data_9O90
# 
_entry.id   9O90 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9O90         pdb_00009o90 10.2210/pdb9o90/pdb 
WWPDB D_1000295116 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_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                        9O90 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-17 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu                    Scott    Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 isabelle.phan@seattlechildrens.org Isabelle Phan   ? 'principal investigator/group leader' 0000-0001-6873-3401 
4 julie.early@seattlechildrens.org   Julie    Early  ? 'principal investigator/group leader' 0000-0003-1224-2747 
5 peter.myler@seattlechildrens.org   Peter    Myler  ? 'principal investigator/group leader' 0000-0002-0056-0513 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Seattle Structural Genomics Center for Infectious Disease'          1 ? 
'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of UTP--glucose-1-phosphate uridylyltransferase from Bordetella pertussis' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liu, L.'        1 0000-0003-0514-281X 
primary 'Lovell, S.'     2 0000-0002-3215-4472 
primary 'Seibold, S.'    3 0000-0001-8297-229X 
primary 'Battaile, K.P.' 4 0000-0003-0833-3259 
# 
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 'UTP--glucose-1-phosphate uridylyltransferase' 30991.625 2   2.7.7.9 ? ? ? 
2 non-polymer syn GLYCINE                                        75.067    4   ?       ? ? ? 
3 non-polymer syn GLYCEROL                                       92.094    3   ?       ? ? ? 
4 water       nat water                                          18.015    280 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'UDP-glucose pyrophosphorylase' 
# 
_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       
;MAHHHHHHVVRKAVFPVAGMGTRFLPATKAMPKEMLPVVDKPLIQYAVEEAVAAGITDLIFVTGRNKRAIEDHFDAAPEL
ETDLEAKGKHELLALVRDILPAHVNCLYIRQSAPLGLGHAVLTAAPAVGNEPFAVLLADDLIDADTPVLKQLIDVAVARQ
GSVLGVQEVPREDTRKYGIVASQPVDARTERVTHIVEKPAPEQAPTTLAVVGRYVLEAAIFDHLRATTVGAGNEIQLTDG
IAALLRERDVYAHRYDGKRYDCGSKAGMFQATVALGRKYHGLIPE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHVVRKAVFPVAGMGTRFLPATKAMPKEMLPVVDKPLIQYAVEEAVAAGITDLIFVTGRNKRAIEDHFDAAPEL
ETDLEAKGKHELLALVRDILPAHVNCLYIRQSAPLGLGHAVLTAAPAVGNEPFAVLLADDLIDADTPVLKQLIDVAVARQ
GSVLGVQEVPREDTRKYGIVASQPVDARTERVTHIVEKPAPEQAPTTLAVVGRYVLEAAIFDHLRATTVGAGNEIQLTDG
IAALLRERDVYAHRYDGKRYDCGSKAGMFQATVALGRKYHGLIPE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCINE  GLY 
3 GLYCEROL GOL 
4 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   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   VAL n 
1 10  VAL n 
1 11  ARG n 
1 12  LYS n 
1 13  ALA n 
1 14  VAL n 
1 15  PHE n 
1 16  PRO n 
1 17  VAL n 
1 18  ALA n 
1 19  GLY n 
1 20  MET n 
1 21  GLY n 
1 22  THR n 
1 23  ARG n 
1 24  PHE n 
1 25  LEU n 
1 26  PRO n 
1 27  ALA n 
1 28  THR n 
1 29  LYS n 
1 30  ALA n 
1 31  MET n 
1 32  PRO n 
1 33  LYS n 
1 34  GLU n 
1 35  MET n 
1 36  LEU n 
1 37  PRO n 
1 38  VAL n 
1 39  VAL n 
1 40  ASP n 
1 41  LYS n 
1 42  PRO n 
1 43  LEU n 
1 44  ILE n 
1 45  GLN n 
1 46  TYR n 
1 47  ALA n 
1 48  VAL n 
1 49  GLU n 
1 50  GLU n 
1 51  ALA n 
1 52  VAL n 
1 53  ALA n 
1 54  ALA n 
1 55  GLY n 
1 56  ILE n 
1 57  THR n 
1 58  ASP n 
1 59  LEU n 
1 60  ILE n 
1 61  PHE n 
1 62  VAL n 
1 63  THR n 
1 64  GLY n 
1 65  ARG n 
1 66  ASN n 
1 67  LYS n 
1 68  ARG n 
1 69  ALA n 
1 70  ILE n 
1 71  GLU n 
1 72  ASP n 
1 73  HIS n 
1 74  PHE n 
1 75  ASP n 
1 76  ALA n 
1 77  ALA n 
1 78  PRO n 
1 79  GLU n 
1 80  LEU n 
1 81  GLU n 
1 82  THR n 
1 83  ASP n 
1 84  LEU n 
1 85  GLU n 
1 86  ALA n 
1 87  LYS n 
1 88  GLY n 
1 89  LYS n 
1 90  HIS n 
1 91  GLU n 
1 92  LEU n 
1 93  LEU n 
1 94  ALA n 
1 95  LEU n 
1 96  VAL n 
1 97  ARG n 
1 98  ASP n 
1 99  ILE n 
1 100 LEU n 
1 101 PRO n 
1 102 ALA n 
1 103 HIS n 
1 104 VAL n 
1 105 ASN n 
1 106 CYS n 
1 107 LEU n 
1 108 TYR n 
1 109 ILE n 
1 110 ARG n 
1 111 GLN n 
1 112 SER n 
1 113 ALA n 
1 114 PRO n 
1 115 LEU n 
1 116 GLY n 
1 117 LEU n 
1 118 GLY n 
1 119 HIS n 
1 120 ALA n 
1 121 VAL n 
1 122 LEU n 
1 123 THR n 
1 124 ALA n 
1 125 ALA n 
1 126 PRO n 
1 127 ALA n 
1 128 VAL n 
1 129 GLY n 
1 130 ASN n 
1 131 GLU n 
1 132 PRO n 
1 133 PHE n 
1 134 ALA n 
1 135 VAL n 
1 136 LEU n 
1 137 LEU n 
1 138 ALA n 
1 139 ASP n 
1 140 ASP n 
1 141 LEU n 
1 142 ILE n 
1 143 ASP n 
1 144 ALA n 
1 145 ASP n 
1 146 THR n 
1 147 PRO n 
1 148 VAL n 
1 149 LEU n 
1 150 LYS n 
1 151 GLN n 
1 152 LEU n 
1 153 ILE n 
1 154 ASP n 
1 155 VAL n 
1 156 ALA n 
1 157 VAL n 
1 158 ALA n 
1 159 ARG n 
1 160 GLN n 
1 161 GLY n 
1 162 SER n 
1 163 VAL n 
1 164 LEU n 
1 165 GLY n 
1 166 VAL n 
1 167 GLN n 
1 168 GLU n 
1 169 VAL n 
1 170 PRO n 
1 171 ARG n 
1 172 GLU n 
1 173 ASP n 
1 174 THR n 
1 175 ARG n 
1 176 LYS n 
1 177 TYR n 
1 178 GLY n 
1 179 ILE n 
1 180 VAL n 
1 181 ALA n 
1 182 SER n 
1 183 GLN n 
1 184 PRO n 
1 185 VAL n 
1 186 ASP n 
1 187 ALA n 
1 188 ARG n 
1 189 THR n 
1 190 GLU n 
1 191 ARG n 
1 192 VAL n 
1 193 THR n 
1 194 HIS n 
1 195 ILE n 
1 196 VAL n 
1 197 GLU n 
1 198 LYS n 
1 199 PRO n 
1 200 ALA n 
1 201 PRO n 
1 202 GLU n 
1 203 GLN n 
1 204 ALA n 
1 205 PRO n 
1 206 THR n 
1 207 THR n 
1 208 LEU n 
1 209 ALA n 
1 210 VAL n 
1 211 VAL n 
1 212 GLY n 
1 213 ARG n 
1 214 TYR n 
1 215 VAL n 
1 216 LEU n 
1 217 GLU n 
1 218 ALA n 
1 219 ALA n 
1 220 ILE n 
1 221 PHE n 
1 222 ASP n 
1 223 HIS n 
1 224 LEU n 
1 225 ARG n 
1 226 ALA n 
1 227 THR n 
1 228 THR n 
1 229 VAL n 
1 230 GLY n 
1 231 ALA n 
1 232 GLY n 
1 233 ASN n 
1 234 GLU n 
1 235 ILE n 
1 236 GLN n 
1 237 LEU n 
1 238 THR n 
1 239 ASP n 
1 240 GLY n 
1 241 ILE n 
1 242 ALA n 
1 243 ALA n 
1 244 LEU n 
1 245 LEU n 
1 246 ARG n 
1 247 GLU n 
1 248 ARG n 
1 249 ASP n 
1 250 VAL n 
1 251 TYR n 
1 252 ALA n 
1 253 HIS n 
1 254 ARG n 
1 255 TYR n 
1 256 ASP n 
1 257 GLY n 
1 258 LYS n 
1 259 ARG n 
1 260 TYR n 
1 261 ASP n 
1 262 CYS n 
1 263 GLY n 
1 264 SER n 
1 265 LYS n 
1 266 ALA n 
1 267 GLY n 
1 268 MET n 
1 269 PHE n 
1 270 GLN n 
1 271 ALA n 
1 272 THR n 
1 273 VAL n 
1 274 ALA n 
1 275 LEU n 
1 276 GLY n 
1 277 ARG n 
1 278 LYS n 
1 279 TYR n 
1 280 HIS n 
1 281 GLY n 
1 282 LEU n 
1 283 ILE n 
1 284 PRO n 
1 285 GLU 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                   285 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 BP3403 
_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      'Bordetella pertussis Tohama I' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     257313 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       BopeA.00118.a.B2 
_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 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
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 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   18  ?   ?   ?   A . n 
A 1 2   ALA 2   19  ?   ?   ?   A . n 
A 1 3   HIS 3   20  ?   ?   ?   A . n 
A 1 4   HIS 4   21  ?   ?   ?   A . n 
A 1 5   HIS 5   22  ?   ?   ?   A . n 
A 1 6   HIS 6   23  ?   ?   ?   A . n 
A 1 7   HIS 7   24  ?   ?   ?   A . n 
A 1 8   HIS 8   25  2   HIS HIS A . n 
A 1 9   VAL 9   26  3   VAL VAL A . n 
A 1 10  VAL 10  27  4   VAL VAL A . n 
A 1 11  ARG 11  28  5   ARG ARG A . n 
A 1 12  LYS 12  29  6   LYS LYS A . n 
A 1 13  ALA 13  30  7   ALA ALA A . n 
A 1 14  VAL 14  31  8   VAL VAL A . n 
A 1 15  PHE 15  32  9   PHE PHE A . n 
A 1 16  PRO 16  33  10  PRO PRO A . n 
A 1 17  VAL 17  34  11  VAL VAL A . n 
A 1 18  ALA 18  35  12  ALA ALA A . n 
A 1 19  GLY 19  36  13  GLY GLY A . n 
A 1 20  MET 20  37  14  MET MET A . n 
A 1 21  GLY 21  38  15  GLY GLY A . n 
A 1 22  THR 22  39  16  THR THR A . n 
A 1 23  ARG 23  40  17  ARG ARG A . n 
A 1 24  PHE 24  41  18  PHE PHE A . n 
A 1 25  LEU 25  42  19  LEU LEU A . n 
A 1 26  PRO 26  43  20  PRO PRO A . n 
A 1 27  ALA 27  44  21  ALA ALA A . n 
A 1 28  THR 28  45  22  THR THR A . n 
A 1 29  LYS 29  46  23  LYS LYS A . n 
A 1 30  ALA 30  47  24  ALA ALA A . n 
A 1 31  MET 31  48  25  MET MET A . n 
A 1 32  PRO 32  49  26  PRO PRO A . n 
A 1 33  LYS 33  50  27  LYS LYS A . n 
A 1 34  GLU 34  51  28  GLU GLU A . n 
A 1 35  MET 35  52  29  MET MET A . n 
A 1 36  LEU 36  53  30  LEU LEU A . n 
A 1 37  PRO 37  54  31  PRO PRO A . n 
A 1 38  VAL 38  55  32  VAL VAL A . n 
A 1 39  VAL 39  56  33  VAL VAL A . n 
A 1 40  ASP 40  57  34  ASP ASP A . n 
A 1 41  LYS 41  58  35  LYS LYS A . n 
A 1 42  PRO 42  59  36  PRO PRO A . n 
A 1 43  LEU 43  60  37  LEU LEU A . n 
A 1 44  ILE 44  61  38  ILE ILE A . n 
A 1 45  GLN 45  62  39  GLN GLN A . n 
A 1 46  TYR 46  63  40  TYR TYR A . n 
A 1 47  ALA 47  64  41  ALA ALA A . n 
A 1 48  VAL 48  65  42  VAL VAL A . n 
A 1 49  GLU 49  66  43  GLU GLU A . n 
A 1 50  GLU 50  67  44  GLU GLU A . n 
A 1 51  ALA 51  68  45  ALA ALA A . n 
A 1 52  VAL 52  69  46  VAL VAL A . n 
A 1 53  ALA 53  70  47  ALA ALA A . n 
A 1 54  ALA 54  71  48  ALA ALA A . n 
A 1 55  GLY 55  72  49  GLY GLY A . n 
A 1 56  ILE 56  73  50  ILE ILE A . n 
A 1 57  THR 57  74  51  THR THR A . n 
A 1 58  ASP 58  75  52  ASP ASP A . n 
A 1 59  LEU 59  76  53  LEU LEU A . n 
A 1 60  ILE 60  77  54  ILE ILE A . n 
A 1 61  PHE 61  78  55  PHE PHE A . n 
A 1 62  VAL 62  79  56  VAL VAL A . n 
A 1 63  THR 63  80  57  THR THR A . n 
A 1 64  GLY 64  81  58  GLY GLY A . n 
A 1 65  ARG 65  82  59  ARG ARG A . n 
A 1 66  ASN 66  83  60  ASN ASN A . n 
A 1 67  LYS 67  84  61  LYS LYS A . n 
A 1 68  ARG 68  85  62  ARG ARG A . n 
A 1 69  ALA 69  86  63  ALA ALA A . n 
A 1 70  ILE 70  87  64  ILE ILE A . n 
A 1 71  GLU 71  88  65  GLU GLU A . n 
A 1 72  ASP 72  89  66  ASP ASP A . n 
A 1 73  HIS 73  90  67  HIS HIS A . n 
A 1 74  PHE 74  91  68  PHE PHE A . n 
A 1 75  ASP 75  92  69  ASP ASP A . n 
A 1 76  ALA 76  93  70  ALA ALA A . n 
A 1 77  ALA 77  94  71  ALA ALA A . n 
A 1 78  PRO 78  95  72  PRO PRO A . n 
A 1 79  GLU 79  96  73  GLU GLU A . n 
A 1 80  LEU 80  97  74  LEU LEU A . n 
A 1 81  GLU 81  98  75  GLU GLU A . n 
A 1 82  THR 82  99  76  THR THR A . n 
A 1 83  ASP 83  100 77  ASP ASP A . n 
A 1 84  LEU 84  101 78  LEU LEU A . n 
A 1 85  GLU 85  102 79  GLU GLU A . n 
A 1 86  ALA 86  103 80  ALA ALA A . n 
A 1 87  LYS 87  104 81  LYS LYS A . n 
A 1 88  GLY 88  105 82  GLY GLY A . n 
A 1 89  LYS 89  106 83  LYS LYS A . n 
A 1 90  HIS 90  107 84  HIS HIS A . n 
A 1 91  GLU 91  108 85  GLU GLU A . n 
A 1 92  LEU 92  109 86  LEU LEU A . n 
A 1 93  LEU 93  110 87  LEU LEU A . n 
A 1 94  ALA 94  111 88  ALA ALA A . n 
A 1 95  LEU 95  112 89  LEU LEU A . n 
A 1 96  VAL 96  113 90  VAL VAL A . n 
A 1 97  ARG 97  114 91  ARG ARG A . n 
A 1 98  ASP 98  115 92  ASP ASP A . n 
A 1 99  ILE 99  116 93  ILE ILE A . n 
A 1 100 LEU 100 117 94  LEU LEU A . n 
A 1 101 PRO 101 118 95  PRO PRO A . n 
A 1 102 ALA 102 119 96  ALA ALA A . n 
A 1 103 HIS 103 120 97  HIS HIS A . n 
A 1 104 VAL 104 121 98  VAL VAL A . n 
A 1 105 ASN 105 122 99  ASN ASN A . n 
A 1 106 CYS 106 123 100 CYS CYS A . n 
A 1 107 LEU 107 124 101 LEU LEU A . n 
A 1 108 TYR 108 125 102 TYR TYR A . n 
A 1 109 ILE 109 126 103 ILE ILE A . n 
A 1 110 ARG 110 127 104 ARG ARG A . n 
A 1 111 GLN 111 128 105 GLN GLN A . n 
A 1 112 SER 112 129 106 SER SER A . n 
A 1 113 ALA 113 130 107 ALA ALA A . n 
A 1 114 PRO 114 131 108 PRO PRO A . n 
A 1 115 LEU 115 132 109 LEU LEU A . n 
A 1 116 GLY 116 133 110 GLY GLY A . n 
A 1 117 LEU 117 134 111 LEU LEU A . n 
A 1 118 GLY 118 135 112 GLY GLY A . n 
A 1 119 HIS 119 136 113 HIS HIS A . n 
A 1 120 ALA 120 137 114 ALA ALA A . n 
A 1 121 VAL 121 138 115 VAL VAL A . n 
A 1 122 LEU 122 139 116 LEU LEU A . n 
A 1 123 THR 123 140 117 THR THR A . n 
A 1 124 ALA 124 141 118 ALA ALA A . n 
A 1 125 ALA 125 142 119 ALA ALA A . n 
A 1 126 PRO 126 143 120 PRO PRO A . n 
A 1 127 ALA 127 144 121 ALA ALA A . n 
A 1 128 VAL 128 145 122 VAL VAL A . n 
A 1 129 GLY 129 146 123 GLY GLY A . n 
A 1 130 ASN 130 147 124 ASN ASN A . n 
A 1 131 GLU 131 148 125 GLU GLU A . n 
