C 5   ? 0.1905 0.2265 0.1998 -0.0130 -0.0049 -0.0108 5   TRP C O   
4235 C CB  . TRP C 5   ? 0.1749 0.1981 0.1850 0.0003  -0.0094 -0.0043 5   TRP C CB  
4236 C CG  . TRP C 5   ? 0.1571 0.1744 0.1622 -0.0054 -0.0107 -0.0030 5   TRP C CG  
4237 C CD1 . TRP C 5   ? 0.1806 0.1963 0.1842 -0.0071 -0.0132 -0.0020 5   TRP C CD1 
4238 C CD2 . TRP C 5   ? 0.1624 0.1745 0.1640 -0.0099 -0.0100 -0.0027 5   TRP C CD2 
4239 N NE1 . TRP C 5   ? 0.1789 0.1884 0.1796 -0.0116 -0.0143 -0.0003 5   TRP C NE1 
4240 C CE2 . TRP C 5   ? 0.1652 0.1730 0.1642 -0.0139 -0.0128 -0.0003 5   TRP C CE2 
4241 C CE3 . TRP C 5   ? 0.1652 0.1756 0.1649 -0.0115 -0.0075 -0.0044 5   TRP C CE3 
4242 C CZ2 . TRP C 5   ? 0.1820 0.1846 0.1774 -0.0189 -0.0141 0.0018  5   TRP C CZ2 
4243 C CZ3 . TRP C 5   ? 0.1901 0.1953 0.1843 -0.0175 -0.0084 -0.0031 5   TRP C CZ3 
4244 C CH2 . TRP C 5   ? 0.1914 0.1934 0.1837 -0.0212 -0.0121 0.0005  5   TRP C CH2 
4245 N N   . GLY C 6   ? 0.1718 0.2029 0.1850 -0.0038 -0.0015 -0.0124 6   GLY C N   
4246 C CA  . GLY C 6   ? 0.1795 0.2101 0.1885 -0.0093 0.0022  -0.0157 6   GLY C CA  
4247 C C   . GLY C 6   ? 0.1641 0.1864 0.1713 -0.0067 0.0047  -0.0177 6   GLY C C   
4248 O O   . GLY C 6   ? 0.1856 0.1994 0.1919 -0.0036 0.0025  -0.0147 6   GLY C O   
4249 N N   . TYR C 7   ? 0.1914 0.2162 0.1973 -0.0092 0.0098  -0.0232 7   TYR C N   
4250 C CA  . TYR C 7   ? 0.1874 0.2038 0.1909 -0.0076 0.0131  -0.0270 7   TYR C CA  
4251 C C   . TYR C 7   ? 0.2107 0.2333 0.2226 -0.0019 0.0190  -0.0335 7   TYR C C   
4252 O O   . TYR C 7   ? 0.2368 0.2533 0.2462 -0.0017 0.0235  -0.0391 7   TYR C O   
4253 C CB  . TYR C 7   ? 0.2070 0.2181 0.1983 -0.0172 0.0141  -0.0286 7   TYR C CB  
4254 C CG  . TYR C 7   ? 0.1977 0.2016 0.1826 -0.0218 0.0080  -0.0218 7   TYR C CG  
4255 C CD1 . TYR C 7   ? 0.2025 0.1962 0.1862 -0.0200 0.0055  -0.0194 7   TYR C CD1 
4256 C CD2 . TYR C 7   ? 0.2149 0.2222 0.1964 -0.0277 0.0045  -0.0177 7   TYR C CD2 
4257 C CE1 . TYR C 7   ? 0.2062 0.1956 0.1867 -0.0236 0.0002  -0.0134 7   TYR C CE1 
4258 C CE2 . TYR C 7   ? 0.2049 0.2059 0.1828 -0.0309 -0.0011 -0.0117 7   TYR C CE2 
4259 C CZ  . TYR C 7   ? 0.1960 0.1893 0.1741 -0.0286 -0.0029 -0.0098 7   TYR C CZ  
4260 O OH  . TYR C 7   ? 0.2292 0.2184 0.2061 -0.0311 -0.0081 -0.0040 7   TYR C OH  
4261 N N   . GLY C 8   ? 0.2090 0.2440 0.2314 0.0027  0.0190  -0.0334 8   GLY C N   
4262 C CA  . GLY C 8   ? 0.2159 0.2593 0.2494 0.0090  0.0244  -0.0392 8   GLY C CA  
4263 C C   . GLY C 8   ? 0.2122 0.2498 0.2551 0.0198  0.0225  -0.0375 8   GLY C C   
4264 O O   . GLY C 8   ? 0.2000 0.2264 0.2390 0.0215  0.0178  -0.0321 8   GLY C O   
4265 N N   . LYS C 9   ? 0.2065 0.2528 0.2625 0.0271  0.0263  -0.0418 9   LYS C N   
4266 C CA  . LYS C 9   ? 0.2110 0.2513 0.2774 0.0381  0.0248  -0.0403 9   LYS C CA  
4267 C C   . LYS C 9   ? 0.2111 0.2535 0.2813 0.0421  0.0167  -0.0312 9   LYS C C   
4268 O O   . LYS C 9   ? 0.2289 0.2605 0.3006 0.0480  0.0133  -0.0269 9   LYS C O   
4269 C CB  . LYS C 9   ? 0.2333 0.2847 0.3156 0.0458  0.0306  -0.0468 9   LYS C CB  
4270 C CG  . LYS C 9   ? 0.2903 0.3420 0.3687 0.0416  0.0400  -0.0572 9   LYS C CG  
4271 C CD  . LYS C 9   ? 0.3266 0.3571 0.3945 0.0407  0.0417  -0.0600 9   LYS C CD  
4272 C CE  . LYS C 9   ? 0.4072 0.4368 0.4718 0.0381  0.0522  -0.0723 9   LYS C CE  
4273 N NZ  . LYS C 9   ? 0.4655 0.5001 0.5484 0.0498  0.0580  -0.0790 9   LYS C NZ  
4274 N N   . HIS C 10  ? 0.2078 0.2637 0.2792 0.0386  0.0135  -0.0283 10  HIS C N   
4275 C CA  . HIS C 10  ? 0.1995 0.2586 0.2734 0.0416  0.0061  -0.0207 10  HIS C CA  
4276 C C   . HIS C 10  ? 0.2007 0.2522 0.2609 0.0349  0.0020  -0.0160 10  HIS C C   
4277 O O   . HIS C 10  ? 0.2204 0.2681 0.2786 0.0374  -0.0033 -0.0099 10  HIS C O   
4278 C CB  . HIS C 10  ? 0.2065 0.2858 0.2913 0.0422  0.0045  -0.0208 10  HIS C CB  
4279 C CG  . HIS C 10  ? 0.2424 0.3328 0.3446 0.0503  0.0079  -0.0247 10  HIS C CG  
4280 N ND1 . HIS C 10  ? 0.2937 0.3798 0.4060 0.0608  0.0056  -0.0219 10  HIS C ND1 
4281 C CD2 . HIS C 10  ? 0.2810 0.3876 0.3937 0.0497  0.0134  -0.0308 10  HIS C CD2 
4282 C CE1 . HIS C 10  ? 0.2492 0.3473 0.3784 0.0674  0.0097  -0.0266 10  HIS C CE1 
4283 N NE2 . HIS C 10  ? 0.3109 0.4227 0.4410 0.0608  0.0148  -0.0324 10  HIS C NE2 
4284 N N   . ASN C 11  ? 0.1770 0.2257 0.2276 0.0265  0.0044  -0.0185 11  ASN C N   
4285 C CA  . ASN C 11  ? 0.1651 0.2085 0.2053 0.0206  0.0006  -0.0144 11  ASN C CA  
4286 C C   . ASN C 11  ? 0.1801 0.2093 0.2104 0.0167  0.0016  -0.0141 11  ASN C C   
4287 O O   . ASN C 11  ? 0.1724 0.1978 0.1955 0.0118  -0.0008 -0.0113 11  ASN C O   
4288 C CB  . ASN C 11  ? 0.1631 0.2164 0.2016 0.0135  0.0003  -0.0157 11  ASN C CB  
4289 C CG  . ASN C 11  ? 0.2008 0.2554 0.2359 0.0071  0.0053  -0.0205 11  ASN C CG  
4290 O OD1 . ASN C 11  ? 0.2134 0.2610 0.2458 0.0073  0.0090  -0.0235 11  ASN C OD1 
4291 N ND2 . ASN C 11  ? 0.2227 0.2856 0.2565 0.0004  0.0052  -0.0211 11  ASN C ND2 
4292 N N   . GLY C 12  ? 0.1765 0.1979 0.2069 0.0188  0.0050  -0.0170 12  GLY C N   
4293 C CA  . GLY C 12  ? 0.1871 0.1967 0.2082 0.0137  0.0060  -0.0175 12  GLY C CA  
4294 C C   . GLY C 12  ? 0.1855 0.1841 0.2036 0.0153  0.0028  -0.0123 12  GLY C C   
4295 O O   . GLY C 12  ? 0.1892 0.1885 0.2109 0.0202  -0.0002 -0.0077 12  GLY C O   
4296 N N   . PRO C 13  ? 0.1912 0.1800 0.2023 0.0106  0.0035  -0.0129 13  PRO C N   
4297 C CA  . PRO C 13  ? 0.2003 0.1801 0.2082 0.0099  0.0006  -0.0076 13  PRO C CA  
4298 C C   . PRO C 13  ? 0.1950 0.1701 0.2075 0.0167  -0.0006 -0.0039 13  PRO C C   
4299 O O   . PRO C 13  ? 0.2043 0.1788 0.2156 0.0171  -0.0035 0.0019  13  PRO C O   
4300 C CB  . PRO C 13  ? 0.2270 0.1980 0.2285 0.0039  0.0023  -0.0107 13  PRO C CB  
4301 C CG  . PRO C 13  ? 0.2114 0.1892 0.2091 -0.0016 0.0041  -0.0150 13  PRO C CG  
4302 C CD  . PRO C 13  ? 0.1968 0.1850 0.2014 0.0034  0.0062  -0.0176 13  PRO C CD  
4303 N N   . GLU C 14  ? 0.1993 0.1706 0.2170 0.0222  0.0016  -0.0069 14  GLU C N   
4304 C CA  . GLU C 14  ? 0.1989 0.1634 0.2204 0.0284  -0.0006 -0.0019 14  GLU C CA  
4305 C C   . GLU C 14  ? 0.2180 0.1923 0.2433 0.0326  -0.0043 0.0034  14  GLU C C   
4306 O O   . GLU C 14  ? 0.2350 0.2048 0.2609 0.0360  -0.0071 0.0095  14  GLU C O   
4307 C CB  . GLU C 14  ? 0.2111 0.1684 0.2391 0.0345  0.0021  -0.0061 14  GLU C CB  
4308 C CG  . GLU C 14  ? 0.2156 0.1851 0.2536 0.0406  0.0037  -0.0097 14  GLU C CG  
4309 C CD  . GLU C 14  ? 0.2698 0.2321 0.3171 0.0490  0.0056  -0.0124 14  GLU C CD  
4310 O OE1 . GLU C 14  ? 0.2838 0.2299 0.3292 0.0504  0.0048  -0.0100 14  GLU C OE1 
4311 O OE2 . GLU C 14  ? 0.2988 0.2717 0.3563 0.0543  0.0080  -0.0166 14  GLU C OE2 
4312 N N   . HIS C 15  ? 0.1953 0.1826 0.2223 0.0316  -0.0045 0.0015  15  HIS C N   
4313 C CA  . HIS C 15  ? 0.1962 0.1935 0.2257 0.0343  -0.0082 0.0055  15  HIS C CA  
4314 C C   . HIS C 15  ? 0.1823 0.1829 0.2046 0.0290  -0.0100 0.0078  15  HIS C C   
4315 O O   . HIS C 15  ? 0.1929 0.2005 0.2149 0.0303  -0.0130 0.0108  15  HIS C O   
4316 C CB  . HIS C 15  ? 0.1899 0.2004 0.2277 0.0368  -0.0075 0.0015  15  HIS C CB  
4317 C CG  . HIS C 15  ? 0.2447 0.2543 0.2924 0.0436  -0.0054 -0.0013 15  HIS C CG  
4318 N ND1 . HIS C 15  ? 0.2825 0.2852 0.3348 0.0505  -0.0080 0.0035  15  HIS C ND1 
4319 C CD2 . HIS C 15  ? 0.2587 0.2717 0.3123 0.0447  -0.0004 -0.0085 15  HIS C CD2 
4320 C CE1 . HIS C 15  ? 0.3044 0.3061 0.3666 0.0565  -0.0050 -0.0009 15  HIS C CE1 
4321 N NE2 . HIS C 15  ? 0.2828 0.2918 0.3461 0.0531  0.0001  -0.0086 15  HIS C NE2 
4322 N N   . TRP C 16  ? 0.1685 0.1646 0.1852 0.0232  -0.0083 0.0063  16  TRP C N   
4323 C CA  . TRP C 16  ? 0.1653 0.1648 0.1775 0.0192  -0.0096 0.0076  16  TRP C CA  
4324 C C   . TRP C 16  ? 0.1867 0.1856 0.1961 0.0208  -0.0116 0.0128  16  TRP C C   
4325 O O   . TRP C 16  ? 0.1867 0.1912 0.1937 0.0197  -0.0129 0.0130  16  TRP C O   
4326 C CB  . TRP C 16  ? 0.1587 0.1531 0.1672 0.0135  -0.0083 0.0066  16  TRP C CB  
4327 C CG  . TRP C 16  ? 0.1791 0.1756 0.1875 0.0099  -0.0067 0.0019  16  TRP C CG  
4328 C CD1 . TRP C 16  ? 0.1678 0.1721 0.1793 0.0104  -0.0058 -0.0017 16  TRP C CD1 
4329 C CD2 . TRP C 16  ? 0.1821 0.1740 0.1866 0.0041  -0.0061 0.0007  16  TRP C CD2 
4330 N NE1 . TRP C 16  ? 0.1685 0.1731 0.1772 0.0049  -0.0039 -0.0051 16  TRP C NE1 
4331 C CE2 . TRP C 16  ? 0.1626 0.1592 0.1664 0.0010  -0.0044 -0.0036 16  TRP C CE2 
4332 C CE3 . TRP C 16  ? 0.1782 0.1637 0.1798 0.0007  -0.0070 0.0031  16  TRP C CE3 
4333 C CZ2 . TRP C 16  ? 0.1799 0.1738 0.1784 -0.0057 -0.0039 -0.0051 16  TRP C CZ2 
4334 C CZ3 . TRP C 16  ? 0.1933 0.1764 0.1910 -0.0055 -0.0071 0.0016  16  TRP C CZ3 
4335 C CH2 . TRP C 16  ? 0.1858 0.1728 0.1810 -0.0088 -0.0058 -0.0023 16  TRP C CH2 
4336 N N   . HIS C 17  ? 0.1832 0.1748 0.1919 0.0228  -0.0117 0.0168  17  HIS C N   
4337 C CA  . HIS C 17  ? 0.1825 0.1739 0.1870 0.0233  -0.0132 0.0223  17  HIS C CA  
4338 C C   . HIS C 17  ? 0.1989 0.1984 0.2027 0.0261  -0.0161 0.0238  17  HIS C C   
4339 O O   . HIS C 17  ? 0.2217 0.2232 0.2196 0.0249  -0.0169 0.0269  17  HIS C O   
4340 C CB  . HIS C 17  ? 0.2262 0.2079 0.2302 0.0246  -0.0133 0.0271  17  HIS C CB  
4341 C CG  . HIS C 17  ? 0.2190 0.1982 0.2280 0.0302  -0.0150 0.0281  17  HIS C CG  
4342 N ND1 . HIS C 17  ? 0.2807 0.2617 0.2895 0.0341  -0.0186 0.0337  17  HIS C ND1 
4343 C CD2 . HIS C 17  ? 0.1888 0.1648 0.2040 0.0329  -0.0138 0.0238  17  HIS C CD2 
4344 C CE1 . HIS C 17  ? 0.2678 0.2465 0.2842 0.0397  -0.0199 0.0334  17  HIS C CE1 
4345 N NE2 . HIS C 17  ? 0.2436 0.2195 0.2641 0.0393  -0.0164 0.0268  17  HIS C NE2 
4346 N N   . LYS C 18  ? 0.1744 0.1796 0.1841 0.0294  -0.0177 0.0217  18  LYS C N   
4347 C CA  . LYS C 18  ? 0.1710 0.1852 0.1809 0.0316  -0.0217 0.0238  18  LYS C CA  
4348 C C   . LYS C 18  ? 0.1884 0.2092 0.1928 0.0273  -0.0220 0.0210  18  LYS C C   
4349 O O   . LYS C 18  ? 0.1911 0.2175 0.1912 0.0272  -0.0251 0.0232  18  LYS C O   
4350 C CB  . LYS C 18  ? 0.1843 0.2051 0.2043 0.0359  -0.0230 0.0216  18  LYS C CB  
4351 C CG  . LYS C 18  ? 0.2878 0.3008 0.3137 0.0414  -0.0229 0.0244  18  LYS C CG  
4352 C CD  . LYS C 18  ? 0.3067 0.3273 0.3449 0.0463  -0.0229 0.0207  18  LYS C CD  
4353 C CE  . LYS C 18  ? 0.3444 0.3555 0.3899 0.0525  -0.0217 0.0216  18  LYS C CE  
4354 N NZ  . LYS C 18  ? 0.3920 0.4132 0.4514 0.0580  -0.0207 0.0170  18  LYS C NZ  
4355 N N   . ASP C 19  ? 0.1737 0.1932 0.1779 0.0236  -0.0191 0.0163  19  ASP C N   
4356 C CA  . ASP C 19  ? 0.1736 0.1965 0.1731 0.0196  -0.0191 0.0132  19  ASP C CA  
4357 C C   . ASP C 19  ? 0.1956 0.2121 0.1908 0.0171  -0.0161 0.0130  19  ASP C C   
4358 O O   . ASP C 19  ? 0.1868 0.2047 0.1774 0.0152  -0.0158 0.0112  19  ASP C O   
4359 C CB  . ASP C 19  ? 0.1668 0.1941 0.1705 0.0170  -0.0189 0.0083  19  ASP C CB  
4360 C CG  . ASP C 19  ? 0.1980 0.2346 0.2078 0.0191  -0.0214 0.0079  19  ASP C CG  
4361 O OD1 . ASP C 19  ? 0.2335 0.2768 0.2415 0.0192  -0.0248 0.0089  19  ASP C OD1 
4362 O OD2 . ASP C 19  ? 0.2214 0.2594 0.2380 0.0207  -0.0198 0.0065  19  ASP C OD2 
4363 N N   . PHE C 20  ? 0.1791 0.1892 0.1764 0.0171  -0.0140 0.0145  20  PHE C N   
4364 C CA  . PHE C 20  ? 0.1890 0.1949 0.1852 0.0148  -0.0116 0.0147  20  PHE C CA  
4365 C C   . PHE C 20  ? 0.1841 0.1858 0.1793 0.0156  -0.0104 0.0195  20  PHE C C   
4366 O O   . PHE C 20  ? 0.2154 0.2118 0.2134 0.0150  -0.0098 0.0205  20  PHE C O   
4367 C CB  . PHE C 20  ? 0.1869 0.1901 0.1868 0.0122  -0.0110 0.0122  20  PHE C CB  
4368 C CG  . PHE C 20  ? 0.1675 0.1743 0.1681 0.0104  -0.0122 0.0083  20  PHE C CG  
4369 C CD1 . PHE C 20  ? 0.1925 0.1996 0.1918 0.0087  -0.0124 0.0063  20  PHE C CD1 
4370 C CD2 . PHE C 20  ? 0.1846 0.1943 0.1878 0.0104  -0.0129 0.0066  20  PHE C CD2 
4371 C CE1 . PHE C 20  ? 0.1664 0.1756 0.1658 0.0061  -0.0138 0.0032  20  PHE C CE1 
4372 C CE2 . PHE C 20  ? 0.1735 0.1876 0.1774 0.0076  -0.0138 0.0034  20  PHE C CE2 
4373 C CZ  . PHE C 20  ? 0.1892 0.2024 0.1906 0.0050  -0.0146 0.0020  20  PHE C CZ  
4374 N N   . PRO C 21  ? 0.1714 0.1749 0.1615 0.0163  -0.0102 0.0225  21  PRO C N   
4375 C CA  . PRO C 21  ? 0.2018 0.2008 0.1903 0.0164  -0.0096 0.0282  21  PRO C CA  
4376 C C   . PRO C 21  ? 0.1855 0.1810 0.1768 0.0135  -0.0067 0.0291  21  PRO C C   
4377 O O   . PRO C 21  ? 0.2137 0.2038 0.2050 0.0126  -0.0065 0.0335  21  PRO C O   
4378 C CB  . PRO C 21  ? 0.2416 0.2448 0.2223 0.0163  -0.0098 0.0312  21  PRO C CB  
4379 C CG  . PRO C 21  ? 0.2504 0.2597 0.2286 0.0159  -0.0099 0.0258  21  PRO C CG  
4380 C CD  . PRO C 21  ? 0.1824 0.1917 0.1669 0.0164  -0.0113 0.0211  21  PRO C CD  
4381 N N   A ILE C 22  ? 0.1836 0.1818 0.1778 0.0119  -0.0050 0.0256  22  ILE C N   
4382 N N   B ILE C 22  ? 0.1832 0.1814 0.1775 0.0119  -0.0050 0.0256  22  ILE C N   
4383 C CA  A ILE C 22  ? 0.1809 0.1776 0.1799 0.0091  -0.0032 0.0269  22  ILE C CA  
4384 C CA  B ILE C 22  ? 0.1815 0.1782 0.1804 0.0092  -0.0032 0.0269  22  ILE C CA  
4385 C C   A ILE C 22  ? 0.1941 0.1844 0.1958 0.0076  -0.0050 0.0273  22  ILE C C   
4386 C C   B ILE C 22  ? 0.1932 0.1836 0.1950 0.0076  -0.0050 0.0272  22  ILE C C   
4387 O O   A ILE C 22  ? 0.2010 0.1892 0.2058 0.0044  -0.0044 0.0294  22  ILE C O   
4388 O O   B ILE C 22  ? 0.2005 0.1889 0.2055 0.0044  -0.0044 0.0291  22  ILE C O   
4389 C CB  A ILE C 22  ? 0.1862 0.1871 0.1894 0.0088  -0.0019 0.0233  22  ILE C CB  
4390 C CB  B ILE C 22  ? 0.1855 0.1865 0.1885 0.0088  -0.0018 0.0233  22  ILE C CB  
4391 C CG1 A ILE C 22  ? 0.1828 0.1853 0.1926 0.0064  -0.0002 0.0255  22  ILE C CG1 
4392 C CG1 B ILE C 22  ? 0.1869 0.1902 0.1961 0.0066  0.0004  0.0257  22  ILE C CG1 
4393 C CG2 A ILE C 22  ? 0.1998 0.1989 0.2048 0.0087  -0.0047 0.0197  22  ILE C CG2 
4394 C CG2 B ILE C 22  ? 0.1964 0.1955 0.2023 0.0083  -0.0045 0.0200  22  ILE C CG2 
4395 C CD1 A ILE C 22  ? 0.1867 0.1927 0.1952 0.0055  0.0035  0.0290  22  ILE C CD1 
4396 C CD1 B ILE C 22  ? 0.1844 0.1914 0.2003 0.0074  0.0011  0.0227  22  ILE C CD1 
4397 N N   . ALA C 23  ? 0.1780 0.1658 0.1790 0.0095  -0.0069 0.0251  23  ALA C N   
4398 C CA  . ALA C 23  ? 0.1995 0.1803 0.2018 0.0081  -0.0076 0.0245  23  ALA C CA  
4399 C C   . ALA C 23  ? 0.1926 0.1665 0.1942 0.0067  -0.0072 0.0289  23  ALA C C   
4400 O O   . ALA C 23  ? 0.2159 0.1833 0.2184 0.0037  -0.0074 0.0281  23  ALA C O   
4401 C CB  . ALA C 23  ? 0.1986 0.1788 0.2010 0.0117  -0.0087 0.0217  23  ALA C CB  
4402 N N   . LYS C 24  ? 0.2011 0.1756 0.2000 0.0080  -0.0067 0.0335  24  LYS C N   
4403 C CA  . LYS C 24  ? 0.2064 0.1737 0.2037 0.0059  -0.0065 0.0388  24  LYS C CA  
4404 C C   . LYS C 24  ? 0.2181 0.1903 0.2160 0.0016  -0.0041 0.0421  24  LYS C C   
4405 O O   . LYS C 24  ? 0.2600 0.2290 0.2555 -0.0009 -0.0033 0.0476  24  LYS C O   
4406 C CB  . LYS C 24  ? 0.2619 0.2263 0.2555 0.0098  -0.0081 0.0430  24  LYS C CB  
4407 C CG  . LYS C 24  ? 0.3068 0.2664 0.3031 0.0147  -0.0103 0.0400  24  LYS C CG  
4408 C CD  . LYS C 24  ? 0.4075 0.3638 0.4022 0.0189  -0.0129 0.0454  24  LYS C CD  
4409 C CE  . LYS C 24  ? 0.4529 0.4070 0.4531 0.0249  -0.0148 0.0423  24  LYS C CE  
4410 N NZ  . LYS C 24  ? 0.5053 0.4471 0.5093 0.0253  -0.0136 0.0392  24  LYS C NZ  
4411 N N   . GLY C 25  ? 0.2350 0.2148 0.2368 0.0004  -0.0029 0.0389  25  GLY C N   
4412 C CA  . GLY C 25  ? 0.2157 0.2031 0.2209 -0.0025 0.0000  0.0409  25  GLY C CA  
4413 C C   . GLY C 25  ? 0.2359 0.2208 0.2454 -0.0082 -0.0001 0.0440  25  GLY C C   
4414 O O   . GLY C 25  ? 0.2411 0.2165 0.2495 -0.0105 -0.0023 0.0444  25  GLY C O   
4415 N N   . GLU C 26  ? 0.2077 0.2019 0.2230 -0.0106 0.0026  0.0455  26  GLU C N   
4416 C CA  . GLU C 26  ? 0.2496 0.2449 0.2703 -0.0168 0.0028  0.0492  26  GLU C CA  
4417 C C   . GLU C 26  ? 0.2306 0.2282 0.2590 -0.0193 -0.0002 0.0471  26  GLU C C   
4418 O O   . GLU C 26  ? 0.2897 0.2875 0.3224 -0.0254 -0.0015 0.0500  26  GLU C O   
4419 C CB  . GLU C 26  ? 0.2443 0.2511 0.2688 -0.0183 0.0078  0.0523  26  GLU C CB  
4420 C CG  . GLU C 26  ? 0.2844 0.2892 0.2992 -0.0179 0.0107  0.0558  26  GLU C CG  
4421 C CD  . GLU C 26  ? 0.3883 0.3806 0.3977 -0.0222 0.0082  0.0610  26  GLU C CD  
4422 O OE1 . GLU C 26  ? 0.4270 0.4187 0.4414 -0.0285 0.0079  0.0639  26  GLU C OE1 
4423 O OE2 . GLU C 26  ? 0.4427 0.4258 0.4440 -0.0191 0.0061  0.0619  26  GLU C OE2 
4424 N N   . ARG C 27  ? 0.2081 0.2077 0.2381 -0.0155 -0.0019 0.0429  27  ARG C N   
4425 C CA  A ARG C 27  ? 0.1981 0.2011 0.2351 -0.0178 -0.0054 0.0420  27  ARG C CA  
4426 C CA  B ARG C 27  ? 0.1972 0.1995 0.2339 -0.0184 -0.0056 0.0421  27  ARG C CA  
4427 C C   . ARG C 27  ? 0.1852 0.1812 0.2167 -0.0167 -0.0088 0.0379  27  ARG C C   
4428 O O   . ARG C 27  ? 0.2068 0.2065 0.2418 -0.0151 -0.0107 0.0363  27  ARG C O   
4429 C CB  A ARG C 27  ? 0.2045 0.2198 0.2518 -0.0147 -0.0034 0.0419  27  ARG C CB  
4430 C CB  B ARG C 27  ? 0.2007 0.2157 0.2490 -0.0167 -0.0044 0.0429  27  ARG C CB  
4431 C CG  A ARG C 27  ? 0.2278 0.2493 0.2860 -0.0169 -0.0074 0.0431  27  ARG C CG  
4432 C CG  B ARG C 27  ? 0.1952 0.2194 0.2494 -0.0177 0.0005  0.0460  27  ARG C CG  
4433 C CD  A ARG C 27  ? 0.2070 0.2399 0.2773 -0.0119 -0.0048 0.0426  27  ARG C CD  
4434 C CD  B ARG C 27  ? 0.1947 0.2325 0.2641 -0.0158 0.0014  0.0463  27  ARG C CD  
4435 N NE  A ARG C 27  ? 0.1034 0.1369 0.1798 -0.0103 -0.0098 0.0422  27  ARG C NE  
4436 N NE  B ARG C 27  ? 0.1949 0.2343 0.2671 -0.0090 0.0017  0.0421  27  ARG C NE  
4437 C CZ  A ARG C 27  ? 0.2102 0.2527 0.3004 -0.0069 -0.0098 0.0430  27  ARG C CZ  
4438 C CZ  B ARG C 27  ? 0.2152 0.2564 0.2843 -0.0038 0.0070  0.0386  27  ARG C CZ  
4439 N NH1 A ARG C 27  ? 0.2334 0.2866 0.3337 -0.0044 -0.0041 0.0433  27  ARG C NH1 
4440 N NH1 B ARG C 27  ? 0.1782 0.2194 0.2500 0.0017  0.0070  0.0344  27  ARG C NH1 
4441 N NH2 A ARG C 27  ? 0.2271 0.2679 0.3215 -0.0060 -0.0153 0.0436  27  ARG C NH2 
4442 N NH2 B ARG C 27  ? 0.2423 0.2842 0.3039 -0.0047 0.0120  0.0393  27  ARG C NH2 
4443 N N   . GLN C 28  ? 0.1984 0.1842 0.2216 -0.0172 -0.0094 0.0364  28  GLN C N   
4444 C CA  . GLN C 28  ? 0.1892 0.1700 0.2071 -0.0157 -0.0112 0.0319  28  GLN C CA  
4445 C C   . GLN C 28  ? 0.2010 0.1776 0.2172 -0.0219 -0.0146 0.0306  28  GLN C C   
4446 O O   . GLN C 28  ? 0.2110 0.1849 0.2278 -0.0274 -0.0158 0.0326  28  GLN C O   
4447 C CB  . GLN C 28  ? 0.2098 0.1832 0.2213 -0.0121 -0.0095 0.0302  28  GLN C CB  
4448 C CG  . GLN C 28  ? 0.1909 0.1692 0.2020 -0.0064 -0.0072 0.0309  28  GLN C CG  
4449 C CD  . GLN C 28  ? 0.1823 0.1658 0.1941 -0.0036 -0.0079 0.0273  28  GLN C CD  
4450 O OE1 . GLN C 28  ? 0.1917 0.1727 0.2007 -0.0027 -0.0089 0.0239  28  GLN C OE1 
4451 N NE2 . GLN C 28  ? 0.1818 0.1725 0.1979 -0.0026 -0.0069 0.0279  28  GLN C NE2 
4452 N N   . SER C 29  ? 0.1908 0.1670 0.2039 -0.0218 -0.0162 0.0272  29  SER C N   
4453 C CA  . SER C 29  ? 0.1866 0.1596 0.1955 -0.0281 -0.0195 0.0255  29  SER C CA  
4454 C C   . SER C 29  ? 0.2226 0.1899 0.2235 -0.0270 -0.0178 0.0199  29  SER C C   
4455 O O   . SER C 29  ? 0.2104 0.1792 0.2113 -0.0212 -0.0156 0.0181  29  SER C O   
4456 C CB  . SER C 29  ? 0.2027 0.1831 0.2163 -0.0300 -0.0234 0.0280  29  SER C CB  
4457 O OG  . SER C 29  ? 0.1909 0.1783 0.2143 -0.0306 -0.0247 0.0329  29  SER C OG  
4458 N N   . PRO C 30  ? 0.2123 0.1738 0.2064 -0.0328 -0.0188 0.0167  30  PRO C N   
4459 C CA  . PRO C 30  ? 0.1999 0.1590 0.1919 -0.0411 -0.0223 0.0181  30  PRO C CA  
4460 C C   . PRO C 30  ? 0.2181 0.1698 0.2103 -0.0424 -0.0208 0.0185  30  PRO C C   
4461 O O   . PRO C 30  ? 0.2315 0.1793 0.2251 -0.0363 -0.0173 0.0181  30  PRO C O   
4462 C CB  . PRO C 30  ? 0.2321 0.1868 0.2137 -0.0462 -0.0224 0.0126  30  PRO C CB  
4463 C CG  . PRO C 30  ? 0.2311 0.1812 0.2103 -0.0395 -0.0168 0.0069  30  PRO C CG  
4464 C CD  . PRO C 30  ? 0.2231 0.1804 0.2103 -0.0317 -0.0160 0.0104  30  PRO C CD  
4465 N N   . VAL C 31  ? 0.2259 0.1755 0.2167 -0.0506 -0.0241 0.0198  31  VAL C N   
4466 C CA  . VAL C 31  ? 0.2295 0.1705 0.2196 -0.0540 -0.0233 0.0203  31  VAL C CA  
4467 C C   . VAL C 31  ? 0.2545 0.1871 0.2353 -0.0635 -0.0256 0.0159  31  VAL C C   
4468 O O   . VAL C 31  ? 0.2706 0.2071 0.2464 -0.0688 -0.0290 0.0145  31  VAL C O   
4469 C CB  . VAL C 31  ? 0.2308 0.1799 0.2309 -0.0558 -0.0251 0.0276  31  VAL C CB  
4470 C CG1 . VAL C 31  ? 0.2447 0.2021 0.2526 -0.0470 -0.0220 0.0311  31  VAL C CG1 
4471 C CG2 . VAL C 31  ? 0.2413 0.2008 0.2457 -0.0626 -0.0309 0.0310  31  VAL C CG2 
4472 N N   . ASP C 32  ? 0.2457 0.1658 0.2230 -0.0664 -0.0242 0.0138  32  ASP C N   
4473 C CA  . ASP C 32  ? 0.2639 0.1758 0.2328 -0.0771 -0.0269 0.0101  32  ASP C CA  
4474 C C   . ASP C 32  ? 0.2964 0.2177 0.2715 -0.0854 -0.0328 0.0171  32  ASP C C   
4475 O O   . ASP C 32  ? 0.3064 0.2333 0.2916 -0.0838 -0.0327 0.0236  32  ASP C O   
4476 C CB  . ASP C 32  ? 0.2762 0.1697 0.2400 -0.0774 -0.0235 0.0055  32  ASP C CB  
4477 C CG  . ASP C 32  ? 0.3185 0.2015 0.2723 -0.0894 -0.0260 0.0005  32  ASP C CG  
4478 O OD1 . ASP C 32  ? 0.3301 0.2134 0.2743 -0.0941 -0.0269 -0.0054 32  ASP C OD1 
4479 O OD2 . ASP C 32  ? 0.3551 0.2293 0.3095 -0.0949 -0.0272 0.0023  32  ASP C OD2 
4480 N N   . ILE C 33  ? 0.2737 0.1980 0.2429 -0.0947 -0.0379 0.0160  33  ILE C N   
4481 C CA  . ILE C 33  ? 0.2622 0.1968 0.2376 -0.1025 -0.0441 0.0221  33  ILE C CA  
4482 C C   . ILE C 33  ? 0.2958 0.2198 0.2629 -0.1096 -0.0442 0.0177  33  ILE C C   
4483 O O   . ILE C 33  ? 0.3332 0.2502 0.2873 -0.1143 -0.0446 0.0110  33  ILE C O   
4484 C CB  . ILE C 33  ? 0.2620 0.2093 0.2367 -0.1047 -0.0497 0.0246  33  ILE C CB  
4485 C CG1 . ILE C 33  ? 0.2930 0.2485 0.2757 -0.0968 -0.0489 0.0281  33  ILE C CG1 
4486 C CG2 . ILE C 33  ? 0.3031 0.2622 0.2849 -0.1100 -0.0557 0.0307  33  ILE C CG2 
4487 C CD1 . ILE C 33  ? 0.3189 0.2817 0.2978 -0.0986 -0.0537 0.0294  33  ILE C CD1 
4488 N N   . ASP C 34  ? 0.3243 0.2465 0.2982 -0.1107 -0.0433 0.0211  34  ASP C N   
4489 C CA  . ASP C 34  ? 0.3401 0.2520 0.3071 -0.1179 -0.0438 0.0173  34  ASP C CA  
4490 C C   . ASP C 34  ? 0.3911 0.3169 0.3624 -0.1252 -0.0501 0.0221  34  ASP C C   
4491 O O   . ASP C 34  ? 0.3861 0.3261 0.3710 -0.1244 -0.0520 0.0299  34  ASP C O   
4492 C CB  . ASP C 34  ? 0.3529 0.2533 0.3236 -0.1160 -0.0396 0.0184  34  ASP C CB  
4493 C CG  . ASP C 34  ? 0.3695 0.2578 0.3332 -0.1236 -0.0402 0.0142  34  ASP C CG  
4494 O OD1 . ASP C 34  ? 0.4016 0.2997 0.3695 -0.1305 -0.0444 0.0182  34  ASP C OD1 
4495 O OD2 . ASP C 34  ? 0.4335 0.3035 0.3885 -0.1222 -0.0365 0.0069  34  ASP C OD2 
4496 N N   . THR C 35  ? 0.4499 0.3723 0.2590 -0.1597 -0.0475 0.0509  35  THR C N   
4497 C CA  . THR C 35  ? 0.4505 0.3803 0.2796 -0.1720 -0.0641 0.0552  35  THR C CA  
4498 C C   . THR C 35  ? 0.5189 0.4541 0.3692 -0.1811 -0.0634 0.0617  35  THR C C   
4499 O O   . THR C 35  ? 0.5643 0.5120 0.4395 -0.1902 -0.0765 0.0673  35  THR C O   
4500 C CB  . THR C 35  ? 0.4625 0.3714 0.2676 -0.1808 -0.0770 0.0522  35  THR C CB  
4501 O OG1 . THR C 35  ? 0.4709 0.3555 0.2505 -0.1860 -0.0720 0.0493  35  THR C OG1 
4502 C CG2 . THR C 35  ? 0.4505 0.3555 0.2456 -0.1685 -0.0724 0.0477  35  THR C CG2 
4503 N N   . HIS C 36  ? 0.4638 0.3891 0.3048 -0.1796 -0.0493 0.0616  36  HIS C N   
4504 C CA  . HIS C 36  ? 0.5207 0.4503 0.3819 -0.1885 -0.0472 0.0680  36  HIS C CA  
4505 C C   . HIS C 36  ? 0.4964 0.4552 0.3921 -0.1779 -0.0376 0.0740  36  HIS C C   
4506 O O   . HIS C 36  ? 0.5183 0.4890 0.4417 -0.1854 -0.0392 0.0811  36  HIS C O   
4507 C CB  . HIS C 36  ? 0.5814 0.4887 0.4196 -0.1875 -0.0352 0.0642  36  HIS C CB  
4508 C CG  . HIS C 36  ? 0.7287 0.6092 0.5308 -0.1888 -0.0392 0.0551  36  HIS C CG  
4509 N ND1 . HIS C 36  ? 0.7641 0.6286 0.5428 -0.1788 -0.0259 0.0490  36  HIS C ND1 
4510 C CD2 . HIS C 36  ? 0.7798 0.6488 0.5667 -0.1966 -0.0543 0.0511  36  HIS C CD2 
4511 C CE1 . HIS C 36  ? 0.8006 0.6438 0.5520 -0.1824 -0.0319 0.0413  36  HIS C CE1 
4512 N NE2 . HIS C 36  ? 0.7933 0.6379 0.5458 -0.1934 -0.0487 0.0430  36  HIS C NE2 
4513 N N   . THR C 37  ? 0.4207 0.3903 0.3144 -0.1610 -0.0269 0.0715  37  THR C N   
4514 C CA  . THR C 37  ? 0.3792 0.3732 0.3001 -0.1502 -0.0154 0.0761  37  THR C CA  
4515 C C   . THR C 37  ? 0.3504 0.3658 0.2934 -0.1428 -0.0210 0.0765  37  THR C C   
4516 O O   . THR C 37  ? 0.3808 0.4171 0.3529 -0.1372 -0.0137 0.0816  37  THR C O   
4517 C CB  . THR C 37  ? 0.4033 0.3940 0.3064 -0.1366 0.0031  0.0739  37  THR C CB  
4518 O OG1 . THR C 37  ? 0.4475 0.4291 0.3242 -0.1288 0.0024  0.0668  37  THR C OG1 
4519 C CG2 . THR C 37  ? 0.4386 0.4114 0.3282 -0.1428 0.0114  0.0762  37  THR C CG2 
4520 N N   . ALA C 38  ? 0.3574 0.3674 0.2873 -0.1422 -0.0322 0.0714  38  ALA C N   
4521 C CA  . ALA C 38  ? 0.3604 0.3889 0.3129 -0.1364 -0.0385 0.0726  38  ALA C CA  
4522 C C   . ALA C 38  ? 0.4104 0.4547 0.4002 -0.1459 -0.0482 0.0815  38  ALA C C   
4523 O O   . ALA C 38  ? 0.4946 0.5298 0.4837 -0.1611 -0.0597 0.0846  38  ALA C O   
4524 C CB  . ALA C 38  ? 0.3668 0.3837 0.2976 -0.1370 -0.0504 0.0667  38  ALA C CB  
4525 N N   . LYS C 39  ? 0.3320 0.3997 0.3550 -0.1371 -0.0427 0.0860  39  LYS C N   
4526 C CA  . LYS C 39  ? 0.3305 0.4175 0.3954 -0.1438 -0.0485 0.0962  39  LYS C CA  
4527 C C   . LYS C 39  ? 0.3217 0.4241 0.4122 -0.1406 -0.0597 0.0996  39  LYS C C   
4528 O O   . LYS C 39  ? 0.2848 0.3933 0.3761 -0.1267 -0.0521 0.0958  39  LYS C O   
4529 C CB  . LYS C 39  ? 0.3777 0.4809 0.4663 -0.1362 -0.0293 0.1009  39  LYS C CB  
4530 C CG  . LYS C 39  ? 0.4822 0.5747 0.5589 -0.1429 -0.0203 0.1022  39  LYS C CG  
4531 C CD  . LYS C 39  ? 0.5323 0.6431 0.6380 -0.1370 -0.0028 0.1091  39  LYS C CD  
4532 C CE  . LYS C 39  ? 0.5813 0.7161 0.7355 -0.1414 -0.0099 0.1191  39  LYS C CE  
4533 N NZ  . LYS C 39  ? 0.6060 0.7587 0.7914 -0.1374 0.0078  0.1271  39  LYS C NZ  
4534 N N   . TYR C 40  ? 0.3336 0.4435 0.4479 -0.1535 -0.0772 0.1079  40  TYR C N   
4535 C CA  . TYR C 40  ? 0.3142 0.4416 0.4597 -0.1504 -0.0878 0.1140  40  TYR C CA  
4536 C C   . TYR C 40  ? 0.2872 0.4377 0.4683 -0.1354 -0.0706 0.1180  40  TYR C C   
4537 O O   . TYR C 40  ? 0.2915 0.4527 0.4919 -0.1346 -0.0574 0.1225  40  TYR C O   
4538 C CB  . TYR C 40  ? 0.3167 0.4502 0.4844 -0.1670 -0.1086 0.1238  40  TYR C CB  
4539 C CG  . TYR C 40  ? 0.3027 0.4563 0.5089 -0.1606 -0.1164 0.1323  40  TYR C CG  
4540 C CD1 . TYR C 40  ? 0.3154 0.4650 0.5139 -0.1551 -0.1264 0.1304  40  TYR C CD1 
4541 C CD2 . TYR C 40  ? 0.3168 0.4922 0.5667 -0.1594 -0.1128 0.1424  40  TYR C CD2 
4542 C CE1 . TYR C 40  ? 0.3207 0.4874 0.5550 -0.1488 -0.1327 0.1392  40  TYR C CE1 
4543 C CE2 . TYR C 40  ? 0.3501 0.5430 0.6359 -0.1530 -0.1192 0.1510  40  TYR C CE2 
4544 C CZ  . TYR C 40  ? 0.3326 0.5212 0.6108 -0.1476 -0.1289 0.1496  40  TYR C CZ  
4545 O OH  . TYR C 40  ? 0.3772 0.5820 0.6915 -0.1408 -0.1345 0.1590  40  TYR C OH  
4546 N N   . ASP C 41  ? 0.2985 0.4548 0.4863 -0.1233 -0.0695 0.1160  41  ASP C N   
4547 C CA  . ASP C 41  ? 0.2958 0.4710 0.5148 -0.1082 -0.0526 0.1188  41  ASP C CA  
4548 C C   . ASP C 41  ? 0.3103 0.5040 0.5717 -0.1081 -0.0649 0.1292  41  ASP C C   
4549 O O   . ASP C 41  ? 0.2724 0.4618 0.5284 -0.1037 -0.0738 0.1270  41  ASP C O   
4550 C CB  . ASP C 41  ? 0.2818 0.4468 0.4730 -0.0931 -0.0385 0.1071  41  ASP C CB  
4551 C CG  . ASP C 41  ? 0.3208 0.5011 0.5381 -0.0778 -0.0188 0.1083  41  ASP C CG  
4552 O OD1 . ASP C 41  ? 0.3257 0.5263 0.5871 -0.0773 -0.0160 0.1189  41  ASP C OD1 
4553 O OD2 . ASP C 41  ? 0.3403 0.5116 0.5328 -0.0665 -0.0057 0.0984  41  ASP C OD2 
4554 N N   . PRO C 42  ? 0.2861 0.5013 0.5921 -0.1123 -0.0652 0.1415  42  PRO C N   
4555 C CA  . PRO C 42  ? 0.2583 0.4932 0.6085 -0.1120 -0.0779 0.1534  42  PRO C CA  
4556 C C   . PRO C 42  ? 0.2608 0.5034 0.6279 -0.0932 -0.0650 0.1520  42  PRO C C   
4557 O O   . PRO C 42  ? 0.2994 0.5549 0.6988 -0.0914 -0.0763 0.1612  42  PRO C O   
4558 C CB  . PRO C 42  ? 0.2775 0.5317 0.6680 -0.1178 -0.0754 0.1651  42  PRO C CB  
4559 C CG  . PRO C 42  ? 0.3009 0.5524 0.6789 -0.1160 -0.0534 0.1602  42  PRO C CG  
4560 C CD  . PRO C 42  ? 0.2883 0.5113 0.6075 -0.1166 -0.0529 0.1457  42  PRO C CD  
4561 N N   . SER C 43  ? 0.2493 0.4842 0.5965 -0.0796 -0.0421 0.1416  43  SER C N   
4562 C CA  . SER C 43  ? 0.2839 0.5220 0.6418 -0.0621 -0.0280 0.1383  43  SER C CA  
4563 C C   . SER C 43  ? 0.3022 0.5231 0.6307 -0.0589 -0.0384 0.1300  43  SER C C   
4564 O O   . SER C 43  ? 0.3290 0.5518 0.6697 -0.0460 -0.0308 0.1287  43  SER C O   
4565 C CB  . SER C 43  ? 0.2872 0.5216 0.6307 -0.0502 0.0002  0.1298  43  SER C CB  
4566 O OG  . SER C 43  ? 0.3112 0.5229 0.6013 -0.0492 0.0036  0.1156  43  SER C OG  
4567 N N   . LEU C 44  ? 0.2658 0.4689 0.5560 -0.0699 -0.0540 0.1244  44  LEU C N   
4568 C CA  . LEU C 44  ? 0.2666 0.4540 0.5307 -0.0679 -0.0644 0.1177  44  LEU C CA  
4569 C C   . LEU C 44  ? 0.2965 0.4946 0.5937 -0.0691 -0.0815 0.1290  44  LEU C C   
4570 O O   . LEU C 44  ? 0.2895 0.5000 0.6125 -0.0802 -0.0973 0.1411  44  LEU C O   
4571 C CB  . LEU C 44  ? 0.2682 0.4349 0.4864 -0.0802 -0.0769 0.1107  44  LEU C CB  
4572 C CG  . LEU C 44  ? 0.2628 0.4173 0.4457 -0.0775 -0.0603 0.0995  44  LEU C CG  
4573 C CD1 . LEU C 44  ? 0.2613 0.3976 0.4063 -0.0906 -0.0713 0.0952  44  LEU C CD1 
4574 C CD2 . LEU C 44  ? 0.2616 0.4069 0.4233 -0.0636 -0.0469 0.0884  44  LEU C CD2 
4575 N N   . LYS C 45  ? 0.2968 0.4899 0.5935 -0.0580 -0.0789 0.1256  45  LYS C N   
4576 C CA  . LYS C 45  ? 0.2659 0.4666 0.5904 -0.0583 -0.0956 0.1363  45  LYS C CA  
4577 C C   . LYS C 45  ? 0.2500 0.4323 0.5388 -0.0691 -0.1167 0.1333  45  LYS C C   
4578 O O   . LYS C 45  ? 0.2648 0.4277 0.5082 -0.0724 -0.1144 0.1212  45  LYS C O   
4579 C CB  . LYS C 45  ? 0.2738 0.4763 0.6163 -0.0406 -0.0810 0.1345  45  LYS C CB  
4580 C CG  . LYS C 45  ? 0.3378 0.5532 0.7065 -0.0282 -0.0553 0.1343  45  LYS C CG  
4581 C CD  . LYS C 45  ? 0.4095 0.6509 0.8287 -0.0319 -0.0577 0.1501  45  LYS C CD  
4582 C CE  . LYS C 45  ? 0.4755 0.7283 0.9164 -0.0204 -0.0298 0.1492  45  LYS C CE  
4583 N NZ  . LYS C 45  ? 0.5130 0.7935 1.0090 -0.0231 -0.0307 0.1660  45  LYS C NZ  
4584 N N   . PRO C 46  ? 0.2390 0.4265 0.5467 -0.0743 -0.1372 0.1446  46  PRO C N   
4585 C CA  . PRO C 46  ? 0.2696 0.4380 0.5413 -0.0843 -0.1566 0.1420  46  PRO C CA  
4586 C C   . PRO C 46  ? 0.2629 0.4110 0.4986 -0.0751 -0.1462 0.1280  46  PRO C C   
4587 O O   . PRO C 46  ? 0.2648 0.4154 0.5149 -0.0605 -0.1323 0.1254  46  PRO C O   
4588 C CB  . PRO C 46  ? 0.2694 0.4388 0.5619 -0.0836 -0.1686 0.1535  46  PRO C CB  
4589 C CG  . PRO C 46  ? 0.2756 0.4699 0.6178 -0.0809 -0.1634 0.1653  46  PRO C CG  
4590 C CD  . PRO C 46  ? 0.2812 0.4925 0.6449 -0.0705 -0.1430 0.1610  46  PRO C CD  
4591 N N   . LEU C 47  ? 0.2484 0.3761 0.4379 -0.0840 -0.1527 0.1192  47  LEU C N   
4592 C CA  . LEU C 47  ? 0.2623 0.3709 0.4165 -0.0775 -0.1450 0.1065  47  LEU C CA  
4593 C C   . LEU C 47  ? 0.2829 0.3837 0.4357 -0.0779 -0.1599 0.1112  47  LEU C C   
4594 O O   . LEU C 47  ? 0.3404 0.4324 0.4851 -0.0868 -0.1726 0.1168  47  LEU C O   
4595 C CB  . LEU C 47  ? 0.3060 0.3969 0.4138 -0.0861 -0.1442 0.0960  47  LEU C CB  
4596 C CG  . LEU C 47  ? 0.3132 0.3869 0.3871 -0.0794 -0.1351 0.0833  47  LEU C CG  
4597 C CD1 . LEU C 47  ? 0.3088 0.3877 0.3878 -0.0659 -0.1127 0.0752  47  LEU C CD1 
4598 C CD2 . LEU C 47  ? 0.3569 0.4132 0.3878 -0.0896 -0.1386 0.0761  47  LEU C CD2 
4599 N N   . SER C 48  ? 0.2573 0.3530 0.4111 -0.0652 -0.1493 0.1059  48  SER C N   
4600 C CA  A SER C 48  ? 0.2947 0.3817 0.4476 -0.0635 -0.1603 0.1098  48  SER C CA  
4601 C CA  B SER C 48  ? 0.2938 0.3807 0.4469 -0.0632 -0.1600 0.1097  48  SER C CA  
4602 C C   . SER C 48  ? 0.2915 0.3566 0.4013 -0.0625 -0.1546 0.0961  48  SER C C   
4603 O O   . SER C 48  ? 0.3035 0.3649 0.4056 -0.0527 -0.1366 0.0853  48  SER C O   
4604 C CB  A SER C 48  ? 0.2987 0.3980 0.4942 -0.0496 -0.1529 0.1166  48  SER C CB  
4605 C CB  B SER C 48  ? 0.3013 0.3993 0.4948 -0.0487 -0.1514 0.1153  48  SER C CB  
4606 O OG  A SER C 48  ? 0.3211 0.4095 0.5136 -0.0467 -0.1611 0.1193  48  SER C OG  
4607 O OG  B SER C 48  ? 0.3283 0.4473 0.5661 -0.0495 -0.1596 0.1308  48  SER C OG  
4608 N N   . VAL C 49  ? 0.3233 0.3727 0.4041 -0.0724 -0.1680 0.0963  49  VAL C N   
4609 C CA  . VAL C 49  ? 0.3528 0.3814 0.3949 -0.0720 -0.1625 0.0847  49  VAL C CA  
4610 C C   . VAL C 49  ? 0.3543 0.3739 0.4004 -0.0698 -0.1699 0.0898  49  VAL C C   
4611 O O   . VAL C 49  ? 0.4246 0.4348 0.4634 -0.0763 -0.1756 0.0943  49  VAL C O   
4612 C CB  . VAL C 49  ? 0.3886 0.3993 0.3924 -0.0801 -0.1557 0.0764  49  VAL C CB  
4613 C CG1 . VAL C 49  ? 0.4379 0.4302 0.4097 -0.0777 -0.1469 0.0654  49  VAL C CG1 
4614 C CG2 . VAL C 49  ? 0.3871 0.4058 0.3884 -0.0826 -0.1493 0.0730  49  VAL C CG2 
4615 N N   . SER C 50  ? 0.3472 0.3666 0.4031 -0.0598 -0.1662 0.0879  50  SER C N   
4616 C CA  . SER C 50  ? 0.3579 0.3719 0.4269 -0.0562 -0.1748 0.0958  50  SER C CA  
4617 C C   . SER C 50  ? 0.3462 0.3398 0.3814 -0.0562 -0.1708 0.0856  50  SER C C   
4618 O O   . SER C 50  ? 0.3698 0.3584 0.4040 -0.0469 -0.1559 0.0761  50  SER C O   
4619 C CB  . SER C 50  ? 0.4072 0.4325 0.5180 -0.0422 -0.1652 0.1004  50  SER C CB  
4620 O OG  . SER C 50  ? 0.4819 0.5281 0.6270 -0.0417 -0.1672 0.1102  50  SER C OG  
4621 N N   . TYR C 51  ? 0.3268 0.3600 0.3966 -0.0156 -0.1224 0.1266  51  TYR C N   
4622 C CA  . TYR C 51  ? 0.3384 0.3549 0.3877 -0.0163 -0.1190 0.1224  51  TYR C CA  
4623 C C   . TYR C 51  ? 0.3879 0.3984 0.4283 -0.0166 -0.1221 0.1283  51  TYR C C   
4624 O O   . TYR C 51  ? 0.4145 0.4115 0.4353 -0.0192 -0.1202 0.1254  51  TYR C O   
4625 C CB  . TYR C 51  ? 0.3565 0.3663 0.3834 -0.0257 -0.1201 0.1133  51  TYR C CB  
4626 C CG  . TYR C 51  ? 0.3038 0.3137 0.3332 -0.0253 -0.1115 0.1027  51  TYR C CG  
4627 C CD1 . TYR C 51  ? 0.3072 0.3218 0.3555 -0.0171 -0.1033 0.1012  51  TYR C CD1 
4628 C CD2 . TYR C 51  ? 0.2957 0.2998 0.3071 -0.0330 -0.1110 0.0942  51  TYR C CD2 
4629 C CE1 . TYR C 51  ? 0.2775 0.2918 0.3260 -0.0171 -0.0956 0.0919  51  TYR C CE1 
4630 C CE2 . TYR C 51  ? 0.2718 0.2757 0.2851 -0.0325 -0.1034 0.0854  51  TYR C CE2 
4631 C CZ  . TYR C 51  ? 0.2685 0.2778 0.2999 -0.0248 -0.0961 0.0844  51  TYR C CZ  
4632 O OH  . TYR C 51  ? 0.2700 0.2786 0.3010 -0.0248 -0.0891 0.0763  51  TYR C OH  
4633 N N   . ASP C 52  ? 0.3844 0.4050 0.4389 -0.0141 -0.1266 0.1369  52  ASP C N   
4634 C CA  . ASP C 52  ? 0.4261 0.4423 0.4725 -0.0146 -0.1306 0.1435  52  ASP C CA  
4635 C C   . ASP C 52  ? 0.4221 0.4244 0.4659 -0.0074 -0.1229 0.1444  52  ASP C C   
4636 O O   . ASP C 52  ? 0.4797 0.4730 0.5087 -0.0096 -0.1246 0.1471  52  ASP C O   
4637 C CB  . ASP C 52  ? 0.4551 0.4861 0.5208 -0.0120 -0.1364 0.1534  52  ASP C CB  
4638 C CG  . ASP C 52  ? 0.5356 0.5787 0.6007 -0.0214 -0.1455 0.1537  52  ASP C CG  
4639 O OD1 . ASP C 52  ? 0.5527 0.5912 0.6001 -0.0302 -0.1475 0.1460  52  ASP C OD1 
4640 O OD2 . ASP C 52  ? 0.5600 0.6169 0.6422 -0.0202 -0.1507 0.1619  52  ASP C OD2 
4641 N N   . GLN C 53  ? 0.3727 0.3720 0.4300 0.0009  -0.1142 0.1424  53  GLN C N   
4642 C CA  . GLN C 53  ? 0.3856 0.3704 0.4419 0.0076  -0.1065 0.1434  53  GLN C CA  
4643 C C   . GLN C 53  ? 0.3974 0.3691 0.4430 0.0066  -0.0993 0.1347  53  GLN C C   
4644 O O   . GLN C 53  ? 0.4221 0.3840 0.4731 0.0130  -0.0899 0.1320  53  GLN C O   
4645 C CB  . GLN C 53  ? 0.4154 0.4040 0.4960 0.0188  -0.1009 0.1488  53  GLN C CB  
4646 C CG  . GLN C 53  ? 0.4424 0.4428 0.5344 0.0206  -0.1075 0.1589  53  GLN C CG  
4647 C CD  . GLN C 53  ? 0.5240 0.5244 0.6374 0.0325  -0.1004 0.1646  53  GLN C CD  
4648 O OE1 . GLN C 53  ? 0.5473 0.5542 0.6784 0.0385  -0.0945 0.1631  53  GLN C OE1 
4649 N NE2 . GLN C 53  ? 0.5990 0.5908 0.7097 0.0361  -0.1001 0.1710  53  GLN C NE2 
4650 N N   . ALA C 54  ? 0.3768 0.3487 0.4067 -0.0017 -0.1007 0.1265  54  ALA C N   
4651 C CA  . ALA C 54  ? 0.3719 0.3350 0.3923 -0.0031 -0.0905 0.1137  54  ALA C CA  
4652 C C   . ALA C 54  ? 0.3810 0.3286 0.3861 -0.0047 -0.0860 0.1121  54  ALA C C   
4653 O O   . ALA C 54  ? 0.4010 0.3443 0.3931 -0.0090 -0.0916 0.1178  54  ALA C O   
4654 C CB  . ALA C 54  ? 0.3739 0.3418 0.3830 -0.0109 -0.0929 0.1061  54  ALA C CB  
4655 N N   . THR C 55  ? 0.3408 0.2797 0.3469 -0.0018 -0.0758 0.1047  55  THR C N   
4656 C CA  . THR C 55  ? 0.3248 0.2493 0.3190 -0.0036 -0.0709 0.1034  55  THR C CA  
4657 C C   . THR C 55  ? 0.3243 0.2463 0.3078 -0.0086 -0.0647 0.0916  55  THR C C   
4658 O O   . THR C 55  ? 0.3324 0.2529 0.3221 -0.0060 -0.0577 0.0846  55  THR C O   
4659 C CB  . THR C 55  ? 0.3693 0.2841 0.3743 0.0038  -0.0646 0.1059  55  THR C CB  
4660 O OG1 . THR C 55  ? 0.4182 0.3367 0.4354 0.0095  -0.0703 0.1179  55  THR C OG1 
4661 C CG2 . THR C 55  ? 0.3875 0.2868 0.3801 0.0007  -0.0597 0.1044  55  THR C CG2 
4662 N N   . SER C 56  ? 0.3015 0.2226 0.2686 -0.0158 -0.0669 0.0898  56  SER C N   
4663 C CA  . SER C 56  ? 0.2919 0.2107 0.2504 -0.0199 -0.0604 0.0800  56  SER C CA  
4664 C C   . SER C 56  ? 0.3005 0.2079 0.2545 -0.0208 -0.0540 0.0788  56  SER C C   
4665 O O   . SER C 56  ? 0.3407 0.2399 0.2919 -0.0203 -0.0552 0.0859  56  SER C O   
4666 C CB  . SER C 56  ? 0.2833 0.2043 0.2264 -0.0266 -0.0632 0.0782  56  SER C CB  
4667 O OG  . SER C 56  ? 0.3284 0.2418 0.2576 -0.0304 -0.0654 0.0839  56  SER C OG  
4668 N N   . LEU C 57  ? 0.3109 0.2179 0.2652 -0.0222 -0.0474 0.0702  57  LEU C N   
4669 C CA  . LEU C 57  ? 0.3156 0.2127 0.2670 -0.0241 -0.0416 0.0684  57  LEU C CA  
4670 C C   . LEU C 57  ? 0.3045 0.2022 0.2460 -0.0304 -0.0377 0.0635  57  LEU C C   
4671 O O   . LEU C 57  ? 0.3284 0.2184 0.2626 -0.0341 -0.0354 0.0660  57  LEU C O   
4672 C CB  . LEU C 57  ? 0.3808 0.2753 0.3425 -0.0205 -0.0367 0.0632  57  LEU C CB  
4673 C CG  . LEU C 57  ? 0.4179 0.3084 0.3902 -0.0134 -0.0378 0.0684  57  LEU C CG  
4674 C CD1 . LEU C 57  ? 0.4316 0.3199 0.4114 -0.0104 -0.0318 0.0610  57  LEU C CD1 
4675 C CD2 . LEU C 57  ? 0.4300 0.3081 0.3994 -0.0130 -0.0383 0.0765  57  LEU C CD2 
4676 N N   . ARG C 58  ? 0.2751 0.1816 0.2176 -0.0314 -0.0362 0.0570  58  ARG C N   
4677 C CA  . ARG C 58  ? 0.2974 0.2058 0.2349 -0.0361 -0.0313 0.0522  58  ARG C CA  
4678 C C   . ARG C 58  ? 0.2759 0.1940 0.2130 -0.0361 -0.0313 0.0477  58  ARG C C   
4679 O O   . ARG C 58  ? 0.2937 0.2172 0.2361 -0.0328 -0.0344 0.0468  58  ARG C O   
4680 C CB  . ARG C 58  ? 0.3584 0.2638 0.3017 -0.0372 -0.0267 0.0481  58  ARG C CB  
4681 C CG  . ARG C 58  ? 0.3973 0.3064 0.3498 -0.0335 -0.0264 0.0434  58  ARG C CG  
4682 C CD  . ARG C 58  ? 0.4459 0.3494 0.4008 -0.0362 -0.0224 0.0394  58  ARG C CD  
4683 N NE  . ARG C 58  ? 0.5077 0.3982 0.4603 -0.0372 -0.0216 0.0436  58  ARG C NE  
4684 C CZ  . ARG C 58  ? 0.5139 0.3950 0.4704 -0.0330 -0.0214 0.0453  58  ARG C CZ  
4685 N NH1 . ARG C 58  ? 0.4841 0.3525 0.4379 -0.0342 -0.0202 0.0497  58  ARG C NH1 
4686 N NH2 . ARG C 58  ? 0.4771 0.3612 0.4405 -0.0272 -0.0218 0.0429  58  ARG C NH2 
4687 N N   . ILE C 59  ? 0.2652 0.1854 0.1968 -0.0398 -0.0270 0.0453  59  ILE C N   
4688 C CA  . ILE C 59  ? 0.2776 0.2056 0.2088 -0.0397 -0.0254 0.0410  59  ILE C CA  
4689 C C   . ILE C 59  ? 0.2631 0.1964 0.1997 -0.0412 -0.0200 0.0371  59  ILE C C   
4690 O O   . ILE C 59  ? 0.2873 0.2180 0.2225 -0.0446 -0.0166 0.0383  59  ILE C O   
4691 C CB  . ILE C 59  ? 0.2618 0.1870 0.1798 -0.0422 -0.0255 0.0429  59  ILE C CB  
4692 C CG1 . ILE C 59  ? 0.2910 0.2219 0.2084 -0.0413 -0.0238 0.0383  59  ILE C CG1 
4693 C CG2 . ILE C 59  ? 0.2980 0.2179 0.2073 -0.0463 -0.0205 0.0452  59  ILE C CG2 
4694 C CD1 . ILE C 59  ? 0.3148 0.2405 0.2167 -0.0442 -0.0235 0.0390  59  ILE C CD1 
4695 N N   . LEU C 60  ? 0.2707 0.2118 0.2141 -0.0389 -0.0195 0.0331  60  LEU C N   
4696 C CA  . LEU C 60  ? 0.2692 0.2173 0.2197 -0.0400 -0.0161 0.0300  60  LEU C CA  
4697 C C   . LEU C 60  ? 0.2499 0.2057 0.2018 -0.0386 -0.0135 0.0280  60  LEU C C   
4698 O O   . LEU C 60  ? 0.2640 0.2212 0.2159 -0.0356 -0.0157 0.0268  60  LEU C O   
4699 C CB  . LEU C 60  ? 0.2735 0.2230 0.2316 -0.0383 -0.0182 0.0275  60  LEU C CB  
4700 C CG  . LEU C 60  ? 0.2514 0.2094 0.2162 -0.0394 -0.0164 0.0242  60  LEU C CG  
4701 C CD1 . LEU C 60  ? 0.2642 0.2219 0.2300 -0.0448 -0.0142 0.0247  60  LEU C CD1 
4702 C CD2 . LEU C 60  ? 0.2789 0.2366 0.2476 -0.0372 -0.0185 0.0213  60  LEU C CD2 
4703 N N   . ASN C 61  ? 0.2511 0.2123 0.2053 -0.0405 -0.0088 0.0279  61  ASN C N   
4704 C CA  . ASN C 61  ? 0.2105 0.1802 0.1694 -0.0381 -0.0058 0.0263  61  ASN C CA  
4705 C C   . ASN C 61  ? 0.2113 0.1895 0.1805 -0.0375 -0.0077 0.0246  61  ASN C C   
4706 O O   . ASN C 61  ? 0.2375 0.2195 0.2116 -0.0409 -0.0074 0.0250  61  ASN C O   
4707 C CB  . ASN C 61  ? 0.2438 0.2164 0.2023 -0.0399 0.0008  0.0281  61  ASN C CB  
4708 C CG  . ASN C 61  ? 0.2283 0.2099 0.1937 -0.0367 0.0050  0.0274  61  ASN C CG  
4709 O OD1 . ASN C 61  ? 0.2233 0.2113 0.1960 -0.0343 0.0026  0.0262  61  ASN C OD1 
4710 N ND2 . ASN C 61  ? 0.2524 0.2337 0.2150 -0.0363 0.0120  0.0286  61  ASN C ND2 
4711 N N   . ASN C 62  ? 0.2170 0.1974 0.1884 -0.0341 -0.0102 0.0229  62  ASN C N   
4712 C CA  . ASN C 62  ? 0.2220 0.2093 0.2005 -0.0337 -0.0121 0.0213  62  ASN C CA  
4713 C C   . ASN C 62  ? 0.1932 0.1916 0.1787 -0.0322 -0.0098 0.0220  62  ASN C C   
4714 O O   . ASN C 62  ? 0.2221 0.2270 0.2123 -0.0315 -0.0119 0.0212  62  ASN C O   
4715 C CB  . ASN C 62  ? 0.1996 0.1837 0.1775 -0.0309 -0.0156 0.0195  62  ASN C CB  
4716 C CG  . ASN C 62  ? 0.2254 0.2112 0.2034 -0.0272 -0.0154 0.0195  62  ASN C CG  
4717 O OD1 . ASN C 62  ? 0.2121 0.1989 0.1888 -0.0265 -0.0125 0.0204  62  ASN C OD1 
4718 N ND2 . ASN C 62  ? 0.2164 0.2016 0.1959 -0.0247 -0.0178 0.0185  62  ASN C ND2 
4719 N N   . GLY C 63  ? 0.2049 0.2055 0.1910 -0.0316 -0.0052 0.0239  63  GLY C N   
4720 C CA  . GLY C 63  ? 0.1875 0.1984 0.1817 -0.0290 -0.0022 0.0256  63  GLY C CA  
4721 C C   . GLY C 63  ? 0.2021 0.2115 0.1953 -0.0242 -0.0015 0.0249  63  GLY C C   
4722 O O   . GLY C 63  ? 0.2269 0.2439 0.2272 -0.0211 0.0013  0.0269  63  GLY C O   
4723 N N   . HIS C 64  ? 0.2002 0.2004 0.1860 -0.0235 -0.0040 0.0228  64  HIS C N   
4724 C CA  . HIS C 64  ? 0.1839 0.1815 0.1684 -0.0202 -0.0039 0.0220  64  HIS C CA  
4725 C C   . HIS C 64  ? 0.2328 0.2193 0.2071 -0.0210 -0.0032 0.0207  64  HIS C C   
4726 O O   . HIS C 64  ? 0.2448 0.2271 0.2158 -0.0193 0.0003  0.0202  64  HIS C O   
4727 C CB  . HIS C 64  ? 0.1841 0.1836 0.1709 -0.0193 -0.0086 0.0210  64  HIS C CB  
4728 C CG  . HIS C 64  ? 0.1768 0.1854 0.1699 -0.0199 -0.0104 0.0216  64  HIS C CG  
4729 N ND1 . HIS C 64  ? 0.1863 0.2045 0.1863 -0.0181 -0.0089 0.0239  64  HIS C ND1 
4730 C CD2 . HIS C 64  ? 0.2006 0.2097 0.1934 -0.0224 -0.0136 0.0202  64  HIS C CD2 
4731 C CE1 . HIS C 64  ? 0.2017 0.2265 0.2044 -0.0202 -0.0121 0.0239  64  HIS C CE1 
4732 N NE2 . HIS C 64  ? 0.1866 0.2050 0.1842 -0.0230 -0.0146 0.0211  64  HIS C NE2 
4733 N N   . THR C 65  ? 0.2081 0.1890 0.1766 -0.0238 -0.0064 0.0204  65  THR C N   
4734 C CA  . THR C 65  ? 0.2045 0.1754 0.1622 -0.0257 -0.0076 0.0200  65  THR C CA  
4735 C C   . THR C 65  ? 0.2127 0.1803 0.1667 -0.0287 -0.0095 0.0215  65  THR C C   
4736 O O   . THR C 65  ? 0.2350 0.2070 0.1940 -0.0297 -0.0081 0.0223  65  THR C O   
4737 C CB  . THR C 65  ? 0.2294 0.1981 0.1867 -0.0251 -0.0124 0.0193  65  THR C CB  
4738 O OG1 . THR C 65  ? 0.2547 0.2145 0.2008 -0.0279 -0.0143 0.0194  65  THR C OG1 
4739 C CG2 . THR C 65  ? 0.2260 0.1983 0.1898 -0.0244 -0.0171 0.0200  65  THR C CG2 
4740 N N   . PHE C 66  ? 0.2307 0.1902 0.1752 -0.0308 -0.0127 0.0224  66  PHE C N   
4741 C CA  . PHE C 66  ? 0.2258 0.1817 0.1679 -0.0329 -0.0154 0.0247  66  PHE C CA  
4742 C C   . PHE C 66  ? 0.2247 0.1792 0.1688 -0.0319 -0.0220 0.0259  66  PHE C C   
4743 O O   . PHE C 66  ? 0.2440 0.1974 0.1857 -0.0317 -0.0250 0.0258  66  PHE C O   
4744 C CB  . PHE C 66  ? 0.2621 0.2102 0.1916 -0.0362 -0.0131 0.0265  66  PHE C CB  
4745 C CG  . PHE C 66  ? 0.2639 0.2049 0.1810 -0.0378 -0.0153 0.0263  66  PHE C CG  
4746 C CD1 . PHE C 66  ? 0.2626 0.1995 0.1751 -0.0393 -0.0224 0.0291  66  PHE C CD1 
4747 C CD2 . PHE C 66  ? 0.2751 0.2129 0.1851 -0.0380 -0.0104 0.0235  66  PHE C CD2 
4748 C CE1 . PHE C 66  ? 0.2937 0.2246 0.1942 -0.0421 -0.0258 0.0291  66  PHE C CE1 
4749 C CE2 . PHE C 66  ? 0.2931 0.2227 0.1899 -0.0407 -0.0129 0.0225  66  PHE C CE2 
4750 C CZ  . PHE C 66  ? 0.3104 0.2369 0.2018 -0.0433 -0.0212 0.0255  66  PHE C CZ  
4751 N N   . ASN C 67  ? 0.2460 0.2007 0.1956 -0.0313 -0.0239 0.0272  67  ASN C N   
4752 C CA  . ASN C 67  ? 0.2347 0.1886 0.1888 -0.0293 -0.0288 0.0291  67  ASN C CA  
4753 C C   . ASN C 67  ? 0.2660 0.2128 0.2151 -0.0308 -0.0314 0.0333  67  ASN C C   
4754 O O   . ASN C 67  ? 0.2754 0.2186 0.2228 -0.0325 -0.0287 0.0339  67  ASN C O   
4755 C CB  . ASN C 67  ? 0.2305 0.1879 0.1943 -0.0267 -0.0278 0.0272  67  ASN C CB  
4756 C CG  . ASN C 67  ? 0.2405 0.2051 0.2092 -0.0251 -0.0259 0.0241  67  ASN C CG  
4757 O OD1 . ASN C 67  ? 0.2414 0.2085 0.2088 -0.0248 -0.0259 0.0235  67  ASN C OD1 
4758 N ND2 . ASN C 67  ? 0.2606 0.2280 0.2342 -0.0243 -0.0241 0.0219  67  ASN C ND2 
4759 N N   . VAL C 68  ? 0.2577 0.2029 0.2052 -0.0304 -0.0368 0.0369  68  VAL C N   
4760 C CA  . VAL C 68  ? 0.2604 0.1998 0.2053 -0.0307 -0.0402 0.0424  68  VAL C CA  
4761 C C   . VAL C 68  ? 0.2686 0.2097 0.2259 -0.0260 -0.0420 0.0442  68  VAL C C   
4762 O O   . VAL C 68  ? 0.2665 0.2135 0.2310 -0.0237 -0.0449 0.0447  68  VAL C O   
4763 C CB  . VAL C 68  ? 0.2814 0.2186 0.2165 -0.0335 -0.0458 0.0463  68  VAL C CB  
4764 C CG1 . VAL C 68  ? 0.3062 0.2392 0.2413 -0.0328 -0.0506 0.0535  68  VAL C CG1 
4765 C CG2 . VAL C 68  ? 0.2702 0.2028 0.1903 -0.0381 -0.0424 0.0443  68  VAL C CG2 
4766 N N   . GLU C 69  ? 0.2705 0.2062 0.2307 -0.0248 -0.0396 0.0450  69  GLU C N   
4767 C CA  . GLU C 69  ? 0.2924 0.2275 0.2634 -0.0200 -0.0387 0.0452  69  GLU C CA  
4768 C C   . GLU C 69  ? 0.2885 0.2191 0.2623 -0.0174 -0.0427 0.0528  69  GLU C C   
4769 O O   . GLU C 69  ? 0.3326 0.2570 0.2984 -0.0200 -0.0443 0.0571  69  GLU C O   
4770 C CB  . GLU C 69  ? 0.3849 0.3146 0.3560 -0.0208 -0.0332 0.0409  69  GLU C CB  
4771 C CG  . GLU C 69  ? 0.5277 0.4541 0.5071 -0.0163 -0.0305 0.0395  69  GLU C CG  
4772 C CD  . GLU C 69  ? 0.6502 0.5663 0.6266 -0.0185 -0.0262 0.0367  69  GLU C CD  
4773 O OE1 . GLU C 69  ? 0.6697 0.5833 0.6392 -0.0238 -0.0254 0.0361  69  GLU C OE1 
4774 O OE2 . GLU C 69  ? 0.6840 0.5938 0.6647 -0.0151 -0.0232 0.0351  69  GLU C OE2 
4775 N N   . PHE C 70  ? 0.2702 0.2042 0.2557 -0.0120 -0.0438 0.0551  70  PHE C N   
4776 C CA  . PHE C 70  ? 0.2746 0.2065 0.2671 -0.0079 -0.0473 0.0633  70  PHE C CA  
4777 C C   . PHE C 70  ? 0.3183 0.2435 0.3200 -0.0021 -0.0418 0.0628  70  PHE C C   
4778 O O   . PHE C 70  ? 0.3183 0.2436 0.3229 -0.0007 -0.0363 0.0561  70  PHE C O   
4779 C CB  . PHE C 70  ? 0.2639 0.2071 0.2649 -0.0061 -0.0535 0.0678  70  PHE C CB  
4780 C CG  . PHE C 70  ? 0.2770 0.2239 0.2674 -0.0122 -0.0598 0.0693  70  PHE C CG  
4781 C CD1 . PHE C 70  ? 0.2986 0.2482 0.2810 -0.0166 -0.0580 0.0623  70  PHE C CD1 
4782 C CD2 . PHE C 70  ? 0.3005 0.2469 0.2873 -0.0137 -0.0671 0.0777  70  PHE C CD2 
4783 C CE1 . PHE C 70  ? 0.2770 0.2272 0.2474 -0.0223 -0.0629 0.0630  70  PHE C CE1 
4784 C CE2 . PHE C 70  ? 0.2956 0.2435 0.2695 -0.0201 -0.0729 0.0786  70  PHE C CE2 
4785 C CZ  . PHE C 70  ? 0.3083 0.2571 0.2733 -0.0245 -0.0702 0.0706  70  PHE C CZ  
4786 N N   . ASP C 71  ? 0.3071 0.2259 0.3130 0.0015  -0.0431 0.0704  71  ASP C N   
4787 C CA  . ASP C 71  ? 0.3041 0.2156 0.3201 0.0083  -0.0374 0.0708  71  ASP C CA  
4788 C C   . ASP C 71  ? 0.3243 0.2470 0.3552 0.0143  -0.0376 0.0725  71  ASP C C   
4789 O O   . ASP C 71  ? 0.3412 0.2731 0.3802 0.0162  -0.0441 0.0806  71  ASP C O   
4790 C CB  . ASP C 71  ? 0.3223 0.2240 0.3394 0.0110  -0.0390 0.0798  71  ASP C CB  
4791 C CG  . ASP C 71  ? 0.3648 0.2555 0.3914 0.0184  -0.0317 0.0803  71  ASP C CG  
4792 O OD1 . ASP C 71  ? 0.3617 0.2574 0.3993 0.0240  -0.0280 0.0783  71  ASP C OD1 
4793 O OD2 . ASP C 71  ? 0.3873 0.2631 0.4103 0.0190  -0.0291 0.0833  71  ASP C OD2 
4794 N N   . ASP C 72  ? 0.2881 0.2112 0.3222 0.0164  -0.0310 0.0650  72  ASP C N   
4795 C CA  . ASP C 72  ? 0.2634 0.1972 0.3116 0.0219  -0.0296 0.0663  72  ASP C CA  
4796 C C   . ASP C 72  ? 0.2901 0.2160 0.3486 0.0303  -0.0215 0.0670  72  ASP C C   
4797 O O   . ASP C 72  ? 0.2822 0.2128 0.3485 0.0344  -0.0161 0.0640  72  ASP C O   
4798 C CB  . ASP C 72  ? 0.2618 0.2030 0.3057 0.0183  -0.0278 0.0580  72  ASP C CB  
4799 C CG  . ASP C 72  ? 0.2805 0.2115 0.3146 0.0165  -0.0203 0.0485  72  ASP C CG  
4800 O OD1 . ASP C 72  ? 0.3204 0.2376 0.3489 0.0164  -0.0170 0.0472  72  ASP C OD1 
4801 O OD2 . ASP C 72  ? 0.2904 0.2270 0.3221 0.0148  -0.0180 0.0425  72  ASP C OD2 
4802 N N   . SER C 73  ? 0.2976 0.2110 0.3565 0.0334  -0.0200 0.0715  73  SER C N   
4803 C CA  . SER C 73  ? 0.3038 0.2063 0.3712 0.0417  -0.0109 0.0718  73  SER C CA  
4804 C C   . SER C 73  ? 0.3344 0.2464 0.4228 0.0509  -0.0116 0.0822  73  SER C C   
4805 O O   . SER C 73  ? 0.3591 0.2639 0.4571 0.0593  -0.0025 0.0826  73  SER C O   
4806 C CB  . SER C 73  ? 0.3435 0.2261 0.4022 0.0410  -0.0079 0.0720  73  SER C CB  
4807 O OG  . SER C 73  ? 0.3576 0.2412 0.4202 0.0420  -0.0150 0.0832  73  SER C OG  
4808 N N   . GLN C 74  ? 0.2973 0.2249 0.3930 0.0495  -0.0218 0.0910  74  GLN C N   
4809 C CA  . GLN C 74  ? 0.2933 0.2323 0.4107 0.0574  -0.0244 0.1028  74  GLN C CA  
4810 C C   . GLN C 74  ? 0.2817 0.2422 0.4067 0.0538  -0.0329 0.1060  74  GLN C C   
4811 O O   . GLN C 74  ? 0.3024 0.2671 0.4140 0.0448  -0.0387 0.1009  74  GLN C O   
4812 C CB  . GLN C 74  ? 0.3141 0.2485 0.4345 0.0596  -0.0304 0.1144  74  GLN C CB  
4813 C CG  . GLN C 74  ? 0.3240 0.2363 0.4394 0.0639  -0.0216 0.1126  74  GLN C CG  
4814 C CD  . GLN C 74  ? 0.3960 0.3035 0.5154 0.0668  -0.0272 0.1254  74  GLN C CD  
4815 O OE1 . GLN C 74  ? 0.4146 0.3258 0.5239 0.0598  -0.0373 0.1297  74  GLN C OE1 
4816 N NE2 . GLN C 74  ? 0.4292 0.3297 0.5610 0.0766  -0.0202 0.1301  74  GLN C NE2 
4817 N N   . ASP C 75  ? 0.3189 0.2925 0.4665 0.0611  -0.0328 0.1145  75  ASP C N   
4818 C CA  . ASP C 75  ? 0.3463 0.3413 0.5049 0.0579  -0.0405 0.1186  75  ASP C CA  
4819 C C   . ASP C 75  ? 0.3949 0.3984 0.5520 0.0522  -0.0551 0.1283  75  ASP C C   
4820 O O   . ASP C 75  ? 0.4466 0.4647 0.6194 0.0540  -0.0609 0.1377  75  ASP C O   
4821 C CB  . ASP C 75  ? 0.3714 0.3787 0.5565 0.0674  -0.0350 0.1252  75  ASP C CB  
4822 C CG  . ASP C 75  ? 0.4062 0.4100 0.5914 0.0707  -0.0219 0.1151  75  ASP C CG  
4823 O OD1 . ASP C 75  ? 0.3767 0.3711 0.5422 0.0647  -0.0188 0.1034  75  ASP C OD1 
4824 O OD2 . ASP C 75  ? 0.4248 0.4363 0.6307 0.0794  -0.0146 0.1196  75  ASP C OD2 
4825 N N   . LYS C 76  ? 0.3662 0.3598 0.5009 0.0442  -0.0598 0.1238  76  LYS C N   
4826 C CA  . LYS C 76  ? 0.3763 0.3754 0.5052 0.0381  -0.0729 0.1322  76  LYS C CA  
4827 C C   . LYS C 76  ? 0.3812 0.3884 0.4980 0.0275  -0.0800 0.1266  76  LYS C C   
4828 O O   . LYS C 76  ? 0.4054 0.4288 0.5337 0.0253  -0.0875 0.1322  76  LYS C O   
4829 C CB  . LYS C 76  ? 0.4065 0.3886 0.5198 0.0370  -0.0730 0.1333  76  LYS C CB  
4830 C CG  . LYS C 76  ? 0.4387 0.4149 0.5655 0.0472  -0.0676 0.1407  76  LYS C CG  
4831 C CD  . LYS C 76  ? 0.4480 0.4065 0.5603 0.0464  -0.0671 0.1427  76  LYS C CD  
4832 C CE  . LYS C 76  ? 0.4508 0.4063 0.5768 0.0559  -0.0625 0.1499  76  LYS C CE  
4833 N NZ  . LYS C 76  ? 0.4747 0.4094 0.5890 0.0571  -0.0582 0.1504  76  LYS C NZ  
4834 N N   . ALA C 77  ? 0.3135 0.3101 0.4090 0.0211  -0.0769 0.1157  77  ALA C N   
4835 C CA  . ALA C 77  ? 0.3055 0.3078 0.3894 0.0118  -0.0822 0.1102  77  ALA C CA  
4836 C C   . ALA C 77  ? 0.3022 0.3120 0.3961 0.0136  -0.0760 0.1040  77  ALA C C   
4837 O O   . ALA C 77  ? 0.2824 0.2843 0.3708 0.0153  -0.0665 0.0949  77  ALA C O   
4838 C CB  . ALA C 77  ? 0.3426 0.3317 0.4023 0.0054  -0.0803 0.1020  77  ALA C CB  
4839 N N   . VAL C 78  ? 0.2892 0.3147 0.3978 0.0128  -0.0816 0.1093  78  VAL C N   
4840 C CA  . VAL C 78  ? 0.2913 0.3251 0.4127 0.0154  -0.0753 0.1056  78  VAL C CA  
4841 C C   . VAL C 78  ? 0.2784 0.3245 0.4015 0.0076  -0.0832 0.1064  78  VAL C C   
4842 O O   . VAL C 78  ? 0.2868 0.3389 0.4083 0.0018  -0.0945 0.1127  78  VAL C O   
4843 C CB  . VAL C 78  ? 0.2594 0.3009 0.4055 0.0257  -0.0701 0.1129  78  VAL C CB  
4844 C CG1 . VAL C 78  ? 0.2807 0.3073 0.4246 0.0335  -0.0615 0.1117  78  VAL C CG1 
4845 C CG2 . VAL C 78  ? 0.2926 0.3490 0.4556 0.0259  -0.0804 0.1258  78  VAL C CG2 
4846 N N   . LEU C 79  ? 0.2614 0.3116 0.3891 0.0078  -0.0769 0.1005  79  LEU C N   
4847 C CA  . LEU C 79  ? 0.2494 0.3116 0.3833 0.0016  -0.0819 0.1013  79  LEU C CA  
4848 C C   . LEU C 79  ? 0.2579 0.3334 0.4172 0.0084  -0.0765 0.1062  79  LEU C C   
4849 O O   . LEU C 79  ? 0.2896 0.3604 0.4527 0.0160  -0.0650 0.1022  79  LEU C O   
4850 C CB  . LEU C 79  ? 0.2753 0.3287 0.3911 -0.0038 -0.0778 0.0902  79  LEU C CB  
4851 C CG  . LEU C 79  ? 0.3221 0.3813 0.4360 -0.0119 -0.0821 0.0881  79  LEU C CG  
4852 C CD1 . LEU C 79  ? 0.3680 0.4283 0.4740 -0.0201 -0.0947 0.0926  79  LEU C CD1 
4853 C CD2 . LEU C 79  ? 0.2497 0.2973 0.3457 -0.0142 -0.0755 0.0775  79  LEU C CD2 
4854 N N   . LYS C 80  ? 0.2465 0.3387 0.4232 0.0055  -0.0844 0.1148  80  LYS C N   
4855 C CA  . LYS C 80  ? 0.2589 0.3664 0.4625 0.0115  -0.0796 0.1209  80  LYS C CA  
4856 C C   . LYS C 80  ? 0.2476 0.3692 0.4589 0.0022  -0.0876 0.1238  80  LYS C C   
4857 O O   . LYS C 80  ? 0.2711 0.3898 0.4674 -0.0081 -0.0977 0.1223  80  LYS C O   
4858 C CB  . LYS C 80  ? 0.3147 0.4284 0.5357 0.0193  -0.0791 0.1306  80  LYS C CB  
4859 C CG  . LYS C 80  ? 0.3402 0.4400 0.5575 0.0294  -0.0712 0.1296  80  LYS C CG  
4860 C CD  . LYS C 80  ? 0.3543 0.4584 0.5880 0.0373  -0.0679 0.1376  80  LYS C CD  
4861 C CE  . LYS C 80  ? 0.4388 0.5499 0.6715 0.0306  -0.0804 0.1448  80  LYS C CE  
4862 N NZ  . LYS C 80  ? 0.5054 0.6185 0.7516 0.0386  -0.0782 0.1532  80  LYS C NZ  
4863 N N   . GLY C 81  ? 0.2213 0.3553 0.4528 0.0052  -0.0812 0.1266  81  GLY C N   
4864 C CA  . GLY C 81  ? 0.2209 0.3662 0.4589 -0.0041 -0.0869 0.1288  81  GLY C CA  
4865 C C   . GLY C 81  ? 0.2292 0.3699 0.4549 -0.0116 -0.0876 0.1211  81  GLY C C   
4866 O O   . GLY C 81  ? 0.2212 0.3494 0.4333 -0.0083 -0.0783 0.1122  81  GLY C O   
4867 N N   . GLY C 82  ? 0.2296 0.3749 0.4529 -0.0228 -0.0957 0.1217  82  GLY C N   
4868 C CA  . GLY C 82  ? 0.2280 0.3692 0.4419 -0.0305 -0.0957 0.1151  82  GLY C CA  
4869 C C   . GLY C 82  ? 0.2271 0.3714 0.4520 -0.0240 -0.0823 0.1128  82  GLY C C   
4870 O O   . GLY C 82  ? 0.2445 0.4036 0.4931 -0.0197 -0.0783 0.1198  82  GLY C O   
4871 N N   . PRO C 83  ? 0.2208 0.3498 0.4263 -0.0232 -0.0740 0.1026  83  PRO C N   
4872 C CA  . PRO C 83  ? 0.2154 0.3450 0.4267 -0.0172 -0.0607 0.0998  83  PRO C CA  
4873 C C   . PRO C 83  ? 0.2560 0.3823 0.4702 -0.0049 -0.0501 0.0990  83  PRO C C   
4874 O O   . PRO C 83  ? 0.2889 0.4144 0.5053 0.0002  -0.0386 0.0962  83  PRO C O   
4875 C CB  . PRO C 83  ? 0.2018 0.3154 0.3889 -0.0220 -0.0582 0.0898  83  PRO C CB  
4876 C CG  . PRO C 83  ? 0.2011 0.3019 0.3681 -0.0237 -0.0643 0.0856  83  PRO C CG  
4877 C CD  . PRO C 83  ? 0.2209 0.3319 0.3983 -0.0282 -0.0767 0.0939  83  PRO C CD  
4878 N N   . LEU C 84  ? 0.2254 0.3480 0.4374 -0.0006 -0.0534 0.1009  84  LEU C N   
4879 C CA  . LEU C 84  ? 0.2030 0.3169 0.4116 0.0097  -0.0435 0.0979  84  LEU C CA  
4880 C C   . LEU C 84  ? 0.1878 0.3140 0.4220 0.0189  -0.0375 0.1062  84  LEU C C   
4881 O O   . LEU C 84  ? 0.2081 0.3481 0.4613 0.0186  -0.0451 0.1161  84  LEU C O   
4882 C CB  . LEU C 84  ? 0.1932 0.2954 0.3866 0.0097  -0.0493 0.0961  84  LEU C CB  
4883 C CG  . LEU C 84  ? 0.2144 0.3052 0.3836 0.0008  -0.0552 0.0888  84  LEU C CG  
4884 C CD1 . LEU C 84  ? 0.2348 0.3158 0.3910 0.0006  -0.0612 0.0887  84  LEU C CD1 
4885 C CD2 . LEU C 84  ? 0.2036 0.2836 0.3576 0.0016  -0.0457 0.0791  84  LEU C CD2 
4886 N N   . ASP C 85  ? 0.2438 0.3638 0.4772 0.0273  -0.0240 0.1021  85  ASP C N   
4887 C CA  . ASP C 85  ? 0.2516 0.3769 0.5042 0.0382  -0.0156 0.1080  85  ASP C CA  
4888 C C   . ASP C 85  ? 0.2469 0.3562 0.4870 0.0440  -0.0132 0.1045  85  ASP C C   
4889 O O   . ASP C 85  ? 0.2675 0.3605 0.4845 0.0429  -0.0092 0.0946  85  ASP C O   
4890 C CB  . ASP C 85  ? 0.2743 0.4010 0.5322 0.0435  -0.0009 0.1053  85  ASP C CB  
4891 C CG  . ASP C 85  ? 0.3637 0.5070 0.6365 0.0379  -0.0025 0.1100  85  ASP C CG  
4892 O OD1 . ASP C 85  ? 0.3861 0.5465 0.6812 0.0358  -0.0103 0.1202  85  ASP C OD1 
4893 O OD2 . ASP C 85  ? 0.3907 0.5298 0.6525 0.0348  0.0032  0.1041  85  ASP C OD2 
4894 N N   . GLY C 86  ? 0.2658 0.3798 0.5211 0.0497  -0.0161 0.1130  86  GLY C N   
4895 C CA  . GLY C 86  ? 0.2679 0.3655 0.5120 0.0553  -0.0132 0.1103  86  GLY C CA  
4896 C C   . GLY C 86  ? 0.2943 0.3846 0.5217 0.0481  -0.0259 0.1094  86  GLY C C   
4897 O O   . GLY C 86  ? 0.2851 0.3845 0.5130 0.0398  -0.0382 0.1132  86  GLY C O   
4898 N N   . THR C 87  ? 0.2372 0.3094 0.4479 0.0507  -0.0223 0.1036  87  THR C N   
4899 C CA  . THR C 87  ? 0.2149 0.2789 0.4115 0.0459  -0.0321 0.1041  87  THR C CA  
4900 C C   . THR C 87  ? 0.2313 0.2794 0.4011 0.0407  -0.0298 0.0921  87  THR C C   
4901 O O   . THR C 87  ? 0.2548 0.2920 0.4170 0.0447  -0.0191 0.0847  87  THR C O   
4902 C CB  . THR C 87  ? 0.2397 0.2973 0.4439 0.0543  -0.0302 0.1103  87  THR C CB  
4903 O OG1 . THR C 87  ? 0.2731 0.3481 0.5048 0.0593  -0.0334 0.1231  87  THR C OG1 
4904 C CG2 . THR C 87  ? 0.2662 0.3131 0.4532 0.0492  -0.0392 0.1105  87  THR C CG2 
4905 N N   . TYR C 88  ? 0.2284 0.2751 0.3838 0.0317  -0.0395 0.0901  88  TYR C N   
4906 C CA  . TYR C 88  ? 0.2038 0.2373 0.3357 0.0267  -0.0375 0.0798  88  TYR C CA  
4907 C C   . TYR C 88  ? 0.2341 0.2578 0.3525 0.0236  -0.0438 0.0804  88  TYR C C   
4908 O O   . TYR C 88  ? 0.2376 0.2664 0.3554 0.0187  -0.0539 0.0858  88  TYR C O   
4909 C CB  . TYR C 88  ? 0.2000 0.2389 0.3250 0.0190  -0.0409 0.0757  88  TYR C CB  
4910 C CG  . TYR C 88  ? 0.1748 0.2203 0.3080 0.0211  -0.0333 0.0733  88  TYR C CG  
4911 C CD1 . TYR C 88  ? 0.1829 0.2425 0.3382 0.0247  -0.0324 0.0807  88  TYR C CD1 
4912 C CD2 . TYR C 88  ? 0.1747 0.2135 0.2940 0.0192  -0.0276 0.0646  88  TYR C CD2 
4913 C CE1 . TYR C 88  ? 0.1876 0.2534 0.3498 0.0261  -0.0249 0.0788  88  TYR C CE1 
4914 C CE2 . TYR C 88  ? 0.1696 0.2139 0.2948 0.0209  -0.0207 0.0630  88  TYR C CE2 
4915 C CZ  . TYR C 88  ? 0.2142 0.2715 0.3602 0.0242  -0.0190 0.0699  88  TYR C CZ  
4916 O OH  . TYR C 88  ? 0.2193 0.2822 0.3707 0.0254  -0.0115 0.0686  88  TYR C OH  
4917 N N   . ARG C 89  ? 0.2365 0.2457 0.3435 0.0258  -0.0377 0.0750  89  ARG C N   
4918 C CA  . ARG C 89  ? 0.2398 0.2386 0.3348 0.0234  -0.0419 0.0759  89  ARG C CA  
4919 C C   . ARG C 89  ? 0.2239 0.2179 0.2995 0.0151  -0.0451 0.0694  89  ARG C C   
4920 O O   . ARG C 89  ? 0.2262 0.2172 0.2939 0.0134  -0.0398 0.0614  89  ARG C O   
4921 C CB  . ARG C 89  ? 0.2352 0.2197 0.3270 0.0289  -0.0336 0.0731  89  ARG C CB  
4922 C CG  . ARG C 89  ? 0.2825 0.2678 0.3921 0.0380  -0.0303 0.0810  89  ARG C CG  
4923 C CD  . ARG C 89  ? 0.2598 0.2267 0.3622 0.0419  -0.0223 0.0772  89  ARG C CD  
4924 N NE  . ARG C 89  ? 0.2870 0.2524 0.4064 0.0522  -0.0154 0.0827  89  ARG C NE  
4925 C CZ  . ARG C 89  ? 0.2792 0.2286 0.3958 0.0575  -0.0052 0.0786  89  ARG C CZ  
4926 N NH1 . ARG C 89  ? 0.2968 0.2309 0.3943 0.0526  -0.0018 0.0693  89  ARG C NH1 
4927 N NH2 . ARG C 89  ? 0.3510 0.3001 0.4847 0.0675  0.0018  0.0840  89  ARG C NH2 
4928 N N   . LEU C 90  ? 0.2252 0.2183 0.2930 0.0101  -0.0533 0.0732  90  LEU C N   
4929 C CA  . LEU C 90  ? 0.2225 0.2093 0.2715 0.0030  -0.0551 0.0675  90  LEU C CA  
4930 C C   . LEU C 90  ? 0.2374 0.2117 0.2764 0.0038  -0.0485 0.0619  90  LEU C C   
4931 O O   . LEU C 90  ? 0.2584 0.2250 0.2982 0.0068  -0.0474 0.0653  90  LEU C O   
4932 C CB  . LEU C 90  ? 0.2459 0.2328 0.2880 -0.0018 -0.0646 0.0737  90  LEU C CB  
4933 C CG  . LEU C 90  ? 0.2508 0.2300 0.2726 -0.0088 -0.0652 0.0683  90  LEU C CG  
4934 C CD1 . LEU C 90  ? 0.2459 0.2291 0.2631 -0.0131 -0.0645 0.0621  90  LEU C CD1 
4935 C CD2 . LEU C 90  ? 0.2862 0.2629 0.2990 -0.0130 -0.0734 0.0747  90  LEU C CD2 
4936 N N   . ILE C 91  ? 0.2177 0.1898 0.2478 0.0009  -0.0442 0.0539  91  ILE C N   
4937 C CA  . ILE C 91  ? 0.2361 0.1979 0.2563 -0.0002 -0.0392 0.0487  91  ILE C CA  
4938 C C   . ILE C 91  ? 0.2524 0.2113 0.2587 -0.0066 -0.0415 0.0466  91  ILE C C   
4939 O O   . ILE C 91  ? 0.2443 0.1948 0.2431 -0.0084 -0.0401 0.0462  91  ILE C O   
4940 C CB  . ILE C 91  ? 0.2308 0.1922 0.2522 0.0017  -0.0320 0.0419  91  ILE C CB  
4941 C CG1 . ILE C 91  ? 0.2451 0.1967 0.2561 -0.0010 -0.0283 0.0369  91  ILE C CG1 
4942 C CG2 . ILE C 91  ? 0.2428 0.2129 0.2637 -0.0004 -0.0320 0.0384  91  ILE C CG2 
4943 C CD1 . ILE C 91  ? 0.2613 0.2100 0.2721 0.0007  -0.0218 0.0308  91  ILE C CD1 
4944 N N   . GLN C 92  ? 0.2325 0.1971 0.2349 -0.0102 -0.0442 0.0453  92  GLN C N   
4945 C CA  . GLN C 92  ? 0.2283 0.1894 0.2175 -0.0156 -0.0445 0.0427  92  GLN C CA  
4946 C C   . GLN C 92  ? 0.2359 0.2019 0.2218 -0.0189 -0.0482 0.0426  92  GLN C C   
4947 O O   . GLN C 92  ? 0.2467 0.2195 0.2409 -0.0175 -0.0496 0.0430  92  GLN C O   
4948 C CB  . GLN C 92  ? 0.2327 0.1922 0.2181 -0.0164 -0.0384 0.0364  92  GLN C CB  
4949 C CG  . GLN C 92  ? 0.2364 0.2027 0.2276 -0.0146 -0.0356 0.0325  92  GLN C CG  
4950 C CD  . GLN C 92  ? 0.2241 0.1932 0.2094 -0.0176 -0.0345 0.0294  92  GLN C CD  
4951 O OE1 . GLN C 92  ? 0.2437 0.2122 0.2236 -0.0203 -0.0373 0.0306  92  GLN C OE1 
4952 N NE2 . GLN C 92  ? 0.2578 0.2295 0.2437 -0.0172 -0.0304 0.0255  92  GLN C NE2 
4953 N N   . PHE C 93  ? 0.2323 0.1937 0.2052 -0.0235 -0.0491 0.0418  93  PHE C N   
4954 C CA  . PHE C 93  ? 0.2228 0.1857 0.1898 -0.0270 -0.0500 0.0392  93  PHE C CA  
4955 C C   . PHE C 93  ? 0.2502 0.2089 0.2074 -0.0290 -0.0443 0.0345  93  PHE C C   
4956 O O   . PHE C 93  ? 0.2421 0.1968 0.1951 -0.0293 -0.0413 0.0344  93  PHE C O   
4957 C CB  . PHE C 93  ? 0.2573 0.2189 0.2173 -0.0313 -0.0575 0.0433  93  PHE C CB  
4958 C CG  . PHE C 93  ? 0.2554 0.2090 0.2009 -0.0349 -0.0589 0.0453  93  PHE C CG  
4959 C CD1 . PHE C 93  ? 0.2604 0.2073 0.1912 -0.0385 -0.0546 0.0411  93  PHE C CD1 
4960 C CD2 . PHE C 93  ? 0.2704 0.2230 0.2168 -0.0344 -0.0642 0.0520  93  PHE C CD2 
4961 C CE1 . PHE C 93  ? 0.2799 0.2193 0.1963 -0.0420 -0.0551 0.0432  93  PHE C CE1 
4962 C CE2 . PHE C 93  ? 0.2965 0.2415 0.2283 -0.0380 -0.0656 0.0547  93  PHE C CE2 
4963 C CZ  . PHE C 93  ? 0.2969 0.2352 0.2132 -0.0420 -0.0609 0.0501  93  PHE C CZ  
4964 N N   . HIS C 94  ? 0.2346 0.1942 0.1891 -0.0304 -0.0426 0.0312  94  HIS C N   
4965 C CA  . HIS C 94  ? 0.2411 0.1976 0.1883 -0.0313 -0.0365 0.0274  94  HIS C CA  
4966 C C   . HIS C 94  ? 0.2397 0.1937 0.1810 -0.0338 -0.0367 0.0251  94  HIS C C   
4967 O O   . HIS C 94  ? 0.2482 0.2040 0.1923 -0.0351 -0.0417 0.0264  94  HIS C O   
4968 C CB  . HIS C 94  ? 0.2101 0.1722 0.1664 -0.0278 -0.0314 0.0249  94  HIS C CB  
4969 C CG  . HIS C 94  ? 0.1884 0.1565 0.1540 -0.0253 -0.0319 0.0241  94  HIS C CG  
4970 N ND1 . HIS C 94  ? 0.2108 0.1831 0.1858 -0.0228 -0.0344 0.0259  94  HIS C ND1 
4971 C CD2 . HIS C 94  ? 0.2069 0.1766 0.1736 -0.0250 -0.0298 0.0223  94  HIS C CD2 
4972 C CE1 . HIS C 94  ? 0.2103 0.1874 0.1917 -0.0213 -0.0337 0.0251  94  HIS C CE1 
4973 N NE2 . HIS C 94  ? 0.1981 0.1736 0.1746 -0.0228 -0.0314 0.0231  94  HIS C NE2 
4974 N N   . PHE C 95  ? 0.2406 0.1904 0.1749 -0.0343 -0.0306 0.0220  95  PHE C N   
4975 C CA  . PHE C 95  ? 0.2431 0.1873 0.1697 -0.0366 -0.0290 0.0191  95  PHE C CA  
4976 C C   . PHE C 95  ? 0.2630 0.2097 0.1957 -0.0328 -0.0219 0.0166  95  PHE C C   
4977 O O   . PHE C 95  ? 0.2573 0.2097 0.1971 -0.0295 -0.0180 0.0170  95  PHE C O   
4978 C CB  . PHE C 95  ? 0.2618 0.1949 0.1702 -0.0409 -0.0272 0.0178  95  PHE C CB  
4979 C CG  . PHE C 95  ? 0.2712 0.2010 0.1708 -0.0452 -0.0346 0.0209  95  PHE C CG  
4980 C CD1 . PHE C 95  ? 0.2764 0.2083 0.1776 -0.0443 -0.0359 0.0246  95  PHE C CD1 
4981 C CD2 . PHE C 95  ? 0.2933 0.2178 0.1830 -0.0507 -0.0407 0.0208  95  PHE C CD2 
4982 C CE1 . PHE C 95  ? 0.2934 0.2220 0.1862 -0.0479 -0.0428 0.0286  95  PHE C CE1 
4983 C CE2 . PHE C 95  ? 0.3161 0.2386 0.1975 -0.0550 -0.0487 0.0249  95  PHE C CE2 
4984 C CZ  . PHE C 95  ? 0.3318 0.2566 0.2151 -0.0531 -0.0495 0.0292  95  PHE C CZ  
4985 N N   . HIS C 96  ? 0.2470 0.1890 0.1764 -0.0339 -0.0205 0.0144  96  HIS C N   
4986 C CA  . HIS C 96  ? 0.2437 0.1847 0.1758 -0.0306 -0.0131 0.0125  96  HIS C CA  
4987 C C   . HIS C 96  ? 0.2603 0.1878 0.1772 -0.0337 -0.0089 0.0091  96  HIS C C   
4988 O O   . HIS C 96  ? 0.2745 0.1945 0.1812 -0.0390 -0.0136 0.0079  96  HIS C O   
4989 C CB  . HIS C 96  ? 0.2453 0.1916 0.1883 -0.0288 -0.0147 0.0131  96  HIS C CB  
4990 C CG  . HIS C 96  ? 0.2278 0.1856 0.1834 -0.0262 -0.0183 0.0157  96  HIS C CG  
4991 N ND1 . HIS C 96  ? 0.2408 0.2066 0.2056 -0.0217 -0.0149 0.0167  96  HIS C ND1 
4992 C CD2 . HIS C 96  ? 0.2188 0.1811 0.1788 -0.0273 -0.0245 0.0177  96  HIS C CD2 
4993 C CE1 . HIS C 96  ? 0.2166 0.1895 0.1889 -0.0207 -0.0186 0.0182  96  HIS C CE1 
4994 N NE2 . HIS C 96  ? 0.2264 0.1974 0.1968 -0.0235 -0.0238 0.0190  96  HIS C NE2 
4995 N N   . TRP C 97  ? 0.2533 0.1773 0.1681 -0.0305 0.0001  0.0078  97  TRP C N   
4996 C CA  . TRP C 97  ? 0.2613 0.1703 0.1600 -0.0329 0.0060  0.0040  97  TRP C CA  
4997 C C   . TRP C 97  ? 0.3025 0.2095 0.2058 -0.0272 0.0166  0.0033  97  TRP C C   
4998 O O   . TRP C 97  ? 0.2783 0.1971 0.1974 -0.0218 0.0185  0.0064  97  TRP C O   
4999 C CB  . TRP C 97  ? 0.2858 0.1890 0.1705 -0.0362 0.0069  0.0036  97  TRP C CB  
5000 C CG  . TRP C 97  ? 0.2861 0.1979 0.1786 -0.0322 0.0119  0.0063  97  TRP C CG  
5001 C CD1 . TRP C 97  ? 0.2891 0.1992 0.1815 -0.0287 0.0223  0.0059  97  TRP C CD1 
5002 C CD2 . TRP C 97  ? 0.2557 0.1788 0.1576 -0.0319 0.0066  0.0099  97  TRP C CD2 
5003 N NE1 . TRP C 97  ? 0.2810 0.2023 0.1831 -0.0268 0.0234  0.0093  97  TRP C NE1 
5004 C CE2 . TRP C 97  ? 0.2810 0.2091 0.1879 -0.0291 0.0138  0.0115  97  TRP C CE2 
5005 C CE3 . TRP C 97  ? 0.2423 0.1715 0.1496 -0.0336 -0.0029 0.0122  97  TRP C CE3 
5006 C CZ2 . TRP C 97  ? 0.2711 0.2089 0.1867 -0.0290 0.0111  0.0147  97  TRP C CZ2 
5007 C CZ3 . TRP C 97  ? 0.2595 0.1969 0.1748 -0.0326 -0.0045 0.0151  97  TRP C CZ3 
5008 C CH2 . TRP C 97  ? 0.2689 0.2097 0.1871 -0.0309 0.0022  0.0161  97  TRP C CH2 
5009 N N   . GLY C 98  ? 0.3013 0.1930 0.1906 -0.0284 0.0237  -0.0006 98  GLY C N   
5010 C CA  . GLY C 98  ? 0.3064 0.1938 0.2000 -0.0225 0.0345  -0.0012 98  GLY C CA  
5011 C C   . GLY C 98  ? 0.3255 0.2097 0.2147 -0.0193 0.0452  -0.0014 98  GLY C C   
5012 O O   . GLY C 98  ? 0.3279 0.2121 0.2088 -0.0223 0.0446  -0.0014 98  GLY C O   
5013 N N   . SER C 99  ? 0.3308 0.2126 0.2268 -0.0127 0.0557  -0.0008 99  SER C N   
5014 C CA  . SER C 99  ? 0.3526 0.2295 0.2447 -0.0089 0.0681  -0.0012 99  SER C CA  
5015 C C   . SER C 99  ? 0.3759 0.2290 0.2432 -0.0129 0.0751  -0.0079 99  SER C C   
5016 O O   . SER C 99  ? 0.4079 0.2550 0.2681 -0.0107 0.0860  -0.0089 99  SER C O   
5017 C CB  . SER C 99  ? 0.3513 0.2363 0.2625 0.0005  0.0769  0.0032  99  SER C CB  
5018 O OG  . SER C 99  ? 0.3892 0.2665 0.3024 0.0025  0.0774  0.0023  99  SER C OG  
5019 N N   . HIS C 100 ? 0.3915 0.2313 0.2452 -0.0190 0.0694  -0.0124 100 HIS C N   
5020 C CA  . HIS C 100 ? 0.4082 0.2244 0.2349 -0.0251 0.0735  -0.0195 100 HIS C CA  
5021 C C   . HIS C 100 ? 0.4120 0.2243 0.2292 -0.0344 0.0597  -0.0218 100 HIS C C   
5022 O O   . HIS C 100 ? 0.4243 0.2507 0.2575 -0.0343 0.0500  -0.0180 100 HIS C O   
5023 C CB  . HIS C 100 ? 0.4326 0.2314 0.2550 -0.0201 0.0875  -0.0231 100 HIS C CB  
5024 C CG  . HIS C 100 ? 0.4354 0.2348 0.2707 -0.0176 0.0851  -0.0219 100 HIS C CG  
5025 N ND1 . HIS C 100 ? 0.4736 0.2588 0.2966 -0.0250 0.0792  -0.0265 100 HIS C ND1 
5026 C CD2 . HIS C 100 ? 0.4424 0.2555 0.3017 -0.0090 0.0873  -0.0160 100 HIS C CD2 
5027 C CE1 . HIS C 100 ? 0.4697 0.2591 0.3087 -0.0208 0.0787  -0.0236 100 HIS C CE1 
5028 N NE2 . HIS C 100 ? 0.4334 0.2395 0.2940 -0.0109 0.0835  -0.0170 100 HIS C NE2 
5029 N N   . ASP C 101 ? 0.4281 0.2213 0.2190 -0.0428 0.0591  -0.0278 101 ASP C N   
5030 C CA  . ASP C 101 ? 0.4501 0.2421 0.2322 -0.0528 0.0445  -0.0289 101 ASP C CA  
5031 C C   . ASP C 101 ? 0.4489 0.2387 0.2389 -0.0544 0.0400  -0.0297 101 ASP C C   
5032 O O   . ASP C 101 ? 0.4582 0.2519 0.2474 -0.0619 0.0272  -0.0290 101 ASP C O   
5033 C CB  . ASP C 101 ? 0.5012 0.2728 0.2517 -0.0622 0.0444  -0.0350 101 ASP C CB  
5034 C CG  . ASP C 101 ? 0.4902 0.2649 0.2302 -0.0633 0.0451  -0.0331 101 ASP C CG  
5035 O OD1 . ASP C 101 ? 0.5104 0.3039 0.2684 -0.0577 0.0438  -0.0270 101 ASP C OD1 
5036 O OD2 . ASP C 101 ? 0.5538 0.3105 0.2654 -0.0706 0.0467  -0.0382 101 ASP C OD2 
5037 N N   . GLY C 102 ? 0.4390 0.2221 0.2366 -0.0480 0.0503  -0.0308 102 GLY C N   
5038 C CA  . GLY C 102 ? 0.4378 0.2163 0.2411 -0.0500 0.0471  -0.0316 102 GLY C CA  
5039 C C   . GLY C 102 ? 0.4324 0.2327 0.2623 -0.0455 0.0401  -0.0247 102 GLY C C   
5040 O O   . GLY C 102 ? 0.4546 0.2528 0.2908 -0.0473 0.0372  -0.0244 102 GLY C O   
5041 N N   . GLN C 103 ? 0.3867 0.2074 0.2317 -0.0402 0.0375  -0.0192 103 GLN C N   
5042 C CA  . GLN C 103 ? 0.3635 0.2043 0.2308 -0.0368 0.0302  -0.0132 103 GLN C CA  
5043 C C   . GLN C 103 ? 0.3609 0.2181 0.2337 -0.0368 0.0234  -0.0097 103 GLN C C   
5044 O O   . GLN C 103 ? 0.3579 0.2115 0.2195 -0.0381 0.0256  -0.0111 103 GLN C O   
5045 C CB  . GLN C 103 ? 0.3594 0.2067 0.2444 -0.0269 0.0383  -0.0093 103 GLN C CB  
5046 C CG  . GLN C 103 ? 0.3786 0.2317 0.2689 -0.0191 0.0475  -0.0072 103 GLN C CG  
5047 C CD  . GLN C 103 ? 0.3722 0.2289 0.2778 -0.0098 0.0561  -0.0032 103 GLN C CD  
5048 O OE1 . GLN C 103 ? 0.4060 0.2519 0.3114 -0.0090 0.0594  -0.0040 103 GLN C OE1 
5049 N NE2 . GLN C 103 ? 0.3394 0.2115 0.2591 -0.0030 0.0593  0.0018  103 GLN C NE2 
5050 N N   . GLY C 104 ? 0.3393 0.2136 0.2292 -0.0350 0.0160  -0.0050 104 GLY C N   
5051 C CA  . GLY C 104 ? 0.2930 0.1814 0.1888 -0.0348 0.0098  -0.0017 104 GLY C CA  
5052 C C   . GLY C 104 ? 0.2875 0.1874 0.1936 -0.0372 -0.0006 0.0012  104 GLY C C   
5053 O O   . GLY C 104 ? 0.2934 0.2074 0.2119 -0.0337 -0.0034 0.0049  104 GLY C O   
5054 N N   . SER C 105 ? 0.2914 0.1852 0.1923 -0.0436 -0.0063 -0.0002 105 SER C N   
5055 C CA  . SER C 105 ? 0.2796 0.1859 0.1928 -0.0452 -0.0154 0.0034  105 SER C CA  
5056 C C   . SER C 105 ? 0.2659 0.1821 0.1963 -0.0393 -0.0128 0.0064  105 SER C C   
5057 O O   . SER C 105 ? 0.2709 0.1826 0.2030 -0.0353 -0.0053 0.0057  105 SER C O   
5058 C CB  . SER C 105 ? 0.2837 0.1835 0.1896 -0.0540 -0.0227 0.0021  105 SER C CB  
5059 O OG  . SER C 105 ? 0.3084 0.1980 0.2123 -0.0561 -0.0190 -0.0004 105 SER C OG  
5060 N N   . GLU C 106 ? 0.2529 0.1825 0.1957 -0.0385 -0.0188 0.0100  106 GLU C N   
5061 C CA  . GLU C 106 ? 0.2163 0.1560 0.1739 -0.0336 -0.0171 0.0130  106 GLU C CA  
5062 C C   . GLU C 106 ? 0.2430 0.1816 0.2050 -0.0376 -0.0199 0.0139  106 GLU C C   
5063 O O   . GLU C 106 ? 0.2504 0.1845 0.2144 -0.0363 -0.0151 0.0139  106 GLU C O   
5064 C CB  . GLU C 106 ? 0.2453 0.1986 0.2127 -0.0302 -0.0202 0.0160  106 GLU C CB  
5065 C CG  . GLU C 106 ? 0.2427 0.1971 0.2068 -0.0268 -0.0170 0.0153  106 GLU C CG  
5066 C CD  . GLU C 106 ? 0.2275 0.1937 0.2020 -0.0223 -0.0169 0.0177  106 GLU C CD  
5067 O OE1 . GLU C 106 ? 0.2201 0.1921 0.1998 -0.0229 -0.0216 0.0192  106 GLU C OE1 
5068 O OE2 . GLU C 106 ? 0.2428 0.2118 0.2200 -0.0184 -0.0122 0.0181  106 GLU C OE2 
5069 N N   . HIS C 107 ? 0.2473 0.1896 0.2109 -0.0429 -0.0276 0.0151  107 HIS C N   
5070 C CA  . HIS C 107 ? 0.2644 0.2046 0.2310 -0.0487 -0.0308 0.0157  107 HIS C CA  
5071 C C   . HIS C 107 ? 0.2748 0.1973 0.2258 -0.0546 -0.0290 0.0111  107 HIS C C   
5072 O O   . HIS C 107 ? 0.2806 0.1935 0.2173 -0.0559 -0.0276 0.0075  107 HIS C O   
5073 C CB  . HIS C 107 ? 0.2367 0.1869 0.2103 -0.0531 -0.0400 0.0191  107 HIS C CB  
5074 C CG  . HIS C 107 ? 0.2319 0.1974 0.2214 -0.0470 -0.0401 0.0234  107 HIS C CG  
5075 N ND1 . HIS C 107 ? 0.2348 0.2058 0.2252 -0.0424 -0.0403 0.0242  107 HIS C ND1 
5076 C CD2 . HIS C 107 ? 0.2308 0.2055 0.2343 -0.0445 -0.0383 0.0266  107 HIS C CD2 
5077 C CE1 . HIS C 107 ? 0.2342 0.2163 0.2379 -0.0375 -0.0391 0.0273  107 HIS C CE1 
5078 N NE2 . HIS C 107 ? 0.2254 0.2105 0.2371 -0.0385 -0.0377 0.0289  107 HIS C NE2 
5079 N N   . THR C 108 ? 0.2597 0.1768 0.2129 -0.0584 -0.0282 0.0109  108 THR C N   
5080 C CA  . THR C 108 ? 0.2850 0.1836 0.2230 -0.0659 -0.0274 0.0061  108 THR C CA  
5081 C C   . THR C 108 ? 0.3040 0.2047 0.2456 -0.0756 -0.0358 0.0075  108 THR C C   
5082 O O   . THR C 108 ? 0.2880 0.2039 0.2465 -0.0747 -0.0394 0.0126  108 THR C O   
5083 C CB  . THR C 108 ? 0.2831 0.1690 0.2187 -0.0619 -0.0171 0.0042  108 THR C CB  
5084 O OG1 . THR C 108 ? 0.2980 0.1929 0.2496 -0.0588 -0.0156 0.0088  108 THR C OG1 
5085 C CG2 . THR C 108 ? 0.3174 0.2016 0.2501 -0.0528 -0.0088 0.0033  108 THR C CG2 
5086 N N   . VAL C 109 ? 0.2886 0.1739 0.2141 -0.0853 -0.0388 0.0029  109 VAL C N   
5087 C CA  . VAL C 109 ? 0.3029 0.1888 0.2302 -0.0967 -0.0477 0.0039  109 VAL C CA  
5088 C C   . VAL C 109 ? 0.3560 0.2211 0.2721 -0.1023 -0.0423 -0.0011 109 VAL C C   
5089 O O   . VAL C 109 ? 0.3767 0.2219 0.2719 -0.1052 -0.0385 -0.0077 109 VAL C O   
5090 C CB  . VAL C 109 ? 0.3361 0.2241 0.2535 -0.1051 -0.0588 0.0037  109 VAL C CB  
5091 C CG1 . VAL C 109 ? 0.3707 0.2622 0.2929 -0.1175 -0.0690 0.0058  109 VAL C CG1 
5092 C CG2 . VAL C 109 ? 0.3448 0.2524 0.2746 -0.0981 -0.0627 0.0093  109 VAL C CG2 
5093 N N   . ASP C 110 ? 0.3305 0.1988 0.2601 -0.1035 -0.0412 0.0019  110 ASP C N   
5094 C CA  . ASP C 110 ? 0.3414 0.1890 0.2625 -0.1080 -0.0349 -0.0021 110 ASP C CA  
5095 C C   . ASP C 110 ? 0.3795 0.2109 0.2886 -0.0993 -0.0227 -0.0065 110 ASP C C   
5096 O O   . ASP C 110 ? 0.4435 0.2513 0.3345 -0.1035 -0.0176 -0.0129 110 ASP C O   
5097 C CB  . ASP C 110 ? 0.3999 0.2336 0.3058 -0.1236 -0.0427 -0.0067 110 ASP C CB  
5098 C CG  . ASP C 110 ? 0.4718 0.3238 0.3933 -0.1323 -0.0548 -0.0010 110 ASP C CG  
5099 O OD1 . ASP C 110 ? 0.4037 0.2732 0.3480 -0.1275 -0.0541 0.0059  110 ASP C OD1 
5100 O OD2 . ASP C 110 ? 0.5089 0.3577 0.4198 -0.1445 -0.0649 -0.0031 110 ASP C OD2 
5101 N N   . LYS C 111 ? 0.3552 0.1994 0.2749 -0.0869 -0.0178 -0.0028 111 LYS C N   
5102 C CA  . LYS C 111 ? 0.3709 0.2069 0.2864 -0.0764 -0.0065 -0.0042 111 LYS C CA  
5103 C C   . LYS C 111 ? 0.4215 0.2478 0.3193 -0.0760 -0.0044 -0.0096 111 LYS C C   
5104 O O   . LYS C 111 ? 0.4679 0.2898 0.3635 -0.0670 0.0050  -0.0104 111 LYS C O   
5105 C CB  . LYS C 111 ? 0.4141 0.2314 0.3267 -0.0755 0.0030  -0.0057 111 LYS C CB  
5106 C CG  . LYS C 111 ? 0.4952 0.3204 0.4245 -0.0759 0.0021  0.0001  111 LYS C CG  
5107 C CD  . LYS C 111 ? 0.5688 0.4174 0.5164 -0.0658 0.0022  0.0073  111 LYS C CD  
5108 C CE  . LYS C 111 ? 0.6206 0.4669 0.5672 -0.0539 0.0116  0.0078  111 LYS C CE  
5109 N NZ  . LYS C 111 ? 0.5548 0.4219 0.5162 -0.0449 0.0115  0.0140  111 LYS C NZ  
5110 N N   . LYS C 112 ? 0.3967 0.2218 0.2830 -0.0849 -0.0129 -0.0124 112 LYS C N   
5111 C CA  . LYS C 112 ? 0.4392 0.2540 0.3063 -0.0855 -0.0109 -0.0174 112 LYS C CA  
5112 C C   . LYS C 112 ? 0.3923 0.2255 0.2676 -0.0781 -0.0128 -0.0135 112 LYS C C   
5113 O O   . LYS C 112 ? 0.3621 0.2143 0.2514 -0.0781 -0.0212 -0.0083 112 LYS C O   
5114 C CB  . LYS C 112 ? 0.5127 0.3179 0.3619 -0.0993 -0.0202 -0.0216 112 LYS C CB  
5115 C CG  . LYS C 112 ? 0.6406 0.4371 0.4688 -0.1007 -0.0194 -0.0260 112 LYS C CG  
5116 C CD  . LYS C 112 ? 0.7225 0.5185 0.5375 -0.1141 -0.0329 -0.0270 112 LYS C CD  
5117 C CE  . LYS C 112 ? 0.7354 0.5414 0.5456 -0.1119 -0.0372 -0.0247 112 LYS C CE  
5118 N NZ  . LYS C 112 ? 0.7669 0.5565 0.5578 -0.1077 -0.0258 -0.0303 112 LYS C NZ  
5119 N N   . LYS C 113 ? 0.3596 0.1862 0.2259 -0.0720 -0.0045 -0.0160 113 LYS C N   
5120 C CA  . LYS C 113 ? 0.3584 0.1995 0.2297 -0.0662 -0.0057 -0.0130 113 LYS C CA  
5121 C C   . LYS C 113 ? 0.3705 0.2049 0.2225 -0.0724 -0.0098 -0.0162 113 LYS C C   
5122 O O   . LYS C 113 ? 0.4450 0.2597 0.2759 -0.0789 -0.0073 -0.0222 113 LYS C O   
5123 C CB  . LYS C 113 ? 0.3520 0.1935 0.2290 -0.0551 0.0060  -0.0122 113 LYS C CB  
5124 C CG  . LYS C 113 ? 0.3698 0.2231 0.2671 -0.0480 0.0082  -0.0072 113 LYS C CG  
5125 C CD  . LYS C 113 ? 0.4170 0.2730 0.3208 -0.0375 0.0184  -0.0053 113 LYS C CD  
5126 C CE  . LYS C 113 ? 0.3950 0.2664 0.3190 -0.0310 0.0181  0.0008  113 LYS C CE  
5127 N NZ  . LYS C 113 ? 0.4053 0.2878 0.3392 -0.0215 0.0238  0.0045  113 LYS C NZ  
5128 N N   . TYR C 114 ? 0.3535 0.2037 0.2122 -0.0708 -0.0162 -0.0120 114 TYR C N   
5129 C CA  . TYR C 114 ? 0.4088 0.2546 0.2508 -0.0748 -0.0192 -0.0135 114 TYR C CA  
5130 C C   . TYR C 114 ? 0.3722 0.2201 0.2147 -0.0663 -0.0101 -0.0131 114 TYR C C   
5131 O O   . TYR C 114 ? 0.3478 0.2045 0.2062 -0.0577 -0.0041 -0.0106 114 TYR C O   
5132 C CB  . TYR C 114 ? 0.3951 0.2560 0.2441 -0.0789 -0.0323 -0.0083 114 TYR C CB  
5133 C CG  . TYR C 114 ? 0.4031 0.2631 0.2510 -0.0887 -0.0424 -0.0080 114 TYR C CG  
5134 C CD1 . TYR C 114 ? 0.3951 0.2662 0.2628 -0.0878 -0.0455 -0.0045 114 TYR C CD1 
5135 C CD2 . TYR C 114 ? 0.4720 0.3206 0.2987 -0.0996 -0.0492 -0.0108 114 TYR C CD2 
5136 C CE1 . TYR C 114 ? 0.4458 0.3178 0.3145 -0.0974 -0.0549 -0.0036 114 TYR C CE1 
5137 C CE2 . TYR C 114 ? 0.4812 0.3303 0.3078 -0.1098 -0.0595 -0.0101 114 TYR C CE2 
5138 C CZ  . TYR C 114 ? 0.4788 0.3402 0.3277 -0.1084 -0.0621 -0.0063 114 TYR C CZ  
5139 O OH  . TYR C 114 ? 0.5384 0.4023 0.3896 -0.1190 -0.0725 -0.0048 114 TYR C OH  
5140 N N   . ALA C 115 ? 0.3763 0.2175 0.2016 -0.0693 -0.0099 -0.0148 115 ALA C N   
5141 C CA  . ALA C 115 ? 0.3594 0.2024 0.1847 -0.0623 -0.0010 -0.0142 115 ALA C CA  
5142 C C   . ALA C 115 ? 0.3564 0.2197 0.2011 -0.0567 -0.0048 -0.0080 115 ALA C C   
5143 O O   . ALA C 115 ? 0.3503 0.2192 0.2028 -0.0496 0.0027  -0.0066 115 ALA C O   
5144 C CB  . ALA C 115 ? 0.4136 0.2436 0.2139 -0.0680 0.0002  -0.0173 115 ALA C CB  
5145 N N   . ALA C 116 ? 0.3311 0.2057 0.1845 -0.0595 -0.0161 -0.0041 116 ALA C N   
5146 C CA  . ALA C 116 ? 0.3273 0.2188 0.1981 -0.0539 -0.0187 0.0011  116 ALA C CA  
5147 C C   . ALA C 116 ? 0.3176 0.2197 0.2003 -0.0563 -0.0293 0.0048  116 ALA C C   
5148 O O   . ALA C 116 ? 0.3158 0.2131 0.1928 -0.0629 -0.0353 0.0039  116 ALA C O   
5149 C CB  . ALA C 116 ? 0.3254 0.2172 0.1883 -0.0539 -0.0182 0.0027  116 ALA C CB  
5150 N N   . GLU C 117 ? 0.2967 0.2129 0.1960 -0.0511 -0.0312 0.0090  117 GLU C N   
5151 C CA  . GLU C 117 ? 0.2776 0.2049 0.1901 -0.0518 -0.0396 0.0131  117 GLU C CA  
5152 C C   . GLU C 117 ? 0.2662 0.2027 0.1864 -0.0481 -0.0419 0.0171  117 GLU C C   
5153 O O   . GLU C 117 ? 0.2716 0.2108 0.1959 -0.0430 -0.0361 0.0168  117 GLU C O   
5154 C CB  . GLU C 117 ? 0.2622 0.1959 0.1896 -0.0484 -0.0373 0.0133  117 GLU C CB  
5155 C CG  . GLU C 117 ? 0.2636 0.2085 0.2051 -0.0493 -0.0447 0.0176  117 GLU C CG  
5156 C CD  . GLU C 117 ? 0.2723 0.2214 0.2255 -0.0470 -0.0416 0.0177  117 GLU C CD  
5157 O OE1 . GLU C 117 ? 0.2637 0.2040 0.2112 -0.0481 -0.0367 0.0144  117 GLU C OE1 
5158 O OE2 . GLU C 117 ? 0.2520 0.2127 0.2201 -0.0440 -0.0434 0.0212  117 GLU C OE2 
5159 N N   . LEU C 118 ? 0.2528 0.1937 0.1749 -0.0511 -0.0507 0.0212  118 LEU C N   
5160 C CA  . LEU C 118 ? 0.2503 0.1984 0.1799 -0.0479 -0.0537 0.0257  118 LEU C CA  
5161 C C   . LEU C 118 ? 0.2376 0.1975 0.1867 -0.0438 -0.0557 0.0289  118 LEU C C   
5162 O O   . LEU C 118 ? 0.2527 0.2170 0.2086 -0.0462 -0.0601 0.0304  118 LEU C O   
5163 C CB  . LEU C 118 ? 0.2617 0.2070 0.1814 -0.0534 -0.0621 0.0294  118 LEU C CB  
5164 C CG  . LEU C 118 ? 0.2645 0.2173 0.1939 -0.0504 -0.0671 0.0358  118 LEU C CG  
5165 C CD1 . LEU C 118 ? 0.2694 0.2204 0.1987 -0.0456 -0.0609 0.0356  118 LEU C CD1 
5166 C CD2 . LEU C 118 ? 0.2829 0.2329 0.2012 -0.0567 -0.0764 0.0402  118 LEU C CD2 
5167 N N   . HIS C 119 ? 0.2361 0.2009 0.1941 -0.0379 -0.0521 0.0298  119 HIS C N   
5168 C CA  . HIS C 119 ? 0.2184 0.1929 0.1933 -0.0334 -0.0524 0.0324  119 HIS C CA  
5169 C C   . HIS C 119 ? 0.2289 0.2055 0.2084 -0.0307 -0.0550 0.0366  119 HIS C C   
5170 O O   . HIS C 119 ? 0.2308 0.2036 0.2062 -0.0288 -0.0514 0.0355  119 HIS C O   
5171 C CB  . HIS C 119 ? 0.2199 0.1969 0.2003 -0.0287 -0.0450 0.0292  119 HIS C CB  
5172 C CG  . HIS C 119 ? 0.2085 0.1844 0.1879 -0.0301 -0.0423 0.0264  119 HIS C CG  
5173 N ND1 . HIS C 119 ? 0.2053 0.1816 0.1858 -0.0270 -0.0360 0.0238  119 HIS C ND1 
5174 C CD2 . HIS C 119 ? 0.2096 0.1837 0.1872 -0.0345 -0.0455 0.0265  119 HIS C CD2 
5175 C CE1 . HIS C 119 ? 0.2362 0.2101 0.2155 -0.0288 -0.0347 0.0225  119 HIS C CE1 
5176 N NE2 . HIS C 119 ? 0.2312 0.2030 0.2083 -0.0337 -0.0402 0.0236  119 HIS C NE2 
5177 N N   . LEU C 120 ? 0.2347 0.2177 0.2240 -0.0305 -0.0608 0.0418  120 LEU C N   
5178 C CA  . LEU C 120 ? 0.2198 0.2054 0.2173 -0.0264 -0.0626 0.0468  120 LEU C CA  
5179 C C   . LEU C 120 ? 0.2318 0.2241 0.2448 -0.0204 -0.0578 0.0467  120 LEU C C   
5180 O O   . LEU C 120 ? 0.2095 0.2096 0.2331 -0.0201 -0.0589 0.0483  120 LEU C O   
5181 C CB  . LEU C 120 ? 0.2442 0.2335 0.2440 -0.0295 -0.0719 0.0536  120 LEU C CB  
5182 C CG  . LEU C 120 ? 0.2567 0.2377 0.2380 -0.0357 -0.0764 0.0537  120 LEU C CG  
5183 C CD1 . LEU C 120 ? 0.3127 0.2965 0.2903 -0.0431 -0.0848 0.0556  120 LEU C CD1 
5184 C CD2 . LEU C 120 ? 0.2799 0.2576 0.2581 -0.0343 -0.0792 0.0592  120 LEU C CD2 
5185 N N   . VAL C 121 ? 0.2366 0.2255 0.2501 -0.0160 -0.0522 0.0446  121 VAL C N   
5186 C CA  . VAL C 121 ? 0.2157 0.2079 0.2385 -0.0110 -0.0461 0.0425  121 VAL C CA  
5187 C C   . VAL C 121 ? 0.2219 0.2158 0.2561 -0.0057 -0.0457 0.0471  121 VAL C C   
5188 O O   . VAL C 121 ? 0.2262 0.2139 0.2573 -0.0047 -0.0464 0.0490  121 VAL C O   
5189 C CB  . VAL C 121 ? 0.2004 0.1869 0.2147 -0.0107 -0.0402 0.0368  121 VAL C CB  
5190 C CG1 . VAL C 121 ? 0.2042 0.1932 0.2250 -0.0064 -0.0342 0.0341  121 VAL C CG1 
5191 C CG2 . VAL C 121 ? 0.2348 0.2198 0.2392 -0.0149 -0.0399 0.0332  121 VAL C CG2 
5192 N N   . HIS C 122 ? 0.1997 0.2012 0.2474 -0.0020 -0.0436 0.0490  122 HIS C N   
5193 C CA  . HIS C 122 ? 0.2035 0.2073 0.2645 0.0041  -0.0420 0.0539  122 HIS C CA  
5194 C C   . HIS C 122 ? 0.2067 0.2117 0.2741 0.0092  -0.0332 0.0506  122 HIS C C   
5195 O O   . HIS C 122 ? 0.2018 0.2112 0.2688 0.0077  -0.0308 0.0475  122 HIS C O   
5196 C CB  . HIS C 122 ? 0.2047 0.2194 0.2796 0.0040  -0.0486 0.0620  122 HIS C CB  
5197 C CG  . HIS C 122 ? 0.1944 0.2092 0.2615 -0.0027 -0.0583 0.0651  122 HIS C CG  
5198 N ND1 . HIS C 122 ? 0.2021 0.2168 0.2590 -0.0096 -0.0613 0.0614  122 HIS C ND1 
5199 C CD2 . HIS C 122 ? 0.2040 0.2187 0.2713 -0.0036 -0.0654 0.0717  122 HIS C CD2 
5200 C CE1 . HIS C 122 ? 0.2051 0.2183 0.2544 -0.0149 -0.0695 0.0648  122 HIS C CE1 
5201 N NE2 . HIS C 122 ? 0.2358 0.2499 0.2914 -0.0116 -0.0727 0.0714  122 HIS C NE2 
5202 N N   . TRP C 123 ? 0.2122 0.2125 0.2851 0.0153  -0.0281 0.0517  123 TRP C N   
5203 C CA  . TRP C 123 ? 0.2065 0.2060 0.2834 0.0202  -0.0189 0.0482  123 TRP C CA  
5204 C C   . TRP C 123 ? 0.2018 0.2059 0.2964 0.0276  -0.0154 0.0544  123 TRP C C   
5205 O O   . TRP C 123 ? 0.2265 0.2305 0.3291 0.0303  -0.0188 0.0608  123 TRP C O   
5206 C CB  . TRP C 123 ? 0.1966 0.1830 0.2596 0.0203  -0.0131 0.0409  123 TRP C CB  
5207 C CG  . TRP C 123 ? 0.2187 0.1944 0.2790 0.0218  -0.0136 0.0424  123 TRP C CG  
5208 C CD1 . TRP C 123 ? 0.2119 0.1823 0.2631 0.0173  -0.0193 0.0430  123 TRP C CD1 
5209 C CD2 . TRP C 123 ? 0.2237 0.1917 0.2906 0.0285  -0.0075 0.0440  123 TRP C CD2 
5210 N NE1 . TRP C 123 ? 0.2356 0.1954 0.2870 0.0204  -0.0173 0.0449  123 TRP C NE1 
5211 C CE2 . TRP C 123 ? 0.2249 0.1827 0.2863 0.0275  -0.0103 0.0457  123 TRP C CE2 
5212 C CE3 . TRP C 123 ? 0.2338 0.2016 0.3104 0.0356  0.0010  0.0442  123 TRP C CE3 
5213 C CZ2 . TRP C 123 ? 0.2294 0.1760 0.2945 0.0332  -0.0050 0.0473  123 TRP C CZ2 
5214 C CZ3 . TRP C 123 ? 0.2402 0.1971 0.3210 0.0418  0.0067  0.0458  123 TRP C CZ3 
5215 C CH2 . TRP C 123 ? 0.2658 0.2118 0.3409 0.0406  0.0035  0.0474  123 TRP C CH2 
5216 N N   . ASN C 124 ? 0.2148 0.2238 0.3162 0.0309  -0.0081 0.0530  124 ASN C N   
5217 C CA  . ASN C 124 ? 0.2040 0.2202 0.3247 0.0382  -0.0031 0.0590  124 ASN C CA  
5218 C C   . ASN C 124 ? 0.2377 0.2416 0.3586 0.0455  0.0050  0.0579  124 ASN C C   
5219 O O   . ASN C 124 ? 0.2503 0.2427 0.3583 0.0461  0.0128  0.0499  124 ASN C O   
5220 C CB  . ASN C 124 ? 0.2137 0.2373 0.3380 0.0386  0.0032  0.0568  124 ASN C CB  
5221 C CG  . ASN C 124 ? 0.2355 0.2699 0.3820 0.0454  0.0084  0.0638  124 ASN C CG  
5222 O OD1 . ASN C 124 ? 0.2393 0.2738 0.3984 0.0517  0.0098  0.0695  124 ASN C OD1 
5223 N ND2 . ASN C 124 ? 0.2297 0.2744 0.3826 0.0444  0.0117  0.0643  124 ASN C ND2 
5224 N N   . THR C 125 ? 0.2208 0.2270 0.3567 0.0509  0.0033  0.0663  125 THR C N   
5225 C CA  . THR C 125 ? 0.2292 0.2216 0.3659 0.0584  0.0117  0.0656  125 THR C CA  
5226 C C   . THR C 125 ? 0.2757 0.2665 0.4192 0.0658  0.0253  0.0632  125 THR C C   
5227 O O   . THR C 125 ? 0.3273 0.3047 0.4706 0.0725  0.0344  0.0616  125 THR C O   
5228 C CB  . THR C 125 ? 0.2605 0.2561 0.4125 0.0630  0.0066  0.0764  125 THR C CB  
5229 O OG1 . THR C 125 ? 0.2811 0.2955 0.4569 0.0670  0.0051  0.0857  125 THR C OG1 
5230 C CG2 . THR C 125 ? 0.2459 0.2411 0.3884 0.0557  -0.0058 0.0786  125 THR C CG2 
5231 N N   . LYS C 126 ? 0.2653 0.2686 0.4148 0.0649  0.0275  0.0631  126 LYS C N   
5232 C CA  . LYS C 126 ? 0.3093 0.3093 0.4590 0.0701  0.0411  0.0587  126 LYS C CA  
5233 C C   . LYS C 126 ? 0.3054 0.2855 0.4300 0.0678  0.0476  0.0470  126 LYS C C   
5234 O O   . LYS C 126 ? 0.3280 0.2970 0.4490 0.0735  0.0601  0.0427  126 LYS C O   
5235 C CB  . LYS C 126 ? 0.3276 0.3440 0.4835 0.0665  0.0400  0.0601  126 LYS C CB  
5236 C CG  . LYS C 126 ? 0.3322 0.3463 0.4835 0.0694  0.0529  0.0548  126 LYS C CG  
5237 C CD  . LYS C 126 ? 0.3324 0.3636 0.4915 0.0652  0.0504  0.0580  126 LYS C CD  
5238 C CE  . LYS C 126 ? 0.3718 0.4005 0.5254 0.0681  0.0641  0.0534  126 LYS C CE  
5239 N NZ  . LYS C 126 ? 0.3579 0.4008 0.5163 0.0635  0.0624  0.0559  126 LYS C NZ  
5240 N N   . TYR C 127 ? 0.2768 0.2518 0.3839 0.0594  0.0394  0.0420  127 TYR C N   
5241 C CA  . TYR C 127 ? 0.2947 0.2539 0.3784 0.0551  0.0429  0.0315  127 TYR C CA  
5242 C C   . TYR C 127 ? 0.3517 0.2969 0.4285 0.0541  0.0398  0.0305  127 TYR C C   
5243 O O   . TYR C 127 ? 0.3683 0.3170 0.4565 0.0560  0.0338  0.0380  127 TYR C O   
5244 C CB  . TYR C 127 ? 0.2603 0.2265 0.3318 0.0464  0.0365  0.0275  127 TYR C CB  
5245 C CG  . TYR C 127 ? 0.2796 0.2597 0.3598 0.0475  0.0393  0.0300  127 TYR C CG  
5246 C CD1 . TYR C 127 ? 0.2858 0.2625 0.3640 0.0519  0.0511  0.0268  127 TYR C CD1 
5247 C CD2 . TYR C 127 ? 0.2353 0.2310 0.3255 0.0439  0.0309  0.0357  127 TYR C CD2 
5248 C CE1 . TYR C 127 ? 0.2858 0.2748 0.3723 0.0529  0.0546  0.0297  127 TYR C CE1 
5249 C CE2 . TYR C 127 ? 0.2483 0.2559 0.3472 0.0445  0.0338  0.0384  127 TYR C CE2 
5250 C CZ  . TYR C 127 ? 0.2690 0.2737 0.3667 0.0492  0.0459  0.0357  127 TYR C CZ  
5251 O OH  . TYR C 127 ? 0.2881 0.3045 0.3945 0.0499  0.0499  0.0388  127 TYR C OH  
5252 N N   . GLY C 128 ? 0.3866 0.3154 0.4442 0.0506  0.0437  0.0217  128 GLY C N   
5253 C CA  . GLY C 128 ? 0.3767 0.2899 0.4297 0.0509  0.0434  0.0211  128 GLY C CA  
5254 C C   . GLY C 128 ? 0.3362 0.2523 0.3854 0.0441  0.0316  0.0236  128 GLY C C   
5255 O O   . GLY C 128 ? 0.3770 0.2849 0.4282 0.0452  0.0294  0.0272  128 GLY C O   
5256 N N   . ASP C 129 ? 0.2976 0.2238 0.3401 0.0370  0.0249  0.0216  129 ASP C N   
5257 C CA  . ASP C 129 ? 0.2774 0.2051 0.3131 0.0299  0.0155  0.0222  129 ASP C CA  
5258 C C   . ASP C 129 ? 0.2794 0.2208 0.3123 0.0248  0.0103  0.0212  129 ASP C C   
5259 O O   . ASP C 129 ? 0.2646 0.2130 0.2999 0.0264  0.0140  0.0199  129 ASP C O   
5260 C CB  . ASP C 129 ? 0.3056 0.2172 0.3253 0.0247  0.0169  0.0156  129 ASP C CB  
5261 C CG  . ASP C 129 ? 0.3823 0.2875 0.3887 0.0220  0.0230  0.0064  129 ASP C CG  
5262 O OD1 . ASP C 129 ? 0.3464 0.2622 0.3504 0.0197  0.0216  0.0048  129 ASP C OD1 
5263 O OD2 . ASP C 129 ? 0.4315 0.3202 0.4290 0.0220  0.0292  0.0011  129 ASP C OD2 
5264 N N   . PHE C 130 ? 0.2534 0.1975 0.2806 0.0187  0.0028  0.0217  130 PHE C N   
5265 C CA  . PHE C 130 ? 0.2492 0.2048 0.2742 0.0143  -0.0018 0.0212  130 PHE C CA  
5266 C C   . PHE C 130 ? 0.2536 0.2091 0.2692 0.0121  0.0023  0.0147  130 PHE C C   
5267 O O   . PHE C 130 ? 0.2423 0.2072 0.2606 0.0123  0.0026  0.0151  130 PHE C O   
5268 C CB  . PHE C 130 ? 0.2519 0.2079 0.2707 0.0085  -0.0087 0.0221  130 PHE C CB  
5269 C CG  . PHE C 130 ? 0.2287 0.1942 0.2445 0.0045  -0.0121 0.0211  130 PHE C CG  
5270 C CD1 . PHE C 130 ? 0.2417 0.2073 0.2483 0.0007  -0.0108 0.0160  130 PHE C CD1 