A 1 132 PRO 132 149 126 PRO PRO A . n 
A 1 133 PHE 133 150 127 PHE PHE A . n 
A 1 134 ALA 134 151 128 ALA ALA A . n 
A 1 135 VAL 135 152 129 VAL VAL A . n 
A 1 136 LEU 136 153 130 LEU LEU A . n 
A 1 137 LEU 137 154 131 LEU LEU A . n 
A 1 138 ALA 138 155 132 ALA ALA A . n 
A 1 139 ASP 139 156 133 ASP ASP A . n 
A 1 140 ASP 140 157 134 ASP ASP A . n 
A 1 141 LEU 141 158 135 LEU LEU A . n 
A 1 142 ILE 142 159 136 ILE ILE A . n 
A 1 143 ASP 143 160 137 ASP ASP A . n 
A 1 144 ALA 144 161 138 ALA ALA A . n 
A 1 145 ASP 145 162 139 ASP ASP A . n 
A 1 146 THR 146 163 140 THR THR A . n 
A 1 147 PRO 147 164 141 PRO PRO A . n 
A 1 148 VAL 148 165 142 VAL VAL A . n 
A 1 149 LEU 149 166 143 LEU LEU A . n 
A 1 150 LYS 150 167 144 LYS LYS A . n 
A 1 151 GLN 151 168 145 GLN GLN A . n 
A 1 152 LEU 152 169 146 LEU LEU A . n 
A 1 153 ILE 153 170 147 ILE ILE A . n 
A 1 154 ASP 154 171 148 ASP ASP A . n 
A 1 155 VAL 155 172 149 VAL VAL A . n 
A 1 156 ALA 156 173 150 ALA ALA A . n 
A 1 157 VAL 157 174 151 VAL VAL A . n 
A 1 158 ALA 158 175 152 ALA ALA A . n 
A 1 159 ARG 159 176 153 ARG ARG A . n 
A 1 160 GLN 160 177 154 GLN GLN A . n 
A 1 161 GLY 161 178 155 GLY GLY A . n 
A 1 162 SER 162 179 156 SER SER A . n 
A 1 163 VAL 163 180 157 VAL VAL A . n 
A 1 164 LEU 164 181 158 LEU LEU A . n 
A 1 165 GLY 165 182 159 GLY GLY A . n 
A 1 166 VAL 166 183 160 VAL VAL A . n 
A 1 167 GLN 167 184 161 GLN GLN A . n 
A 1 168 GLU 168 185 162 GLU GLU A . n 
A 1 169 VAL 169 186 163 VAL VAL A . n 
A 1 170 PRO 170 187 164 PRO PRO A . n 
A 1 171 ARG 171 188 165 ARG ARG A . n 
A 1 172 GLU 172 189 166 GLU GLU A . n 
A 1 173 ASP 173 190 167 ASP ASP A . n 
A 1 174 THR 174 191 168 THR THR A . n 
A 1 175 ARG 175 192 169 ARG ARG A . n 
A 1 176 LYS 176 193 170 LYS LYS A . n 
A 1 177 TYR 177 194 171 TYR TYR A . n 
A 1 178 GLY 178 195 172 GLY GLY A . n 
A 1 179 ILE 179 196 173 ILE ILE A . n 
A 1 180 VAL 180 197 174 VAL VAL A . n 
A 1 181 ALA 181 198 175 ALA ALA A . n 
A 1 182 SER 182 199 176 SER SER A . n 
A 1 183 GLN 183 200 177 GLN GLN A . n 
A 1 184 PRO 184 201 178 PRO PRO A . n 
A 1 185 VAL 185 202 179 VAL VAL A . n 
A 1 186 ASP 186 203 180 ASP ASP A . n 
A 1 187 ALA 187 204 181 ALA ALA A . n 
A 1 188 ARG 188 205 182 ARG ARG A . n 
A 1 189 THR 189 206 183 THR THR A . n 
A 1 190 GLU 190 207 184 GLU GLU A . n 
A 1 191 ARG 191 208 185 ARG ARG A . n 
A 1 192 VAL 192 209 186 VAL VAL A . n 
A 1 193 THR 193 210 187 THR THR A . n 
A 1 194 HIS 194 211 188 HIS HIS A . n 
A 1 195 ILE 195 212 189 ILE ILE A . n 
A 1 196 VAL 196 213 190 VAL VAL A . n 
A 1 197 GLU 197 214 191 GLU GLU A . n 
A 1 198 LYS 198 215 192 LYS LYS A . n 
A 1 199 PRO 199 216 193 PRO PRO A . n 
A 1 200 ALA 200 217 194 ALA ALA A . n 
A 1 201 PRO 201 218 195 PRO PRO A . n 
A 1 202 GLU 202 219 196 GLU GLU A . n 
A 1 203 GLN 203 220 197 GLN GLN A . n 
A 1 204 ALA 204 221 198 ALA ALA A . n 
A 1 205 PRO 205 222 199 PRO PRO A . n 
A 1 206 THR 206 223 200 THR THR A . n 
A 1 207 THR 207 224 201 THR THR A . n 
A 1 208 LEU 208 225 202 LEU LEU A . n 
A 1 209 ALA 209 226 203 ALA ALA A . n 
A 1 210 VAL 210 227 204 VAL VAL A . n 
A 1 211 VAL 211 228 205 VAL VAL A . n 
A 1 212 GLY 212 229 206 GLY GLY A . n 
A 1 213 ARG 213 230 207 ARG ARG A . n 
A 1 214 TYR 214 231 208 TYR TYR A . n 
A 1 215 VAL 215 232 209 VAL VAL A . n 
A 1 216 LEU 216 233 210 LEU LEU A . n 
A 1 217 GLU 217 234 211 GLU GLU A . n 
A 1 218 ALA 218 235 212 ALA ALA A . n 
A 1 219 ALA 219 236 213 ALA ALA A . n 
A 1 220 ILE 220 237 214 ILE ILE A . n 
A 1 221 PHE 221 238 215 PHE PHE A . n 
A 1 222 ASP 222 239 216 ASP ASP A . n 
A 1 223 HIS 223 240 217 HIS HIS A . n 
A 1 224 LEU 224 241 218 LEU LEU A . n 
A 1 225 ARG 225 242 219 ARG ARG A . n 
A 1 226 ALA 226 243 220 ALA ALA A . n 
A 1 227 THR 227 244 221 THR THR A . n 
A 1 228 THR 228 245 222 THR THR A . n 
A 1 229 VAL 229 246 ?   ?   ?   A . n 
A 1 230 GLY 230 247 ?   ?   ?   A . n 
A 1 231 ALA 231 248 ?   ?   ?   A . n 
A 1 232 GLY 232 249 ?   ?   ?   A . n 
A 1 233 ASN 233 250 ?   ?   ?   A . n 
A 1 234 GLU 234 251 228 GLU GLU A . n 
A 1 235 ILE 235 252 229 ILE ILE A . n 
A 1 236 GLN 236 253 230 GLN GLN A . n 
A 1 237 LEU 237 254 231 LEU LEU A . n 
A 1 238 THR 238 255 232 THR THR A . n 
A 1 239 ASP 239 256 233 ASP ASP A . n 
A 1 240 GLY 240 257 234 GLY GLY A . n 
A 1 241 ILE 241 258 235 ILE ILE A . n 
A 1 242 ALA 242 259 236 ALA ALA A . n 
A 1 243 ALA 243 260 237 ALA ALA A . n 
A 1 244 LEU 244 261 238 LEU LEU A . n 
A 1 245 LEU 245 262 239 LEU LEU A . n 
A 1 246 ARG 246 263 240 ARG ARG A . n 
A 1 247 GLU 247 264 241 GLU GLU A . n 
A 1 248 ARG 248 265 242 ARG ARG A . n 
A 1 249 ASP 249 266 243 ASP ASP A . n 
A 1 250 VAL 250 267 244 VAL VAL A . n 
A 1 251 TYR 251 268 245 TYR TYR A . n 
A 1 252 ALA 252 269 246 ALA ALA A . n 
A 1 253 HIS 253 270 247 HIS HIS A . n 
A 1 254 ARG 254 271 248 ARG ARG A . n 
A 1 255 TYR 255 272 249 TYR TYR A . n 
A 1 256 ASP 256 273 250 ASP ASP A . n 
A 1 257 GLY 257 274 251 GLY GLY A . n 
A 1 258 LYS 258 275 252 LYS LYS A . n 
A 1 259 ARG 259 276 253 ARG ARG A . n 
A 1 260 TYR 260 277 254 TYR TYR A . n 
A 1 261 ASP 261 278 255 ASP ASP A . n 
A 1 262 CYS 262 279 256 CYS CYS A . n 
A 1 263 GLY 263 280 257 GLY GLY A . n 
A 1 264 SER 264 281 258 SER SER A . n 
A 1 265 LYS 265 282 259 LYS LYS A . n 
A 1 266 ALA 266 283 260 ALA ALA A . n 
A 1 267 GLY 267 284 261 GLY GLY A . n 
A 1 268 MET 268 285 262 MET MET A . n 
A 1 269 PHE 269 286 263 PHE PHE A . n 
A 1 270 GLN 270 287 264 GLN GLN A . n 
A 1 271 ALA 271 288 265 ALA ALA A . n 
A 1 272 THR 272 289 266 THR THR A . n 
A 1 273 VAL 273 290 267 VAL VAL A . n 
A 1 274 ALA 274 291 268 ALA ALA A . n 
A 1 275 LEU 275 292 269 LEU LEU A . n 
A 1 276 GLY 276 293 270 GLY GLY A . n 
A 1 277 ARG 277 294 271 ARG ARG A . n 
A 1 278 LYS 278 295 272 LYS LYS A . n 
A 1 279 TYR 279 296 273 TYR TYR A . n 
A 1 280 HIS 280 297 274 HIS HIS A . n 
A 1 281 GLY 281 298 275 GLY GLY A . n 
A 1 282 LEU 282 299 276 LEU LEU A . n 
A 1 283 ILE 283 300 277 ILE ILE A . n 
A 1 284 PRO 284 301 278 PRO PRO A . n 
A 1 285 GLU 285 302 279 GLU GLU A . n 
B 1 1   MET 1   18  ?   ?   ?   B . n 
B 1 2   ALA 2   19  ?   ?   ?   B . n 
B 1 3   HIS 3   20  ?   ?   ?   B . n 
B 1 4   HIS 4   21  ?   ?   ?   B . n 
B 1 5   HIS 5   22  ?   ?   ?   B . n 
B 1 6   HIS 6   23  ?   ?   ?   B . n 
B 1 7   HIS 7   24  1   HIS HIS B . n 
B 1 8   HIS 8   25  2   HIS HIS B . n 
B 1 9   VAL 9   26  3   VAL VAL B . n 
B 1 10  VAL 10  27  4   VAL VAL B . n 
B 1 11  ARG 11  28  5   ARG ARG B . n 
B 1 12  LYS 12  29  6   LYS LYS B . n 
B 1 13  ALA 13  30  7   ALA ALA B . n 
B 1 14  VAL 14  31  8   VAL VAL B . n 
B 1 15  PHE 15  32  9   PHE PHE B . n 
B 1 16  PRO 16  33  10  PRO PRO B . n 
B 1 17  VAL 17  34  11  VAL VAL B . n 
B 1 18  ALA 18  35  12  ALA ALA B . n 
B 1 19  GLY 19  36  13  GLY GLY B . n 
B 1 20  MET 20  37  14  MET MET B . n 
B 1 21  GLY 21  38  15  GLY GLY B . n 
B 1 22  THR 22  39  16  THR THR B . n 
B 1 23  ARG 23  40  17  ARG ARG B . n 
B 1 24  PHE 24  41  18  PHE PHE B . n 
B 1 25  LEU 25  42  19  LEU LEU B . n 
B 1 26  PRO 26  43  20  PRO PRO B . n 
B 1 27  ALA 27  44  21  ALA ALA B . n 
B 1 28  THR 28  45  22  THR THR B . n 
B 1 29  LYS 29  46  23  LYS LYS B . n 
B 1 30  ALA 30  47  24  ALA ALA B . n 
B 1 31  MET 31  48  25  MET MET B . n 
B 1 32  PRO 32  49  26  PRO PRO B . n 
B 1 33  LYS 33  50  27  LYS LYS B . n 
B 1 34  GLU 34  51  28  GLU GLU B . n 
B 1 35  MET 35  52  29  MET MET B . n 
B 1 36  LEU 36  53  30  LEU LEU B . n 
B 1 37  PRO 37  54  31  PRO PRO B . n 
B 1 38  VAL 38  55  32  VAL VAL B . n 
B 1 39  VAL 39  56  33  VAL VAL B . n 
B 1 40  ASP 40  57  34  ASP ASP B . n 
B 1 41  LYS 41  58  35  LYS LYS B . n 
B 1 42  PRO 42  59  36  PRO PRO B . n 
B 1 43  LEU 43  60  37  LEU LEU B . n 
B 1 44  ILE 44  61  38  ILE ILE B . n 
B 1 45  GLN 45  62  39  GLN GLN B . n 
B 1 46  TYR 46  63  40  TYR TYR B . n 
B 1 47  ALA 47  64  41  ALA ALA B . n 
B 1 48  VAL 48  65  42  VAL VAL B . n 
B 1 49  GLU 49  66  43  GLU GLU B . n 
B 1 50  GLU 50  67  44  GLU GLU B . n 
B 1 51  ALA 51  68  45  ALA ALA B . n 
B 1 52  VAL 52  69  46  VAL VAL B . n 
B 1 53  ALA 53  70  47  ALA ALA B . n 
B 1 54  ALA 54  71  48  ALA ALA B . n 
B 1 55  GLY 55  72  49  GLY GLY B . n 
B 1 56  ILE 56  73  50  ILE ILE B . n 
B 1 57  THR 57  74  51  THR THR B . n 
B 1 58  ASP 58  75  52  ASP ASP B . n 
B 1 59  LEU 59  76  53  LEU LEU B . n 
B 1 60  ILE 60  77  54  ILE ILE B . n 
B 1 61  PHE 61  78  55  PHE PHE B . n 
B 1 62  VAL 62  79  56  VAL VAL B . n 
B 1 63  THR 63  80  57  THR THR B . n 
B 1 64  GLY 64  81  58  GLY GLY B . n 
B 1 65  ARG 65  82  59  ARG ARG B . n 
B 1 66  ASN 66  83  60  ASN ASN B . n 
B 1 67  LYS 67  84  61  LYS LYS B . n 
B 1 68  ARG 68  85  62  ARG ARG B . n 
B 1 69  ALA 69  86  63  ALA ALA B . n 
B 1 70  ILE 70  87  64  ILE ILE B . n 
B 1 71  GLU 71  88  65  GLU GLU B . n 
B 1 72  ASP 72  89  66  ASP ASP B . n 
B 1 73  HIS 73  90  67  HIS HIS B . n 
B 1 74  PHE 74  91  68  PHE PHE B . n 
B 1 75  ASP 75  92  69  ASP ASP B . n 
B 1 76  ALA 76  93  70  ALA ALA B . n 
B 1 77  ALA 77  94  71  ALA ALA B . n 
B 1 78  PRO 78  95  72  PRO PRO B . n 
B 1 79  GLU 79  96  73  GLU GLU B . n 
B 1 80  LEU 80  97  74  LEU LEU B . n 
B 1 81  GLU 81  98  75  GLU GLU B . n 
B 1 82  THR 82  99  76  THR THR B . n 
B 1 83  ASP 83  100 77  ASP ASP B . n 
B 1 84  LEU 84  101 78  LEU LEU B . n 
B 1 85  GLU 85  102 79  GLU GLU B . n 
B 1 86  ALA 86  103 80  ALA ALA B . n 
B 1 87  LYS 87  104 81  LYS LYS B . n 
B 1 88  GLY 88  105 82  GLY GLY B . n 
B 1 89  LYS 89  106 83  LYS LYS B . n 
B 1 90  HIS 90  107 84  HIS HIS B . n 
B 1 91  GLU 91  108 85  GLU GLU B . n 
B 1 92  LEU 92  109 86  LEU LEU B . n 
B 1 93  LEU 93  110 87  LEU LEU B . n 
B 1 94  ALA 94  111 88  ALA ALA B . n 
B 1 95  LEU 95  112 89  LEU LEU B . n 
B 1 96  VAL 96  113 90  VAL VAL B . n 
B 1 97  ARG 97  114 91  ARG ARG B . n 
B 1 98  ASP 98  115 92  ASP ASP B . n 
B 1 99  ILE 99  116 93  ILE ILE B . n 
B 1 100 LEU 100 117 94  LEU LEU B . n 
B 1 101 PRO 101 118 95  PRO PRO B . n 
B 1 102 ALA 102 119 96  ALA ALA B . n 
B 1 103 HIS 103 120 97  HIS HIS B . n 
B 1 104 VAL 104 121 98  VAL VAL B . n 
B 1 105 ASN 105 122 99  ASN ASN B . n 
B 1 106 CYS 106 123 100 CYS CYS B . n 
B 1 107 LEU 107 124 101 LEU LEU B . n 
B 1 108 TYR 108 125 102 TYR TYR B . n 
B 1 109 ILE 109 126 103 ILE ILE B . n 
B 1 110 ARG 110 127 104 ARG ARG B . n 
B 1 111 GLN 111 128 105 GLN GLN B . n 
B 1 112 SER 112 129 106 SER SER B . n 
B 1 113 ALA 113 130 107 ALA ALA B . n 
B 1 114 PRO 114 131 108 PRO PRO B . n 
B 1 115 LEU 115 132 109 LEU LEU B . n 
B 1 116 GLY 116 133 110 GLY GLY B . n 
B 1 117 LEU 117 134 111 LEU LEU B . n 
B 1 118 GLY 118 135 112 GLY GLY B . n 
B 1 119 HIS 119 136 113 HIS HIS B . n 
B 1 120 ALA 120 137 114 ALA ALA B . n 
B 1 121 VAL 121 138 115 VAL VAL B . n 
B 1 122 LEU 122 139 116 LEU LEU B . n 
B 1 123 THR 123 140 117 THR THR B . n 
B 1 124 ALA 124 141 118 ALA ALA B . n 
B 1 125 ALA 125 142 119 ALA ALA B . n 
B 1 126 PRO 126 143 120 PRO PRO B . n 
B 1 127 ALA 127 144 121 ALA ALA B . n 
B 1 128 VAL 128 145 122 VAL VAL B . n 
B 1 129 GLY 129 146 123 GLY GLY B . n 
B 1 130 ASN 130 147 124 ASN ASN B . n 
B 1 131 GLU 131 148 125 GLU GLU B . n 
B 1 132 PRO 132 149 126 PRO PRO B . n 
B 1 133 PHE 133 150 127 PHE PHE B . n 
B 1 134 ALA 134 151 128 ALA ALA B . n 
B 1 135 VAL 135 152 129 VAL VAL B . n 
B 1 136 LEU 136 153 130 LEU LEU B . n 
B 1 137 LEU 137 154 131 LEU LEU B . n 
B 1 138 ALA 138 155 132 ALA ALA B . n 
B 1 139 ASP 139 156 133 ASP ASP B . n 
B 1 140 ASP 140 157 134 ASP ASP B . n 
B 1 141 LEU 141 158 135 LEU LEU B . n 
B 1 142 ILE 142 159 136 ILE ILE B . n 
B 1 143 ASP 143 160 137 ASP ASP B . n 
B 1 144 ALA 144 161 138 ALA ALA B . n 
B 1 145 ASP 145 162 139 ASP ASP B . n 
B 1 146 THR 146 163 140 THR THR B . n 
B 1 147 PRO 147 164 141 PRO PRO B . n 
B 1 148 VAL 148 165 142 VAL VAL B . n 
B 1 149 LEU 149 166 143 LEU LEU B . n 
B 1 150 LYS 150 167 144 LYS LYS B . n 
B 1 151 GLN 151 168 145 GLN GLN B . n 
B 1 152 LEU 152 169 146 LEU LEU B . n 