5271 C CD2 . PHE C 130 ? 0.2362 0.2106 0.2585 0.0043  -0.0167 0.0257  130 PHE C CD2 
5272 C CE1 . PHE C 130 ? 0.2465 0.2207 0.2517 -0.0018 -0.0132 0.0159  130 PHE C CE1 
5273 C CE2 . PHE C 130 ? 0.2285 0.2094 0.2477 0.0009  -0.0188 0.0246  130 PHE C CE2 
5274 C CZ  . PHE C 130 ? 0.2376 0.2184 0.2488 -0.0016 -0.0167 0.0200  130 PHE C CZ  
5275 N N   . GLY C 131 ? 0.2662 0.2105 0.2702 0.0095  0.0053  0.0089  131 GLY C N   
5276 C CA  . GLY C 131 ? 0.2626 0.2071 0.2559 0.0062  0.0078  0.0030  131 GLY C CA  
5277 C C   . GLY C 131 ? 0.2651 0.2114 0.2604 0.0108  0.0146  0.0020  131 GLY C C   
5278 O O   . GLY C 131 ? 0.2660 0.2188 0.2566 0.0090  0.0150  0.0004  131 GLY C O   
5279 N N   . LYS C 132 ? 0.2609 0.2015 0.2636 0.0172  0.0205  0.0035  132 LYS C N   
5280 C CA  . LYS C 132 ? 0.2488 0.1921 0.2553 0.0222  0.0281  0.0034  132 LYS C CA  
5281 C C   . LYS C 132 ? 0.2786 0.2382 0.2991 0.0241  0.0250  0.0099  132 LYS C C   
5282 O O   . LYS C 132 ? 0.2668 0.2330 0.2869 0.0246  0.0283  0.0096  132 LYS C O   
5283 C CB  . LYS C 132 ? 0.2591 0.1914 0.2711 0.0293  0.0365  0.0035  132 LYS C CB  
5284 C CG  . LYS C 132 ? 0.3167 0.2303 0.3121 0.0268  0.0413  -0.0044 132 LYS C CG  
5285 C CD  . LYS C 132 ? 0.3802 0.2803 0.3817 0.0343  0.0499  -0.0038 132 LYS C CD  
5286 C CE  . LYS C 132 ? 0.4763 0.3553 0.4594 0.0310  0.0552  -0.0126 132 LYS C CE  
5287 N NZ  . LYS C 132 ? 0.5617 0.4367 0.5391 0.0238  0.0465  -0.0131 132 LYS C NZ  
5288 N N   . ALA C 133 ? 0.2441 0.2099 0.2763 0.0246  0.0185  0.0160  133 ALA C N   
5289 C CA  . ALA C 133 ? 0.2217 0.2018 0.2675 0.0257  0.0154  0.0222  133 ALA C CA  
5290 C C   . ALA C 133 ? 0.2453 0.2327 0.2847 0.0204  0.0115  0.0208  133 ALA C C   
5291 O O   . ALA C 133 ? 0.2160 0.2127 0.2626 0.0211  0.0125  0.0237  133 ALA C O   
5292 C CB  . ALA C 133 ? 0.2154 0.1995 0.2718 0.0258  0.0079  0.0287  133 ALA C CB  
5293 N N   . VAL C 134 ? 0.2201 0.2037 0.2474 0.0151  0.0071  0.0173  134 VAL C N   
5294 C CA  . VAL C 134 ? 0.2057 0.1963 0.2290 0.0108  0.0031  0.0173  134 VAL C CA  
5295 C C   . VAL C 134 ? 0.2384 0.2314 0.2562 0.0110  0.0081  0.0150  134 VAL C C   
5296 O O   . VAL C 134 ? 0.2186 0.2183 0.2357 0.0088  0.0060  0.0163  134 VAL C O   
5297 C CB  . VAL C 134 ? 0.2186 0.2054 0.2323 0.0058  -0.0019 0.0148  134 VAL C CB  
5298 C CG1 . VAL C 134 ? 0.2373 0.2161 0.2389 0.0039  0.0009  0.0092  134 VAL C CG1 
5299 C CG2 . VAL C 134 ? 0.2110 0.2051 0.2233 0.0024  -0.0060 0.0161  134 VAL C CG2 
5300 N N   . GLN C 135 ? 0.2353 0.2221 0.2486 0.0137  0.0151  0.0117  135 GLN C N   
5301 C CA  . GLN C 135 ? 0.2338 0.2219 0.2400 0.0140  0.0206  0.0097  135 GLN C CA  
5302 C C   . GLN C 135 ? 0.2724 0.2675 0.2906 0.0185  0.0260  0.0138  135 GLN C C   
5303 O O   . GLN C 135 ? 0.3155 0.3118 0.3280 0.0191  0.0317  0.0128  135 GLN C O   
5304 C CB  . GLN C 135 ? 0.2522 0.2285 0.2443 0.0138  0.0262  0.0032  135 GLN C CB  
5305 C CG  . GLN C 135 ? 0.2436 0.2135 0.2235 0.0079  0.0207  -0.0010 135 GLN C CG  
5306 C CD  . GLN C 135 ? 0.2534 0.2314 0.2274 0.0029  0.0149  -0.0003 135 GLN C CD  
5307 O OE1 . GLN C 135 ? 0.3028 0.2871 0.2751 0.0032  0.0166  0.0012  135 GLN C OE1 
5308 N NE2 . GLN C 135 ? 0.2246 0.2026 0.1963 -0.0014 0.0085  -0.0008 135 GLN C NE2 
5309 N N   . GLN C 136 ? 0.2502 0.2509 0.2847 0.0212  0.0242  0.0191  136 GLN C N   
5310 C CA  . GLN C 136 ? 0.2475 0.2561 0.2964 0.0255  0.0295  0.0238  136 GLN C CA  
5311 C C   . GLN C 136 ? 0.2236 0.2438 0.2845 0.0229  0.0232  0.0297  136 GLN C C   
5312 O O   . GLN C 136 ? 0.2260 0.2469 0.2886 0.0198  0.0150  0.0311  136 GLN C O   
5313 C CB  . GLN C 136 ? 0.2478 0.2537 0.3085 0.0316  0.0338  0.0260  136 GLN C CB  
5314 C CG  . GLN C 136 ? 0.2999 0.2915 0.3484 0.0343  0.0410  0.0197  136 GLN C CG  
5315 C CD  . GLN C 136 ? 0.3630 0.3515 0.4019 0.0358  0.0511  0.0159  136 GLN C CD  
5316 O OE1 . GLN C 136 ? 0.4183 0.4164 0.4648 0.0372  0.0548  0.0196  136 GLN C OE1 
5317 N NE2 . GLN C 136 ? 0.4101 0.3846 0.4307 0.0347  0.0554  0.0085  136 GLN C NE2 
5318 N N   . PRO C 137 ? 0.2237 0.2521 0.2922 0.0236  0.0271  0.0331  137 PRO C N   
5319 C CA  . PRO C 137 ? 0.2425 0.2803 0.3211 0.0198  0.0208  0.0381  137 PRO C CA  
5320 C C   . PRO C 137 ? 0.2353 0.2782 0.3287 0.0198  0.0147  0.0429  137 PRO C C   
5321 O O   . PRO C 137 ? 0.2491 0.2949 0.3442 0.0149  0.0067  0.0448  137 PRO C O   
5322 C CB  . PRO C 137 ? 0.2479 0.2930 0.3336 0.0212  0.0280  0.0413  137 PRO C CB  
5323 C CG  . PRO C 137 ? 0.3168 0.3546 0.3877 0.0235  0.0362  0.0364  137 PRO C CG  
5324 C CD  . PRO C 137 ? 0.2691 0.2974 0.3343 0.0266  0.0373  0.0320  137 PRO C CD  
5325 N N   . ASP C 138 ? 0.1932 0.2369 0.2971 0.0253  0.0184  0.0451  138 ASP C N   
5326 C CA  . ASP C 138 ? 0.1971 0.2464 0.3156 0.0258  0.0120  0.0508  138 ASP C CA  
5327 C C   . ASP C 138 ? 0.1989 0.2383 0.3092 0.0265  0.0081  0.0483  138 ASP C C   
5328 O O   . ASP C 138 ? 0.2189 0.2607 0.3405 0.0291  0.0050  0.0531  138 ASP C O   
5329 C CB  . ASP C 138 ? 0.1917 0.2500 0.3307 0.0321  0.0182  0.0569  138 ASP C CB  
5330 C CG  . ASP C 138 ? 0.2505 0.3001 0.3859 0.0396  0.0293  0.0535  138 ASP C CG  
5331 O OD1 . ASP C 138 ? 0.2644 0.3014 0.3807 0.0390  0.0322  0.0460  138 ASP C OD1 
5332 O OD2 . ASP C 138 ? 0.2803 0.3357 0.4328 0.0461  0.0356  0.0585  138 ASP C OD2 
5333 N N   . GLY C 139 ? 0.2058 0.2348 0.2976 0.0239  0.0078  0.0416  139 GLY C N   
5334 C CA  . GLY C 139 ? 0.2142 0.2327 0.2977 0.0246  0.0060  0.0389  139 GLY C CA  
5335 C C   . GLY C 139 ? 0.2010 0.2195 0.2840 0.0205  -0.0040 0.0415  139 GLY C C   
5336 O O   . GLY C 139 ? 0.2107 0.2244 0.2954 0.0226  -0.0059 0.0432  139 GLY C O   
5337 N N   . LEU C 140 ? 0.2026 0.2254 0.2821 0.0148  -0.0101 0.0417  140 LEU C N   
5338 C CA  . LEU C 140 ? 0.1801 0.2005 0.2542 0.0101  -0.0185 0.0426  140 LEU C CA  
5339 C C   . LEU C 140 ? 0.2014 0.2307 0.2842 0.0063  -0.0252 0.0477  140 LEU C C   
5340 O O   . LEU C 140 ? 0.1959 0.2324 0.2858 0.0054  -0.0237 0.0491  140 LEU C O   
5341 C CB  . LEU C 140 ? 0.1856 0.1994 0.2433 0.0058  -0.0193 0.0369  140 LEU C CB  
5342 C CG  . LEU C 140 ? 0.1954 0.2008 0.2430 0.0076  -0.0141 0.0316  140 LEU C CG  
5343 C CD1 . LEU C 140 ? 0.2113 0.2137 0.2465 0.0029  -0.0165 0.0279  140 LEU C CD1 
5344 C CD2 . LEU C 140 ? 0.2252 0.2232 0.2729 0.0103  -0.0137 0.0320  140 LEU C CD2 
5345 N N   . ALA C 141 ? 0.1912 0.2190 0.2719 0.0032  -0.0329 0.0504  141 ALA C N   
5346 C CA  . ALA C 141 ? 0.1935 0.2270 0.2771 -0.0027 -0.0408 0.0540  141 ALA C CA  
5347 C C   . ALA C 141 ? 0.2088 0.2336 0.2761 -0.0078 -0.0458 0.0511  141 ALA C C   
5348 O O   . ALA C 141 ? 0.2201 0.2392 0.2820 -0.0066 -0.0473 0.0515  141 ALA C O   
5349 C CB  . ALA C 141 ? 0.2117 0.2548 0.3117 -0.0015 -0.0460 0.0623  141 ALA C CB  
5350 N N   . VAL C 142 ? 0.1883 0.2111 0.2473 -0.0133 -0.0475 0.0482  142 VAL C N   
5351 C CA  . VAL C 142 ? 0.2012 0.2151 0.2442 -0.0180 -0.0508 0.0452  142 VAL C CA  
5352 C C   . VAL C 142 ? 0.2085 0.2241 0.2502 -0.0249 -0.0588 0.0479  142 VAL C C   
5353 O O   . VAL C 142 ? 0.2222 0.2421 0.2692 -0.0280 -0.0595 0.0483  142 VAL C O   
5354 C CB  . VAL C 142 ? 0.2019 0.2094 0.2338 -0.0184 -0.0453 0.0390  142 VAL C CB  
5355 C CG1 . VAL C 142 ? 0.2202 0.2187 0.2366 -0.0226 -0.0478 0.0366  142 VAL C CG1 
5356 C CG2 . VAL C 142 ? 0.2111 0.2172 0.2431 -0.0129 -0.0389 0.0365  142 VAL C CG2 
5357 N N   . LEU C 143 ? 0.2133 0.2253 0.2477 -0.0278 -0.0649 0.0500  143 LEU C N   
5358 C CA  . LEU C 143 ? 0.2449 0.2565 0.2735 -0.0356 -0.0734 0.0521  143 LEU C CA  
5359 C C   . LEU C 143 ? 0.2590 0.2581 0.2674 -0.0401 -0.0715 0.0457  143 LEU C C   
5360 O O   . LEU C 143 ? 0.2530 0.2445 0.2503 -0.0387 -0.0691 0.0435  143 LEU C O   
5361 C CB  . LEU C 143 ? 0.2561 0.2709 0.2871 -0.0360 -0.0812 0.0589  143 LEU C CB  
5362 C CG  . LEU C 143 ? 0.2877 0.3029 0.3117 -0.0448 -0.0917 0.0620  143 LEU C CG  
5363 C CD1 . LEU C 143 ? 0.2892 0.3148 0.3265 -0.0490 -0.0959 0.0648  143 LEU C CD1 
5364 C CD2 . LEU C 143 ? 0.2720 0.2910 0.2988 -0.0440 -0.0993 0.0700  143 LEU C CD2 
5365 N N   . GLY C 144 ? 0.2277 0.2241 0.2324 -0.0450 -0.0713 0.0426  144 GLY C N   
5366 C CA  . GLY C 144 ? 0.2606 0.2444 0.2474 -0.0484 -0.0678 0.0364  144 GLY C CA  
5367 C C   . GLY C 144 ? 0.2600 0.2371 0.2334 -0.0575 -0.0751 0.0361  144 GLY C C   
5368 O O   . GLY C 144 ? 0.2658 0.2483 0.2456 -0.0628 -0.0819 0.0392  144 GLY C O   
5369 N N   . ILE C 145 ? 0.2468 0.2122 0.2015 -0.0597 -0.0737 0.0327  145 ILE C N   
5370 C CA  . ILE C 145 ? 0.2886 0.2452 0.2257 -0.0687 -0.0801 0.0318  145 ILE C CA  
5371 C C   . ILE C 145 ? 0.3021 0.2428 0.2201 -0.0705 -0.0725 0.0243  145 ILE C C   
5372 O O   . ILE C 145 ? 0.3137 0.2505 0.2277 -0.0651 -0.0647 0.0220  145 ILE C O   
5373 C CB  . ILE C 145 ? 0.3073 0.2654 0.2389 -0.0695 -0.0866 0.0367  145 ILE C CB  
5374 C CG1 . ILE C 145 ? 0.3095 0.2836 0.2628 -0.0662 -0.0930 0.0448  145 ILE C CG1 
5375 C CG2 . ILE C 145 ? 0.3195 0.2671 0.2291 -0.0797 -0.0933 0.0353  145 ILE C CG2 
5376 C CD1 . ILE C 145 ? 0.3136 0.2908 0.2657 -0.0655 -0.0997 0.0516  145 ILE C CD1 
5377 N N   . PHE C 146 ? 0.3096 0.2409 0.2165 -0.0783 -0.0742 0.0206  146 PHE C N   
5378 C CA  . PHE C 146 ? 0.3039 0.2183 0.1924 -0.0797 -0.0659 0.0134  146 PHE C CA  
5379 C C   . PHE C 146 ? 0.3432 0.2464 0.2088 -0.0842 -0.0671 0.0116  146 PHE C C   
5380 O O   . PHE C 146 ? 0.3645 0.2693 0.2233 -0.0907 -0.0772 0.0150  146 PHE C O   
5381 C CB  . PHE C 146 ? 0.3208 0.2264 0.2043 -0.0866 -0.0664 0.0095  146 PHE C CB  
5382 C CG  . PHE C 146 ? 0.3209 0.2355 0.2248 -0.0825 -0.0637 0.0111  146 PHE C CG  
5383 C CD1 . PHE C 146 ? 0.3098 0.2256 0.2220 -0.0734 -0.0534 0.0098  146 PHE C CD1 
5384 C CD2 . PHE C 146 ? 0.3146 0.2371 0.2294 -0.0882 -0.0717 0.0144  146 PHE C CD2 
5385 C CE1 . PHE C 146 ? 0.3187 0.2420 0.2477 -0.0699 -0.0509 0.0117  146 PHE C CE1 
5386 C CE2 . PHE C 146 ? 0.3014 0.2323 0.2348 -0.0847 -0.0685 0.0163  146 PHE C CE2 
5387 C CZ  . PHE C 146 ? 0.3079 0.2383 0.2473 -0.0754 -0.0579 0.0148  146 PHE C CZ  
5388 N N   . LEU C 147 ? 0.3590 0.2510 0.2128 -0.0808 -0.0565 0.0068  147 LEU C N   
5389 C CA  . LEU C 147 ? 0.3681 0.2467 0.1975 -0.0850 -0.0548 0.0040  147 LEU C CA  
5390 C C   . LEU C 147 ? 0.3954 0.2548 0.2056 -0.0900 -0.0484 -0.0037 147 LEU C C   
5391 O O   . LEU C 147 ? 0.4054 0.2598 0.2197 -0.0843 -0.0375 -0.0074 147 LEU C O   
5392 C CB  . LEU C 147 ? 0.3708 0.2507 0.2007 -0.0776 -0.0465 0.0047  147 LEU C CB  
5393 C CG  . LEU C 147 ? 0.3327 0.2254 0.1727 -0.0746 -0.0524 0.0116  147 LEU C CG  
5394 C CD1 . LEU C 147 ? 0.3379 0.2475 0.2041 -0.0693 -0.0565 0.0164  147 LEU C CD1 
5395 C CD2 . LEU C 147 ? 0.3495 0.2404 0.1861 -0.0695 -0.0438 0.0116  147 LEU C CD2 
5396 N N   . LYS C 148 ? 0.4253 0.2733 0.2139 -0.1003 -0.0547 -0.0060 148 LYS C N   
5397 C CA  . LYS C 148 ? 0.4727 0.2992 0.2388 -0.1064 -0.0488 -0.0141 148 LYS C CA  
5398 C C   . LYS C 148 ? 0.5249 0.3369 0.2645 -0.1086 -0.0434 -0.0174 148 LYS C C   
5399 O O   . LYS C 148 ? 0.5926 0.4090 0.3243 -0.1121 -0.0511 -0.0132 148 LYS C O   
5400 C CB  . LYS C 148 ? 0.5559 0.3790 0.3154 -0.1184 -0.0607 -0.0149 148 LYS C CB  
5401 C CG  . LYS C 148 ? 0.6596 0.4584 0.3930 -0.1272 -0.0566 -0.0237 148 LYS C CG  
5402 C CD  . LYS C 148 ? 0.7123 0.5142 0.4453 -0.1385 -0.0699 -0.0217 148 LYS C CD  
5403 C CE  . LYS C 148 ? 0.7742 0.5920 0.5105 -0.1413 -0.0827 -0.0132 148 LYS C CE  
5404 N NZ  . LYS C 148 ? 0.8622 0.6820 0.5955 -0.1514 -0.0930 -0.0108 148 LYS C NZ  
5405 N N   . VAL C 149 ? 0.5188 0.3130 0.2443 -0.1066 -0.0297 -0.0246 149 VAL C N   
5406 C CA  . VAL C 149 ? 0.5798 0.3585 0.2788 -0.1084 -0.0221 -0.0284 149 VAL C CA  
5407 C C   . VAL C 149 ? 0.5931 0.3562 0.2616 -0.1223 -0.0304 -0.0321 149 VAL C C   
5408 O O   . VAL C 149 ? 0.6346 0.3890 0.2992 -0.1281 -0.0321 -0.0358 149 VAL C O   
5409 C CB  . VAL C 149 ? 0.6316 0.3963 0.3264 -0.1014 -0.0038 -0.0346 149 VAL C CB  
5410 C CG1 . VAL C 149 ? 0.6801 0.4258 0.3443 -0.1046 0.0050  -0.0395 149 VAL C CG1 
5411 C CG2 . VAL C 149 ? 0.6258 0.4078 0.3482 -0.0886 0.0033  -0.0297 149 VAL C CG2 
5412 N N   . GLY C 150 ? 0.5832 0.3487 0.2410 -0.1244 -0.0338 -0.0281 150 GLY C N   
5413 C CA  . GLY C 150 ? 0.6121 0.3713 0.2535 -0.1336 -0.0405 -0.0274 150 GLY C CA  
5414 C C   . GLY C 150 ? 0.6035 0.3663 0.2363 -0.1332 -0.0418 -0.0224 150 GLY C C   
5415 O O   . GLY C 150 ? 0.6027 0.3599 0.2291 -0.1272 -0.0297 -0.0242 150 GLY C O   
5416 N N   . SER C 151 ? 0.6230 0.3957 0.2571 -0.1391 -0.0558 -0.0156 151 SER C N   
5417 C CA  . SER C 151 ? 0.5935 0.3703 0.2210 -0.1390 -0.0585 -0.0097 151 SER C CA  
5418 C C   . SER C 151 ? 0.5549 0.3473 0.2016 -0.1302 -0.0587 -0.0034 151 SER C C   
5419 O O   . SER C 151 ? 0.5791 0.3838 0.2469 -0.1260 -0.0627 -0.0011 151 SER C O   
5420 C CB  . SER C 151 ? 0.6358 0.4202 0.2626 -0.1472 -0.0740 -0.0034 151 SER C CB  
5421 O OG  . SER C 151 ? 0.7593 0.5278 0.3641 -0.1563 -0.0734 -0.0089 151 SER C OG  
5422 N N   . ALA C 152 ? 0.6019 0.3930 0.2405 -0.1276 -0.0541 -0.0006 152 ALA C N   
5423 C CA  . ALA C 152 ? 0.5905 0.3949 0.2456 -0.1199 -0.0538 0.0059  152 ALA C CA  
5424 C C   . ALA C 152 ? 0.5960 0.4185 0.2706 -0.1203 -0.0695 0.0153  152 ALA C C   
5425 O O   . ALA C 152 ? 0.6138 0.4384 0.2845 -0.1267 -0.0799 0.0187  152 ALA C O   
5426 C CB  . ALA C 152 ? 0.6063 0.4048 0.2478 -0.1182 -0.0457 0.0075  152 ALA C CB  
5427 N N   . LEU C 153 ? 0.5450 0.3807 0.2412 -0.1131 -0.0709 0.0197  153 LEU C N   
5428 C CA  . LEU C 153 ? 0.5123 0.3653 0.2301 -0.1115 -0.0837 0.0288  153 LEU C CA  
5429 C C   . LEU C 153 ? 0.4740 0.3317 0.1945 -0.1075 -0.0840 0.0364  153 LEU C C   
5430 O O   . LEU C 153 ? 0.4669 0.3251 0.1922 -0.1013 -0.0760 0.0368  153 LEU C O   
5431 C CB  . LEU C 153 ? 0.4948 0.3588 0.2355 -0.1059 -0.0848 0.0290  153 LEU C CB  
5432 C CG  . LEU C 153 ? 0.5108 0.3927 0.2760 -0.1041 -0.0972 0.0378  153 LEU C CG  
5433 C CD1 . LEU C 153 ? 0.5363 0.4210 0.3015 -0.1117 -0.1072 0.0389  153 LEU C CD1 
5434 C CD2 . LEU C 153 ? 0.4610 0.3545 0.2548 -0.0956 -0.0930 0.0370  153 LEU C CD2 
5435 N N   . PRO C 154 ? 0.4826 0.3253 0.2169 -0.1383 -0.1075 0.0547  154 PRO C N   
5436 C CA  . PRO C 154 ? 0.4833 0.3364 0.2164 -0.1565 -0.1072 0.0704  154 PRO C CA  
5437 C C   . PRO C 154 ? 0.4760 0.3203 0.2425 -0.1456 -0.1099 0.0815  154 PRO C C   
5438 O O   . PRO C 154 ? 0.5103 0.3663 0.2780 -0.1535 -0.1050 0.0854  154 PRO C O   
5439 C CB  . PRO C 154 ? 0.5522 0.3952 0.2849 -0.1747 -0.1209 0.0857  154 PRO C CB  
5440 C CG  . PRO C 154 ? 0.5770 0.4142 0.2898 -0.1716 -0.1206 0.0743  154 PRO C CG  
5441 C CD  . PRO C 154 ? 0.5287 0.3564 0.2538 -0.1462 -0.1192 0.0615  154 PRO C CD  
5442 N N   . GLY C 155 ? 0.4939 0.3231 0.2919 -0.1272 -0.1153 0.0828  155 GLY C N   
5443 C CA  . GLY C 155 ? 0.4837 0.3137 0.3205 -0.1131 -0.1142 0.0845  155 GLY C CA  
5444 C C   . GLY C 155 ? 0.4438 0.2789 0.2815 -0.1043 -0.0996 0.0752  155 GLY C C   
5445 O O   . GLY C 155 ? 0.4734 0.3070 0.3343 -0.0973 -0.0986 0.0778  155 GLY C O   
5446 N N   . LEU C 156 ? 0.4302 0.2795 0.2532 -0.1000 -0.0873 0.0567  156 LEU C N   
5447 C CA  . LEU C 156 ? 0.3896 0.2530 0.2227 -0.0891 -0.0732 0.0419  156 LEU C CA  
5448 C C   . LEU C 156 ? 0.4000 0.2875 0.2188 -0.1030 -0.0641 0.0397  156 LEU C C   
5449 O O   . LEU C 156 ? 0.4083 0.3090 0.2390 -0.0966 -0.0541 0.0316  156 LEU C O   
5450 C CB  . LEU C 156 ? 0.4131 0.2778 0.2459 -0.0744 -0.0692 0.0212  156 LEU C CB  
5451 C CG  . LEU C 156 ? 0.4180 0.2923 0.2662 -0.0604 -0.0600 0.0052  156 LEU C CG  
5452 C CD1 . LEU C 156 ? 0.3620 0.2255 0.2329 -0.0541 -0.0607 0.0148  156 LEU C CD1 
5453 C CD2 . LEU C 156 ? 0.4077 0.2762 0.2550 -0.0474 -0.0642 -0.0140 156 LEU C CD2 
5454 N N   . GLN C 157 ? 0.4263 0.3218 0.2187 -0.1248 -0.0682 0.0483  157 GLN C N   
5455 C CA  . GLN C 157 ? 0.4290 0.3581 0.2030 -0.1415 -0.0566 0.0422  157 GLN C CA  
5456 C C   . GLN C 157 ? 0.4251 0.3567 0.2111 -0.1489 -0.0573 0.0558  157 GLN C C   
5457 O O   . GLN C 157 ? 0.4144 0.3756 0.2017 -0.1514 -0.0439 0.0454  157 GLN C O   
5458 C CB  . GLN C 157 ? 0.4875 0.4267 0.2244 -0.1695 -0.0618 0.0503  157 GLN C CB  
5459 C CG  . GLN C 157 ? 0.5435 0.5311 0.2581 -0.1857 -0.0439 0.0338  157 GLN C CG  
5460 C CD  . GLN C 157 ? 0.5629 0.5760 0.2911 -0.1605 -0.0254 -0.0034 157 GLN C CD  
5461 O OE1 . GLN C 157 ? 0.5501 0.5459 0.2828 -0.1410 -0.0284 -0.0185 157 GLN C OE1 
5462 N NE2 . GLN C 157 ? 0.5120 0.5671 0.2471 -0.1628 -0.0090 -0.0178 157 GLN C NE2 
5463 N N   . LYS C 158 ? 0.4327 0.3336 0.2314 -0.1506 -0.0740 0.0770  158 LYS C N   
5464 C CA  . LYS C 158 ? 0.4318 0.3292 0.2406 -0.1574 -0.0783 0.0888  158 LYS C CA  
5465 C C   . LYS C 158 ? 0.3903 0.2954 0.2220 -0.1366 -0.0642 0.0729  158 LYS C C   
5466 O O   . LYS C 158 ? 0.4090 0.3275 0.2424 -0.1442 -0.0600 0.0749  158 LYS C O   
5467 C CB  . LYS C 158 ? 0.4602 0.3302 0.2945 -0.1502 -0.0991 0.1000  158 LYS C CB  
5468 C CG  . LYS C 158 ? 0.5077 0.3766 0.3547 -0.1537 -0.1080 0.1061  158 LYS C CG  
5469 C CD  . LYS C 158 ? 0.5274 0.3748 0.4051 -0.1365 -0.1246 0.1075  158 LYS C CD  
5470 C CE  . LYS C 158 ? 0.5243 0.3657 0.4122 -0.1377 -0.1344 0.1116  158 LYS C CE  
5471 N NZ  . LYS C 158 ? 0.5326 0.3737 0.4081 -0.1606 -0.1571 0.1259  158 LYS C NZ  
5472 N N   . VAL C 159 ? 0.3596 0.2548 0.2080 -0.1130 -0.0596 0.0595  159 VAL C N   
5473 C CA  . VAL C 159 ? 0.3229 0.2235 0.1898 -0.0958 -0.0491 0.0453  159 VAL C CA  
5474 C C   . VAL C 159 ? 0.3518 0.2876 0.2128 -0.0976 -0.0351 0.0288  159 VAL C C   
5475 O O   . VAL C 159 ? 0.3499 0.3009 0.2197 -0.0989 -0.0290 0.0263  159 VAL C O   
5476 C CB  . VAL C 159 ? 0.3445 0.2287 0.2247 -0.0763 -0.0502 0.0367  159 VAL C CB  
5477 C CG1 . VAL C 159 ? 0.3533 0.2430 0.2475 -0.0629 -0.0425 0.0230  159 VAL C CG1 
5478 C CG2 . VAL C 159 ? 0.3700 0.2294 0.2644 -0.0723 -0.0609 0.0486  159 VAL C CG2 
5479 N N   . VAL C 160 ? 0.3822 0.3330 0.2309 -0.0962 -0.0304 0.0148  160 VAL C N   
5480 C CA  A VAL C 160 ? 0.4078 0.3961 0.2578 -0.0926 -0.0169 -0.0084 160 VAL C CA  
5481 C CA  B VAL C 160 ? 0.4027 0.3898 0.2554 -0.0914 -0.0170 -0.0079 160 VAL C CA  
5482 C C   . VAL C 160 ? 0.4146 0.4386 0.2560 -0.1143 -0.0086 -0.0031 160 VAL C C   
5483 O O   . VAL C 160 ? 0.4069 0.4628 0.2629 -0.1105 0.0020  -0.0170 160 VAL C O   
5484 C CB  A VAL C 160 ? 0.4536 0.4504 0.2875 -0.0901 -0.0152 -0.0255 160 VAL C CB  
5485 C CB  B VAL C 160 ? 0.4454 0.4400 0.2894 -0.0822 -0.0148 -0.0296 160 VAL C CB  
5486 C CG1 A VAL C 160 ? 0.4509 0.4985 0.2797 -0.0953 0.0004  -0.0491 160 VAL C CG1 
5487 C CG1 B VAL C 160 ? 0.4521 0.4124 0.3112 -0.0602 -0.0250 -0.0347 160 VAL C CG1 
5488 C CG2 A VAL C 160 ? 0.4648 0.4349 0.3132 -0.0660 -0.0228 -0.0377 160 VAL C CG2 
5489 C CG2 B VAL C 160 ? 0.4570 0.4509 0.2705 -0.1016 -0.0185 -0.0199 160 VAL C CG2 
5490 N N   . ASP C 161 ? 0.3887 0.4083 0.2070 -0.1397 -0.0161 0.0189  161 ASP C N   
5491 C CA  . ASP C 161 ? 0.4239 0.4788 0.2258 -0.1689 -0.0114 0.0280  161 ASP C CA  
5492 C C   . ASP C 161 ? 0.4366 0.4914 0.2558 -0.1712 -0.0130 0.0385  161 ASP C C   
5493 O O   . ASP C 161 ? 0.5204 0.6144 0.3322 -0.1927 -0.0059 0.0410  161 ASP C O   
5494 C CB  . ASP C 161 ? 0.4826 0.5233 0.2536 -0.1990 -0.0264 0.0541  161 ASP C CB  
5495 C CG  . ASP C 161 ? 0.5087 0.5657 0.2517 -0.2089 -0.0221 0.0439  161 ASP C CG  
5496 O OD1 . ASP C 161 ? 0.5113 0.5982 0.2577 -0.1940 -0.0052 0.0134  161 ASP C OD1 
5497 O OD2 . ASP C 161 ? 0.6651 0.7027 0.3940 -0.2278 -0.0378 0.0635  161 ASP C OD2 
5498 N N   . VAL C 162 ? 0.3762 0.3899 0.2158 -0.1529 -0.0226 0.0451  162 VAL C N   
5499 C CA  . VAL C 162 ? 0.3669 0.3733 0.2198 -0.1556 -0.0268 0.0553  162 VAL C CA  
5500 C C   . VAL C 162 ? 0.3463 0.3693 0.2243 -0.1348 -0.0149 0.0353  162 VAL C C   
5501 O O   . VAL C 162 ? 0.3473 0.3734 0.2352 -0.1391 -0.0161 0.0411  162 VAL C O   
5502 C CB  . VAL C 162 ? 0.3745 0.3280 0.2349 -0.1485 -0.0447 0.0713  162 VAL C CB  
5503 C CG1 . VAL C 162 ? 0.3887 0.3207 0.2696 -0.1194 -0.0416 0.0573  162 VAL C CG1 
5504 C CG2 . VAL C 162 ? 0.4273 0.3682 0.2895 -0.1622 -0.0560 0.0879  162 VAL C CG2 
5505 N N   . LEU C 163 ? 0.3273 0.3597 0.2155 -0.1142 -0.0066 0.0125  163 LEU C N   
5506 C CA  . LEU C 163 ? 0.3072 0.3417 0.2217 -0.0934 -0.0034 -0.0030 163 LEU C CA  
5507 C C   . LEU C 163 ? 0.3388 0.4201 0.2666 -0.1006 0.0064  -0.0114 163 LEU C C   
5508 O O   . LEU C 163 ? 0.3115 0.3900 0.2602 -0.0915 0.0043  -0.0138 163 LEU C O   
5509 C CB  . LEU C 163 ? 0.3198 0.3482 0.2426 -0.0712 -0.0031 -0.0239 163 LEU C CB  
5510 C CG  . LEU C 163 ? 0.3180 0.3026 0.2321 -0.0643 -0.0134 -0.0148 163 LEU C CG  
5511 C CD1 . LEU C 163 ? 0.3245 0.3030 0.2458 -0.0452 -0.0165 -0.0346 163 LEU C CD1 
5512 C CD2 . LEU C 163 ? 0.3209 0.2728 0.2432 -0.0611 -0.0209 -0.0009 163 LEU C CD2 
5513 N N   . ASP C 164 ? 0.3619 0.4908 0.2784 -0.1181 0.0172  -0.0170 164 ASP C N   
5514 C CA  . ASP C 164 ? 0.3565 0.5388 0.2901 -0.1255 0.0279  -0.0266 164 ASP C CA  
5515 C C   . ASP C 164 ? 0.3292 0.5028 0.2616 -0.1441 0.0204  -0.0015 164 ASP C C   
5516 O O   . ASP C 164 ? 0.3560 0.5661 0.3083 -0.1476 0.0259  -0.0067 164 ASP C O   
5517 C CB  . ASP C 164 ? 0.4737 0.7187 0.3931 -0.1450 0.0436  -0.0392 164 ASP C CB  
5518 C CG  . ASP C 164 ? 0.5991 0.8737 0.5354 -0.1207 0.0547  -0.0777 164 ASP C CG  
5519 O OD1 . ASP C 164 ? 0.6215 0.8763 0.5878 -0.0901 0.0489  -0.0945 164 ASP C OD1 
5520 O OD2 . ASP C 164 ? 0.6531 0.9686 0.5715 -0.1331 0.0671  -0.0919 164 ASP C OD2 
5521 N N   . SER C 165 ? 0.3282 0.4530 0.2410 -0.1545 0.0058  0.0240  165 SER C N   
5522 C CA  . SER C 165 ? 0.3231 0.4299 0.2344 -0.1698 -0.0056 0.0462  165 SER C CA  
5523 C C   . SER C 165 ? 0.3173 0.3847 0.2475 -0.1485 -0.0129 0.0444  165 SER C C   
5524 O O   . SER C 165 ? 0.3561 0.4091 0.2868 -0.1592 -0.0223 0.0591  165 SER C O   
5525 C CB  . SER C 165 ? 0.4333 0.5058 0.3169 -0.1922 -0.0221 0.0730  165 SER C CB  
5526 O OG  . SER C 165 ? 0.4442 0.4623 0.3277 -0.1740 -0.0329 0.0754  165 SER C OG  
5527 N N   . ILE C 166 ? 0.3101 0.2898 0.2338 -0.0676 0.0060  0.0277  166 ILE C N   
5528 C CA  . ILE C 166 ? 0.2813 0.2682 0.2188 -0.0641 0.0046  0.0281  166 ILE C CA  
5529 C C   . ILE C 166 ? 0.2851 0.2792 0.2301 -0.0589 0.0078  0.0252  166 ILE C C   
5530 O O   . ILE C 166 ? 0.2598 0.2539 0.2115 -0.0550 0.0047  0.0252  166 ILE C O   
5531 C CB  . ILE C 166 ? 0.2694 0.2495 0.2094 -0.0630 -0.0023 0.0308  166 ILE C CB  
5532 C CG1 . ILE C 166 ? 0.2545 0.2267 0.1884 -0.0617 -0.0060 0.0303  166 ILE C CG1 
5533 C CG2 . ILE C 166 ? 0.2828 0.2568 0.2182 -0.0674 -0.0044 0.0347  166 ILE C CG2 
5534 C CD1 . ILE C 166 ? 0.2657 0.2361 0.2079 -0.0587 -0.0116 0.0322  166 ILE C CD1 
5535 N N   . LYS C 167 ? 0.2958 0.2964 0.2405 -0.0587 0.0143  0.0231  167 LYS C N   
5536 C CA  . LYS C 167 ? 0.3021 0.3068 0.2523 -0.0531 0.0182  0.0206  167 LYS C CA  
5537 C C   . LYS C 167 ? 0.2776 0.2933 0.2430 -0.0490 0.0171  0.0220  167 LYS C C   
5538 O O   . LYS C 167 ? 0.2679 0.2836 0.2384 -0.0436 0.0172  0.0211  167 LYS C O   
5539 C CB  . LYS C 167 ? 0.3144 0.3242 0.2621 -0.0534 0.0265  0.0186  167 LYS C CB  
5540 C CG  . LYS C 167 ? 0.3916 0.4046 0.3455 -0.0465 0.0319  0.0162  167 LYS C CG  
5541 C CD  . LYS C 167 ? 0.4545 0.4736 0.4078 -0.0462 0.0415  0.0144  167 LYS C CD  
5542 C CE  . LYS C 167 ? 0.5506 0.5717 0.5115 -0.0383 0.0474  0.0125  167 LYS C CE  
5543 N NZ  . LYS C 167 ? 0.6385 0.6684 0.6033 -0.0366 0.0576  0.0115  167 LYS C NZ  
5544 N N   . THR C 168 ? 0.2525 0.2773 0.2243 -0.0518 0.0163  0.0242  168 THR C N   
5545 C CA  . THR C 168 ? 0.2412 0.2777 0.2261 -0.0491 0.0154  0.0257  168 THR C CA  
5546 C C   . THR C 168 ? 0.2497 0.2838 0.2365 -0.0512 0.0097  0.0274  168 THR C C   
5547 O O   . THR C 168 ? 0.2338 0.2590 0.2136 -0.0552 0.0073  0.0278  168 THR C O   
5548 C CB  . THR C 168 ? 0.2593 0.3113 0.2512 -0.0511 0.0199  0.0267  168 THR C CB  
5549 O OG1 . THR C 168 ? 0.2812 0.3313 0.2661 -0.0582 0.0203  0.0270  168 THR C OG1 
5550 C CG2 . THR C 168 ? 0.2814 0.3375 0.2750 -0.0471 0.0266  0.0253  168 THR C CG2 
5551 N N   . LYS C 169 ? 0.2399 0.2821 0.2365 -0.0485 0.0082  0.0286  169 LYS C N   
5552 C CA  . LYS C 169 ? 0.2407 0.2803 0.2390 -0.0500 0.0038  0.0297  169 LYS C CA  
5553 C C   . LYS C 169 ? 0.2345 0.2729 0.2285 -0.0570 0.0037  0.0301  169 LYS C C   
5554 O O   . LYS C 169 ? 0.2476 0.2952 0.2428 -0.0610 0.0063  0.0304  169 LYS C O   
5555 C CB  . LYS C 169 ? 0.2242 0.2750 0.2327 -0.0475 0.0028  0.0314  169 LYS C CB  
5556 C CG  . LYS C 169 ? 0.2189 0.2660 0.2278 -0.0494 -0.0010 0.0321  169 LYS C CG  
5557 C CD  . LYS C 169 ? 0.2215 0.2794 0.2389 -0.0475 -0.0024 0.0341  169 LYS C CD  
5558 C CE  . LYS C 169 ? 0.2654 0.3183 0.2810 -0.0503 -0.0052 0.0343  169 LYS C CE  
5559 N NZ  . LYS C 169 ? 0.3163 0.3783 0.3388 -0.0483 -0.0071 0.0366  169 LYS C NZ  
5560 N N   . GLY C 170 ? 0.2241 0.2513 0.2138 -0.0584 0.0009  0.0304  170 GLY C N   
5561 C CA  . GLY C 170 ? 0.2457 0.2688 0.2313 -0.0643 0.0012  0.0308  170 GLY C CA  
5562 C C   . GLY C 170 ? 0.2537 0.2678 0.2306 -0.0672 0.0023  0.0312  170 GLY C C   
5563 O O   . GLY C 170 ? 0.2858 0.2928 0.2586 -0.0713 0.0025  0.0320  170 GLY C O   
5564 N N   . LYS C 171 ? 0.2326 0.2463 0.2058 -0.0655 0.0034  0.0307  171 LYS C N   
5565 C CA  . LYS C 171 ? 0.2474 0.2525 0.2109 -0.0688 0.0041  0.0315  171 LYS C CA  
5566 C C   . LYS C 171 ? 0.2584 0.2511 0.2185 -0.0672 -0.0002 0.0335  171 LYS C C   
5567 O O   . LYS C 171 ? 0.2549 0.2459 0.2183 -0.0628 -0.0033 0.0334  171 LYS C O   
5568 C CB  . LYS C 171 ? 0.2689 0.2762 0.2276 -0.0681 0.0071  0.0302  171 LYS C CB  
5569 C CG  . LYS C 171 ? 0.2916 0.3122 0.2548 -0.0697 0.0121  0.0291  171 LYS C CG  
5570 C CD  . LYS C 171 ? 0.3792 0.3996 0.3355 -0.0704 0.0165  0.0279  171 LYS C CD  
5571 C CE  . LYS C 171 ? 0.3987 0.4110 0.3438 -0.0766 0.0173  0.0293  171 LYS C CE  
5572 N NZ  . LYS C 171 ? 0.4491 0.4620 0.3865 -0.0782 0.0227  0.0280  171 LYS C NZ  
5573 N N   . SER C 172 ? 0.2675 0.2517 0.2212 -0.0709 -0.0005 0.0358  172 SER C N   
5574 C CA  A SER C 172 ? 0.2731 0.2466 0.2247 -0.0694 -0.0048 0.0389  172 SER C CA  
5575 C CA  B SER C 172 ? 0.2724 0.2456 0.2242 -0.0697 -0.0046 0.0391  172 SER C CA  
5576 C C   . SER C 172 ? 0.2860 0.2521 0.2273 -0.0732 -0.0048 0.0416  172 SER C C   
5577 O O   . SER C 172 ? 0.3169 0.2852 0.2527 -0.0774 -0.0009 0.0407  172 SER C O   
5578 C CB  A SER C 172 ? 0.2891 0.2586 0.2466 -0.0690 -0.0053 0.0404  172 SER C CB  
5579 C CB  B SER C 172 ? 0.2898 0.2590 0.2467 -0.0701 -0.0044 0.0404  172 SER C CB  
5580 O OG  A SER C 172 ? 0.2894 0.2569 0.2437 -0.0740 -0.0016 0.0405  172 SER C OG  
5581 O OG  B SER C 172 ? 0.2738 0.2336 0.2316 -0.0680 -0.0078 0.0444  172 SER C OG  
5582 N N   . ALA C 173 ? 0.2719 0.2298 0.2106 -0.0719 -0.0095 0.0453  173 ALA C N   
5583 C CA  . ALA C 173 ? 0.2927 0.2429 0.2210 -0.0755 -0.0107 0.0491  173 ALA C CA  
5584 C C   . ALA C 173 ? 0.2681 0.2104 0.1992 -0.0736 -0.0159 0.0549  173 ALA C C   
5585 O O   . ALA C 173 ? 0.2886 0.2319 0.2273 -0.0696 -0.0195 0.0556  173 ALA C O   
5586 C CB  . ALA C 173 ? 0.3017 0.2523 0.2197 -0.0770 -0.0113 0.0477  173 ALA C CB  
5587 N N   . ASP C 174 ? 0.2824 0.2167 0.2076 -0.0765 -0.0162 0.0598  174 ASP C N   
5588 C CA  . ASP C 174 ? 0.3012 0.2290 0.2294 -0.0742 -0.0217 0.0667  174 ASP C CA  
5589 C C   . ASP C 174 ? 0.3369 0.2663 0.2618 -0.0735 -0.0283 0.0682  174 ASP C C   
5590 O O   . ASP C 174 ? 0.3333 0.2642 0.2477 -0.0766 -0.0283 0.0655  174 ASP C O   
5591 C CB  . ASP C 174 ? 0.3061 0.2250 0.2269 -0.0775 -0.0216 0.0726  174 ASP C CB  
5592 C CG  . ASP C 174 ? 0.3532 0.2680 0.2748 -0.0797 -0.0149 0.0713  174 ASP C CG  
5593 O OD1 . ASP C 174 ? 0.3666 0.2833 0.2969 -0.0777 -0.0116 0.0680  174 ASP C OD1 
5594 O OD2 . ASP C 174 ? 0.4556 0.3641 0.3681 -0.0840 -0.0132 0.0743  174 ASP C OD2 
5595 N N   . PHE C 175 ? 0.2820 0.2109 0.2157 -0.0700 -0.0335 0.0727  175 PHE C N   
5596 C CA  . PHE C 175 ? 0.2898 0.2208 0.2209 -0.0701 -0.0403 0.0739  175 PHE C CA  
5597 C C   . PHE C 175 ? 0.2698 0.1988 0.2097 -0.0677 -0.0465 0.0825  175 PHE C C   
5598 O O   . PHE C 175 ? 0.3129 0.2452 0.2660 -0.0633 -0.0478 0.0832  175 PHE C O   
5599 C CB  . PHE C 175 ? 0.2882 0.2255 0.2247 -0.0676 -0.0393 0.0674  175 PHE C CB  
5600 C CG  . PHE C 175 ? 0.3038 0.2417 0.2336 -0.0695 -0.0447 0.0668  175 PHE C CG  
5601 C CD1 . PHE C 175 ? 0.3362 0.2722 0.2509 -0.0738 -0.0432 0.0632  175 PHE C CD1 
5602 C CD2 . PHE C 175 ? 0.2901 0.2298 0.2279 -0.0676 -0.0509 0.0699  175 PHE C CD2 
5603 C CE1 . PHE C 175 ? 0.3673 0.3017 0.2732 -0.0765 -0.0476 0.0616  175 PHE C CE1 
5604 C CE2 . PHE C 175 ? 0.3294 0.2687 0.2592 -0.0707 -0.0559 0.0687  175 PHE C CE2 
5605 C CZ  . PHE C 175 ? 0.3576 0.2935 0.2710 -0.0752 -0.0542 0.0644  175 PHE C CZ  
5606 N N   . THR C 176 ? 0.2883 0.2124 0.2208 -0.0706 -0.0505 0.0894  176 THR C N   
5607 C CA  . THR C 176 ? 0.3049 0.2270 0.2467 -0.0679 -0.0555 0.0992  176 THR C CA  
5608 C C   . THR C 176 ? 0.3620 0.2863 0.2990 -0.0708 -0.0654 0.1051  176 THR C C   
5609 O O   . THR C 176 ? 0.3584 0.2829 0.2808 -0.0761 -0.0677 0.1018  176 THR C O   
5610 C CB  . THR C 176 ? 0.3345 0.2485 0.2730 -0.0686 -0.0523 0.1043  176 THR C CB  
5611 O OG1 . THR C 176 ? 0.3536 0.2643 0.2743 -0.0749 -0.0527 0.1040  176 THR C OG1 
5612 C CG2 . THR C 176 ? 0.3389 0.2501 0.2825 -0.0666 -0.0428 0.0986  176 THR C CG2 
5613 N N   . ASN C 177 ? 0.3481 0.2747 0.2982 -0.0673 -0.0710 0.1138  177 ASN C N   
5614 C CA  . ASN C 177 ? 0.3826 0.3123 0.3299 -0.0705 -0.0816 0.1217  177 ASN C CA  
5615 C C   . ASN C 177 ? 0.3879 0.3228 0.3297 -0.0742 -0.0860 0.1160  177 ASN C C   
5616 O O   . ASN C 177 ? 0.4423 0.3778 0.3729 -0.0802 -0.0939 0.1194  177 ASN C O   
5617 C CB  . ASN C 177 ? 0.4226 0.3464 0.3536 -0.0761 -0.0847 0.1272  177 ASN C CB  
5618 C CG  . ASN C 177 ? 0.4201 0.3369 0.3555 -0.0729 -0.0799 0.1330  177 ASN C CG  
5619 O OD1 . ASN C 177 ? 0.4731 0.3829 0.3963 -0.0759 -0.0744 0.1304  177 ASN C OD1 
5620 N ND2 . ASN C 177 ? 0.3892 0.3081 0.3432 -0.0665 -0.0814 0.1405  177 ASN C ND2 
5621 N N   . PHE C 178 ? 0.3439 0.2820 0.2927 -0.0711 -0.0812 0.1079  178 PHE C N   
5622 C CA  . PHE C 178 ? 0.3251 0.2665 0.2693 -0.0741 -0.0844 0.1024  178 PHE C CA  
5623 C C   . PHE C 178 ? 0.3650 0.3136 0.3248 -0.0720 -0.0914 0.1083  178 PHE C C   
5624 O O   . PHE C 178 ? 0.3696 0.3216 0.3473 -0.0657 -0.0886 0.1104  178 PHE C O   
5625 C CB  . PHE C 178 ? 0.3377 0.2792 0.2817 -0.0719 -0.0760 0.0913  178 PHE C CB  
5626 C CG  . PHE C 178 ? 0.3207 0.2634 0.2586 -0.0750 -0.0787 0.0858  178 PHE C CG  
5627 C CD1 . PHE C 178 ? 0.3774 0.3156 0.2961 -0.0816 -0.0807 0.0828  178 PHE C CD1 
5628 C CD2 . PHE C 178 ? 0.2793 0.2268 0.2301 -0.0717 -0.0793 0.0842  178 PHE C CD2 
5629 C CE1 . PHE C 178 ? 0.3759 0.3134 0.2883 -0.0849 -0.0828 0.0776  178 PHE C CE1 
5630 C CE2 . PHE C 178 ? 0.3272 0.2746 0.2724 -0.0748 -0.0817 0.0795  178 PHE C CE2 
5631 C CZ  . PHE C 178 ? 0.3327 0.2746 0.2588 -0.0813 -0.0833 0.0760  178 PHE C CZ  
5632 N N   . ASP C 179 ? 0.3510 0.3017 0.3034 -0.0780 -0.1000 0.1105  179 ASP C N   
5633 C CA  . ASP C 179 ? 0.3487 0.3074 0.3148 -0.0777 -0.1078 0.1165  179 ASP C CA  
5634 C C   . ASP C 179 ? 0.3595 0.3199 0.3267 -0.0783 -0.1061 0.1081  179 ASP C C   
5635 O O   . ASP C 179 ? 0.3447 0.3017 0.2961 -0.0849 -0.1088 0.1030  179 ASP C O   
5636 C CB  . ASP C 179 ? 0.3384 0.2987 0.2944 -0.0855 -0.1192 0.1245  179 ASP C CB  
5637 C CG  . ASP C 179 ? 0.3826 0.3528 0.3525 -0.0866 -0.1286 0.1317  179 ASP C CG  
5638 O OD1 . ASP C 179 ? 0.3654 0.3409 0.3539 -0.0807 -0.1254 0.1308  179 ASP C OD1 
5639 O OD2 . ASP C 179 ? 0.4391 0.4121 0.4016 -0.0938 -0.1382 0.1374  179 ASP C OD2 
5640 N N   . PRO C 180 ? 0.3136 0.2781 0.2981 -0.0719 -0.1015 0.1062  180 PRO C N   
5641 C CA  . PRO C 180 ? 0.3120 0.2774 0.2968 -0.0726 -0.0999 0.0985  180 PRO C CA  
5642 C C   . PRO C 180 ? 0.3075 0.2777 0.2936 -0.0782 -0.1097 0.1024  180 PRO C C   
5643 O O   . PRO C 180 ? 0.3150 0.2836 0.2967 -0.0809 -0.1093 0.0960  180 PRO C O   
5644 C CB  . PRO C 180 ? 0.3049 0.2737 0.3078 -0.0646 -0.0927 0.0970  180 PRO C CB  
5645 C CG  . PRO C 180 ? 0.3197 0.2920 0.3365 -0.0605 -0.0943 0.1070  180 PRO C CG  
5646 C CD  . PRO C 180 ? 0.3144 0.2819 0.3176 -0.0641 -0.0971 0.1109  180 PRO C CD  
5647 N N   . ARG C 181 ? 0.3185 0.2945 0.3099 -0.0807 -0.1186 0.1130  181 ARG C N   
5648 C CA  . ARG C 181 ? 0.3595 0.3405 0.3501 -0.0879 -0.1288 0.1166  181 ARG C CA  
5649 C C   . ARG C 181 ? 0.3339 0.3064 0.2992 -0.0972 -0.1311 0.1095  181 ARG C C   
5650 O O   . ARG C 181 ? 0.3567 0.3302 0.3178 -0.1039 -0.1370 0.1084  181 ARG C O   
5651 C CB  . ARG C 181 ? 0.3832 0.3730 0.3835 -0.0894 -0.1387 0.1303  181 ARG C CB  
5652 C CG  . ARG C 181 ? 0.3847 0.3832 0.4118 -0.0802 -0.1365 0.1380  181 ARG C CG  
5653 C CD  . ARG C 181 ? 0.3727 0.3789 0.4100 -0.0802 -0.1416 0.1485  181 ARG C CD  
5654 N NE  . ARG C 181 ? 0.4306 0.4291 0.4520 -0.0818 -0.1410 0.1491  181 ARG C NE  
5655 C CZ  . ARG C 181 ? 0.4732 0.4759 0.4969 -0.0834 -0.1454 0.1566  181 ARG C CZ  
5656 N NH1 . ARG C 181 ? 0.5252 0.5400 0.5669 -0.0834 -0.1505 0.1642  181 ARG C NH1 
5657 N NH2 . ARG C 181 ? 0.4773 0.4725 0.4857 -0.0852 -0.1446 0.1569  181 ARG C NH2 
5658 N N   . GLY C 182 ? 0.3683 0.3321 0.3163 -0.0983 -0.1264 0.1051  182 GLY C N   
5659 C CA  . GLY C 182 ? 0.3736 0.3281 0.2969 -0.1067 -0.1270 0.0978  182 GLY C CA  
5660 C C   . GLY C 182 ? 0.3755 0.3240 0.2944 -0.1058 -0.1196 0.0863  182 GLY C C   
5661 O O   . GLY C 182 ? 0.3992 0.3386 0.2979 -0.1126 -0.1190 0.0796  182 GLY C O   
5662 N N   . LEU C 183 ? 0.3432 0.2956 0.2798 -0.0976 -0.1135 0.0841  183 LEU C N   
5663 C CA  . LEU C 183 ? 0.3146 0.2623 0.2498 -0.0958 -0.1069 0.0746  183 LEU C CA  
5664 C C   . LEU C 183 ? 0.3376 0.2902 0.2844 -0.0973 -0.1118 0.0764  183 LEU C C   
5665 O O   . LEU C 183 ? 0.3318 0.2811 0.2803 -0.0952 -0.1067 0.0698  183 LEU C O   
5666 C CB  . LEU C 183 ? 0.3104 0.2588 0.2553 -0.0864 -0.0965 0.0705  183 LEU C CB  
5667 C CG  . LEU C 183 ? 0.3393 0.2830 0.2728 -0.0853 -0.0907 0.0680  183 LEU C CG  
5668 C CD1 . LEU C 183 ? 0.3269 0.2729 0.2711 -0.0771 -0.0816 0.0648  183 LEU C CD1 
5669 C CD2 . LEU C 183 ? 0.3522 0.2861 0.2636 -0.0908 -0.0880 0.0605  183 LEU C CD2 
5670 N N   . LEU C 184 ? 0.3464 0.3072 0.3014 -0.1012 -0.1218 0.0856  184 LEU C N   
5671 C CA  . LEU C 184 ? 0.3369 0.3040 0.3043 -0.1035 -0.1270 0.0882  184 LEU C CA  
5672 C C   . LEU C 184 ? 0.3386 0.3010 0.2894 -0.1154 -0.1349 0.0868  184 LEU C C   
5673 O O   . LEU C 184 ? 0.3673 0.3276 0.3034 -0.1224 -0.1411 0.0897  184 LEU C O   
5674 C CB  . LEU C 184 ? 0.3567 0.3377 0.3465 -0.1004 -0.1330 0.1000  184 LEU C CB  
5675 C CG  . LEU C 184 ? 0.3707 0.3557 0.3770 -0.0893 -0.1254 0.1024  184 LEU C CG  
5676 C CD1 . LEU C 184 ? 0.3518 0.3495 0.3790 -0.0869 -0.1316 0.1148  184 LEU C CD1 
5677 C CD2 . LEU C 184 ? 0.3492 0.3326 0.3637 -0.0832 -0.1163 0.0952  184 LEU C CD2 
5678 N N   . PRO C 185 ? 0.3420 0.3027 0.2942 -0.1187 -0.1355 0.0829  185 PRO C N   
5679 C CA  . PRO C 185 ? 0.3846 0.3413 0.3225 -0.1312 -0.1440 0.0825  185 PRO C CA  
5680 C C   . PRO C 185 ? 0.3708 0.3423 0.3223 -0.1362 -0.1565 0.0947  185 PRO C C   
5681 O O   . PRO C 185 ? 0.3902 0.3745 0.3643 -0.1288 -0.1574 0.1030  185 PRO C O   
5682 C CB  . PRO C 185 ? 0.3583 0.3088 0.2974 -0.1314 -0.1392 0.0749  185 PRO C CB  
5683 C CG  . PRO C 185 ? 0.3461 0.3064 0.3112 -0.1197 -0.1336 0.0778  185 PRO C CG  
5684 C CD  . PRO C 185 ? 0.3291 0.2919 0.2976 -0.1112 -0.1286 0.0798  185 PRO C CD  
5685 N N   . GLU C 186 ? 0.3860 0.3545 0.3244 -0.1466 -0.1623 0.0952  186 GLU C N   
5686 C CA  . GLU C 186 ? 0.4272 0.4088 0.3790 -0.1489 -0.1695 0.1065  186 GLU C CA  
5687 C C   . GLU C 186 ? 0.4174 0.4102 0.3939 -0.1450 -0.1698 0.1105  186 GLU C C   
5688 O O   . GLU C 186 ? 0.4437 0.4507 0.4417 -0.1409 -0.1727 0.1208  186 GLU C O   
5689 C CB  . GLU C 186 ? 0.5267 0.5015 0.4569 -0.1612 -0.1746 0.1057  186 GLU C CB  
5690 C CG  . GLU C 186 ? 0.6746 0.6627 0.6164 -0.1657 -0.1829 0.1173  186 GLU C CG  
5691 C CD  . GLU C 186 ? 0.8191 0.8001 0.7370 -0.1785 -0.1883 0.1171  186 GLU C CD  
5692 O OE1 . GLU C 186 ? 0.8623 0.8539 0.7872 -0.1826 -0.1956 0.1274  186 GLU C OE1 
5693 O OE2 . GLU C 186 ? 0.8723 0.8371 0.7645 -0.1846 -0.1848 0.1068  186 GLU C OE2 
5694 N N   . SER C 187 ? 0.3597 0.3457 0.3332 -0.1465 -0.1661 0.1025  187 SER C N   
5695 C CA  . SER C 187 ? 0.3659 0.3614 0.3610 -0.1434 -0.1656 0.1056  187 SER C CA  
5696 C C   . SER C 187 ? 0.3488 0.3483 0.3621 -0.1325 -0.1589 0.1044  187 SER C C   
5697 O O   . SER C 187 ? 0.3395 0.3290 0.3437 -0.1299 -0.1532 0.0962  187 SER C O   
5698 C CB  . SER C 187 ? 0.3834 0.3689 0.3664 -0.1506 -0.1645 0.0979  187 SER C CB  
5699 O OG  . SER C 187 ? 0.3981 0.3933 0.4026 -0.1472 -0.1634 0.1011  187 SER C OG  
5700 N N   . LEU C 188 ? 0.3497 0.3635 0.3888 -0.1264 -0.1588 0.1123  188 LEU C N   
5701 C CA  . LEU C 188 ? 0.3335 0.3510 0.3902 -0.1166 -0.1517 0.1111  188 LEU C CA  
5702 C C   . LEU C 188 ? 0.3413 0.3602 0.4083 -0.1166 -0.1482 0.1085  188 LEU C C   
5703 O O   . LEU C 188 ? 0.3475 0.3723 0.4328 -0.1087 -0.1423 0.1097  188 LEU C O   
5704 C CB  . LEU C 188 ? 0.3706 0.4012 0.4489 -0.1080 -0.1513 0.1210  188 LEU C CB  
5705 C CG  . LEU C 188 ? 0.3774 0.4067 0.4482 -0.1061 -0.1533 0.1246  188 LEU C CG  
5706 C CD1 . LEU C 188 ? 0.3977 0.4382 0.4916 -0.0966 -0.1508 0.1341  188 LEU C CD1 
5707 C CD2 . LEU C 188 ? 0.3634 0.3780 0.4153 -0.1031 -0.1456 0.1144  188 LEU C CD2 
5708 N N   . ASP C 189 ? 0.3082 0.3202 0.3621 -0.1251 -0.1508 0.1046  189 ASP C N   
5709 C CA  . ASP C 189 ? 0.2968 0.3061 0.3556 -0.1256 -0.1466 0.1002  189 ASP C CA  
5710 C C   . ASP C 189 ? 0.2756 0.2759 0.3336 -0.1193 -0.1376 0.0924  189 ASP C C   
5711 O O   . ASP C 189 ? 0.2911 0.2794 0.3316 -0.1171 -0.1332 0.0858  189 ASP C O   
5712 C CB  . ASP C 189 ? 0.3241 0.3224 0.3626 -0.1362 -0.1497 0.0948  189 ASP C CB  
5713 C CG  . ASP C 189 ? 0.3847 0.3928 0.4263 -0.1430 -0.1579 0.1027  189 ASP C CG  
5714 O OD1 . ASP C 189 ? 0.4153 0.4388 0.4758 -0.1392 -0.1609 0.1127  189 ASP C OD1 
5715 O OD2 . ASP C 189 ? 0.4203 0.4203 0.4456 -0.1525 -0.1609 0.0990  189 ASP C OD2 
5716 N N   . TYR C 190 ? 0.2706 0.2709 0.2783 -0.0994 -0.1270 0.0695  190 TYR C N   
5717 C CA  . TYR C 190 ? 0.2715 0.2642 0.2786 -0.0901 -0.1143 0.0627  190 TYR C CA  
5718 C C   . TYR C 190 ? 0.2825 0.2780 0.3003 -0.0905 -0.1099 0.0612  190 TYR C C   
5719 O O   . TYR C 190 ? 0.2852 0.2921 0.3159 -0.0963 -0.1157 0.0666  190 TYR C O   
5720 C CB  . TYR C 190 ? 0.2563 0.2580 0.2770 -0.0784 -0.1083 0.0657  190 TYR C CB  
5721 C CG  . TYR C 190 ? 0.2567 0.2793 0.3046 -0.0747 -0.1096 0.0740  190 TYR C CG  
5722 C CD1 . TYR C 190 ? 0.2644 0.2937 0.3266 -0.0703 -0.1022 0.0730  190 TYR C CD1 
5723 C CD2 . TYR C 190 ? 0.2570 0.2930 0.3164 -0.0755 -0.1178 0.0832  190 TYR C CD2 
5724 C CE1 . TYR C 190 ? 0.2698 0.3187 0.3574 -0.0665 -0.1021 0.0804  190 TYR C CE1 
5725 C CE2 . TYR C 190 ? 0.2588 0.3151 0.3456 -0.0713 -0.1181 0.0912  190 TYR C CE2 
5726 C CZ  . TYR C 190 ? 0.2434 0.3058 0.3439 -0.0667 -0.1097 0.0894  190 TYR C CZ  
5727 O OH  . TYR C 190 ? 0.2634 0.3459 0.3907 -0.0627 -0.1091 0.0972  190 TYR C OH  
5728 N N   . TRP C 191 ? 0.2674 0.2526 0.2795 -0.0846 -0.0999 0.0543  191 TRP C N   
5729 C CA  . TRP C 191 ? 0.2556 0.2442 0.2787 -0.0821 -0.0936 0.0535  191 TRP C CA  
5730 C C   . TRP C 191 ? 0.2627 0.2604 0.2989 -0.0706 -0.0852 0.0542  191 TRP C C   
5731 O O   . TRP C 191 ? 0.2536 0.2470 0.2838 -0.0646 -0.0817 0.0517  191 TRP C O   
5732 C CB  . TRP C 191 ? 0.2844 0.2542 0.2910 -0.0841 -0.0889 0.0457  191 TRP C CB  
5733 C CG  . TRP C 191 ? 0.3024 0.2598 0.2940 -0.0955 -0.0957 0.0434  191 TRP C CG  
5734 C CD1 . TRP C 191 ? 0.3060 0.2661 0.3028 -0.1045 -0.1013 0.0462  191 TRP C CD1 
5735 C CD2 . TRP C 191 ? 0.3108 0.2495 0.2786 -0.0996 -0.0969 0.0369  191 TRP C CD2 
5736 N NE1 . TRP C 191 ? 0.3619 0.3055 0.3392 -0.1144 -0.1065 0.0417  191 TRP C NE1 
5737 C CE2 . TRP C 191 ? 0.3518 0.2816 0.3104 -0.1113 -0.1034 0.0356  191 TRP C CE2 
5738 C CE3 . TRP C 191 ? 0.3638 0.2923 0.3169 -0.0948 -0.0926 0.0321  191 TRP C CE3 
5739 C CZ2 . TRP C 191 ? 0.3674 0.2775 0.3009 -0.1183 -0.1058 0.0289  191 TRP C CZ2 
5740 C CZ3 . TRP C 191 ? 0.3636 0.2738 0.2929 -0.1013 -0.0944 0.0260  191 TRP C CZ3 
5741 C CH2 . TRP C 191 ? 0.3959 0.2964 0.3150 -0.1126 -0.1006 0.0241  191 TRP C CH2 
5742 N N   . THR C 192 ? 0.2372 0.2468 0.2904 -0.0678 -0.0813 0.0572  192 THR C N   
5743 C CA  . THR C 192 ? 0.2229 0.2403 0.2870 -0.0575 -0.0730 0.0570  192 THR C CA  
5744 C C   . THR C 192 ? 0.2264 0.2455 0.2957 -0.0555 -0.0660 0.0555  192 THR C C   
5745 O O   . THR C 192 ? 0.2448 0.2673 0.3191 -0.0615 -0.0683 0.0582  192 THR C O   
5746 C CB  . THR C 192 ? 0.1985 0.2335 0.2819 -0.0538 -0.0751 0.0642  192 THR C CB  
5747 O OG1 . THR C 192 ? 0.1995 0.2391 0.2910 -0.0439 -0.0662 0.0627  192 THR C OG1 
5748 C CG2 . THR C 192 ? 0.2171 0.2674 0.3177 -0.0587 -0.0792 0.0712  192 THR C CG2 
5749 N N   . TYR C 193 ? 0.2119 0.2294 0.2805 -0.0476 -0.0579 0.0517  193 TYR C N   
5750 C CA  . TYR C 193 ? 0.2004 0.2203 0.2730 -0.0451 -0.0512 0.0507  193 TYR C CA  
5751 C C   . TYR C 193 ? 0.1979 0.2208 0.2730 -0.0360 -0.0435 0.0478  193 TYR C C   
5752 O O   . TYR C 193 ? 0.2110 0.2294 0.2810 -0.0325 -0.0432 0.0452  193 TYR C O   
5753 C CB  . TYR C 193 ? 0.2145 0.2196 0.2730 -0.0489 -0.0506 0.0468  193 TYR C CB  
5754 C CG  . TYR C 193 ? 0.1920 0.1843 0.2366 -0.0445 -0.0470 0.0405  193 TYR C CG  
5755 C CD1 . TYR C 193 ? 0.2264 0.2086 0.2591 -0.0467 -0.0507 0.0378  193 TYR C CD1 
5756 C CD2 . TYR C 193 ? 0.1829 0.1741 0.2263 -0.0385 -0.0398 0.0376  193 TYR C CD2 
5757 C CE1 . TYR C 193 ? 0.2258 0.1973 0.2469 -0.0425 -0.0466 0.0323  193 TYR C CE1 
5758 C CE2 . TYR C 193 ? 0.1956 0.1771 0.2285 -0.0345 -0.0366 0.0325  193 TYR C CE2 
5759 C CZ  . TYR C 193 ? 0.2159 0.1877 0.2382 -0.0365 -0.0397 0.0299  193 TYR C CZ  
5760 O OH  . TYR C 193 ? 0.2241 0.1876 0.2373 -0.0325 -0.0358 0.0253  193 TYR C OH  
5761 N N   . PRO C 194 ? 0.1835 0.2141 0.2662 -0.0328 -0.0374 0.0483  194 PRO C N   
5762 C CA  . PRO C 194 ? 0.2010 0.2335 0.2841 -0.0252 -0.0302 0.0447  194 PRO C CA  
5763 C C   . PRO C 194 ? 0.1825 0.2033 0.2518 -0.0240 -0.0275 0.0395  194 PRO C C   
5764 O O   . PRO C 194 ? 0.1803 0.1969 0.2450 -0.0268 -0.0271 0.0397  194 PRO C O   
5765 C CB  . PRO C 194 ? 0.1819 0.2270 0.2768 -0.0238 -0.0252 0.0477  194 PRO C CB  
5766 C CG  . PRO C 194 ? 0.2118 0.2579 0.3084 -0.0310 -0.0289 0.0519  194 PRO C CG  
5767 C CD  . PRO C 194 ? 0.1973 0.2367 0.2895 -0.0367 -0.0372 0.0530  194 PRO C CD  
5768 N N   . GLY C 195 ? 0.1655 0.1813 0.2291 -0.0198 -0.0254 0.0353  195 GLY C N   
5769 C CA  . GLY C 195 ? 0.1674 0.1739 0.2198 -0.0182 -0.0229 0.0308  195 GLY C CA  
5770 C C   . GLY C 195 ? 0.1673 0.1744 0.2186 -0.0129 -0.0185 0.0269  195 GLY C C   
5771 O O   . GLY C 195 ? 0.1808 0.1960 0.2396 -0.0097 -0.0151 0.0270  195 GLY C O   
5772 N N   . SER C 196 ? 0.1685 0.1666 0.2104 -0.0120 -0.0182 0.0234  196 SER C N   
5773 C CA  . SER C 196 ? 0.1820 0.1804 0.2220 -0.0080 -0.0141 0.0195  196 SER C CA  
5774 C C   . SER C 196 ? 0.1860 0.1767 0.2199 -0.0076 -0.0150 0.0171  196 SER C C   
5775 O O   . SER C 196 ? 0.1871 0.1711 0.2156 -0.0104 -0.0184 0.0179  196 SER C O   
5776 C CB  . SER C 196 ? 0.1783 0.1758 0.2140 -0.0071 -0.0115 0.0181  196 SER C CB  
5777 O OG  . SER C 196 ? 0.1937 0.1817 0.2217 -0.0083 -0.0129 0.0173  196 SER C OG  
5778 N N   . LEU C 197 ? 0.1691 0.1606 0.2028 -0.0046 -0.0116 0.0139  197 LEU C N   
5779 C CA  . LEU C 197 ? 0.1735 0.1577 0.2005 -0.0044 -0.0114 0.0116  197 LEU C CA  
5780 C C   . LEU C 197 ? 0.1948 0.1733 0.2148 -0.0054 -0.0113 0.0108  197 LEU C C   
5781 O O   . LEU C 197 ? 0.1855 0.1666 0.2065 -0.0048 -0.0102 0.0111  197 LEU C O   
5782 C CB  . LEU C 197 ? 0.1741 0.1608 0.2026 -0.0019 -0.0077 0.0083  197 LEU C CB  
5783 C CG  . LEU C 197 ? 0.1605 0.1508 0.1955 -0.0002 -0.0063 0.0080  197 LEU C CG  
5784 C CD1 . LEU C 197 ? 0.1894 0.1803 0.2236 0.0010  -0.0028 0.0038  197 LEU C CD1 
5785 C CD2 . LEU C 197 ? 0.1904 0.1766 0.2264 -0.0006 -0.0088 0.0103  197 LEU C CD2 
5786 N N   . THR C 198 ? 0.1862 0.1564 0.1989 -0.0066 -0.0120 0.0098  198 THR C N   
5787 C CA  . THR C 198 ? 0.1887 0.1523 0.1951 -0.0067 -0.0106 0.0086  198 THR C CA  
5788 C C   . THR C 198 ? 0.1856 0.1497 0.1915 -0.0037 -0.0066 0.0061  198 THR C C   
5789 O O   . THR C 198 ? 0.1788 0.1375 0.1807 -0.0028 -0.0046 0.0051  198 THR C O   
5790 C CB  . THR C 198 ? 0.2033 0.1563 0.2002 -0.0099 -0.0127 0.0083  198 THR C CB  
5791 O OG1 . THR C 198 ? 0.2104 0.1610 0.2035 -0.0098 -0.0119 0.0071  198 THR C OG1 
5792 C CG2 . THR C 198 ? 0.2027 0.1559 0.2003 -0.0140 -0.0179 0.0112  198 THR C CG2 
5793 N N   . THR C 199 ? 0.1838 0.1542 0.1945 -0.0023 -0.0052 0.0051  199 THR C N   
5794 C CA  . THR C 199 ? 0.1908 0.1643 0.2031 -0.0003 -0.0020 0.0031  199 THR C CA  
5795 C C   . THR C 199 ? 0.1721 0.1548 0.1904 0.0006  -0.0018 0.0029  199 THR C C   
5796 O O   . THR C 199 ? 0.1870 0.1727 0.2081 0.0000  -0.0030 0.0035  199 THR C O   
5797 C CB  . THR C 199 ? 0.1975 0.1686 0.2082 -0.0007 -0.0004 0.0015  199 THR C CB  
5798 O OG1 . THR C 199 ? 0.2017 0.1754 0.2159 -0.0013 -0.0015 0.0016  199 THR C OG1 
5799 C CG2 . THR C 199 ? 0.2058 0.1675 0.2083 -0.0022 -0.0005 0.0017  199 THR C CG2 
5800 N N   . PRO C 200 ? 0.1823 0.1701 0.2028 0.0018  -0.0003 0.0020  200 PRO C N   
5801 C CA  . PRO C 200 ? 0.1518 0.1476 0.1758 0.0016  -0.0001 0.0007  200 PRO C CA  
5802 C C   . PRO C 200 ? 0.1723 0.1670 0.1974 0.0006  0.0004  -0.0015 200 PRO C C   
5803 O O   . PRO C 200 ? 0.1743 0.1639 0.1983 0.0001  0.0010  -0.0022 200 PRO C O   
5804 C CB  . PRO C 200 ? 0.1765 0.1770 0.2023 0.0022  0.0010  0.0000  200 PRO C CB  
5805 C CG  . PRO C 200 ? 0.1853 0.1819 0.2101 0.0043  0.0015  0.0025  200 PRO C CG  
5806 C CD  . PRO C 200 ? 0.1802 0.1667 0.2001 0.0033  0.0016  0.0020  200 PRO C CD  
5807 N N   . PRO C 201 ? 0.1653 0.1641 0.1924 0.0005  0.0007  -0.0024 201 PRO C N   
5808 C CA  . PRO C 201 ? 0.1588 0.1643 0.1861 0.0006  0.0006  -0.0018 201 PRO C CA  
5809 C C   . PRO C 201 ? 0.1546 0.1602 0.1823 0.0009  -0.0005 0.0018  201 PRO C C   
5810 O O   . PRO C 201 ? 0.1705 0.1817 0.1982 0.0008  -0.0001 0.0028  201 PRO C O   
5811 C CB  . PRO C 201 ? 0.1619 0.1704 0.1902 0.0000  0.0026  -0.0054 201 PRO C CB  
5812 C CG  . PRO C 201 ? 0.1595 0.1617 0.1903 0.0007  0.0033  -0.0058 201 PRO C CG  
5813 C CD  . PRO C 201 ? 0.1752 0.1721 0.2044 0.0003  0.0020  -0.0046 201 PRO C CD  
5814 N N   . LEU C 202 ? 0.1657 0.1654 0.1931 0.0007  -0.0020 0.0038  202 LEU C N   
5815 C CA  . LEU C 202 ? 0.1569 0.1558 0.1844 -0.0001 -0.0037 0.0074  202 LEU C CA  
5816 C C   . LEU C 202 ? 0.1620 0.1667 0.1939 -0.0004 -0.0031 0.0086  202 LEU C C   
5817 O O   . LEU C 202 ? 0.1726 0.1798 0.2056 -0.0014 -0.0037 0.0118  202 LEU C O   
5818 C CB  . LEU C 202 ? 0.1730 0.1723 0.1984 0.0003  -0.0039 0.0094  202 LEU C CB  
5819 C CG  . LEU C 202 ? 0.1660 0.1594 0.1884 0.0014  -0.0037 0.0085  202 LEU C CG  
5820 C CD1 . LEU C 202 ? 0.1773 0.1724 0.1999 0.0029  -0.0034 0.0109  202 LEU C CD1 
5821 C CD2 . LEU C 202 ? 0.1774 0.1611 0.1962 0.0001  -0.0048 0.0089  202 LEU C CD2 
5822 N N   . LEU C 203 ? 0.1731 0.1798 0.2081 0.0005  -0.0013 0.0064  203 LEU C N   
5823 C CA  . LEU C 203 ? 0.1548 0.1674 0.1950 0.0011  0.0007  0.0072  203 LEU C CA  
5824 C C   . LEU C 203 ? 0.1525 0.1657 0.1976 0.0000  -0.0018 0.0117  203 LEU C C   
5825 O O   . LEU C 203 ? 0.1595 0.1676 0.2046 -0.0009 -0.0049 0.0131  203 LEU C O   
5826 C CB  . LEU C 203 ? 0.1679 0.1804 0.2108 0.0029  0.0036  0.0037  203 LEU C CB  
5827 C CG  . LEU C 203 ? 0.1781 0.1910 0.2161 0.0028  0.0058  -0.0012 203 LEU C CG  
5828 C CD1 . LEU C 203 ? 0.2072 0.2168 0.2474 0.0040  0.0086  -0.0052 203 LEU C CD1 
5829 C CD2 . LEU C 203 ? 0.1943 0.2142 0.2295 0.0022  0.0079  -0.0016 203 LEU C CD2 
5830 N N   . GLU C 204 ? 0.1636 0.1835 0.2129 -0.0003 -0.0002 0.0140  204 GLU C N   
5831 C CA  . GLU C 204 ? 0.1647 0.1870 0.2198 -0.0023 -0.0027 0.0189  204 GLU C CA  
5832 C C   . GLU C 204 ? 0.1718 0.1988 0.2366 -0.0005 -0.0017 0.0201  204 GLU C C   
5833 O O   . GLU C 204 ? 0.1917 0.2268 0.2644 0.0000  0.0006  0.0226  204 GLU C O   
5834 C CB  . GLU C 204 ? 0.1810 0.2085 0.2363 -0.0040 -0.0014 0.0217  204 GLU C CB  
5835 C CG  . GLU C 204 ? 0.1711 0.1925 0.2179 -0.0053 -0.0033 0.0217  204 GLU C CG  
5836 C CD  . GLU C 204 ? 0.1878 0.2128 0.2337 -0.0070 -0.0024 0.0253  204 GLU C CD  
5837 O OE1 . GLU C 204 ? 0.2037 0.2371 0.2529 -0.0068 0.0012  0.0264  204 GLU C OE1 
5838 O OE2 . GLU C 204 ? 0.1871 0.2058 0.2284 -0.0084 -0.0046 0.0270  204 GLU C OE2 
5839 N N   . SER C 205 ? 0.1628 0.1844 0.2273 0.0006  -0.0035 0.0189  205 SER C N   
5840 C CA  A SER C 205 ? 0.1588 0.1833 0.2326 0.0034  -0.0025 0.0201  205 SER C CA  
5841 C CA  B SER C 205 ? 0.1592 0.1835 0.2328 0.0034  -0.0025 0.0200  205 SER C CA  
5842 C C   . SER C 205 ? 0.1540 0.1762 0.2305 0.0016  -0.0085 0.0244  205 SER C C   
5843 O O   . SER C 205 ? 0.1855 0.2087 0.2692 0.0042  -0.0086 0.0262  205 SER C O   
5844 C CB  A SER C 205 ? 0.1754 0.1954 0.2469 0.0066  0.0014  0.0151  205 SER C CB  
5845 C CB  B SER C 205 ? 0.1724 0.1923 0.2435 0.0065  0.0013  0.0150  205 SER C CB  
5846 O OG  A SER C 205 ? 0.1819 0.1939 0.2442 0.0049  -0.0011 0.0129  205 SER C OG  
5847 O OG  B SER C 205 ? 0.1734 0.1948 0.2392 0.0067  0.0055  0.0108  205 SER C OG  
5848 N N   . VAL C 206 ? 0.1746 0.1933 0.2454 -0.0028 -0.0136 0.0264  206 VAL C N   
5849 C CA  . VAL C 206 ? 0.1832 0.1978 0.2524 -0.0054 -0.0198 0.0296  206 VAL C CA  
5850 C C   . VAL C 206 ? 0.2000 0.2207 0.2755 -0.0095 -0.0245 0.0350  206 VAL C C   
5851 O O   . VAL C 206 ? 0.2091 0.2299 0.2819 -0.0128 -0.0251 0.0353  206 VAL C O   
5852 C CB  . VAL C 206 ? 0.1838 0.1873 0.2390 -0.0080 -0.0218 0.0266  206 VAL C CB  
5853 C CG1 . VAL C 206 ? 0.1922 0.1911 0.2434 -0.0116 -0.0283 0.0298  206 VAL C CG1 
5854 C CG2 . VAL C 206 ? 0.1755 0.1738 0.2253 -0.0047 -0.0175 0.0217  206 VAL C CG2 
5855 N N   . THR C 207 ? 0.1717 0.1971 0.2555 -0.0097 -0.0286 0.0398  207 THR C N   
5856 C CA  . THR C 207 ? 0.1716 0.2013 0.2591 -0.0153 -0.0356 0.0453  207 THR C CA  
5857 C C   . THR C 207 ? 0.2053 0.2241 0.2791 -0.0197 -0.0416 0.0446  207 THR C C   
5858 O O   . THR C 207 ? 0.2008 0.2164 0.2726 -0.0179 -0.0431 0.0453  207 THR C O   
5859 C CB  . THR C 207 ? 0.1695 0.2114 0.2741 -0.0133 -0.0375 0.0518  207 THR C CB  
5860 O OG1 . THR C 207 ? 0.2051 0.2567 0.3216 -0.0090 -0.0306 0.0518  207 THR C OG1 
5861 C CG2 . THR C 207 ? 0.1975 0.2448 0.3059 -0.0203 -0.0459 0.0577  207 THR C CG2 
5862 N N   . TRP C 208 ? 0.1872 0.1989 0.2506 -0.0252 -0.0440 0.0428  208 TRP C N   
5863 C CA  . TRP C 208 ? 0.2075 0.2074 0.2555 -0.0299 -0.0488 0.0411  208 TRP C CA  
5864 C C   . TRP C 208 ? 0.2248 0.2282 0.2747 -0.0363 -0.0576 0.0465  208 TRP C C   
5865 O O   . TRP C 208 ? 0.2120 0.2230 0.2705 -0.0402 -0.0606 0.0501  208 TRP C O   
5866 C CB  . TRP C 208 ? 0.2029 0.1923 0.2390 -0.0327 -0.0468 0.0364  208 TRP C CB  
5867 C CG  . TRP C 208 ? 0.1870 0.1708 0.2174 -0.0272 -0.0399 0.0311  208 TRP C CG  
5868 C CD1 . TRP C 208 ? 0.1879 0.1756 0.2232 -0.0228 -0.0338 0.0292  208 TRP C CD1 
5869 C CD2 . TRP C 208 ? 0.2078 0.1824 0.2272 -0.0259 -0.0386 0.0276  208 TRP C CD2 
5870 N NE1 . TRP C 208 ? 0.1979 0.1800 0.2267 -0.0189 -0.0295 0.0248  208 TRP C NE1 
5871 C CE2 . TRP C 208 ? 0.2089 0.1832 0.2287 -0.0207 -0.0320 0.0239  208 TRP C CE2 
5872 C CE3 . TRP C 208 ? 0.2321 0.1991 0.2409 -0.0290 -0.0424 0.0277  208 TRP C CE3 
5873 C CZ2 . TRP C 208 ? 0.1974 0.1647 0.2090 -0.0185 -0.0288 0.0203  208 TRP C CZ2 
5874 C CZ3 . TRP C 208 ? 0.2339 0.1931 0.2333 -0.0265 -0.0385 0.0239  208 TRP C CZ3 
5875 C CH2 . TRP C 208 ? 0.2099 0.1699 0.2118 -0.0212 -0.0318 0.0204  208 TRP C CH2 
5876 N N   . ILE C 209 ? 0.2212 0.2192 0.2626 -0.0380 -0.0620 0.0474  209 ILE C N   
5877 C CA  . ILE C 209 ? 0.2158 0.2156 0.2552 -0.0450 -0.0716 0.0524  209 ILE C CA  
5878 C C   . ILE C 209 ? 0.2501 0.2339 0.2672 -0.0497 -0.0734 0.0476  209 ILE C C   
5879 O O   . ILE C 209 ? 0.2565 0.2344 0.2654 -0.0469 -0.0717 0.0462  209 ILE C O   
5880 C CB  . ILE C 209 ? 0.2406 0.2506 0.2919 -0.0419 -0.0752 0.0593  209 ILE C CB  
5881 C CG1 . ILE C 209 ? 0.2570 0.2822 0.3308 -0.0363 -0.0716 0.0632  209 ILE C CG1 
5882 C CG2 . ILE C 209 ? 0.2401 0.2525 0.2880 -0.0497 -0.0863 0.0651  209 ILE C CG2 
5883 C CD1 . ILE C 209 ? 0.2453 0.2794 0.3332 -0.0303 -0.0723 0.0694  209 ILE C CD1 
5884 N N   . VAL C 210 ? 0.2504 0.2262 0.2571 -0.0566 -0.0759 0.0447  210 VAL C N   
5885 C CA  . VAL C 210 ? 0.2655 0.2243 0.2500 -0.0607 -0.0758 0.0388  210 VAL C CA  
5886 C C   . VAL C 210 ? 0.2907 0.2471 0.2656 -0.0705 -0.0860 0.0417  210 VAL C C   
5887 O O   . VAL C 210 ? 0.2779 0.2382 0.2573 -0.0771 -0.0917 0.0441  210 VAL C O   
5888 C CB  . VAL C 210 ? 0.2833 0.2317 0.2612 -0.0611 -0.0702 0.0326  210 VAL C CB  
5889 C CG1 . VAL C 210 ? 0.2794 0.2094 0.2345 -0.0649 -0.0691 0.0263  210 VAL C CG1 
5890 C CG2 . VAL C 210 ? 0.2548 0.2066 0.2416 -0.0520 -0.0610 0.0304  210 VAL C CG2 
5891 N N   . LEU C 211 ? 0.2807 0.2319 0.2430 -0.0719 -0.0889 0.0421  211 LEU C N   
5892 C CA  . LEU C 211 ? 0.3006 0.2504 0.2524 -0.0816 -0.0995 0.0454  211 LEU C CA  
5893 C C   . LEU C 211 ? 0.3323 0.2656 0.2639 -0.0901 -0.1005 0.0384  211 LEU C C   
5894 O O   . LEU C 211 ? 0.3526 0.2715 0.2712 -0.0877 -0.0925 0.0306  211 LEU C O   
5895 C CB  . LEU C 211 ? 0.3041 0.2521 0.2462 -0.0810 -0.1020 0.0481  211 LEU C CB  
5896 C CG  . LEU C 211 ? 0.3050 0.2673 0.2659 -0.0732 -0.1019 0.0556  211 LEU C CG  
5897 C CD1 . LEU C 211 ? 0.3015 0.2594 0.2489 -0.0747 -0.1058 0.0589  211 LEU C CD1 
5898 C CD2 . LEU C 211 ? 0.3155 0.2955 0.2978 -0.0747 -0.1094 0.0641  211 LEU C CD2 
5899 N N   . LYS C 212 ? 0.3422 0.2777 0.2721 -0.1001 -0.1102 0.0412  212 LYS C N   
5900 C CA  . LYS C 212 ? 0.3428 0.2613 0.2529 -0.1091 -0.1116 0.0343  212 LYS C CA  
5901 C C   . LYS C 212 ? 0.3912 0.2936 0.2738 -0.1135 -0.1122 0.0292  212 LYS C C   
5902 O O   . LYS C 212 ? 0.4231 0.3066 0.2871 -0.1159 -0.1068 0.0204  212 LYS C O   
5903 C CB  . LYS C 212 ? 0.3863 0.3126 0.3031 -0.1196 -0.1225 0.0390  212 LYS C CB  
5904 C CG  . LYS C 212 ? 0.4197 0.3277 0.3149 -0.1310 -0.1259 0.0323  212 LYS C CG  
5905 C CD  . LYS C 212 ? 0.5041 0.4206 0.4102 -0.1410 -0.1351 0.0368  212 LYS C CD  
5906 C CE  . LYS C 212 ? 0.5811 0.4776 0.4639 -0.1520 -0.1374 0.0295  212 LYS C CE  
5907 N NZ  . LYS C 212 ? 0.6202 0.5270 0.5143 -0.1591 -0.1441 0.0350  212 LYS C NZ  
5908 N N   . GLU C 213 ? 0.3613 0.2701 0.2402 -0.1147 -0.1183 0.0347  213 GLU C N   
5909 C CA  . GLU C 213 ? 0.3947 0.2890 0.2460 -0.1200 -0.1195 0.0307  213 GLU C CA  
5910 C C   . GLU C 213 ? 0.3932 0.2802 0.2382 -0.1105 -0.1079 0.0264  213 GLU C C   
5911 O O   . GLU C 213 ? 0.3785 0.2772 0.2386 -0.1023 -0.1056 0.0319  213 GLU C O   
5912 C CB  . GLU C 213 ? 0.4079 0.3124 0.2567 -0.1263 -0.1319 0.0395  213 GLU C CB  
5913 C CG  . GLU C 213 ? 0.4677 0.3572 0.2853 -0.1330 -0.1337 0.0357  213 GLU C CG  
5914 C CD  . GLU C 213 ? 0.5254 0.4245 0.3379 -0.1409 -0.1478 0.0451  213 GLU C CD  
5915 O OE1 . GLU C 213 ? 0.5134 0.4324 0.3495 -0.1384 -0.1547 0.0558  213 GLU C OE1 
5916 O OE2 . GLU C 213 ? 0.6163 0.5035 0.4048 -0.1474 -0.1482 0.0418  213 GLU C OE2 
5917 N N   . PRO C 214 ? 0.4032 0.2714 0.2271 -0.1113 -0.1002 0.0170  214 PRO C N   
5918 C CA  . PRO C 214 ? 0.4161 0.2790 0.2348 -0.1028 -0.0894 0.0139  214 PRO C CA  
5919 C C   . PRO C 214 ? 0.4089 0.2720 0.2136 -0.1056 -0.0934 0.0179  214 PRO C C   
5920 O O   . PRO C 214 ? 0.4686 0.3308 0.2600 -0.1153 -0.1037 0.0208  214 PRO C O   
5921 C CB  . PRO C 214 ? 0.4436 0.2863 0.2439 -0.1037 -0.0804 0.0029  214 PRO C CB  
5922 C CG  . PRO C 214 ? 0.5547 0.3912 0.3514 -0.1126 -0.0866 0.0003  214 PRO C CG  
5923 C CD  . PRO C 214 ? 0.4665 0.3164 0.2693 -0.1202 -0.1006 0.0088  214 PRO C CD  
5924 N N   . ILE C 215 ? 0.4080 0.2721 0.2150 -0.0973 -0.0849 0.0182  215 ILE C N   
5925 C CA  . ILE C 215 ? 0.4124 0.2717 0.2013 -0.0994 -0.0851 0.0200  215 ILE C CA  
5926 C C   . ILE C 215 ? 0.4539 0.2946 0.2194 -0.1003 -0.0748 0.0098  215 ILE C C   
5927 O O   . ILE C 215 ? 0.4615 0.2958 0.2311 -0.0952 -0.0653 0.0027  215 ILE C O   
5928 C CB  . ILE C 215 ? 0.3970 0.2681 0.2022 -0.0910 -0.0825 0.0271  215 ILE C CB  
5929 C CG1 . ILE C 215 ? 0.4022 0.2730 0.2199 -0.0808 -0.0696 0.0221  215 ILE C CG1 
5930 C CG2 . ILE C 215 ? 0.3999 0.2885 0.2274 -0.0903 -0.0926 0.0372  215 ILE C CG2 
5931 C CD1 . ILE C 215 ? 0.4142 0.2945 0.2468 -0.0730 -0.0660 0.0280  215 ILE C CD1 
5932 N N   . SER C 216 ? 0.4959 0.3275 0.2361 -0.1071 -0.0768 0.0092  216 SER C N   
5933 C CA  A SER C 216 ? 0.5251 0.3383 0.2401 -0.1088 -0.0670 -0.0005 216 SER C CA  
5934 C CA  B SER C 216 ? 0.5236 0.3368 0.2390 -0.1086 -0.0669 -0.0006 216 SER C CA  
5935 C C   . SER C 216 ? 0.5629 0.3768 0.2764 -0.1021 -0.0574 0.0007  216 SER C C   
5936 O O   . SER C 216 ? 0.5956 0.4166 0.3073 -0.1034 -0.0625 0.0088  216 SER C O   
5937 C CB  A SER C 216 ? 0.5708 0.3725 0.2555 -0.1214 -0.0746 -0.0025 216 SER C CB  
5938 C CB  B SER C 216 ? 0.5741 0.3749 0.2592 -0.1213 -0.0740 -0.0033 216 SER C CB  
5939 O OG  A SER C 216 ? 0.5915 0.3766 0.2505 -0.1223 -0.0641 -0.0105 216 SER C OG  
5940 O OG  B SER C 216 ? 0.5546 0.3504 0.2383 -0.1280 -0.0804 -0.0073 216 SER C OG  
5941 N N   . VAL C 217 ? 0.5112 0.3176 0.2250 -0.0953 -0.0437 -0.0068 217 VAL C N   
5942 C CA  . VAL C 217 ? 0.5241 0.3300 0.2354 -0.0897 -0.0330 -0.0069 217 VAL C CA  
5943 C C   . VAL C 217 ? 0.5351 0.3232 0.2231 -0.0908 -0.0216 -0.0172 217 VAL C C   
5944 O O   . VAL C 217 ? 0.5542 0.3309 0.2347 -0.0931 -0.0198 -0.0249 217 VAL C O   
5945 C CB  . VAL C 217 ? 0.5280 0.3457 0.2676 -0.0789 -0.0267 -0.0050 217 VAL C CB  
5946 C CG1 . VAL C 217 ? 0.5307 0.3646 0.2921 -0.0775 -0.0369 0.0045  217 VAL C CG1 
5947 C CG2 . VAL C 217 ? 0.4914 0.3037 0.2387 -0.0747 -0.0201 -0.0128 217 VAL C CG2 
5948 N N   . SER C 218 ? 0.5379 0.3231 0.2147 -0.0893 -0.0130 -0.0173 218 SER C N   
5949 C CA  . SER C 218 ? 0.5598 0.3284 0.2152 -0.0896 -0.0006 -0.0272 218 SER C CA  
5950 C C   . SER C 218 ? 0.5293 0.2991 0.2029 -0.0789 0.0126  -0.0321 218 SER C C   
5951 O O   . SER C 218 ? 0.4900 0.2740 0.1888 -0.0717 0.0138  -0.0270 218 SER C O   
5952 C CB  . SER C 218 ? 0.5778 0.3420 0.2111 -0.0931 0.0041  -0.0256 218 SER C CB  
5953 O OG  . SER C 218 ? 0.5548 0.3304 0.2048 -0.0857 0.0108  -0.0202 218 SER C OG  
5954 N N   . SER C 219 ? 0.5099 0.3630 0.2331 -0.0775 -0.0014 -0.0542 219 SER C N   
5955 C CA  . SER C 219 ? 0.4939 0.3500 0.2385 -0.0661 0.0118  -0.0579 219 SER C CA  
5956 C C   . SER C 219 ? 0.4664 0.3455 0.2143 -0.0640 0.0254  -0.0492 219 SER C C   
5957 O O   . SER C 219 ? 0.4571 0.3463 0.2320 -0.0586 0.0302  -0.0420 219 SER C O   
5958 C CB  . SER C 219 ? 0.5702 0.4104 0.3037 -0.0575 0.0177  -0.0799 219 SER C CB  
5959 O OG  . SER C 219 ? 0.6755 0.4886 0.4108 -0.0605 0.0033  -0.0866 219 SER C OG  
5960 N N   . GLU C 220 ? 0.5099 0.3972 0.2294 -0.0705 0.0298  -0.0481 220 GLU C N   
5961 C CA  . GLU C 220 ? 0.5080 0.4162 0.2276 -0.0736 0.0414  -0.0370 220 GLU C CA  
5962 C C   . GLU C 220 ? 0.4897 0.4002 0.2300 -0.0771 0.0322  -0.0179 220 GLU C C   
5963 O O   . GLU C 220 ? 0.4636 0.3874 0.2240 -0.0755 0.0399  -0.0109 220 GLU C O   
5964 C CB  . GLU C 220 ? 0.5833 0.4967 0.2625 -0.0841 0.0445  -0.0354 220 GLU C CB  
5965 C CG  . GLU C 220 ? 0.7446 0.6604 0.3976 -0.0800 0.0559  -0.0575 220 GLU C CG  
5966 C CD  . GLU C 220 ? 0.8089 0.7009 0.4371 -0.0816 0.0412  -0.0705 220 GLU C CD  
5967 O OE1 . GLU C 220 ? 0.8619 0.7561 0.4503 -0.0876 0.0433  -0.0781 220 GLU C OE1 
5968 O OE2 . GLU C 220 ? 0.7562 0.6293 0.4027 -0.0790 0.0272  -0.0727 220 GLU C OE2 
5969 N N   . GLN C 221 ? 0.4643 0.3639 0.2026 -0.0808 0.0150  -0.0111 221 GLN C N   
5970 C CA  . GLN C 221 ? 0.4408 0.3430 0.1997 -0.0804 0.0055  0.0031  221 GLN C CA  
5971 C C   . GLN C 221 ? 0.4191 0.3272 0.2120 -0.0722 0.0090  0.0016  221 GLN C C   
5972 O O   . GLN C 221 ? 0.3979 0.3135 0.2072 -0.0706 0.0107  0.0095  221 GLN C O   
5973 C CB  . GLN C 221 ? 0.4456 0.3413 0.1999 -0.0826 -0.0134 0.0073  221 GLN C CB  
5974 C CG  . GLN C 221 ? 0.4546 0.3439 0.1767 -0.0905 -0.0221 0.0151  221 GLN C CG  
5975 C CD  . GLN C 221 ? 0.4864 0.3727 0.2073 -0.0905 -0.0427 0.0180  221 GLN C CD  
5976 O OE1 . GLN C 221 ? 0.4701 0.3594 0.2004 -0.0896 -0.0479 0.0093  221 GLN C OE1 
5977 N NE2 . GLN C 221 ? 0.4708 0.3514 0.1820 -0.0916 -0.0563 0.0309  221 GLN C NE2 
5978 N N   . VAL C 222 ? 0.3851 0.2877 0.1872 -0.0680 0.0083  -0.0076 222 VAL C N   
5979 C CA  . VAL C 222 ? 0.3606 0.2676 0.1908 -0.0616 0.0100  -0.0064 222 VAL C CA  
5980 C C   . VAL C 222 ? 0.3784 0.2943 0.2193 -0.0555 0.0236  -0.0085 222 VAL C C   
5981 O O   . VAL C 222 ? 0.3608 0.2855 0.2240 -0.0513 0.0242  -0.0033 222 VAL C O   
5982 C CB  . VAL C 222 ? 0.4010 0.2957 0.2359 -0.0611 0.0049  -0.0130 222 VAL C CB  
5983 C CG1 . VAL C 222 ? 0.3901 0.2903 0.2511 -0.0568 0.0040  -0.0070 222 VAL C CG1 
5984 C CG2 . VAL C 222 ? 0.4673 0.3588 0.2932 -0.0694 -0.0078 -0.0117 222 VAL C CG2 
5985 N N   . SER C 223 ? 0.3874 0.3047 0.2137 -0.0543 0.0345  -0.0180 223 SER C N   
5986 C CA  . SER C 223 ? 0.3909 0.3251 0.2321 -0.0478 0.0482  -0.0215 223 SER C CA  
5987 C C   . SER C 223 ? 0.3760 0.3267 0.2263 -0.0544 0.0503  -0.0079 223 SER C C   
5988 O O   . SER C 223 ? 0.3509 0.3178 0.2241 -0.0503 0.0566  -0.0067 223 SER C O   
5989 C CB  . SER C 223 ? 0.4429 0.3836 0.2659 -0.0450 0.0616  -0.0358 223 SER C CB  
5990 O OG  . SER C 223 ? 0.4991 0.4507 0.2985 -0.0570 0.0667  -0.0290 223 SER C OG  
5991 N N   . LYS C 224 ? 0.3605 0.3057 0.1933 -0.0649 0.0432  0.0023  224 LYS C N   
5992 C CA  . LYS C 224 ? 0.3633 0.3154 0.2034 -0.0723 0.0410  0.0156  224 LYS C CA  
5993 C C   . LYS C 224 ? 0.3312 0.2826 0.1976 -0.0665 0.0321  0.0193  224 LYS C C   
5994 O O   . LYS C 224 ? 0.3273 0.2882 0.2088 -0.0693 0.0331  0.0252  224 LYS C O   
5995 C CB  . LYS C 224 ? 0.3804 0.3191 0.1949 -0.0828 0.0307  0.0261  224 LYS C CB  
5996 C CG  . LYS C 224 ? 0.4738 0.4153 0.2560 -0.0915 0.0392  0.0248  224 LYS C CG  
5997 C CD  . LYS C 224 ? 0.5401 0.5055 0.3247 -0.0984 0.0567  0.0267  224 LYS C CD  
5998 C CE  . LYS C 224 ? 0.6619 0.6365 0.4106 -0.1080 0.0678  0.0249  224 LYS C CE  
5999 N NZ  . LYS C 224 ? 0.7222 0.7320 0.4776 -0.1123 0.0897  0.0216  224 LYS C NZ  
6000 N N   . PHE C 225 ? 0.3051 0.2477 0.1765 -0.0599 0.0233  0.0158  225 PHE C N   
6001 C CA  . PHE C 225 ? 0.3271 0.2741 0.2207 -0.0541 0.0171  0.0179  225 PHE C CA  
6002 C C   . PHE C 225 ? 0.2948 0.2546 0.2088 -0.0488 0.0254  0.0154  225 PHE C C   
6003 O O   . PHE C 225 ? 0.2873 0.2552 0.2178 -0.0474 0.0219  0.0191  225 PHE C O   
6004 C CB  . PHE C 225 ? 0.3188 0.2609 0.2144 -0.0503 0.0099  0.0149  225 PHE C CB  
6005 C CG  . PHE C 225 ? 0.3242 0.2616 0.2088 -0.0531 -0.0010 0.0167  225 PHE C CG  
6006 C CD1 . PHE C 225 ? 0.3769 0.3085 0.2489 -0.0567 -0.0068 0.0213  225 PHE C CD1 
6007 C CD2 . PHE C 225 ? 0.3526 0.2922 0.2406 -0.0529 -0.0064 0.0147  225 PHE C CD2 
6008 C CE1 . PHE C 225 ? 0.3858 0.3145 0.2504 -0.0565 -0.0189 0.0222  225 PHE C CE1 
6009 C CE2 . PHE C 225 ? 0.4041 0.3469 0.2871 -0.0546 -0.0168 0.0152  225 PHE C CE2 
6010 C CZ  . PHE C 225 ? 0.3703 0.3078 0.2425 -0.0545 -0.0236 0.0182  225 PHE C CZ  
6011 N N   . ARG C 226 ? 0.2931 0.2547 0.2066 -0.0443 0.0346  0.0075  226 ARG C N   
6012 C CA  . ARG C 226 ? 0.2818 0.2549 0.2173 -0.0352 0.0398  0.0036  226 ARG C CA  
6013 C C   . ARG C 226 ? 0.2875 0.2838 0.2359 -0.0382 0.0486  0.0055  226 ARG C C   
6014 O O   . ARG C 226 ? 0.2997 0.3114 0.2713 -0.0304 0.0511  0.0031  226 ARG C O   
6015 C CB  . ARG C 226 ? 0.2913 0.2553 0.2232 -0.0263 0.0446  -0.0080 226 ARG C CB  
6016 C CG  . ARG C 226 ? 0.3188 0.2581 0.2378 -0.0274 0.0346  -0.0090 226 ARG C CG  
6017 C CD  . ARG C 226 ? 0.3266 0.2504 0.2464 -0.0172 0.0356  -0.0208 226 ARG C CD  
6018 N NE  . ARG C 226 ? 0.3522 0.2509 0.2583 -0.0228 0.0251  -0.0208 226 ARG C NE  
6019 C CZ  . ARG C 226 ? 0.3653 0.2499 0.2495 -0.0274 0.0244  -0.0295 226 ARG C CZ  
6020 N NH1 . ARG C 226 ? 0.3940 0.2859 0.2632 -0.0257 0.0349  -0.0400 226 ARG C NH1 
6021 N NH2 . ARG C 226 ? 0.3894 0.2554 0.2652 -0.0355 0.0132  -0.0275 226 ARG C NH2 
6022 N N   . LYS C 227 ? 0.2847 0.2846 0.2194 -0.0506 0.0515  0.0114  227 LYS C N   
6023 C CA  . LYS C 227 ? 0.2860 0.3095 0.2336 -0.0586 0.0587  0.0163  227 LYS C CA  
6024 C C   . LYS C 227 ? 0.2696 0.2917 0.2310 -0.0642 0.0470  0.0255  227 LYS C C   
6025 O O   . LYS C 227 ? 0.2841 0.3258 0.2608 -0.0726 0.0503  0.0302  227 LYS C O   
6026 C CB  . LYS C 227 ? 0.3234 0.3503 0.2473 -0.0729 0.0665  0.0212  227 LYS C CB  
6027 C CG  . LYS C 227 ? 0.3622 0.3957 0.2700 -0.0676 0.0799  0.0092  227 LYS C CG  
6028 C CD  . LYS C 227 ? 0.4996 0.5357 0.3776 -0.0844 0.0856  0.0169  227 LYS C CD  
6029 C CE  . LYS C 227 ? 0.5720 0.6399 0.4620 -0.0986 0.0963  0.0259  227 LYS C CE  
6030 N NZ  . LYS C 227 ? 0.6423 0.7137 0.4998 -0.1187 0.1021  0.0372  227 LYS C NZ  
6031 N N   . LEU C 228 ? 0.2601 0.2620 0.2164 -0.0606 0.0336  0.0271  228 LEU C N   
6032 C CA  . LEU C 228 ? 0.2492 0.2512 0.2196 -0.0615 0.0224  0.0307  228 LEU C CA  
6033 C C   . LEU C 228 ? 0.2407 0.2610 0.2357 -0.0526 0.0236  0.0270  228 LEU C C   
6034 O O   . LEU C 228 ? 0.2359 0.2615 0.2363 -0.0425 0.0299  0.0216  228 LEU C O   
6035 C CB  . LEU C 228 ? 0.2612 0.2444 0.2211 -0.0564 0.0097  0.0298  228 LEU C CB  
6036 C CG  . LEU C 228 ? 0.2837 0.2482 0.2219 -0.0628 0.0044  0.0338  228 LEU C CG  
6037 C CD1 . LEU C 228 ? 0.3051 0.2602 0.2370 -0.0542 -0.0052 0.0298  228 LEU C CD1 
6038 C CD2 . LEU C 228 ? 0.3164 0.2722 0.2550 -0.0725 -0.0042 0.0404  228 LEU C CD2 
6039 N N   . ASN C 229 ? 0.2299 0.2563 0.2387 -0.0557 0.0147  0.0296  229 ASN C N   
6040 C CA  . ASN C 229 ? 0.2208 0.2655 0.2525 -0.0486 0.0119  0.0278  229 ASN C CA  
6041 C C   . ASN C 229 ? 0.2265 0.2625 0.2556 -0.0448 -0.0023 0.0272  229 ASN C C   
6042 O O   . ASN C 229 ? 0.2234 0.2458 0.2423 -0.0504 -0.0109 0.0273  229 ASN C O   
6043 C CB  . ASN C 229 ? 0.2435 0.3136 0.2974 -0.0582 0.0149  0.0304  229 ASN C CB  
6044 C CG  . ASN C 229 ? 0.2968 0.3902 0.3601 -0.0581 0.0317  0.0283  229 ASN C CG  
6045 O OD1 . ASN C 229 ? 0.3094 0.3970 0.3626 -0.0488 0.0400  0.0229  229 ASN C OD1 
6046 N ND2 . ASN C 229 ? 0.3504 0.4731 0.4344 -0.0686 0.0364  0.0312  229 ASN C ND2 
6047 N N   . PHE C 230 ? 0.2070 0.2508 0.2446 -0.0347 -0.0055 0.0264  230 PHE C N   
6048 C CA  . PHE C 230 ? 0.2091 0.2523 0.2433 -0.0320 -0.0179 0.0258  230 PHE C CA  
6049 C C   . PHE C 230 ? 0.2284 0.2830 0.2763 -0.0379 -0.0267 0.0248  230 PHE C C   
6050 O O   . PHE C 230 ? 0.2460 0.2951 0.2857 -0.0386 -0.0376 0.0210  230 PHE C O   
6051 C CB  . PHE C 230 ? 0.2126 0.2612 0.2498 -0.0225 -0.0206 0.0285  230 PHE C CB  
6052 C CG  . PHE C 230 ? 0.2098 0.2445 0.2322 -0.0190 -0.0165 0.0305  230 PHE C CG  
6053 C CD1 . PHE C 230 ? 0.2032 0.2299 0.2072 -0.0216 -0.0180 0.0294  230 PHE C CD1 
6054 C CD2 . PHE C 230 ? 0.2249 0.2558 0.2535 -0.0124 -0.0131 0.0328  230 PHE C CD2 
6055 C CE1 . PHE C 230 ? 0.2191 0.2370 0.2120 -0.0213 -0.0155 0.0326  230 PHE C CE1 
6056 C CE2 . PHE C 230 ? 0.2177 0.2320 0.2325 -0.0116 -0.0124 0.0357  230 PHE C CE2 
6057 C CZ  . PHE C 230 ? 0.2216 0.2309 0.2190 -0.0178 -0.0133 0.0366  230 PHE C CZ  
6058 N N   . ASN C 231 ? 0.2067 0.2802 0.2766 -0.0414 -0.0228 0.0268  231 ASN C N   
6059 C CA  . ASN C 231 ? 0.2106 0.3004 0.2986 -0.0483 -0.0326 0.0266  231 ASN C CA  
6060 C C   . ASN C 231 ? 0.2402 0.3183 0.3239 -0.0643 -0.0374 0.0268  231 ASN C C   
6061 O O   . ASN C 231 ? 0.2438 0.3051 0.3138 -0.0705 -0.0313 0.0291  231 ASN C O   
6062 C CB  . ASN C 231 ? 0.2164 0.3370 0.3340 -0.0465 -0.0263 0.0285  231 ASN C CB  
6063 C CG  . ASN C 231 ? 0.2089 0.3370 0.3303 -0.0522 -0.0093 0.0296  231 ASN C CG  
6064 O OD1 . ASN C 231 ? 0.2077 0.3266 0.3181 -0.0436 0.0007  0.0278  231 ASN C OD1 
6065 N ND2 . ASN C 231 ? 0.2368 0.3825 0.3723 -0.0685 -0.0066 0.0327  231 ASN C ND2 
6066 N N   . GLY C 232 ? 0.2605 0.3447 0.3548 -0.0716 -0.0511 0.0248  232 GLY C N   
6067 C CA  . GLY C 232 ? 0.2912 0.3650 0.3875 -0.0901 -0.0582 0.0268  232 GLY C CA  
6068 C C   . GLY C 232 ? 0.2744 0.3768 0.3958 -0.1047 -0.0488 0.0346  232 GLY C C   
6069 O O   . GLY C 232 ? 0.2721 0.4082 0.4158 -0.0979 -0.0397 0.0353  232 GLY C O   
6070 N N   . GLU C 233 ? 0.3080 0.3980 0.4267 -0.1253 -0.0517 0.0409  233 GLU C N   
6071 C CA  . GLU C 233 ? 0.3836 0.5067 0.5266 -0.1444 -0.0425 0.0499  233 GLU C CA  
6072 C C   . GLU C 233 ? 0.3274 0.4887 0.5047 -0.1466 -0.0498 0.0474  233 GLU C C   
6073 O O   . GLU C 233 ? 0.3566 0.5062 0.5341 -0.1468 -0.0692 0.0418  233 GLU C O   
6074 C CB  . GLU C 233 ? 0.5033 0.6006 0.6344 -0.1705 -0.0496 0.0599  233 GLU C CB  
6075 C CG  . GLU C 233 ? 0.6147 0.7447 0.7596 -0.1920 -0.0332 0.0726  233 GLU C CG  
6076 C CD  . GLU C 233 ? 0.7692 0.8677 0.8960 -0.2204 -0.0409 0.0870  233 GLU C CD  
6077 O OE1 . GLU C 233 ? 0.8104 0.8556 0.9083 -0.2169 -0.0554 0.0862  233 GLU C OE1 
6078 O OE2 . GLU C 233 ? 0.8265 0.9512 0.9655 -0.2400 -0.0324 0.0968  233 GLU C OE2 
6079 N N   . GLY C 234 ? 0.3097 0.5196 0.5166 -0.1461 -0.0350 0.0496  234 GLY C N   
6080 C CA  . GLY C 234 ? 0.3018 0.5544 0.5462 -0.1463 -0.0424 0.0474  234 GLY C CA  
6081 C C   . GLY C 234 ? 0.2917 0.5550 0.5440 -0.1186 -0.0467 0.0395  234 GLY C C   
6082 O O   . GLY C 234 ? 0.2936 0.5937 0.5779 -0.1159 -0.0548 0.0379  234 GLY C O   
6083 N N   . GLU C 235 ? 0.2916 0.5253 0.5168 -0.0992 -0.0425 0.0359  235 GLU C N   
6084 C CA  . GLU C 235 ? 0.2637 0.5020 0.4917 -0.0746 -0.0455 0.0318  235 GLU C CA  
6085 C C   . GLU C 235 ? 0.2893 0.5389 0.5227 -0.0594 -0.0265 0.0303  235 GLU C C   
6086 O O   . GLU C 235 ? 0.2611 0.5060 0.4843 -0.0667 -0.0107 0.0312  235 GLU C O   
6087 C CB  . GLU C 235 ? 0.3062 0.5030 0.4982 -0.0664 -0.0557 0.0294  235 GLU C CB  
6088 C CG  . GLU C 235 ? 0.3405 0.5209 0.5215 -0.0796 -0.0737 0.0267  235 GLU C CG  
6089 C CD  . GLU C 235 ? 0.4068 0.5548 0.5533 -0.0689 -0.0814 0.0216  235 GLU C CD  
6090 O OE1 . GLU C 235 ? 0.3612 0.4900 0.4877 -0.0609 -0.0703 0.0222  235 GLU C OE1 
6091 O OE2 . GLU C 235 ? 0.4487 0.5944 0.5885 -0.0687 -0.0983 0.0163  235 GLU C OE2 
6092 N N   . PRO C 236 ? 0.2813 0.5435 0.5291 -0.0379 -0.0291 0.0276  236 PRO C N   
6093 C CA  . PRO C 236 ? 0.2781 0.5474 0.5318 -0.0214 -0.0129 0.0230  236 PRO C CA  
6094 C C   . PRO C 236 ? 0.2358 0.4635 0.4511 -0.0209 -0.0038 0.0226  236 PRO C C   
6095 O O   . PRO C 236 ? 0.2527 0.4462 0.4401 -0.0224 -0.0131 0.0256  236 PRO C O   
6096 C CB  . PRO C 236 ? 0.3203 0.5952 0.5897 0.0019  -0.0251 0.0218  236 PRO C CB  
6097 C CG  . PRO C 236 ? 0.3247 0.6236 0.6149 -0.0058 -0.0436 0.0254  236 PRO C CG  
6098 C CD  . PRO C 236 ? 0.3089 0.5826 0.5712 -0.0282 -0.0484 0.0285  236 PRO C CD  
6099 N N   . GLU C 237 ? 0.2855 0.5211 0.5002 -0.0195 0.0146  0.0181  237 GLU C N   
6100 C CA  . GLU C 237 ? 0.3249 0.5251 0.5040 -0.0223 0.0229  0.0177  237 GLU C CA  
6101 C C   . GLU C 237 ? 0.2971 0.4651 0.4592 -0.0050 0.0167  0.0159  237 GLU C C   
6102 O O   . GLU C 237 ? 0.3063 0.4806 0.4837 0.0133  0.0159  0.0110  237 GLU C O   
6103 C CB  . GLU C 237 ? 0.4091 0.6280 0.5891 -0.0246 0.0436  0.0123  237 GLU C CB  
6104 C CG  . GLU C 237 ? 0.5231 0.7060 0.6673 -0.0227 0.0503  0.0098  237 GLU C CG  
6105 C CD  . GLU C 237 ? 0.6417 0.8387 0.7748 -0.0337 0.0686  0.0078  237 GLU C CD  
6106 O OE1 . GLU C 237 ? 0.6635 0.8722 0.7949 -0.0553 0.0711  0.0167  237 GLU C OE1 
6107 O OE2 . GLU C 237 ? 0.6874 0.8818 0.8111 -0.0216 0.0796  -0.0025 237 GLU C OE2 
6108 N N   . GLU C 238 ? 0.2869 0.4015 0.3549 -0.0106 0.0420  0.0670  238 GLU C N   
6109 C CA  . GLU C 238 ? 0.2710 0.3638 0.3218 -0.0029 0.0424  0.0569  238 GLU C CA  
6110 C C   . GLU C 238 ? 0.2735 0.3388 0.3086 -0.0046 0.0416  0.0503  238 GLU C C   
6111 O O   . GLU C 238 ? 0.2781 0.3323 0.3149 -0.0147 0.0331  0.0437  238 GLU C O   
6112 C CB  . GLU C 238 ? 0.2772 0.3692 0.3337 -0.0080 0.0334  0.0492  238 GLU C CB  
6113 C CG  . GLU C 238 ? 0.3805 0.5001 0.4538 -0.0080 0.0318  0.0549  238 GLU C CG  
6114 C CD  . GLU C 238 ? 0.5087 0.6271 0.5883 -0.0150 0.0208  0.0473  238 GLU C CD  
6115 O OE1 . GLU C 238 ? 0.5498 0.6888 0.6423 -0.0156 0.0177  0.0506  238 GLU C OE1 
6116 O OE2 . GLU C 238 ? 0.5377 0.6351 0.6087 -0.0191 0.0153  0.0383  238 GLU C OE2 
6117 N N   . PRO C 239 ? 0.2785 0.3311 0.2967 0.0060  0.0496  0.0513  239 PRO C N   
6118 C CA  . PRO C 239 ? 0.2835 0.3096 0.2859 0.0047  0.0482  0.0449  239 PRO C CA  
6119 C C   . PRO C 239 ? 0.2490 0.2572 0.2465 -0.0005 0.0400  0.0336  239 PRO C C   
6120 O O   . PRO C 239 ? 0.2616 0.2685 0.2571 0.0033  0.0392  0.0300  239 PRO C O   
6121 C CB  . PRO C 239 ? 0.3344 0.3496 0.3173 0.0194  0.0575  0.0472  239 PRO C CB  
6122 C CG  . PRO C 239 ? 0.3708 0.4129 0.3629 0.0273  0.0656  0.0588  239 PRO C CG  
6123 C CD  . PRO C 239 ? 0.3286 0.3912 0.3405 0.0203  0.0603  0.0592  239 PRO C CD  
6124 N N   . MET C 240 ? 0.2455 0.2403 0.2407 -0.0086 0.0343  0.0286  240 MET C N   
6125 C CA  . MET C 240 ? 0.2325 0.2125 0.2237 -0.0134 0.0266  0.0189  240 MET C CA  
6126 C C   . MET C 240 ? 0.2736 0.2320 0.2458 -0.0063 0.0292  0.0143  240 MET C C   
6127 O O   . MET C 240 ? 0.2580 0.2006 0.2195 -0.0070 0.0287  0.0119  240 MET C O   
6128 C CB  . MET C 240 ? 0.2371 0.2113 0.2318 -0.0235 0.0194  0.0156  240 MET C CB  
6129 C CG  . MET C 240 ? 0.2394 0.2024 0.2314 -0.0273 0.0114  0.0064  240 MET C CG  
6130 S SD  . MET C 240 ? 0.2413 0.1961 0.2346 -0.0371 0.0030  0.0025  240 MET C SD  
6131 C CE  . MET C 240 ? 0.2403 0.2135 0.2508 -0.0440 -0.0029 0.0055  240 MET C CE  
6132 N N   . VAL C 241 ? 0.2619 0.2186 0.2295 0.0000  0.0313  0.0132  241 VAL C N   
6133 C CA  . VAL C 241 ? 0.2616 0.1964 0.2109 0.0059  0.0326  0.0093  241 VAL C CA  
6134 C C   . VAL C 241 ? 0.2689 0.2030 0.2203 0.0055  0.0295  0.0057  241 VAL C C   
6135 O O   . VAL C 241 ? 0.2712 0.2226 0.2350 0.0051  0.0292  0.0077  241 VAL C O   
6136 C CB  . VAL C 241 ? 0.2912 0.2211 0.2266 0.0181  0.0412  0.0144  241 VAL C CB  
6137 C CG1 . VAL C 241 ? 0.2927 0.2231 0.2247 0.0197  0.0451  0.0188  241 VAL C CG1 
6138 C CG2 . VAL C 241 ? 0.2954 0.2439 0.2378 0.0253  0.0466  0.0204  241 VAL C CG2 
6139 N N   . ASP C 242 ? 0.2610 0.1750 0.1999 0.0056  0.0268  0.0009  242 ASP C N   
6140 C CA  . ASP C 242 ? 0.2647 0.1771 0.2046 0.0054  0.0245  -0.0012 242 ASP C CA  
6141 C C   . ASP C 242 ? 0.2524 0.1809 0.2091 -0.0016 0.0193  -0.0031 242 ASP C C   
6142 O O   . ASP C 242 ? 0.2625 0.2021 0.2263 0.0002  0.0195  -0.0020 242 ASP C O   
6143 C CB  . ASP C 242 ? 0.2971 0.2116 0.2316 0.0152  0.0308  0.0029  242 ASP C CB  
6144 C CG  . ASP C 242 ? 0.3289 0.2208 0.2417 0.0231  0.0344  0.0034  242 ASP C CG  
6145 O OD1 . ASP C 242 ? 0.3195 0.1907 0.2211 0.0196  0.0301  -0.0008 242 ASP C OD1 
6146 O OD2 . ASP C 242 ? 0.3537 0.2492 0.2604 0.0333  0.0412  0.0081  242 ASP C OD2 
6147 N N   . ASN C 243 ? 0.2358 0.1636 0.1966 -0.0087 0.0142  -0.0062 243 ASN C N   
6148 C CA  . ASN C 243 ? 0.2288 0.1671 0.2012 -0.0144 0.0081  -0.0090 243 ASN C CA  
6149 C C   . ASN C 243 ? 0.2442 0.1735 0.2131 -0.0171 0.0036  -0.0130 243 ASN C C   
6150 O O   . ASN C 243 ? 0.2455 0.1742 0.2168 -0.0219 -0.0017 -0.0163 243 ASN C O   
6151 C CB  . ASN C 243 ? 0.2194 0.1626 0.1979 -0.0198 0.0047  -0.0095 243 ASN C CB  
6152 C CG  . ASN C 243 ? 0.2343 0.1627 0.2033 -0.0220 0.0042  -0.0112 243 ASN C CG  
6153 O OD1 . ASN C 243 ? 0.2704 0.1846 0.2280 -0.0195 0.0058  -0.0123 243 ASN C OD1 
6154 N ND2 . ASN C 243 ? 0.2514 0.1819 0.2244 -0.0269 0.0010  -0.0115 243 ASN C ND2 
6155 N N   . TRP C 244 ? 0.2403 0.1632 0.2035 -0.0138 0.0059  -0.0119 244 TRP C N   
6156 C CA  . TRP C 244 ? 0.2402 0.1566 0.2015 -0.0167 0.0023  -0.0137 244 TRP C CA  
6157 C C   . TRP C 244 ? 0.2495 0.1748 0.2158 -0.0137 0.0037  -0.0115 244 TRP C C   
6158 O O   . TRP C 244 ? 0.2601 0.1895 0.2259 -0.0081 0.0084  -0.0086 244 TRP C O   
6159 C CB  . TRP C 244 ? 0.2808 0.1763 0.2282 -0.0172 0.0024  -0.0141 244 TRP C CB  
6160 C CG  . TRP C 244 ? 0.3105 0.1959 0.2467 -0.0104 0.0081  -0.0113 244 TRP C CG  
6161 C CD1 . TRP C 244 ? 0.3100 0.1895 0.2380 -0.0058 0.0120  -0.0104 244 TRP C CD1 
6162 C CD2 . TRP C 244 ? 0.3355 0.2150 0.2659 -0.0061 0.0108  -0.0087 244 TRP C CD2 
6163 N NE1 . TRP C 244 ? 0.3013 0.1713 0.2178 0.0019  0.0169  -0.0077 244 TRP C NE1 
6164 C CE2 . TRP C 244 ? 0.3507 0.2201 0.2684 0.0018  0.0161  -0.0068 244 TRP C CE2 
6165 C CE3 . TRP C 244 ? 0.3409 0.2232 0.2754 -0.0074 0.0097  -0.0072 244 TRP C CE3 
6166 C CZ2 . TRP C 244 ? 0.4148 0.2747 0.3220 0.0088  0.0199  -0.0041 244 TRP C CZ2 
6167 C CZ3 . TRP C 244 ? 0.3856 0.2587 0.3110 -0.0016 0.0134  -0.0041 244 TRP C CZ3 
6168 C CH2 . TRP C 244 ? 0.3987 0.2593 0.3096 0.0065  0.0181  -0.0030 244 TRP C CH2 
6169 N N   . ARG C 245 ? 0.2343 0.1635 0.2052 -0.0167 -0.0001 -0.0123 245 ARG C N   
6170 C CA  . ARG C 245 ? 0.2293 0.1657 0.2039 -0.0138 0.0013  -0.0095 245 ARG C CA  
6171 C C   . ARG C 245 ? 0.2588 0.1801 0.2252 -0.0155 0.0020  -0.0070 245 ARG C C   
6172 O O   . ARG C 245 ? 0.2762 0.1875 0.2388 -0.0210 -0.0016 -0.0082 245 ARG C O   
6173 C CB  . ARG C 245 ? 0.2123 0.1621 0.1959 -0.0152 -0.0030 -0.0106 245 ARG C CB  
6174 C CG  . ARG C 245 ? 0.1968 0.1565 0.1845 -0.0107 -0.0009 -0.0072 245 ARG C CG  
6175 C CD  . ARG C 245 ? 0.2138 0.1863 0.2083 -0.0103 -0.0046 -0.0075 245 ARG C CD  
6176 N NE  . ARG C 245 ? 0.1969 0.1798 0.1946 -0.0044 -0.0020 -0.0043 245 ARG C NE  
6177 C CZ  . ARG C 245 ? 0.1727 0.1670 0.1746 -0.0016 -0.0032 -0.0025 245 ARG C CZ  
6178 N NH1 . ARG C 245 ? 0.1773 0.1752 0.1813 -0.0041 -0.0069 -0.0030 245 ARG C NH1 
6179 N NH2 . ARG C 245 ? 0.1775 0.1810 0.1813 0.0050  -0.0004 0.0004  245 ARG C NH2 
6180 N N   . PRO C 246 ? 0.2676 0.1864 0.2305 -0.0110 0.0060  -0.0035 246 PRO C N   
6181 C CA  . PRO C 246 ? 0.2667 0.1697 0.2215 -0.0136 0.0055  -0.0005 246 PRO C CA  
6182 C C   . PRO C 246 ? 0.2707 0.1802 0.2335 -0.0202 0.0011  0.0012  246 PRO C C   
6183 O O   . PRO C 246 ? 0.2558 0.1839 0.2296 -0.0194 0.0001  0.0010  246 PRO C O   
6184 C CB  . PRO C 246 ? 0.3229 0.2269 0.2748 -0.0066 0.0107  0.0033  246 PRO C CB  
6185 C CG  . PRO C 246 ? 0.2932 0.2087 0.2478 0.0005  0.0146  0.0019  246 PRO C CG  
6186 C CD  . PRO C 246 ? 0.2888 0.2186 0.2545 -0.0035 0.0106  -0.0018 246 PRO C CD  
6187 N N   . THR C 247 ? 0.2876 0.1818 0.2443 -0.0264 -0.0020 0.0032  247 THR C N   
6188 C CA  . THR C 247 ? 0.2681 0.1716 0.2342 -0.0328 -0.0057 0.0067  247 THR C CA  
6189 C C   . THR C 247 ? 0.2529 0.1695 0.2260 -0.0294 -0.0023 0.0122  247 THR C C   
6190 O O   . THR C 247 ? 0.2823 0.1932 0.2498 -0.0242 0.0020  0.0144  247 THR C O   
6191 C CB  . THR C 247 ? 0.2908 0.1759 0.2502 -0.0416 -0.0108 0.0088  247 THR C CB  
6192 O OG1 . THR C 247 ? 0.3161 0.1802 0.2624 -0.0403 -0.0090 0.0109  247 THR C OG1 
6193 C CG2 . THR C 247 ? 0.2996 0.1740 0.2528 -0.0449 -0.0150 0.0033  247 THR C CG2 
6194 N N   . GLN C 248 ? 0.2344 0.1697 0.2192 -0.0309 -0.0040 0.0147  248 GLN C N   
6195 C CA  . GLN C 248 ? 0.2063 0.1583 0.1989 -0.0263 -0.0008 0.0200  248 GLN C CA  
6196 C C   . GLN C 248 ? 0.2125 0.1680 0.2109 -0.0332 -0.0025 0.0281  248 GLN C C   
6197 O O   . GLN C 248 ? 0.2425 0.1920 0.2417 -0.0419 -0.0074 0.0289  248 GLN C O   
6198 C CB  . GLN C 248 ? 0.2058 0.1789 0.2064 -0.0200 -0.0010 0.0168  248 GLN C CB  
6199 C CG  . GLN C 248 ? 0.2117 0.1833 0.2086 -0.0147 -0.0003 0.0097  248 GLN C CG  
6200 C CD  . GLN C 248 ? 0.2006 0.1689 0.1932 -0.0086 0.0047  0.0108  248 GLN C CD  
6201 O OE1 . GLN C 248 ? 0.2274 0.2044 0.2226 -0.0038 0.0076  0.0151  248 GLN C OE1 
6202 N NE2 . GLN C 248 ? 0.2259 0.1817 0.2112 -0.0082 0.0059  0.0077  248 GLN C NE2 
6203 N N   . PRO C 249 ? 0.2185 0.1835 0.2211 -0.0298 0.0013  0.0348  249 PRO C N   
6204 C CA  . PRO C 249 ? 0.2426 0.2113 0.2515 -0.0371 0.0001  0.0444  249 PRO C CA  
6205 C C   . PRO C 249 ? 0.2222 0.2108 0.2428 -0.0403 -0.0033 0.0466  249 PRO C C   
6206 O O   . PRO C 249 ? 0.2186 0.2252 0.2439 -0.0324 -0.0022 0.0437  249 PRO C O   
6207 C CB  . PRO C 249 ? 0.2516 0.2312 0.2630 -0.0295 0.0061  0.0505  249 PRO C CB  
6208 C CG  . PRO C 249 ? 0.2620 0.2322 0.2635 -0.0205 0.0097  0.0439  249 PRO C CG  
6209 C CD  . PRO C 249 ? 0.2503 0.2218 0.2512 -0.0191 0.0068  0.0344  249 PRO C CD  
6210 N N   . LEU C 250 ? 0.2262 0.2110 0.2507 -0.0516 -0.0079 0.0520  250 LEU C N   
6211 C CA  . LEU C 250 ? 0.2319 0.2381 0.2686 -0.0546 -0.0110 0.0558  250 LEU C CA  
6212 C C   . LEU C 250 ? 0.2175 0.2507 0.2654 -0.0482 -0.0063 0.0649  250 LEU C C   
6213 O O   . LEU C 250 ? 0.2187 0.2740 0.2742 -0.0435 -0.0067 0.0659  250 LEU C O   
6214 C CB  . LEU C 250 ? 0.2776 0.2739 0.3168 -0.0693 -0.0178 0.0606  250 LEU C CB  
6215 C CG  . LEU C 250 ? 0.2891 0.3042 0.3394 -0.0739 -0.0226 0.0632  250 LEU C CG  
6216 C CD1 . LEU C 250 ? 0.2607 0.2788 0.3071 -0.0668 -0.0237 0.0526  250 LEU C CD1 
6217 C CD2 . LEU C 250 ? 0.3208 0.3217 0.3718 -0.0897 -0.0306 0.0674  250 LEU C CD2 
6218 N N   . LYS C 251 ? 0.2088 0.2409 0.2566 -0.0469 -0.0017 0.0720  251 LYS C N   
6219 C CA  . LYS C 251 ? 0.2120 0.2694 0.2693 -0.0400 0.0034  0.0816  251 LYS C CA  
6220 C C   . LYS C 251 ? 0.2469 0.3255 0.3183 -0.0466 0.0007  0.0911  251 LYS C C   
6221 O O   . LYS C 251 ? 0.2627 0.3321 0.3375 -0.0607 -0.0045 0.0955  251 LYS C O   
6222 C CB  . LYS C 251 ? 0.2323 0.3022 0.2863 -0.0240 0.0073  0.0750  251 LYS C CB  
6223 C CG  . LYS C 251 ? 0.2937 0.3438 0.3355 -0.0189 0.0098  0.0672  251 LYS C CG  
6224 C CD  . LYS C 251 ? 0.3036 0.3656 0.3425 -0.0039 0.0133  0.0627  251 LYS C CD  
6225 C CE  . LYS C 251 ? 0.3557 0.4006 0.3845 -0.0001 0.0153  0.0562  251 LYS C CE  
6226 N NZ  . LYS C 251 ? 0.3780 0.4341 0.4042 0.0135  0.0176  0.0519  251 LYS C NZ  
6227 N N   . ASN C 252 ? 0.2024 0.3092 0.2815 -0.0366 0.0037  0.0950  252 ASN C N   
6228 C CA  . ASN C 252 ? 0.2315 0.3635 0.3253 -0.0410 0.0028  0.1070  252 ASN C CA  
6229 C C   . ASN C 252 ? 0.2893 0.4279 0.3845 -0.0410 -0.0025 0.1005  252 ASN C C   
6230 O O   . ASN C 252 ? 0.3115 0.4736 0.4103 -0.0300 -0.0008 0.1016  252 ASN C O   
6231 C CB  . ASN C 252 ? 0.2879 0.4476 0.3879 -0.0281 0.0101  0.1164  252 ASN C CB  
6232 C CG  . ASN C 252 ? 0.3605 0.5474 0.4770 -0.0333 0.0104  0.1319  252 ASN C CG  
6233 O OD1 . ASN C 252 ? 0.3398 0.5239 0.4643 -0.0488 0.0047  0.1364  252 ASN C OD1 
6234 N ND2 . ASN C 252 ? 0.4058 0.6208 0.5277 -0.0202 0.0169  0.1406  252 ASN C ND2 
6235 N N   . ARG C 253 ? 0.2240 0.3397 0.3140 -0.0521 -0.0089 0.0933  253 ARG C N   
6236 C CA  . ARG C 253 ? 0.2098 0.3270 0.2995 -0.0538 -0.0147 0.0866  253 ARG C CA  
6237 C C   . ARG C 253 ? 0.2368 0.3425 0.3306 -0.0712 -0.0220 0.0900  253 ARG C C   
6238 O O   . ARG C 253 ? 0.2696 0.3573 0.3616 -0.0815 -0.0234 0.0938  253 ARG C O   
6239 C CB  . ARG C 253 ? 0.1853 0.2832 0.2604 -0.0469 -0.0157 0.0708  253 ARG C CB  
6240 C CG  . ARG C 253 ? 0.1931 0.3029 0.2640 -0.0304 -0.0108 0.0669  253 ARG C CG  
6241 C CD  . ARG C 253 ? 0.1966 0.2875 0.2547 -0.0257 -0.0124 0.0527  253 ARG C CD  
6242 N NE  . ARG C 253 ? 0.1901 0.2579 0.2408 -0.0298 -0.0109 0.0490  253 ARG C NE  
6243 C CZ  . ARG C 253 ? 0.1856 0.2356 0.2262 -0.0280 -0.0119 0.0385  253 ARG C CZ  
6244 N NH1 . ARG C 253 ? 0.1974 0.2471 0.2339 -0.0240 -0.0149 0.0304  253 ARG C NH1 
6245 N NH2 . ARG C 253 ? 0.1855 0.2178 0.2197 -0.0299 -0.0096 0.0367  253 ARG C NH2 
6246 N N   . GLN C 254 ? 0.2186 0.3345 0.3171 -0.0738 -0.0273 0.0888  254 GLN C N   
6247 C CA  . GLN C 254 ? 0.2719 0.3792 0.3744 -0.0896 -0.0358 0.0911  254 GLN C CA  
6248 C C   . GLN C 254 ? 0.2863 0.3786 0.3779 -0.0879 -0.0405 0.0778  254 GLN C C   
6249 O O   . GLN C 254 ? 0.3125 0.4175 0.4024 -0.0764 -0.0387 0.0725  254 GLN C O   
6250 C CB  . GLN C 254 ? 0.3200 0.4598 0.4416 -0.0950 -0.0379 0.1052  254 GLN C CB  
6251 C CG  . GLN C 254 ? 0.4286 0.5881 0.5619 -0.0946 -0.0319 0.1197  254 GLN C CG  
6252 C CD  . GLN C 254 ? 0.5027 0.7008 0.6559 -0.0964 -0.0322 0.1346  254 GLN C CD  
6253 O OE1 . GLN C 254 ? 0.5293 0.7480 0.6854 -0.0875 -0.0324 0.1328  254 GLN C OE1 
6254 N NE2 . GLN C 254 ? 0.5478 0.7562 0.7147 -0.1078 -0.0322 0.1501  254 GLN C NE2 
6255 N N   . ILE C 255 ? 0.2605 0.3237 0.3429 -0.0984 -0.0465 0.0722  255 ILE C N   
6256 C CA  . ILE C 255 ? 0.2508 0.2994 0.3231 -0.0983 -0.0515 0.0611  255 ILE C CA  
6257 C C   . ILE C 255 ? 0.2624 0.3232 0.3449 -0.1085 -0.0596 0.0668  255 ILE C C   
6258 O O   . ILE C 255 ? 0.2983 0.3561 0.3875 -0.1221 -0.0650 0.0751  255 ILE C O   
6259 C CB  . ILE C 255 ? 0.2735 0.2850 0.3287 -0.1019 -0.0533 0.0521  255 ILE C CB  
6260 C CG1 . ILE C 255 ? 0.2992 0.3029 0.3464 -0.0914 -0.0450 0.0478  255 ILE C CG1 
6261 C CG2 . ILE C 255 ? 0.3027 0.3010 0.3476 -0.1006 -0.0578 0.0412  255 ILE C CG2 
6262 C CD1 . ILE C 255 ? 0.2800 0.2489 0.3093 -0.0923 -0.0452 0.0394  255 ILE C CD1 
6263 N N   . LYS C 256 ? 0.2465 0.3226 0.3308 -0.1018 -0.0608 0.0632  256 LYS C N   
6264 C CA  . LYS C 256 ? 0.2464 0.3376 0.3406 -0.1096 -0.0685 0.0683  256 LYS C CA  
6265 C C   . LYS C 256 ? 0.2448 0.3115 0.3257 -0.1130 -0.0754 0.0571  256 LYS C C   
6266 O O   . LYS C 256 ? 0.2622 0.3111 0.3285 -0.1047 -0.0726 0.0457  256 LYS C O   
6267 C CB  . LYS C 256 ? 0.2442 0.3713 0.3489 -0.0983 -0.0651 0.0730  256 LYS C CB  
6268 C CG  . LYS C 256 ? 0.2714 0.4266 0.3890 -0.0926 -0.0578 0.0851  256 LYS C CG  
6269 C CD  . LYS C 256 ? 0.3250 0.4882 0.4579 -0.1084 -0.0610 0.0994  256 LYS C CD  
6270 C CE  . LYS C 256 ? 0.3716 0.5685 0.5196 -0.1025 -0.0537 0.1137  256 LYS C CE  
6271 N NZ  . LYS C 256 ? 0.4015 0.6040 0.5645 -0.1198 -0.0573 0.1284  256 LYS C NZ  
6272 N N   . ALA C 257 ? 0.2719 0.3386 0.3581 -0.1255 -0.0848 0.0610  257 ALA C N   
6273 C CA  . ALA C 257 ? 0.2989 0.3454 0.3731 -0.1286 -0.0924 0.0516  257 ALA C CA  
6274 C C   . ALA C 257 ? 0.2860 0.3584 0.3689 -0.1257 -0.0961 0.0535  257 ALA C C   
6275 O O   . ALA C 257 ? 0.2766 0.3803 0.3778 -0.1290 -0.0974 0.0653  257 ALA C O   
6276 C CB  . ALA C 257 ? 0.3324 0.3531 0.3987 -0.1389 -0.0984 0.0517  257 ALA C CB  
6277 N N   . SER C 258 ? 0.2948 0.3544 0.3644 -0.1191 -0.0977 0.0425  258 SER C N   
6278 C CA  . SER C 258 ? 0.2765 0.3552 0.3502 -0.1154 -0.1019 0.0425  258 SER C CA  
6279 C C   . SER C 258 ? 0.3100 0.3847 0.3862 -0.1265 -0.1112 0.0451  258 SER C C   
6280 O O   . SER C 258 ? 0.3182 0.4130 0.4009 -0.1248 -0.1151 0.0475  258 SER C O   
6281 C CB  . SER C 258 ? 0.2583 0.3198 0.3140 -0.1038 -0.0996 0.0292  258 SER C CB  
6282 O OG  . SER C 258 ? 0.2912 0.3196 0.3317 -0.1102 -0.1052 0.0209  258 SER C OG  
6283 N N   . PHE C 259 ? 0.2999 0.3474 0.3680 -0.1342 -0.1128 0.0440  259 PHE C N   
6284 C CA  . PHE C 259 ? 0.3155 0.3519 0.3800 -0.1410 -0.1202 0.0440  259 PHE C CA  
6285 C C   . PHE C 259 ? 0.3861 0.4287 0.4619 -0.1515 -0.1224 0.0555  259 PHE C C   
6286 O O   . PHE C 259 ? 0.3891 0.4273 0.4664 -0.1533 -0.1180 0.0591  259 PHE C O   
6287 C CB  . PHE C 259 ? 0.3576 0.3544 0.3984 -0.1381 -0.1211 0.0316  259 PHE C CB  
6288 C CG  . PHE C 259 ? 0.3828 0.3556 0.4124 -0.1362 -0.1154 0.0281  259 PHE C CG  
6289 C CD1 . PHE C 259 ? 0.3590 0.3275 0.3824 -0.1275 -0.1081 0.0220  259 PHE C CD1 
6290 C CD2 . PHE C 259 ? 0.4170 0.3727 0.4425 -0.1430 -0.1177 0.0314  259 PHE C CD2 
6291 C CE1 . PHE C 259 ? 0.3780 0.3257 0.3915 -0.1252 -0.1026 0.0192  259 PHE C CE1 
6292 C CE2 . PHE C 259 ? 0.4116 0.3463 0.4263 -0.1401 -0.1124 0.0285  259 PHE C CE2 
6293 C CZ  . PHE C 259 ? 0.4083 0.3398 0.4174 -0.1311 -0.1045 0.0225  259 PHE C CZ  
6304 N N   . ALA D 2   ? 0.1722 0.2522 0.2207 -0.0080 0.0287  -0.0155 2   ALA D N   
6305 C CA  . ALA D 2   ? 0.1691 0.2497 0.2064 -0.0081 0.0340  -0.0158 2   ALA D CA  
6306 C C   . ALA D 2   ? 0.1744 0.2484 0.2018 -0.0047 0.0307  -0.0173 2   ALA D C   
6307 O O   . ALA D 2   ? 0.1722 0.2448 0.2057 -0.0015 0.0266  -0.0205 2   ALA D O   
6308 C CB  . ALA D 2   ? 0.1582 0.2362 0.1886 -0.0133 0.0377  -0.0100 2   ALA D CB  
6309 N N   . HIS D 3   ? 0.1784 0.2482 0.1917 -0.0051 0.0319  -0.0150 3   HIS D N   
6310 C CA  . HIS D 3   ? 0.1906 0.2556 0.1969 -0.0016 0.0276  -0.0175 3   HIS D CA  
6311 C C   . HIS D 3   ? 0.1925 0.2496 0.2015 -0.0016 0.0219  -0.0150 3   HIS D C   
6312 O O   . HIS D 3   ? 0.2009 0.2532 0.2076 -0.0046 0.0214  -0.0097 3   HIS D O   
6313 C CB  . HIS D 3   ? 0.2092 0.2721 0.1990 -0.0013 0.0294  -0.0155 3   HIS D CB  
6314 C CG  . HIS D 3   ? 0.2619 0.3320 0.2458 0.0004  0.0347  -0.0197 3   HIS D CG  
6315 N ND1 . HIS D 3   ? 0.2900 0.3678 0.2799 -0.0015 0.0417  -0.0204 3   HIS D ND1 
6316 C CD2 . HIS D 3   ? 0.2943 0.3656 0.2678 0.0041  0.0337  -0.0246 3   HIS D CD2 