B 1 153 ILE 153 170 147 ILE ILE B . n 
B 1 154 ASP 154 171 148 ASP ASP B . n 
B 1 155 VAL 155 172 149 VAL VAL B . n 
B 1 156 ALA 156 173 150 ALA ALA B . n 
B 1 157 VAL 157 174 151 VAL VAL B . n 
B 1 158 ALA 158 175 152 ALA ALA B . n 
B 1 159 ARG 159 176 153 ARG ARG B . n 
B 1 160 GLN 160 177 154 GLN GLN B . n 
B 1 161 GLY 161 178 155 GLY GLY B . n 
B 1 162 SER 162 179 156 SER SER B . n 
B 1 163 VAL 163 180 157 VAL VAL B . n 
B 1 164 LEU 164 181 158 LEU LEU B . n 
B 1 165 GLY 165 182 159 GLY GLY B . n 
B 1 166 VAL 166 183 160 VAL VAL B . n 
B 1 167 GLN 167 184 161 GLN GLN B . n 
B 1 168 GLU 168 185 162 GLU GLU B . n 
B 1 169 VAL 169 186 163 VAL VAL B . n 
B 1 170 PRO 170 187 164 PRO PRO B . n 
B 1 171 ARG 171 188 165 ARG ARG B . n 
B 1 172 GLU 172 189 166 GLU GLU B . n 
B 1 173 ASP 173 190 167 ASP ASP B . n 
B 1 174 THR 174 191 168 THR THR B . n 
B 1 175 ARG 175 192 169 ARG ARG B . n 
B 1 176 LYS 176 193 170 LYS LYS B . n 
B 1 177 TYR 177 194 171 TYR TYR B . n 
B 1 178 GLY 178 195 172 GLY GLY B . n 
B 1 179 ILE 179 196 173 ILE ILE B . n 
B 1 180 VAL 180 197 174 VAL VAL B . n 
B 1 181 ALA 181 198 175 ALA ALA B . n 
B 1 182 SER 182 199 176 SER SER B . n 
B 1 183 GLN 183 200 177 GLN GLN B . n 
B 1 184 PRO 184 201 178 PRO PRO B . n 
B 1 185 VAL 185 202 179 VAL VAL B . n 
B 1 186 ASP 186 203 180 ASP ASP B . n 
B 1 187 ALA 187 204 181 ALA ALA B . n 
B 1 188 ARG 188 205 182 ARG ARG B . n 
B 1 189 THR 189 206 183 THR THR B . n 
B 1 190 GLU 190 207 184 GLU GLU B . n 
B 1 191 ARG 191 208 185 ARG ARG B . n 
B 1 192 VAL 192 209 186 VAL VAL B . n 
B 1 193 THR 193 210 187 THR THR B . n 
B 1 194 HIS 194 211 188 HIS HIS B . n 
B 1 195 ILE 195 212 189 ILE ILE B . n 
B 1 196 VAL 196 213 190 VAL VAL B . n 
B 1 197 GLU 197 214 191 GLU GLU B . n 
B 1 198 LYS 198 215 192 LYS LYS B . n 
B 1 199 PRO 199 216 193 PRO PRO B . n 
B 1 200 ALA 200 217 194 ALA ALA B . n 
B 1 201 PRO 201 218 195 PRO PRO B . n 
B 1 202 GLU 202 219 196 GLU GLU B . n 
B 1 203 GLN 203 220 197 GLN GLN B . n 
B 1 204 ALA 204 221 198 ALA ALA B . n 
B 1 205 PRO 205 222 199 PRO PRO B . n 
B 1 206 THR 206 223 200 THR THR B . n 
B 1 207 THR 207 224 201 THR THR B . n 
B 1 208 LEU 208 225 202 LEU LEU B . n 
B 1 209 ALA 209 226 203 ALA ALA B . n 
B 1 210 VAL 210 227 204 VAL VAL B . n 
B 1 211 VAL 211 228 205 VAL VAL B . n 
B 1 212 GLY 212 229 206 GLY GLY B . n 
B 1 213 ARG 213 230 207 ARG ARG B . n 
B 1 214 TYR 214 231 208 TYR TYR B . n 
B 1 215 VAL 215 232 209 VAL VAL B . n 
B 1 216 LEU 216 233 210 LEU LEU B . n 
B 1 217 GLU 217 234 211 GLU GLU B . n 
B 1 218 ALA 218 235 212 ALA ALA B . n 
B 1 219 ALA 219 236 213 ALA ALA B . n 
B 1 220 ILE 220 237 214 ILE ILE B . n 
B 1 221 PHE 221 238 215 PHE PHE B . n 
B 1 222 ASP 222 239 216 ASP ASP B . n 
B 1 223 HIS 223 240 217 HIS HIS B . n 
B 1 224 LEU 224 241 218 LEU LEU B . n 
B 1 225 ARG 225 242 219 ARG ARG B . n 
B 1 226 ALA 226 243 220 ALA ALA B . n 
B 1 227 THR 227 244 221 THR THR B . n 
B 1 228 THR 228 245 ?   ?   ?   B . n 
B 1 229 VAL 229 246 ?   ?   ?   B . n 
B 1 230 GLY 230 247 ?   ?   ?   B . n 
B 1 231 ALA 231 248 ?   ?   ?   B . n 
B 1 232 GLY 232 249 ?   ?   ?   B . n 
B 1 233 ASN 233 250 ?   ?   ?   B . n 
B 1 234 GLU 234 251 228 GLU GLU B . n 
B 1 235 ILE 235 252 229 ILE ILE B . n 
B 1 236 GLN 236 253 230 GLN GLN B . n 
B 1 237 LEU 237 254 231 LEU LEU B . n 
B 1 238 THR 238 255 232 THR THR B . n 
B 1 239 ASP 239 256 233 ASP ASP B . n 
B 1 240 GLY 240 257 234 GLY GLY B . n 
B 1 241 ILE 241 258 235 ILE ILE B . n 
B 1 242 ALA 242 259 236 ALA ALA B . n 
B 1 243 ALA 243 260 237 ALA ALA B . n 
B 1 244 LEU 244 261 238 LEU LEU B . n 
B 1 245 LEU 245 262 239 LEU LEU B . n 
B 1 246 ARG 246 263 240 ARG ARG B . n 
B 1 247 GLU 247 264 241 GLU GLU B . n 
B 1 248 ARG 248 265 242 ARG ARG B . n 
B 1 249 ASP 249 266 243 ASP ASP B . n 
B 1 250 VAL 250 267 244 VAL VAL B . n 
B 1 251 TYR 251 268 245 TYR TYR B . n 
B 1 252 ALA 252 269 246 ALA ALA B . n 
B 1 253 HIS 253 270 247 HIS HIS B . n 
B 1 254 ARG 254 271 248 ARG ARG B . n 
B 1 255 TYR 255 272 249 TYR TYR B . n 
B 1 256 ASP 256 273 250 ASP ASP B . n 
B 1 257 GLY 257 274 251 GLY GLY B . n 
B 1 258 LYS 258 275 252 LYS LYS B . n 
B 1 259 ARG 259 276 253 ARG ARG B . n 
B 1 260 TYR 260 277 254 TYR TYR B . n 
B 1 261 ASP 261 278 255 ASP ASP B . n 
B 1 262 CYS 262 279 256 CYS CYS B . n 
B 1 263 GLY 263 280 257 GLY GLY B . n 
B 1 264 SER 264 281 258 SER SER B . n 
B 1 265 LYS 265 282 259 LYS LYS B . n 
B 1 266 ALA 266 283 260 ALA ALA B . n 
B 1 267 GLY 267 284 261 GLY GLY B . n 
B 1 268 MET 268 285 262 MET MET B . n 
B 1 269 PHE 269 286 263 PHE PHE B . n 
B 1 270 GLN 270 287 264 GLN GLN B . n 
B 1 271 ALA 271 288 265 ALA ALA B . n 
B 1 272 THR 272 289 266 THR THR B . n 
B 1 273 VAL 273 290 267 VAL VAL B . n 
B 1 274 ALA 274 291 268 ALA ALA B . n 
B 1 275 LEU 275 292 269 LEU LEU B . n 
B 1 276 GLY 276 293 270 GLY GLY B . n 
B 1 277 ARG 277 294 271 ARG ARG B . n 
B 1 278 LYS 278 295 272 LYS LYS B . n 
B 1 279 TYR 279 296 273 TYR TYR B . n 
B 1 280 HIS 280 297 274 HIS HIS B . n 
B 1 281 GLY 281 298 275 GLY GLY B . n 
B 1 282 LEU 282 299 276 LEU LEU B . n 
B 1 283 ILE 283 300 277 ILE ILE B . n 
B 1 284 PRO 284 301 278 PRO PRO B . n 
B 1 285 GLU 285 302 279 GLU GLU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 GLY 1   401 1   GLY GLY A . 
D 2 GLY 1   402 3   GLY GLY A . 
E 3 GOL 1   403 101 GOL GOL A . 
F 3 GOL 1   404 102 GOL GOL A . 
G 2 GLY 1   401 2   GLY GLY B . 
H 2 GLY 1   402 4   GLY GLY B . 
I 3 GOL 1   403 103 GOL GOL B . 
J 4 HOH 1   501 261 HOH HOH A . 
J 4 HOH 2   502 238 HOH HOH A . 
J 4 HOH 3   503 246 HOH HOH A . 
J 4 HOH 4   504 269 HOH HOH A . 
J 4 HOH 5   505 257 HOH HOH A . 
J 4 HOH 6   506 259 HOH HOH A . 
J 4 HOH 7   507 245 HOH HOH A . 
J 4 HOH 8   508 164 HOH HOH A . 
J 4 HOH 9   509 152 HOH HOH A . 
J 4 HOH 10  510 134 HOH HOH A . 
J 4 HOH 11  511 254 HOH HOH A . 
J 4 HOH 12  512 270 HOH HOH A . 
J 4 HOH 13  513 168 HOH HOH A . 
J 4 HOH 14  514 144 HOH HOH A . 
J 4 HOH 15  515 229 HOH HOH A . 
J 4 HOH 16  516 34  HOH HOH A . 
J 4 HOH 17  517 111 HOH HOH A . 
J 4 HOH 18  518 156 HOH HOH A . 
J 4 HOH 19  519 279 HOH HOH A . 
J 4 HOH 20  520 75  HOH HOH A . 
J 4 HOH 21  521 163 HOH HOH A . 
J 4 HOH 22  522 20  HOH HOH A . 
J 4 HOH 23  523 44  HOH HOH A . 
J 4 HOH 24  524 102 HOH HOH A . 
J 4 HOH 25  525 91  HOH HOH A . 
J 4 HOH 26  526 166 HOH HOH A . 
J 4 HOH 27  527 242 HOH HOH A . 
J 4 HOH 28  528 201 HOH HOH A . 
J 4 HOH 29  529 265 HOH HOH A . 
J 4 HOH 30  530 178 HOH HOH A . 
J 4 HOH 31  531 236 HOH HOH A . 
J 4 HOH 32  532 274 HOH HOH A . 
J 4 HOH 33  533 27  HOH HOH A . 
J 4 HOH 34  534 33  HOH HOH A . 
J 4 HOH 35  535 150 HOH HOH A . 
J 4 HOH 36  536 127 HOH HOH A . 
J 4 HOH 37  537 58  HOH HOH A . 
J 4 HOH 38  538 239 HOH HOH A . 
J 4 HOH 39  539 22  HOH HOH A . 
J 4 HOH 40  540 45  HOH HOH A . 
J 4 HOH 41  541 170 HOH HOH A . 
J 4 HOH 42  542 141 HOH HOH A . 
J 4 HOH 43  543 240 HOH HOH A . 
J 4 HOH 44  544 180 HOH HOH A . 
J 4 HOH 45  545 199 HOH HOH A . 
J 4 HOH 46  546 130 HOH HOH A . 
J 4 HOH 47  547 81  HOH HOH A . 
J 4 HOH 48  548 182 HOH HOH A . 
J 4 HOH 49  549 28  HOH HOH A . 
J 4 HOH 50  550 23  HOH HOH A . 
J 4 HOH 51  551 63  HOH HOH A . 
J 4 HOH 52  552 51  HOH HOH A . 
J 4 HOH 53  553 42  HOH HOH A . 
J 4 HOH 54  554 228 HOH HOH A . 
J 4 HOH 55  555 121 HOH HOH A . 
J 4 HOH 56  556 32  HOH HOH A . 
J 4 HOH 57  557 250 HOH HOH A . 
J 4 HOH 58  558 15  HOH HOH A . 
J 4 HOH 59  559 30  HOH HOH A . 
J 4 HOH 60  560 214 HOH HOH A . 
J 4 HOH 61  561 161 HOH HOH A . 
J 4 HOH 62  562 212 HOH HOH A . 
J 4 HOH 63  563 53  HOH HOH A . 
J 4 HOH 64  564 17  HOH HOH A . 
J 4 HOH 65  565 103 HOH HOH A . 
J 4 HOH 66  566 232 HOH HOH A . 
J 4 HOH 67  567 69  HOH HOH A . 
J 4 HOH 68  568 6   HOH HOH A . 
J 4 HOH 69  569 122 HOH HOH A . 
J 4 HOH 70  570 92  HOH HOH A . 
J 4 HOH 71  571 49  HOH HOH A . 
J 4 HOH 72  572 105 HOH HOH A . 
J 4 HOH 73  573 253 HOH HOH A . 
J 4 HOH 74  574 2   HOH HOH A . 
J 4 HOH 75  575 114 HOH HOH A . 
J 4 HOH 76  576 140 HOH HOH A . 
J 4 HOH 77  577 217 HOH HOH A . 
J 4 HOH 78  578 248 HOH HOH A . 
J 4 HOH 79  579 196 HOH HOH A . 
J 4 HOH 80  580 209 HOH HOH A . 
J 4 HOH 81  581 21  HOH HOH A . 
J 4 HOH 82  582 128 HOH HOH A . 
J 4 HOH 83  583 40  HOH HOH A . 
J 4 HOH 84  584 72  HOH HOH A . 
J 4 HOH 85  585 98  HOH HOH A . 
J 4 HOH 86  586 107 HOH HOH A . 
J 4 HOH 87  587 26  HOH HOH A . 
J 4 HOH 88  588 129 HOH HOH A . 
J 4 HOH 89  589 256 HOH HOH A . 
J 4 HOH 90  590 280 HOH HOH A . 
J 4 HOH 91  591 37  HOH HOH A . 
J 4 HOH 92  592 48  HOH HOH A . 
J 4 HOH 93  593 263 HOH HOH A . 
J 4 HOH 94  594 16  HOH HOH A . 
J 4 HOH 95  595 187 HOH HOH A . 
J 4 HOH 96  596 109 HOH HOH A . 
J 4 HOH 97  597 221 HOH HOH A . 
J 4 HOH 98  598 185 HOH HOH A . 
J 4 HOH 99  599 25  HOH HOH A . 
J 4 HOH 100 600 148 HOH HOH A . 
J 4 HOH 101 601 131 HOH HOH A . 
J 4 HOH 102 602 258 HOH HOH A . 
J 4 HOH 103 603 78  HOH HOH A . 
J 4 HOH 104 604 86  HOH HOH A . 
J 4 HOH 105 605 186 HOH HOH A . 
J 4 HOH 106 606 200 HOH HOH A . 
J 4 HOH 107 607 216 HOH HOH A . 
J 4 HOH 108 608 268 HOH HOH A . 
J 4 HOH 109 609 89  HOH HOH A . 
J 4 HOH 110 610 116 HOH HOH A . 
J 4 HOH 111 611 10  HOH HOH A . 
J 4 HOH 112 612 251 HOH HOH A . 
J 4 HOH 113 613 64  HOH HOH A . 
J 4 HOH 114 614 194 HOH HOH A . 
J 4 HOH 115 615 223 HOH HOH A . 
J 4 HOH 116 616 183 HOH HOH A . 
J 4 HOH 117 617 99  HOH HOH A . 
J 4 HOH 118 618 112 HOH HOH A . 
J 4 HOH 119 619 219 HOH HOH A . 
J 4 HOH 120 620 158 HOH HOH A . 
J 4 HOH 121 621 260 HOH HOH A . 
J 4 HOH 122 622 73  HOH HOH A . 
J 4 HOH 123 623 3   HOH HOH A . 
J 4 HOH 124 624 113 HOH HOH A . 
J 4 HOH 125 625 272 HOH HOH A . 
J 4 HOH 126 626 208 HOH HOH A . 
J 4 HOH 127 627 264 HOH HOH A . 
J 4 HOH 128 628 213 HOH HOH A . 
J 4 HOH 129 629 95  HOH HOH A . 
J 4 HOH 130 630 120 HOH HOH A . 
J 4 HOH 131 631 39  HOH HOH A . 
J 4 HOH 132 632 267 HOH HOH A . 
J 4 HOH 133 633 97  HOH HOH A . 
J 4 HOH 134 634 126 HOH HOH A . 
J 4 HOH 135 635 192 HOH HOH A . 
J 4 HOH 136 636 165 HOH HOH A . 
J 4 HOH 137 637 271 HOH HOH A . 
J 4 HOH 138 638 202 HOH HOH A . 
J 4 HOH 139 639 171 HOH HOH A . 
J 4 HOH 140 640 210 HOH HOH A . 
J 4 HOH 141 641 234 HOH HOH A . 
J 4 HOH 142 642 50  HOH HOH A . 
J 4 HOH 143 643 184 HOH HOH A . 
J 4 HOH 144 644 190 HOH HOH A . 
J 4 HOH 145 645 172 HOH HOH A . 
J 4 HOH 146 646 100 HOH HOH A . 
J 4 HOH 147 647 139 HOH HOH A . 
J 4 HOH 148 648 169 HOH HOH A . 
J 4 HOH 149 649 154 HOH HOH A . 
K 4 HOH 1   501 230 HOH HOH B . 
K 4 HOH 2   502 133 HOH HOH B . 
K 4 HOH 3   503 12  HOH HOH B . 
K 4 HOH 4   504 115 HOH HOH B . 
K 4 HOH 5   505 136 HOH HOH B . 
K 4 HOH 6   506 205 HOH HOH B . 
K 4 HOH 7   507 46  HOH HOH B . 
K 4 HOH 8   508 188 HOH HOH B . 
K 4 HOH 9   509 62  HOH HOH B . 
K 4 HOH 10  510 118 HOH HOH B . 
K 4 HOH 11  511 193 HOH HOH B . 
K 4 HOH 12  512 123 HOH HOH B . 
K 4 HOH 13  513 207 HOH HOH B . 
K 4 HOH 14  514 244 HOH HOH B . 
K 4 HOH 15  515 11  HOH HOH B . 
K 4 HOH 16  516 19  HOH HOH B . 
K 4 HOH 17  517 94  HOH HOH B . 
K 4 HOH 18  518 84  HOH HOH B . 
K 4 HOH 19  519 57  HOH HOH B . 
K 4 HOH 20  520 203 HOH HOH B . 
K 4 HOH 21  521 61  HOH HOH B . 
K 4 HOH 22  522 162 HOH HOH B . 
K 4 HOH 23  523 173 HOH HOH B . 
K 4 HOH 24  524 198 HOH HOH B . 
K 4 HOH 25  525 79  HOH HOH B . 
K 4 HOH 26  526 4   HOH HOH B . 
K 4 HOH 27  527 278 HOH HOH B . 
K 4 HOH 28  528 52  HOH HOH B . 
K 4 HOH 29  529 88  HOH HOH B . 
K 4 HOH 30  530 204 HOH HOH B . 
K 4 HOH 31  531 56  HOH HOH B . 
K 4 HOH 32  532 125 HOH HOH B . 
K 4 HOH 33  533 252 HOH HOH B . 
K 4 HOH 34  534 70  HOH HOH B . 
K 4 HOH 35  535 215 HOH HOH B . 
K 4 HOH 36  536 59  HOH HOH B . 
K 4 HOH 37  537 237 HOH HOH B . 
K 4 HOH 38  538 55  HOH HOH B . 
K 4 HOH 39  539 117 HOH HOH B . 
K 4 HOH 40  540 262 HOH HOH B . 
K 4 HOH 41  541 108 HOH HOH B . 
K 4 HOH 42  542 243 HOH HOH B . 
K 4 HOH 43  543 241 HOH HOH B . 
K 4 HOH 44  544 167 HOH HOH B . 
K 4 HOH 45  545 160 HOH HOH B . 
K 4 HOH 46  546 82  HOH HOH B . 
K 4 HOH 47  547 177 HOH HOH B . 