6317 C CE1 . HIS D 3   ? 0.2550 0.3380 0.2365 0.0010  0.0461  -0.0248 3   HIS D CE1 
6318 N NE2 . HIS D 3   ? 0.3444 0.4234 0.3152 0.0045  0.0410  -0.0278 3   HIS D NE2 
6319 N N   . HIS D 4   ? 0.1634 0.2189 0.1776 0.0015  0.0181  -0.0190 4   HIS D N   
6320 C CA  . HIS D 4   ? 0.1762 0.2245 0.1932 0.0015  0.0140  -0.0166 4   HIS D CA  
6321 C C   . HIS D 4   ? 0.1675 0.2103 0.1748 0.0015  0.0120  -0.0142 4   HIS D C   
6322 O O   . HIS D 4   ? 0.1883 0.2326 0.1876 0.0031  0.0117  -0.0162 4   HIS D O   
6323 C CB  . HIS D 4   ? 0.1585 0.2068 0.1858 0.0046  0.0116  -0.0213 4   HIS D CB  
6324 C CG  . HIS D 4   ? 0.1469 0.1884 0.1790 0.0047  0.0089  -0.0189 4   HIS D CG  
6325 N ND1 . HIS D 4   ? 0.1365 0.1748 0.1707 0.0031  0.0089  -0.0143 4   HIS D ND1 
6326 C CD2 . HIS D 4   ? 0.1631 0.2009 0.1993 0.0064  0.0066  -0.0210 4   HIS D CD2 
6327 C CE1 . HIS D 4   ? 0.1672 0.1997 0.2048 0.0039  0.0075  -0.0131 4   HIS D CE1 
6328 N NE2 . HIS D 4   ? 0.1581 0.1904 0.1984 0.0057  0.0063  -0.0171 4   HIS D NE2 
6329 N N   . TRP D 5   ? 0.1607 0.1970 0.1686 0.0002  0.0103  -0.0103 5   TRP D N   
6330 C CA  . TRP D 5   ? 0.1659 0.1970 0.1671 0.0007  0.0082  -0.0079 5   TRP D CA  
6331 C C   . TRP D 5   ? 0.1872 0.2186 0.1907 0.0041  0.0044  -0.0125 5   TRP D C   
6332 O O   . TRP D 5   ? 0.1844 0.2183 0.1966 0.0057  0.0035  -0.0173 5   TRP D O   
6333 C CB  . TRP D 5   ? 0.1639 0.1882 0.1668 -0.0010 0.0077  -0.0040 5   TRP D CB  
6334 C CG  . TRP D 5   ? 0.1629 0.1852 0.1748 0.0001  0.0066  -0.0056 5   TRP D CG  
6335 C CD1 . TRP D 5   ? 0.1791 0.2021 0.1965 -0.0005 0.0076  -0.0053 5   TRP D CD1 
6336 C CD2 . TRP D 5   ? 0.1589 0.1783 0.1755 0.0021  0.0046  -0.0071 5   TRP D CD2 
6337 N NE1 . TRP D 5   ? 0.1665 0.1860 0.1902 0.0009  0.0070  -0.0058 5   TRP D NE1 
6338 C CE2 . TRP D 5   ? 0.1558 0.1735 0.1804 0.0022  0.0056  -0.0072 5   TRP D CE2 
6339 C CE3 . TRP D 5   ? 0.1574 0.1759 0.1733 0.0040  0.0019  -0.0083 5   TRP D CE3 
6340 C CZ2 . TRP D 5   ? 0.1737 0.1886 0.2058 0.0034  0.0054  -0.0082 5   TRP D CZ2 
6341 C CZ3 . TRP D 5   ? 0.1701 0.1869 0.1952 0.0054  0.0006  -0.0102 5   TRP D CZ3 
6342 C CH2 . TRP D 5   ? 0.1782 0.1932 0.2118 0.0048  0.0030  -0.0101 5   TRP D CH2 
6343 N N   . GLY D 6   ? 0.1787 0.2076 0.1752 0.0054  0.0018  -0.0112 6   GLY D N   
6344 C CA  . GLY D 6   ? 0.1873 0.2173 0.1869 0.0086  -0.0030 -0.0161 6   GLY D CA  
6345 C C   . GLY D 6   ? 0.1694 0.1953 0.1635 0.0100  -0.0067 -0.0129 6   GLY D C   
6346 O O   . GLY D 6   ? 0.1859 0.2065 0.1790 0.0085  -0.0053 -0.0075 6   GLY D O   
6347 N N   . TYR D 7   ? 0.1909 0.2196 0.1819 0.0133  -0.0118 -0.0169 7   TYR D N   
6348 C CA  . TYR D 7   ? 0.1921 0.2180 0.1783 0.0158  -0.0168 -0.0145 7   TYR D CA  
6349 C C   . TYR D 7   ? 0.2289 0.2569 0.1987 0.0184  -0.0196 -0.0143 7   TYR D C   
6350 O O   . TYR D 7   ? 0.2520 0.2791 0.2173 0.0219  -0.0260 -0.0138 7   TYR D O   
6351 C CB  . TYR D 7   ? 0.1981 0.2252 0.1987 0.0180  -0.0222 -0.0197 7   TYR D CB  
6352 C CG  . TYR D 7   ? 0.1798 0.2035 0.1949 0.0157  -0.0188 -0.0184 7   TYR D CG  
6353 C CD1 . TYR D 7   ? 0.1808 0.1990 0.1970 0.0154  -0.0179 -0.0130 7   TYR D CD1 
6354 C CD2 . TYR D 7   ? 0.1847 0.2101 0.2119 0.0142  -0.0160 -0.0222 7   TYR D CD2 
6355 C CE1 . TYR D 7   ? 0.1766 0.1917 0.2040 0.0137  -0.0140 -0.0121 7   TYR D CE1 
6356 C CE2 . TYR D 7   ? 0.1854 0.2072 0.2235 0.0125  -0.0124 -0.0201 7   TYR D CE2 
6357 C CZ  . TYR D 7   ? 0.1777 0.1947 0.2150 0.0122  -0.0112 -0.0154 7   TYR D CZ  
6358 O OH  . TYR D 7   ? 0.1988 0.2124 0.2452 0.0108  -0.0069 -0.0139 7   TYR D OH  
6359 N N   . GLY D 8   ? 0.2237 0.2550 0.1845 0.0173  -0.0151 -0.0148 8   GLY D N   
6360 C CA  . GLY D 8   ? 0.2367 0.2701 0.1796 0.0197  -0.0161 -0.0146 8   GLY D CA  
6361 C C   . GLY D 8   ? 0.2483 0.2760 0.1775 0.0184  -0.0126 -0.0044 8   GLY D C   
6362 O O   . GLY D 8   ? 0.2481 0.2699 0.1827 0.0159  -0.0104 0.0016  8   GLY D O   
6363 N N   . LYS D 9   ? 0.2634 0.2927 0.1746 0.0203  -0.0117 -0.0029 9   LYS D N   
6364 C CA  . LYS D 9   ? 0.2830 0.3061 0.1791 0.0195  -0.0083 0.0075  9   LYS D CA  
6365 C C   . LYS D 9   ? 0.2748 0.2963 0.1750 0.0138  0.0013  0.0127  9   LYS D C   
6366 O O   . LYS D 9   ? 0.2851 0.2992 0.1817 0.0117  0.0039  0.0215  9   LYS D O   
6367 C CB  . LYS D 9   ? 0.3146 0.3402 0.1885 0.0229  -0.0083 0.0080  9   LYS D CB  
6368 C CG  . LYS D 9   ? 0.3706 0.3992 0.2388 0.0288  -0.0188 0.0015  9   LYS D CG  
6369 C CD  . LYS D 9   ? 0.3815 0.4036 0.2526 0.0314  -0.0267 0.0067  9   LYS D CD  
6370 C CE  . LYS D 9   ? 0.4993 0.5245 0.3620 0.0382  -0.0388 0.0014  9   LYS D CE  
6371 N NZ  . LYS D 9   ? 0.5914 0.6153 0.4260 0.0418  -0.0394 0.0064  9   LYS D NZ  
6372 N N   . HIS D 10  ? 0.2635 0.2915 0.1718 0.0112  0.0065  0.0073  10  HIS D N   
6373 C CA  . HIS D 10  ? 0.2629 0.2908 0.1767 0.0058  0.0148  0.0114  10  HIS D CA  
6374 C C   . HIS D 10  ? 0.2586 0.2855 0.1907 0.0029  0.0143  0.0097  10  HIS D C   
6375 O O   . HIS D 10  ? 0.2720 0.2962 0.2090 -0.0014 0.0187  0.0142  10  HIS D O   
6376 C CB  . HIS D 10  ? 0.2874 0.3238 0.1986 0.0049  0.0216  0.0074  10  HIS D CB  
6377 C CG  . HIS D 10  ? 0.3323 0.3699 0.2233 0.0072  0.0245  0.0095  10  HIS D CG  
6378 N ND1 . HIS D 10  ? 0.4022 0.4466 0.2856 0.0110  0.0237  0.0016  10  HIS D ND1 
6379 C CD2 . HIS D 10  ? 0.3776 0.4099 0.2536 0.0062  0.0287  0.0189  10  HIS D CD2 
6380 C CE1 . HIS D 10  ? 0.4226 0.4663 0.2850 0.0126  0.0271  0.0059  10  HIS D CE1 
6381 N NE2 . HIS D 10  ? 0.3824 0.4184 0.2398 0.0098  0.0302  0.0171  10  HIS D NE2 
6382 N N   . ASN D 11  ? 0.2258 0.2546 0.1679 0.0052  0.0091  0.0033  11  ASN D N   
6383 C CA  . ASN D 11  ? 0.1931 0.2212 0.1505 0.0028  0.0093  0.0017  11  ASN D CA  
6384 C C   . ASN D 11  ? 0.1985 0.2207 0.1621 0.0040  0.0044  0.0025  11  ASN D C   
6385 O O   . ASN D 11  ? 0.1867 0.2082 0.1615 0.0028  0.0043  0.0008  11  ASN D O   
6386 C CB  . ASN D 11  ? 0.2016 0.2369 0.1683 0.0037  0.0097  -0.0058 11  ASN D CB  
6387 C CG  . ASN D 11  ? 0.2402 0.2774 0.2087 0.0079  0.0041  -0.0124 11  ASN D CG  
6388 O OD1 . ASN D 11  ? 0.2406 0.2745 0.2048 0.0102  -0.0009 -0.0116 11  ASN D OD1 
6389 N ND2 . ASN D 11  ? 0.2530 0.2955 0.2296 0.0089  0.0045  -0.0193 11  ASN D ND2 
6390 N N   . GLY D 12  ? 0.2001 0.2181 0.1566 0.0066  0.0004  0.0052  12  GLY D N   
6391 C CA  . GLY D 12  ? 0.1999 0.2138 0.1642 0.0085  -0.0044 0.0047  12  GLY D CA  
6392 C C   . GLY D 12  ? 0.1971 0.2031 0.1640 0.0063  -0.0028 0.0102  12  GLY D C   
6393 O O   . GLY D 12  ? 0.2089 0.2122 0.1728 0.0027  0.0018  0.0143  12  GLY D O   
6394 N N   . PRO D 13  ? 0.1881 0.1906 0.1617 0.0086  -0.0066 0.0097  13  PRO D N   
6395 C CA  . PRO D 13  ? 0.1963 0.1915 0.1746 0.0070  -0.0047 0.0130  13  PRO D CA  
6396 C C   . PRO D 13  ? 0.2111 0.1996 0.1813 0.0047  -0.0020 0.0196  13  PRO D C   
6397 O O   . PRO D 13  ? 0.2167 0.2012 0.1904 0.0012  0.0017  0.0205  13  PRO D O   
6398 C CB  . PRO D 13  ? 0.2227 0.2164 0.2077 0.0112  -0.0099 0.0116  13  PRO D CB  
6399 C CG  . PRO D 13  ? 0.2082 0.2098 0.1992 0.0131  -0.0130 0.0052  13  PRO D CG  
6400 C CD  . PRO D 13  ? 0.1990 0.2055 0.1798 0.0124  -0.0121 0.0043  13  PRO D CD  
6401 N N   . GLU D 14  ? 0.2009 0.1873 0.1600 0.0065  -0.0035 0.0243  14  GLU D N   
6402 C CA  . GLU D 14  ? 0.2220 0.2002 0.1753 0.0041  -0.0002 0.0315  14  GLU D CA  
6403 C C   . GLU D 14  ? 0.2301 0.2102 0.1825 -0.0016 0.0062  0.0323  14  GLU D C   
6404 O O   . GLU D 14  ? 0.2573 0.2307 0.2089 -0.0050 0.0097  0.0371  14  GLU D O   
6405 C CB  . GLU D 14  ? 0.2313 0.2059 0.1717 0.0075  -0.0030 0.0377  14  GLU D CB  
6406 C CG  . GLU D 14  ? 0.2393 0.2205 0.1676 0.0077  -0.0014 0.0378  14  GLU D CG  
6407 C CD  . GLU D 14  ? 0.2999 0.2757 0.2125 0.0102  -0.0023 0.0459  14  GLU D CD  
6408 O OE1 . GLU D 14  ? 0.3205 0.2862 0.2320 0.0111  -0.0033 0.0529  14  GLU D OE1 
6409 O OE2 . GLU D 14  ? 0.3421 0.3234 0.2425 0.0114  -0.0014 0.0456  14  GLU D OE2 
6410 N N   . HIS D 15  ? 0.2270 0.2161 0.1808 -0.0025 0.0077  0.0275  15  HIS D N   
6411 C CA  . HIS D 15  ? 0.2192 0.2124 0.1745 -0.0073 0.0134  0.0274  15  HIS D CA  
6412 C C   . HIS D 15  ? 0.2046 0.2006 0.1713 -0.0097 0.0138  0.0226  15  HIS D C   
6413 O O   . HIS D 15  ? 0.2092 0.2085 0.1794 -0.0136 0.0175  0.0222  15  HIS D O   
6414 C CB  . HIS D 15  ? 0.2415 0.2436 0.1906 -0.0062 0.0152  0.0252  15  HIS D CB  
6415 C CG  . HIS D 15  ? 0.2953 0.2952 0.2300 -0.0038 0.0153  0.0303  15  HIS D CG  
6416 N ND1 . HIS D 15  ? 0.3480 0.3405 0.2757 -0.0062 0.0190  0.0384  15  HIS D ND1 
6417 C CD2 . HIS D 15  ? 0.3199 0.3230 0.2448 0.0009  0.0116  0.0285  15  HIS D CD2 
6418 C CE1 . HIS D 15  ? 0.3605 0.3517 0.2735 -0.0027 0.0179  0.0425  15  HIS D CE1 
6419 N NE2 . HIS D 15  ? 0.3442 0.3422 0.2547 0.0017  0.0131  0.0361  15  HIS D NE2 
6420 N N   . TRP D 16  ? 0.1746 0.1695 0.1472 -0.0073 0.0103  0.0191  16  TRP D N   
6421 C CA  . TRP D 16  ? 0.1787 0.1762 0.1595 -0.0089 0.0109  0.0151  16  TRP D CA  
6422 C C   . TRP D 16  ? 0.1963 0.1900 0.1792 -0.0133 0.0132  0.0165  16  TRP D C   
6423 O O   . TRP D 16  ? 0.1979 0.1961 0.1854 -0.0154 0.0139  0.0140  16  TRP D O   
6424 C CB  . TRP D 16  ? 0.1763 0.1716 0.1623 -0.0060 0.0082  0.0124  16  TRP D CB  
6425 C CG  . TRP D 16  ? 0.1783 0.1790 0.1665 -0.0023 0.0055  0.0091  16  TRP D CG  
6426 C CD1 . TRP D 16  ? 0.1765 0.1839 0.1621 -0.0013 0.0052  0.0070  16  TRP D CD1 
6427 C CD2 . TRP D 16  ? 0.1769 0.1766 0.1714 0.0007  0.0030  0.0066  16  TRP D CD2 
6428 N NE1 . TRP D 16  ? 0.1744 0.1847 0.1648 0.0020  0.0020  0.0028  16  TRP D NE1 
6429 C CE2 . TRP D 16  ? 0.1535 0.1594 0.1500 0.0031  0.0005  0.0028  16  TRP D CE2 
6430 C CE3 . TRP D 16  ? 0.1721 0.1666 0.1717 0.0015  0.0030  0.0067  16  TRP D CE3 
6431 C CZ2 . TRP D 16  ? 0.1678 0.1750 0.1729 0.0059  -0.0023 -0.0008 16  TRP D CZ2 
6432 C CZ3 . TRP D 16  ? 0.1831 0.1793 0.1911 0.0044  0.0010  0.0037  16  TRP D CZ3 
6433 C CH2 . TRP D 16  ? 0.1855 0.1882 0.1970 0.0064  -0.0019 0.0000  16  TRP D CH2 
6434 N N   . HIS D 17  ? 0.2004 0.1858 0.1809 -0.0146 0.0137  0.0201  17  HIS D N   
6435 C CA  . HIS D 17  ? 0.1874 0.1685 0.1711 -0.0192 0.0155  0.0204  17  HIS D CA  
6436 C C   . HIS D 17  ? 0.2074 0.1946 0.1935 -0.0235 0.0184  0.0207  17  HIS D C   
6437 O O   . HIS D 17  ? 0.2204 0.2072 0.2119 -0.0273 0.0186  0.0188  17  HIS D O   
6438 C CB  . HIS D 17  ? 0.2311 0.2015 0.2126 -0.0199 0.0161  0.0246  17  HIS D CB  
6439 C CG  . HIS D 17  ? 0.2310 0.2000 0.2067 -0.0203 0.0182  0.0306  17  HIS D CG  
6440 N ND1 . HIS D 17  ? 0.2955 0.2631 0.2721 -0.0254 0.0224  0.0339  17  HIS D ND1 
6441 C CD2 . HIS D 17  ? 0.2222 0.1919 0.1905 -0.0163 0.0170  0.0338  17  HIS D CD2 
6442 C CE1 . HIS D 17  ? 0.2712 0.2377 0.2399 -0.0243 0.0245  0.0399  17  HIS D CE1 
6443 N NE2 . HIS D 17  ? 0.2688 0.2367 0.2314 -0.0186 0.0207  0.0397  17  HIS D NE2 
6444 N N   . LYS D 18  ? 0.1978 0.1911 0.1807 -0.0230 0.0206  0.0225  18  LYS D N   
6445 C CA  . LYS D 18  ? 0.1885 0.1884 0.1754 -0.0272 0.0247  0.0228  18  LYS D CA  
6446 C C   . LYS D 18  ? 0.2027 0.2108 0.1982 -0.0278 0.0231  0.0174  18  LYS D C   
6447 O O   . LYS D 18  ? 0.1946 0.2075 0.1975 -0.0318 0.0250  0.0166  18  LYS D O   
6448 C CB  . LYS D 18  ? 0.2146 0.2194 0.1947 -0.0257 0.0281  0.0253  18  LYS D CB  
6449 C CG  . LYS D 18  ? 0.3104 0.3066 0.2808 -0.0252 0.0297  0.0320  18  LYS D CG  
6450 C CD  . LYS D 18  ? 0.3371 0.3384 0.2973 -0.0227 0.0325  0.0340  18  LYS D CD  
6451 C CE  . LYS D 18  ? 0.3735 0.3657 0.3210 -0.0209 0.0328  0.0416  18  LYS D CE  
6452 N NZ  . LYS D 18  ? 0.4285 0.4267 0.3635 -0.0181 0.0355  0.0427  18  LYS D NZ  
6453 N N   . ASP D 19  ? 0.1814 0.1912 0.1768 -0.0237 0.0195  0.0141  19  ASP D N   
6454 C CA  . ASP D 19  ? 0.1824 0.1984 0.1848 -0.0233 0.0173  0.0100  19  ASP D CA  
6455 C C   . ASP D 19  ? 0.1963 0.2068 0.1986 -0.0225 0.0137  0.0084  19  ASP D C   
6456 O O   . ASP D 19  ? 0.1880 0.2017 0.1946 -0.0231 0.0115  0.0060  19  ASP D O   
6457 C CB  . ASP D 19  ? 0.1765 0.1993 0.1798 -0.0193 0.0170  0.0076  19  ASP D CB  
6458 C CG  . ASP D 19  ? 0.1939 0.2231 0.1965 -0.0197 0.0210  0.0080  19  ASP D CG  
6459 O OD1 . ASP D 19  ? 0.2202 0.2558 0.2295 -0.0226 0.0235  0.0074  19  ASP D OD1 
6460 O OD2 . ASP D 19  ? 0.2228 0.2513 0.2182 -0.0171 0.0217  0.0086  19  ASP D OD2 
6461 N N   . PHE D 20  ? 0.1869 0.1893 0.1841 -0.0207 0.0131  0.0096  20  PHE D N   
6462 C CA  . PHE D 20  ? 0.1878 0.1846 0.1837 -0.0194 0.0111  0.0079  20  PHE D CA  
6463 C C   . PHE D 20  ? 0.1997 0.1875 0.1929 -0.0212 0.0118  0.0090  20  PHE D C   
6464 O O   . PHE D 20  ? 0.2303 0.2125 0.2211 -0.0188 0.0121  0.0105  20  PHE D O   
6465 C CB  . PHE D 20  ? 0.1999 0.1967 0.1952 -0.0149 0.0106  0.0074  20  PHE D CB  
6466 C CG  . PHE D 20  ? 0.1686 0.1734 0.1678 -0.0131 0.0101  0.0060  20  PHE D CG  
6467 C CD1 . PHE D 20  ? 0.1925 0.1998 0.1944 -0.0125 0.0089  0.0046  20  PHE D CD1 
6468 C CD2 . PHE D 20  ? 0.1685 0.1774 0.1678 -0.0116 0.0108  0.0060  20  PHE D CD2 
6469 C CE1 . PHE D 20  ? 0.1661 0.1798 0.1730 -0.0105 0.0084  0.0034  20  PHE D CE1 
6470 C CE2 . PHE D 20  ? 0.1652 0.1811 0.1689 -0.0096 0.0105  0.0036  20  PHE D CE2 
6471 C CZ  . PHE D 20  ? 0.1809 0.1990 0.1895 -0.0091 0.0094  0.0024  20  PHE D CZ  
6472 N N   . PRO D 21  ? 0.1736 0.1597 0.1688 -0.0253 0.0116  0.0081  21  PRO D N   
6473 C CA  . PRO D 21  ? 0.2005 0.1771 0.1946 -0.0273 0.0127  0.0092  21  PRO D CA  
6474 C C   . PRO D 21  ? 0.1977 0.1665 0.1885 -0.0245 0.0120  0.0072  21  PRO D C   
6475 O O   . PRO D 21  ? 0.2262 0.1865 0.2167 -0.0246 0.0130  0.0084  21  PRO D O   
6476 C CB  . PRO D 21  ? 0.2438 0.2211 0.2428 -0.0327 0.0121  0.0070  21  PRO D CB  
6477 C CG  . PRO D 21  ? 0.2330 0.2203 0.2349 -0.0326 0.0099  0.0044  21  PRO D CG  
6478 C CD  . PRO D 21  ? 0.1893 0.1826 0.1897 -0.0284 0.0106  0.0061  21  PRO D CD  
6479 N N   A ILE D 22  ? 0.1886 0.1596 0.1773 -0.0218 0.0110  0.0045  22  ILE D N   
6480 N N   B ILE D 22  ? 0.1889 0.1599 0.1776 -0.0218 0.0110  0.0045  22  ILE D N   
6481 C CA  A ILE D 22  ? 0.1943 0.1587 0.1801 -0.0190 0.0119  0.0027  22  ILE D CA  
6482 C CA  B ILE D 22  ? 0.1954 0.1600 0.1813 -0.0190 0.0119  0.0027  22  ILE D CA  
6483 C C   A ILE D 22  ? 0.2113 0.1733 0.1989 -0.0156 0.0131  0.0054  22  ILE D C   
6484 C C   B ILE D 22  ? 0.2092 0.1714 0.1969 -0.0156 0.0131  0.0053  22  ILE D C   
6485 O O   A ILE D 22  ? 0.2149 0.1711 0.2028 -0.0134 0.0145  0.0041  22  ILE D O   
6486 O O   B ILE D 22  ? 0.2134 0.1699 0.2013 -0.0133 0.0145  0.0040  22  ILE D O   
6487 C CB  A ILE D 22  ? 0.2038 0.1712 0.1863 -0.0170 0.0115  0.0005  22  ILE D CB  
6488 C CB  B ILE D 22  ? 0.2032 0.1710 0.1858 -0.0170 0.0115  0.0006  22  ILE D CB  
6489 C CG1 A ILE D 22  ? 0.2123 0.1727 0.1910 -0.0148 0.0138  -0.0019 22  ILE D CG1 
6490 C CG1 B ILE D 22  ? 0.2131 0.1737 0.1911 -0.0154 0.0134  -0.0023 22  ILE D CG1 
6491 C CG2 A ILE D 22  ? 0.2006 0.1745 0.1859 -0.0143 0.0117  0.0027  22  ILE D CG2 
6492 C CG2 B ILE D 22  ? 0.2011 0.1744 0.1864 -0.0139 0.0120  0.0027  22  ILE D CG2 
6493 C CD1 A ILE D 22  ? 0.2227 0.1764 0.1979 -0.0173 0.0133  -0.0058 22  ILE D CD1 
6494 C CD1 B ILE D 22  ? 0.2053 0.1680 0.1783 -0.0132 0.0140  -0.0030 22  ILE D CD1 
6495 N N   . ALA D 23  ? 0.1929 0.1596 0.1820 -0.0151 0.0126  0.0086  23  ALA D N   
6496 C CA  . ALA D 23  ? 0.2059 0.1705 0.1962 -0.0117 0.0122  0.0110  23  ALA D CA  
6497 C C   . ALA D 23  ? 0.2079 0.1627 0.1984 -0.0116 0.0127  0.0123  23  ALA D C   
6498 O O   . ALA D 23  ? 0.2264 0.1784 0.2194 -0.0078 0.0120  0.0132  23  ALA D O   
6499 C CB  . ALA D 23  ? 0.2088 0.1785 0.1973 -0.0117 0.0114  0.0144  23  ALA D CB  
6500 N N   . LYS D 24  ? 0.2143 0.1640 0.2041 -0.0156 0.0136  0.0122  24  LYS D N   
6501 C CA  . LYS D 24  ? 0.2250 0.1640 0.2163 -0.0158 0.0143  0.0132  24  LYS D CA  
6502 C C   . LYS D 24  ? 0.2196 0.1530 0.2117 -0.0163 0.0153  0.0074  24  LYS D C   
6503 O O   . LYS D 24  ? 0.2591 0.1833 0.2531 -0.0178 0.0160  0.0064  24  LYS D O   
6504 C CB  . LYS D 24  ? 0.2632 0.1992 0.2545 -0.0203 0.0151  0.0170  24  LYS D CB  
6505 C CG  . LYS D 24  ? 0.3160 0.2559 0.3040 -0.0191 0.0149  0.0235  24  LYS D CG  
6506 C CD  . LYS D 24  ? 0.3953 0.3310 0.3829 -0.0235 0.0173  0.0287  24  LYS D CD  
6507 C CE  . LYS D 24  ? 0.4599 0.3999 0.4413 -0.0220 0.0180  0.0349  24  LYS D CE  
6508 N NZ  . LYS D 24  ? 0.5049 0.4396 0.4817 -0.0163 0.0155  0.0396  24  LYS D NZ  
6509 N N   . GLY D 25  ? 0.2395 0.1776 0.2297 -0.0147 0.0158  0.0036  25  GLY D N   
6510 C CA  . GLY D 25  ? 0.2436 0.1777 0.2311 -0.0148 0.0172  -0.0022 25  GLY D CA  
6511 C C   . GLY D 25  ? 0.2646 0.1912 0.2551 -0.0111 0.0196  -0.0042 25  GLY D C   
6512 O O   . GLY D 25  ? 0.2633 0.1873 0.2591 -0.0083 0.0194  -0.0009 25  GLY D O   
6513 N N   . GLU D 26  ? 0.2356 0.1591 0.2222 -0.0108 0.0218  -0.0098 26  GLU D N   
6514 C CA  . GLU D 26  ? 0.2730 0.1890 0.2624 -0.0076 0.0252  -0.0134 26  GLU D CA  
6515 C C   . GLU D 26  ? 0.2627 0.1829 0.2548 -0.0031 0.0287  -0.0134 26  GLU D C   
6516 O O   . GLU D 26  ? 0.3123 0.2278 0.3097 0.0002  0.0321  -0.0159 26  GLU D O   
6517 C CB  . GLU D 26  ? 0.2920 0.2022 0.2746 -0.0095 0.0264  -0.0207 26  GLU D CB  
6518 C CG  . GLU D 26  ? 0.3192 0.2243 0.3020 -0.0144 0.0231  -0.0222 26  GLU D CG  
6519 C CD  . GLU D 26  ? 0.4193 0.3161 0.4114 -0.0137 0.0232  -0.0195 26  GLU D CD  
6520 O OE1 . GLU D 26  ? 0.4730 0.3632 0.4689 -0.0100 0.0261  -0.0222 26  GLU D OE1 
6521 O OE2 . GLU D 26  ? 0.4817 0.3789 0.4772 -0.0165 0.0208  -0.0141 26  GLU D OE2 
6522 N N   . ARG D 27  ? 0.2506 0.1792 0.2408 -0.0030 0.0286  -0.0110 27  ARG D N   
6523 C CA  A ARG D 27  ? 0.2399 0.1725 0.2336 0.0003  0.0327  -0.0112 27  ARG D CA  
6524 C CA  B ARG D 27  ? 0.2365 0.1690 0.2310 0.0006  0.0327  -0.0111 27  ARG D CA  
6525 C C   . ARG D 27  ? 0.2143 0.1551 0.2140 0.0011  0.0302  -0.0066 27  ARG D C   
6526 O O   . ARG D 27  ? 0.2446 0.1907 0.2434 0.0013  0.0319  -0.0058 27  ARG D O   
6527 C CB  A ARG D 27  ? 0.2590 0.1919 0.2419 -0.0004 0.0362  -0.0140 27  ARG D CB  
6528 C CB  B ARG D 27  ? 0.2544 0.1868 0.2397 0.0005  0.0373  -0.0143 27  ARG D CB  
6529 C CG  A ARG D 27  ? 0.2798 0.2148 0.2646 0.0025  0.0428  -0.0144 27  ARG D CG  
6530 C CG  B ARG D 27  ? 0.2414 0.1662 0.2178 -0.0005 0.0389  -0.0200 27  ARG D CG  
6531 C CD  A ARG D 27  ? 0.2655 0.1998 0.2357 0.0017  0.0458  -0.0159 27  ARG D CD  
6532 C CD  B ARG D 27  ? 0.2527 0.1774 0.2190 0.0009  0.0449  -0.0227 27  ARG D CD  
6533 N NE  A ARG D 27  ? 0.1848 0.1240 0.1568 0.0029  0.0498  -0.0122 27  ARG D NE  
6534 N NE  B ARG D 27  ? 0.2601 0.1903 0.2178 -0.0003 0.0434  -0.0194 27  ARG D NE  
6535 C CZ  A ARG D 27  ? 0.2682 0.2061 0.2299 0.0037  0.0552  -0.0121 27  ARG D CZ  
6536 C CZ  B ARG D 27  ? 0.2958 0.2265 0.2430 -0.0029 0.0383  -0.0201 27  ARG D CZ  
6537 N NH1 A ARG D 27  ? 0.3290 0.2614 0.2757 0.0036  0.0569  -0.0162 27  ARG D NH1 
6538 N NH1 B ARG D 27  ? 0.3171 0.2438 0.2624 -0.0054 0.0341  -0.0242 27  ARG D NH1 
6539 N NH2 A ARG D 27  ? 0.3106 0.2522 0.2766 0.0045  0.0591  -0.0079 27  ARG D NH2 
6540 N NH2 B ARG D 27  ? 0.2701 0.2056 0.2107 -0.0031 0.0370  -0.0166 27  ARG D NH2 
6541 N N   . GLN D 28  ? 0.2230 0.1645 0.2281 0.0016  0.0260  -0.0035 28  GLN D N   
6542 C CA  . GLN D 28  ? 0.2017 0.1510 0.2107 0.0023  0.0228  -0.0002 28  GLN D CA  
6543 C C   . GLN D 28  ? 0.2131 0.1655 0.2337 0.0063  0.0232  -0.0005 28  GLN D C   
6544 O O   . GLN D 28  ? 0.2259 0.1744 0.2533 0.0091  0.0245  -0.0018 28  GLN D O   
6545 C CB  . GLN D 28  ? 0.2158 0.1646 0.2224 0.0009  0.0182  0.0033  28  GLN D CB  
6546 C CG  . GLN D 28  ? 0.2132 0.1618 0.2114 -0.0037 0.0177  0.0034  28  GLN D CG  
6547 C CD  . GLN D 28  ? 0.1997 0.1565 0.1961 -0.0046 0.0173  0.0035  28  GLN D CD  
6548 O OE1 . GLN D 28  ? 0.1937 0.1564 0.1923 -0.0039 0.0151  0.0055  28  GLN D OE1 
6549 N NE2 . GLN D 28  ? 0.2090 0.1660 0.2009 -0.0058 0.0191  0.0012  28  GLN D NE2 
6550 N N   . SER D 29  ? 0.1898 0.1497 0.2143 0.0068  0.0214  0.0005  29  SER D N   
6551 C CA  . SER D 29  ? 0.1796 0.1444 0.2171 0.0100  0.0209  -0.0005 29  SER D CA  
6552 C C   . SER D 29  ? 0.2095 0.1800 0.2484 0.0107  0.0144  0.0011  29  SER D C   
6553 O O   . SER D 29  ? 0.1982 0.1705 0.2285 0.0084  0.0124  0.0027  29  SER D O   
6554 C CB  . SER D 29  ? 0.1966 0.1649 0.2389 0.0095  0.0262  -0.0022 29  SER D CB  
6555 O OG  . SER D 29  ? 0.1915 0.1546 0.2308 0.0094  0.0329  -0.0038 29  SER D OG  
6556 N N   . PRO D 30  ? 0.1845 0.1587 0.2344 0.0142  0.0108  0.0002  30  PRO D N   
6557 C CA  . PRO D 30  ? 0.1762 0.1505 0.2403 0.0174  0.0126  -0.0022 30  PRO D CA  
6558 C C   . PRO D 30  ? 0.1906 0.1579 0.2537 0.0198  0.0111  -0.0007 30  PRO D C   
6559 O O   . PRO D 30  ? 0.2049 0.1669 0.2561 0.0184  0.0091  0.0024  30  PRO D O   
6560 C CB  . PRO D 30  ? 0.1833 0.1656 0.2587 0.0199  0.0067  -0.0038 30  PRO D CB  
6561 C CG  . PRO D 30  ? 0.1844 0.1671 0.2472 0.0198  -0.0002 -0.0009 30  PRO D CG  
6562 C CD  . PRO D 30  ? 0.1967 0.1765 0.2461 0.0153  0.0040  0.0008  30  PRO D CD  
6563 N N   . VAL D 31  ? 0.1900 0.1569 0.2666 0.0233  0.0129  -0.0030 31  VAL D N   
6564 C CA  . VAL D 31  ? 0.1956 0.1557 0.2750 0.0265  0.0116  -0.0022 31  VAL D CA  
6565 C C   . VAL D 31  ? 0.2108 0.1760 0.3082 0.0319  0.0072  -0.0037 31  VAL D C   
6566 O O   . VAL D 31  ? 0.2119 0.1860 0.3223 0.0325  0.0074  -0.0068 31  VAL D O   
6567 C CB  . VAL D 31  ? 0.2030 0.1559 0.2810 0.0256  0.0199  -0.0049 31  VAL D CB  
6568 C CG1 . VAL D 31  ? 0.2133 0.1617 0.2740 0.0204  0.0229  -0.0041 31  VAL D CG1 
6569 C CG2 . VAL D 31  ? 0.2244 0.1824 0.3149 0.0263  0.0275  -0.0094 31  VAL D CG2 
6570 N N   . ASP D 32  ? 0.1934 0.1531 0.2936 0.0359  0.0032  -0.0016 32  ASP D N   
6571 C CA  . ASP D 32  ? 0.2056 0.1692 0.3252 0.0417  -0.0004 -0.0037 32  ASP D CA  
6572 C C   . ASP D 32  ? 0.2235 0.1863 0.3563 0.0425  0.0091  -0.0086 32  ASP D C   
6573 O O   . ASP D 32  ? 0.2467 0.2007 0.3719 0.0410  0.0156  -0.0093 32  ASP D O   
6574 C CB  . ASP D 32  ? 0.2125 0.1695 0.3301 0.0464  -0.0082 0.0011  32  ASP D CB  
6575 C CG  . ASP D 32  ? 0.2421 0.2034 0.3812 0.0534  -0.0131 -0.0009 32  ASP D CG  
6576 O OD1 . ASP D 32  ? 0.2354 0.2078 0.3861 0.0549  -0.0178 -0.0037 32  ASP D OD1 
6577 O OD2 . ASP D 32  ? 0.2681 0.2221 0.4140 0.0573  -0.0124 -0.0004 32  ASP D OD2 
6578 N N   . ILE D 33  ? 0.1961 0.1681 0.3491 0.0448  0.0101  -0.0127 33  ILE D N   
6579 C CA  . ILE D 33  ? 0.2034 0.1759 0.3719 0.0463  0.0197  -0.0176 33  ILE D CA  
6580 C C   . ILE D 33  ? 0.2132 0.1860 0.3998 0.0533  0.0145  -0.0185 33  ILE D C   
6581 O O   . ILE D 33  ? 0.2219 0.2036 0.4249 0.0569  0.0067  -0.0192 33  ILE D O   
6582 C CB  . ILE D 33  ? 0.1893 0.1720 0.3711 0.0440  0.0256  -0.0212 33  ILE D CB  
6583 C CG1 . ILE D 33  ? 0.2250 0.2064 0.3879 0.0378  0.0296  -0.0192 33  ILE D CG1 
6584 C CG2 . ILE D 33  ? 0.2164 0.2005 0.4152 0.0459  0.0365  -0.0260 33  ILE D CG2 
6585 C CD1 . ILE D 33  ? 0.2411 0.2317 0.4144 0.0350  0.0323  -0.0209 33  ILE D CD1 
6586 N N   . ASP D 34  ? 0.2496 0.2123 0.4338 0.0556  0.0175  -0.0185 34  ASP D N   
6587 C CA  . ASP D 34  ? 0.2433 0.2057 0.4434 0.0619  0.0129  -0.0191 34  ASP D CA  
6588 C C   . ASP D 34  ? 0.2908 0.2593 0.5052 0.0615  0.0222  -0.0251 34  ASP D C   
6589 O O   . ASP D 34  ? 0.3032 0.2665 0.5111 0.0590  0.0331  -0.0282 34  ASP D O   
6590 C CB  . ASP D 34  ? 0.2455 0.1934 0.4351 0.0642  0.0105  -0.0155 34  ASP D CB  
6591 C CG  . ASP D 34  ? 0.2680 0.2163 0.4706 0.0697  0.0060  -0.0157 34  ASP D CG  
6592 O OD1 . ASP D 34  ? 0.3066 0.2567 0.5191 0.0701  0.0137  -0.0210 34  ASP D OD1 
6593 O OD2 . ASP D 34  ? 0.2661 0.2143 0.4688 0.0736  -0.0053 -0.0105 34  ASP D OD2 
6594 N N   . THR D 35  ? 0.2692 0.2362 0.5645 0.0183  -0.0067 -0.0764 35  THR D N   
6595 C CA  . THR D 35  ? 0.2879 0.2654 0.6026 0.0236  0.0071  -0.0773 35  THR D CA  
6596 C C   . THR D 35  ? 0.3665 0.3309 0.6757 0.0276  0.0125  -0.0835 35  THR D C   
6597 O O   . THR D 35  ? 0.4010 0.3707 0.7212 0.0315  0.0271  -0.0849 35  THR D O   
6598 C CB  . THR D 35  ? 0.2705 0.2611 0.6098 0.0242  0.0019  -0.0725 35  THR D CB  
6599 O OG1 . THR D 35  ? 0.2870 0.2700 0.6296 0.0255  -0.0131 -0.0732 35  THR D OG1 
6600 C CG2 . THR D 35  ? 0.2445 0.2448 0.5850 0.0198  -0.0022 -0.0666 35  THR D CG2 
6601 N N   . HIS D 36  ? 0.3072 0.2541 0.5986 0.0265  0.0012  -0.0862 36  HIS D N   
6602 C CA  . HIS D 36  ? 0.3768 0.3087 0.6603 0.0306  0.0059  -0.0921 36  HIS D CA  
6603 C C   . HIS D 36  ? 0.3958 0.3132 0.6535 0.0274  0.0174  -0.0986 36  HIS D C   
6604 O O   . HIS D 36  ? 0.4215 0.3281 0.6732 0.0317  0.0279  -0.1042 36  HIS D O   
6605 C CB  . HIS D 36  ? 0.4450 0.3624 0.7170 0.0301  -0.0111 -0.0915 36  HIS D CB  
6606 C CG  . HIS D 36  ? 0.5711 0.4992 0.8608 0.0310  -0.0249 -0.0856 36  HIS D CG  
6607 N ND1 . HIS D 36  ? 0.6060 0.5259 0.8788 0.0267  -0.0407 -0.0819 36  HIS D ND1 
6608 C CD2 . HIS D 36  ? 0.6020 0.5468 0.9224 0.0343  -0.0252 -0.0830 36  HIS D CD2 
6609 C CE1 . HIS D 36  ? 0.6198 0.5500 0.9112 0.0284  -0.0503 -0.0779 36  HIS D CE1 
6610 N NE2 . HIS D 36  ? 0.5975 0.5430 0.9190 0.0322  -0.0421 -0.0788 36  HIS D NE2 
6611 N N   . THR D 37  ? 0.3135 0.2349 0.5472 0.0175  0.0141  -0.0945 37  THR D N   
6612 C CA  . THR D 37  ? 0.3008 0.2143 0.4989 0.0103  0.0205  -0.0959 37  THR D CA  
6613 C C   . THR D 37  ? 0.2941 0.2233 0.4865 0.0076  0.0331  -0.0918 37  THR D C   
6614 O O   . THR D 37  ? 0.3555 0.2755 0.5205 0.0040  0.0410  -0.0943 37  THR D O   
6615 C CB  . THR D 37  ? 0.3357 0.2410 0.5055 -0.0008 0.0061  -0.0932 37  THR D CB  
6616 O OG1 . THR D 37  ? 0.3705 0.2925 0.5479 -0.0051 -0.0016 -0.0855 37  THR D OG1 
6617 C CG2 . THR D 37  ? 0.3742 0.2574 0.5417 0.0014  -0.0047 -0.0979 37  THR D CG2 
6618 N N   . ALA D 38  ? 0.3002 0.2499 0.5145 0.0090  0.0342  -0.0855 38  ALA D N   
6619 C CA  . ALA D 38  ? 0.2949 0.2574 0.5056 0.0077  0.0469  -0.0814 38  ALA D CA  
6620 C C   . ALA D 38  ? 0.3569 0.3116 0.5708 0.0146  0.0656  -0.0872 38  ALA D C   
6621 O O   . ALA D 38  ? 0.4237 0.3754 0.6649 0.0234  0.0702  -0.0920 38  ALA D O   
6622 C CB  . ALA D 38  ? 0.2579 0.2410 0.4959 0.0095  0.0453  -0.0744 38  ALA D CB  
6623 N N   . LYS D 39  ? 0.3168 0.2662 0.5016 0.0107  0.0762  -0.0870 39  LYS D N   
6624 C CA  . LYS D 39  ? 0.3309 0.2670 0.5081 0.0161  0.0956  -0.0932 39  LYS D CA  
6625 C C   . LYS D 39  ? 0.3583 0.3041 0.5361 0.0168  0.1120  -0.0883 39  LYS D C   
6626 O O   . LYS D 39  ? 0.3371 0.2893 0.4943 0.0097  0.1081  -0.0815 39  LYS D O   
6627 C CB  . LYS D 39  ? 0.4377 0.3495 0.5704 0.0107  0.0948  -0.0989 39  LYS D CB  
6628 C CG  . LYS D 39  ? 0.5599 0.4552 0.6925 0.0125  0.0850  -0.1061 39  LYS D CG  
6629 C CD  . LYS D 39  ? 0.6611 0.5288 0.7514 0.0083  0.0870  -0.1133 39  LYS D CD  
6630 C CE  . LYS D 39  ? 0.7683 0.6230 0.8470 0.0144  0.1104  -0.1188 39  LYS D CE  
6631 N NZ  . LYS D 39  ? 0.8417 0.6643 0.8783 0.0117  0.1127  -0.1276 39  LYS D NZ  
6632 N N   . TYR D 40  ? 0.3516 0.2967 0.5514 0.0253  0.1312  -0.0919 40  TYR D N   
6633 C CA  . TYR D 40  ? 0.3406 0.2901 0.5373 0.0260  0.1503  -0.0880 40  TYR D CA  
6634 C C   . TYR D 40  ? 0.3750 0.3062 0.5176 0.0192  0.1554  -0.0880 40  TYR D C   
6635 O O   . TYR D 40  ? 0.3969 0.3057 0.5093 0.0182  0.1561  -0.0954 40  TYR D O   
6636 C CB  . TYR D 40  ? 0.3460 0.2936 0.5731 0.0361  0.1722  -0.0935 40  TYR D CB  
6637 C CG  . TYR D 40  ? 0.3846 0.3294 0.6002 0.0365  0.1962  -0.0910 40  TYR D CG  
6638 C CD1 . TYR D 40  ? 0.3758 0.3386 0.6061 0.0338  0.1985  -0.0811 40  TYR D CD1 
6639 C CD2 . TYR D 40  ? 0.4513 0.3730 0.6374 0.0387  0.2158  -0.0975 40  TYR D CD2 
6640 C CE1 . TYR D 40  ? 0.4082 0.3658 0.6232 0.0327  0.2184  -0.0769 40  TYR D CE1 
6641 C CE2 . TYR D 40  ? 0.4963 0.4129 0.6661 0.0377  0.2361  -0.0934 40  TYR D CE2 
6642 C CZ  . TYR D 40  ? 0.4554 0.3898 0.6395 0.0346  0.2373  -0.0831 40  TYR D CZ  
6643 O OH  . TYR D 40  ? 0.5127 0.4388 0.6781 0.0332  0.2572  -0.0786 40  TYR D OH  
6644 N N   . ASP D 41  ? 0.3598 0.2988 0.4889 0.0144  0.1574  -0.0795 41  ASP D N   
6645 C CA  . ASP D 41  ? 0.4047 0.3268 0.4823 0.0075  0.1599  -0.0778 41  ASP D CA  
6646 C C   . ASP D 41  ? 0.4233 0.3403 0.4947 0.0105  0.1841  -0.0754 41  ASP D C   
6647 O O   . ASP D 41  ? 0.3847 0.3172 0.4696 0.0097  0.1865  -0.0664 41  ASP D O   
6648 C CB  . ASP D 41  ? 0.3819 0.3161 0.4460 -0.0013 0.1391  -0.0687 41  ASP D CB  
6649 C CG  . ASP D 41  ? 0.4587 0.3757 0.4709 -0.0091 0.1363  -0.0666 41  ASP D CG  
6650 O OD1 . ASP D 41  ? 0.5097 0.4036 0.4910 -0.0081 0.1523  -0.0712 41  ASP D OD1 
6651 O OD2 . ASP D 41  ? 0.4809 0.4071 0.4834 -0.0164 0.1170  -0.0603 41  ASP D OD2 
6652 N N   . PRO D 42  ? 0.4674 0.3610 0.5168 0.0139  0.2036  -0.0831 42  PRO D N   
6653 C CA  . PRO D 42  ? 0.4741 0.3605 0.5156 0.0166  0.2295  -0.0807 42  PRO D CA  
6654 C C   . PRO D 42  ? 0.5065 0.3858 0.5054 0.0087  0.2265  -0.0718 42  PRO D C   
6655 O O   . PRO D 42  ? 0.5593 0.4353 0.5537 0.0099  0.2461  -0.0671 42  PRO D O   
6656 C CB  . PRO D 42  ? 0.5263 0.3844 0.5455 0.0215  0.2494  -0.0923 42  PRO D CB  
6657 C CG  . PRO D 42  ? 0.5620 0.4064 0.5560 0.0176  0.2290  -0.0989 42  PRO D CG  
6658 C CD  . PRO D 42  ? 0.4971 0.3673 0.5239 0.0150  0.2029  -0.0941 42  PRO D CD  
6659 N N   . SER D 43  ? 0.4977 0.3740 0.4660 0.0005  0.2030  -0.0688 43  SER D N   
6660 C CA  . SER D 43  ? 0.5603 0.4305 0.4904 -0.0068 0.1970  -0.0596 43  SER D CA  
6661 C C   . SER D 43  ? 0.5321 0.4298 0.4934 -0.0071 0.1901  -0.0477 43  SER D C   
6662 O O   . SER D 43  ? 0.5822 0.4756 0.5176 -0.0112 0.1889  -0.0390 43  SER D O   
6663 C CB  . SER D 43  ? 0.5802 0.4386 0.4702 -0.0157 0.1730  -0.0604 43  SER D CB  
6664 O OG  . SER D 43  ? 0.5470 0.4308 0.4649 -0.0189 0.1489  -0.0558 43  SER D OG  
6665 N N   . LEU D 44  ? 0.4398 0.3631 0.4536 -0.0028 0.1849  -0.0472 44  LEU D N   
6666 C CA  . LEU D 44  ? 0.4214 0.3683 0.4647 -0.0027 0.1795  -0.0368 44  LEU D CA  
6667 C C   . LEU D 44  ? 0.4672 0.4113 0.5157 0.0004  0.2032  -0.0321 44  LEU D C   
6668 O O   . LEU D 44  ? 0.4574 0.3950 0.5198 0.0057  0.2249  -0.0379 44  LEU D O   
6669 C CB  . LEU D 44  ? 0.3800 0.3503 0.4752 0.0013  0.1698  -0.0385 44  LEU D CB  
6670 C CG  . LEU D 44  ? 0.3392 0.3138 0.4305 -0.0026 0.1461  -0.0411 44  LEU D CG  
6671 C CD1 . LEU D 44  ? 0.3267 0.3164 0.4626 0.0018  0.1388  -0.0451 44  LEU D CD1 
6672 C CD2 . LEU D 44  ? 0.3293 0.3143 0.4074 -0.0088 0.1290  -0.0310 44  LEU D CD2 
6673 N N   . LYS D 45  ? 0.4632 0.4121 0.5017 -0.0028 0.1994  -0.0210 45  LYS D N   
6674 C CA  . LYS D 45  ? 0.4553 0.4019 0.5006 -0.0007 0.2213  -0.0152 45  LYS D CA  
6675 C C   . LYS D 45  ? 0.3880 0.3607 0.4898 0.0029  0.2204  -0.0113 45  LYS D C   
6676 O O   . LYS D 45  ? 0.3493 0.3400 0.4759 0.0030  0.2004  -0.0112 45  LYS D O   
6677 C CB  . LYS D 45  ? 0.4954 0.4291 0.4971 -0.0059 0.2181  -0.0049 45  LYS D CB  
6678 C CG  . LYS D 45  ? 0.6361 0.5432 0.5784 -0.0108 0.2122  -0.0081 45  LYS D CG  
6679 C CD  . LYS D 45  ? 0.7577 0.6541 0.6591 -0.0162 0.2021  0.0033  45  LYS D CD  
6680 C CE  . LYS D 45  ? 0.8364 0.7166 0.6902 -0.0228 0.1813  0.0017  45  LYS D CE  
6681 N NZ  . LYS D 45  ? 0.8148 0.7182 0.6896 -0.0254 0.1526  0.0036  45  LYS D NZ  
6682 N N   . PRO D 46  ? 0.3817 0.3560 0.5041 0.0053  0.2417  -0.0079 46  PRO D N   
6683 C CA  . PRO D 46  ? 0.3509 0.3485 0.5265 0.0077  0.2394  -0.0041 46  PRO D CA  
6684 C C   . PRO D 46  ? 0.3284 0.3377 0.5027 0.0048  0.2174  0.0048  46  PRO D C   
6685 O O   . PRO D 46  ? 0.3497 0.3491 0.4865 0.0011  0.2129  0.0123  46  PRO D O   
6686 C CB  . PRO D 46  ? 0.3657 0.3539 0.5423 0.0079  0.2553  0.0005  46  PRO D CB  
6687 C CG  . PRO D 46  ? 0.4277 0.3922 0.5697 0.0084  0.2765  -0.0058 46  PRO D CG  
6688 C CD  . PRO D 46  ? 0.4692 0.4222 0.5651 0.0052  0.2691  -0.0071 46  PRO D CD  
6689 N N   . LEU D 47  ? 0.2792 0.3083 0.4938 0.0067  0.2034  0.0039  47  LEU D N   
6690 C CA  . LEU D 47  ? 0.2669 0.3079 0.4854 0.0051  0.1839  0.0113  47  LEU D CA  
6691 C C   . LEU D 47  ? 0.2934 0.3371 0.5268 0.0053  0.1889  0.0199  47  LEU D C   
6692 O O   . LEU D 47  ? 0.3226 0.3636 0.5753 0.0070  0.1906  0.0173  47  LEU D O   
6693 C CB  . LEU D 47  ? 0.2699 0.3256 0.5177 0.0068  0.1659  0.0061  47  LEU D CB  
6694 C CG  . LEU D 47  ? 0.2572 0.3238 0.5071 0.0056  0.1472  0.0127  47  LEU D CG  
6695 C CD1 . LEU D 47  ? 0.2732 0.3355 0.4855 0.0021  0.1340  0.0154  47  LEU D CD1 
6696 C CD2 . LEU D 47  ? 0.2893 0.3614 0.5606 0.0075  0.1290  0.0072  47  LEU D CD2 
6697 N N   . SER D 48  ? 0.2746 0.3181 0.4900 0.0032  0.1851  0.0299  48  SER D N   
6698 C CA  A SER D 48  ? 0.2957 0.3399 0.5213 0.0031  0.1904  0.0393  48  SER D CA  
6699 C CA  B SER D 48  ? 0.2945 0.3387 0.5198 0.0031  0.1905  0.0394  48  SER D CA  
6700 C C   . SER D 48  ? 0.2587 0.3165 0.4998 0.0042  0.1706  0.0438  48  SER D C   
6701 O O   . SER D 48  ? 0.2633 0.3222 0.4825 0.0034  0.1566  0.0475  48  SER D O   
6702 C CB  A SER D 48  ? 0.3341 0.3605 0.5180 0.0003  0.2013  0.0480  48  SER D CB  
6703 C CB  B SER D 48  ? 0.3354 0.3621 0.5187 0.0003  0.2002  0.0484  48  SER D CB  
6704 O OG  A SER D 48  ? 0.3578 0.3840 0.5504 0.0001  0.2058  0.0582  48  SER D OG  
6705 O OG  B SER D 48  ? 0.3992 0.4106 0.5683 -0.0006 0.2232  0.0455  48  SER D OG  
6706 N N   . VAL D 49  ? 0.2692 0.3287 0.5334 0.0061  0.1606  0.0414  49  VAL D N   
6707 C CA  . VAL D 49  ? 0.2653 0.3322 0.5402 0.0076  0.1435  0.0444  49  VAL D CA  
6708 C C   . VAL D 49  ? 0.2808 0.3420 0.5603 0.0077  0.1497  0.0528  49  VAL D C   
6709 O O   . VAL D 49  ? 0.3263 0.3814 0.6205 0.0077  0.1519  0.0500  49  VAL D O   
6710 C CB  . VAL D 49  ? 0.2716 0.3391 0.5622 0.0088  0.1278  0.0352  49  VAL D CB  
6711 C CG1 . VAL D 49  ? 0.3052 0.3756 0.5998 0.0101  0.1126  0.0383  49  VAL D CG1 
6712 C CG2 . VAL D 49  ? 0.2938 0.3647 0.5800 0.0086  0.1231  0.0272  49  VAL D CG2 
6713 N N   . SER D 50  ? 0.2715 0.3343 0.5398 0.0075  0.1528  0.0642  50  SER D N   
6714 C CA  . SER D 50  ? 0.2875 0.3420 0.5562 0.0071  0.1619  0.0737  50  SER D CA  
6715 C C   . SER D 50  ? 0.2544 0.3145 0.5354 0.0100  0.1483  0.0787  50  SER D C   
6716 O O   . SER D 50  ? 0.2853 0.3508 0.5575 0.0112  0.1444  0.0882  50  SER D O   
6717 C CB  . SER D 50  ? 0.3777 0.4221 0.6164 0.0044  0.1770  0.0851  50  SER D CB  
6718 O OG  . SER D 50  ? 0.4738 0.5099 0.6954 0.0020  0.1904  0.0797  50  SER D OG  
6719 N N   . TYR D 51  ? 0.3680 0.3550 0.4633 -0.0781 0.1794  0.0134  51  TYR D N   
6720 C CA  . TYR D 51  ? 0.3359 0.3195 0.4379 -0.0747 0.1632  0.0200  51  TYR D CA  
6721 C C   . TYR D 51  ? 0.3826 0.3626 0.4954 -0.0794 0.1658  0.0290  51  TYR D C   
6722 O O   . TYR D 51  ? 0.3977 0.3748 0.5225 -0.0766 0.1536  0.0327  51  TYR D O   
6723 C CB  . TYR D 51  ? 0.3250 0.3150 0.4543 -0.0671 0.1524  0.0126  51  TYR D CB  
6724 C CG  . TYR D 51  ? 0.2947 0.2844 0.4126 -0.0615 0.1443  0.0060  51  TYR D CG  
6725 C CD1 . TYR D 51  ? 0.3155 0.3006 0.4010 -0.0636 0.1450  0.0061  51  TYR D CD1 
6726 C CD2 . TYR D 51  ? 0.2579 0.2516 0.3970 -0.0547 0.1356  -0.0002 51  TYR D CD2 
6727 C CE1 . TYR D 51  ? 0.2921 0.2767 0.3683 -0.0598 0.1376  -0.0004 51  TYR D CE1 
6728 C CE2 . TYR D 51  ? 0.2449 0.2366 0.3740 -0.0503 0.1288  -0.0056 51  TYR D CE2 
6729 C CZ  . TYR D 51  ? 0.2463 0.2334 0.3445 -0.0532 0.1300  -0.0060 51  TYR D CZ  
6730 O OH  . TYR D 51  ? 0.2623 0.2473 0.3531 -0.0500 0.1235  -0.0119 51  TYR D OH  
6731 N N   . ASP D 52  ? 0.4172 0.3969 0.5231 -0.0847 0.1773  0.0310  52  ASP D N   
6732 C CA  . ASP D 52  ? 0.4388 0.4150 0.5545 -0.0889 0.1783  0.0380  52  ASP D CA  
6733 C C   . ASP D 52  ? 0.4465 0.4084 0.5441 -0.0904 0.1707  0.0510  52  ASP D C   
6734 O O   . ASP D 52  ? 0.4901 0.4471 0.6012 -0.0918 0.1662  0.0557  52  ASP D O   
6735 C CB  . ASP D 52  ? 0.4912 0.4694 0.5991 -0.0951 0.1935  0.0382  52  ASP D CB  
6736 C CG  . ASP D 52  ? 0.5616 0.5536 0.6936 -0.0931 0.2017  0.0259  52  ASP D CG  
6737 O OD1 . ASP D 52  ? 0.5392 0.5394 0.6957 -0.0868 0.1953  0.0177  52  ASP D OD1 
6738 O OD2 . ASP D 52  ? 0.5942 0.5888 0.7209 -0.0978 0.2150  0.0248  52  ASP D OD2 
6739 N N   . GLN D 53  ? 0.4042 0.3588 0.4714 -0.0899 0.1689  0.0567  53  GLN D N   
6740 C CA  . GLN D 53  ? 0.4304 0.3709 0.4773 -0.0894 0.1610  0.0700  53  GLN D CA  
6741 C C   . GLN D 53  ? 0.4241 0.3654 0.4669 -0.0800 0.1418  0.0688  53  GLN D C   
6742 O O   . GLN D 53  ? 0.4661 0.4004 0.4843 -0.0770 0.1337  0.0772  53  GLN D O   
6743 C CB  . GLN D 53  ? 0.4599 0.3926 0.4691 -0.0943 0.1691  0.0790  53  GLN D CB  
6744 C CG  . GLN D 53  ? 0.4919 0.4255 0.5018 -0.1012 0.1822  0.0797  53  GLN D CG  
6745 C CD  . GLN D 53  ? 0.5953 0.5190 0.5668 -0.1057 0.1874  0.0911  53  GLN D CD  
6746 O OE1 . GLN D 53  ? 0.6287 0.5550 0.5738 -0.1062 0.1901  0.0893  53  GLN D OE1 
6747 N NE2 . GLN D 53  ? 0.6639 0.5759 0.6316 -0.1091 0.1883  0.1027  53  GLN D NE2 
6748 N N   . ALA D 54  ? 0.3727 0.3232 0.4389 -0.0750 0.1348  0.0584  54  ALA D N   
6749 C CA  . ALA D 54  ? 0.3603 0.3124 0.4224 -0.0668 0.1183  0.0563  54  ALA D CA  
6750 C C   . ALA D 54  ? 0.3699 0.3127 0.4366 -0.0630 0.1072  0.0640  54  ALA D C   
6751 O O   . ALA D 54  ? 0.3666 0.3046 0.4533 -0.0656 0.1094  0.0653  54  ALA D O   
6752 C CB  . ALA D 54  ? 0.3696 0.3322 0.4540 -0.0629 0.1146  0.0439  54  ALA D CB  
6753 N N   . THR D 55  ? 0.3489 0.2893 0.3983 -0.0570 0.0954  0.0683  55  THR D N   
6754 C CA  . THR D 55  ? 0.3256 0.2557 0.3773 -0.0522 0.0857  0.0758  55  THR D CA  
6755 C C   . THR D 55  ? 0.2973 0.2343 0.3568 -0.0443 0.0721  0.0689  55  THR D C   
6756 O O   . THR D 55  ? 0.3089 0.2510 0.3523 -0.0399 0.0650  0.0696  55  THR D O   
6757 C CB  . THR D 55  ? 0.3772 0.2975 0.4016 -0.0510 0.0841  0.0893  55  THR D CB  
6758 O OG1 . THR D 55  ? 0.4329 0.3458 0.4474 -0.0592 0.0978  0.0961  55  THR D OG1 
6759 C CG2 . THR D 55  ? 0.3713 0.2794 0.3996 -0.0445 0.0741  0.0967  55  THR D CG2 
6760 N N   . SER D 56  ? 0.2582 0.1962 0.3419 -0.0429 0.0685  0.0621  56  SER D N   
6761 C CA  . SER D 56  ? 0.2449 0.1874 0.3336 -0.0356 0.0563  0.0565  56  SER D CA  
6762 C C   . SER D 56  ? 0.2473 0.1803 0.3308 -0.0297 0.0477  0.0636  56  SER D C   
6763 O O   . SER D 56  ? 0.3031 0.2229 0.3865 -0.0312 0.0505  0.0716  56  SER D O   
6764 C CB  . SER D 56  ? 0.2303 0.1770 0.3438 -0.0357 0.0544  0.0469  56  SER D CB  
6765 O OG  . SER D 56  ? 0.2602 0.1976 0.3893 -0.0377 0.0543  0.0489  56  SER D OG  
6766 N N   . LEU D 57  ? 0.2573 0.1965 0.3357 -0.0228 0.0379  0.0609  57  LEU D N   
6767 C CA  . LEU D 57  ? 0.2608 0.1928 0.3349 -0.0155 0.0300  0.0668  57  LEU D CA  
6768 C C   . LEU D 57  ? 0.2542 0.1873 0.3418 -0.0100 0.0218  0.0593  57  LEU D C   
6769 O O   . LEU D 57  ? 0.2551 0.1764 0.3491 -0.0065 0.0188  0.0617  57  LEU D O   
6770 C CB  . LEU D 57  ? 0.3318 0.2712 0.3856 -0.0114 0.0255  0.0724  57  LEU D CB  
6771 C CG  . LEU D 57  ? 0.3808 0.3161 0.4163 -0.0156 0.0318  0.0822  57  LEU D CG  
6772 C CD1 . LEU D 57  ? 0.4080 0.3551 0.4244 -0.0118 0.0252  0.0852  57  LEU D CD1 
6773 C CD2 . LEU D 57  ? 0.4158 0.3320 0.4505 -0.0148 0.0343  0.0935  57  LEU D CD2 
6774 N N   . ARG D 58  ? 0.2285 0.1738 0.3180 -0.0089 0.0184  0.0508  58  ARG D N   
6775 C CA  . ARG D 58  ? 0.2180 0.1652 0.3148 -0.0031 0.0106  0.0447  58  ARG D CA  
6776 C C   . ARG D 58  ? 0.2202 0.1772 0.3216 -0.0051 0.0099  0.0352  58  ARG D C   
6777 O O   . ARG D 58  ? 0.2318 0.1955 0.3290 -0.0096 0.0147  0.0334  58  ARG D O   
6778 C CB  . ARG D 58  ? 0.3035 0.2543 0.3907 0.0046  0.0044  0.0487  58  ARG D CB  
6779 C CG  . ARG D 58  ? 0.3427 0.3072 0.4164 0.0039  0.0038  0.0499  58  ARG D CG  
6780 C CD  . ARG D 58  ? 0.3946 0.3644 0.4623 0.0122  -0.0032 0.0548  58  ARG D CD  
6781 N NE  . ARG D 58  ? 0.4580 0.4141 0.5243 0.0166  -0.0035 0.0646  58  ARG D NE  
6782 C CZ  . ARG D 58  ? 0.4705 0.4240 0.5236 0.0162  -0.0023 0.0749  58  ARG D CZ  
6783 N NH1 . ARG D 58  ? 0.4421 0.4069 0.4816 0.0111  -0.0007 0.0757  58  ARG D NH1 
6784 N NH2 . ARG D 58  ? 0.4296 0.3674 0.4817 0.0206  -0.0025 0.0843  58  ARG D NH2 
6785 N N   . ILE D 59  ? 0.2009 0.1573 0.3099 -0.0017 0.0044  0.0291  59  ILE D N   
6786 C CA  . ILE D 59  ? 0.2002 0.1638 0.3119 -0.0026 0.0026  0.0211  59  ILE D CA  
6787 C C   . ILE D 59  ? 0.2045 0.1728 0.3111 0.0028  -0.0033 0.0180  59  ILE D C   
6788 O O   . ILE D 59  ? 0.2124 0.1756 0.3210 0.0077  -0.0069 0.0188  59  ILE D O   
6789 C CB  . ILE D 59  ? 0.1792 0.1379 0.3058 -0.0050 0.0020  0.0162  59  ILE D CB  
6790 C CG1 . ILE D 59  ? 0.2045 0.1696 0.3324 -0.0054 0.0003  0.0096  59  ILE D CG1 
6791 C CG2 . ILE D 59  ? 0.2235 0.1727 0.3569 -0.0020 -0.0030 0.0149  59  ILE D CG2 
6792 C CD1 . ILE D 59  ? 0.2321 0.1948 0.3754 -0.0073 -0.0014 0.0053  59  ILE D CD1 
6793 N N   . LEU D 60  ? 0.2057 0.1834 0.3056 0.0016  -0.0034 0.0145  60  LEU D N   
6794 C CA  . LEU D 60  ? 0.2143 0.1994 0.3087 0.0053  -0.0072 0.0121  60  LEU D CA  
6795 C C   . LEU D 60  ? 0.1970 0.1842 0.2907 0.0033  -0.0079 0.0053  60  LEU D C   
6796 O O   . LEU D 60  ? 0.2118 0.2003 0.3036 -0.0012 -0.0046 0.0037  60  LEU D O   
6797 C CB  . LEU D 60  ? 0.1974 0.1935 0.2818 0.0045  -0.0064 0.0156  60  LEU D CB  
6798 C CG  . LEU D 60  ? 0.1864 0.1946 0.2667 0.0062  -0.0092 0.0123  60  LEU D CG  
6799 C CD1 . LEU D 60  ? 0.2060 0.2153 0.2908 0.0141  -0.0133 0.0135  60  LEU D CD1 
6800 C CD2 . LEU D 60  ? 0.2149 0.2352 0.2858 0.0030  -0.0086 0.0148  60  LEU D CD2 
6801 N N   . ASN D 61  ? 0.1933 0.1802 0.2875 0.0067  -0.0114 0.0015  61  ASN D N   
6802 C CA  . ASN D 61  ? 0.1677 0.1570 0.2570 0.0048  -0.0118 -0.0038 61  ASN D CA  
6803 C C   . ASN D 61  ? 0.1621 0.1636 0.2440 0.0038  -0.0104 -0.0039 61  ASN D C   
6804 O O   . ASN D 61  ? 0.1780 0.1858 0.2603 0.0080  -0.0121 -0.0035 61  ASN D O   
6805 C CB  . ASN D 61  ? 0.1992 0.1826 0.2903 0.0083  -0.0157 -0.0079 61  ASN D CB  
6806 C CG  . ASN D 61  ? 0.1953 0.1796 0.2786 0.0066  -0.0159 -0.0123 61  ASN D CG  
6807 O OD1 . ASN D 61  ? 0.1849 0.1760 0.2617 0.0034  -0.0130 -0.0124 61  ASN D OD1 
6808 N ND2 . ASN D 61  ? 0.2117 0.1885 0.2946 0.0081  -0.0196 -0.0158 61  ASN D ND2 
6809 N N   . ASN D 62  ? 0.1770 0.1823 0.2532 -0.0017 -0.0073 -0.0047 62  ASN D N   
6810 C CA  . ASN D 62  ? 0.1704 0.1884 0.2403 -0.0044 -0.0062 -0.0055 62  ASN D CA  
6811 C C   . ASN D 62  ? 0.1473 0.1672 0.2126 -0.0070 -0.0052 -0.0104 62  ASN D C   
6812 O O   . ASN D 62  ? 0.1866 0.2167 0.2473 -0.0115 -0.0034 -0.0122 62  ASN D O   
6813 C CB  . ASN D 62  ? 0.1541 0.1756 0.2185 -0.0100 -0.0030 -0.0042 62  ASN D CB  
6814 C CG  . ASN D 62  ? 0.1808 0.1942 0.2415 -0.0155 0.0012  -0.0078 62  ASN D CG  
6815 O OD1 . ASN D 62  ? 0.1785 0.1833 0.2414 -0.0142 0.0007  -0.0098 62  ASN D OD1 
6816 N ND2 . ASN D 62  ? 0.1755 0.1908 0.2299 -0.0210 0.0051  -0.0086 62  ASN D ND2 
6817 N N   . GLY D 63  ? 0.1727 0.1833 0.2387 -0.0047 -0.0065 -0.0125 63  GLY D N   
6818 C CA  . GLY D 63  ? 0.1821 0.1918 0.2411 -0.0072 -0.0051 -0.0163 63  GLY D CA  
6819 C C   . GLY D 63  ? 0.2011 0.2028 0.2537 -0.0129 -0.0022 -0.0172 63  GLY D C   
6820 O O   . GLY D 63  ? 0.2263 0.2251 0.2711 -0.0160 -0.0003 -0.0193 63  GLY D O   
6821 N N   . HIS D 64  ? 0.1841 0.1814 0.2393 -0.0144 -0.0010 -0.0155 64  HIS D N   
6822 C CA  . HIS D 64  ? 0.1647 0.1532 0.2156 -0.0185 0.0024  -0.0166 64  HIS D CA  
6823 C C   . HIS D 64  ? 0.2127 0.1919 0.2713 -0.0149 0.0009  -0.0151 64  HIS D C   
6824 O O   . HIS D 64  ? 0.2331 0.2021 0.2908 -0.0141 0.0004  -0.0155 64  HIS D O   
6825 C CB  . HIS D 64  ? 0.1812 0.1755 0.2277 -0.0248 0.0071  -0.0178 64  HIS D CB  
6826 C CG  . HIS D 64  ? 0.1607 0.1688 0.2029 -0.0289 0.0076  -0.0194 64  HIS D CG  
6827 N ND1 . HIS D 64  ? 0.1737 0.1825 0.2100 -0.0330 0.0095  -0.0222 64  HIS D ND1 
6828 C CD2 . HIS D 64  ? 0.1650 0.1878 0.2087 -0.0296 0.0064  -0.0186 64  HIS D CD2 
6829 C CE1 . HIS D 64  ? 0.1977 0.2227 0.2341 -0.0366 0.0098  -0.0237 64  HIS D CE1 
6830 N NE2 . HIS D 64  ? 0.1689 0.2031 0.2099 -0.0340 0.0071  -0.0215 64  HIS D NE2 
6831 N N   . THR D 65  ? 0.1760 0.1587 0.2429 -0.0126 0.0001  -0.0129 65  THR D N   
6832 C CA  . THR D 65  ? 0.1707 0.1480 0.2482 -0.0100 -0.0006 -0.0116 65  THR D CA  
6833 C C   . THR D 65  ? 0.1811 0.1624 0.2655 -0.0075 -0.0026 -0.0088 65  THR D C   
6834 O O   . THR D 65  ? 0.1811 0.1674 0.2624 -0.0059 -0.0048 -0.0082 65  THR D O   