K 4 HOH 48  548 155 HOH HOH B . 
K 4 HOH 49  549 159 HOH HOH B . 
K 4 HOH 50  550 67  HOH HOH B . 
K 4 HOH 51  551 218 HOH HOH B . 
K 4 HOH 52  552 13  HOH HOH B . 
K 4 HOH 53  553 153 HOH HOH B . 
K 4 HOH 54  554 35  HOH HOH B . 
K 4 HOH 55  555 142 HOH HOH B . 
K 4 HOH 56  556 143 HOH HOH B . 
K 4 HOH 57  557 80  HOH HOH B . 
K 4 HOH 58  558 54  HOH HOH B . 
K 4 HOH 59  559 43  HOH HOH B . 
K 4 HOH 60  560 149 HOH HOH B . 
K 4 HOH 61  561 275 HOH HOH B . 
K 4 HOH 62  562 255 HOH HOH B . 
K 4 HOH 63  563 29  HOH HOH B . 
K 4 HOH 64  564 195 HOH HOH B . 
K 4 HOH 65  565 206 HOH HOH B . 
K 4 HOH 66  566 8   HOH HOH B . 
K 4 HOH 67  567 96  HOH HOH B . 
K 4 HOH 68  568 106 HOH HOH B . 
K 4 HOH 69  569 226 HOH HOH B . 
K 4 HOH 70  570 277 HOH HOH B . 
K 4 HOH 71  571 71  HOH HOH B . 
K 4 HOH 72  572 85  HOH HOH B . 
K 4 HOH 73  573 224 HOH HOH B . 
K 4 HOH 74  574 14  HOH HOH B . 
K 4 HOH 75  575 176 HOH HOH B . 
K 4 HOH 76  576 77  HOH HOH B . 
K 4 HOH 77  577 132 HOH HOH B . 
K 4 HOH 78  578 101 HOH HOH B . 
K 4 HOH 79  579 233 HOH HOH B . 
K 4 HOH 80  580 225 HOH HOH B . 
K 4 HOH 81  581 68  HOH HOH B . 
K 4 HOH 82  582 47  HOH HOH B . 
K 4 HOH 83  583 276 HOH HOH B . 
K 4 HOH 84  584 5   HOH HOH B . 
K 4 HOH 85  585 38  HOH HOH B . 
K 4 HOH 86  586 36  HOH HOH B . 
K 4 HOH 87  587 235 HOH HOH B . 
K 4 HOH 88  588 90  HOH HOH B . 
K 4 HOH 89  589 7   HOH HOH B . 
K 4 HOH 90  590 222 HOH HOH B . 
K 4 HOH 91  591 31  HOH HOH B . 
K 4 HOH 92  592 9   HOH HOH B . 
K 4 HOH 93  593 175 HOH HOH B . 
K 4 HOH 94  594 211 HOH HOH B . 
K 4 HOH 95  595 104 HOH HOH B . 
K 4 HOH 96  596 24  HOH HOH B . 
K 4 HOH 97  597 138 HOH HOH B . 
K 4 HOH 98  598 93  HOH HOH B . 
K 4 HOH 99  599 147 HOH HOH B . 
K 4 HOH 100 600 124 HOH HOH B . 
K 4 HOH 101 601 60  HOH HOH B . 
K 4 HOH 102 602 247 HOH HOH B . 
K 4 HOH 103 603 65  HOH HOH B . 
K 4 HOH 104 604 41  HOH HOH B . 
K 4 HOH 105 605 273 HOH HOH B . 
K 4 HOH 106 606 227 HOH HOH B . 
K 4 HOH 107 607 249 HOH HOH B . 
K 4 HOH 108 608 119 HOH HOH B . 
K 4 HOH 109 609 66  HOH HOH B . 
K 4 HOH 110 610 76  HOH HOH B . 
K 4 HOH 111 611 74  HOH HOH B . 
K 4 HOH 112 612 181 HOH HOH B . 
K 4 HOH 113 613 151 HOH HOH B . 
K 4 HOH 114 614 1   HOH HOH B . 
K 4 HOH 115 615 137 HOH HOH B . 
K 4 HOH 116 616 157 HOH HOH B . 
K 4 HOH 117 617 189 HOH HOH B . 
K 4 HOH 118 618 179 HOH HOH B . 
K 4 HOH 119 619 87  HOH HOH B . 
K 4 HOH 120 620 174 HOH HOH B . 
K 4 HOH 121 621 191 HOH HOH B . 
K 4 HOH 122 622 231 HOH HOH B . 
K 4 HOH 123 623 83  HOH HOH B . 
K 4 HOH 124 624 266 HOH HOH B . 
K 4 HOH 125 625 135 HOH HOH B . 
K 4 HOH 126 626 110 HOH HOH B . 
K 4 HOH 127 627 145 HOH HOH B . 
K 4 HOH 128 628 18  HOH HOH B . 
K 4 HOH 129 629 220 HOH HOH B . 
K 4 HOH 130 630 197 HOH HOH B . 
K 4 HOH 131 631 146 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A THR 245 ? OG1 ? A THR 228 OG1 
2 1 Y 1 A THR 245 ? CG2 ? A THR 228 CG2 
3 1 Y 1 B HIS 24  ? CG  ? B HIS 7   CG  
4 1 Y 1 B HIS 24  ? ND1 ? B HIS 7   ND1 
5 1 Y 1 B HIS 24  ? CD2 ? B HIS 7   CD2 
6 1 Y 1 B HIS 24  ? CE1 ? B HIS 7   CE1 
7 1 Y 1 B HIS 24  ? NE2 ? B HIS 7   NE2 
8 1 Y 1 B THR 244 ? OG1 ? B THR 227 OG1 
9 1 Y 1 B THR 244 ? CG2 ? B THR 227 CG2 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.21rc1_5156 ? 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .            ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .            ? 3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .            ? 4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .            ? 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.80 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9O90 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     115.848 
_cell.length_a_esd                 ? 
_cell.length_b                     94.336 
_cell.length_b_esd                 ? 
_cell.length_c                     80.541 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9O90 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9O90 
_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             3.34 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.18 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Morpheus H5: 20% PEG 550 MME, 10% PEG 20K, 0.1M HEPES/MOPS, pH 7.5, 20mM each of DL-Alanine, Glycine, DL-Lysine, DL-Serine, DL-Glutamic acid. BopeA.00118.a.B2.PW39372 at 25.3 mg/mL. plate 19783 H5 drop 1, Puck: PSL-1103, Cryo: direct.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2025-03-15 
_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                    'Double Crystal Si 111' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9786 
_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                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9786 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9O90 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.93 
_reflns.d_resolution_low                               47.17 
_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                                     61154 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.04 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.198 
_reflns.pdbx_Rpim_I_all                                0.076 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       417462 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.183 
_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                                    1.93 
_reflns_shell.d_res_low                                     1.98 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           31316 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4464 
_reflns_shell.percent_possible_obs                          99.9 
_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                               7.0 
_reflns_shell.pdbx_chi_squared                              0.92 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.426 
_reflns_shell.pdbx_Rpim_I_all                               0.535 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.524 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.321 
_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                                 9O90 
_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                            1.93 
_refine.ls_d_res_low                             47.17 
_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                     61137 
_refine.ls_number_reflns_R_free                  2994 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.85 
_refine.ls_percent_reflns_R_free                 4.90 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1858 
_refine.ls_R_factor_R_free                       0.2148 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1843 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.35 
_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             1.10 
_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                 23.20 
_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                            0.21 
_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                       1.93 
_refine_hist.d_res_low                        47.17 
_refine_hist.number_atoms_solvent             280 
_refine_hist.number_atoms_total               4492 
_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        4174 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  ? 4312 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 1.042  ? 5862 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 11.892 ? 1607 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.057  ? 687  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.016  ? 769  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 1.93 1.96  . . 146 2765 100.00 . . . . 0.2989 . . . . . . . . . . . . . . . 0.3100 
'X-RAY DIFFRACTION' 1.96 2.00  . . 125 2754 100.00 . . . . 0.2957 . . . . . . . . . . . . . . . 0.3070 
'X-RAY DIFFRACTION' 2.00 2.03  . . 135 2750 100.00 . . . . 0.2752 . . . . . . . . . . . . . . . 0.3253 
'X-RAY DIFFRACTION' 2.03 2.07  . . 132 2800 100.00 . . . . 0.2663 . . . . . . . . . . . . . . . 0.3114 
'X-RAY DIFFRACTION' 2.07 2.11  . . 153 2726 100.00 . . . . 0.2467 . . . . . . . . . . . . . . . 0.2821 
'X-RAY DIFFRACTION' 2.11 2.16  . . 135 2754 100.00 . . . . 0.2338 . . . . . . . . . . . . . . . 0.2702 
'X-RAY DIFFRACTION' 2.16 2.21  . . 136 2790 100.00 . . . . 0.2160 . . . . . . . . . . . . . . . 0.2467 
'X-RAY DIFFRACTION' 2.21 2.26  . . 150 2735 100.00 . . . . 0.2077 . . . . . . . . . . . . . . . 0.2774 
'X-RAY DIFFRACTION' 2.26 2.33  . . 137 2758 100.00 . . . . 0.2001 . . . . . . . . . . . . . . . 0.2406 
'X-RAY DIFFRACTION' 2.33 2.39  . . 166 2742 100.00 . . . . 0.1847 . . . . . . . . . . . . . . . 0.2438 
'X-RAY DIFFRACTION' 2.39 2.47  . . 151 2765 100.00 . . . . 0.1835 . . . . . . . . . . . . . . . 0.2304 
'X-RAY DIFFRACTION' 2.47 2.56  . . 141 2771 100.00 . . . . 0.1871 . . . . . . . . . . . . . . . 0.2504 
'X-RAY DIFFRACTION' 2.56 2.66  . . 128 2778 100.00 . . . . 0.1909 . . . . . . . . . . . . . . . 0.2509 
'X-RAY DIFFRACTION' 2.66 2.78  . . 147 2774 100.00 . . . . 0.1989 . . . . . . . . . . . . . . . 0.2507 
'X-RAY DIFFRACTION' 2.78 2.93  . . 139 2764 100.00 . . . . 0.1825 . . . . . . . . . . . . . . . 0.1959 
'X-RAY DIFFRACTION' 2.93 3.11  . . 164 2777 100.00 . . . . 0.1899 . . . . . . . . . . . . . . . 0.2111 
'X-RAY DIFFRACTION' 3.11 3.35  . . 119 2783 100.00 . . . . 0.1917 . . . . . . . . . . . . . . . 0.2150 
'X-RAY DIFFRACTION' 3.35 3.69  . . 140 2758 100.00 . . . . 0.1676 . . . . . . . . . . . . . . . 0.1978 
'X-RAY DIFFRACTION' 3.69 4.23  . . 146 2779 100.00 . . . . 0.1540 . . . . . . . . . . . . . . . 0.1593 
'X-RAY DIFFRACTION' 4.23 5.32  . . 149 2793 99.00  . . . . 0.1359 . . . . . . . . . . . . . . . 0.1618 
'X-RAY DIFFRACTION' 5.32 47.17 . . 155 2827 100.00 . . . . 0.1690 . . . . . . . . . . . . . . . 0.2020 
# 
_struct.entry_id                     9O90 
_struct.title                        'Crystal structure of UTP--glucose-1-phosphate uridylyltransferase from Bordetella pertussis' 
_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        9O90 
_struct_keywords.text            
'SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, TRANSFERASE, Bordetella pertussis' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q7VTV0_BORPE 
_struct_ref.pdbx_db_accession          Q7VTV0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VVRKAVFPVAGMGTRFLPATKAMPKEMLPVVDKPLIQYAVEEAVAAGITDLIFVTGRNKRAIEDHFDAAPELETDLEAKG
KHELLALVRDILPAHVNCLYIRQSAPLGLGHAVLTAAPAVGNEPFAVLLADDLIDADTPVLKQLIDVAVARQGSVLGVQE
VPREDTRKYGIVASQPVDARTERVTHIVEKPAPEQAPTTLAVVGRYVLEAAIFDHLRATTVGAGNEIQLTDGIAALLRER
DVYAHRYDGKRYDCGSKAGMFQATVALGRKYHGLIPE
;
_struct_ref.pdbx_align_begin           26 
# 
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 9O90 A 9 ? 285 ? Q7VTV0 26 ? 302 ? 26 302 
2 1 9O90 B 9 ? 285 ? Q7VTV0 26 ? 302 ? 26 302 
# 
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 9O90 MET A 1 ? UNP Q7VTV0 ? ? 'initiating methionine' 18 1  
1 9O90 ALA A 2 ? UNP Q7VTV0 ? ? 'expression tag'        19 2  
1 9O90 HIS A 3 ? UNP Q7VTV0 ? ? 'expression tag'        20 3  
1 9O90 HIS A 4 ? UNP Q7VTV0 ? ? 'expression tag'        21 4  
1 9O90 HIS A 5 ? UNP Q7VTV0 ? ? 'expression tag'        22 5  
1 9O90 HIS A 6 ? UNP Q7VTV0 ? ? 'expression tag'        23 6  
1 9O90 HIS A 7 ? UNP Q7VTV0 ? ? 'expression tag'        24 7  
1 9O90 HIS A 8 ? UNP Q7VTV0 ? ? 'expression tag'        25 8  
2 9O90 MET B 1 ? UNP Q7VTV0 ? ? 'initiating methionine' 18 9  
2 9O90 ALA B 2 ? UNP Q7VTV0 ? ? 'expression tag'        19 10 
2 9O90 HIS B 3 ? UNP Q7VTV0 ? ? 'expression tag'        20 11 
2 9O90 HIS B 4 ? UNP Q7VTV0 ? ? 'expression tag'        21 12 
2 9O90 HIS B 5 ? UNP Q7VTV0 ? ? 'expression tag'        22 13 
2 9O90 HIS B 6 ? UNP Q7VTV0 ? ? 'expression tag'        23 14 
2 9O90 HIS B 7 ? UNP Q7VTV0 ? ? 'expression tag'        24 15 
2 9O90 HIS B 8 ? UNP Q7VTV0 ? ? 'expression tag'        25 16 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4570  ? 
1 MORE         -36   ? 
1 'SSA (A^2)'  22560 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,J 
1 2 B,G,H,I,K   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 115.8480000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 21  ? LEU A 25  ? GLY A 38  LEU A 42  5 ? 5  
HELX_P HELX_P2  AA2 PRO A 32  ? MET A 35  ? PRO A 49  MET A 52  5 ? 4  
HELX_P HELX_P3  AA3 LEU A 43  ? ALA A 54  ? LEU A 60  ALA A 71  1 ? 12 
HELX_P HELX_P4  AA4 ASN A 66  ? ASP A 75  ? ASN A 83  ASP A 92  1 ? 10 
HELX_P HELX_P5  AA5 ALA A 77  ? LYS A 87  ? ALA A 94  LYS A 104 1 ? 11 
HELX_P HELX_P6  AA6 LYS A 89  ? ASP A 98  ? LYS A 106 ASP A 115 1 ? 10 
HELX_P HELX_P7  AA7 GLY A 116 ? ALA A 124 ? GLY A 133 ALA A 141 1 ? 9  
HELX_P HELX_P8  AA8 ALA A 124 ? GLY A 129 ? ALA A 141 GLY A 146 1 ? 6  
HELX_P HELX_P9  AA9 PRO A 147 ? GLN A 160 ? PRO A 164 GLN A 177 1 ? 14 
HELX_P HELX_P10 AB1 PRO A 170 ? LYS A 176 ? PRO A 187 LYS A 193 5 ? 7  
HELX_P HELX_P11 AB2 ALA A 200 ? ALA A 204 ? ALA A 217 ALA A 221 5 ? 5  
HELX_P HELX_P12 AB3 ALA A 219 ? THR A 227 ? ALA A 236 THR A 244 1 ? 9  
HELX_P HELX_P13 AB4 GLN A 236 ? LEU A 245 ? GLN A 253 LEU A 262 1 ? 10 
HELX_P HELX_P14 AB5 SER A 264 ? GLY A 281 ? SER A 281 GLY A 298 1 ? 18 
HELX_P HELX_P15 AB6 GLY B 21  ? LEU B 25  ? GLY B 38  LEU B 42  5 ? 5  
HELX_P HELX_P16 AB7 PRO B 32  ? MET B 35  ? PRO B 49  MET B 52  5 ? 4  
HELX_P HELX_P17 AB8 LEU B 43  ? ALA B 54  ? LEU B 60  ALA B 71  1 ? 12 
HELX_P HELX_P18 AB9 ASN B 66  ? ASP B 75  ? ASN B 83  ASP B 92  1 ? 10 
HELX_P HELX_P19 AC1 ALA B 77  ? LYS B 87  ? ALA B 94  LYS B 104 1 ? 11 
HELX_P HELX_P20 AC2 LYS B 89  ? ILE B 99  ? LYS B 106 ILE B 116 1 ? 11 
HELX_P HELX_P21 AC3 GLY B 116 ? ALA B 124 ? GLY B 133 ALA B 141 1 ? 9  
HELX_P HELX_P22 AC4 ALA B 124 ? GLY B 129 ? ALA B 141 GLY B 146 1 ? 6  
HELX_P HELX_P23 AC5 PRO B 147 ? GLN B 160 ? PRO B 164 GLN B 177 1 ? 14 
HELX_P HELX_P24 AC6 PRO B 170 ? LYS B 176 ? PRO B 187 LYS B 193 5 ? 7  
HELX_P HELX_P25 AC7 ALA B 200 ? ALA B 204 ? ALA B 217 ALA B 221 5 ? 5  
HELX_P HELX_P26 AC8 ALA B 219 ? THR B 227 ? ALA B 236 THR B 244 1 ? 9  
HELX_P HELX_P27 AC9 GLN B 236 ? ARG B 246 ? GLN B 253 ARG B 263 1 ? 11 
HELX_P HELX_P28 AD1 SER B 264 ? GLY B 281 ? SER B 281 GLY B 298 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 LEU 25 A . ? LEU 42 A PRO 26 A ? PRO 43 A 1 4.83 
2 LEU 25 B . ? LEU 42 B PRO 26 B ? PRO 43 B 1 5.10 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 2  ? 
AA3 ? 2  ? 
AA4 ? 10 ? 
AA5 ? 2  ? 
AA6 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? anti-parallel 
AA1 5 6  ? anti-parallel 
AA1 6 7  ? anti-parallel 
AA1 7 8  ? anti-parallel 
AA1 8 9  ? parallel      
AA1 9 10 ? anti-parallel 
AA2 1 2  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? anti-parallel 
AA4 5 6  ? anti-parallel 
AA4 6 7  ? anti-parallel 
AA4 7 8  ? anti-parallel 
AA4 8 9  ? parallel      
AA4 9 10 ? anti-parallel 
AA5 1 2  ? anti-parallel 
AA6 1 2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASN A 105 ? ARG A 110 ? ASN A 122 ARG A 127 
AA1 2  ASP A 58  ? THR A 63  ? ASP A 75  THR A 80  
AA1 3  LYS A 12  ? VAL A 17  ? LYS A 29  VAL A 34  
AA1 4  PHE A 133 ? LEU A 136 ? PHE A 150 LEU A 153 
AA1 5  LEU A 208 ? LEU A 216 ? LEU A 225 LEU A 233 
AA1 6  GLY A 178 ? PRO A 184 ? GLY A 195 PRO A 201 
AA1 7  THR A 189 ? GLU A 197 ? THR A 206 GLU A 214 
AA1 8  VAL A 250 ? ARG A 254 ? VAL A 267 ARG A 271 
AA1 9  SER A 162 ? GLU A 168 ? SER A 179 GLU A 185 
AA1 10 LEU A 208 ? LEU A 216 ? LEU A 225 LEU A 233 
AA2 1  PRO A 37  ? VAL A 38  ? PRO A 54  VAL A 55  
AA2 2  LYS A 41  ? PRO A 42  ? LYS A 58  PRO A 59  
AA3 1  ASP A 140 ? ASP A 143 ? ASP A 157 ASP A 160 
AA3 2  LYS A 258 ? ASP A 261 ? LYS A 275 ASP A 278 
AA4 1  ASN B 105 ? ARG B 110 ? ASN B 122 ARG B 127 
AA4 2  ASP B 58  ? THR B 63  ? ASP B 75  THR B 80  
AA4 3  LYS B 12  ? PRO B 16  ? LYS B 29  PRO B 33  
AA4 4  PHE B 133 ? LEU B 136 ? PHE B 150 LEU B 153 
AA4 5  LEU B 208 ? LEU B 216 ? LEU B 225 LEU B 233 
AA4 6  GLY B 178 ? PRO B 184 ? GLY B 195 PRO B 201 
AA4 7  THR B 189 ? GLU B 197 ? THR B 206 GLU B 214 
AA4 8  VAL B 250 ? ARG B 254 ? VAL B 267 ARG B 271 
AA4 9  SER B 162 ? GLU B 168 ? SER B 179 GLU B 185 
AA4 10 LEU B 208 ? LEU B 216 ? LEU B 225 LEU B 233 
AA5 1  PRO B 37  ? VAL B 38  ? PRO B 54  VAL B 55  
AA5 2  LYS B 41  ? PRO B 42  ? LYS B 58  PRO B 59  
AA6 1  ASP B 140 ? ASP B 143 ? ASP B 157 ASP B 160 
AA6 2  LYS B 258 ? ASP B 261 ? LYS B 275 ASP B 278 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O ASN A 105 ? O ASN A 122 N LEU A 59  ? N LEU A 76  
AA1 2 3  O ILE A 60  ? O ILE A 77  N PHE A 15  ? N PHE A 32  
AA1 3 4  N LYS A 12  ? N LYS A 29  O ALA A 134 ? O ALA A 151 
AA1 4 5  N PHE A 133 ? N PHE A 150 O LEU A 216 ? O LEU A 233 
AA1 5 6  O LEU A 208 ? O LEU A 225 N VAL A 180 ? N VAL A 197 
AA1 6 7  N ILE A 179 ? N ILE A 196 O VAL A 196 ? O VAL A 213 
AA1 7 8  N VAL A 192 ? N VAL A 209 O VAL A 250 ? O VAL A 267 
AA1 8 9  O TYR A 251 ? O TYR A 268 N SER A 162 ? N SER A 179 
AA1 9 10 N GLN A 167 ? N GLN A 184 O ALA A 209 ? O ALA A 226 
AA2 1 2  N VAL A 38  ? N VAL A 55  O LYS A 41  ? O LYS A 58  
AA3 1 2  N LEU A 141 ? N LEU A 158 O TYR A 260 ? O TYR A 277 
AA4 1 2  O ASN B 105 ? O ASN B 122 N LEU B 59  ? N LEU B 76  
AA4 2 3  O ILE B 60  ? O ILE B 77  N PHE B 15  ? N PHE B 32  
AA4 3 4  N VAL B 14  ? N VAL B 31  O ALA B 134 ? O ALA B 151 
AA4 4 5  N PHE B 133 ? N PHE B 150 O LEU B 216 ? O LEU B 233 
AA4 5 6  O VAL B 210 ? O VAL B 227 N GLY B 178 ? N GLY B 195 
AA4 6 7  N GLN B 183 ? N GLN B 200 O ARG B 191 ? O ARG B 208 
AA4 7 8  N VAL B 192 ? N VAL B 209 O VAL B 250 ? O VAL B 267 
AA4 8 9  O HIS B 253 ? O HIS B 270 N LEU B 164 ? N LEU B 181 
AA4 9 10 N VAL B 163 ? N VAL B 180 O VAL B 215 ? O VAL B 232 
AA5 1 2  N VAL B 38  ? N VAL B 55  O LYS B 41  ? O LYS B 58  
AA6 1 2  N LEU B 141 ? N LEU B 158 O TYR B 260 ? O TYR B 277 
# 
_pdbx_entry_details.entry_id                   9O90 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 VAL A 56  ? ? 64.13   -88.26 
2 1 ASN A 147 ? ? -100.79 55.65  
3 1 VAL B 56  ? ? 66.22   -91.77 
4 1 LYS B 104 ? ? -67.62  3.00   
5 1 ASN B 147 ? ? -100.72 55.27  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     40 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.213 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Seattle Structural Genomics Center for Infectious Disease' 
_pdbx_SG_project.initial_of_center     SSGCID 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     620 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   K 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1  ? refined 47.026 -2.383  15.710  0.2754 0.2309 0.2473 -0.0173 0.0183  -0.0020 0.9203 0.0562 0.2181 -0.2640 
-0.2225 0.1452  0.0622  -0.0514 -0.0000 -0.1145 0.0102  -0.0168 0.0908  0.0022  -0.0778 
'X-RAY DIFFRACTION' 2  ? refined 39.223 -2.962  15.823  0.2113 0.2149 0.2202 -0.0158 -0.0033 0.0189  1.1129 1.6071 0.7291 -0.3586 
0.0134  0.1775  -0.0377 0.0334  -0.0009 0.1097  -0.0783 -0.1150 -0.0392 0.1467  -0.1505 
'X-RAY DIFFRACTION' 3  ? refined 31.827 11.762  17.525  0.3282 0.3399 0.2583 0.1034  0.0061  0.0316  0.3486 1.1348 0.2939 -0.4574 
0.0015  0.4526  0.0513  -0.0927 -0.0050 0.0907  0.0974  -0.2886 -0.1524 -0.4412 -0.1012 
'X-RAY DIFFRACTION' 4  ? refined 44.144 -1.832  28.721  0.2684 0.2293 0.2526 0.0170  0.0123  0.0056  0.8510 0.2425 0.8085 0.1221  
-0.6177 0.0677  -0.0082 0.0277  0.0005  -0.1825 -0.0555 0.0036  0.0593  0.0701  -0.0771 
'X-RAY DIFFRACTION' 5  ? refined 45.595 -8.793  -13.118 0.2916 0.2233 0.2873 -0.0332 0.0156  -0.0323 0.6629 0.0578 0.4316 0.0567  
-0.0735 -0.1891 -0.0508 0.0996  -0.0015 -0.4978 -0.2313 0.0431  0.0385  0.1571  -0.0009 
'X-RAY DIFFRACTION' 6  ? refined 45.408 -1.840  -14.601 0.2705 0.2469 0.2320 -0.0088 0.0027  0.0049  0.8267 0.4806 0.1689 0.6338  
-0.3480 -0.2510 -0.0140 -0.0762 -0.0000 0.1358  -0.0437 -0.0151 -0.1059 0.0003  0.1275  
'X-RAY DIFFRACTION' 7  ? refined 54.493 7.786   -6.638  0.3551 0.2274 0.4245 -0.0499 -0.0244 -0.0677 0.6264 0.1199 0.3222 0.1908  
0.1560  0.1736  0.0320  0.0881  0.0680  -0.2911 0.4206  -0.4113 0.7382  -0.2961 -0.0537 
'X-RAY DIFFRACTION' 8  ? refined 45.563 2.684   -8.574  0.3258 0.2122 0.2803 0.0295  0.0270  -0.0100 0.3585 0.1631 0.6439 0.0880  
0.2097  0.3276  0.1729  -0.1837 -0.0003 -0.1987 0.1057  -0.0214 -0.1845 -0.0304 0.0883  
'X-RAY DIFFRACTION' 9  ? refined 33.150 -5.619  -16.011 0.2608 0.3131 0.2890 0.0029  -0.0105 0.0185  0.8302 0.7211 0.4174 0.4890  
0.5400  0.4927  -0.0201 -0.0162 0.0000  -0.0603 0.1604  0.1297  -0.0221 -0.0747 -0.2789 
'X-RAY DIFFRACTION' 10 ? refined 34.304 -16.263 -28.423 0.2669 0.3495 0.3049 -0.1089 0.0098  -0.0155 0.3619 0.5663 0.5602 -0.1733 
-0.0709 -0.1120 0.0546  0.1257  0.0068  0.0739  0.1013  0.0817  -0.5109 -0.3835 -0.0460 
'X-RAY DIFFRACTION' 11 ? refined 27.481 -18.601 -27.734 0.3174 0.3420 0.3037 -0.1393 -0.1054 -0.0041 1.3855 0.2969 1.2737 -0.0168 
-0.9380 -0.0117 -0.3107 0.1278  -0.3462 0.3049  -0.2591 0.3443  -0.3422 0.2607  -0.0991 
'X-RAY DIFFRACTION' 12 ? refined 31.802 -13.617 -23.032 0.2958 0.3776 0.2816 -0.1009 -0.0171 -0.0126 0.0797 0.1505 0.0066 0.1149  
0.0205  0.0205  -0.0090 0.0257  0.0001  0.1505  0.0818  0.1761  -0.2529 0.1019  -0.3915 
'X-RAY DIFFRACTION' 13 ? refined 29.653 -19.726 -10.834 0.4724 0.3931 0.3405 -0.1825 -0.0772 0.0259  0.3681 0.1720 0.6833 0.2538  
0.5073  0.3466  0.3379  0.0520  0.0647  -0.1572 -0.2953 0.2024  0.0825  0.7723  -0.1456 
'X-RAY DIFFRACTION' 14 ? refined 33.004 -9.526  -24.700 0.3809 0.3658 0.2724 -0.1112 -0.1069 0.0473  0.2083 1.1925 0.2323 0.2024  
-0.1239 0.0091  -0.1093 0.1085  -0.0519 0.1890  -0.0252 0.1632  -0.4313 0.2422  -0.1674 
'X-RAY DIFFRACTION' 15 ? refined 53.557 -0.910  -31.718 0.4065 0.2839 0.2705 -0.0017 0.0400  0.0139  0.3700 0.0663 0.1737 0.0331  
0.2197  -0.0344 -0.0078 -0.0010 -0.0000 0.1382  -0.0954 -0.0624 -0.3371 0.2081  0.2170  
'X-RAY DIFFRACTION' 16 ? refined 44.387 -3.670  -0.058  0.6913 0.6732 0.9603 0.1152  -0.0676 -0.2497 0.0950 0.0514 0.0544 0.0549  
-0.0476 0.0072  0.1862  -0.0193 -0.0001 0.0288  -0.3605 0.2102  0.0082  -0.1540 0.1685  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1  A 2   A 47  '( CHAIN A AND RESID 2:47 )'                                       ? ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  A 48  A 191 '( CHAIN A AND RESID 48:191 )'                                     ? ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  A 192 A 240 '( CHAIN A AND RESID 192:240 )'                                    ? ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  A 241 A 279 '( CHAIN A AND RESID 241:279 )'                                    ? ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  B 1   B 26  '( CHAIN B AND RESID 1:26 )'                                       ? ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  B 27  B 60  '( CHAIN B AND RESID 27:60 )'                                      ? ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  B 61  B 83  '( CHAIN B AND RESID 61:83 )'                                      ? ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  B 84  B 110 '( CHAIN B AND RESID 84:110 )'                                     ? ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  B 111 B 153 '( CHAIN B AND RESID 111:153 )'                                    ? ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 B 154 B 171 '( CHAIN B AND RESID 154:171 )'                                    ? ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 B 172 B 197 '( CHAIN B AND RESID 172:197 )'                                    ? ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 B 198 B 211 '( CHAIN B AND RESID 198:211 )'                                    ? ? ? ? ? 
'X-RAY DIFFRACTION' 13 13 B 212 B 240 '( CHAIN B AND RESID 212:240 )'                                    ? ? ? ? ? 
'X-RAY DIFFRACTION' 14 14 B 241 B 258 '( CHAIN B AND RESID 241:258 )'                                    ? ? ? ? ? 
'X-RAY DIFFRACTION' 15 15 B 259 B 279 '( CHAIN B AND RESID 259:279 )'                                    ? ? ? ? ? 
'X-RAY DIFFRACTION' 16 16 A 301 A 302 '( CHAIN A AND RESID 301:302 )  OR  ( CHAIN B AND RESID 301:302 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 17 16 B 301 B 302 '( CHAIN A AND RESID 301:302 )  OR  ( CHAIN B AND RESID 301:302 )' ? ? ? ? ? 
# 
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 18  ? A MET 1   
2  1 Y 1 A ALA 19  ? A ALA 2   
3  1 Y 1 A HIS 20  ? A HIS 3   
4  1 Y 1 A HIS 21  ? A HIS 4   
5  1 Y 1 A HIS 22  ? A HIS 5   
6  1 Y 1 A HIS 23  ? A HIS 6   
7  1 Y 1 A HIS 24  ? A HIS 7   
8  1 Y 1 A VAL 246 ? A VAL 229 
9  1 Y 1 A GLY 247 ? A GLY 230 
10 1 Y 1 A ALA 248 ? A ALA 231 
11 1 Y 1 A GLY 249 ? A GLY 232 
12 1 Y 1 A ASN 250 ? A ASN 233 
13 1 Y 1 B MET 18  ? B MET 1   
14 1 Y 1 B ALA 19  ? B ALA 2   
15 1 Y 1 B HIS 20  ? B HIS 3   
16 1 Y 1 B HIS 21  ? B HIS 4   
17 1 Y 1 B HIS 22  ? B HIS 5   
18 1 Y 1 B HIS 23  ? B HIS 6   
19 1 Y 1 B THR 245 ? B THR 228 
20 1 Y 1 B VAL 246 ? B VAL 229 
21 1 Y 1 B GLY 247 ? B GLY 230 
22 1 Y 1 B ALA 248 ? B ALA 231 
23 1 Y 1 B GLY 249 ? B GLY 232 
24 1 Y 1 B ASN 250 ? B ASN 233 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PHE N    N N N 264 
PHE CA   C N S 265 
PHE C    C N N 266 
PHE O    O N N 267 
PHE CB   C N N 268 
PHE CG   C Y N 269 
PHE CD1  C Y N 270 
PHE CD2  C Y N 271 
PHE CE1  C Y N 272 
PHE CE2  C Y N 273 
PHE CZ   C Y N 274 
PHE OXT  O N N 275 
PHE H    H N N 276 
PHE H2   H N N 277 
PHE HA   H N N 278 
PHE HB2  H N N 279 
PHE HB3  H N N 280 
PHE HD1  H N N 281 
PHE HD2  H N N 282 
PHE HE1  H N N 283 
PHE HE2  H N N 284 
PHE HZ   H N N 285 
PHE HXT  H N N 286 
PRO N    N N N 287 
PRO CA   C N S 288 
PRO C    C N N 289 
PRO O    O N N 290 
PRO CB   C N N 291 
PRO CG   C N N 292 
PRO CD   C N N 293 
PRO OXT  O N N 294 
PRO H    H N N 295 
PRO HA   H N N 296 
PRO HB2  H N N 297 
PRO HB3  H N N 298 
PRO HG2  H N N 299 
PRO HG3  H N N 300 
PRO HD2  H N N 301 
PRO HD3  H N N 302 
PRO HXT  H N N 303 
SER N    N N N 304 
SER CA   C N S 305 
SER C    C N N 306 
SER O    O N N 307 
SER CB   C N N 308 
SER OG   O N N 309 
SER OXT  O N N 310 
SER H    H N N 311 
SER H2   H N N 312 
SER HA   H N N 313 
SER HB2  H N N 314 
SER HB3  H N N 315 
SER HG   H N N 316 
SER HXT  H N N 317 
THR N    N N N 318 
THR CA   C N S 319 
THR C    C N N 320 
THR O    O N N 321 
THR CB   C N R 322 
THR OG1  O N N 323 
THR CG2  C N N 324 
THR OXT  O N N 325 
THR H    H N N 326 
THR H2   H N N 327 
THR HA   H N N 328 
THR HB   H N N 329 
THR HG1  H N N 330 
THR HG21 H N N 331 
THR HG22 H N N 332 
THR HG23 H N N 333 
THR HXT  H N N 334 
TYR N    N N N 335 
TYR CA   C N S 336 
TYR C    C N N 337 
TYR O    O N N 338 
TYR CB   C N N 339 
TYR CG   C Y N 340 
TYR CD1  C Y N 341 
TYR CD2  C Y N 342 
TYR CE1  C Y N 343 
TYR CE2  C Y N 344 
TYR CZ   C Y N 345 
TYR OH   O N N 346 
TYR OXT  O N N 347 
TYR H    H N N 348 
TYR H2   H N N 349 
TYR HA   H N N 350 
TYR HB2  H N N 351 
TYR HB3  H N N 352 
TYR HD1  H N N 353 
TYR HD2  H N N 354 
TYR HE1  H N N 355 
TYR HE2  H N N 356 
TYR HH   H N N 357 
TYR HXT  H N N 358 
VAL N    N N N 359 
VAL CA   C N S 360 
VAL C    C N N 361 
VAL O    O N N 362 