6835 C CB  . THR D 65  ? 0.1769 0.1521 0.2550 -0.0132 0.0056  -0.0122 65  THR D CB  
6836 O OG1 . THR D 65  ? 0.2035 0.1751 0.2948 -0.0104 0.0053  -0.0114 65  THR D OG1 
6837 C CG2 . THR D 65  ? 0.1875 0.1699 0.2607 -0.0169 0.0100  -0.0111 65  THR D CG2 
6838 N N   . PHE D 66  ? 0.1795 0.1582 0.2744 -0.0069 -0.0016 -0.0072 66  PHE D N   
6839 C CA  . PHE D 66  ? 0.1615 0.1419 0.2611 -0.0060 -0.0016 -0.0036 66  PHE D CA  
6840 C C   . PHE D 66  ? 0.1674 0.1497 0.2668 -0.0096 0.0052  -0.0012 66  PHE D C   
6841 O O   . PHE D 66  ? 0.1843 0.1647 0.2878 -0.0115 0.0094  -0.0030 66  PHE D O   
6842 C CB  . PHE D 66  ? 0.1840 0.1590 0.2958 -0.0034 -0.0059 -0.0037 66  PHE D CB  
6843 C CG  . PHE D 66  ? 0.1780 0.1508 0.3021 -0.0045 -0.0050 -0.0051 66  PHE D CG  
6844 C CD1 . PHE D 66  ? 0.1947 0.1682 0.3278 -0.0070 0.0002  -0.0027 66  PHE D CD1 
6845 C CD2 . PHE D 66  ? 0.1972 0.1677 0.3242 -0.0027 -0.0096 -0.0084 66  PHE D CD2 
6846 C CE1 . PHE D 66  ? 0.1924 0.1665 0.3403 -0.0077 0.0015  -0.0045 66  PHE D CE1 
6847 C CE2 . PHE D 66  ? 0.2087 0.1793 0.3495 -0.0025 -0.0097 -0.0095 66  PHE D CE2 
6848 C CZ  . PHE D 66  ? 0.2127 0.1862 0.3660 -0.0050 -0.0041 -0.0080 66  PHE D CZ  
6849 N N   . ASN D 67  ? 0.1892 0.1753 0.2824 -0.0101 0.0063  0.0029  67  ASN D N   
6850 C CA  . ASN D 67  ? 0.1862 0.1739 0.2748 -0.0138 0.0126  0.0059  67  ASN D CA  
6851 C C   . ASN D 67  ? 0.1948 0.1783 0.2896 -0.0129 0.0135  0.0114  67  ASN D C   
6852 O O   . ASN D 67  ? 0.2090 0.1910 0.3038 -0.0093 0.0089  0.0149  67  ASN D O   
6853 C CB  . ASN D 67  ? 0.1877 0.1832 0.2618 -0.0154 0.0124  0.0074  67  ASN D CB  
6854 C CG  . ASN D 67  ? 0.2069 0.2066 0.2738 -0.0182 0.0126  0.0019  67  ASN D CG  
6855 O OD1 . ASN D 67  ? 0.2013 0.1959 0.2714 -0.0195 0.0149  -0.0025 67  ASN D OD1 
6856 N ND2 . ASN D 67  ? 0.2287 0.2377 0.2861 -0.0194 0.0100  0.0024  67  ASN D ND2 
6857 N N   . VAL D 68  ? 0.2031 0.1841 0.3031 -0.0164 0.0203  0.0124  68  VAL D N   
6858 C CA  . VAL D 68  ? 0.2070 0.1834 0.3105 -0.0176 0.0235  0.0184  68  VAL D CA  
6859 C C   . VAL D 68  ? 0.2191 0.1979 0.3064 -0.0208 0.0288  0.0231  68  VAL D C   
6860 O O   . VAL D 68  ? 0.2223 0.2039 0.3044 -0.0248 0.0355  0.0202  68  VAL D O   
6861 C CB  . VAL D 68  ? 0.2013 0.1750 0.3220 -0.0202 0.0283  0.0165  68  VAL D CB  
6862 C CG1 . VAL D 68  ? 0.2412 0.2100 0.3631 -0.0237 0.0344  0.0232  68  VAL D CG1 
6863 C CG2 . VAL D 68  ? 0.1971 0.1688 0.3328 -0.0171 0.0209  0.0123  68  VAL D CG2 
6864 N N   . GLU D 69  ? 0.2177 0.1951 0.2960 -0.0186 0.0257  0.0302  69  GLU D N   
6865 C CA  . GLU D 69  ? 0.2556 0.2364 0.3154 -0.0206 0.0278  0.0354  69  GLU D CA  
6866 C C   . GLU D 69  ? 0.2487 0.2216 0.3058 -0.0239 0.0349  0.0429  69  GLU D C   
6867 O O   . GLU D 69  ? 0.2760 0.2400 0.3436 -0.0226 0.0348  0.0468  69  GLU D O   
6868 C CB  . GLU D 69  ? 0.3286 0.3136 0.3808 -0.0149 0.0188  0.0397  69  GLU D CB  
6869 C CG  . GLU D 69  ? 0.4761 0.4675 0.5092 -0.0161 0.0180  0.0453  69  GLU D CG  
6870 C CD  . GLU D 69  ? 0.5926 0.5864 0.6221 -0.0085 0.0091  0.0527  69  GLU D CD  
6871 O OE1 . GLU D 69  ? 0.5987 0.5889 0.6407 -0.0024 0.0044  0.0522  69  GLU D OE1 
6872 O OE2 . GLU D 69  ? 0.6327 0.6316 0.6467 -0.0084 0.0068  0.0590  69  GLU D OE2 
6873 N N   . PHE D 70  ? 0.2238 0.1990 0.2652 -0.0288 0.0414  0.0447  70  PHE D N   
6874 C CA  . PHE D 70  ? 0.2516 0.2198 0.2852 -0.0332 0.0499  0.0521  70  PHE D CA  
6875 C C   . PHE D 70  ? 0.3031 0.2721 0.3124 -0.0328 0.0472  0.0608  70  PHE D C   
6876 O O   . PHE D 70  ? 0.3096 0.2882 0.3072 -0.0314 0.0408  0.0588  70  PHE D O   
6877 C CB  . PHE D 70  ? 0.2569 0.2270 0.2915 -0.0399 0.0620  0.0462  70  PHE D CB  
6878 C CG  . PHE D 70  ? 0.2495 0.2189 0.3093 -0.0402 0.0654  0.0395  70  PHE D CG  
6879 C CD1 . PHE D 70  ? 0.2698 0.2444 0.3409 -0.0367 0.0595  0.0310  70  PHE D CD1 
6880 C CD2 . PHE D 70  ? 0.2541 0.2184 0.3267 -0.0439 0.0737  0.0421  70  PHE D CD2 
6881 C CE1 . PHE D 70  ? 0.2367 0.2115 0.3311 -0.0362 0.0611  0.0256  70  PHE D CE1 
6882 C CE2 . PHE D 70  ? 0.2531 0.2196 0.3513 -0.0440 0.0754  0.0359  70  PHE D CE2 
6883 C CZ  . PHE D 70  ? 0.2472 0.2190 0.3558 -0.0395 0.0682  0.0278  70  PHE D CZ  
6884 N N   . ASP D 71  ? 0.3263 0.1883 0.3407 -0.0159 0.0328  0.0416  71  ASP D N   
6885 C CA  . ASP D 71  ? 0.3350 0.1786 0.3250 -0.0119 0.0316  0.0455  71  ASP D CA  
6886 C C   . ASP D 71  ? 0.3580 0.2029 0.3371 -0.0118 0.0401  0.0478  71  ASP D C   
6887 O O   . ASP D 71  ? 0.3986 0.2447 0.3816 -0.0173 0.0518  0.0516  71  ASP D O   
6888 C CB  . ASP D 71  ? 0.3928 0.2156 0.3742 -0.0164 0.0343  0.0519  71  ASP D CB  
6889 C CG  . ASP D 71  ? 0.4145 0.2144 0.3677 -0.0119 0.0313  0.0566  71  ASP D CG  
6890 O OD1 . ASP D 71  ? 0.4314 0.2301 0.3700 -0.0087 0.0332  0.0574  71  ASP D OD1 
6891 O OD2 . ASP D 71  ? 0.4524 0.2329 0.3961 -0.0118 0.0268  0.0599  71  ASP D OD2 
6892 N N   . ASP D 72  ? 0.3332 0.1803 0.3017 -0.0056 0.0344  0.0448  72  ASP D N   
6893 C CA  . ASP D 72  ? 0.3186 0.1643 0.2738 -0.0050 0.0410  0.0460  72  ASP D CA  
6894 C C   . ASP D 72  ? 0.3730 0.1963 0.2978 -0.0016 0.0384  0.0501  72  ASP D C   
6895 O O   . ASP D 72  ? 0.3728 0.1937 0.2829 0.0015  0.0373  0.0488  72  ASP D O   
6896 C CB  . ASP D 72  ? 0.3161 0.1795 0.2804 -0.0017 0.0363  0.0395  72  ASP D CB  
6897 C CG  . ASP D 72  ? 0.3278 0.1928 0.2896 0.0041  0.0225  0.0354  72  ASP D CG  
6898 O OD1 . ASP D 72  ? 0.3620 0.2166 0.3187 0.0066  0.0156  0.0367  72  ASP D OD1 
6899 O OD2 . ASP D 72  ? 0.3320 0.2089 0.2980 0.0062  0.0184  0.0307  72  ASP D OD2 
6900 N N   . SER D 73  ? 0.3890 0.1936 0.3023 -0.0024 0.0369  0.0552  73  SER D N   
6901 C CA  . SER D 73  ? 0.4212 0.2021 0.3037 0.0013  0.0323  0.0594  73  SER D CA  
6902 C C   . SER D 73  ? 0.4866 0.2510 0.3464 -0.0027 0.0461  0.0658  73  SER D C   
6903 O O   . SER D 73  ? 0.5201 0.2624 0.3493 0.0003  0.0428  0.0694  73  SER D O   
6904 C CB  . SER D 73  ? 0.4386 0.2038 0.3160 0.0031  0.0237  0.0623  73  SER D CB  
6905 O OG  . SER D 73  ? 0.4582 0.2140 0.3382 -0.0042 0.0337  0.0679  73  SER D OG  
6906 N N   . GLN D 74  ? 0.4223 0.1960 0.2961 -0.0091 0.0613  0.0673  74  GLN D N   
6907 C CA  . GLN D 74  ? 0.4446 0.2036 0.2992 -0.0132 0.0773  0.0735  74  GLN D CA  
6908 C C   . GLN D 74  ? 0.4363 0.2144 0.3075 -0.0153 0.0902  0.0706  74  GLN D C   
6909 O O   . GLN D 74  ? 0.4368 0.2389 0.3379 -0.0156 0.0879  0.0654  74  GLN D O   
6910 C CB  . GLN D 74  ? 0.4788 0.2246 0.3330 -0.0204 0.0859  0.0810  74  GLN D CB  
6911 C CG  . GLN D 74  ? 0.4818 0.2038 0.3155 -0.0179 0.0740  0.0849  74  GLN D CG  
6912 C CD  . GLN D 74  ? 0.5649 0.2704 0.3954 -0.0260 0.0831  0.0930  74  GLN D CD  
6913 O OE1 . GLN D 74  ? 0.5593 0.2786 0.4182 -0.0326 0.0882  0.0928  74  GLN D OE1 
6914 N NE2 . GLN D 74  ? 0.6043 0.2801 0.4000 -0.0260 0.0847  0.1001  74  GLN D NE2 
6915 N N   . ASP D 75  ? 0.4912 0.2565 0.3406 -0.0160 0.1041  0.0742  75  ASP D N   
6916 C CA  . ASP D 75  ? 0.5164 0.2965 0.3778 -0.0166 0.1180  0.0716  75  ASP D CA  
6917 C C   . ASP D 75  ? 0.5507 0.3444 0.4410 -0.0239 0.1323  0.0750  75  ASP D C   
6918 O O   . ASP D 75  ? 0.6096 0.3996 0.4960 -0.0271 0.1506  0.0790  75  ASP D O   
6919 C CB  . ASP D 75  ? 0.5810 0.3407 0.4068 -0.0140 0.1284  0.0736  75  ASP D CB  
6920 C CG  . ASP D 75  ? 0.5946 0.3467 0.3980 -0.0071 0.1151  0.0684  75  ASP D CG  
6921 O OD1 . ASP D 75  ? 0.5368 0.3032 0.3561 -0.0042 0.0995  0.0629  75  ASP D OD1 
6922 O OD2 . ASP D 75  ? 0.6599 0.3911 0.4289 -0.0047 0.1208  0.0696  75  ASP D OD2 
6923 N N   . LYS D 76  ? 0.4950 0.3041 0.4144 -0.0269 0.1239  0.0734  76  LYS D N   
6924 C CA  . LYS D 76  ? 0.4766 0.2988 0.4255 -0.0347 0.1345  0.0764  76  LYS D CA  
6925 C C   . LYS D 76  ? 0.4804 0.3314 0.4632 -0.0336 0.1340  0.0704  76  LYS D C   
6926 O O   . LYS D 76  ? 0.5212 0.3819 0.5136 -0.0337 0.1481  0.0706  76  LYS D O   
6927 C CB  . LYS D 76  ? 0.4904 0.3059 0.4462 -0.0400 0.1262  0.0795  76  LYS D CB  
6928 C CG  . LYS D 76  ? 0.5389 0.3235 0.4618 -0.0428 0.1314  0.0877  76  LYS D CG  
6929 C CD  . LYS D 76  ? 0.5461 0.3195 0.4729 -0.0479 0.1232  0.0912  76  LYS D CD  
6930 C CE  . LYS D 76  ? 0.5856 0.3342 0.4832 -0.0510 0.1286  0.0984  76  LYS D CE  
6931 N NZ  . LYS D 76  ? 0.6079 0.3389 0.4983 -0.0530 0.1170  0.1014  76  LYS D NZ  
6932 N N   . ALA D 77  ? 0.4013 0.2651 0.4003 -0.0316 0.1183  0.0648  77  ALA D N   
6933 C CA  . ALA D 77  ? 0.3549 0.2434 0.3829 -0.0304 0.1168  0.0596  77  ALA D CA  
6934 C C   . ALA D 77  ? 0.3670 0.2563 0.3807 -0.0228 0.1152  0.0549  77  ALA D C   
6935 O O   . ALA D 77  ? 0.3466 0.2327 0.3486 -0.0184 0.1021  0.0510  77  ALA D O   
6936 C CB  . ALA D 77  ? 0.3816 0.2809 0.4291 -0.0316 0.1017  0.0557  77  ALA D CB  
6937 N N   . VAL D 78  ? 0.3596 0.2532 0.3749 -0.0211 0.1288  0.0551  78  VAL D N   
6938 C CA  . VAL D 78  ? 0.3680 0.2569 0.3644 -0.0143 0.1286  0.0511  78  VAL D CA  
6939 C C   . VAL D 78  ? 0.3368 0.2428 0.3544 -0.0118 0.1367  0.0482  78  VAL D C   
6940 O O   . VAL D 78  ? 0.3753 0.2942 0.4183 -0.0150 0.1469  0.0505  78  VAL D O   
6941 C CB  . VAL D 78  ? 0.3867 0.2514 0.3462 -0.0125 0.1378  0.0544  78  VAL D CB  
6942 C CG1 . VAL D 78  ? 0.4137 0.2592 0.3502 -0.0141 0.1284  0.0578  78  VAL D CG1 
6943 C CG2 . VAL D 78  ? 0.4283 0.2916 0.3911 -0.0154 0.1582  0.0591  78  VAL D CG2 
6944 N N   . LEU D 79  ? 0.3271 0.2315 0.3332 -0.0058 0.1319  0.0432  79  LEU D N   
6945 C CA  . LEU D 79  ? 0.3363 0.2505 0.3535 -0.0014 0.1394  0.0400  79  LEU D CA  
6946 C C   . LEU D 79  ? 0.3787 0.2732 0.3624 0.0033  0.1481  0.0392  79  LEU D C   
6947 O O   . LEU D 79  ? 0.4150 0.2933 0.3702 0.0047  0.1390  0.0379  79  LEU D O   
6948 C CB  . LEU D 79  ? 0.3525 0.2787 0.3823 0.0010  0.1245  0.0346  79  LEU D CB  
6949 C CG  . LEU D 79  ? 0.3931 0.3316 0.4400 0.0054  0.1265  0.0310  79  LEU D CG  
6950 C CD1 . LEU D 79  ? 0.4168 0.3729 0.4974 0.0026  0.1340  0.0338  79  LEU D CD1 
6951 C CD2 . LEU D 79  ? 0.2859 0.2305 0.3372 0.0058  0.1099  0.0270  79  LEU D CD2 
6952 N N   . LYS D 80  ? 0.3694 0.2649 0.3563 0.0060  0.1655  0.0398  80  LYS D N   
6953 C CA  . LYS D 80  ? 0.4197 0.2949 0.3735 0.0110  0.1759  0.0385  80  LYS D CA  
6954 C C   . LYS D 80  ? 0.4211 0.3067 0.3912 0.0169  0.1880  0.0352  80  LYS D C   
6955 O O   . LYS D 80  ? 0.4010 0.3094 0.4086 0.0164  0.1899  0.0353  80  LYS D O   
6956 C CB  . LYS D 80  ? 0.5081 0.3647 0.4376 0.0080  0.1903  0.0444  80  LYS D CB  
6957 C CG  . LYS D 80  ? 0.5475 0.3898 0.4572 0.0031  0.1788  0.0483  80  LYS D CG  
6958 C CD  . LYS D 80  ? 0.5947 0.4115 0.4696 0.0016  0.1919  0.0538  80  LYS D CD  
6959 C CE  . LYS D 80  ? 0.6941 0.5189 0.5866 -0.0017 0.2133  0.0582  80  LYS D CE  
6960 N NZ  . LYS D 80  ? 0.7133 0.5639 0.6503 -0.0074 0.2101  0.0602  80  LYS D NZ  
6961 N N   . GLY D 81  ? 0.4106 0.2782 0.3516 0.0230  0.1952  0.0319  81  GLY D N   
6962 C CA  . GLY D 81  ? 0.4185 0.2927 0.3717 0.0301  0.2077  0.0282  81  GLY D CA  
6963 C C   . GLY D 81  ? 0.3995 0.2858 0.3706 0.0339  0.1934  0.0229  81  GLY D C   
6964 O O   . GLY D 81  ? 0.3765 0.2601 0.3403 0.0318  0.1749  0.0209  81  GLY D O   
6965 N N   . GLY D 82  ? 0.4003 0.2997 0.3956 0.0398  0.2029  0.0207  82  GLY D N   
6966 C CA  . GLY D 82  ? 0.4035 0.3101 0.4119 0.0446  0.1914  0.0159  82  GLY D CA  
6967 C C   . GLY D 82  ? 0.3920 0.2746 0.3627 0.0476  0.1832  0.0110  82  GLY D C   
6968 O O   . GLY D 82  ? 0.4575 0.3195 0.3981 0.0517  0.1941  0.0090  82  GLY D O   
6969 N N   . PRO D 83  ? 0.3819 0.2660 0.3529 0.0452  0.1640  0.0088  83  PRO D N   
6970 C CA  . PRO D 83  ? 0.4180 0.2806 0.3557 0.0462  0.1543  0.0044  83  PRO D CA  
6971 C C   . PRO D 83  ? 0.4612 0.3084 0.3693 0.0406  0.1474  0.0059  83  PRO D C   
6972 O O   . PRO D 83  ? 0.5034 0.3331 0.3846 0.0406  0.1378  0.0023  83  PRO D O   
6973 C CB  . PRO D 83  ? 0.3479 0.2220 0.3036 0.0447  0.1375  0.0025  83  PRO D CB  
6974 C CG  . PRO D 83  ? 0.3249 0.2211 0.3100 0.0390  0.1330  0.0070  83  PRO D CG  
6975 C CD  . PRO D 83  ? 0.3434 0.2489 0.3454 0.0410  0.1507  0.0103  83  PRO D CD  
6976 N N   . LEU D 84  ? 0.3941 0.2469 0.3073 0.0358  0.1508  0.0112  84  LEU D N   
6977 C CA  . LEU D 84  ? 0.3935 0.2348 0.2844 0.0307  0.1406  0.0131  84  LEU D CA  
6978 C C   . LEU D 84  ? 0.4220 0.2375 0.2745 0.0324  0.1504  0.0139  84  LEU D C   
6979 O O   . LEU D 84  ? 0.4655 0.2780 0.3162 0.0346  0.1689  0.0163  84  LEU D O   
6980 C CB  . LEU D 84  ? 0.3547 0.2118 0.2678 0.0249  0.1380  0.0184  84  LEU D CB  
6981 C CG  . LEU D 84  ? 0.3421 0.2234 0.2917 0.0233  0.1294  0.0176  84  LEU D CG  
6982 C CD1 . LEU D 84  ? 0.3582 0.2531 0.3291 0.0176  0.1281  0.0225  84  LEU D CD1 
6983 C CD2 . LEU D 84  ? 0.3380 0.2187 0.2826 0.0223  0.1114  0.0136  84  LEU D CD2 
6984 N N   . ASP D 85  ? 0.4847 0.2821 0.3072 0.0309  0.1377  0.0123  85  ASP D N   
6985 C CA  . ASP D 85  ? 0.5285 0.3002 0.3122 0.0308  0.1419  0.0143  85  ASP D CA  
6986 C C   . ASP D 85  ? 0.4977 0.2719 0.2828 0.0254  0.1333  0.0198  85  ASP D C   
6987 O O   . ASP D 85  ? 0.5156 0.2994 0.3122 0.0225  0.1158  0.0189  85  ASP D O   
6988 C CB  . ASP D 85  ? 0.5911 0.3396 0.3399 0.0328  0.1312  0.0090  85  ASP D CB  
6989 C CG  . ASP D 85  ? 0.6929 0.4346 0.4364 0.0387  0.1402  0.0033  85  ASP D CG  
6990 O OD1 . ASP D 85  ? 0.7363 0.4751 0.4785 0.0431  0.1604  0.0041  85  ASP D OD1 
6991 O OD2 . ASP D 85  ? 0.7173 0.4573 0.4600 0.0389  0.1278  -0.0018 85  ASP D OD2 
6992 N N   . GLY D 86  ? 0.5235 0.2889 0.2976 0.0241  0.1461  0.0254  86  GLY D N   
6993 C CA  . GLY D 86  ? 0.5365 0.3004 0.3091 0.0194  0.1381  0.0309  86  GLY D CA  
6994 C C   . GLY D 86  ? 0.5182 0.3077 0.3315 0.0154  0.1399  0.0344  86  GLY D C   
6995 O O   . GLY D 86  ? 0.5152 0.3227 0.3571 0.0157  0.1512  0.0343  86  GLY D O   
6996 N N   . THR D 87  ? 0.4552 0.2459 0.2714 0.0119  0.1272  0.0374  87  THR D N   
6997 C CA  . THR D 87  ? 0.4261 0.2344 0.2732 0.0075  0.1286  0.0413  87  THR D CA  
6998 C C   . THR D 87  ? 0.4282 0.2528 0.2966 0.0067  0.1100  0.0381  87  THR D C   
6999 O O   . THR D 87  ? 0.4445 0.2605 0.2970 0.0079  0.0953  0.0364  87  THR D O   
7000 C CB  . THR D 87  ? 0.4662 0.2575 0.2950 0.0041  0.1323  0.0483  87  THR D CB  
7001 O OG1 . THR D 87  ? 0.5226 0.2989 0.3315 0.0042  0.1522  0.0518  87  THR D OG1 
7002 C CG2 . THR D 87  ? 0.4532 0.2604 0.3128 -0.0011 0.1310  0.0520  87  THR D CG2 
7003 N N   . TYR D 88  ? 0.3875 0.2353 0.2916 0.0047  0.1106  0.0373  88  TYR D N   
7004 C CA  . TYR D 88  ? 0.3452 0.2083 0.2690 0.0039  0.0948  0.0340  88  TYR D CA  
7005 C C   . TYR D 88  ? 0.3474 0.2201 0.2926 -0.0003 0.0936  0.0374  88  TYR D C   
7006 O O   . TYR D 88  ? 0.3359 0.2191 0.3019 -0.0030 0.1035  0.0395  88  TYR D O   
7007 C CB  . TYR D 88  ? 0.3240 0.2033 0.2673 0.0057  0.0934  0.0291  88  TYR D CB  
7008 C CG  . TYR D 88  ? 0.3172 0.1870 0.2409 0.0094  0.0902  0.0247  88  TYR D CG  
7009 C CD1 . TYR D 88  ? 0.3342 0.1882 0.2355 0.0124  0.1017  0.0247  88  TYR D CD1 
7010 C CD2 . TYR D 88  ? 0.3075 0.1836 0.2350 0.0095  0.0764  0.0203  88  TYR D CD2 
7011 C CE1 . TYR D 88  ? 0.3504 0.1933 0.2322 0.0156  0.0980  0.0200  88  TYR D CE1 
7012 C CE2 . TYR D 88  ? 0.3083 0.1750 0.2188 0.0117  0.0726  0.0163  88  TYR D CE2 
7013 C CZ  . TYR D 88  ? 0.3544 0.2038 0.2415 0.0148  0.0827  0.0159  88  TYR D CZ  
7014 O OH  . TYR D 88  ? 0.3860 0.2239 0.2549 0.0168  0.0784  0.0113  88  TYR D OH  
7015 N N   . ARG D 89  ? 0.3439 0.2127 0.2844 -0.0009 0.0812  0.0377  89  ARG D N   
7016 C CA  . ARG D 89  ? 0.3280 0.2007 0.2835 -0.0046 0.0792  0.0408  89  ARG D CA  
7017 C C   . ARG D 89  ? 0.2985 0.1916 0.2823 -0.0056 0.0715  0.0367  89  ARG D C   
7018 O O   . ARG D 89  ? 0.2939 0.1931 0.2787 -0.0030 0.0615  0.0321  89  ARG D O   
7019 C CB  . ARG D 89  ? 0.3295 0.1866 0.2664 -0.0036 0.0696  0.0429  89  ARG D CB  
7020 C CG  . ARG D 89  ? 0.3810 0.2143 0.2884 -0.0038 0.0769  0.0486  89  ARG D CG  
7021 C CD  . ARG D 89  ? 0.3847 0.2034 0.2775 -0.0023 0.0649  0.0509  89  ARG D CD  
7022 N NE  . ARG D 89  ? 0.4219 0.2144 0.2795 -0.0014 0.0687  0.0559  89  ARG D NE  
7023 C CZ  . ARG D 89  ? 0.4186 0.1935 0.2548 0.0017  0.0571  0.0578  89  ARG D CZ  
7024 N NH1 . ARG D 89  ? 0.4382 0.2206 0.2871 0.0046  0.0422  0.0550  89  ARG D NH1 
7025 N NH2 . ARG D 89  ? 0.5191 0.2684 0.3203 0.0025  0.0606  0.0624  89  ARG D NH2 
7026 N N   . LEU D 90  ? 0.2818 0.1843 0.2876 -0.0098 0.0760  0.0386  90  LEU D N   
7027 C CA  . LEU D 90  ? 0.2572 0.1752 0.2862 -0.0111 0.0675  0.0351  90  LEU D CA  
7028 C C   . LEU D 90  ? 0.2540 0.1671 0.2772 -0.0099 0.0552  0.0335  90  LEU D C   
7029 O O   . LEU D 90  ? 0.2913 0.1918 0.3058 -0.0112 0.0547  0.0370  90  LEU D O   
7030 C CB  . LEU D 90  ? 0.2815 0.2072 0.3329 -0.0167 0.0737  0.0380  90  LEU D CB  
7031 C CG  . LEU D 90  ? 0.2574 0.1960 0.3305 -0.0188 0.0642  0.0346  90  LEU D CG  
7032 C CD1 . LEU D 90  ? 0.2528 0.2052 0.3358 -0.0158 0.0608  0.0301  90  LEU D CD1 
7033 C CD2 . LEU D 90  ? 0.2624 0.2051 0.3555 -0.0254 0.0688  0.0381  90  LEU D CD2 
7034 N N   . ILE D 91  ? 0.2406 0.1630 0.2687 -0.0073 0.0459  0.0282  91  ILE D N   
7035 C CA  . ILE D 91  ? 0.2586 0.1794 0.2855 -0.0055 0.0356  0.0259  91  ILE D CA  
7036 C C   . ILE D 91  ? 0.2246 0.1563 0.2703 -0.0075 0.0312  0.0227  91  ILE D C   
7037 O O   . ILE D 91  ? 0.2370 0.1638 0.2840 -0.0076 0.0263  0.0223  91  ILE D O   
7038 C CB  . ILE D 91  ? 0.2391 0.1604 0.2552 -0.0010 0.0282  0.0224  91  ILE D CB  
7039 C CG1 . ILE D 91  ? 0.2813 0.2033 0.3002 0.0017  0.0187  0.0197  91  ILE D CG1 
7040 C CG2 . ILE D 91  ? 0.2461 0.1800 0.2692 -0.0008 0.0278  0.0185  91  ILE D CG2 
7041 C CD1 . ILE D 91  ? 0.2898 0.2111 0.2990 0.0061  0.0113  0.0174  91  ILE D CD1 
7042 N N   . GLN D 92  ? 0.2040 0.1483 0.2627 -0.0089 0.0324  0.0205  92  GLN D N   
7043 C CA  . GLN D 92  ? 0.1950 0.1473 0.2679 -0.0107 0.0269  0.0173  92  GLN D CA  
7044 C C   . GLN D 92  ? 0.1874 0.1508 0.2738 -0.0126 0.0295  0.0169  92  GLN D C   
7045 O O   . GLN D 92  ? 0.2144 0.1802 0.2983 -0.0111 0.0346  0.0177  92  GLN D O   
7046 C CB  . GLN D 92  ? 0.2008 0.1563 0.2699 -0.0074 0.0191  0.0123  92  GLN D CB  
7047 C CG  . GLN D 92  ? 0.2148 0.1765 0.2785 -0.0050 0.0188  0.0102  92  GLN D CG  
7048 C CD  . GLN D 92  ? 0.1906 0.1621 0.2622 -0.0060 0.0162  0.0067  92  GLN D CD  
7049 O OE1 . GLN D 92  ? 0.2015 0.1768 0.2829 -0.0085 0.0170  0.0072  92  GLN D OE1 
7050 N NE2 . GLN D 92  ? 0.2310 0.2065 0.2983 -0.0042 0.0126  0.0033  92  GLN D NE2 
7051 N N   . PHE D 93  ? 0.1984 0.1673 0.2983 -0.0154 0.0251  0.0153  93  PHE D N   
7052 C CA  . PHE D 93  ? 0.1765 0.1558 0.2874 -0.0158 0.0237  0.0138  93  PHE D CA  
7053 C C   . PHE D 93  ? 0.1954 0.1768 0.3063 -0.0159 0.0147  0.0093  93  PHE D C   
7054 O O   . PHE D 93  ? 0.1794 0.1554 0.2866 -0.0164 0.0104  0.0074  93  PHE D O   
7055 C CB  . PHE D 93  ? 0.1935 0.1788 0.3234 -0.0194 0.0277  0.0169  93  PHE D CB  
7056 C CG  . PHE D 93  ? 0.1834 0.1676 0.3246 -0.0244 0.0229  0.0172  93  PHE D CG  
7057 C CD1 . PHE D 93  ? 0.1705 0.1577 0.3176 -0.0259 0.0129  0.0136  93  PHE D CD1 
7058 C CD2 . PHE D 93  ? 0.1969 0.1756 0.3419 -0.0283 0.0284  0.0212  93  PHE D CD2 
7059 C CE1 . PHE D 93  ? 0.2022 0.1865 0.3587 -0.0309 0.0077  0.0134  93  PHE D CE1 
7060 C CE2 . PHE D 93  ? 0.2024 0.1788 0.3582 -0.0339 0.0237  0.0215  93  PHE D CE2 
7061 C CZ  . PHE D 93  ? 0.2136 0.1928 0.3755 -0.0352 0.0130  0.0174  93  PHE D CZ  
7062 N N   . HIS D 94  ? 0.1785 0.1663 0.2925 -0.0152 0.0122  0.0077  94  HIS D N   
7063 C CA  . HIS D 94  ? 0.1820 0.1704 0.2932 -0.0154 0.0046  0.0038  94  HIS D CA  
7064 C C   . HIS D 94  ? 0.1788 0.1731 0.2980 -0.0157 0.0021  0.0043  94  HIS D C   
7065 O O   . HIS D 94  ? 0.1747 0.1732 0.3017 -0.0147 0.0069  0.0070  94  HIS D O   
7066 C CB  . HIS D 94  ? 0.1584 0.1451 0.2551 -0.0127 0.0042  0.0008  94  HIS D CB  
7067 C CG  . HIS D 94  ? 0.1481 0.1375 0.2401 -0.0109 0.0081  0.0019  94  HIS D CG  
7068 N ND1 . HIS D 94  ? 0.1606 0.1478 0.2479 -0.0093 0.0133  0.0038  94  HIS D ND1 
7069 C CD2 . HIS D 94  ? 0.1712 0.1631 0.2614 -0.0107 0.0070  0.0014  94  HIS D CD2 
7070 C CE1 . HIS D 94  ? 0.1641 0.1524 0.2469 -0.0082 0.0151  0.0039  94  HIS D CE1 
7071 N NE2 . HIS D 94  ? 0.1443 0.1355 0.2294 -0.0091 0.0116  0.0026  94  HIS D NE2 
7072 N N   . PHE D 95  ? 0.1807 0.1739 0.2960 -0.0163 -0.0052 0.0015  95  PHE D N   
7073 C CA  . PHE D 95  ? 0.1654 0.1617 0.2859 -0.0161 -0.0098 0.0021  95  PHE D CA  
7074 C C   . PHE D 95  ? 0.1854 0.1780 0.2898 -0.0149 -0.0121 -0.0002 95  PHE D C   
7075 O O   . PHE D 95  ? 0.1987 0.1876 0.2904 -0.0150 -0.0112 -0.0028 95  PHE D O   
7076 C CB  . PHE D 95  ? 0.1604 0.1570 0.2918 -0.0191 -0.0187 0.0016  95  PHE D CB  
7077 C CG  . PHE D 95  ? 0.1707 0.1717 0.3207 -0.0219 -0.0169 0.0040  95  PHE D CG  
7078 C CD1 . PHE D 95  ? 0.1863 0.1820 0.3337 -0.0243 -0.0150 0.0034  95  PHE D CD1 
7079 C CD2 . PHE D 95  ? 0.1788 0.1890 0.3500 -0.0223 -0.0169 0.0069  95  PHE D CD2 
7080 C CE1 . PHE D 95  ? 0.1689 0.1672 0.3330 -0.0282 -0.0133 0.0062  95  PHE D CE1 
7081 C CE2 . PHE D 95  ? 0.1843 0.1996 0.3747 -0.0260 -0.0142 0.0095  95  PHE D CE2 
7082 C CZ  . PHE D 95  ? 0.2064 0.2151 0.3924 -0.0296 -0.0123 0.0093  95  PHE D CZ  
7083 N N   . HIS D 96  ? 0.1772 0.1706 0.2833 -0.0138 -0.0151 0.0011  96  HIS D N   
7084 C CA  . HIS D 96  ? 0.1841 0.1720 0.2754 -0.0138 -0.0188 -0.0001 96  HIS D CA  
7085 C C   . HIS D 96  ? 0.1835 0.1693 0.2795 -0.0142 -0.0289 0.0005  96  HIS D C   
7086 O O   . HIS D 96  ? 0.1905 0.1821 0.3042 -0.0130 -0.0311 0.0027  96  HIS D O   
7087 C CB  . HIS D 96  ? 0.1884 0.1760 0.2750 -0.0117 -0.0138 0.0016  96  HIS D CB  
7088 C CG  . HIS D 96  ? 0.1632 0.1525 0.2460 -0.0114 -0.0057 0.0011  96  HIS D CG  
7089 N ND1 . HIS D 96  ? 0.1915 0.1787 0.2612 -0.0127 -0.0035 -0.0007 96  HIS D ND1 
7090 C CD2 . HIS D 96  ? 0.1573 0.1498 0.2473 -0.0101 0.0001  0.0024  96  HIS D CD2 
7091 C CE1 . HIS D 96  ? 0.1802 0.1697 0.2504 -0.0119 0.0018  -0.0007 96  HIS D CE1 
7092 N NE2 . HIS D 96  ? 0.1635 0.1548 0.2437 -0.0103 0.0040  0.0012  96  HIS D NE2 
7093 N N   . TRP D 97  ? 0.1876 0.1649 0.2679 -0.0157 -0.0352 -0.0015 97  TRP D N   
7094 C CA  . TRP D 97  ? 0.1805 0.1535 0.2624 -0.0161 -0.0470 -0.0011 97  TRP D CA  
7095 C C   . TRP D 97  ? 0.2243 0.1850 0.2818 -0.0169 -0.0513 -0.0021 97  TRP D C   
7096 O O   . TRP D 97  ? 0.2185 0.1754 0.2599 -0.0178 -0.0442 -0.0033 97  TRP D O   
7097 C CB  . TRP D 97  ? 0.1978 0.1711 0.2882 -0.0187 -0.0533 -0.0030 97  TRP D CB  
7098 C CG  . TRP D 97  ? 0.2086 0.1738 0.2815 -0.0207 -0.0515 -0.0073 97  TRP D CG  
7099 C CD1 . TRP D 97  ? 0.2385 0.1915 0.2908 -0.0220 -0.0576 -0.0104 97  TRP D CD1 
7100 C CD2 . TRP D 97  ? 0.2060 0.1742 0.2807 -0.0208 -0.0430 -0.0089 97  TRP D CD2 
7101 N NE1 . TRP D 97  ? 0.2388 0.1878 0.2812 -0.0224 -0.0524 -0.0144 97  TRP D NE1 
7102 C CE2 . TRP D 97  ? 0.2264 0.1848 0.2828 -0.0215 -0.0440 -0.0134 97  TRP D CE2 
7103 C CE3 . TRP D 97  ? 0.1789 0.1555 0.2670 -0.0199 -0.0347 -0.0070 97  TRP D CE3 
7104 C CZ2 . TRP D 97  ? 0.2204 0.1784 0.2748 -0.0207 -0.0377 -0.0162 97  TRP D CZ2 
7105 C CZ3 . TRP D 97  ? 0.1913 0.1663 0.2752 -0.0197 -0.0293 -0.0091 97  TRP D CZ3 
7106 C CH2 . TRP D 97  ? 0.2123 0.1786 0.2809 -0.0198 -0.0313 -0.0137 97  TRP D CH2 
7107 N N   . GLY D 98  ? 0.2244 0.1994 0.2556 0.0050  -0.0451 -0.0068 98  GLY D N   
7108 C CA  . GLY D 98  ? 0.2464 0.2062 0.2547 0.0018  -0.0499 -0.0046 98  GLY D CA  
7109 C C   . GLY D 98  ? 0.2731 0.2217 0.2624 -0.0026 -0.0542 -0.0057 98  GLY D C   
7110 O O   . GLY D 98  ? 0.2679 0.2220 0.2635 -0.0026 -0.0548 -0.0079 98  GLY D O   
7111 N N   . SER D 99  ? 0.2849 0.2149 0.2477 -0.0070 -0.0568 -0.0042 99  SER D N   
7112 C CA  . SER D 99  ? 0.3053 0.2178 0.2441 -0.0121 -0.0624 -0.0045 99  SER D CA  
7113 C C   . SER D 99  ? 0.3275 0.2298 0.2672 -0.0105 -0.0812 -0.0016 99  SER D C   
7114 O O   . SER D 99  ? 0.3782 0.2655 0.2993 -0.0144 -0.0882 -0.0018 99  SER D O   
7115 C CB  . SER D 99  ? 0.3570 0.2487 0.2631 -0.0189 -0.0565 -0.0048 99  SER D CB  
7116 O OG  . SER D 99  ? 0.3854 0.2685 0.2857 -0.0180 -0.0608 -0.0011 99  SER D OG  
7117 N N   . HIS D 100 ? 0.3283 0.2374 0.2901 -0.0051 -0.0897 0.0006  100 HIS D N   
7118 C CA  . HIS D 100 ? 0.3314 0.2344 0.3043 -0.0024 -0.1084 0.0021  100 HIS D CA  
7119 C C   . HIS D 100 ? 0.3203 0.2433 0.3322 0.0041  -0.1081 0.0013  100 HIS D C   
7120 O O   . HIS D 100 ? 0.3172 0.2530 0.3387 0.0056  -0.0948 0.0008  100 HIS D O   
7121 C CB  . HIS D 100 ? 0.3494 0.2236 0.2943 -0.0052 -0.1236 0.0059  100 HIS D CB  
7122 C CG  . HIS D 100 ? 0.3757 0.2462 0.3167 -0.0042 -0.1211 0.0083  100 HIS D CG  
7123 N ND1 . HIS D 100 ? 0.3955 0.2728 0.3629 0.0016  -0.1301 0.0096  100 HIS D ND1 
7124 C CD2 . HIS D 100 ? 0.4020 0.2627 0.3172 -0.0086 -0.1101 0.0092  100 HIS D CD2 
7125 C CE1 . HIS D 100 ? 0.3839 0.2558 0.3403 0.0010  -0.1252 0.0118  100 HIS D CE1 
7126 N NE2 . HIS D 100 ? 0.3827 0.2447 0.3076 -0.0051 -0.1129 0.0116  100 HIS D NE2 
7127 N N   . ASP D 101 ? 0.3117 0.2361 0.3468 0.0074  -0.1223 0.0006  101 ASP D N   
7128 C CA  . ASP D 101 ? 0.2945 0.2383 0.3703 0.0126  -0.1189 -0.0021 101 ASP D CA  
7129 C C   . ASP D 101 ? 0.2984 0.2427 0.3835 0.0154  -0.1185 -0.0003 101 ASP D C   
7130 O O   . ASP D 101 ? 0.2910 0.2507 0.4060 0.0186  -0.1106 -0.0029 101 ASP D O   
7131 C CB  . ASP D 101 ? 0.3247 0.2696 0.4277 0.0153  -0.1342 -0.0046 101 ASP D CB  
7132 C CG  . ASP D 101 ? 0.3064 0.2569 0.4110 0.0135  -0.1320 -0.0074 101 ASP D CG  
7133 O OD1 . ASP D 101 ? 0.3310 0.2868 0.4194 0.0107  -0.1177 -0.0078 101 ASP D OD1 
7134 O OD2 . ASP D 101 ? 0.3411 0.2905 0.4663 0.0153  -0.1462 -0.0097 101 ASP D OD2 
7135 N N   . GLY D 102 ? 0.3106 0.2367 0.3697 0.0137  -0.1261 0.0036  102 GLY D N   
7136 C CA  . GLY D 102 ? 0.3068 0.2319 0.3740 0.0164  -0.1273 0.0054  102 GLY D CA  
7137 C C   . GLY D 102 ? 0.2999 0.2340 0.3601 0.0157  -0.1085 0.0061  102 GLY D C   
7138 O O   . GLY D 102 ? 0.3105 0.2442 0.3765 0.0177  -0.1080 0.0076  102 GLY D O   
7139 N N   . GLN D 103 ? 0.2728 0.2144 0.3217 0.0129  -0.0938 0.0047  103 GLN D N   
7140 C CA  . GLN D 103 ? 0.2688 0.2198 0.3160 0.0128  -0.0773 0.0045  103 GLN D CA  
7141 C C   . GLN D 103 ? 0.2684 0.2324 0.3214 0.0120  -0.0652 0.0011  103 GLN D C   
7142 O O   . GLN D 103 ? 0.2484 0.2132 0.3022 0.0110  -0.0686 -0.0006 103 GLN D O   
7143 C CB  . GLN D 103 ? 0.3056 0.2429 0.3209 0.0089  -0.0738 0.0069  103 GLN D CB  
7144 C CG  . GLN D 103 ? 0.3378 0.2641 0.3254 0.0033  -0.0720 0.0059  103 GLN D CG  
7145 C CD  . GLN D 103 ? 0.3417 0.2495 0.2975 -0.0017 -0.0694 0.0076  103 GLN D CD  
7146 O OE1 . GLN D 103 ? 0.3731 0.2702 0.3225 -0.0011 -0.0762 0.0107  103 GLN D OE1 
7147 N NE2 . GLN D 103 ? 0.3143 0.2173 0.2506 -0.0071 -0.0589 0.0049  103 GLN D NE2 
7148 N N   . GLY D 104 ? 0.2459 0.2184 0.3015 0.0125  -0.0520 0.0003  104 GLY D N   
7149 C CA  . GLY D 104 ? 0.1934 0.1750 0.2525 0.0119  -0.0420 -0.0028 104 GLY D CA  
7150 C C   . GLY D 104 ? 0.1970 0.1865 0.2691 0.0139  -0.0319 -0.0039 104 GLY D C   
7151 O O   . GLY D 104 ? 0.2119 0.2037 0.2774 0.0129  -0.0238 -0.0055 104 GLY D O   
7152 N N   . SER D 105 ? 0.1804 0.1723 0.2711 0.0164  -0.0325 -0.0037 105 SER D N   
7153 C CA  . SER D 105 ? 0.1834 0.1789 0.2820 0.0172  -0.0214 -0.0049 105 SER D CA  
7154 C C   . SER D 105 ? 0.1897 0.1816 0.2737 0.0170  -0.0170 -0.0027 105 SER D C   
7155 O O   . SER D 105 ? 0.2099 0.1971 0.2821 0.0165  -0.0219 -0.0002 105 SER D O   
7156 C CB  . SER D 105 ? 0.1802 0.1782 0.3035 0.0190  -0.0206 -0.0064 105 SER D CB  
7157 O OG  . SER D 105 ? 0.2068 0.2019 0.3347 0.0209  -0.0274 -0.0038 105 SER D OG  
7158 N N   . GLU D 106 ? 0.1862 0.1781 0.2698 0.0169  -0.0078 -0.0039 106 GLU D N   
7159 C CA  . GLU D 106 ? 0.1737 0.1620 0.2461 0.0169  -0.0037 -0.0024 106 GLU D CA  
7160 C C   . GLU D 106 ? 0.1905 0.1771 0.2716 0.0185  -0.0011 -0.0008 106 GLU D C   
7161 O O   . GLU D 106 ? 0.1938 0.1786 0.2709 0.0192  -0.0044 0.0018  106 GLU D O   
7162 C CB  . GLU D 106 ? 0.1898 0.1757 0.2544 0.0160  0.0022  -0.0046 106 GLU D CB  
7163 C CG  . GLU D 106 ? 0.1869 0.1750 0.2445 0.0146  -0.0007 -0.0066 106 GLU D CG  
7164 C CD  . GLU D 106 ? 0.1981 0.1831 0.2473 0.0142  0.0018  -0.0087 106 GLU D CD  
7165 O OE1 . GLU D 106 ? 0.1953 0.1748 0.2433 0.0144  0.0048  -0.0097 106 GLU D OE1 
7166 O OE2 . GLU D 106 ? 0.2125 0.1985 0.2562 0.0132  0.0006  -0.0097 106 GLU D OE2 
7167 N N   . HIS D 107 ? 0.1843 0.1703 0.2774 0.0186  0.0052  -0.0028 107 HIS D N   
7168 C CA  . HIS D 107 ? 0.1922 0.1771 0.2983 0.0198  0.0081  -0.0023 107 HIS D CA  
7169 C C   . HIS D 107 ? 0.1974 0.1867 0.3203 0.0216  -0.0014 -0.0019 107 HIS D C   
7170 O O   . HIS D 107 ? 0.2011 0.1934 0.3281 0.0216  -0.0085 -0.0028 107 HIS D O   
7171 C CB  . HIS D 107 ? 0.1746 0.1551 0.2890 0.0181  0.0195  -0.0058 107 HIS D CB  
7172 C CG  . HIS D 107 ? 0.1847 0.1555 0.2792 0.0162  0.0264  -0.0056 107 HIS D CG  
7173 N ND1 . HIS D 107 ? 0.2046 0.1718 0.2864 0.0147  0.0266  -0.0070 107 HIS D ND1 
7174 C CD2 . HIS D 107 ? 0.1962 0.1590 0.2805 0.0160  0.0311  -0.0041 107 HIS D CD2 
7175 C CE1 . HIS D 107 ? 0.2175 0.1735 0.2825 0.0136  0.0303  -0.0065 107 HIS D CE1 
7176 N NE2 . HIS D 107 ? 0.2091 0.1621 0.2746 0.0142  0.0331  -0.0048 107 HIS D NE2 
7177 N N   . THR D 108 ? 0.1831 0.1712 0.3141 0.0234  -0.0031 -0.0004 108 THR D N   
7178 C CA  . THR D 108 ? 0.1894 0.1793 0.3405 0.0256  -0.0133 -0.0008 108 THR D CA  
7179 C C   . THR D 108 ? 0.1839 0.1752 0.3605 0.0266  -0.0060 -0.0040 108 THR D C   
7180 O O   . THR D 108 ? 0.2010 0.1892 0.3727 0.0253  0.0062  -0.0045 108 THR D O   
7181 C CB  . THR D 108 ? 0.1901 0.1745 0.3275 0.0268  -0.0248 0.0038  108 THR D CB  
7182 O OG1 . THR D 108 ? 0.2122 0.1936 0.3393 0.0269  -0.0183 0.0061  108 THR D OG1 
7183 C CG2 . THR D 108 ? 0.2191 0.1998 0.3315 0.0248  -0.0305 0.0059  108 THR D CG2 
7184 N N   . VAL D 109 ? 0.1737 0.1683 0.3784 0.0286  -0.0136 -0.0069 109 VAL D N   
7185 C CA  . VAL D 109 ? 0.1597 0.1563 0.3958 0.0294  -0.0066 -0.0116 109 VAL D CA  
7186 C C   . VAL D 109 ? 0.2032 0.1985 0.4526 0.0332  -0.0218 -0.0099 109 VAL D C   
7187 O O   . VAL D 109 ? 0.1988 0.1942 0.4578 0.0352  -0.0379 -0.0100 109 VAL D O   
7188 C CB  . VAL D 109 ? 0.1847 0.1863 0.4490 0.0279  -0.0002 -0.0189 109 VAL D CB  
7189 C CG1 . VAL D 109 ? 0.2123 0.2147 0.5103 0.0278  0.0104  -0.0251 109 VAL D CG1 
7190 C CG2 . VAL D 109 ? 0.2091 0.2079 0.4526 0.0238  0.0136  -0.0197 109 VAL D CG2 
7191 N N   . ASP D 110 ? 0.1949 0.1872 0.4433 0.0342  -0.0180 -0.0082 110 ASP D N   
7192 C CA  . ASP D 110 ? 0.1889 0.1774 0.4460 0.0378  -0.0336 -0.0060 110 ASP D CA  
7193 C C   . ASP D 110 ? 0.2342 0.2156 0.4650 0.0383  -0.0514 -0.0004 110 ASP D C   
7194 O O   . ASP D 110 ? 0.2636 0.2397 0.5043 0.0409  -0.0698 -0.0001 110 ASP D O   
7195 C CB  . ASP D 110 ? 0.1911 0.1841 0.4950 0.0406  -0.0388 -0.0127 110 ASP D CB  
7196 C CG  . ASP D 110 ? 0.2524 0.2494 0.5804 0.0390  -0.0187 -0.0189 110 ASP D CG  
7197 O OD1 . ASP D 110 ? 0.2354 0.2285 0.5435 0.0373  -0.0064 -0.0161 110 ASP D OD1 
7198 O OD2 . ASP D 110 ? 0.2912 0.2937 0.6507 0.0364  -0.0155 -0.0264 110 ASP D OD2 
7199 N N   . LYS D 111 ? 0.2152 0.1941 0.4112 0.0354  -0.0458 0.0034  111 LYS D N   
7200 C CA  . LYS D 111 ? 0.2558 0.2259 0.4196 0.0340  -0.0562 0.0082  111 LYS D CA  
7201 C C   . LYS D 111 ? 0.2863 0.2561 0.4510 0.0333  -0.0657 0.0068  111 LYS D C   
7202 O O   . LYS D 111 ? 0.3405 0.3013 0.4773 0.0311  -0.0730 0.0100  111 LYS D O   
7203 C CB  . LYS D 111 ? 0.3312 0.2890 0.4843 0.0354  -0.0699 0.0123  111 LYS D CB  
7204 C CG  . LYS D 111 ? 0.4548 0.4132 0.6109 0.0365  -0.0616 0.0134  111 LYS D CG  
7205 C CD  . LYS D 111 ? 0.5805 0.5419 0.7153 0.0338  -0.0453 0.0149  111 LYS D CD  
7206 C CE  . LYS D 111 ? 0.6698 0.6222 0.7694 0.0306  -0.0485 0.0185  111 LYS D CE  
7207 N NZ  . LYS D 111 ? 0.7100 0.6653 0.7915 0.0280  -0.0345 0.0190  111 LYS D NZ  
7208 N N   . LYS D 112 ? 0.2342 0.2126 0.4290 0.0344  -0.0645 0.0017  112 LYS D N   
7209 C CA  . LYS D 112 ? 0.2727 0.2510 0.4707 0.0339  -0.0742 0.0001  112 LYS D CA  
7210 C C   . LYS D 112 ? 0.2446 0.2280 0.4258 0.0306  -0.0622 -0.0005 112 LYS D C   
7211 O O   . LYS D 112 ? 0.2206 0.2109 0.4054 0.0294  -0.0458 -0.0026 112 LYS D O   
7212 C CB  . LYS D 112 ? 0.3298 0.3154 0.5714 0.0364  -0.0780 -0.0062 112 LYS D CB  
7213 C CG  . LYS D 112 ? 0.4644 0.4517 0.7151 0.0360  -0.0870 -0.0090 112 LYS D CG  
7214 C CD  . LYS D 112 ? 0.5025 0.5017 0.7685 0.0338  -0.0694 -0.0144 112 LYS D CD  
7215 C CE  . LYS D 112 ? 0.5345 0.5375 0.8248 0.0343  -0.0783 -0.0192 112 LYS D CE  
7216 N NZ  . LYS D 112 ? 0.5906 0.5846 0.8564 0.0339  -0.0955 -0.0151 112 LYS D NZ  
7217 N N   . LYS D 113 ? 0.2193 0.1972 0.3809 0.0289  -0.0710 0.0013  113 LYS D N   
7218 C CA  . LYS D 113 ? 0.2126 0.1949 0.3607 0.0260  -0.0621 0.0002  113 LYS D CA  
7219 C C   . LYS D 113 ? 0.2161 0.2039 0.3840 0.0262  -0.0661 -0.0038 113 LYS D C   
7220 O O   . LYS D 113 ? 0.2710 0.2555 0.4550 0.0281  -0.0809 -0.0049 113 LYS D O   
7221 C CB  . LYS D 113 ? 0.2240 0.1960 0.3361 0.0231  -0.0663 0.0040  113 LYS D CB  
7222 C CG  . LYS D 113 ? 0.2478 0.2161 0.3406 0.0220  -0.0588 0.0068  113 LYS D CG  
7223 C CD  . LYS D 113 ? 0.3169 0.2743 0.3762 0.0179  -0.0601 0.0089  113 LYS D CD  
7224 C CE  . LYS D 113 ? 0.3222 0.2787 0.3667 0.0165  -0.0494 0.0101  113 LYS D CE  
7225 N NZ  . LYS D 113 ? 0.3489 0.2999 0.3683 0.0119  -0.0439 0.0093  113 LYS D NZ  
7226 N N   . TYR D 114 ? 0.2015 0.1965 0.3689 0.0243  -0.0535 -0.0064 114 TYR D N   
7227 C CA  . TYR D 114 ? 0.2207 0.2204 0.4011 0.0237  -0.0556 -0.0100 114 TYR D CA  
7228 C C   . TYR D 114 ? 0.2043 0.1997 0.3565 0.0212  -0.0589 -0.0079 114 TYR D C   
7229 O O   . TYR D 114 ? 0.2125 0.2030 0.3382 0.0195  -0.0557 -0.0048 114 TYR D O   
7230 C CB  . TYR D 114 ? 0.2153 0.2226 0.4115 0.0225  -0.0389 -0.0147 114 TYR D CB  
7231 C CG  . TYR D 114 ? 0.2174 0.2280 0.4455 0.0240  -0.0336 -0.0187 114 TYR D CG  
7232 C CD1 . TYR D 114 ? 0.2307 0.2393 0.4560 0.0242  -0.0245 -0.0175 114 TYR D CD1 
7233 C CD2 . TYR D 114 ? 0.2574 0.2730 0.5206 0.0248  -0.0368 -0.0245 114 TYR D CD2 
7234 C CE1 . TYR D 114 ? 0.2714 0.2823 0.5264 0.0249  -0.0179 -0.0219 114 TYR D CE1 
7235 C CE2 . TYR D 114 ? 0.2578 0.2765 0.5542 0.0256  -0.0303 -0.0296 114 TYR D CE2 
7236 C CZ  . TYR D 114 ? 0.2653 0.2812 0.5563 0.0256  -0.0205 -0.0282 114 TYR D CZ  
7237 O OH  . TYR D 114 ? 0.3443 0.3623 0.6679 0.0258  -0.0119 -0.0339 114 TYR D OH  
7238 N N   . ALA D 115 ? 0.2101 0.2078 0.3700 0.0205  -0.0636 -0.0104 115 ALA D N   
7239 C CA  . ALA D 115 ? 0.2023 0.1954 0.3371 0.0179  -0.0665 -0.0091 115 ALA D CA  
7240 C C   . ALA D 115 ? 0.1964 0.1940 0.3170 0.0158  -0.0519 -0.0098 115 ALA D C   
7241 O O   . ALA D 115 ? 0.2219 0.2152 0.3192 0.0134  -0.0516 -0.0086 115 ALA D O   
7242 C CB  . ALA D 115 ? 0.2232 0.2179 0.3718 0.0178  -0.0752 -0.0119 115 ALA D CB  
7243 N N   . ALA D 116 ? 0.2140 0.1914 0.3035 0.0068  -0.0541 0.0088  116 ALA D N   
7244 C CA  . ALA D 116 ? 0.2160 0.1933 0.2985 0.0037  -0.0401 0.0065  116 ALA D CA  
7245 C C   . ALA D 116 ? 0.2123 0.1967 0.3129 0.0060  -0.0287 0.0080  116 ALA D C   
7246 O O   . ALA D 116 ? 0.1993 0.1893 0.3198 0.0096  -0.0304 0.0098  116 ALA D O   
7247 C CB  . ALA D 116 ? 0.2252 0.2056 0.3111 -0.0008 -0.0409 0.0011  116 ALA D CB  
7248 N N   . GLU D 117 ? 0.1996 0.1830 0.2926 0.0040  -0.0171 0.0070  117 GLU D N   
7249 C CA  . GLU D 117 ? 0.1863 0.1744 0.2907 0.0052  -0.0057 0.0080  117 GLU D CA  
7250 C C   . GLU D 117 ? 0.1947 0.1844 0.2978 0.0018  0.0021  0.0058  117 GLU D C   
7251 O O   . GLU D 117 ? 0.2042 0.1892 0.2910 -0.0004 0.0030  0.0044  117 GLU D O   
7252 C CB  . GLU D 117 ? 0.1884 0.1700 0.2796 0.0073  -0.0006 0.0106  117 GLU D CB  
7253 C CG  . GLU D 117 ? 0.1846 0.1693 0.2855 0.0087  0.0102  0.0110  117 GLU D CG  
7254 C CD  . GLU D 117 ? 0.1954 0.1727 0.2848 0.0107  0.0138  0.0128  117 GLU D CD  
7255 O OE1 . GLU D 117 ? 0.2159 0.1875 0.2999 0.0128  0.0067  0.0150  117 GLU D OE1 
7256 O OE2 . GLU D 117 ? 0.2129 0.1894 0.2987 0.0100  0.0231  0.0122  117 GLU D OE2 
7257 N N   . LEU D 118 ? 0.1680 0.1642 0.2890 0.0014  0.0084  0.0058  118 LEU D N   
7258 C CA  . LEU D 118 ? 0.1694 0.1661 0.2909 -0.0014 0.0161  0.0051  118 LEU D CA  
7259 C C   . LEU D 118 ? 0.1657 0.1604 0.2801 -0.0005 0.0264  0.0072  118 LEU D C   
7260 O O   . LEU D 118 ? 0.1829 0.1792 0.3041 0.0017  0.0308  0.0083  118 LEU D O   
7261 C CB  . LEU D 118 ? 0.1762 0.1799 0.3213 -0.0032 0.0168  0.0043  118 LEU D CB  
7262 C CG  . LEU D 118 ? 0.1778 0.1813 0.3265 -0.0059 0.0268  0.0052  118 LEU D CG  
7263 C CD1 . LEU D 118 ? 0.1815 0.1790 0.3165 -0.0082 0.0255  0.0040  118 LEU D CD1 
7264 C CD2 . LEU D 118 ? 0.1726 0.1834 0.3474 -0.0082 0.0280  0.0044  118 LEU D CD2 
7265 N N   . HIS D 119 ? 0.1783 0.1690 0.2790 -0.0020 0.0300  0.0073  119 HIS D N   
7266 C CA  . HIS D 119 ? 0.1870 0.1753 0.2791 -0.0018 0.0381  0.0091  119 HIS D CA  
7267 C C   . HIS D 119 ? 0.1916 0.1791 0.2852 -0.0038 0.0431  0.0103  119 HIS D C   
7268 O O   . HIS D 119 ? 0.1905 0.1760 0.2797 -0.0050 0.0405  0.0097  119 HIS D O   
7269 C CB  . HIS D 119 ? 0.1911 0.1751 0.2656 -0.0016 0.0369  0.0087  119 HIS D CB  
7270 C CG  . HIS D 119 ? 0.1857 0.1677 0.2557 0.0001  0.0339  0.0087  119 HIS D CG  
7271 N ND1 . HIS D 119 ? 0.1681 0.1461 0.2244 -0.0005 0.0317  0.0081  119 HIS D ND1 
7272 C CD2 . HIS D 119 ? 0.1725 0.1552 0.2508 0.0024  0.0330  0.0093  119 HIS D CD2 
7273 C CE1 . HIS D 119 ? 0.1927 0.1676 0.2470 0.0011  0.0294  0.0090  119 HIS D CE1 
7274 N NE2 . HIS D 119 ? 0.1820 0.1598 0.2501 0.0033  0.0295  0.0098  119 HIS D NE2 
7275 N N   . LEU D 120 ? 0.2013 0.1891 0.2999 -0.0042 0.0508  0.0122  120 LEU D N   
7276 C CA  . LEU D 120 ? 0.2010 0.1854 0.2968 -0.0063 0.0567  0.0148  120 LEU D CA  
7277 C C   . LEU D 120 ? 0.2099 0.1892 0.2876 -0.0057 0.0602  0.0163  120 LEU D C   
7278 O O   . LEU D 120 ? 0.1984 0.1769 0.2724 -0.0049 0.0650  0.0160  120 LEU D O   
7279 C CB  . LEU D 120 ? 0.1977 0.1846 0.3091 -0.0080 0.0639  0.0158  120 LEU D CB  
7280 C CG  . LEU D 120 ? 0.1931 0.1856 0.3247 -0.0095 0.0594  0.0139  120 LEU D CG  
7281 C CD1 . LEU D 120 ? 0.2394 0.2395 0.3910 -0.0087 0.0618  0.0124  120 LEU D CD1 
7282 C CD2 . LEU D 120 ? 0.2382 0.2277 0.3755 -0.0133 0.0624  0.0157  120 LEU D CD2 
7283 N N   . VAL D 121 ? 0.2111 0.1869 0.2784 -0.0059 0.0573  0.0176  121 VAL D N   
7284 C CA  . VAL D 121 ? 0.2104 0.1828 0.2617 -0.0054 0.0570  0.0183  121 VAL D CA  
7285 C C   . VAL D 121 ? 0.2241 0.1903 0.2662 -0.0066 0.0616  0.0225  121 VAL D C   
7286 O O   . VAL D 121 ? 0.2277 0.1911 0.2726 -0.0073 0.0613  0.0253  121 VAL D O   
7287 C CB  . VAL D 121 ? 0.2083 0.1821 0.2566 -0.0045 0.0502  0.0169  121 VAL D CB  
7288 C CG1 . VAL D 121 ? 0.2046 0.1766 0.2399 -0.0042 0.0487  0.0172  121 VAL D CG1 
7289 C CG2 . VAL D 121 ? 0.2242 0.2019 0.2781 -0.0039 0.0462  0.0132  121 VAL D CG2 
7290 N N   . HIS D 122 ? 0.2219 0.1843 0.2513 -0.0070 0.0656  0.0228  122 HIS D N   
7291 C CA  . HIS D 122 ? 0.2342 0.1887 0.2502 -0.0085 0.0702  0.0269  122 HIS D CA  
7292 C C   . HIS D 122 ? 0.2471 0.1976 0.2446 -0.0084 0.0664  0.0267  122 HIS D C   
7293 O O   . HIS D 122 ? 0.2498 0.2030 0.2453 -0.0080 0.0648  0.0226  122 HIS D O   
7294 C CB  . HIS D 122 ? 0.2429 0.1946 0.2598 -0.0102 0.0815  0.0272  122 HIS D CB  
7295 C CG  . HIS D 122 ? 0.2353 0.1933 0.2744 -0.0105 0.0851  0.0260  122 HIS D CG  
7296 N ND1 . HIS D 122 ? 0.2199 0.1858 0.2736 -0.0086 0.0822  0.0218  122 HIS D ND1 
7297 C CD2 . HIS D 122 ? 0.2452 0.2026 0.2950 -0.0128 0.0909  0.0286  122 HIS D CD2 
7298 C CE1 . HIS D 122 ? 0.2262 0.1971 0.2995 -0.0095 0.0849  0.0216  122 HIS D CE1 
7299 N NE2 . HIS D 122 ? 0.2540 0.2202 0.3262 -0.0124 0.0909  0.0254  122 HIS D NE2 
7300 N N   . TRP D 123 ? 0.2623 0.2054 0.2456 -0.0091 0.0647  0.0313  123 TRP D N   
7301 C CA  . TRP D 123 ? 0.2658 0.2051 0.2314 -0.0093 0.0593  0.0312  123 TRP D CA  
7302 C C   . TRP D 123 ? 0.2783 0.2060 0.2219 -0.0116 0.0645  0.0346  123 TRP D C   
7303 O O   . TRP D 123 ? 0.3113 0.2324 0.2516 -0.0127 0.0703  0.0396  123 TRP D O   
7304 C CB  . TRP D 123 ? 0.2493 0.1915 0.2176 -0.0073 0.0482  0.0328  123 TRP D CB  
7305 C CG  . TRP D 123 ? 0.2615 0.1987 0.2316 -0.0062 0.0467  0.0390  123 TRP D CG  
7306 C CD1 . TRP D 123 ? 0.2591 0.1993 0.2464 -0.0051 0.0473  0.0396  123 TRP D CD1 
7307 C CD2 . TRP D 123 ? 0.2800 0.2065 0.2331 -0.0064 0.0438  0.0457  123 TRP D CD2 
7308 N NE1 . TRP D 123 ? 0.2711 0.2032 0.2546 -0.0043 0.0453  0.0460  123 TRP D NE1 
7309 C CE2 . TRP D 123 ? 0.2670 0.1903 0.2293 -0.0050 0.0434  0.0505  123 TRP D CE2 
7310 C CE3 . TRP D 123 ? 0.3089 0.2272 0.2386 -0.0077 0.0410  0.0480  123 TRP D CE3 
7311 C CZ2 . TRP D 123 ? 0.2792 0.1910 0.2288 -0.0045 0.0400  0.0583  123 TRP D CZ2 
7312 C CZ3 . TRP D 123 ? 0.3239 0.2307 0.2387 -0.0074 0.0374  0.0558  123 TRP D CZ3 
7313 C CH2 . TRP D 123 ? 0.3366 0.2400 0.2617 -0.0056 0.0369  0.0614  123 TRP D CH2 
7314 N N   . ASN D 124 ? 0.3073 0.2314 0.2344 -0.0127 0.0627  0.0317  124 ASN D N   
7315 C CA  . ASN D 124 ? 0.3152 0.2269 0.2168 -0.0154 0.0682  0.0331  124 ASN D CA  
7316 C C   . ASN D 124 ? 0.3393 0.2422 0.2238 -0.0156 0.0609  0.0403  124 ASN D C   
7317 O O   . ASN D 124 ? 0.3519 0.2577 0.2353 -0.0142 0.0482  0.0407  124 ASN D O   
7318 C CB  . ASN D 124 ? 0.3208 0.2318 0.2117 -0.0167 0.0663  0.0265  124 ASN D CB  
7319 C CG  . ASN D 124 ? 0.3828 0.2804 0.2463 -0.0198 0.0737  0.0255  124 ASN D CG  
7320 O OD1 . ASN D 124 ? 0.4060 0.2933 0.2530 -0.0213 0.0779  0.0311  124 ASN D OD1 
7321 N ND2 . ASN D 124 ? 0.3748 0.2709 0.2322 -0.0211 0.0762  0.0182  124 ASN D ND2 
7322 N N   . THR D 125 ? 0.3425 0.2343 0.2143 -0.0175 0.0690  0.0461  125 THR D N   
7323 C CA  . THR D 125 ? 0.3647 0.2456 0.2180 -0.0175 0.0615  0.0543  125 THR D CA  
7324 C C   . THR D 125 ? 0.4051 0.2767 0.2286 -0.0191 0.0542  0.0540  125 THR D C   
7325 O O   . THR D 125 ? 0.4780 0.3396 0.2832 -0.0188 0.0455  0.0611  125 THR D O   
7326 C CB  . THR D 125 ? 0.4132 0.2825 0.2582 -0.0199 0.0730  0.0612  125 THR D CB  
7327 O OG1 . THR D 125 ? 0.4678 0.3290 0.2948 -0.0237 0.0869  0.0584  125 THR D OG1 
7328 C CG2 . THR D 125 ? 0.3969 0.2752 0.2722 -0.0188 0.0784  0.0612  125 THR D CG2 
7329 N N   . LYS D 126 ? 0.4079 0.2812 0.2248 -0.0209 0.0570  0.0460  126 LYS D N   
7330 C CA  . LYS D 126 ? 0.4810 0.3486 0.2747 -0.0225 0.0468  0.0436  126 LYS D CA  
7331 C C   . LYS D 126 ? 0.4398 0.3160 0.2447 -0.0195 0.0283  0.0454  126 LYS D C   
7332 O O   . LYS D 126 ? 0.4922 0.3619 0.2776 -0.0201 0.0161  0.0476  126 LYS D O   
7333 C CB  . LYS D 126 ? 0.5008 0.3717 0.2954 -0.0244 0.0530  0.0333  126 LYS D CB  
7334 C CG  . LYS D 126 ? 0.4926 0.3607 0.2703 -0.0267 0.0425  0.0279  126 LYS D CG  
7335 C CD  . LYS D 126 ? 0.5028 0.3724 0.2837 -0.0285 0.0514  0.0176  126 LYS D CD  
7336 C CE  . LYS D 126 ? 0.5546 0.4204 0.3185 -0.0317 0.0403  0.0116  126 LYS D CE  
7337 N NZ  . LYS D 126 ? 0.5442 0.4108 0.3128 -0.0335 0.0466  0.0015  126 LYS D NZ  
7338 N N   . TYR D 127 ? 0.3844 0.2750 0.2207 -0.0162 0.0259  0.0443  127 TYR D N   
7339 C CA  . TYR D 127 ? 0.3915 0.2926 0.2441 -0.0131 0.0111  0.0446  127 TYR D CA  
7340 C C   . TYR D 127 ? 0.4380 0.3381 0.3012 -0.0093 0.0082  0.0526  127 TYR D C   
7341 O O   . TYR D 127 ? 0.4466 0.3396 0.3077 -0.0098 0.0183  0.0570  127 TYR D O   
7342 C CB  . TYR D 127 ? 0.3438 0.2602 0.2217 -0.0127 0.0122  0.0364  127 TYR D CB  
7343 C CG  . TYR D 127 ? 0.3569 0.2711 0.2230 -0.0166 0.0165  0.0289  127 TYR D CG  
7344 C CD1 . TYR D 127 ? 0.3885 0.2984 0.2369 -0.0191 0.0069  0.0265  127 TYR D CD1 
7345 C CD2 . TYR D 127 ? 0.3392 0.2548 0.2123 -0.0175 0.0293  0.0241  127 TYR D CD2 
7346 C CE1 . TYR D 127 ? 0.3897 0.2955 0.2261 -0.0230 0.0109  0.0193  127 TYR D CE1 
7347 C CE2 . TYR D 127 ? 0.3549 0.2668 0.2180 -0.0205 0.0335  0.0174  127 TYR D CE2 
7348 C CZ  . TYR D 127 ? 0.3739 0.2806 0.2183 -0.0235 0.0247  0.0145  127 TYR D CZ  
7349 O OH  . TYR D 127 ? 0.4179 0.3190 0.2508 -0.0268 0.0288  0.0071  127 TYR D OH  
7350 N N   . GLY D 128 ? 0.4579 0.3647 0.3340 -0.0057 -0.0052 0.0545  128 GLY D N   
7351 C CA  . GLY D 128 ? 0.4476 0.3491 0.3286 -0.0019 -0.0088 0.0630  128 GLY D CA  
7352 C C   . GLY D 128 ? 0.3996 0.3078 0.3062 0.0001  -0.0005 0.0621  128 GLY D C   