VAL CB   C N N 363 
VAL CG1  C N N 364 
VAL CG2  C N N 365 
VAL OXT  O N N 366 
VAL H    H N N 367 
VAL H2   H N N 368 
VAL HA   H N N 369 
VAL HB   H N N 370 
VAL HG11 H N N 371 
VAL HG12 H N N 372 
VAL HG13 H N N 373 
VAL HG21 H N N 374 
VAL HG22 H N N 375 
VAL HG23 H N N 376 
VAL HXT  H N N 377 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TYR N   CA   sing N N 319 
TYR N   H    sing N N 320 
TYR N   H2   sing N N 321 
TYR CA  C    sing N N 322 
TYR CA  CB   sing N N 323 
TYR CA  HA   sing N N 324 
TYR C   O    doub N N 325 
TYR C   OXT  sing N N 326 
TYR CB  CG   sing N N 327 
TYR CB  HB2  sing N N 328 
TYR CB  HB3  sing N N 329 
TYR CG  CD1  doub Y N 330 
TYR CG  CD2  sing Y N 331 
TYR CD1 CE1  sing Y N 332 
TYR CD1 HD1  sing N N 333 
TYR CD2 CE2  doub Y N 334 
TYR CD2 HD2  sing N N 335 
TYR CE1 CZ   doub Y N 336 
TYR CE1 HE1  sing N N 337 
TYR CE2 CZ   sing Y N 338 
TYR CE2 HE2  sing N N 339 
TYR CZ  OH   sing N N 340 
TYR OH  HH   sing N N 341 
TYR OXT HXT  sing N N 342 
VAL N   CA   sing N N 343 
VAL N   H    sing N N 344 
VAL N   H2   sing N N 345 
VAL CA  C    sing N N 346 
VAL CA  CB   sing N N 347 
VAL CA  HA   sing N N 348 
VAL C   O    doub N N 349 
VAL C   OXT  sing N N 350 
VAL CB  CG1  sing N N 351 
VAL CB  CG2  sing N N 352 
VAL CB  HB   sing N N 353 
VAL CG1 HG11 sing N N 354 
VAL CG1 HG12 sing N N 355 
VAL CG1 HG13 sing N N 356 
VAL CG2 HG21 sing N N 357 
VAL CG2 HG22 sing N N 358 
VAL CG2 HG23 sing N N 359 
VAL OXT HXT  sing N N 360 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 75N93022C00036 1 
'National Institutes of Health/Office of the Director'                                            'United States' S10OD030394    2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-Q7VTV0-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9O90 
_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]   0.008632 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003108 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010600 
_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]   0.013196 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . HIS A 1 8   ? 20.064 -5.999  12.526  1.00 74.95  ? 25  HIS A N   1 
ATOM   2    C CA  . HIS A 1 8   ? 21.498 -5.799  12.694  1.00 66.38  ? 25  HIS A CA  1 
ATOM   3    C C   . HIS A 1 8   ? 22.256 -7.096  12.634  1.00 59.90  ? 25  HIS A C   1 
ATOM   4    O O   . HIS A 1 8   ? 22.034 -7.994  13.451  1.00 58.24  ? 25  HIS A O   1 
ATOM   5    C CB  . HIS A 1 8   ? 21.837 -5.192  14.045  1.00 65.32  ? 25  HIS A CB  1 
ATOM   6    C CG  . HIS A 1 8   ? 21.881 -3.704  14.065  1.00 70.17  ? 25  HIS A CG  1 
ATOM   7    N ND1 . HIS A 1 8   ? 22.877 -3.002  14.711  1.00 58.58  ? 25  HIS A ND1 1 
ATOM   8    C CD2 . HIS A 1 8   ? 21.017 -2.781  13.581  1.00 79.74  ? 25  HIS A CD2 1 
ATOM   9    C CE1 . HIS A 1 8   ? 22.642 -1.707  14.592  1.00 61.62  ? 25  HIS A CE1 1 
ATOM   10   N NE2 . HIS A 1 8   ? 21.517 -1.546  13.916  1.00 74.28  ? 25  HIS A NE2 1 
ATOM   11   N N   . VAL A 1 9   ? 23.176 -7.187  11.693  1.00 50.37  ? 26  VAL A N   1 
ATOM   12   C CA  . VAL A 1 9   ? 24.223 -8.196  11.722  1.00 45.05  ? 26  VAL A CA  1 
ATOM   13   C C   . VAL A 1 9   ? 25.528 -7.455  11.475  1.00 45.67  ? 26  VAL A C   1 
ATOM   14   O O   . VAL A 1 9   ? 25.653 -6.719  10.489  1.00 39.04  ? 26  VAL A O   1 
ATOM   15   C CB  . VAL A 1 9   ? 23.992 -9.316  10.692  1.00 47.96  ? 26  VAL A CB  1 
ATOM   16   C CG1 . VAL A 1 9   ? 23.842 -8.735  9.317   1.00 59.87  ? 26  VAL A CG1 1 
ATOM   17   C CG2 . VAL A 1 9   ? 25.137 -10.309 10.739  1.00 51.00  ? 26  VAL A CG2 1 
ATOM   18   N N   . VAL A 1 10  ? 26.481 -7.618  12.381  1.00 34.48  ? 27  VAL A N   1 
ATOM   19   C CA  . VAL A 1 10  ? 27.744 -6.910  12.309  1.00 34.76  ? 27  VAL A CA  1 
ATOM   20   C C   . VAL A 1 10  ? 28.808 -7.945  11.993  1.00 34.19  ? 27  VAL A C   1 
ATOM   21   O O   . VAL A 1 10  ? 29.147 -8.780  12.834  1.00 34.24  ? 27  VAL A O   1 
ATOM   22   C CB  . VAL A 1 10  ? 28.053 -6.152  13.606  1.00 33.64  ? 27  VAL A CB  1 
ATOM   23   C CG1 . VAL A 1 10  ? 29.275 -5.277  13.381  1.00 28.55  ? 27  VAL A CG1 1 
ATOM   24   C CG2 . VAL A 1 10  ? 26.869 -5.326  14.028  1.00 37.00  ? 27  VAL A CG2 1 
ATOM   25   N N   . ARG A 1 11  ? 29.323 -7.914  10.777  1.00 30.98  ? 28  ARG A N   1 
ATOM   26   C CA  . ARG A 1 11  ? 30.356 -8.854  10.370  1.00 32.23  ? 28  ARG A CA  1 
ATOM   27   C C   . ARG A 1 11  ? 31.607 -8.178  9.823   1.00 27.98  ? 28  ARG A C   1 
ATOM   28   O O   . ARG A 1 11  ? 32.589 -8.867  9.535   1.00 28.07  ? 28  ARG A O   1 
ATOM   29   C CB  . ARG A 1 11  ? 29.768 -9.822  9.343   1.00 32.49  ? 28  ARG A CB  1 
ATOM   30   C CG  . ARG A 1 11  ? 29.566 -9.232  7.986   1.00 41.35  ? 28  ARG A CG  1 
ATOM   31   C CD  . ARG A 1 11  ? 28.746 -10.217 7.183   1.00 54.55  ? 28  ARG A CD  1 
ATOM   32   N NE  . ARG A 1 11  ? 29.021 -10.229 5.759   1.00 60.26  ? 28  ARG A NE  1 
ATOM   33   C CZ  . ARG A 1 11  ? 28.492 -9.395  4.876   1.00 60.89  ? 28  ARG A CZ  1 
ATOM   34   N NH1 . ARG A 1 11  ? 27.696 -8.409  5.242   1.00 57.63  ? 28  ARG A NH1 1 
ATOM   35   N NH2 . ARG A 1 11  ? 28.749 -9.574  3.588   1.00 68.25  ? 28  ARG A NH2 1 
ATOM   36   N N   . LYS A 1 12  ? 31.610 -6.858  9.694   1.00 29.20  ? 29  LYS A N   1 
ATOM   37   C CA  . LYS A 1 12  ? 32.757 -6.109  9.201   1.00 25.26  ? 29  LYS A CA  1 
ATOM   38   C C   . LYS A 1 12  ? 33.345 -5.244  10.305  1.00 25.86  ? 29  LYS A C   1 
ATOM   39   O O   . LYS A 1 12  ? 32.606 -4.596  11.039  1.00 24.44  ? 29  LYS A O   1 
ATOM   40   C CB  . LYS A 1 12  ? 32.336 -5.209  8.039   1.00 31.85  ? 29  LYS A CB  1 
ATOM   41   C CG  . LYS A 1 12  ? 31.907 -5.955  6.776   1.00 32.94  ? 29  LYS A CG  1 
ATOM   42   C CD  . LYS A 1 12  ? 31.409 -4.971  5.712   1.00 36.31  ? 29  LYS A CD  1 
ATOM   43   C CE  . LYS A 1 12  ? 30.856 -5.689  4.487   1.00 34.41  ? 29  LYS A CE  1 
ATOM   44   N NZ  . LYS A 1 12  ? 31.950 -6.421  3.811   1.00 35.83  ? 29  LYS A NZ  1 
ATOM   45   N N   . ALA A 1 13  ? 34.675 -5.176  10.376  1.00 23.69  ? 30  ALA A N   1 
ATOM   46   C CA  . ALA A 1 13  ? 35.352 -4.296  11.316  1.00 24.43  ? 30  ALA A CA  1 
ATOM   47   C C   . ALA A 1 13  ? 36.428 -3.506  10.591  1.00 23.34  ? 30  ALA A C   1 
ATOM   48   O O   . ALA A 1 13  ? 37.118 -4.027  9.707   1.00 24.30  ? 30  ALA A O   1 
ATOM   49   C CB  . ALA A 1 13  ? 35.991 -5.077  12.471  1.00 22.79  ? 30  ALA A CB  1 
ATOM   50   N N   . VAL A 1 14  ? 36.557 -2.247  10.980  1.00 23.28  ? 31  VAL A N   1 
ATOM   51   C CA  . VAL A 1 14  ? 37.507 -1.307  10.401  1.00 21.67  ? 31  VAL A CA  1 
ATOM   52   C C   . VAL A 1 14  ? 38.604 -1.029  11.413  1.00 23.04  ? 31  VAL A C   1 
ATOM   53   O O   . VAL A 1 14  ? 38.312 -0.658  12.562  1.00 20.98  ? 31  VAL A O   1 
ATOM   54   C CB  . VAL A 1 14  ? 36.796 0.001   10.008  1.00 23.97  ? 31  VAL A CB  1 
ATOM   55   C CG1 . VAL A 1 14  ? 37.829 1.049   9.579   1.00 22.26  ? 31  VAL A CG1 1 
ATOM   56   C CG2 . VAL A 1 14  ? 35.806 -0.263  8.910   1.00 27.02  ? 31  VAL A CG2 1 
ATOM   57   N N   . PHE A 1 15  ? 39.856 -1.167  10.983  1.00 22.13  ? 32  PHE A N   1 
ATOM   58   C CA  . PHE A 1 15  ? 41.031 -0.930  11.821  1.00 21.74  ? 32  PHE A CA  1 
ATOM   59   C C   . PHE A 1 15  ? 41.897 0.168   11.231  1.00 25.15  ? 32  PHE A C   1 
ATOM   60   O O   . PHE A 1 15  ? 42.629 -0.071  10.248  1.00 25.28  ? 32  PHE A O   1 
ATOM   61   C CB  . PHE A 1 15  ? 41.863 -2.204  11.968  1.00 22.52  ? 32  PHE A CB  1 
ATOM   62   C CG  . PHE A 1 15  ? 41.093 -3.381  12.459  1.00 20.76  ? 32  PHE A CG  1 
ATOM   63   C CD1 . PHE A 1 15  ? 40.406 -4.173  11.577  1.00 21.56  ? 32  PHE A CD1 1 
ATOM   64   C CD2 . PHE A 1 15  ? 41.056 -3.693  13.821  1.00 22.05  ? 32  PHE A CD2 1 
ATOM   65   C CE1 . PHE A 1 15  ? 39.706 -5.256  12.015  1.00 23.37  ? 32  PHE A CE1 1 
ATOM   66   C CE2 . PHE A 1 15  ? 40.351 -4.785  14.275  1.00 20.18  ? 32  PHE A CE2 1 
ATOM   67   C CZ  . PHE A 1 15  ? 39.679 -5.571  13.363  1.00 22.48  ? 32  PHE A CZ  1 
ATOM   68   N N   . PRO A 1 16  ? 41.867 1.378   11.780  1.00 24.17  ? 33  PRO A N   1 
ATOM   69   C CA  . PRO A 1 16  ? 42.817 2.404   11.325  1.00 25.65  ? 33  PRO A CA  1 
ATOM   70   C C   . PRO A 1 16  ? 44.203 2.055   11.820  1.00 30.16  ? 33  PRO A C   1 
ATOM   71   O O   . PRO A 1 16  ? 44.437 1.948   13.034  1.00 25.02  ? 33  PRO A O   1 
ATOM   72   C CB  . PRO A 1 16  ? 42.288 3.697   11.956  1.00 22.69  ? 33  PRO A CB  1 
ATOM   73   C CG  . PRO A 1 16  ? 40.839 3.383   12.324  1.00 24.20  ? 33  PRO A CG  1 
ATOM   74   C CD  . PRO A 1 16  ? 40.863 1.932   12.707  1.00 26.56  ? 33  PRO A CD  1 
ATOM   75   N N   . VAL A 1 17  ? 45.100 1.821   10.877  1.00 22.86  ? 34  VAL A N   1 
ATOM   76   C CA  . VAL A 1 17  ? 46.438 1.345   11.192  1.00 24.50  ? 34  VAL A CA  1 
ATOM   77   C C   . VAL A 1 17  ? 47.464 2.197   10.469  1.00 30.23  ? 34  VAL A C   1 
ATOM   78   O O   . VAL A 1 17  ? 48.424 1.675   9.894   1.00 30.58  ? 34  VAL A O   1 
ATOM   79   C CB  . VAL A 1 17  ? 46.610 -0.143  10.872  1.00 23.69  ? 34  VAL A CB  1 
ATOM   80   C CG1 . VAL A 1 17  ? 45.833 -0.996  11.898  1.00 25.33  ? 34  VAL A CG1 1 
ATOM   81   C CG2 . VAL A 1 17  ? 46.179 -0.435  9.456   1.00 27.28  ? 34  VAL A CG2 1 
ATOM   82   N N   . ALA A 1 18  ? 47.194 3.488   10.374  1.00 28.97  ? 35  ALA A N   1 
ATOM   83   C CA  . ALA A 1 18  ? 48.144 4.448   9.839   1.00 32.22  ? 35  ALA A CA  1 
ATOM   84   C C   . ALA A 1 18  ? 48.733 5.334   10.941  1.00 43.23  ? 35  ALA A C   1 
ATOM   85   O O   . ALA A 1 18  ? 49.204 6.445   10.658  1.00 36.68  ? 35  ALA A O   1 
ATOM   86   C CB  . ALA A 1 18  ? 47.459 5.291   8.764   1.00 29.83  ? 35  ALA A CB  1 
ATOM   87   N N   . GLY A 1 19  ? 48.700 4.881   12.209  1.00 36.76  ? 36  GLY A N   1 
ATOM   88   C CA  . GLY A 1 19  ? 49.176 5.735   13.289  1.00 36.04  ? 36  GLY A CA  1 
ATOM   89   C C   . GLY A 1 19  ? 50.622 6.184   13.159  1.00 39.84  ? 36  GLY A C   1 
ATOM   90   O O   . GLY A 1 19  ? 51.548 5.353   13.121  1.00 34.22  ? 36  GLY A O   1 
ATOM   91   N N   . MET A 1 20  ? 50.841 7.510   13.145  1.00 42.04  ? 37  MET A N   1 
ATOM   92   C CA  . MET A 1 20  ? 52.200 8.024   13.006  1.00 35.66  ? 37  MET A CA  1 
ATOM   93   C C   . MET A 1 20  ? 53.059 7.690   14.217  1.00 46.16  ? 37  MET A C   1 
ATOM   94   O O   . MET A 1 20  ? 54.274 7.470   14.076  1.00 41.17  ? 37  MET A O   1 
ATOM   95   C CB  . MET A 1 20  ? 52.177 9.523   12.770  1.00 40.63  ? 37  MET A CB  1 
ATOM   96   C CG  . MET A 1 20  ? 51.657 9.908   11.404  1.00 50.93  ? 37  MET A CG  1 
ATOM   97   S SD  . MET A 1 20  ? 51.937 11.666  11.029  1.00 74.68  ? 37  MET A SD  1 
ATOM   98   C CE  . MET A 1 20  ? 53.729 11.763  11.025  1.00 44.91  ? 37  MET A CE  1 
ATOM   99   N N   . GLY A 1 21  ? 52.457 7.662   15.405  1.00 39.08  ? 38  GLY A N   1 
ATOM   100  C CA  . GLY A 1 21  ? 53.178 7.282   16.593  1.00 36.79  ? 38  GLY A CA  1 
ATOM   101  C C   . GLY A 1 21  ? 54.421 8.118   16.722  1.00 38.65  ? 38  GLY A C   1 
ATOM   102  O O   . GLY A 1 21  ? 55.498 7.581   16.997  1.00 35.49  ? 38  GLY A O   1 
ATOM   103  N N   . THR A 1 22  ? 54.283 9.437   16.509  1.00 34.28  ? 39  THR A N   1 
ATOM   104  C CA  . THR A 1 22  ? 55.439 10.315  16.621  1.00 37.59  ? 39  THR A CA  1 
ATOM   105  C C   . THR A 1 22  ? 56.036 10.201  18.002  1.00 34.82  ? 39  THR A C   1 
ATOM   106  O O   . THR A 1 22  ? 57.253 10.315  18.166  1.00 32.69  ? 39  THR A O   1 
ATOM   107  C CB  . THR A 1 22  ? 55.048 11.760  16.367  1.00 43.24  ? 39  THR A CB  1 
ATOM   108  O OG1 . THR A 1 22  ? 54.101 12.147  17.372  1.00 44.57  ? 39  THR A OG1 1 
ATOM   109  C CG2 . THR A 1 22  ? 54.444 11.899  14.990  1.00 48.44  ? 39  THR A CG2 1 
ATOM   110  N N   . ARG A 1 23  ? 55.189 9.916   18.984  1.00 37.45  ? 40  ARG A N   1 
ATOM   111  C CA  . ARG A 1 23  ? 55.674 9.747   20.374  1.00 38.40  ? 40  ARG A CA  1 
ATOM   112  C C   . ARG A 1 23  ? 56.568 8.505   20.466  1.00 33.40  ? 40  ARG A C   1 
ATOM   113  O O   . ARG A 1 23  ? 57.323 8.408   21.438  1.00 38.08  ? 40  ARG A O   1 
ATOM   114  C CB  . ARG A 1 23  ? 54.482 9.614   21.320  1.00 47.88  ? 40  ARG A CB  1 
ATOM   115  C CG  . ARG A 1 23  ? 53.855 10.923  21.778  1.00 56.66  ? 40  ARG A CG  1 
ATOM   116  C CD  . ARG A 1 23  ? 52.365 10.747  22.021  1.00 65.43  ? 40  ARG A CD  1 
ATOM   117  N NE  . ARG A 1 23  ? 51.823 11.661  23.031  1.00 72.46  ? 40  ARG A NE  1 
ATOM   118  C CZ  . ARG A 1 23  ? 50.879 11.329  23.902  1.00 79.53  ? 40  ARG A CZ  1 
ATOM   119  N NH1 . ARG A 1 23  ? 49.799 10.686  23.496  1.00 74.45  ? 40  ARG A NH1 1 
ATOM   120  N NH2 . ARG A 1 23  ? 51.022 11.634  25.179  1.00 68.28  ? 40  ARG A NH2 1 