7353 O O   . GLY D 128 ? 0.4228 0.3229 0.3305 0.0015  0.0021  0.0687  128 GLY D O   
7354 N N   . ASP D 129 ? 0.3450 0.2667 0.2713 -0.0001 0.0030  0.0542  129 ASP D N   
7355 C CA  . ASP D 129 ? 0.3233 0.2522 0.2736 0.0018  0.0084  0.0521  129 ASP D CA  
7356 C C   . ASP D 129 ? 0.2983 0.2389 0.2603 0.0002  0.0130  0.0434  129 ASP D C   
7357 O O   . ASP D 129 ? 0.2982 0.2410 0.2517 -0.0022 0.0117  0.0394  129 ASP D O   
7358 C CB  . ASP D 129 ? 0.3317 0.2648 0.2994 0.0069  -0.0007 0.0543  129 ASP D CB  
7359 C CG  . ASP D 129 ? 0.3845 0.3269 0.3581 0.0086  -0.0123 0.0512  129 ASP D CG  
7360 O OD1 . ASP D 129 ? 0.3568 0.3085 0.3350 0.0063  -0.0106 0.0442  129 ASP D OD1 
7361 O OD2 . ASP D 129 ? 0.4340 0.3741 0.4083 0.0123  -0.0233 0.0561  129 ASP D OD2 
7362 N N   . PHE D 130 ? 0.2789 0.2258 0.2595 0.0012  0.0177  0.0406  130 PHE D N   
7363 C CA  . PHE D 130 ? 0.2715 0.2272 0.2614 -0.0003 0.0220  0.0336  130 PHE D CA  
7364 C C   . PHE D 130 ? 0.2576 0.2218 0.2518 -0.0002 0.0154  0.0291  130 PHE D C   
7365 O O   . PHE D 130 ? 0.2467 0.2135 0.2374 -0.0029 0.0178  0.0247  130 PHE D O   
7366 C CB  . PHE D 130 ? 0.2725 0.2327 0.2799 0.0010  0.0257  0.0315  130 PHE D CB  
7367 C CG  . PHE D 130 ? 0.2257 0.1934 0.2404 -0.0003 0.0288  0.0252  130 PHE D CG  
7368 C CD1 . PHE D 130 ? 0.2357 0.2114 0.2592 0.0004  0.0253  0.0210  130 PHE D CD1 
7369 C CD2 . PHE D 130 ? 0.2430 0.2097 0.2561 -0.0022 0.0356  0.0237  130 PHE D CD2 
7370 C CE1 . PHE D 130 ? 0.2420 0.2224 0.2691 -0.0012 0.0285  0.0161  130 PHE D CE1 
7371 C CE2 . PHE D 130 ? 0.2332 0.2050 0.2517 -0.0030 0.0373  0.0189  130 PHE D CE2 
7372 C CZ  . PHE D 130 ? 0.2346 0.2123 0.2581 -0.0028 0.0339  0.0154  130 PHE D CZ  
7373 N N   . GLY D 131 ? 0.2628 0.2312 0.2666 0.0027  0.0073  0.0302  131 GLY D N   
7374 C CA  . GLY D 131 ? 0.2360 0.2143 0.2488 0.0024  0.0018  0.0255  131 GLY D CA  
7375 C C   . GLY D 131 ? 0.2547 0.2313 0.2529 -0.0008 -0.0029 0.0246  131 GLY D C   
7376 O O   . GLY D 131 ? 0.2445 0.2278 0.2473 -0.0034 -0.0033 0.0191  131 GLY D O   
7377 N N   . LYS D 132 ? 0.2486 0.2151 0.2280 -0.0010 -0.0064 0.0296  132 LYS D N   
7378 C CA  . LYS D 132 ? 0.2581 0.2206 0.2195 -0.0046 -0.0104 0.0279  132 LYS D CA  
7379 C C   . LYS D 132 ? 0.2941 0.2523 0.2454 -0.0083 0.0004  0.0239  132 LYS D C   
7380 O O   . LYS D 132 ? 0.2856 0.2450 0.2322 -0.0117 -0.0002 0.0186  132 LYS D O   
7381 C CB  . LYS D 132 ? 0.2928 0.2434 0.2330 -0.0039 -0.0171 0.0348  132 LYS D CB  
7382 C CG  . LYS D 132 ? 0.3112 0.2661 0.2622 0.0003  -0.0305 0.0387  132 LYS D CG  
7383 C CD  . LYS D 132 ? 0.3888 0.3292 0.3174 0.0017  -0.0373 0.0476  132 LYS D CD  
7384 C CE  . LYS D 132 ? 0.4548 0.4002 0.3970 0.0067  -0.0523 0.0514  132 LYS D CE  
7385 N NZ  . LYS D 132 ? 0.5712 0.5002 0.4882 0.0080  -0.0599 0.0611  132 LYS D NZ  
7386 N N   . ALA D 133 ? 0.2859 0.2388 0.2353 -0.0077 0.0103  0.0262  133 ALA D N   
7387 C CA  . ALA D 133 ? 0.2668 0.2154 0.2083 -0.0103 0.0205  0.0229  133 ALA D CA  
7388 C C   . ALA D 133 ? 0.2818 0.2386 0.2371 -0.0113 0.0231  0.0167  133 ALA D C   
7389 O O   . ALA D 133 ? 0.2669 0.2205 0.2148 -0.0138 0.0273  0.0126  133 ALA D O   
7390 C CB  . ALA D 133 ? 0.2613 0.2052 0.2041 -0.0093 0.0301  0.0264  133 ALA D CB  
7391 N N   . VAL D 134 ? 0.2494 0.2152 0.2235 -0.0094 0.0214  0.0160  134 VAL D N   
7392 C CA  . VAL D 134 ? 0.2336 0.2049 0.2179 -0.0105 0.0252  0.0112  134 VAL D CA  
7393 C C   . VAL D 134 ? 0.2546 0.2285 0.2373 -0.0138 0.0212  0.0068  134 VAL D C   
7394 O O   . VAL D 134 ? 0.2443 0.2194 0.2311 -0.0156 0.0250  0.0032  134 VAL D O   
7395 C CB  . VAL D 134 ? 0.2268 0.2053 0.2281 -0.0082 0.0251  0.0114  134 VAL D CB  
7396 C CG1 . VAL D 134 ? 0.2203 0.2057 0.2310 -0.0071 0.0176  0.0112  134 VAL D CG1 
7397 C CG2 . VAL D 134 ? 0.2186 0.2000 0.2267 -0.0095 0.0299  0.0076  134 VAL D CG2 
7398 N N   . GLN D 135 ? 0.2483 0.2221 0.2248 -0.0147 0.0131  0.0071  135 GLN D N   
7399 C CA  . GLN D 135 ? 0.2453 0.2214 0.2205 -0.0187 0.0083  0.0023  135 GLN D CA  
7400 C C   . GLN D 135 ? 0.2900 0.2554 0.2452 -0.0219 0.0108  -0.0003 135 GLN D C   
7401 O O   . GLN D 135 ? 0.3495 0.3149 0.3016 -0.0259 0.0065  -0.0049 135 GLN D O   
7402 C CB  . GLN D 135 ? 0.2658 0.2479 0.2458 -0.0182 -0.0036 0.0034  135 GLN D CB  
7403 C CG  . GLN D 135 ? 0.2403 0.2336 0.2433 -0.0147 -0.0054 0.0047  135 GLN D CG  
7404 C CD  . GLN D 135 ? 0.2256 0.2270 0.2448 -0.0169 0.0002  -0.0002 135 GLN D CD  
7405 O OE1 . GLN D 135 ? 0.2775 0.2789 0.2949 -0.0215 0.0013  -0.0045 135 GLN D OE1 
7406 N NE2 . GLN D 135 ? 0.1982 0.2052 0.2318 -0.0138 0.0040  0.0005  135 GLN D NE2 
7407 N N   . GLN D 136 ? 0.2832 0.2396 0.2260 -0.0207 0.0182  0.0019  136 GLN D N   
7408 C CA  . GLN D 136 ? 0.3177 0.2628 0.2400 -0.0234 0.0218  -0.0010 136 GLN D CA  
7409 C C   . GLN D 136 ? 0.3073 0.2479 0.2313 -0.0230 0.0334  -0.0034 136 GLN D C   
7410 O O   . GLN D 136 ? 0.2980 0.2417 0.2330 -0.0198 0.0389  -0.0005 136 GLN D O   
7411 C CB  . GLN D 136 ? 0.3385 0.2746 0.2412 -0.0226 0.0212  0.0035  136 GLN D CB  
7412 C CG  . GLN D 136 ? 0.3733 0.3120 0.2730 -0.0222 0.0082  0.0071  136 GLN D CG  
7413 C CD  . GLN D 136 ? 0.4324 0.3713 0.3248 -0.0262 -0.0018 0.0021  136 GLN D CD  
7414 O OE1 . GLN D 136 ? 0.4863 0.4185 0.3672 -0.0300 0.0019  -0.0039 136 GLN D OE1 
7415 N NE2 . GLN D 136 ? 0.4348 0.3816 0.3361 -0.0254 -0.0149 0.0040  136 GLN D NE2 
7416 N N   . PRO D 137 ? 0.3110 0.2442 0.2254 -0.0258 0.0368  -0.0089 137 PRO D N   
7417 C CA  . PRO D 137 ? 0.3193 0.2484 0.2385 -0.0244 0.0473  -0.0110 137 PRO D CA  
7418 C C   . PRO D 137 ? 0.3364 0.2621 0.2535 -0.0213 0.0560  -0.0078 137 PRO D C   
7419 O O   . PRO D 137 ? 0.3449 0.2728 0.2753 -0.0185 0.0623  -0.0073 137 PRO D O   
7420 C CB  . PRO D 137 ? 0.3566 0.2757 0.2624 -0.0281 0.0491  -0.0179 137 PRO D CB  
7421 C CG  . PRO D 137 ? 0.4079 0.3304 0.3108 -0.0322 0.0380  -0.0200 137 PRO D CG  
7422 C CD  . PRO D 137 ? 0.3752 0.3039 0.2769 -0.0305 0.0305  -0.0141 137 PRO D CD  
7423 N N   . ASP D 138 ? 0.3061 0.2260 0.2066 -0.0219 0.0567  -0.0056 138 ASP D N   
7424 C CA  . ASP D 138 ? 0.3195 0.2359 0.2181 -0.0200 0.0661  -0.0023 138 ASP D CA  
7425 C C   . ASP D 138 ? 0.3002 0.2227 0.2070 -0.0180 0.0624  0.0048  138 ASP D C   
7426 O O   . ASP D 138 ? 0.3235 0.2414 0.2240 -0.0177 0.0683  0.0087  138 ASP D O   
7427 C CB  . ASP D 138 ? 0.3363 0.2394 0.2085 -0.0226 0.0718  -0.0041 138 ASP D CB  
7428 C CG  . ASP D 138 ? 0.3931 0.2921 0.2453 -0.0251 0.0611  -0.0017 138 ASP D CG  
7429 O OD1 . ASP D 138 ? 0.3913 0.2985 0.2525 -0.0248 0.0493  0.0003  138 ASP D OD1 
7430 O OD2 . ASP D 138 ? 0.4500 0.3367 0.2764 -0.0275 0.0646  -0.0018 138 ASP D OD2 
7431 N N   . GLY D 139 ? 0.2888 0.2208 0.2096 -0.0169 0.0535  0.0062  139 GLY D N   
7432 C CA  . GLY D 139 ? 0.2842 0.2205 0.2113 -0.0150 0.0487  0.0122  139 GLY D CA  
7433 C C   . GLY D 139 ? 0.2701 0.2103 0.2131 -0.0126 0.0549  0.0150  139 GLY D C   
7434 O O   . GLY D 139 ? 0.2744 0.2126 0.2167 -0.0119 0.0553  0.0200  139 GLY D O   
7435 N N   . LEU D 140 ? 0.2581 0.2032 0.2156 -0.0115 0.0585  0.0120  140 LEU D N   
7436 C CA  . LEU D 140 ? 0.2277 0.1779 0.2020 -0.0095 0.0614  0.0140  140 LEU D CA  
7437 C C   . LEU D 140 ? 0.2634 0.2125 0.2442 -0.0088 0.0702  0.0119  140 LEU D C   
7438 O O   . LEU D 140 ? 0.2734 0.2192 0.2498 -0.0091 0.0734  0.0081  140 LEU D O   
7439 C CB  . LEU D 140 ? 0.2133 0.1715 0.2014 -0.0083 0.0552  0.0129  140 LEU D CB  
7440 C CG  . LEU D 140 ? 0.2407 0.2025 0.2285 -0.0083 0.0470  0.0138  140 LEU D CG  
7441 C CD1 . LEU D 140 ? 0.2360 0.2047 0.2372 -0.0074 0.0443  0.0120  140 LEU D CD1 
7442 C CD2 . LEU D 140 ? 0.2534 0.2130 0.2393 -0.0074 0.0449  0.0187  140 LEU D CD2 
7443 N N   . ALA D 141 ? 0.2485 0.2007 0.2424 -0.0078 0.0737  0.0143  141 ALA D N   
7444 C CA  . ALA D 141 ? 0.2479 0.2025 0.2556 -0.0064 0.0805  0.0125  141 ALA D CA  
7445 C C   . ALA D 141 ? 0.2367 0.1990 0.2630 -0.0050 0.0759  0.0136  141 ALA D C   
7446 O O   . ALA D 141 ? 0.2440 0.2075 0.2737 -0.0058 0.0742  0.0166  141 ALA D O   
7447 C CB  . ALA D 141 ? 0.2767 0.2267 0.2817 -0.0076 0.0916  0.0136  141 ALA D CB  
7448 N N   . VAL D 142 ? 0.2119 0.1780 0.2488 -0.0030 0.0732  0.0113  142 VAL D N   
7449 C CA  . VAL D 142 ? 0.2157 0.1880 0.2677 -0.0020 0.0677  0.0119  142 VAL D CA  
7450 C C   . VAL D 142 ? 0.2058 0.1818 0.2752 -0.0002 0.0714  0.0109  142 VAL D C   
7451 O O   . VAL D 142 ? 0.2337 0.2081 0.3050 0.0019  0.0739  0.0089  142 VAL D O   
7452 C CB  . VAL D 142 ? 0.2084 0.1819 0.2575 -0.0014 0.0594  0.0108  142 VAL D CB  
7453 C CG1 . VAL D 142 ? 0.2146 0.1928 0.2759 -0.0009 0.0536  0.0110  142 VAL D CG1 
7454 C CG2 . VAL D 142 ? 0.2188 0.1907 0.2554 -0.0031 0.0563  0.0113  142 VAL D CG2 
7455 N N   . LEU D 143 ? 0.2183 0.1990 0.3020 -0.0010 0.0720  0.0121  143 LEU D N   
7456 C CA  . LEU D 143 ? 0.2143 0.2010 0.3199 0.0004  0.0743  0.0111  143 LEU D CA  
7457 C C   . LEU D 143 ? 0.2085 0.1997 0.3231 0.0019  0.0628  0.0104  143 LEU D C   
7458 O O   . LEU D 143 ? 0.2086 0.2008 0.3223 0.0001  0.0568  0.0109  143 LEU D O   
7459 C CB  . LEU D 143 ? 0.2282 0.2172 0.3446 -0.0024 0.0815  0.0125  143 LEU D CB  
7460 C CG  . LEU D 143 ? 0.2452 0.2422 0.3885 -0.0017 0.0850  0.0112  143 LEU D CG  
7461 C CD1 . LEU D 143 ? 0.2493 0.2463 0.3977 0.0012  0.0935  0.0089  143 LEU D CD1 
7462 C CD2 . LEU D 143 ? 0.2254 0.2234 0.3772 -0.0060 0.0931  0.0130  143 LEU D CD2 
7463 N N   . GLY D 144 ? 0.1913 0.1831 0.3115 0.0053  0.0595  0.0094  144 GLY D N   
7464 C CA  . GLY D 144 ? 0.2114 0.2050 0.3355 0.0068  0.0479  0.0094  144 GLY D CA  
7465 C C   . GLY D 144 ? 0.1878 0.1892 0.3374 0.0089  0.0447  0.0089  144 GLY D C   
7466 O O   . GLY D 144 ? 0.1920 0.1961 0.3558 0.0113  0.0512  0.0081  144 GLY D O   
7467 N N   . ILE D 145 ? 0.1739 0.1791 0.3303 0.0076  0.0351  0.0086  145 ILE D N   
7468 C CA  . ILE D 145 ? 0.1911 0.2050 0.3736 0.0087  0.0295  0.0077  145 ILE D CA  
7469 C C   . ILE D 145 ? 0.1952 0.2079 0.3741 0.0100  0.0141  0.0079  145 ILE D C   
7470 O O   . ILE D 145 ? 0.2024 0.2104 0.3642 0.0073  0.0087  0.0075  145 ILE D O   
7471 C CB  . ILE D 145 ? 0.1865 0.2061 0.3826 0.0043  0.0332  0.0066  145 ILE D CB  
7472 C CG1 . ILE D 145 ? 0.2062 0.2244 0.4007 0.0026  0.0490  0.0074  145 ILE D CG1 
7473 C CG2 . ILE D 145 ? 0.1852 0.2156 0.4121 0.0047  0.0265  0.0051  145 ILE D CG2 
7474 C CD1 . ILE D 145 ? 0.2417 0.2626 0.4467 -0.0024 0.0553  0.0075  145 ILE D CD1 
7475 N N   . PHE D 146 ? 0.1864 0.2025 0.3805 0.0143  0.0071  0.0086  146 PHE D N   
7476 C CA  . PHE D 146 ? 0.1764 0.1897 0.3650 0.0158  -0.0088 0.0096  146 PHE D CA  
7477 C C   . PHE D 146 ? 0.2024 0.2232 0.4064 0.0129  -0.0186 0.0073  146 PHE D C   
7478 O O   . PHE D 146 ? 0.1980 0.2292 0.4291 0.0119  -0.0149 0.0055  146 PHE D O   
7479 C CB  . PHE D 146 ? 0.1670 0.1798 0.3663 0.0222  -0.0143 0.0120  146 PHE D CB  
7480 C CG  . PHE D 146 ? 0.1992 0.2025 0.3824 0.0248  -0.0062 0.0139  146 PHE D CG  
7481 C CD1 . PHE D 146 ? 0.1934 0.1851 0.3461 0.0229  -0.0075 0.0156  146 PHE D CD1 
7482 C CD2 . PHE D 146 ? 0.1989 0.2047 0.3983 0.0286  0.0037  0.0133  146 PHE D CD2 
7483 C CE1 . PHE D 146 ? 0.2290 0.2119 0.3683 0.0245  -0.0004 0.0169  146 PHE D CE1 
7484 C CE2 . PHE D 146 ? 0.2036 0.1994 0.3880 0.0306  0.0108  0.0142  146 PHE D CE2 
7485 C CZ  . PHE D 146 ? 0.2268 0.2111 0.3811 0.0283  0.0083  0.0161  146 PHE D CZ  
7486 N N   . LEU D 147 ? 0.1971 0.2120 0.3835 0.0111  -0.0307 0.0069  147 LEU D N   
7487 C CA  . LEU D 147 ? 0.1971 0.2170 0.3948 0.0082  -0.0430 0.0040  147 LEU D CA  
7488 C C   . LEU D 147 ? 0.2084 0.2270 0.4076 0.0121  -0.0601 0.0060  147 LEU D C   
7489 O O   . LEU D 147 ? 0.2335 0.2404 0.4053 0.0134  -0.0660 0.0086  147 LEU D O   
7490 C CB  . LEU D 147 ? 0.2079 0.2206 0.3826 0.0029  -0.0444 0.0010  147 LEU D CB  
7491 C CG  . LEU D 147 ? 0.1931 0.2080 0.3720 -0.0015 -0.0323 -0.0014 147 LEU D CG  
7492 C CD1 . LEU D 147 ? 0.2061 0.2183 0.3763 -0.0002 -0.0168 0.0012  147 LEU D CD1 
7493 C CD2 . LEU D 147 ? 0.2104 0.2182 0.3709 -0.0060 -0.0362 -0.0052 147 LEU D CD2 
7494 N N   . LYS D 148 ? 0.2066 0.2368 0.4376 0.0135  -0.0684 0.0049  148 LYS D N   
7495 C CA  . LYS D 148 ? 0.2274 0.2579 0.4646 0.0175  -0.0870 0.0069  148 LYS D CA  
7496 C C   . LYS D 148 ? 0.2608 0.2948 0.5023 0.0127  -0.1021 0.0027  148 LYS D C   
7497 O O   . LYS D 148 ? 0.2968 0.3411 0.5611 0.0083  -0.0983 -0.0016 148 LYS D O   
7498 C CB  . LYS D 148 ? 0.2815 0.3242 0.5567 0.0237  -0.0861 0.0084  148 LYS D CB  
7499 C CG  . LYS D 148 ? 0.3706 0.4163 0.6607 0.0290  -0.1062 0.0109  148 LYS D CG  
7500 C CD  . LYS D 148 ? 0.4212 0.4814 0.7553 0.0350  -0.1011 0.0110  148 LYS D CD  
7501 C CE  . LYS D 148 ? 0.5116 0.5767 0.8678 0.0419  -0.1220 0.0139  148 LYS D CE  
7502 N NZ  . LYS D 148 ? 0.5816 0.6291 0.9039 0.0458  -0.1362 0.0200  148 LYS D NZ  
7503 N N   . VAL D 149 ? 0.2696 0.2943 0.4899 0.0134  -0.1197 0.0042  149 VAL D N   
7504 C CA  . VAL D 149 ? 0.3241 0.3497 0.5438 0.0086  -0.1362 -0.0004 149 VAL D CA  
7505 C C   . VAL D 149 ? 0.2979 0.3406 0.5618 0.0103  -0.1482 -0.0019 149 VAL D C   
7506 O O   . VAL D 149 ? 0.3368 0.3840 0.6182 0.0172  -0.1565 0.0024  149 VAL D O   
7507 C CB  . VAL D 149 ? 0.3808 0.3897 0.5613 0.0088  -0.1514 0.0019  149 VAL D CB  
7508 C CG1 . VAL D 149 ? 0.4249 0.4350 0.6068 0.0045  -0.1715 -0.0030 149 VAL D CG1 
7509 C CG2 . VAL D 149 ? 0.3979 0.3920 0.5385 0.0053  -0.1386 0.0013  149 VAL D CG2 
7510 N N   . GLY D 150 ? 0.2762 0.3279 0.5594 0.0039  -0.1497 -0.0082 150 GLY D N   
7511 C CA  . GLY D 150 ? 0.2800 0.3496 0.6086 0.0038  -0.1601 -0.0109 150 GLY D CA  
7512 C C   . GLY D 150 ? 0.2823 0.3565 0.6210 -0.0054 -0.1592 -0.0184 150 GLY D C   
7513 O O   . GLY D 150 ? 0.2969 0.3589 0.6050 -0.0104 -0.1665 -0.0220 150 GLY D O   
7514 N N   . SER D 151 ? 0.2833 0.3736 0.6639 -0.0079 -0.1496 -0.0211 151 SER D N   
7515 C CA  . SER D 151 ? 0.2407 0.3349 0.6343 -0.0171 -0.1472 -0.0278 151 SER D CA  
7516 C C   . SER D 151 ? 0.2258 0.3070 0.5895 -0.0213 -0.1292 -0.0285 151 SER D C   
7517 O O   . SER D 151 ? 0.2496 0.3247 0.5962 -0.0173 -0.1138 -0.0238 151 SER D O   
7518 C CB  . SER D 151 ? 0.2665 0.3735 0.6976 -0.0176 -0.1340 -0.0284 151 SER D CB  
7519 O OG  . SER D 151 ? 0.3569 0.4709 0.8071 -0.0137 -0.1476 -0.0283 151 SER D OG  
7520 N N   . ALA D 152 ? 0.2655 0.3419 0.6235 -0.0291 -0.1319 -0.0347 152 ALA D N   
7521 C CA  . ALA D 152 ? 0.2778 0.3417 0.6106 -0.0327 -0.1158 -0.0356 152 ALA D CA  
7522 C C   . ALA D 152 ? 0.2783 0.3492 0.6331 -0.0333 -0.0938 -0.0326 152 ALA D C   
7523 O O   . ALA D 152 ? 0.2857 0.3714 0.6801 -0.0351 -0.0912 -0.0332 152 ALA D O   
7524 C CB  . ALA D 152 ? 0.2733 0.3307 0.6004 -0.0410 -0.1240 -0.0436 152 ALA D CB  
7525 N N   . LEU D 153 ? 0.2514 0.3116 0.5803 -0.0321 -0.0778 -0.0294 153 LEU D N   
7526 C CA  . LEU D 153 ? 0.2192 0.2826 0.5608 -0.0327 -0.0572 -0.0260 153 LEU D CA  
7527 C C   . LEU D 153 ? 0.1997 0.2562 0.5398 -0.0399 -0.0496 -0.0290 153 LEU D C   
7528 O O   . LEU D 153 ? 0.2161 0.2589 0.5256 -0.0403 -0.0482 -0.0299 153 LEU D O   
7529 C CB  . LEU D 153 ? 0.2312 0.2871 0.5464 -0.0267 -0.0455 -0.0203 153 LEU D CB  
7530 C CG  . LEU D 153 ? 0.2617 0.3201 0.5860 -0.0263 -0.0250 -0.0161 153 LEU D CG  
7531 C CD1 . LEU D 153 ? 0.2420 0.3160 0.6043 -0.0247 -0.0208 -0.0152 153 LEU D CD1 
7532 C CD2 . LEU D 153 ? 0.2344 0.2834 0.5279 -0.0212 -0.0168 -0.0117 153 LEU D CD2 
7533 N N   . PRO D 154 ? 0.1822 0.2604 0.6082 -0.0130 -0.0314 -0.0174 154 PRO D N   
7534 C CA  . PRO D 154 ? 0.1937 0.2585 0.6359 -0.0191 -0.0226 -0.0307 154 PRO D CA  
7535 C C   . PRO D 154 ? 0.2031 0.2396 0.6181 -0.0140 -0.0085 -0.0203 154 PRO D C   
7536 O O   . PRO D 154 ? 0.2384 0.2667 0.6539 -0.0175 -0.0060 -0.0298 154 PRO D O   
7537 C CB  . PRO D 154 ? 0.2248 0.2838 0.7047 -0.0203 -0.0121 -0.0287 154 PRO D CB  
7538 C CG  . PRO D 154 ? 0.2387 0.3192 0.7223 -0.0194 -0.0238 -0.0249 154 PRO D CG  
7539 C CD  . PRO D 154 ? 0.2228 0.3074 0.6789 -0.0126 -0.0283 -0.0105 154 PRO D CD  
7540 N N   . GLY D 155 ? 0.2166 0.2416 0.6091 -0.0056 0.0001  -0.0027 155 GLY D N   
7541 C CA  . GLY D 155 ? 0.2214 0.2282 0.5862 -0.0005 0.0117  0.0073  155 GLY D CA  
7542 C C   . GLY D 155 ? 0.2093 0.2116 0.5387 0.0001  0.0020  0.0028  155 GLY D C   
7543 O O   . GLY D 155 ? 0.2423 0.2313 0.5527 0.0030  0.0100  0.0096  155 GLY D O   
7544 N N   . LEU D 156 ? 0.1922 0.2100 0.5132 -0.0016 -0.0148 -0.0054 156 LEU D N   
7545 C CA  . LEU D 156 ? 0.2050 0.2230 0.4949 -0.0004 -0.0233 -0.0081 156 LEU D CA  
7546 C C   . LEU D 156 ? 0.2106 0.2359 0.5092 -0.0076 -0.0273 -0.0272 156 LEU D C   
7547 O O   . LEU D 156 ? 0.2097 0.2326 0.4849 -0.0067 -0.0302 -0.0306 156 LEU D O   
7548 C CB  . LEU D 156 ? 0.2017 0.2402 0.4809 0.0037  -0.0374 -0.0015 156 LEU D CB  
7549 C CG  . LEU D 156 ? 0.2109 0.2543 0.4604 0.0075  -0.0456 0.0030  156 LEU D CG  
7550 C CD1 . LEU D 156 ? 0.1888 0.2038 0.4165 0.0122  -0.0360 0.0108  156 LEU D CD1 
7551 C CD2 . LEU D 156 ? 0.1977 0.2687 0.4519 0.0123  -0.0574 0.0166  156 LEU D CD2 
7552 N N   . GLN D 157 ? 0.1991 0.2338 0.5358 -0.0149 -0.0264 -0.0423 157 GLN D N   
7553 C CA  . GLN D 157 ? 0.2109 0.2618 0.5610 -0.0227 -0.0330 -0.0693 157 GLN D CA  
7554 C C   . GLN D 157 ? 0.2146 0.2416 0.5657 -0.0235 -0.0208 -0.0731 157 GLN D C   
7555 O O   . GLN D 157 ? 0.2155 0.2529 0.5561 -0.0260 -0.0263 -0.0914 157 GLN D O   
7556 C CB  . GLN D 157 ? 0.2234 0.2908 0.6247 -0.0314 -0.0345 -0.0889 157 GLN D CB  
7557 C CG  . GLN D 157 ? 0.2694 0.3700 0.6793 -0.0391 -0.0471 -0.1244 157 GLN D CG  
7558 C CD  . GLN D 157 ? 0.3306 0.4731 0.6995 -0.0362 -0.0674 -0.1250 157 GLN D CD  
7559 O OE1 . GLN D 157 ? 0.3211 0.4790 0.6762 -0.0308 -0.0759 -0.1035 157 GLN D OE1 
7560 N NE2 . GLN D 157 ? 0.3018 0.4654 0.6545 -0.0385 -0.0731 -0.1476 157 GLN D NE2 
7561 N N   . LYS D 158 ? 0.2043 0.2037 0.5670 -0.0202 -0.0036 -0.0537 158 LYS D N   
7562 C CA  . LYS D 158 ? 0.2307 0.2111 0.6015 -0.0204 0.0086  -0.0519 158 LYS D CA  
7563 C C   . LYS D 158 ? 0.2024 0.1789 0.5231 -0.0152 0.0023  -0.0466 158 LYS D C   
7564 O O   . LYS D 158 ? 0.2442 0.2151 0.5680 -0.0171 0.0056  -0.0567 158 LYS D O   
7565 C CB  . LYS D 158 ? 0.2592 0.2263 0.6429 -0.0140 0.0274  -0.0233 158 LYS D CB  
7566 C CG  . LYS D 158 ? 0.2936 0.2575 0.6893 -0.0111 0.0408  -0.0159 158 LYS D CG  
7567 C CD  . LYS D 158 ? 0.3198 0.2840 0.7138 -0.0038 0.0557  0.0177  158 LYS D CD  
7568 C CE  . LYS D 158 ? 0.3183 0.2847 0.7259 -0.0003 0.0677  0.0302  158 LYS D CE  
7569 N NZ  . LYS D 158 ? 0.3055 0.2819 0.7770 0.0013  0.0806  0.0292  158 LYS D NZ  
7570 N N   . VAL D 159 ? 0.1754 0.1542 0.4562 -0.0085 -0.0052 -0.0307 159 VAL D N   
7571 C CA  . VAL D 159 ? 0.1829 0.1600 0.4229 -0.0034 -0.0119 -0.0247 159 VAL D CA  
7572 C C   . VAL D 159 ? 0.2165 0.2176 0.4484 -0.0065 -0.0245 -0.0449 159 VAL D C   
7573 O O   . VAL D 159 ? 0.2284 0.2278 0.4492 -0.0064 -0.0235 -0.0520 159 VAL D O   
7574 C CB  . VAL D 159 ? 0.2123 0.1895 0.4268 0.0036  -0.0168 -0.0072 159 VAL D CB  
7575 C CG1 . VAL D 159 ? 0.2204 0.1989 0.4032 0.0085  -0.0246 -0.0014 159 VAL D CG1 
7576 C CG2 . VAL D 159 ? 0.2342 0.1960 0.4486 0.0077  -0.0040 0.0092  159 VAL D CG2 
7577 N N   . VAL D 160 ? 0.2256 0.2556 0.4619 -0.0083 -0.0366 -0.0531 160 VAL D N   
7578 C CA  A VAL D 160 ? 0.2567 0.3243 0.4799 -0.0096 -0.0501 -0.0692 160 VAL D CA  
7579 C CA  B VAL D 160 ? 0.2541 0.3193 0.4747 -0.0091 -0.0494 -0.0679 160 VAL D CA  
7580 C C   . VAL D 160 ? 0.2714 0.3449 0.5135 -0.0172 -0.0458 -0.1012 160 VAL D C   
7581 O O   . VAL D 160 ? 0.2894 0.3841 0.5123 -0.0165 -0.0504 -0.1143 160 VAL D O   
7582 C CB  A VAL D 160 ? 0.2827 0.3875 0.5160 -0.0110 -0.0633 -0.0712 160 VAL D CB  
7583 C CB  B VAL D 160 ? 0.2825 0.3867 0.5042 -0.0084 -0.0641 -0.0650 160 VAL D CB  
7584 C CG1 A VAL D 160 ? 0.2907 0.4455 0.5232 -0.0159 -0.0757 -0.0988 160 VAL D CG1 
7585 C CG1 B VAL D 160 ? 0.2923 0.3872 0.4997 0.0007  -0.0655 -0.0325 160 VAL D CG1 
7586 C CG2 A VAL D 160 ? 0.3005 0.4108 0.5148 -0.0019 -0.0694 -0.0404 160 VAL D CG2 
7587 C CG2 B VAL D 160 ? 0.2744 0.3847 0.5347 -0.0160 -0.0637 -0.0804 160 VAL D CG2 
7588 N N   . ASP D 161 ? 0.2566 0.3131 0.5429 -0.0241 -0.0352 -0.1146 161 ASP D N   
7589 C CA  . ASP D 161 ? 0.2775 0.3409 0.5997 -0.0326 -0.0298 -0.1506 161 ASP D CA  
7590 C C   . ASP D 161 ? 0.2801 0.3207 0.5963 -0.0304 -0.0182 -0.1500 161 ASP D C   
7591 O O   . ASP D 161 ? 0.3820 0.4359 0.7203 -0.0362 -0.0153 -0.1840 161 ASP D O   
7592 C CB  . ASP D 161 ? 0.2988 0.3464 0.6806 -0.0385 -0.0177 -0.1582 161 ASP D CB  
7593 C CG  . ASP D 161 ? 0.2867 0.3639 0.6823 -0.0418 -0.0287 -0.1713 161 ASP D CG  
7594 O OD1 . ASP D 161 ? 0.3006 0.4197 0.6705 -0.0434 -0.0476 -0.1831 161 ASP D OD1 
7595 O OD2 . ASP D 161 ? 0.3136 0.3761 0.7455 -0.0410 -0.0180 -0.1660 161 ASP D OD2 
7596 N N   . VAL D 162 ? 0.2236 0.2328 0.5157 -0.0226 -0.0109 -0.1150 162 VAL D N   
7597 C CA  . VAL D 162 ? 0.2399 0.2261 0.5311 -0.0201 0.0009  -0.1089 162 VAL D CA  
7598 C C   . VAL D 162 ? 0.2414 0.2404 0.4818 -0.0140 -0.0082 -0.1041 162 VAL D C   
7599 O O   . VAL D 162 ? 0.2557 0.2422 0.4945 -0.0123 -0.0002 -0.1044 162 VAL D O   
7600 C CB  . VAL D 162 ? 0.2355 0.1885 0.5314 -0.0150 0.0136  -0.0724 162 VAL D CB  
7601 C CG1 . VAL D 162 ? 0.2703 0.2196 0.5147 -0.0066 0.0057  -0.0448 162 VAL D CG1 
7602 C CG2 . VAL D 162 ? 0.2698 0.2127 0.5853 -0.0136 0.0297  -0.0639 162 VAL D CG2 
7603 N N   . LEU D 163 ? 0.2456 0.2714 0.4510 -0.0100 -0.0236 -0.0976 163 LEU D N   
7604 C CA  . LEU D 163 ? 0.2375 0.2727 0.4010 -0.0021 -0.0299 -0.0820 163 LEU D CA  
7605 C C   . LEU D 163 ? 0.2838 0.3437 0.4415 -0.0034 -0.0292 -0.1075 163 LEU D C   
7606 O O   . LEU D 163 ? 0.2509 0.3063 0.3846 0.0028  -0.0271 -0.0944 163 LEU D O   
7607 C CB  . LEU D 163 ? 0.2288 0.2908 0.3694 0.0032  -0.0443 -0.0647 163 LEU D CB  
7608 C CG  . LEU D 163 ? 0.2268 0.2643 0.3722 0.0059  -0.0433 -0.0405 163 LEU D CG  
7609 C CD1 . LEU D 163 ? 0.2239 0.2902 0.3581 0.0116  -0.0562 -0.0229 163 LEU D CD1 
7610 C CD2 . LEU D 163 ? 0.2307 0.2307 0.3669 0.0102  -0.0341 -0.0204 163 LEU D CD2 
7611 N N   . ASP D 164 ? 0.3032 0.3937 0.4837 -0.0112 -0.0312 -0.1462 164 ASP D N   
7612 C CA  . ASP D 164 ? 0.3321 0.4528 0.5069 -0.0123 -0.0295 -0.1763 164 ASP D CA  
7613 C C   . ASP D 164 ? 0.3025 0.3844 0.5000 -0.0132 -0.0115 -0.1808 164 ASP D C   
7614 O O   . ASP D 164 ? 0.3223 0.4221 0.5107 -0.0118 -0.0074 -0.1990 164 ASP D O   
7615 C CB  . ASP D 164 ? 0.4497 0.6167 0.6499 -0.0217 -0.0352 -0.2253 164 ASP D CB  
7616 C CG  . ASP D 164 ? 0.5676 0.8003 0.7324 -0.0183 -0.0552 -0.2242 164 ASP D CG  
7617 O OD1 . ASP D 164 ? 0.5943 0.8416 0.7170 -0.0077 -0.0619 -0.1886 164 ASP D OD1 
7618 O OD2 . ASP D 164 ? 0.6060 0.8792 0.7905 -0.0260 -0.0641 -0.2568 164 ASP D OD2 
7619 N N   . SER D 165 ? 0.2461 0.2802 0.4733 -0.0146 0.0000  -0.1619 165 SER D N   
7620 C CA  . SER D 165 ? 0.2438 0.2435 0.4972 -0.0143 0.0174  -0.1570 165 SER D CA  
7621 C C   . SER D 165 ? 0.2306 0.2083 0.4461 -0.0048 0.0178  -0.1169 165 SER D C   
7622 O O   . SER D 165 ? 0.2762 0.2302 0.5098 -0.0035 0.0311  -0.1097 165 SER D O   
7623 C CB  . SER D 165 ? 0.3247 0.2964 0.6352 -0.0193 0.0314  -0.1502 165 SER D CB  
7624 O OG  . SER D 165 ? 0.3373 0.2866 0.6334 -0.0147 0.0300  -0.1109 165 SER D OG  
7625 N N   . ILE D 166 ? 0.2311 0.2177 0.4019 0.0017  0.0041  -0.0918 166 ILE D N   
7626 C CA  . ILE D 166 ? 0.2237 0.1912 0.3661 0.0098  0.0037  -0.0578 166 ILE D CA  
7627 C C   . ILE D 166 ? 0.2427 0.2407 0.3455 0.0166  -0.0088 -0.0497 166 ILE D C   
7628 O O   . ILE D 166 ? 0.2162 0.2093 0.2997 0.0224  -0.0162 -0.0223 166 ILE D O   
7629 C CB  . ILE D 166 ? 0.2034 0.1453 0.3462 0.0115  0.0035  -0.0291 166 ILE D CB  
7630 C CG1 . ILE D 166 ? 0.1991 0.1559 0.3343 0.0108  -0.0074 -0.0286 166 ILE D CG1 
7631 C CG2 . ILE D 166 ? 0.2332 0.1506 0.4189 0.0072  0.0193  -0.0272 166 ILE D CG2 
7632 C CD1 . ILE D 166 ? 0.2056 0.1457 0.3275 0.0155  -0.0099 -0.0003 166 ILE D CD1 
7633 N N   . LYS D 167 ? 0.2402 0.2066 0.3246 -0.0073 -0.0111 -0.0418 167 LYS D N   
7634 C CA  . LYS D 167 ? 0.2596 0.2278 0.3343 -0.0084 -0.0132 -0.0414 167 LYS D CA  
7635 C C   . LYS D 167 ? 0.2579 0.2272 0.3227 -0.0077 -0.0081 -0.0410 167 LYS D C   
7636 O O   . LYS D 167 ? 0.2700 0.2399 0.3284 -0.0083 -0.0079 -0.0379 167 LYS D O   
7637 C CB  . LYS D 167 ? 0.2856 0.2529 0.3542 -0.0099 -0.0184 -0.0471 167 LYS D CB  
7638 C CG  . LYS D 167 ? 0.3911 0.3584 0.4467 -0.0111 -0.0210 -0.0463 167 LYS D CG  
7639 C CD  . LYS D 167 ? 0.4617 0.4273 0.5093 -0.0126 -0.0262 -0.0524 167 LYS D CD  
7640 C CE  . LYS D 167 ? 0.5613 0.5254 0.5935 -0.0138 -0.0288 -0.0512 167 LYS D CE  
7641 N NZ  . LYS D 167 ? 0.6479 0.6096 0.6695 -0.0153 -0.0328 -0.0578 167 LYS D NZ  
7642 N N   . THR D 168 ? 0.2344 0.2039 0.2979 -0.0065 -0.0045 -0.0447 168 THR D N   
7643 C CA  . THR D 168 ? 0.2256 0.1971 0.2807 -0.0064 0.0001  -0.0457 168 THR D CA  
7644 C C   . THR D 168 ? 0.2405 0.2128 0.3005 -0.0042 0.0043  -0.0435 168 THR D C   
7645 O O   . THR D 168 ? 0.2221 0.1924 0.2902 -0.0026 0.0041  -0.0421 168 THR D O   
7646 C CB  . THR D 168 ? 0.2685 0.2408 0.3171 -0.0069 0.0008  -0.0531 168 THR D CB  
7647 O OG1 . THR D 168 ? 0.2842 0.2551 0.3406 -0.0052 -0.0005 -0.0568 168 THR D OG1 
7648 C CG2 . THR D 168 ? 0.2947 0.2657 0.3342 -0.0093 -0.0029 -0.0550 168 THR D CG2 
7649 N N   . LYS D 169 ? 0.2366 0.2112 0.2909 -0.0045 0.0082  -0.0434 169 LYS D N   
7650 C CA  . LYS D 169 ? 0.2355 0.2109 0.2931 -0.0026 0.0116  -0.0416 169 LYS D CA  
7651 C C   . LYS D 169 ? 0.2430 0.2177 0.3065 0.0001  0.0114  -0.0448 169 LYS D C   
7652 O O   . LYS D 169 ? 0.2338 0.2097 0.2968 0.0006  0.0111  -0.0508 169 LYS D O   
7653 C CB  . LYS D 169 ? 0.2262 0.2049 0.2774 -0.0037 0.0156  -0.0431 169 LYS D CB  
7654 C CG  . LYS D 169 ? 0.2206 0.2004 0.2752 -0.0018 0.0183  -0.0418 169 LYS D CG  
7655 C CD  . LYS D 169 ? 0.2358 0.2190 0.2856 -0.0035 0.0224  -0.0433 169 LYS D CD  
7656 C CE  . LYS D 169 ? 0.2548 0.2390 0.3086 -0.0014 0.0241  -0.0426 169 LYS D CE  
7657 N NZ  . LYS D 169 ? 0.3173 0.3048 0.3676 -0.0037 0.0281  -0.0440 169 LYS D NZ  
7658 N N   . GLY D 170 ? 0.2195 0.1918 0.2878 0.0021  0.0119  -0.0410 170 GLY D N   
7659 C CA  . GLY D 170 ? 0.2262 0.1962 0.2986 0.0050  0.0114  -0.0427 170 GLY D CA  
7660 C C   . GLY D 170 ? 0.2481 0.2130 0.3259 0.0054  0.0086  -0.0420 170 GLY D C   
7661 O O   . GLY D 170 ? 0.2668 0.2274 0.3476 0.0079  0.0080  -0.0419 170 GLY D O   
7662 N N   . LYS D 171 ? 0.2159 0.1806 0.2948 0.0029  0.0065  -0.0418 171 LYS D N   
7663 C CA  . LYS D 171 ? 0.2315 0.1915 0.3168 0.0027  0.0040  -0.0417 171 LYS D CA  
7664 C C   . LYS D 171 ? 0.2303 0.1867 0.3202 0.0026  0.0056  -0.0352 171 LYS D C   
7665 O O   . LYS D 171 ? 0.2285 0.1870 0.3176 0.0017  0.0075  -0.0311 171 LYS D O   
7666 C CB  . LYS D 171 ? 0.2419 0.2029 0.3280 0.0000  0.0005  -0.0439 171 LYS D CB  
7667 C CG  . LYS D 171 ? 0.2671 0.2303 0.3476 -0.0002 -0.0007 -0.0509 171 LYS D CG  
7668 C CD  . LYS D 171 ? 0.3395 0.3016 0.4208 -0.0025 -0.0051 -0.0539 171 LYS D CD  
7669 C CE  . LYS D 171 ? 0.3602 0.3173 0.4500 -0.0020 -0.0074 -0.0558 171 LYS D CE  
7670 N NZ  . LYS D 171 ? 0.4137 0.3699 0.5042 -0.0044 -0.0123 -0.0601 171 LYS D NZ  
7671 N N   . SER D 172 ? 0.2411 0.1915 0.3358 0.0034  0.0052  -0.0343 172 SER D N   
7672 C CA  A SER D 172 ? 0.2408 0.1869 0.3395 0.0028  0.0077  -0.0284 172 SER D CA  
7673 C CA  B SER D 172 ? 0.2398 0.1854 0.3382 0.0031  0.0078  -0.0284 172 SER D CA  
7674 C C   . SER D 172 ? 0.2412 0.1817 0.3474 0.0013  0.0062  -0.0285 172 SER D C   
7675 O O   . SER D 172 ? 0.2708 0.2099 0.3786 0.0014  0.0029  -0.0334 172 SER D O   
7676 C CB  A SER D 172 ? 0.2533 0.1954 0.3471 0.0057  0.0104  -0.0257 172 SER D CB  
7677 C CB  B SER D 172 ? 0.2584 0.1997 0.3518 0.0062  0.0100  -0.0263 172 SER D CB  
7678 O OG  A SER D 172 ? 0.2507 0.1880 0.3438 0.0082  0.0083  -0.0287 172 SER D OG  
7679 O OG  B SER D 172 ? 0.2477 0.1829 0.3422 0.0059  0.0132  -0.0205 172 SER D OG  
7680 N N   . ALA D 173 ? 0.2200 0.1576 0.3316 -0.0004 0.0090  -0.0235 173 ALA D N   
7681 C CA  . ALA D 173 ? 0.2225 0.1544 0.3425 -0.0027 0.0085  -0.0231 173 ALA D CA  
7682 C C   . ALA D 173 ? 0.2045 0.1305 0.3262 -0.0035 0.0138  -0.0168 173 ALA D C   
7683 O O   . ALA D 173 ? 0.2252 0.1539 0.3449 -0.0034 0.0176  -0.0131 173 ALA D O   
7684 C CB  . ALA D 173 ? 0.2424 0.1794 0.3715 -0.0061 0.0054  -0.0253 173 ALA D CB  
7685 N N   . ASP D 174 ? 0.2151 0.1322 0.3402 -0.0045 0.0146  -0.0157 174 ASP D N   
7686 C CA  . ASP D 174 ? 0.2470 0.1580 0.3741 -0.0063 0.0206  -0.0097 174 ASP D CA  
7687 C C   . ASP D 174 ? 0.2712 0.1891 0.4089 -0.0100 0.0231  -0.0082 174 ASP D C   
7688 O O   . ASP D 174 ? 0.2510 0.1750 0.3980 -0.0121 0.0192  -0.0118 174 ASP D O   
7689 C CB  . ASP D 174 ? 0.2414 0.1414 0.3723 -0.0080 0.0211  -0.0087 174 ASP D CB  
7690 C CG  . ASP D 174 ? 0.3065 0.1981 0.4287 -0.0041 0.0180  -0.0101 174 ASP D CG  
7691 O OD1 . ASP D 174 ? 0.3079 0.2003 0.4201 -0.0001 0.0172  -0.0101 174 ASP D OD1 
7692 O OD2 . ASP D 174 ? 0.4003 0.2836 0.5265 -0.0052 0.0167  -0.0109 174 ASP D OD2 
7693 N N   . PHE D 175 ? 0.2151 0.1317 0.3518 -0.0106 0.0295  -0.0032 175 PHE D N   
7694 C CA  . PHE D 175 ? 0.2205 0.1447 0.3683 -0.0133 0.0322  -0.0021 175 PHE D CA  
7695 C C   . PHE D 175 ? 0.2231 0.1411 0.3710 -0.0151 0.0410  0.0034  175 PHE D C   
7696 O O   . PHE D 175 ? 0.2512 0.1695 0.3916 -0.0134 0.0453  0.0062  175 PHE D O   
7697 C CB  . PHE D 175 ? 0.2280 0.1613 0.3725 -0.0111 0.0303  -0.0033 175 PHE D CB  
7698 C CG  . PHE D 175 ? 0.2420 0.1839 0.3997 -0.0133 0.0303  -0.0035 175 PHE D CG  
7699 C CD1 . PHE D 175 ? 0.2696 0.2168 0.4372 -0.0150 0.0240  -0.0074 175 PHE D CD1 
7700 C CD2 . PHE D 175 ? 0.2128 0.1570 0.3731 -0.0134 0.0363  -0.0002 175 PHE D CD2 
7701 C CE1 . PHE D 175 ? 0.2808 0.2360 0.4615 -0.0165 0.0228  -0.0078 175 PHE D CE1 
7702 C CE2 . PHE D 175 ? 0.2299 0.1825 0.4043 -0.0148 0.0358  -0.0008 175 PHE D CE2 
7703 C CZ  . PHE D 175 ? 0.2533 0.2113 0.4379 -0.0162 0.0288  -0.0044 175 PHE D CZ  
7704 N N   . THR D 176 ? 0.2181 0.1308 0.3751 -0.0189 0.0438  0.0045  176 THR D N   
7705 C CA  . THR D 176 ? 0.2446 0.1483 0.3992 -0.0210 0.0526  0.0098  176 THR D CA  
7706 C C   . THR D 176 ? 0.2864 0.1957 0.4583 -0.0257 0.0584  0.0106  176 THR D C   
7707 O O   . THR D 176 ? 0.2820 0.2007 0.4695 -0.0276 0.0543  0.0068  176 THR D O   
7708 C CB  . THR D 176 ? 0.2796 0.1702 0.4293 -0.0219 0.0525  0.0113  176 THR D CB  
7709 O OG1 . THR D 176 ? 0.2763 0.1689 0.4400 -0.0249 0.0481  0.0073  176 THR D OG1 
7710 C CG2 . THR D 176 ? 0.3020 0.1871 0.4354 -0.0165 0.0470  0.0105  176 THR D CG2 
7711 N N   . ASN D 177 ? 0.2903 0.1942 0.4590 -0.0273 0.0679  0.0152  177 ASN D N   
7712 C CA  . ASN D 177 ? 0.3146 0.2228 0.5003 -0.0321 0.0754  0.0160  177 ASN D CA  
7713 C C   . ASN D 177 ? 0.3124 0.2358 0.5119 -0.0314 0.0733  0.0128  177 ASN D C   
7714 O O   . ASN D 177 ? 0.3322 0.2627 0.5518 -0.0351 0.0753  0.0111  177 ASN D O   
7715 C CB  . ASN D 177 ? 0.3495 0.2542 0.5492 -0.0372 0.0751  0.0149  177 ASN D CB  
7716 C CG  . ASN D 177 ? 0.3791 0.2672 0.5651 -0.0377 0.0766  0.0183  177 ASN D CG  
7717 O OD1 . ASN D 177 ? 0.4026 0.2863 0.5892 -0.0377 0.0699  0.0159  177 ASN D OD1 
7718 N ND2 . ASN D 177 ? 0.3604 0.2385 0.5335 -0.0380 0.0854  0.0239  177 ASN D ND2 
7719 N N   . PHE D 178 ? 0.2840 0.2124 0.4741 -0.0268 0.0692  0.0119  178 PHE D N   
7720 C CA  . PHE D 178 ? 0.2402 0.1812 0.4416 -0.0256 0.0671  0.0095  178 PHE D CA  
7721 C C   . PHE D 178 ? 0.2812 0.2231 0.4828 -0.0255 0.0768  0.0122  178 PHE D C   
7722 O O   . PHE D 178 ? 0.3012 0.2360 0.4856 -0.0234 0.0813  0.0150  178 PHE D O   
7723 C CB  . PHE D 178 ? 0.2613 0.2067 0.4527 -0.0211 0.0583  0.0072  178 PHE D CB  
7724 C CG  . PHE D 178 ? 0.2413 0.1979 0.4436 -0.0198 0.0554  0.0052  178 PHE D CG  
7725 C CD1 . PHE D 178 ? 0.2773 0.2418 0.4973 -0.0217 0.0498  0.0020  178 PHE D CD1 
7726 C CD2 . PHE D 178 ? 0.1991 0.1576 0.3948 -0.0170 0.0584  0.0065  178 PHE D CD2 
7727 C CE1 . PHE D 178 ? 0.2587 0.2329 0.4889 -0.0200 0.0464  0.0005  178 PHE D CE1 
7728 C CE2 . PHE D 178 ? 0.2282 0.1958 0.4338 -0.0155 0.0556  0.0051  178 PHE D CE2 
7729 C CZ  . PHE D 178 ? 0.2244 0.1997 0.4472 -0.0168 0.0495  0.0023  178 PHE D CZ  
7730 N N   . ASP D 179 ? 0.2797 0.2307 0.5012 -0.0275 0.0796  0.0107  179 ASP D N   
7731 C CA  . ASP D 179 ? 0.2557 0.2091 0.4812 -0.0277 0.0893  0.0122  179 ASP D CA  
7732 C C   . ASP D 179 ? 0.2570 0.2187 0.4831 -0.0233 0.0853  0.0105  179 ASP D C   
7733 O O   . ASP D 179 ? 0.2483 0.2204 0.4918 -0.0230 0.0800  0.0075  179 ASP D O   
7734 C CB  . ASP D 179 ? 0.2462 0.2052 0.4962 -0.0326 0.0951  0.0110  179 ASP D CB  
7735 C CG  . ASP D 179 ? 0.3030 0.2653 0.5600 -0.0330 0.1062  0.0118  179 ASP D CG  
7736 O OD1 . ASP D 179 ? 0.2734 0.2321 0.5143 -0.0296 0.1096  0.0135  179 ASP D OD1 
7737 O OD2 . ASP D 179 ? 0.3542 0.3230 0.6336 -0.0369 0.1115  0.0102  179 ASP D OD2 
7738 N N   . PRO D 180 ? 0.2404 0.1980 0.4485 -0.0198 0.0872  0.0121  180 PRO D N   
7739 C CA  . PRO D 180 ? 0.2460 0.2108 0.4554 -0.0159 0.0831  0.0104  180 PRO D CA  
7740 C C   . PRO D 180 ? 0.2493 0.2216 0.4764 -0.0162 0.0893  0.0094  180 PRO D C   
7741 O O   . PRO D 180 ? 0.2276 0.2066 0.4602 -0.0131 0.0850  0.0078  180 PRO D O   
7742 C CB  . PRO D 180 ? 0.2356 0.1930 0.4216 -0.0129 0.0845  0.0122  180 PRO D CB  
7743 C CG  . PRO D 180 ? 0.2720 0.2191 0.4480 -0.0153 0.0936  0.0153  180 PRO D CG  
7744 C CD  . PRO D 180 ? 0.2533 0.1990 0.4395 -0.0192 0.0923  0.0153  180 PRO D CD  
7745 N N   . ARG D 181 ? 0.2526 0.2239 0.4895 -0.0198 0.0995  0.0102  181 ARG D N   
7746 C CA  . ARG D 181 ? 0.2518 0.2317 0.5086 -0.0199 0.1053  0.0084  181 ARG D CA  
7747 C C   . ARG D 181 ? 0.2149 0.2067 0.4947 -0.0195 0.0961  0.0050  181 ARG D C   
7748 O O   . ARG D 181 ? 0.2297 0.2300 0.5259 -0.0176 0.0971  0.0028  181 ARG D O   
7749 C CB  . ARG D 181 ? 0.2748 0.2517 0.5387 -0.0246 0.1185  0.0095  181 ARG D CB  
7750 C CG  . ARG D 181 ? 0.3002 0.2650 0.5409 -0.0249 0.1282  0.0130  181 ARG D CG  
7751 C CD  . ARG D 181 ? 0.3186 0.2787 0.5648 -0.0305 0.1407  0.0147  181 ARG D CD  
7752 N NE  . ARG D 181 ? 0.3597 0.3180 0.6128 -0.0344 0.1366  0.0152  181 ARG D NE  
7753 C CZ  . ARG D 181 ? 0.4054 0.3611 0.6661 -0.0392 0.1442  0.0158  181 ARG D CZ  
7754 N NH1 . ARG D 181 ? 0.4605 0.4152 0.7202 -0.0397 0.1555  0.0156  181 ARG D NH1 
7755 N NH2 . ARG D 181 ? 0.4039 0.3576 0.6698 -0.0422 0.1393  0.0158  181 ARG D NH2 
7756 N N   . GLY D 182 ? 0.2470 0.2392 0.5291 -0.0211 0.0873  0.0041  182 GLY D N   
7757 C CA  . GLY D 182 ? 0.2261 0.2287 0.5281 -0.0206 0.0773  0.0007  182 GLY D CA  
7758 C C   . GLY D 182 ? 0.2470 0.2531 0.5435 -0.0154 0.0674  -0.0001 182 GLY D C   
7759 O O   . GLY D 182 ? 0.2366 0.2509 0.5484 -0.0143 0.0584  -0.0027 182 GLY D O   
7760 N N   . LEU D 183 ? 0.2308 0.2304 0.5056 -0.0124 0.0685  0.0020  183 LEU D N   
7761 C CA  . LEU D 183 ? 0.1952 0.1965 0.4627 -0.0079 0.0607  0.0018  183 LEU D CA  
7762 C C   . LEU D 183 ? 0.2149 0.2181 0.4861 -0.0050 0.0668  0.0021  183 LEU D C   
7763 O O   . LEU D 183 ? 0.2177 0.2206 0.4816 -0.0012 0.0619  0.0023  183 LEU D O   
7764 C CB  . LEU D 183 ? 0.1984 0.1916 0.4405 -0.0068 0.0570  0.0034  183 LEU D CB  
7765 C CG  . LEU D 183 ? 0.2116 0.2028 0.4495 -0.0091 0.0504  0.0025  183 LEU D CG  
7766 C CD1 . LEU D 183 ? 0.2175 0.2014 0.4317 -0.0076 0.0481  0.0035  183 LEU D CD1 
7767 C CD2 . LEU D 183 ? 0.2414 0.2396 0.4919 -0.0087 0.0395  -0.0001 183 LEU D CD2 
7768 N N   . LEU D 184 ? 0.2187 0.2237 0.5017 -0.0067 0.0778  0.0018  184 LEU D N   
7769 C CA  . LEU D 184 ? 0.2180 0.2247 0.5054 -0.0039 0.0848  0.0013  184 LEU D CA  
7770 C C   . LEU D 184 ? 0.1992 0.2171 0.5149 -0.0026 0.0828  -0.0017 184 LEU D C   
7771 O O   . LEU D 184 ? 0.2091 0.2332 0.5441 -0.0056 0.0827  -0.0034 184 LEU D O   
7772 C CB  . LEU D 184 ? 0.2339 0.2351 0.5152 -0.0063 0.0993  0.0023  184 LEU D CB  
7773 C CG  . LEU D 184 ? 0.2983 0.2879 0.5520 -0.0074 0.1017  0.0053  184 LEU D CG  
7774 C CD1 . LEU D 184 ? 0.3117 0.2957 0.5608 -0.0101 0.1160  0.0064  184 LEU D CD1 
7775 C CD2 . LEU D 184 ? 0.2648 0.2506 0.5008 -0.0033 0.0968  0.0058  184 LEU D CD2 
7776 N N   . PRO D 185 ? 0.2059 0.2265 0.5264 0.0019  0.0817  -0.0026 185 PRO D N   
7777 C CA  . PRO D 185 ? 0.2118 0.2431 0.5610 0.0037  0.0811  -0.0057 185 PRO D CA  
7778 C C   . PRO D 185 ? 0.2074 0.2415 0.5699 0.0015  0.0963  -0.0074 185 PRO D C   
7779 O O   . PRO D 185 ? 0.2427 0.2691 0.5894 -0.0010 0.1071  -0.0058 185 PRO D O   
7780 C CB  . PRO D 185 ? 0.1942 0.2247 0.5396 0.0096  0.0753  -0.0056 185 PRO D CB  
7781 C CG  . PRO D 185 ? 0.2082 0.2279 0.5260 0.0099  0.0814  -0.0032 185 PRO D CG  
7782 C CD  . PRO D 185 ? 0.2082 0.2219 0.5084 0.0055  0.0813  -0.0010 185 PRO D CD  
7783 N N   . GLU D 186 ? 0.1978 0.2429 0.5898 0.0025  0.0969  -0.0110 186 GLU D N   
7784 C CA  . GLU D 186 ? 0.2570 0.3006 0.6536 -0.0002 0.1094  -0.0130 186 GLU D CA  
7785 C C   . GLU D 186 ? 0.2894 0.3272 0.6734 0.0026  0.1184  -0.0130 186 GLU D C   
7786 O O   . GLU D 186 ? 0.3034 0.3349 0.6770 -0.0003 0.1310  -0.0128 186 GLU D O   
7787 C CB  . GLU D 186 ? 0.3420 0.3948 0.7650 0.0000  0.1049  -0.0171 186 GLU D CB  
7788 C CG  . GLU D 186 ? 0.4974 0.5502 0.9290 -0.0026 0.1172  -0.0201 186 GLU D CG  
7789 C CD  . GLU D 186 ? 0.6095 0.6721 1.0688 -0.0033 0.1122  -0.0244 186 GLU D CD  
7790 O OE1 . GLU D 186 ? 0.6541 0.7174 1.1222 -0.0065 0.1223  -0.0270 186 GLU D OE1 
7791 O OE2 . GLU D 186 ? 0.6405 0.7099 1.1123 -0.0007 0.0982  -0.0255 186 GLU D OE2 
7792 N N   . SER D 187 ? 0.2277 0.2664 0.6113 0.0083  0.1119  -0.0133 187 SER D N   
7793 C CA  . SER D 187 ? 0.2218 0.2546 0.5937 0.0110  0.1194  -0.0138 187 SER D CA  
7794 C C   . SER D 187 ? 0.2328 0.2571 0.5795 0.0119  0.1210  -0.0106 187 SER D C   
7795 O O   . SER D 187 ? 0.2181 0.2401 0.5544 0.0130  0.1100  -0.0082 187 SER D O   
7796 C CB  . SER D 187 ? 0.2251 0.2619 0.6087 0.0167  0.1116  -0.0158 187 SER D CB  
7797 O OG  . SER D 187 ? 0.2799 0.3101 0.6507 0.0190  0.1189  -0.0165 187 SER D OG  
7798 N N   . LEU D 188 ? 0.2538 0.2702 0.5838 0.0110  0.1324  -0.0107 188 LEU D N   
7799 C CA  . LEU D 188 ? 0.2482 0.2548 0.5510 0.0118  0.1327  -0.0082 188 LEU D CA  
7800 C C   . LEU D 188 ? 0.2467 0.2498 0.5437 0.0166  0.1335  -0.0099 188 LEU D C   
7801 O O   . LEU D 188 ? 0.2922 0.2860 0.5652 0.0168  0.1355  -0.0089 188 LEU D O   
7802 C CB  . LEU D 188 ? 0.3059 0.3046 0.5905 0.0073  0.1438  -0.0066 188 LEU D CB  
7803 C CG  . LEU D 188 ? 0.3254 0.3244 0.6115 0.0022  0.1436  -0.0043 188 LEU D CG  
7804 C CD1 . LEU D 188 ? 0.3591 0.3476 0.6232 -0.0014 0.1543  -0.0021 188 LEU D CD1 
7805 C CD2 . LEU D 188 ? 0.2958 0.2943 0.5749 0.0025  0.1290  -0.0019 188 LEU D CD2 
7806 N N   . ASP D 189 ? 0.2125 0.2215 0.5281 0.0201  0.1293  -0.0124 189 ASP D N   
7807 C CA  . ASP D 189 ? 0.2177 0.2228 0.5281 0.0248  0.1267  -0.0135 189 ASP D CA  
7808 C C   . ASP D 189 ? 0.2054 0.2040 0.4971 0.0264  0.1175  -0.0104 189 ASP D C   
7809 O O   . ASP D 189 ? 0.2095 0.2097 0.4997 0.0252  0.1072  -0.0078 189 ASP D O   
7810 C CB  . ASP D 189 ? 0.2142 0.2265 0.5472 0.0281  0.1194  -0.0155 189 ASP D CB  
7811 C CG  . ASP D 189 ? 0.2807 0.2973 0.6282 0.0265  0.1279  -0.0194 189 ASP D CG  
7812 O OD1 . ASP D 189 ? 0.3259 0.3390 0.6647 0.0228  0.1397  -0.0203 189 ASP D OD1 
7813 O OD2 . ASP D 189 ? 0.3061 0.3292 0.6736 0.0291  0.1225  -0.0215 189 ASP D OD2 
7814 N N   . TYR D 190 ? 0.1857 0.2304 0.4286 0.0201  0.0965  0.0130  190 TYR D N   
7815 C CA  . TYR D 190 ? 0.1734 0.2066 0.3916 0.0202  0.0868  0.0134  190 TYR D CA  
7816 C C   . TYR D 190 ? 0.1953 0.2213 0.4011 0.0259  0.0872  0.0110  190 TYR D C   
7817 O O   . TYR D 190 ? 0.2124 0.2396 0.4232 0.0297  0.0968  0.0086  190 TYR D O   
7818 C CB  . TYR D 190 ? 0.1782 0.2022 0.3734 0.0152  0.0901  0.0154  190 TYR D CB  
7819 C CG  . TYR D 190 ? 0.1984 0.2165 0.3791 0.0158  0.1037  0.0147  190 TYR D CG  
7820 C CD1 . TYR D 190 ? 0.2392 0.2475 0.3983 0.0192  0.1042  0.0125  190 TYR D CD1 
7821 C CD2 . TYR D 190 ? 0.2105 0.2322 0.3980 0.0128  0.1159  0.0162  190 TYR D CD2 
7822 C CE1 . TYR D 190 ? 0.2547 0.2569 0.3987 0.0200  0.1160  0.0112  190 TYR D CE1 
7823 C CE2 . TYR D 190 ? 0.2329 0.2481 0.4044 0.0138  0.1289  0.0155  190 TYR D CE2 
7824 C CZ  . TYR D 190 ? 0.2314 0.2367 0.3804 0.0175  0.1283  0.0128  190 TYR D CZ  
7825 O OH  . TYR D 190 ? 0.2903 0.2891 0.4228 0.0188  0.1404  0.0115  190 TYR D OH  
7826 N N   . TRP D 191 ? 0.1989 0.2171 0.3887 0.0263  0.0770  0.0114  191 TRP D N   
7827 C CA  . TRP D 191 ? 0.1980 0.2063 0.3703 0.0297  0.0765  0.0095  191 TRP D CA  
7828 C C   . TRP D 191 ? 0.2186 0.2175 0.3652 0.0262  0.0775  0.0099  191 TRP D C   
7829 O O   . TRP D 191 ? 0.2093 0.2083 0.3508 0.0220  0.0733  0.0121  191 TRP D O   
7830 C CB  . TRP D 191 ? 0.2171 0.2236 0.3914 0.0326  0.0646  0.0101  191 TRP D CB  
7831 C CG  . TRP D 191 ? 0.2088 0.2239 0.4076 0.0371  0.0615  0.0098  191 TRP D CG  
7832 C CD1 . TRP D 191 ? 0.2359 0.2520 0.4454 0.0428  0.0666  0.0076  191 TRP D CD1 
7833 C CD2 . TRP D 191 ? 0.2099 0.2332 0.4252 0.0368  0.0513  0.0117  191 TRP D CD2 
7834 N NE1 . TRP D 191 ? 0.2504 0.2756 0.4832 0.0465  0.0602  0.0082  191 TRP D NE1 
7835 C CE2 . TRP D 191 ? 0.2152 0.2450 0.4518 0.0428  0.0504  0.0107  191 TRP D CE2 
7836 C CE3 . TRP D 191 ? 0.2372 0.2626 0.4512 0.0325  0.0426  0.0137  191 TRP D CE3 
7837 C CZ2 . TRP D 191 ? 0.2189 0.2581 0.4760 0.0444  0.0402  0.0118  191 TRP D CZ2 
7838 C CZ3 . TRP D 191 ? 0.2302 0.2642 0.4634 0.0338  0.0328  0.0144  191 TRP D CZ3 
7839 C CH2 . TRP D 191 ? 0.2246 0.2654 0.4787 0.0396  0.0313  0.0136  191 TRP D CH2 
7840 N N   . THR D 192 ? 0.2117 0.2022 0.3421 0.0280  0.0824  0.0074  192 THR D N   
7841 C CA  . THR D 192 ? 0.2188 0.2012 0.3255 0.0251  0.0823  0.0074  192 THR D CA  
7842 C C   . THR D 192 ? 0.2242 0.1979 0.3166 0.0270  0.0795  0.0048  192 THR D C   
7843 O O   . THR D 192 ? 0.2591 0.2305 0.3558 0.0308  0.0823  0.0021  192 THR D O   
7844 C CB  . THR D 192 ? 0.2149 0.1955 0.3132 0.0235  0.0935  0.0072  192 THR D CB  
7845 O OG1 . THR D 192 ? 0.2325 0.2054 0.3078 0.0210  0.0917  0.0075  192 THR D OG1 
7846 C CG2 . THR D 192 ? 0.2458 0.2247 0.3450 0.0273  0.1035  0.0036  192 THR D CG2 
7847 N N   . TYR D 193 ? 0.2178 0.1867 0.2939 0.0243  0.0738  0.0053  193 TYR D N   
7848 C CA  . TYR D 193 ? 0.2309 0.1919 0.2935 0.0249  0.0710  0.0028  193 TYR D CA  
7849 C C   . TYR D 193 ? 0.2420 0.1998 0.2870 0.0214  0.0676  0.0032  193 TYR D C   
7850 O O   . TYR D 193 ? 0.2317 0.1931 0.2767 0.0192  0.0650  0.0059  193 TYR D O   
7851 C CB  . TYR D 193 ? 0.2191 0.1794 0.2891 0.0265  0.0633  0.0037  193 TYR D CB  
7852 C CG  . TYR D 193 ? 0.2039 0.1669 0.2727 0.0238  0.0543  0.0070  193 TYR D CG  
7853 C CD1 . TYR D 193 ? 0.2176 0.1879 0.2994 0.0236  0.0511  0.0097  193 TYR D CD1 
7854 C CD2 . TYR D 193 ? 0.2086 0.1670 0.2635 0.0215  0.0493  0.0070  193 TYR D CD2 
7855 C CE1 . TYR D 193 ? 0.1991 0.1711 0.2784 0.0215  0.0430  0.0120  193 TYR D CE1 
7856 C CE2 . TYR D 193 ? 0.2063 0.1674 0.2596 0.0195  0.0420  0.0096  193 TYR D CE2 
7857 C CZ  . TYR D 193 ? 0.2035 0.1708 0.2681 0.0198  0.0391  0.0120  193 TYR D CZ  
7858 O OH  . TYR D 193 ? 0.2124 0.1812 0.2732 0.0180  0.0322  0.0138  193 TYR D OH  
7859 N N   . PRO D 194 ? 0.2163 0.1675 0.2470 0.0211  0.0674  0.0001  194 PRO D N   
7860 C CA  . PRO D 194 ? 0.2300 0.1793 0.2458 0.0183  0.0633  0.0001  194 PRO D CA  
7861 C C   . PRO D 194 ? 0.2278 0.1787 0.2452 0.0167  0.0548  0.0018  194 PRO D C   
7862 O O   . PRO D 194 ? 0.2254 0.1736 0.2457 0.0172  0.0524  0.0010  194 PRO D O   
7863 C CB  . PRO D 194 ? 0.2513 0.1933 0.2538 0.0187  0.0660  -0.0046 194 PRO D CB  
7864 C CG  . PRO D 194 ? 0.2828 0.2217 0.2944 0.0214  0.0688  -0.0068 194 PRO D CG  
7865 C CD  . PRO D 194 ? 0.2417 0.1867 0.2702 0.0236  0.0716  -0.0040 194 PRO D CD  
7866 N N   . GLY D 195 ? 0.2061 0.1605 0.2208 0.0149  0.0506  0.0041  195 GLY D N   
7867 C CA  . GLY D 195 ? 0.2004 0.1567 0.2156 0.0135  0.0434  0.0056  195 GLY D CA  
7868 C C   . GLY D 195 ? 0.1999 0.1581 0.2062 0.0118  0.0400  0.0060  195 GLY D C   
7869 O O   . GLY D 195 ? 0.2163 0.1727 0.2124 0.0114  0.0416  0.0042  195 GLY D O   
7870 N N   . SER D 196 ? 0.1975 0.1591 0.2071 0.0112  0.0349  0.0082  196 SER D N   