ATOM   121  N N   . PHE A 1 24  ? 56.479 7.609   19.484  1.00 33.36  ? 41  PHE A N   1 
ATOM   122  C CA  . PHE A 1 24  ? 57.251 6.371   19.498  1.00 29.84  ? 41  PHE A CA  1 
ATOM   123  C C   . PHE A 1 24  ? 58.335 6.319   18.426  1.00 35.16  ? 41  PHE A C   1 
ATOM   124  O O   . PHE A 1 24  ? 58.939 5.265   18.235  1.00 33.77  ? 41  PHE A O   1 
ATOM   125  C CB  . PHE A 1 24  ? 56.293 5.176   19.358  1.00 26.51  ? 41  PHE A CB  1 
ATOM   126  C CG  . PHE A 1 24  ? 55.415 4.989   20.574  1.00 31.10  ? 41  PHE A CG  1 
ATOM   127  C CD1 . PHE A 1 24  ? 54.318 5.794   20.782  1.00 30.42  ? 41  PHE A CD1 1 
ATOM   128  C CD2 . PHE A 1 24  ? 55.733 4.031   21.535  1.00 35.09  ? 41  PHE A CD2 1 
ATOM   129  C CE1 . PHE A 1 24  ? 53.513 5.620   21.958  1.00 31.50  ? 41  PHE A CE1 1 
ATOM   130  C CE2 . PHE A 1 24  ? 54.942 3.847   22.676  1.00 34.15  ? 41  PHE A CE2 1 
ATOM   131  C CZ  . PHE A 1 24  ? 53.832 4.643   22.867  1.00 32.23  ? 41  PHE A CZ  1 
ATOM   132  N N   . LEU A 1 25  ? 58.602 7.421   17.729  1.00 25.43  ? 42  LEU A N   1 
ATOM   133  C CA  . LEU A 1 25  ? 59.772 7.467   16.882  1.00 31.08  ? 42  LEU A CA  1 
ATOM   134  C C   . LEU A 1 25  ? 60.995 7.281   17.768  1.00 32.56  ? 42  LEU A C   1 
ATOM   135  O O   . LEU A 1 25  ? 61.018 7.737   18.909  1.00 33.18  ? 42  LEU A O   1 
ATOM   136  C CB  . LEU A 1 25  ? 59.887 8.794   16.145  1.00 28.20  ? 42  LEU A CB  1 
ATOM   137  C CG  . LEU A 1 25  ? 58.919 8.901   14.981  1.00 29.84  ? 42  LEU A CG  1 
ATOM   138  C CD1 . LEU A 1 25  ? 58.777 10.337  14.559  1.00 33.01  ? 42  LEU A CD1 1 
ATOM   139  C CD2 . LEU A 1 25  ? 59.360 8.015   13.808  1.00 26.32  ? 42  LEU A CD2 1 
ATOM   140  N N   . PRO A 1 26  ? 62.022 6.629   17.274  1.00 30.54  ? 43  PRO A N   1 
ATOM   141  C CA  . PRO A 1 26  ? 62.222 6.108   15.915  1.00 29.44  ? 43  PRO A CA  1 
ATOM   142  C C   . PRO A 1 26  ? 61.609 4.745   15.622  1.00 26.21  ? 43  PRO A C   1 
ATOM   143  O O   . PRO A 1 26  ? 61.643 4.295   14.488  1.00 23.13  ? 43  PRO A O   1 
ATOM   144  C CB  . PRO A 1 26  ? 63.746 6.034   15.811  1.00 33.86  ? 43  PRO A CB  1 
ATOM   145  C CG  . PRO A 1 26  ? 64.168 5.719   17.223  1.00 32.20  ? 43  PRO A CG  1 
ATOM   146  C CD  . PRO A 1 26  ? 63.240 6.551   18.079  1.00 27.95  ? 43  PRO A CD  1 
ATOM   147  N N   . ALA A 1 27  ? 61.006 4.048   16.579  1.00 23.25  ? 44  ALA A N   1 
ATOM   148  C CA  . ALA A 1 27  ? 60.521 2.693   16.313  1.00 23.74  ? 44  ALA A CA  1 
ATOM   149  C C   . ALA A 1 27  ? 59.429 2.645   15.246  1.00 26.09  ? 44  ALA A C   1 
ATOM   150  O O   . ALA A 1 27  ? 59.258 1.622   14.578  1.00 25.81  ? 44  ALA A O   1 
ATOM   151  C CB  . ALA A 1 27  ? 59.992 2.060   17.604  1.00 26.00  ? 44  ALA A CB  1 
ATOM   152  N N   . THR A 1 28  ? 58.641 3.695   15.120  1.00 20.53  ? 45  THR A N   1 
ATOM   153  C CA  . THR A 1 28  ? 57.585 3.781   14.129  1.00 24.20  ? 45  THR A CA  1 
ATOM   154  C C   . THR A 1 28  ? 58.077 4.406   12.817  1.00 27.56  ? 45  THR A C   1 
ATOM   155  O O   . THR A 1 28  ? 57.265 4.823   11.989  1.00 24.06  ? 45  THR A O   1 
ATOM   156  C CB  . THR A 1 28  ? 56.423 4.599   14.684  1.00 25.42  ? 45  THR A CB  1 
ATOM   157  O OG1 . THR A 1 28  ? 56.961 5.812   15.218  1.00 23.05  ? 45  THR A OG1 1 
ATOM   158  C CG2 . THR A 1 28  ? 55.695 3.828   15.777  1.00 27.47  ? 45  THR A CG2 1 
ATOM   159  N N   . LYS A 1 29  ? 59.385 4.519   12.626  1.00 22.94  ? 46  LYS A N   1 
ATOM   160  C CA  . LYS A 1 29  ? 59.855 4.982   11.324  1.00 24.98  ? 46  LYS A CA  1 
ATOM   161  C C   . LYS A 1 29  ? 59.407 4.064   10.187  1.00 28.58  ? 46  LYS A C   1 
ATOM   162  O O   . LYS A 1 29  ? 59.003 4.540   9.121   1.00 29.61  ? 46  LYS A O   1 
ATOM   163  C CB  . LYS A 1 29  ? 61.366 5.107   11.293  1.00 27.25  ? 46  LYS A CB  1 
ATOM   164  C CG  . LYS A 1 29  ? 61.785 5.417   9.847   1.00 30.46  ? 46  LYS A CG  1 
ATOM   165  C CD  . LYS A 1 29  ? 62.978 6.205   9.720   1.00 33.48  ? 46  LYS A CD  1 
ATOM   166  C CE  . LYS A 1 29  ? 63.345 6.353   8.196   1.00 29.45  ? 46  LYS A CE  1 
ATOM   167  N NZ  . LYS A 1 29  ? 64.783 6.281   8.118   1.00 32.10  ? 46  LYS A NZ  1 
ATOM   168  N N   . ALA A 1 30  ? 59.507 2.756   10.377  1.00 27.70  ? 47  ALA A N   1 
ATOM   169  C CA  . ALA A 1 30  ? 59.223 1.798   9.319   1.00 30.05  ? 47  ALA A CA  1 
ATOM   170  C C   . ALA A 1 30  ? 58.031 0.913   9.617   1.00 29.47  ? 47  ALA A C   1 
ATOM   171  O O   . ALA A 1 30  ? 57.759 -0.011  8.852   1.00 28.21  ? 47  ALA A O   1 
ATOM   172  C CB  . ALA A 1 30  ? 60.446 0.910   9.067   1.00 36.81  ? 47  ALA A CB  1 
ATOM   173  N N   . MET A 1 31  ? 57.324 1.139   10.717  1.00 31.29  ? 48  MET A N   1 
ATOM   174  C CA  . MET A 1 31  ? 56.080 0.425   10.950  1.00 25.59  ? 48  MET A CA  1 
ATOM   175  C C   . MET A 1 31  ? 55.114 1.377   11.630  1.00 27.29  ? 48  MET A C   1 
ATOM   176  O O   . MET A 1 31  ? 55.534 2.308   12.331  1.00 24.11  ? 48  MET A O   1 
ATOM   177  C CB  . MET A 1 31  ? 56.293 -0.834  11.792  1.00 30.33  ? 48  MET A CB  1 
ATOM   178  C CG  . MET A 1 31  ? 56.809 -0.542  13.185  1.00 30.36  ? 48  MET A CG  1 
ATOM   179  S SD  . MET A 1 31  ? 57.527 -1.988  13.982  1.00 36.06  ? 48  MET A SD  1 
ATOM   180  C CE  . MET A 1 31  ? 59.049 -2.089  13.050  1.00 43.70  ? 48  MET A CE  1 
ATOM   181  N N   . PRO A 1 32  ? 53.825 1.219   11.388  1.00 27.71  ? 49  PRO A N   1 
ATOM   182  C CA  . PRO A 1 32  ? 52.859 2.060   12.086  1.00 26.53  ? 49  PRO A CA  1 
ATOM   183  C C   . PRO A 1 32  ? 52.777 1.660   13.554  1.00 25.25  ? 49  PRO A C   1 
ATOM   184  O O   . PRO A 1 32  ? 53.194 0.575   13.976  1.00 23.96  ? 49  PRO A O   1 
ATOM   185  C CB  . PRO A 1 32  ? 51.548 1.800   11.339  1.00 30.36  ? 49  PRO A CB  1 
ATOM   186  C CG  . PRO A 1 32  ? 51.698 0.464   10.810  1.00 29.80  ? 49  PRO A CG  1 
ATOM   187  C CD  . PRO A 1 32  ? 53.161 0.266   10.497  1.00 27.43  ? 49  PRO A CD  1 
ATOM   188  N N   . LYS A 1 33  ? 52.260 2.599   14.330  1.00 25.93  ? 50  LYS A N   1 
ATOM   189  C CA  . LYS A 1 33  ? 52.183 2.456   15.776  1.00 27.35  ? 50  LYS A CA  1 
ATOM   190  C C   . LYS A 1 33  ? 51.498 1.156   16.168  1.00 25.69  ? 50  LYS A C   1 
ATOM   191  O O   . LYS A 1 33  ? 51.936 0.446   17.090  1.00 27.63  ? 50  LYS A O   1 
ATOM   192  C CB  . LYS A 1 33  ? 51.427 3.676   16.319  1.00 30.08  ? 50  LYS A CB  1 
ATOM   193  C CG  . LYS A 1 33  ? 51.097 3.622   17.792  1.00 30.97  ? 50  LYS A CG  1 
ATOM   194  C CD  . LYS A 1 33  ? 52.342 3.321   18.596  1.00 29.43  ? 50  LYS A CD  1 
ATOM   195  C CE  . LYS A 1 33  ? 52.143 3.603   20.083  1.00 38.76  ? 50  LYS A CE  1 
ATOM   196  N NZ  . LYS A 1 33  ? 50.836 3.273   20.622  1.00 37.35  ? 50  LYS A NZ  1 
ATOM   197  N N   . GLU A 1 34  ? 50.444 0.798   15.442  1.00 23.74  ? 51  GLU A N   1 
ATOM   198  C CA  . GLU A 1 34  ? 49.675 -0.379  15.785  1.00 25.09  ? 51  GLU A CA  1 
ATOM   199  C C   . GLU A 1 34  ? 50.424 -1.684  15.531  1.00 29.91  ? 51  GLU A C   1 
ATOM   200  O O   . GLU A 1 34  ? 49.925 -2.737  15.938  1.00 28.18  ? 51  GLU A O   1 
ATOM   201  C CB  . GLU A 1 34  ? 48.355 -0.346  15.033  1.00 24.12  ? 51  GLU A CB  1 
ATOM   202  C CG  . GLU A 1 34  ? 47.403 0.796   15.421  1.00 25.83  ? 51  GLU A CG  1 
ATOM   203  C CD  . GLU A 1 34  ? 47.738 2.166   14.865  1.00 36.57  ? 51  GLU A CD  1 
ATOM   204  O OE1 . GLU A 1 34  ? 48.513 2.296   13.883  1.00 35.46  ? 51  GLU A OE1 1 
ATOM   205  O OE2 . GLU A 1 34  ? 47.203 3.135   15.441  1.00 34.89  ? 51  GLU A OE2 1 
ATOM   206  N N   . MET A 1 35  ? 51.602 -1.658  14.902  1.00 25.52  ? 52  MET A N   1 
ATOM   207  C CA  . MET A 1 35  ? 52.419 -2.865  14.792  1.00 25.27  ? 52  MET A CA  1 
ATOM   208  C C   . MET A 1 35  ? 53.445 -3.017  15.914  1.00 23.18  ? 52  MET A C   1 
ATOM   209  O O   . MET A 1 35  ? 54.084 -4.063  16.001  1.00 27.44  ? 52  MET A O   1 
ATOM   210  C CB  . MET A 1 35  ? 53.148 -2.891  13.434  1.00 25.52  ? 52  MET A CB  1 
ATOM   211  C CG  . MET A 1 35  ? 52.308 -3.291  12.256  1.00 24.13  ? 52  MET A CG  1 
ATOM   212  S SD  . MET A 1 35  ? 51.649 -4.945  12.425  1.00 25.33  ? 52  MET A SD  1 
ATOM   213  C CE  . MET A 1 35  ? 53.142 -5.905  12.558  1.00 28.91  ? 52  MET A CE  1 
ATOM   214  N N   . LEU A 1 36  ? 53.600 -2.049  16.808  1.00 23.79  ? 53  LEU A N   1 
ATOM   215  C CA  . LEU A 1 36  ? 54.473 -2.272  17.958  1.00 27.52  ? 53  LEU A CA  1 
ATOM   216  C C   . LEU A 1 36  ? 53.899 -3.377  18.841  1.00 27.44  ? 53  LEU A C   1 
ATOM   217  O O   . LEU A 1 36  ? 52.682 -3.411  19.098  1.00 27.46  ? 53  LEU A O   1 
ATOM   218  C CB  . LEU A 1 36  ? 54.637 -1.000  18.792  1.00 26.23  ? 53  LEU A CB  1 
ATOM   219  C CG  . LEU A 1 36  ? 55.244 0.164   18.010  1.00 29.18  ? 53  LEU A CG  1 
ATOM   220  C CD1 . LEU A 1 36  ? 55.556 1.325   18.939  1.00 36.13  ? 53  LEU A CD1 1 
ATOM   221  C CD2 . LEU A 1 36  ? 56.478 -0.286  17.235  1.00 33.24  ? 53  LEU A CD2 1 
ATOM   222  N N   . PRO A 1 37  ? 54.742 -4.279  19.328  1.00 24.19  ? 54  PRO A N   1 
ATOM   223  C CA  . PRO A 1 37  ? 54.276 -5.379  20.163  1.00 30.69  ? 54  PRO A CA  1 
ATOM   224  C C   . PRO A 1 37  ? 54.147 -5.047  21.641  1.00 28.05  ? 54  PRO A C   1 
ATOM   225  O O   . PRO A 1 37  ? 54.818 -4.171  22.177  1.00 24.68  ? 54  PRO A O   1 
ATOM   226  C CB  . PRO A 1 37  ? 55.379 -6.427  19.958  1.00 25.69  ? 54  PRO A CB  1 
ATOM   227  C CG  . PRO A 1 37  ? 56.576 -5.647  19.768  1.00 29.59  ? 54  PRO A CG  1 
ATOM   228  C CD  . PRO A 1 37  ? 56.165 -4.443  18.970  1.00 29.04  ? 54  PRO A CD  1 
ATOM   229  N N   . VAL A 1 38  ? 53.253 -5.764  22.284  1.00 26.50  ? 55  VAL A N   1 
ATOM   230  C CA  . VAL A 1 38  ? 53.172 -5.840  23.736  1.00 30.55  ? 55  VAL A CA  1 
ATOM   231  C C   . VAL A 1 38  ? 53.605 -7.260  24.067  1.00 35.06  ? 55  VAL A C   1 
ATOM   232  O O   . VAL A 1 38  ? 52.883 -8.230  23.796  1.00 32.29  ? 55  VAL A O   1 
ATOM   233  C CB  . VAL A 1 38  ? 51.775 -5.494  24.254  1.00 28.64  ? 55  VAL A CB  1 
ATOM   234  C CG1 . VAL A 1 38  ? 51.666 -5.691  25.799  1.00 26.98  ? 55  VAL A CG1 1 
ATOM   235  C CG2 . VAL A 1 38  ? 51.449 -4.038  23.920  1.00 26.57  ? 55  VAL A CG2 1 
ATOM   236  N N   . VAL A 1 39  ? 54.834 -7.364  24.575  1.00 31.24  ? 56  VAL A N   1 
ATOM   237  C CA  . VAL A 1 39  ? 55.570 -8.610  24.769  1.00 30.91  ? 56  VAL A CA  1 
ATOM   238  C C   . VAL A 1 39  ? 55.856 -9.278  23.428  1.00 33.93  ? 56  VAL A C   1 
ATOM   239  O O   . VAL A 1 39  ? 56.917 -9.067  22.842  1.00 37.89  ? 56  VAL A O   1 
ATOM   240  C CB  . VAL A 1 39  ? 54.820 -9.542  25.730  1.00 32.30  ? 56  VAL A CB  1 
ATOM   241  C CG1 . VAL A 1 39  ? 55.627 -10.783 25.997  1.00 40.76  ? 56  VAL A CG1 1 
ATOM   242  C CG2 . VAL A 1 39  ? 54.568 -8.818  27.010  1.00 41.38  ? 56  VAL A CG2 1 
ATOM   243  N N   . ASP A 1 40  ? 54.947 -10.110 22.937  1.00 32.36  ? 57  ASP A N   1 
ATOM   244  C CA  . ASP A 1 40  ? 55.230 -10.884 21.730  1.00 31.36  ? 57  ASP A CA  1 
ATOM   245  C C   . ASP A 1 40  ? 54.181 -10.706 20.638  1.00 32.10  ? 57  ASP A C   1 
ATOM   246  O O   . ASP A 1 40  ? 54.130 -11.513 19.700  1.00 29.29  ? 57  ASP A O   1 
ATOM   247  C CB  . ASP A 1 40  ? 55.341 -12.370 22.090  1.00 35.46  ? 57  ASP A CB  1 
ATOM   248  C CG  . ASP A 1 40  ? 54.048 -12.927 22.701  1.00 35.62  ? 57  ASP A CG  1 
ATOM   249  O OD1 . ASP A 1 40  ? 53.049 -12.175 22.885  1.00 34.08  ? 57  ASP A OD1 1 
ATOM   250  O OD2 . ASP A 1 40  ? 54.025 -14.139 22.960  1.00 39.67  ? 57  ASP A OD2 1 
ATOM   251  N N   . LYS A 1 41  ? 53.337 -9.673  20.727  1.00 30.24  ? 58  LYS A N   1 
ATOM   252  C CA  . LYS A 1 41  ? 52.170 -9.582  19.868  1.00 31.23  ? 58  LYS A CA  1 
ATOM   253  C C   . LYS A 1 41  ? 51.882 -8.133  19.492  1.00 28.17  ? 58  LYS A C   1 
ATOM   254  O O   . LYS A 1 41  ? 51.789 -7.280  20.379  1.00 26.13  ? 58  LYS A O   1 
ATOM   255  C CB  . LYS A 1 41  ? 50.961 -10.213 20.585  1.00 32.86  ? 58  LYS A CB  1 
ATOM   256  C CG  . LYS A 1 41  ? 49.731 -10.239 19.761  1.00 28.86  ? 58  LYS A CG  1 
ATOM   257  C CD  . LYS A 1 41  ? 48.542 -10.888 20.395  1.00 31.94  ? 58  LYS A CD  1 
ATOM   258  C CE  . LYS A 1 41  ? 48.697 -12.375 20.525  1.00 37.33  ? 58  LYS A CE  1 
ATOM   259  N NZ  . LYS A 1 41  ? 47.505 -12.961 21.225  1.00 46.96  ? 58  LYS A NZ  1 
ATOM   260  N N   . PRO A 1 42  ? 51.755 -7.813  18.200  1.00 27.45  ? 59  PRO A N   1 
ATOM   261  C CA  . PRO A 1 42  ? 51.479 -6.423  17.817  1.00 24.53  ? 59  PRO A CA  1 
ATOM   262  C C   . PRO A 1 42  ? 50.155 -5.945  18.391  1.00 21.51  ? 59  PRO A C   1 
ATOM   263  O O   . PRO A 1 42  ? 49.180 -6.691  18.447  1.00 22.36  ? 59  PRO A O   1 
ATOM   264  C CB  . PRO A 1 42  ? 51.418 -6.471  16.281  1.00 27.21  ? 59  PRO A CB  1 