7871 C CA  . SER D 196 ? 0.2083 0.1719 0.2102 0.0100  0.0310  0.0081  196 SER D CA  
7872 C C   . SER D 196 ? 0.2069 0.1733 0.2127 0.0103  0.0280  0.0103  196 SER D C   
7873 O O   . SER D 196 ? 0.1995 0.1669 0.2147 0.0108  0.0277  0.0120  196 SER D O   
7874 C CB  . SER D 196 ? 0.2135 0.1776 0.2129 0.0086  0.0276  0.0075  196 SER D CB  
7875 O OG  . SER D 196 ? 0.2071 0.1723 0.2124 0.0089  0.0243  0.0099  196 SER D OG  
7876 N N   . LEU D 197 ? 0.2008 0.1685 0.1997 0.0101  0.0252  0.0100  197 LEU D N   
7877 C CA  . LEU D 197 ? 0.1911 0.1607 0.1926 0.0104  0.0211  0.0113  197 LEU D CA  
7878 C C   . LEU D 197 ? 0.1995 0.1706 0.2050 0.0102  0.0178  0.0120  197 LEU D C   
7879 O O   . LEU D 197 ? 0.1901 0.1610 0.1928 0.0094  0.0178  0.0114  197 LEU D O   
7880 C CB  . LEU D 197 ? 0.1999 0.1709 0.1935 0.0109  0.0186  0.0102  197 LEU D CB  
7881 C CG  . LEU D 197 ? 0.1954 0.1640 0.1826 0.0118  0.0206  0.0099  197 LEU D CG  
7882 C CD1 . LEU D 197 ? 0.2126 0.1837 0.1937 0.0132  0.0168  0.0085  197 LEU D CD1 
7883 C CD2 . LEU D 197 ? 0.2089 0.1741 0.1998 0.0119  0.0224  0.0121  197 LEU D CD2 
7884 N N   . THR D 198 ? 0.1913 0.1630 0.2024 0.0106  0.0145  0.0132  198 THR D N   
7885 C CA  . THR D 198 ? 0.1892 0.1612 0.2014 0.0108  0.0106  0.0142  198 THR D CA  
7886 C C   . THR D 198 ? 0.1761 0.1493 0.1807 0.0109  0.0070  0.0135  198 THR D C   
7887 O O   . THR D 198 ? 0.1896 0.1623 0.1925 0.0112  0.0037  0.0145  198 THR D O   
7888 C CB  . THR D 198 ? 0.1900 0.1624 0.2124 0.0115  0.0078  0.0155  198 THR D CB  
7889 O OG1 . THR D 198 ? 0.1845 0.1577 0.2086 0.0113  0.0050  0.0150  198 THR D OG1 
7890 C CG2 . THR D 198 ? 0.1861 0.1586 0.2183 0.0119  0.0121  0.0159  198 THR D CG2 
7891 N N   . THR D 199 ? 0.1875 0.1618 0.1866 0.0111  0.0078  0.0119  199 THR D N   
7892 C CA  . THR D 199 ? 0.1792 0.1554 0.1715 0.0117  0.0057  0.0107  199 THR D CA  
7893 C C   . THR D 199 ? 0.1721 0.1510 0.1601 0.0113  0.0084  0.0092  199 THR D C   
7894 O O   . THR D 199 ? 0.2003 0.1785 0.1891 0.0110  0.0109  0.0088  199 THR D O   
7895 C CB  . THR D 199 ? 0.1885 0.1638 0.1796 0.0132  0.0029  0.0095  199 THR D CB  
7896 O OG1 . THR D 199 ? 0.2015 0.1758 0.1925 0.0137  0.0050  0.0090  199 THR D OG1 
7897 C CG2 . THR D 199 ? 0.2100 0.1830 0.2072 0.0131  -0.0005 0.0103  199 THR D CG2 
7898 N N   . PRO D 200 ? 0.1992 0.1816 0.1826 0.0114  0.0080  0.0081  200 PRO D N   
7899 C CA  . PRO D 200 ? 0.1773 0.1640 0.1586 0.0114  0.0095  0.0060  200 PRO D CA  
7900 C C   . PRO D 200 ? 0.1815 0.1669 0.1622 0.0135  0.0089  0.0051  200 PRO D C   
7901 O O   . PRO D 200 ? 0.1912 0.1738 0.1719 0.0152  0.0070  0.0054  200 PRO D O   
7902 C CB  . PRO D 200 ? 0.1811 0.1724 0.1591 0.0121  0.0090  0.0047  200 PRO D CB  
7903 C CG  . PRO D 200 ? 0.1955 0.1839 0.1723 0.0108  0.0086  0.0071  200 PRO D CG  
7904 C CD  . PRO D 200 ? 0.1937 0.1766 0.1737 0.0117  0.0061  0.0084  200 PRO D CD  
7905 N N   . PRO D 201 ? 0.1904 0.1771 0.1699 0.0133  0.0101  0.0040  201 PRO D N   
7906 C CA  . PRO D 201 ? 0.1922 0.1825 0.1719 0.0110  0.0115  0.0027  201 PRO D CA  
7907 C C   . PRO D 201 ? 0.1855 0.1717 0.1670 0.0085  0.0139  0.0036  201 PRO D C   
7908 O O   . PRO D 201 ? 0.1942 0.1816 0.1755 0.0064  0.0149  0.0020  201 PRO D O   
7909 C CB  . PRO D 201 ? 0.1876 0.1805 0.1646 0.0127  0.0103  0.0005  201 PRO D CB  
7910 C CG  . PRO D 201 ? 0.1904 0.1769 0.1644 0.0150  0.0101  0.0021  201 PRO D CG  
7911 C CD  . PRO D 201 ? 0.2149 0.1994 0.1914 0.0157  0.0093  0.0037  201 PRO D CD  
7912 N N   . LEU D 202 ? 0.1797 0.1609 0.1637 0.0088  0.0147  0.0057  202 LEU D N   
7913 C CA  . LEU D 202 ? 0.1742 0.1516 0.1613 0.0072  0.0170  0.0066  202 LEU D CA  
7914 C C   . LEU D 202 ? 0.1946 0.1697 0.1793 0.0068  0.0195  0.0047  202 LEU D C   
7915 O O   . LEU D 202 ? 0.1955 0.1677 0.1814 0.0053  0.0214  0.0040  202 LEU D O   
7916 C CB  . LEU D 202 ? 0.1969 0.1747 0.1849 0.0051  0.0169  0.0073  202 LEU D CB  
7917 C CG  . LEU D 202 ? 0.1970 0.1757 0.1849 0.0058  0.0145  0.0094  202 LEU D CG  
7918 C CD1 . LEU D 202 ? 0.1941 0.1729 0.1801 0.0035  0.0151  0.0105  202 LEU D CD1 
7919 C CD2 . LEU D 202 ? 0.1880 0.1629 0.1802 0.0074  0.0131  0.0115  202 LEU D CD2 
7920 N N   . LEU D 203 ? 0.1938 0.1692 0.1741 0.0083  0.0193  0.0038  203 LEU D N   
7921 C CA  . LEU D 203 ? 0.1895 0.1621 0.1647 0.0083  0.0212  0.0017  203 LEU D CA  
7922 C C   . LEU D 203 ? 0.1927 0.1599 0.1698 0.0085  0.0256  0.0024  203 LEU D C   
7923 O O   . LEU D 203 ? 0.1957 0.1617 0.1776 0.0094  0.0270  0.0049  203 LEU D O   
7924 C CB  . LEU D 203 ? 0.1913 0.1640 0.1596 0.0105  0.0198  0.0014  203 LEU D CB  
7925 C CG  . LEU D 203 ? 0.2166 0.1958 0.1843 0.0110  0.0154  -0.0001 203 LEU D CG  
7926 C CD1 . LEU D 203 ? 0.2461 0.2240 0.2073 0.0144  0.0134  0.0004  203 LEU D CD1 
7927 C CD2 . LEU D 203 ? 0.2370 0.2197 0.2043 0.0087  0.0143  -0.0037 203 LEU D CD2 
7928 N N   . GLU D 204 ? 0.2074 0.1714 0.1810 0.0077  0.0277  -0.0002 204 GLU D N   
7929 C CA  . GLU D 204 ? 0.2185 0.1774 0.1945 0.0082  0.0325  -0.0003 204 GLU D CA  
7930 C C   . GLU D 204 ? 0.2301 0.1857 0.1991 0.0100  0.0362  -0.0005 204 GLU D C   
7931 O O   . GLU D 204 ? 0.2533 0.2046 0.2153 0.0103  0.0391  -0.0033 204 GLU D O   
7932 C CB  . GLU D 204 ? 0.2234 0.1793 0.1992 0.0065  0.0329  -0.0034 204 GLU D CB  
7933 C CG  . GLU D 204 ? 0.2053 0.1633 0.1878 0.0047  0.0301  -0.0017 204 GLU D CG  
7934 C CD  . GLU D 204 ? 0.2132 0.1669 0.1961 0.0024  0.0306  -0.0040 204 GLU D CD  
7935 O OE1 . GLU D 204 ? 0.2503 0.2013 0.2274 0.0013  0.0311  -0.0081 204 GLU D OE1 
7936 O OE2 . GLU D 204 ? 0.2240 0.1763 0.2123 0.0015  0.0299  -0.0017 204 GLU D OE2 
7937 N N   . SER D 205 ? 0.2268 0.1838 0.1975 0.0110  0.0363  0.0027  205 SER D N   
7938 C CA  A SER D 205 ? 0.2334 0.1868 0.1963 0.0123  0.0397  0.0038  205 SER D CA  
7939 C CA  B SER D 205 ? 0.2327 0.1861 0.1957 0.0123  0.0396  0.0038  205 SER D CA  
7940 C C   . SER D 205 ? 0.2309 0.1834 0.2018 0.0125  0.0447  0.0069  205 SER D C   
7941 O O   . SER D 205 ? 0.2550 0.2044 0.2207 0.0130  0.0480  0.0090  205 SER D O   
7942 C CB  A SER D 205 ? 0.2461 0.2005 0.2021 0.0132  0.0351  0.0048  205 SER D CB  
7943 C CB  B SER D 205 ? 0.2429 0.1975 0.1994 0.0131  0.0349  0.0049  205 SER D CB  
7944 O OG  A SER D 205 ? 0.2481 0.2063 0.2123 0.0128  0.0317  0.0067  205 SER D OG  
7945 O OG  B SER D 205 ? 0.2419 0.1999 0.1953 0.0127  0.0299  0.0019  205 SER D OG  
7946 N N   . VAL D 206 ? 0.2315 0.1866 0.2152 0.0121  0.0456  0.0074  206 VAL D N   
7947 C CA  . VAL D 206 ? 0.2294 0.1860 0.2242 0.0119  0.0488  0.0102  206 VAL D CA  
7948 C C   . VAL D 206 ? 0.2387 0.1947 0.2401 0.0128  0.0553  0.0091  206 VAL D C   
7949 O O   . VAL D 206 ? 0.2433 0.1995 0.2488 0.0135  0.0546  0.0071  206 VAL D O   
7950 C CB  . VAL D 206 ? 0.2027 0.1638 0.2086 0.0113  0.0431  0.0116  206 VAL D CB  
7951 C CG1 . VAL D 206 ? 0.2148 0.1782 0.2342 0.0108  0.0459  0.0140  206 VAL D CG1 
7952 C CG2 . VAL D 206 ? 0.2131 0.1749 0.2130 0.0109  0.0372  0.0122  206 VAL D CG2 
7953 N N   . THR D 207 ? 0.2212 0.1763 0.2245 0.0129  0.0622  0.0106  207 THR D N   
7954 C CA  . THR D 207 ? 0.2457 0.2027 0.2609 0.0139  0.0690  0.0102  207 THR D CA  
7955 C C   . THR D 207 ? 0.2365 0.1998 0.2698 0.0129  0.0666  0.0127  207 THR D C   
7956 O O   . THR D 207 ? 0.2303 0.1945 0.2659 0.0110  0.0670  0.0154  207 THR D O   
7957 C CB  . THR D 207 ? 0.2443 0.1978 0.2527 0.0142  0.0788  0.0105  207 THR D CB  
7958 O OG1 . THR D 207 ? 0.2690 0.2161 0.2589 0.0154  0.0800  0.0075  207 THR D OG1 
7959 C CG2 . THR D 207 ? 0.2613 0.2184 0.2843 0.0156  0.0866  0.0097  207 THR D CG2 
7960 N N   . TRP D 208 ? 0.2158 0.1828 0.2612 0.0142  0.0631  0.0119  208 TRP D N   
7961 C CA  . TRP D 208 ? 0.2101 0.1834 0.2731 0.0137  0.0592  0.0138  208 TRP D CA  
7962 C C   . TRP D 208 ? 0.2250 0.2031 0.3040 0.0144  0.0666  0.0140  208 TRP D C   
7963 O O   . TRP D 208 ? 0.2213 0.1989 0.3027 0.0170  0.0723  0.0120  208 TRP D O   
7964 C CB  . TRP D 208 ? 0.2132 0.1877 0.2807 0.0153  0.0516  0.0132  208 TRP D CB  
7965 C CG  . TRP D 208 ? 0.1975 0.1700 0.2540 0.0138  0.0440  0.0138  208 TRP D CG  
7966 C CD1 . TRP D 208 ? 0.1975 0.1658 0.2397 0.0136  0.0420  0.0124  208 TRP D CD1 
7967 C CD2 . TRP D 208 ? 0.1835 0.1584 0.2431 0.0122  0.0380  0.0154  208 TRP D CD2 
7968 N NE1 . TRP D 208 ? 0.2065 0.1755 0.2434 0.0123  0.0358  0.0134  208 TRP D NE1 
7969 C CE2 . TRP D 208 ? 0.1902 0.1625 0.2367 0.0117  0.0333  0.0150  208 TRP D CE2 
7970 C CE3 . TRP D 208 ? 0.2034 0.1829 0.2767 0.0112  0.0360  0.0167  208 TRP D CE3 
7971 C CZ2 . TRP D 208 ? 0.1918 0.1651 0.2368 0.0107  0.0270  0.0158  208 TRP D CZ2 
7972 C CZ3 . TRP D 208 ? 0.2027 0.1822 0.2739 0.0097  0.0290  0.0173  208 TRP D CZ3 
7973 C CH2 . TRP D 208 ? 0.2042 0.1803 0.2606 0.0097  0.0250  0.0168  208 TRP D CH2 
7974 N N   . ILE D 209 ? 0.2057 0.1886 0.2969 0.0120  0.0662  0.0163  209 ILE D N   
7975 C CA  . ILE D 209 ? 0.1970 0.1870 0.3080 0.0119  0.0723  0.0167  209 ILE D CA  
7976 C C   . ILE D 209 ? 0.2096 0.2063 0.3376 0.0110  0.0634  0.0176  209 ILE D C   
7977 O O   . ILE D 209 ? 0.2020 0.1987 0.3302 0.0076  0.0591  0.0191  209 ILE D O   
7978 C CB  . ILE D 209 ? 0.2202 0.2089 0.3289 0.0087  0.0815  0.0188  209 ILE D CB  
7979 C CG1 . ILE D 209 ? 0.2578 0.2388 0.3463 0.0102  0.0893  0.0178  209 ILE D CG1 
7980 C CG2 . ILE D 209 ? 0.2092 0.2068 0.3411 0.0080  0.0884  0.0193  209 ILE D CG2 
7981 C CD1 . ILE D 209 ? 0.2713 0.2476 0.3502 0.0072  0.0974  0.0207  209 ILE D CD1 
7982 N N   . VAL D 210 ? 0.1911 0.1927 0.3323 0.0143  0.0596  0.0164  210 VAL D N   
7983 C CA  . VAL D 210 ? 0.1870 0.1944 0.3423 0.0143  0.0492  0.0169  210 VAL D CA  
7984 C C   . VAL D 210 ? 0.1909 0.2089 0.3726 0.0146  0.0525  0.0168  210 VAL D C   
7985 O O   . VAL D 210 ? 0.1834 0.2049 0.3751 0.0184  0.0577  0.0155  210 VAL D O   
7986 C CB  . VAL D 210 ? 0.1938 0.1982 0.3438 0.0181  0.0411  0.0164  210 VAL D CB  
7987 C CG1 . VAL D 210 ? 0.1805 0.1900 0.3427 0.0185  0.0297  0.0171  210 VAL D CG1 
7988 C CG2 . VAL D 210 ? 0.1922 0.1875 0.3180 0.0172  0.0388  0.0164  210 VAL D CG2 
7989 N N   . LEU D 211 ? 0.1913 0.2146 0.3854 0.0105  0.0498  0.0177  211 LEU D N   
7990 C CA  . LEU D 211 ? 0.1783 0.2131 0.3998 0.0099  0.0534  0.0174  211 LEU D CA  
7991 C C   . LEU D 211 ? 0.1819 0.2241 0.4205 0.0142  0.0440  0.0162  211 LEU D C   
7992 O O   . LEU D 211 ? 0.1930 0.2322 0.4250 0.0154  0.0320  0.0163  211 LEU D O   
7993 C CB  . LEU D 211 ? 0.1609 0.1988 0.3919 0.0036  0.0524  0.0186  211 LEU D CB  
7994 C CG  . LEU D 211 ? 0.1986 0.2289 0.4148 -0.0008 0.0619  0.0206  211 LEU D CG  
7995 C CD1 . LEU D 211 ? 0.1982 0.2321 0.4289 -0.0073 0.0611  0.0218  211 LEU D CD1 
7996 C CD2 . LEU D 211 ? 0.2160 0.2470 0.4319 0.0006  0.0769  0.0209  211 LEU D CD2 
7997 N N   . LYS D 212 ? 0.1767 0.2280 0.4363 0.0172  0.0498  0.0152  212 LYS D N   
7998 C CA  . LYS D 212 ? 0.1685 0.2270 0.4457 0.0222  0.0408  0.0142  212 LYS D CA  
7999 C C   . LYS D 212 ? 0.1914 0.2591 0.4878 0.0193  0.0300  0.0141  212 LYS D C   
8000 O O   . LYS D 212 ? 0.2120 0.2809 0.5117 0.0226  0.0171  0.0139  212 LYS D O   
8001 C CB  . LYS D 212 ? 0.2038 0.2702 0.4997 0.0268  0.0504  0.0126  212 LYS D CB  
8002 C CG  . LYS D 212 ? 0.2280 0.3038 0.5469 0.0325  0.0414  0.0117  212 LYS D CG  
8003 C CD  . LYS D 212 ? 0.3266 0.4072 0.6592 0.0387  0.0510  0.0098  212 LYS D CD  
8004 C CE  . LYS D 212 ? 0.3668 0.4578 0.7252 0.0450  0.0414  0.0089  212 LYS D CE  
8005 N NZ  . LYS D 212 ? 0.3952 0.4919 0.7695 0.0513  0.0519  0.0066  212 LYS D NZ  
8006 N N   . GLU D 213 ? 0.1608 0.2345 0.4698 0.0131  0.0348  0.0143  213 GLU D N   
8007 C CA  . GLU D 213 ? 0.1540 0.2372 0.4844 0.0100  0.0245  0.0134  213 GLU D CA  
8008 C C   . GLU D 213 ? 0.1663 0.2402 0.4779 0.0061  0.0142  0.0138  213 GLU D C   
8009 O O   . GLU D 213 ? 0.1735 0.2390 0.4687 0.0016  0.0201  0.0149  213 GLU D O   
8010 C CB  . GLU D 213 ? 0.1620 0.2561 0.5171 0.0042  0.0341  0.0133  213 GLU D CB  
8011 C CG  . GLU D 213 ? 0.1966 0.3016 0.5772 0.0002  0.0231  0.0118  213 GLU D CG  
8012 C CD  . GLU D 213 ? 0.2470 0.3646 0.6565 -0.0059 0.0329  0.0117  213 GLU D CD  
8013 O OE1 . GLU D 213 ? 0.2594 0.3748 0.6650 -0.0088 0.0488  0.0135  213 GLU D OE1 
8014 O OE2 . GLU D 213 ? 0.3061 0.4366 0.7436 -0.0079 0.0244  0.0097  213 GLU D OE2 
8015 N N   . PRO D 214 ? 0.1664 0.2410 0.4792 0.0080  -0.0010 0.0127  214 PRO D N   
8016 C CA  . PRO D 214 ? 0.1759 0.2418 0.4713 0.0043  -0.0101 0.0123  214 PRO D CA  
8017 C C   . PRO D 214 ? 0.1668 0.2379 0.4788 -0.0031 -0.0109 0.0111  214 PRO D C   
8018 O O   . PRO D 214 ? 0.2007 0.2845 0.5416 -0.0052 -0.0082 0.0103  214 PRO D O   
8019 C CB  . PRO D 214 ? 0.1962 0.2619 0.4889 0.0091  -0.0259 0.0114  214 PRO D CB  
8020 C CG  . PRO D 214 ? 0.2879 0.3612 0.5958 0.0159  -0.0247 0.0119  214 PRO D CG  
8021 C CD  . PRO D 214 ? 0.1995 0.2827 0.5294 0.0138  -0.0112 0.0117  214 PRO D CD  
8022 N N   . ILE D 215 ? 0.1814 0.2424 0.4754 -0.0070 -0.0149 0.0108  215 ILE D N   
8023 C CA  . ILE D 215 ? 0.1687 0.2317 0.4754 -0.0137 -0.0204 0.0089  215 ILE D CA  
8024 C C   . ILE D 215 ? 0.1872 0.2507 0.4935 -0.0118 -0.0381 0.0059  215 ILE D C   
8025 O O   . ILE D 215 ? 0.2126 0.2697 0.4991 -0.0064 -0.0449 0.0060  215 ILE D O   
8026 C CB  . ILE D 215 ? 0.1794 0.2304 0.4685 -0.0189 -0.0143 0.0100  215 ILE D CB  
8027 C CG1 . ILE D 215 ? 0.1815 0.2193 0.4384 -0.0155 -0.0194 0.0099  215 ILE D CG1 
8028 C CG2 . ILE D 215 ? 0.2012 0.2522 0.4917 -0.0208 0.0029  0.0132  215 ILE D CG2 
8029 C CD1 . ILE D 215 ? 0.2111 0.2365 0.4501 -0.0197 -0.0148 0.0106  215 ILE D CD1 
8030 N N   . SER D 216 ? 0.1995 0.2705 0.5280 -0.0165 -0.0456 0.0031  216 SER D N   
8031 C CA  . SER D 216 ? 0.2181 0.2908 0.5488 -0.0149 -0.0632 -0.0003 216 SER D CA  
8032 C C   . SER D 216 ? 0.2799 0.3413 0.5951 -0.0197 -0.0695 -0.0029 216 SER D C   
8033 O O   . SER D 216 ? 0.3211 0.3817 0.6464 -0.0269 -0.0647 -0.0036 216 SER D O   
8034 C CB  . SER D 216 ? 0.3256 0.4149 0.6929 -0.0167 -0.0693 -0.0027 216 SER D CB  
8035 O OG  . SER D 216 ? 0.3985 0.4873 0.7677 -0.0183 -0.0862 -0.0069 216 SER D OG  
8036 N N   . VAL D 217 ? 0.2424 0.2946 0.5334 -0.0156 -0.0800 -0.0044 217 VAL D N   
8037 C CA  . VAL D 217 ? 0.2747 0.3158 0.5494 -0.0187 -0.0878 -0.0079 217 VAL D CA  
8038 C C   . VAL D 217 ? 0.2515 0.2937 0.5247 -0.0159 -0.1059 -0.0119 217 VAL D C   
8039 O O   . VAL D 217 ? 0.2667 0.3147 0.5423 -0.0101 -0.1120 -0.0108 217 VAL D O   
8040 C CB  . VAL D 217 ? 0.3032 0.3303 0.5452 -0.0163 -0.0816 -0.0061 217 VAL D CB  
8041 C CG1 . VAL D 217 ? 0.3116 0.3371 0.5541 -0.0189 -0.0650 -0.0023 217 VAL D CG1 
8042 C CG2 . VAL D 217 ? 0.2588 0.2839 0.4822 -0.0085 -0.0852 -0.0043 217 VAL D CG2 
8043 N N   . SER D 218 ? 0.2559 0.2913 0.5237 -0.0198 -0.1150 -0.0166 218 SER D N   
8044 C CA  . SER D 218 ? 0.2560 0.2914 0.5193 -0.0169 -0.1327 -0.0208 218 SER D CA  
8045 C C   . SER D 218 ? 0.2662 0.2891 0.4933 -0.0106 -0.1360 -0.0203 218 SER D C   
8046 O O   . SER D 218 ? 0.2475 0.2605 0.4535 -0.0103 -0.1267 -0.0187 218 SER D O   
8047 C CB  . SER D 218 ? 0.2829 0.3163 0.5562 -0.0235 -0.1428 -0.0271 218 SER D CB  
8048 O OG  . SER D 218 ? 0.2792 0.2973 0.5288 -0.0255 -0.1401 -0.0291 218 SER D OG  
8049 N N   . SER D 219 ? 0.3043 0.3710 0.4802 -0.0172 -0.1231 -0.0271 219 SER D N   
8050 C CA  . SER D 219 ? 0.3006 0.3556 0.4397 -0.0136 -0.1230 -0.0301 219 SER D CA  
8051 C C   . SER D 219 ? 0.2848 0.3277 0.4174 -0.0210 -0.1209 -0.0450 219 SER D C   
8052 O O   . SER D 219 ? 0.2960 0.3240 0.4071 -0.0189 -0.1115 -0.0453 219 SER D O   
8053 C CB  . SER D 219 ? 0.3715 0.4413 0.4937 -0.0085 -0.1378 -0.0297 219 SER D CB  
8054 O OG  . SER D 219 ? 0.4334 0.5091 0.5572 0.0013  -0.1371 -0.0135 219 SER D OG  
8055 N N   . GLU D 220 ? 0.3004 0.3493 0.4551 -0.0298 -0.1284 -0.0576 220 GLU D N   
8056 C CA  . GLU D 220 ? 0.3294 0.3639 0.4828 -0.0365 -0.1254 -0.0732 220 GLU D CA  
8057 C C   . GLU D 220 ? 0.3011 0.3178 0.4626 -0.0363 -0.1082 -0.0657 220 GLU D C   
8058 O O   . GLU D 220 ? 0.3141 0.3159 0.4608 -0.0355 -0.1011 -0.0722 220 GLU D O   
8059 C CB  . GLU D 220 ? 0.3998 0.4424 0.5829 -0.0474 -0.1358 -0.0885 220 GLU D CB  
8060 C CG  . GLU D 220 ? 0.5478 0.5706 0.7412 -0.0544 -0.1285 -0.1025 220 GLU D CG  
8061 C CD  . GLU D 220 ? 0.7044 0.7312 0.9198 -0.0641 -0.1330 -0.1159 220 GLU D CD  
8062 O OE1 . GLU D 220 ? 0.7376 0.7845 0.9672 -0.0668 -0.1414 -0.1123 220 GLU D OE1 
8063 O OE2 . GLU D 220 ? 0.7683 0.7779 0.9865 -0.0683 -0.1266 -0.1291 220 GLU D OE2 
8064 N N   . GLN D 221 ? 0.2638 0.2843 0.4484 -0.0360 -0.1009 -0.0517 221 GLN D N   
8065 C CA  . GLN D 221 ? 0.2568 0.2657 0.4470 -0.0348 -0.0856 -0.0427 221 GLN D CA  
8066 C C   . GLN D 221 ? 0.2582 0.2597 0.4173 -0.0273 -0.0781 -0.0373 221 GLN D C   
8067 O O   . GLN D 221 ? 0.2531 0.2431 0.4056 -0.0265 -0.0697 -0.0385 221 GLN D O   
8068 C CB  . GLN D 221 ? 0.2461 0.2655 0.4632 -0.0354 -0.0795 -0.0287 221 GLN D CB  
8069 C CG  . GLN D 221 ? 0.2375 0.2613 0.4930 -0.0446 -0.0814 -0.0310 221 GLN D CG  
8070 C CD  . GLN D 221 ? 0.2447 0.2829 0.5250 -0.0443 -0.0739 -0.0153 221 GLN D CD  
8071 O OE1 . GLN D 221 ? 0.2385 0.2899 0.5129 -0.0385 -0.0745 -0.0087 221 GLN D OE1 
8072 N NE2 . GLN D 221 ? 0.2150 0.2504 0.5231 -0.0495 -0.0653 -0.0084 221 GLN D NE2 
8073 N N   . VAL D 222 ? 0.2512 0.2592 0.3939 -0.0217 -0.0806 -0.0309 222 VAL D N   
8074 C CA  . VAL D 222 ? 0.2576 0.2581 0.3749 -0.0163 -0.0730 -0.0262 222 VAL D CA  
8075 C C   . VAL D 222 ? 0.2867 0.2787 0.3805 -0.0161 -0.0743 -0.0359 222 VAL D C   
8076 O O   . VAL D 222 ? 0.2762 0.2606 0.3565 -0.0139 -0.0650 -0.0342 222 VAL D O   
8077 C CB  . VAL D 222 ? 0.2921 0.2982 0.4002 -0.0106 -0.0748 -0.0176 222 VAL D CB  
8078 C CG1 . VAL D 222 ? 0.2764 0.2734 0.3651 -0.0073 -0.0647 -0.0126 222 VAL D CG1 
8079 C CG2 . VAL D 222 ? 0.3503 0.3666 0.4818 -0.0100 -0.0736 -0.0108 222 VAL D CG2 
8080 N N   . SER D 223 ? 0.2775 0.2737 0.3654 -0.0180 -0.0856 -0.0469 223 SER D N   
8081 C CA  . SER D 223 ? 0.3013 0.2917 0.3637 -0.0170 -0.0857 -0.0576 223 SER D CA  
8082 C C   . SER D 223 ? 0.3015 0.2790 0.3723 -0.0193 -0.0759 -0.0653 223 SER D C   
8083 O O   . SER D 223 ? 0.3176 0.2887 0.3689 -0.0164 -0.0695 -0.0703 223 SER D O   
8084 C CB  . SER D 223 ? 0.3334 0.3342 0.3874 -0.0192 -0.1005 -0.0711 223 SER D CB  
8085 O OG  . SER D 223 ? 0.3897 0.3886 0.4683 -0.0270 -0.1049 -0.0858 223 SER D OG  
8086 N N   . LYS D 224 ? 0.2688 0.2432 0.3704 -0.0238 -0.0740 -0.0652 224 LYS D N   
8087 C CA  . LYS D 224 ? 0.2811 0.2425 0.3946 -0.0243 -0.0638 -0.0689 224 LYS D CA  
8088 C C   . LYS D 224 ? 0.2624 0.2221 0.3674 -0.0187 -0.0516 -0.0560 224 LYS D C   
8089 O O   . LYS D 224 ? 0.2638 0.2151 0.3669 -0.0160 -0.0433 -0.0595 224 LYS D O   
8090 C CB  . LYS D 224 ? 0.2616 0.2203 0.4123 -0.0299 -0.0629 -0.0667 224 LYS D CB  
8091 C CG  . LYS D 224 ? 0.3258 0.2869 0.4918 -0.0379 -0.0751 -0.0822 224 LYS D CG  
8092 C CD  . LYS D 224 ? 0.4134 0.3649 0.5667 -0.0394 -0.0779 -0.1047 224 LYS D CD  
8093 C CE  . LYS D 224 ? 0.5193 0.4759 0.6884 -0.0490 -0.0918 -0.1238 224 LYS D CE  
8094 N NZ  . LYS D 224 ? 0.5942 0.5472 0.7406 -0.0498 -0.0969 -0.1493 224 LYS D NZ  
8095 N N   . PHE D 225 ? 0.2416 0.2100 0.3438 -0.0168 -0.0502 -0.0423 225 PHE D N   
8096 C CA  . PHE D 225 ? 0.2526 0.2223 0.3455 -0.0129 -0.0403 -0.0330 225 PHE D CA  
8097 C C   . PHE D 225 ? 0.2400 0.2057 0.3070 -0.0100 -0.0374 -0.0387 225 PHE D C   
8098 O O   . PHE D 225 ? 0.2461 0.2108 0.3102 -0.0075 -0.0284 -0.0365 225 PHE D O   
8099 C CB  . PHE D 225 ? 0.2440 0.2227 0.3348 -0.0121 -0.0402 -0.0223 225 PHE D CB  
8100 C CG  . PHE D 225 ? 0.2215 0.2085 0.3353 -0.0136 -0.0394 -0.0144 225 PHE D CG  
8101 C CD1 . PHE D 225 ? 0.2600 0.2464 0.3966 -0.0159 -0.0381 -0.0131 225 PHE D CD1 
8102 C CD2 . PHE D 225 ? 0.2586 0.2538 0.3711 -0.0124 -0.0390 -0.0082 225 PHE D CD2 
8103 C CE1 . PHE D 225 ? 0.2693 0.2660 0.4256 -0.0170 -0.0360 -0.0035 225 PHE D CE1 
8104 C CE2 . PHE D 225 ? 0.2903 0.2961 0.4212 -0.0130 -0.0368 -0.0013 225 PHE D CE2 
8105 C CZ  . PHE D 225 ? 0.2517 0.2597 0.4039 -0.0153 -0.0351 0.0020  225 PHE D CZ  
8106 N N   . ARG D 226 ? 0.2449 0.2114 0.2933 -0.0099 -0.0450 -0.0446 226 ARG D N   
8107 C CA  . ARG D 226 ? 0.2497 0.2155 0.2711 -0.0068 -0.0411 -0.0463 226 ARG D CA  
8108 C C   . ARG D 226 ? 0.2695 0.2298 0.2845 -0.0055 -0.0370 -0.0600 226 ARG D C   
8109 O O   . ARG D 226 ? 0.3104 0.2718 0.3042 -0.0023 -0.0308 -0.0611 226 ARG D O   
8110 C CB  . ARG D 226 ? 0.2470 0.2184 0.2493 -0.0056 -0.0504 -0.0446 226 ARG D CB  
8111 C CG  . ARG D 226 ? 0.2544 0.2298 0.2657 -0.0053 -0.0538 -0.0315 226 ARG D CG  
8112 C CD  . ARG D 226 ? 0.2963 0.2766 0.2873 -0.0015 -0.0603 -0.0255 226 ARG D CD  
8113 N NE  . ARG D 226 ? 0.2906 0.2732 0.2950 0.0000  -0.0633 -0.0146 226 ARG D NE  
8114 C CZ  . ARG D 226 ? 0.2875 0.2786 0.3036 0.0006  -0.0745 -0.0146 226 ARG D CZ  
8115 N NH1 . ARG D 226 ? 0.3169 0.3162 0.3318 -0.0014 -0.0857 -0.0257 226 ARG D NH1 
8116 N NH2 . ARG D 226 ? 0.2972 0.2902 0.3277 0.0032  -0.0746 -0.0051 226 ARG D NH2 
8117 N N   . LYS D 227 ? 0.2596 0.2134 0.2949 -0.0076 -0.0383 -0.0700 227 LYS D N   
8118 C CA  . LYS D 227 ? 0.2935 0.2392 0.3272 -0.0056 -0.0325 -0.0849 227 LYS D CA  
8119 C C   . LYS D 227 ? 0.2625 0.2045 0.3098 -0.0014 -0.0191 -0.0779 227 LYS D C   
8120 O O   . LYS D 227 ? 0.3000 0.2356 0.3467 0.0024  -0.0115 -0.0886 227 LYS D O   
8121 C CB  . LYS D 227 ? 0.3154 0.2532 0.3678 -0.0104 -0.0396 -0.1009 227 LYS D CB  
8122 C CG  . LYS D 227 ? 0.3461 0.2926 0.3841 -0.0146 -0.0544 -0.1110 227 LYS D CG  
8123 C CD  . LYS D 227 ? 0.4914 0.4322 0.5542 -0.0218 -0.0625 -0.1273 227 LYS D CD  
8124 C CE  . LYS D 227 ? 0.5896 0.5178 0.6538 -0.0220 -0.0578 -0.1509 227 LYS D CE  
8125 N NZ  . LYS D 227 ? 0.6321 0.5545 0.7246 -0.0315 -0.0668 -0.1679 227 LYS D NZ  
8126 N N   . LEU D 228 ? 0.2395 0.1874 0.2995 -0.0014 -0.0163 -0.0609 228 LEU D N   
8127 C CA  . LEU D 228 ? 0.2309 0.1823 0.2993 0.0032  -0.0051 -0.0525 228 LEU D CA  
8128 C C   . LEU D 228 ? 0.2399 0.1979 0.2851 0.0057  0.0011  -0.0521 228 LEU D C   
8129 O O   . LEU D 228 ? 0.2567 0.2171 0.2796 0.0037  -0.0030 -0.0528 228 LEU D O   
8130 C CB  . LEU D 228 ? 0.2398 0.2011 0.3233 0.0020  -0.0050 -0.0359 228 LEU D CB  
8131 C CG  . LEU D 228 ? 0.2444 0.2019 0.3531 0.0000  -0.0085 -0.0322 228 LEU D CG  
8132 C CD1 . LEU D 228 ? 0.2506 0.2219 0.3649 -0.0016 -0.0096 -0.0175 228 LEU D CD1 
8133 C CD2 . LEU D 228 ? 0.2600 0.2116 0.3904 0.0046  -0.0008 -0.0303 228 LEU D CD2 
8134 N N   . ASN D 229 ? 0.2348 0.1975 0.2883 0.0104  0.0116  -0.0486 229 ASN D N   
8135 C CA  . ASN D 229 ? 0.2494 0.2206 0.2874 0.0125  0.0200  -0.0472 229 ASN D CA  
8136 C C   . ASN D 229 ? 0.2599 0.2458 0.3120 0.0124  0.0249  -0.0332 229 ASN D C   
8137 O O   . ASN D 229 ? 0.2322 0.2224 0.3067 0.0150  0.0257  -0.0270 229 ASN D O   
8138 C CB  . ASN D 229 ? 0.2871 0.2539 0.3230 0.0191  0.0293  -0.0598 229 ASN D CB  
8139 C CG  . ASN D 229 ? 0.3646 0.3223 0.3782 0.0187  0.0252  -0.0770 229 ASN D CG  
8140 O OD1 . ASN D 229 ? 0.3743 0.3313 0.3731 0.0140  0.0151  -0.0775 229 ASN D OD1 
8141 N ND2 . ASN D 229 ? 0.4228 0.3757 0.4343 0.0244  0.0333  -0.0919 229 ASN D ND2 
8142 N N   . PHE D 230 ? 0.2274 0.2225 0.2673 0.0094  0.0284  -0.0282 230 PHE D N   
8143 C CA  . PHE D 230 ? 0.2058 0.2182 0.2595 0.0080  0.0332  -0.0186 230 PHE D CA  
8144 C C   . PHE D 230 ? 0.2358 0.2577 0.3018 0.0147  0.0433  -0.0190 230 PHE D C   
8145 O O   . PHE D 230 ? 0.2177 0.2564 0.3033 0.0161  0.0450  -0.0111 230 PHE D O   
8146 C CB  . PHE D 230 ? 0.2210 0.2388 0.2624 0.0016  0.0359  -0.0144 230 PHE D CB  
8147 C CG  . PHE D 230 ? 0.2090 0.2200 0.2434 -0.0044 0.0279  -0.0116 230 PHE D CG  
8148 C CD1 . PHE D 230 ? 0.1873 0.2039 0.2352 -0.0075 0.0218  -0.0082 230 PHE D CD1 
8149 C CD2 . PHE D 230 ? 0.2435 0.2450 0.2581 -0.0064 0.0277  -0.0111 230 PHE D CD2 
8150 C CE1 . PHE D 230 ? 0.2179 0.2281 0.2607 -0.0124 0.0163  -0.0067 230 PHE D CE1 
8151 C CE2 . PHE D 230 ? 0.2155 0.2101 0.2266 -0.0106 0.0215  -0.0069 230 PHE D CE2 
8152 C CZ  . PHE D 230 ? 0.2169 0.2150 0.2429 -0.0136 0.0164  -0.0059 230 PHE D CZ  
8153 N N   . ASN D 231 ? 0.2255 0.2405 0.2800 0.0194  0.0502  -0.0282 231 ASN D N   
8154 C CA  . ASN D 231 ? 0.2449 0.2704 0.3104 0.0266  0.0622  -0.0292 231 ASN D CA  
8155 C C   . ASN D 231 ? 0.2564 0.2777 0.3462 0.0355  0.0639  -0.0306 231 ASN D C   
8156 O O   . ASN D 231 ? 0.2531 0.2592 0.3481 0.0357  0.0570  -0.0337 231 ASN D O   
8157 C CB  . ASN D 231 ? 0.2878 0.3081 0.3307 0.0293  0.0705  -0.0399 231 ASN D CB  
8158 C CG  . ASN D 231 ? 0.2925 0.2926 0.3203 0.0311  0.0647  -0.0547 231 ASN D CG  
8159 O OD1 . ASN D 231 ? 0.2878 0.2802 0.2998 0.0252  0.0546  -0.0552 231 ASN D OD1 
8160 N ND2 . ASN D 231 ? 0.3319 0.3241 0.3677 0.0392  0.0710  -0.0674 231 ASN D ND2 
8161 N N   . GLY D 232 ? 0.2631 0.2990 0.3711 0.0430  0.0739  -0.0269 232 GLY D N   
8162 C CA  . GLY D 232 ? 0.2814 0.3108 0.4129 0.0541  0.0792  -0.0287 232 GLY D CA  
8163 C C   . GLY D 232 ? 0.2987 0.3101 0.4201 0.0601  0.0875  -0.0475 232 GLY D C   
8164 O O   . GLY D 232 ? 0.3367 0.3483 0.4325 0.0579  0.0921  -0.0574 232 GLY D O   
8165 N N   . GLU D 233 ? 0.3136 0.3097 0.4564 0.0684  0.0906  -0.0524 233 GLU D N   
8166 C CA  . GLU D 233 ? 0.4132 0.3911 0.5510 0.0749  0.0995  -0.0741 233 GLU D CA  
8167 C C   . GLU D 233 ? 0.3896 0.3834 0.5214 0.0821  0.1145  -0.0790 233 GLU D C   
8168 O O   . GLU D 233 ? 0.3950 0.4101 0.5477 0.0880  0.1213  -0.0649 233 GLU D O   
8169 C CB  . GLU D 233 ? 0.4802 0.4396 0.6523 0.0835  0.1026  -0.0754 233 GLU D CB  
8170 C CG  . GLU D 233 ? 0.6035 0.5350 0.7726 0.0852  0.1060  -0.1016 233 GLU D CG  
8171 C CD  . GLU D 233 ? 0.7112 0.6207 0.9202 0.0918  0.1087  -0.0998 233 GLU D CD  
8172 O OE1 . GLU D 233 ? 0.7175 0.6168 0.9371 0.0846  0.0983  -0.0914 233 GLU D OE1 
8173 O OE2 . GLU D 233 ? 0.7773 0.6802 1.0081 0.1040  0.1219  -0.1051 233 GLU D OE2 
8174 N N   . GLY D 234 ? 0.3979 0.3855 0.5009 0.0817  0.1197  -0.0984 234 GLY D N   
8175 C CA  . GLY D 234 ? 0.4022 0.4064 0.4975 0.0886  0.1358  -0.1029 234 GLY D CA  
8176 C C   . GLY D 234 ? 0.4176 0.4448 0.4917 0.0806  0.1365  -0.0903 234 GLY D C   
8177 O O   . GLY D 234 ? 0.4332 0.4768 0.5008 0.0852  0.1510  -0.0920 234 GLY D O   
8178 N N   . GLU D 235 ? 0.4204 0.4485 0.4849 0.0690  0.1227  -0.0782 235 GLU D N   
8179 C CA  . GLU D 235 ? 0.3876 0.4309 0.4322 0.0599  0.1225  -0.0673 235 GLU D CA  
8180 C C   . GLU D 235 ? 0.4283 0.4587 0.4360 0.0532  0.1144  -0.0748 235 GLU D C   
8181 O O   . GLU D 235 ? 0.4001 0.4120 0.4017 0.0529  0.1046  -0.0864 235 GLU D O   
8182 C CB  . GLU D 235 ? 0.3972 0.4514 0.4604 0.0519  0.1132  -0.0486 235 GLU D CB  
8183 C CG  . GLU D 235 ? 0.3905 0.4610 0.4909 0.0589  0.1175  -0.0399 235 GLU D CG  
8184 C CD  . GLU D 235 ? 0.4190 0.5050 0.5340 0.0502  0.1073  -0.0239 235 GLU D CD  
8185 O OE1 . GLU D 235 ? 0.4781 0.5903 0.6155 0.0513  0.1121  -0.0143 235 GLU D OE1 
8186 O OE2 . GLU D 235 ? 0.3392 0.4132 0.4433 0.0422  0.0946  -0.0222 235 GLU D OE2 
8187 N N   . PRO D 236 ? 0.4544 0.4954 0.4384 0.0479  0.1184  -0.0673 236 PRO D N   
8188 C CA  . PRO D 236 ? 0.4711 0.5029 0.4193 0.0435  0.1103  -0.0717 236 PRO D CA  
8189 C C   . PRO D 236 ? 0.4005 0.4184 0.3529 0.0365  0.0918  -0.0680 236 PRO D C   
8190 O O   . PRO D 236 ? 0.3925 0.4127 0.3663 0.0314  0.0867  -0.0551 236 PRO D O   
8191 C CB  . PRO D 236 ? 0.5126 0.5594 0.4447 0.0388  0.1189  -0.0564 236 PRO D CB  
8192 C CG  . PRO D 236 ? 0.5164 0.5815 0.4684 0.0439  0.1367  -0.0538 236 PRO D CG  
8193 C CD  . PRO D 236 ? 0.4586 0.5217 0.4485 0.0467  0.1321  -0.0548 236 PRO D CD  
8194 N N   . GLU D 237 ? 0.4763 0.4823 0.4083 0.0363  0.0820  -0.0807 237 GLU D N   
8195 C CA  . GLU D 237 ? 0.4843 0.4780 0.4235 0.0307  0.0652  -0.0793 237 GLU D CA  
8196 C C   . GLU D 237 ? 0.4406 0.4382 0.3730 0.0233  0.0588  -0.0612 237 GLU D C   
8197 O O   . GLU D 237 ? 0.4670 0.4704 0.3742 0.0223  0.0612  -0.0550 237 GLU D O   
8198 C CB  . GLU D 237 ? 0.5716 0.5556 0.4922 0.0312  0.0556  -0.0980 237 GLU D CB  
8199 C CG  . GLU D 237 ? 0.6584 0.6346 0.5837 0.0245  0.0383  -0.0937 237 GLU D CG  
8200 C CD  . GLU D 237 ? 0.7734 0.7397 0.6961 0.0237  0.0278  -0.1142 237 GLU D CD  
8201 O OE1 . GLU D 237 ? 0.8067 0.7627 0.7492 0.0265  0.0317  -0.1285 237 GLU D OE1 
8202 O OE2 . GLU D 237 ? 0.8157 0.7853 0.7186 0.0202  0.0156  -0.1159 237 GLU D OE2 
8203 N N   . GLU D 238 ? 0.3724 0.3171 0.3206 -0.0315 0.0350  -0.0666 238 GLU D N   
8204 C CA  . GLU D 238 ? 0.3524 0.3017 0.2970 -0.0314 0.0240  -0.0551 238 GLU D CA  
8205 C C   . GLU D 238 ? 0.3309 0.2776 0.2846 -0.0255 0.0136  -0.0463 238 GLU D C   
8206 O O   . GLU D 238 ? 0.3303 0.2835 0.3047 -0.0141 0.0135  -0.0429 238 GLU D O   
8207 C CB  . GLU D 238 ? 0.3729 0.3348 0.3307 -0.0237 0.0268  -0.0520 238 GLU D CB  
8208 C CG  . GLU D 238 ? 0.4678 0.4347 0.4209 -0.0279 0.0381  -0.0604 238 GLU D CG  
8209 C CD  . GLU D 238 ? 0.5704 0.5511 0.5411 -0.0192 0.0415  -0.0571 238 GLU D CD  
8210 O OE1 . GLU D 238 ? 0.6254 0.6124 0.5954 -0.0215 0.0506  -0.0627 238 GLU D OE1 
8211 O OE2 . GLU D 238 ? 0.5711 0.5568 0.5559 -0.0106 0.0351  -0.0488 238 GLU D OE2 
8212 N N   . PRO D 239 ? 0.3254 0.2640 0.2648 -0.0335 0.0044  -0.0415 239 PRO D N   
8213 C CA  . PRO D 239 ? 0.3219 0.2589 0.2706 -0.0283 -0.0055 -0.0325 239 PRO D CA  
8214 C C   . PRO D 239 ? 0.2814 0.2280 0.2463 -0.0178 -0.0096 -0.0239 239 PRO D C   
8215 O O   . PRO D 239 ? 0.2802 0.2314 0.2415 -0.0189 -0.0105 -0.0208 239 PRO D O   
8216 C CB  . PRO D 239 ? 0.3460 0.2752 0.2755 -0.0405 -0.0151 -0.0270 239 PRO D CB  
8217 C CG  . PRO D 239 ? 0.4157 0.3392 0.3239 -0.0537 -0.0081 -0.0369 239 PRO D CG  
8218 C CD  . PRO D 239 ? 0.3934 0.3246 0.3074 -0.0490 0.0028  -0.0439 239 PRO D CD  
8219 N N   . MET D 240 ? 0.2588 0.2082 0.2408 -0.0086 -0.0121 -0.0203 240 MET D N   
8220 C CA  . MET D 240 ? 0.2410 0.1996 0.2381 0.0006  -0.0153 -0.0129 240 MET D CA  
8221 C C   . MET D 240 ? 0.2537 0.2092 0.2462 -0.0019 -0.0257 -0.0035 240 MET D C   
8222 O O   . MET D 240 ? 0.2440 0.1971 0.2421 0.0000  -0.0318 0.0015  240 MET D O   
8223 C CB  . MET D 240 ? 0.2225 0.1861 0.2394 0.0102  -0.0139 -0.0123 240 MET D CB  
8224 C CG  . MET D 240 ? 0.2338 0.2082 0.2646 0.0181  -0.0163 -0.0053 240 MET D CG  
8225 S SD  . MET D 240 ? 0.2133 0.1953 0.2668 0.0276  -0.0157 -0.0031 240 MET D SD  
8226 C CE  . MET D 240 ? 0.2171 0.2059 0.2789 0.0299  -0.0052 -0.0099 240 MET D CE  
8227 N N   . VAL D 241 ? 0.2611 0.2167 0.2447 -0.0063 -0.0277 -0.0006 241 VAL D N   
8228 C CA  . VAL D 241 ? 0.2461 0.1988 0.2276 -0.0087 -0.0368 0.0088  241 VAL D CA  
8229 C C   . VAL D 241 ? 0.2401 0.1973 0.2231 -0.0068 -0.0357 0.0110  241 VAL D C   
8230 O O   . VAL D 241 ? 0.2546 0.2153 0.2335 -0.0078 -0.0291 0.0055  241 VAL D O   
8231 C CB  . VAL D 241 ? 0.2728 0.2167 0.2370 -0.0209 -0.0428 0.0112  241 VAL D CB  
8232 C CG1 . VAL D 241 ? 0.2764 0.2147 0.2377 -0.0239 -0.0441 0.0087  241 VAL D CG1 
8233 C CG2 . VAL D 241 ? 0.2739 0.2162 0.2216 -0.0298 -0.0384 0.0058  241 VAL D CG2 
8234 N N   . ASP D 242 ? 0.2301 0.1869 0.2199 -0.0042 -0.0418 0.0193  242 ASP D N   
8235 C CA  . ASP D 242 ? 0.2385 0.1974 0.2299 -0.0029 -0.0410 0.0215  242 ASP D CA  
8236 C C   . ASP D 242 ? 0.2216 0.1892 0.2204 0.0036  -0.0332 0.0161  242 ASP D C   
8237 O O   . ASP D 242 ? 0.2359 0.2059 0.2296 0.0015  -0.0292 0.0135  242 ASP D O   
8238 C CB  . ASP D 242 ? 0.2680 0.2218 0.2434 -0.0130 -0.0427 0.0221  242 ASP D CB  
8239 C CG  . ASP D 242 ? 0.2890 0.2354 0.2597 -0.0198 -0.0524 0.0307  242 ASP D CG  
8240 O OD1 . ASP D 242 ? 0.2578 0.2037 0.2412 -0.0148 -0.0575 0.0379  242 ASP D OD1 
8241 O OD2 . ASP D 242 ? 0.3293 0.2715 0.2843 -0.0305 -0.0546 0.0304  242 ASP D OD2 
8242 N N   . ASN D 243 ? 0.1960 0.1690 0.2075 0.0109  -0.0317 0.0156  243 ASN D N   
8243 C CA  . ASN D 243 ? 0.1906 0.1734 0.2115 0.0166  -0.0258 0.0128  243 ASN D CA  
8244 C C   . ASN D 243 ? 0.1998 0.1855 0.2294 0.0210  -0.0271 0.0171  243 ASN D C   
8245 O O   . ASN D 243 ? 0.1981 0.1910 0.2390 0.0264  -0.0257 0.0178  243 ASN D O   
8246 C CB  . ASN D 243 ? 0.2003 0.1882 0.2306 0.0211  -0.0231 0.0101  243 ASN D CB  
8247 C CG  . ASN D 243 ? 0.1862 0.1715 0.2239 0.0241  -0.0286 0.0143  243 ASN D CG  
8248 O OD1 . ASN D 243 ? 0.2205 0.2009 0.2569 0.0229  -0.0342 0.0194  243 ASN D OD1 
8249 N ND2 . ASN D 243 ? 0.2188 0.2080 0.2659 0.0280  -0.0268 0.0126  243 ASN D ND2 
8250 N N   . TRP D 244 ? 0.2048 0.1849 0.2290 0.0179  -0.0293 0.0197  244 TRP D N   
8251 C CA  . TRP D 244 ? 0.1993 0.1799 0.2306 0.0211  -0.0292 0.0226  244 TRP D CA  
8252 C C   . TRP D 244 ? 0.2134 0.1929 0.2372 0.0174  -0.0260 0.0205  244 TRP D C   
8253 O O   . TRP D 244 ? 0.2375 0.2133 0.2502 0.0117  -0.0264 0.0193  244 TRP D O   
8254 C CB  . TRP D 244 ? 0.2268 0.1999 0.2628 0.0215  -0.0354 0.0292  244 TRP D CB  
8255 C CG  . TRP D 244 ? 0.2422 0.2065 0.2679 0.0145  -0.0408 0.0325  244 TRP D CG  
8256 C CD1 . TRP D 244 ? 0.2414 0.2025 0.2615 0.0105  -0.0454 0.0343  244 TRP D CD1 
8257 C CD2 . TRP D 244 ? 0.2897 0.2474 0.3089 0.0094  -0.0425 0.0350  244 TRP D CD2 
8258 N NE1 . TRP D 244 ? 0.2527 0.2067 0.2626 0.0026  -0.0502 0.0380  244 TRP D NE1 
8259 C CE2 . TRP D 244 ? 0.3227 0.2746 0.3326 0.0021  -0.0488 0.0390  244 TRP D CE2 
8260 C CE3 . TRP D 244 ? 0.3094 0.2653 0.3293 0.0096  -0.0395 0.0343  244 TRP D CE3 
8261 C CZ2 . TRP D 244 ? 0.3709 0.3163 0.3728 -0.0052 -0.0528 0.0433  244 TRP D CZ2 
8262 C CZ3 . TRP D 244 ? 0.3378 0.2862 0.3507 0.0033  -0.0430 0.0380  244 TRP D CZ3 
8263 C CH2 . TRP D 244 ? 0.3363 0.2799 0.3409 -0.0040 -0.0501 0.0431  244 TRP D CH2 
8264 N N   . ARG D 245 ? 0.1997 0.1828 0.2290 0.0200  -0.0226 0.0197  245 ARG D N   
8265 C CA  . ARG D 245 ? 0.1854 0.1660 0.2082 0.0163  -0.0197 0.0180  245 ARG D CA  
8266 C C   . ARG D 245 ? 0.2067 0.1769 0.2325 0.0162  -0.0225 0.0219  245 ARG D C   
8267 O O   . ARG D 245 ? 0.2262 0.1954 0.2629 0.0209  -0.0234 0.0244  245 ARG D O   
8268 C CB  . ARG D 245 ? 0.1732 0.1631 0.1996 0.0178  -0.0142 0.0148  245 ARG D CB  
8269 C CG  . ARG D 245 ? 0.1828 0.1707 0.2008 0.0128  -0.0111 0.0124  245 ARG D CG  
8270 C CD  . ARG D 245 ? 0.1958 0.1922 0.2160 0.0125  -0.0061 0.0098  245 ARG D CD  
8271 N NE  . ARG D 245 ? 0.1964 0.1916 0.2067 0.0064  -0.0036 0.0076  245 ARG D NE  
8272 C CZ  . ARG D 245 ? 0.1802 0.1791 0.1880 0.0031  0.0005  0.0052  245 ARG D CZ  
8273 N NH1 . ARG D 245 ? 0.1709 0.1749 0.1850 0.0050  0.0030  0.0044  245 ARG D NH1 
8274 N NH2 . ARG D 245 ? 0.1938 0.1917 0.1915 -0.0032 0.0021  0.0037  245 ARG D NH2 
8275 N N   . PRO D 246 ? 0.2237 0.1865 0.2413 0.0109  -0.0237 0.0228  246 PRO D N   
8276 C CA  . PRO D 246 ? 0.2364 0.1887 0.2595 0.0110  -0.0259 0.0270  246 PRO D CA  
8277 C C   . PRO D 246 ? 0.2261 0.1791 0.2577 0.0151  -0.0199 0.0237  246 PRO D C   
8278 O O   . PRO D 246 ? 0.2314 0.1922 0.2597 0.0148  -0.0146 0.0184  246 PRO D O   
8279 C CB  . PRO D 246 ? 0.2930 0.2394 0.3043 0.0037  -0.0272 0.0274  246 PRO D CB  
8280 C CG  . PRO D 246 ? 0.2647 0.2173 0.2640 -0.0008 -0.0278 0.0252  246 PRO D CG  
8281 C CD  . PRO D 246 ? 0.2561 0.2200 0.2602 0.0044  -0.0231 0.0205  246 PRO D CD  
8282 N N   . THR D 247 ? 0.2458 0.1911 0.2889 0.0183  -0.0207 0.0272  247 THR D N   
8283 C CA  . THR D 247 ? 0.2292 0.1736 0.2793 0.0211  -0.0136 0.0228  247 THR D CA  
8284 C C   . THR D 247 ? 0.2274 0.1672 0.2677 0.0158  -0.0092 0.0182  247 THR D C   
8285 O O   . THR D 247 ? 0.2485 0.1818 0.2812 0.0109  -0.0126 0.0204  247 THR D O   
8286 C CB  . THR D 247 ? 0.2328 0.1692 0.2996 0.0261  -0.0139 0.0269  247 THR D CB  
8287 O OG1 . THR D 247 ? 0.2469 0.1724 0.3155 0.0235  -0.0196 0.0334  247 THR D OG1 
8288 C CG2 . THR D 247 ? 0.2384 0.1811 0.3157 0.0313  -0.0172 0.0311  247 THR D CG2 
8289 N N   . GLN D 248 ? 0.2145 0.1583 0.2540 0.0156  -0.0019 0.0118  248 GLN D N   
8290 C CA  . GLN D 248 ? 0.1982 0.1399 0.2269 0.0096  0.0030  0.0064  248 GLN D CA  
8291 C C   . GLN D 248 ? 0.2082 0.1397 0.2436 0.0102  0.0096  0.0025  248 GLN D C   
8292 O O   . GLN D 248 ? 0.2201 0.1499 0.2690 0.0158  0.0120  0.0027  248 GLN D O   
8293 C CB  . GLN D 248 ? 0.2069 0.1632 0.2277 0.0068  0.0062  0.0023  248 GLN D CB  
8294 C CG  . GLN D 248 ? 0.2053 0.1717 0.2219 0.0068  0.0013  0.0054  248 GLN D CG  
8295 C CD  . GLN D 248 ? 0.2092 0.1706 0.2157 0.0019  -0.0022 0.0071  248 GLN D CD  
8296 O OE1 . GLN D 248 ? 0.2428 0.2010 0.2407 -0.0038 0.0001  0.0048  248 GLN D OE1 
8297 N NE2 . GLN D 248 ? 0.2176 0.1780 0.2247 0.0032  -0.0077 0.0113  248 GLN D NE2 
8298 N N   . PRO D 249 ? 0.2301 0.1543 0.2569 0.0044  0.0130  -0.0014 249 PRO D N   
8299 C CA  . PRO D 249 ? 0.2497 0.1616 0.2827 0.0044  0.0201  -0.0061 249 PRO D CA  
8300 C C   . PRO D 249 ? 0.2406 0.1592 0.2759 0.0053  0.0284  -0.0129 249 PRO D C   
8301 O O   . PRO D 249 ? 0.2449 0.1762 0.2698 0.0011  0.0299  -0.0159 249 PRO D O   
8302 C CB  . PRO D 249 ? 0.2708 0.1764 0.2893 -0.0040 0.0217  -0.0094 249 PRO D CB  
8303 C CG  . PRO D 249 ? 0.2765 0.1870 0.2863 -0.0068 0.0130  -0.0031 249 PRO D CG  
8304 C CD  . PRO D 249 ? 0.2421 0.1680 0.2537 -0.0028 0.0102  -0.0010 249 PRO D CD  
8305 N N   . LEU D 250 ? 0.2361 0.1467 0.2858 0.0102  0.0339  -0.0150 250 LEU D N   
8306 C CA  . LEU D 250 ? 0.2492 0.1653 0.3008 0.0100  0.0431  -0.0224 250 LEU D CA  
8307 C C   . LEU D 250 ? 0.2551 0.1686 0.2915 0.0005  0.0510  -0.0316 250 LEU D C   
8308 O O   . LEU D 250 ? 0.2818 0.2056 0.3113 -0.0037 0.0563  -0.0370 250 LEU D O   
8309 C CB  . LEU D 250 ? 0.2939 0.2010 0.3662 0.0175  0.0482  -0.0229 250 LEU D CB  
8310 C CG  . LEU D 250 ? 0.3138 0.2280 0.3919 0.0189  0.0574  -0.0293 250 LEU D CG  
8311 C CD1 . LEU D 250 ? 0.2733 0.2065 0.3478 0.0197  0.0519  -0.0253 250 LEU D CD1 
8312 C CD2 . LEU D 250 ? 0.3456 0.2506 0.4479 0.0277  0.0619  -0.0281 250 LEU D CD2 
8313 N N   . LYS D 251 ? 0.2608 0.1608 0.2912 -0.0039 0.0517  -0.0333 251 LYS D N   
8314 C CA  . LYS D 251 ? 0.2746 0.1701 0.2898 -0.0138 0.0591  -0.0421 251 LYS D CA  
8315 C C   . LYS D 251 ? 0.3190 0.2116 0.3385 -0.0146 0.0712  -0.0517 251 LYS D C   
8316 O O   . LYS D 251 ? 0.3281 0.2107 0.3655 -0.0071 0.0758  -0.0527 251 LYS D O   
8317 C CB  . LYS D 251 ? 0.2930 0.2038 0.2898 -0.0220 0.0549  -0.0410 251 LYS D CB  
8318 C CG  . LYS D 251 ? 0.3665 0.2786 0.3604 -0.0209 0.0443  -0.0323 251 LYS D CG  
8319 C CD  . LYS D 251 ? 0.3833 0.3076 0.3605 -0.0294 0.0411  -0.0313 251 LYS D CD  
8320 C CE  . LYS D 251 ? 0.4384 0.3635 0.4137 -0.0282 0.0322  -0.0238 251 LYS D CE  
8321 N NZ  . LYS D 251 ? 0.4481 0.3857 0.4096 -0.0359 0.0296  -0.0225 251 LYS D NZ  
8322 N N   . ASN D 252 ? 0.2943 0.1946 0.2979 -0.0243 0.0768  -0.0587 252 ASN D N   
8323 C CA  . ASN D 252 ? 0.3517 0.2473 0.3549 -0.0284 0.0899  -0.0698 252 ASN D CA  
8324 C C   . ASN D 252 ? 0.3938 0.3062 0.4020 -0.0257 0.0911  -0.0691 252 ASN D C   
8325 O O   . ASN D 252 ? 0.4264 0.3505 0.4210 -0.0352 0.0951  -0.0737 252 ASN D O   
8326 C CB  . ASN D 252 ? 0.3997 0.2933 0.3805 -0.0429 0.0954  -0.0779 252 ASN D CB  
8327 C CG  . ASN D 252 ? 0.4989 0.3823 0.4779 -0.0482 0.1102  -0.0910 252 ASN D CG  
8328 O OD1 . ASN D 252 ? 0.4742 0.3501 0.4711 -0.0399 0.1172  -0.0944 252 ASN D OD1 
8329 N ND2 . ASN D 252 ? 0.5517 0.4355 0.5093 -0.0628 0.1155  -0.0987 252 ASN D ND2 
8330 N N   . ARG D 253 ? 0.3092 0.2231 0.3368 -0.0137 0.0868  -0.0624 253 ARG D N   
8331 C CA  . ARG D 253 ? 0.2857 0.2145 0.3215 -0.0095 0.0870  -0.0603 253 ARG D CA  
8332 C C   . ARG D 253 ? 0.3162 0.2362 0.3752 0.0011  0.0919  -0.0606 253 ARG D C   
8333 O O   . ARG D 253 ? 0.3386 0.2432 0.4098 0.0070  0.0914  -0.0585 253 ARG D O   
8334 C CB  . ARG D 253 ? 0.2693 0.2138 0.3054 -0.0057 0.0740  -0.0492 253 ARG D CB  
8335 C CG  . ARG D 253 ? 0.2701 0.2265 0.2870 -0.0156 0.0700  -0.0484 253 ARG D CG  
8336 C CD  . ARG D 253 ? 0.2470 0.2169 0.2663 -0.0112 0.0583  -0.0381 253 ARG D CD  
8337 N NE  . ARG D 253 ? 0.2417 0.2022 0.2656 -0.0054 0.0511  -0.0324 253 ARG D NE  
8338 C CZ  . ARG D 253 ? 0.2132 0.1811 0.2404 -0.0007 0.0418  -0.0243 253 ARG D CZ  
8339 N NH1 . ARG D 253 ? 0.2159 0.1995 0.2450 0.0004  0.0384  -0.0207 253 ARG D NH1 
8340 N NH2 . ARG D 253 ? 0.2083 0.1677 0.2367 0.0023  0.0358  -0.0198 253 ARG D NH2 
8341 N N   . GLN D 254 ? 0.2918 0.2227 0.3577 0.0029  0.0965  -0.0623 254 GLN D N   
8342 C CA  . GLN D 254 ? 0.3448 0.2714 0.4339 0.0127  0.1019  -0.0622 254 GLN D CA  
8343 C C   . GLN D 254 ? 0.3310 0.2742 0.4285 0.0186  0.0933  -0.0529 254 GLN D C   
8344 O O   . GLN D 254 ? 0.3556 0.3147 0.4412 0.0129  0.0911  -0.0525 254 GLN D O   
8345 C CB  . GLN D 254 ? 0.4161 0.3393 0.5060 0.0081  0.1185  -0.0753 254 GLN D CB  
8346 C CG  . GLN D 254 ? 0.5385 0.4460 0.6163 -0.0002 0.1279  -0.0862 254 GLN D CG  
8347 C CD  . GLN D 254 ? 0.6477 0.5532 0.7208 -0.0076 0.1450  -0.1007 254 GLN D CD  
8348 O OE1 . GLN D 254 ? 0.7212 0.6089 0.8022 -0.0069 0.1570  -0.1100 254 GLN D OE1 
8349 N NE2 . GLN D 254 ? 0.6533 0.5768 0.7135 -0.0155 0.1466  -0.1030 254 GLN D NE2 
8350 N N   . ILE D 255 ? 0.2826 0.2219 0.4004 0.0294  0.0878  -0.0445 255 ILE D N   
8351 C CA  . ILE D 255 ? 0.2617 0.2147 0.3897 0.0354  0.0805  -0.0359 255 ILE D CA  
8352 C C   . ILE D 255 ? 0.2749 0.2305 0.4186 0.0388  0.0914  -0.0406 255 ILE D C   
8353 O O   . ILE D 255 ? 0.3122 0.2554 0.4727 0.0439  0.0991  -0.0436 255 ILE D O   
8354 C CB  . ILE D 255 ? 0.2611 0.2096 0.4010 0.0434  0.0682  -0.0239 255 ILE D CB  
8355 C CG1 . ILE D 255 ? 0.3028 0.2494 0.4255 0.0388  0.0589  -0.0205 255 ILE D CG1 
8356 C CG2 . ILE D 255 ? 0.2780 0.2408 0.4259 0.0482  0.0605  -0.0154 255 ILE D CG2 
8357 C CD1 . ILE D 255 ? 0.2864 0.2289 0.4168 0.0443  0.0464  -0.0089 255 ILE D CD1 
8358 N N   . LYS D 256 ? 0.2616 0.2336 0.4003 0.0355  0.0926  -0.0416 256 LYS D N   
8359 C CA  . LYS D 256 ? 0.2682 0.2453 0.4203 0.0376  0.1033  -0.0463 256 LYS D CA  
8360 C C   . LYS D 256 ? 0.2507 0.2378 0.4200 0.0462  0.0948  -0.0352 256 LYS D C   
8361 O O   . LYS D 256 ? 0.2510 0.2459 0.4154 0.0471  0.0818  -0.0260 256 LYS D O   
8362 C CB  . LYS D 256 ? 0.2872 0.2766 0.4220 0.0264  0.1112  -0.0551 256 LYS D CB  
8363 C CG  . LYS D 256 ? 0.3145 0.2953 0.4299 0.0155  0.1203  -0.0667 256 LYS D CG  
8364 C CD  . LYS D 256 ? 0.3940 0.3551 0.5218 0.0191  0.1333  -0.0758 256 LYS D CD  
8365 C CE  . LYS D 256 ? 0.4839 0.4364 0.5918 0.0068  0.1448  -0.0895 256 LYS D CE  
8366 N NZ  . LYS D 256 ? 0.5174 0.4488 0.6403 0.0114  0.1576  -0.0982 256 LYS D NZ  
8367 N N   . ALA D 257 ? 0.2672 0.2539 0.4579 0.0525  0.1028  -0.0362 257 ALA D N   
8368 C CA  . ALA D 257 ? 0.2698 0.2671 0.4781 0.0598  0.0962  -0.0260 257 ALA D CA  
8369 C C   . ALA D 257 ? 0.2667 0.2794 0.4746 0.0560  0.1042  -0.0308 257 ALA D C   
8370 O O   . ALA D 257 ? 0.2920 0.3034 0.4971 0.0510  0.1190  -0.0427 257 ALA D O   
8371 C CB  . ALA D 257 ? 0.2686 0.2560 0.4943 0.0662  0.0930  -0.0192 257 ALA D CB  
8372 N N   . SER D 258 ? 0.2473 0.2747 0.4575 0.0575  0.0944  -0.0215 258 SER D N   
8373 C CA  . SER D 258 ? 0.2153 0.2590 0.4272 0.0542  0.0996  -0.0233 258 SER D CA  
8374 C C   . SER D 258 ? 0.2682 0.3110 0.5004 0.0601  0.1054  -0.0223 258 SER D C   
8375 O O   . SER D 258 ? 0.2857 0.3409 0.5204 0.0571  0.1126  -0.0256 258 SER D O   
8376 C CB  . SER D 258 ? 0.2003 0.2582 0.4071 0.0536  0.0848  -0.0122 258 SER D CB  
8377 O OG  . SER D 258 ? 0.2194 0.2757 0.4439 0.0630  0.0750  -0.0007 258 SER D OG  
8378 N N   . PHE D 259 ? 0.2630 0.2919 0.5047 0.0659  0.0998  -0.0165 259 PHE D N   
8379 C CA  . PHE D 259 ? 0.2861 0.3142 0.5440 0.0701  0.1006  -0.0121 259 PHE D CA  
8380 C C   . PHE D 259 ? 0.3345 0.3472 0.5999 0.0710  0.1111  -0.0192 259 PHE D C   
8381 O O   . PHE D 259 ? 0.3550 0.3555 0.6140 0.0698  0.1119  -0.0228 259 PHE D O   
8382 C CB  . PHE D 259 ? 0.2753 0.3039 0.5382 0.0743  0.0834  0.0031  259 PHE D CB  
8383 C CG  . PHE D 259 ? 0.2741 0.2912 0.5299 0.0748  0.0729  0.0084  259 PHE D CG  
8384 C CD1 . PHE D 259 ? 0.2865 0.3061 0.5275 0.0727  0.0642  0.0105  259 PHE D CD1 
8385 C CD2 . PHE D 259 ? 0.3043 0.3091 0.5693 0.0769  0.0723  0.0112  259 PHE D CD2 
8386 C CE1 . PHE D 259 ? 0.3035 0.3129 0.5375 0.0726  0.0551  0.0150  259 PHE D CE1 
8387 C CE2 . PHE D 259 ? 0.3024 0.2981 0.5607 0.0765  0.0629  0.0161  259 PHE D CE2 
8388 C CZ  . PHE D 259 ? 0.3146 0.3123 0.5566 0.0742  0.0547  0.0174  259 PHE D CZ  
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