ATOM   265  C CG  . PRO A 1 42  ? 52.037 -7.764  15.899  1.00 29.56  ? 59  PRO A CG  1 
ATOM   266  C CD  . PRO A 1 42  ? 51.841 -8.703  17.034  1.00 33.01  ? 59  PRO A CD  1 
ATOM   267  N N   . LEU A 1 43  ? 50.100 -4.669  18.768  1.00 25.41  ? 60  LEU A N   1 
ATOM   268  C CA  . LEU A 1 43  ? 48.823 -4.124  19.214  1.00 22.73  ? 60  LEU A CA  1 
ATOM   269  C C   . LEU A 1 43  ? 47.670 -4.524  18.295  1.00 25.75  ? 60  LEU A C   1 
ATOM   270  O O   . LEU A 1 43  ? 46.635 -4.999  18.765  1.00 22.47  ? 60  LEU A O   1 
ATOM   271  C CB  . LEU A 1 43  ? 48.917 -2.611  19.327  1.00 22.92  ? 60  LEU A CB  1 
ATOM   272  C CG  . LEU A 1 43  ? 49.722 -2.080  20.521  1.00 29.42  ? 60  LEU A CG  1 
ATOM   273  C CD1 . LEU A 1 43  ? 50.128 -0.630  20.302  1.00 28.38  ? 60  LEU A CD1 1 
ATOM   274  C CD2 . LEU A 1 43  ? 48.902 -2.246  21.830  1.00 26.67  ? 60  LEU A CD2 1 
ATOM   275  N N   . ILE A 1 44  ? 47.831 -4.367  16.968  1.00 23.09  ? 61  ILE A N   1 
ATOM   276  C CA  . ILE A 1 44  ? 46.722 -4.640  16.056  1.00 19.95  ? 61  ILE A CA  1 
ATOM   277  C C   . ILE A 1 44  ? 46.252 -6.078  16.166  1.00 20.40  ? 61  ILE A C   1 
ATOM   278  O O   . ILE A 1 44  ? 45.065 -6.361  15.986  1.00 20.23  ? 61  ILE A O   1 
ATOM   279  C CB  . ILE A 1 44  ? 47.117 -4.266  14.587  1.00 22.14  ? 61  ILE A CB  1 
ATOM   280  C CG1 . ILE A 1 44  ? 45.932 -4.459  13.641  1.00 23.65  ? 61  ILE A CG1 1 
ATOM   281  C CG2 . ILE A 1 44  ? 48.305 -5.090  14.099  1.00 23.64  ? 61  ILE A CG2 1 
ATOM   282  C CD1 . ILE A 1 44  ? 44.695 -3.667  14.048  1.00 23.60  ? 61  ILE A CD1 1 
ATOM   283  N N   . GLN A 1 45  ? 47.148 -7.026  16.449  1.00 22.76  ? 62  GLN A N   1 
ATOM   284  C CA  . GLN A 1 45  ? 46.689 -8.406  16.501  1.00 22.30  ? 62  GLN A CA  1 
ATOM   285  C C   . GLN A 1 45  ? 45.769 -8.650  17.706  1.00 25.47  ? 62  GLN A C   1 
ATOM   286  O O   . GLN A 1 45  ? 44.803 -9.417  17.598  1.00 25.02  ? 62  GLN A O   1 
ATOM   287  C CB  . GLN A 1 45  ? 47.860 -9.382  16.508  1.00 26.85  ? 62  GLN A CB  1 
ATOM   288  C CG  . GLN A 1 45  ? 47.364 -10.826 16.423  1.00 27.17  ? 62  GLN A CG  1 
ATOM   289  C CD  . GLN A 1 45  ? 48.471 -11.845 16.237  1.00 36.40  ? 62  GLN A CD  1 
ATOM   290  O OE1 . GLN A 1 45  ? 49.558 -11.535 15.728  1.00 29.71  ? 62  GLN A OE1 1 
ATOM   291  N NE2 . GLN A 1 45  ? 48.209 -13.068 16.674  1.00 32.11  ? 62  GLN A NE2 1 
ATOM   292  N N   . TYR A 1 46  ? 46.027 -7.993  18.848  1.00 23.59  ? 63  TYR A N   1 
ATOM   293  C CA  . TYR A 1 46  ? 45.085 -8.117  19.966  1.00 23.12  ? 63  TYR A CA  1 
ATOM   294  C C   . TYR A 1 46  ? 43.698 -7.644  19.548  1.00 23.06  ? 63  TYR A C   1 
ATOM   295  O O   . TYR A 1 46  ? 42.696 -8.287  19.854  1.00 24.17  ? 63  TYR A O   1 
ATOM   296  C CB  . TYR A 1 46  ? 45.537 -7.295  21.181  1.00 28.35  ? 63  TYR A CB  1 
ATOM   297  C CG  . TYR A 1 46  ? 46.778 -7.765  21.921  1.00 26.20  ? 63  TYR A CG  1 
ATOM   298  C CD1 . TYR A 1 46  ? 46.688 -8.642  23.010  1.00 30.18  ? 63  TYR A CD1 1 
ATOM   299  C CD2 . TYR A 1 46  ? 48.022 -7.253  21.586  1.00 25.12  ? 63  TYR A CD2 1 
ATOM   300  C CE1 . TYR A 1 46  ? 47.824 -9.033  23.712  1.00 27.32  ? 63  TYR A CE1 1 
ATOM   301  C CE2 . TYR A 1 46  ? 49.148 -7.652  22.256  1.00 29.73  ? 63  TYR A CE2 1 
ATOM   302  C CZ  . TYR A 1 46  ? 49.052 -8.529  23.330  1.00 32.50  ? 63  TYR A CZ  1 
ATOM   303  O OH  . TYR A 1 46  ? 50.205 -8.888  24.002  1.00 32.66  ? 63  TYR A OH  1 
ATOM   304  N N   . ALA A 1 47  ? 43.633 -6.535  18.802  1.00 23.37  ? 64  ALA A N   1 
ATOM   305  C CA  . ALA A 1 47  ? 42.345 -5.992  18.401  1.00 22.74  ? 64  ALA A CA  1 
ATOM   306  C C   . ALA A 1 47  ? 41.673 -6.866  17.351  1.00 21.73  ? 64  ALA A C   1 
ATOM   307  O O   . ALA A 1 47  ? 40.460 -7.084  17.400  1.00 22.92  ? 64  ALA A O   1 
ATOM   308  C CB  . ALA A 1 47  ? 42.519 -4.569  17.909  1.00 21.51  ? 64  ALA A CB  1 
ATOM   309  N N   . VAL A 1 48  ? 42.443 -7.404  16.422  1.00 25.21  ? 65  VAL A N   1 
ATOM   310  C CA  . VAL A 1 48  ? 41.880 -8.325  15.444  1.00 24.39  ? 65  VAL A CA  1 
ATOM   311  C C   . VAL A 1 48  ? 41.342 -9.580  16.133  1.00 24.49  ? 65  VAL A C   1 
ATOM   312  O O   . VAL A 1 48  ? 40.258 -10.080 15.794  1.00 25.81  ? 65  VAL A O   1 
ATOM   313  C CB  . VAL A 1 48  ? 42.945 -8.662  14.377  1.00 25.47  ? 65  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 48  ? 42.512 -9.887  13.578  1.00 23.49  ? 65  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 48  ? 43.181 -7.459  13.436  1.00 27.13  ? 65  VAL A CG2 1 
ATOM   316  N N   . GLU A 1 49  ? 42.080 -10.117 17.098  1.00 26.59  ? 66  GLU A N   1 
ATOM   317  C CA  . GLU A 1 49  ? 41.607 -11.324 17.790  1.00 29.00  ? 66  GLU A CA  1 
ATOM   318  C C   . GLU A 1 49  ? 40.301 -11.060 18.548  1.00 25.48  ? 66  GLU A C   1 
ATOM   319  O O   . GLU A 1 49  ? 39.369 -11.877 18.519  1.00 25.62  ? 66  GLU A O   1 
ATOM   320  C CB  . GLU A 1 49  ? 42.691 -11.837 18.719  1.00 27.54  ? 66  GLU A CB  1 
ATOM   321  C CG  . GLU A 1 49  ? 43.804 -12.541 17.954  1.00 34.50  ? 66  GLU A CG  1 
ATOM   322  C CD  . GLU A 1 49  ? 45.039 -12.888 18.801  1.00 37.61  ? 66  GLU A CD  1 
ATOM   323  O OE1 . GLU A 1 49  ? 45.127 -12.443 19.966  1.00 39.54  ? 66  GLU A OE1 1 
ATOM   324  O OE2 . GLU A 1 49  ? 45.936 -13.596 18.275  1.00 40.13  ? 66  GLU A OE2 1 
ATOM   325  N N   . GLU A 1 50  ? 40.183 -9.894  19.156  1.00 23.38  ? 67  GLU A N   1 
ATOM   326  C CA  . GLU A 1 50  ? 38.918 -9.515  19.774  1.00 25.76  ? 67  GLU A CA  1 
ATOM   327  C C   . GLU A 1 50  ? 37.795 -9.452  18.748  1.00 24.59  ? 67  GLU A C   1 
ATOM   328  O O   . GLU A 1 50  ? 36.690 -9.981  18.977  1.00 24.64  ? 67  GLU A O   1 
ATOM   329  C CB  . GLU A 1 50  ? 39.076 -8.169  20.477  1.00 21.88  ? 67  GLU A CB  1 
ATOM   330  C CG  . GLU A 1 50  ? 37.788 -7.622  21.077  1.00 27.84  ? 67  GLU A CG  1 
ATOM   331  C CD  . GLU A 1 50  ? 37.952 -6.239  21.704  1.00 30.74  ? 67  GLU A CD  1 
ATOM   332  O OE1 . GLU A 1 50  ? 39.052 -5.937  22.229  1.00 28.01  ? 67  GLU A OE1 1 
ATOM   333  O OE2 . GLU A 1 50  ? 36.969 -5.451  21.665  1.00 27.38  ? 67  GLU A OE2 1 
ATOM   334  N N   . ALA A 1 51  ? 38.051 -8.816  17.601  1.00 28.63  ? 68  ALA A N   1 
ATOM   335  C CA  . ALA A 1 51  ? 37.005 -8.690  16.588  1.00 23.63  ? 68  ALA A CA  1 
ATOM   336  C C   . ALA A 1 51  ? 36.551 -10.065 16.106  1.00 26.67  ? 68  ALA A C   1 
ATOM   337  O O   . ALA A 1 51  ? 35.347 -10.337 16.012  1.00 23.32  ? 68  ALA A O   1 
ATOM   338  C CB  . ALA A 1 51  ? 37.510 -7.839  15.414  1.00 27.86  ? 68  ALA A CB  1 
ATOM   339  N N   . VAL A 1 52  ? 37.505 -10.961 15.856  1.00 26.68  ? 69  VAL A N   1 
ATOM   340  C CA  . VAL A 1 52  ? 37.178 -12.294 15.368  1.00 28.38  ? 69  VAL A CA  1 
ATOM   341  C C   . VAL A 1 52  ? 36.423 -13.081 16.427  1.00 28.16  ? 69  VAL A C   1 
ATOM   342  O O   . VAL A 1 52  ? 35.441 -13.774 16.120  1.00 29.48  ? 69  VAL A O   1 
ATOM   343  C CB  . VAL A 1 52  ? 38.472 -13.017 14.926  1.00 26.72  ? 69  VAL A CB  1 
ATOM   344  C CG1 . VAL A 1 52  ? 38.178 -14.470 14.604  1.00 30.26  ? 69  VAL A CG1 1 
ATOM   345  C CG2 . VAL A 1 52  ? 39.062 -12.337 13.734  1.00 31.40  ? 69  VAL A CG2 1 
ATOM   346  N N   . ALA A 1 53  ? 36.862 -12.985 17.692  1.00 26.20  ? 70  ALA A N   1 
ATOM   347  C CA  . ALA A 1 53  ? 36.151 -13.651 18.775  1.00 25.64  ? 70  ALA A CA  1 
ATOM   348  C C   . ALA A 1 53  ? 34.729 -13.138 18.910  1.00 32.10  ? 70  ALA A C   1 
ATOM   349  O O   . ALA A 1 53  ? 33.861 -13.880 19.390  1.00 32.89  ? 70  ALA A O   1 
ATOM   350  C CB  . ALA A 1 53  ? 36.889 -13.478 20.108  1.00 30.99  ? 70  ALA A CB  1 
ATOM   351  N N   . ALA A 1 54  ? 34.464 -11.908 18.463  1.00 30.32  ? 71  ALA A N   1 
ATOM   352  C CA  . ALA A 1 54  ? 33.131 -11.312 18.476  1.00 28.11  ? 71  ALA A CA  1 
ATOM   353  C C   . ALA A 1 54  ? 32.318 -11.584 17.213  1.00 33.50  ? 71  ALA A C   1 
ATOM   354  O O   . ALA A 1 54  ? 31.230 -11.013 17.067  1.00 29.88  ? 71  ALA A O   1 
ATOM   355  C CB  . ALA A 1 54  ? 33.237 -9.797  18.672  1.00 28.18  ? 71  ALA A CB  1 
ATOM   356  N N   . GLY A 1 55  ? 32.798 -12.448 16.312  1.00 30.94  ? 72  GLY A N   1 
ATOM   357  C CA  . GLY A 1 55  ? 32.040 -12.834 15.140  1.00 34.80  ? 72  GLY A CA  1 
ATOM   358  C C   . GLY A 1 55  ? 32.345 -12.065 13.871  1.00 32.00  ? 72  GLY A C   1 
ATOM   359  O O   . GLY A 1 55  ? 31.708 -12.316 12.851  1.00 32.32  ? 72  GLY A O   1 
ATOM   360  N N   . ILE A 1 56  ? 33.330 -11.175 13.884  1.00 30.54  ? 73  ILE A N   1 
ATOM   361  C CA  . ILE A 1 56  ? 33.690 -10.474 12.668  1.00 30.70  ? 73  ILE A CA  1 
ATOM   362  C C   . ILE A 1 56  ? 34.355 -11.443 11.708  1.00 28.55  ? 73  ILE A C   1 
ATOM   363  O O   . ILE A 1 56  ? 35.231 -12.231 12.095  1.00 31.96  ? 73  ILE A O   1 
ATOM   364  C CB  . ILE A 1 56  ? 34.626 -9.298  12.975  1.00 25.93  ? 73  ILE A CB  1 
ATOM   365  C CG1 . ILE A 1 56  ? 33.976 -8.286  13.913  1.00 27.81  ? 73  ILE A CG1 1 
ATOM   366  C CG2 . ILE A 1 56  ? 35.007 -8.623  11.699  1.00 26.17  ? 73  ILE A CG2 1 
ATOM   367  C CD1 . ILE A 1 56  ? 32.711 -7.650  13.406  1.00 27.08  ? 73  ILE A CD1 1 
ATOM   368  N N   . THR A 1 57  ? 33.965 -11.363 10.444  1.00 32.46  ? 74  THR A N   1 
ATOM   369  C CA  . THR A 1 57  ? 34.576 -12.151 9.399   1.00 30.85  ? 74  THR A CA  1 
ATOM   370  C C   . THR A 1 57  ? 35.284 -11.318 8.343   1.00 29.55  ? 74  THR A C   1 
ATOM   371  O O   . THR A 1 57  ? 36.101 -11.878 7.601   1.00 29.20  ? 74  THR A O   1 
ATOM   372  C CB  . THR A 1 57  ? 33.521 -13.014 8.701   1.00 32.87  ? 74  THR A CB  1 
ATOM   373  O OG1 . THR A 1 57  ? 32.551 -12.144 8.145   1.00 31.14  ? 74  THR A OG1 1 
ATOM   374  C CG2 . THR A 1 57  ? 32.848 -13.991 9.675   1.00 38.01  ? 74  THR A CG2 1 
ATOM   375  N N   . ASP A 1 58  ? 34.985 -10.018 8.227   1.00 29.46  ? 75  ASP A N   1 
ATOM   376  C CA  . ASP A 1 58  ? 35.596 -9.156  7.216   1.00 30.93  ? 75  ASP A CA  1 
ATOM   377  C C   . ASP A 1 58  ? 36.419 -8.080  7.916   1.00 29.40  ? 75  ASP A C   1 
ATOM   378  O O   . ASP A 1 58  ? 35.858 -7.197  8.566   1.00 30.33  ? 75  ASP A O   1 
ATOM   379  C CB  . ASP A 1 58  ? 34.548 -8.494  6.321   1.00 34.35  ? 75  ASP A CB  1 
ATOM   380  C CG  . ASP A 1 58  ? 33.678 -9.486  5.598   1.00 40.43  ? 75  ASP A CG  1 
ATOM   381  O OD1 . ASP A 1 58  ? 33.977 -10.694 5.655   1.00 39.13  ? 75  ASP A OD1 1 
ATOM   382  O OD2 . ASP A 1 58  ? 32.674 -9.032  5.006   1.00 40.18  ? 75  ASP A OD2 1 
ATOM   383  N N   . LEU A 1 59  ? 37.735 -8.147  7.778   1.00 24.70  ? 76  LEU A N   1 
ATOM   384  C CA  . LEU A 1 59  ? 38.630 -7.155  8.342   1.00 23.38  ? 76  LEU A CA  1 
ATOM   385  C C   . LEU A 1 59  ? 38.981 -6.141  7.258   1.00 24.99  ? 76  LEU A C   1 
ATOM   386  O O   . LEU A 1 59  ? 39.311 -6.522  6.128   1.00 26.96  ? 76  LEU A O   1 
ATOM   387  C CB  . LEU A 1 59  ? 39.899 -7.815  8.870   1.00 23.69  ? 76  LEU A CB  1 
ATOM   388  C CG  . LEU A 1 59  ? 39.738 -9.084  9.704   1.00 28.84  ? 76  LEU A CG  1 
ATOM   389  C CD1 . LEU A 1 59  ? 41.109 -9.623  10.066  1.00 27.12  ? 76  LEU A CD1 1 
ATOM   390  C CD2 . LEU A 1 59  ? 38.910 -8.815  10.954  1.00 25.47  ? 76  LEU A CD2 1 
ATOM   391  N N   . ILE A 1 60  ? 38.937 -4.859  7.620   1.00 27.19  ? 77  ILE A N   1 
ATOM   392  C CA  . ILE A 1 60  ? 39.240 -3.744  6.736   1.00 24.70  ? 77  ILE A CA  1 
ATOM   393  C C   . ILE A 1 60  ? 40.327 -2.920  7.419   1.00 25.43  ? 77  ILE A C   1 
ATOM   394  O O   . ILE A 1 60  ? 40.103 -2.319  8.483   1.00 22.86  ? 77  ILE A O   1 
ATOM   395  C CB  . ILE A 1 60  ? 37.993 -2.888  6.441   1.00 26.80  ? 77  ILE A CB  1 
ATOM   396  C CG1 . ILE A 1 60  ? 36.939 -3.740  5.772   1.00 25.53  ? 77  ILE A CG1 1 
ATOM   397  C CG2 . ILE A 1 60  ? 38.329 -1.667  5.578   1.00 22.10  ? 77  ILE A CG2 1 
ATOM   398  C CD1 . ILE A 1 60  ? 35.574 -3.109  5.761   1.00 28.02  ? 77  ILE A CD1 1 
ATOM   399  N N   . PHE A 1 61  ? 41.503 -2.928  6.833   1.00 23.42  ? 78  PHE A N   1 
ATOM   400  C CA  . PHE A 1 61  ? 42.662 -2.215  7.340   1.00 20.62  ? 78  PHE A CA  1 
ATOM   401  C C   . PHE A 1 61  ? 42.827 -0.938  6.537   1.00 23.24  ? 78  PHE A C   1 
ATOM   402  O O   . PHE A 1 61  ? 43.003 -0.993  5.307   1.00 23.76  ? 78  PHE A O   1 
ATOM   403  C CB  . PHE A 1 61  ? 43.915 -3.074  7.198   1.00 22.67  ? 78  PHE A CB  1 
ATOM   404  C CG  . PHE A 1 61  ? 43.909 -4.307  8.037   1.00 20.34  ? 78  PHE A CG  1 
ATOM   405  C CD1 . PHE A 1 61  ? 44.042 -4.209  9.442   1.00 25.22  ? 78  PHE A CD1 1 
ATOM   406  C CD2 . PHE A 1 61  ? 43.789 -5.553  7.459   1.00 22.69  ? 78  PHE A CD2 1 
ATOM   407  C CE1 . PHE A 1 61  ? 44.043 -5.352  10.225  1.00 21.91  ? 78  PHE A CE1 1 
ATOM   408  C CE2 . PHE A 1 61  ? 43.797 -6.705  8.251   1.00 25.20  ? 78  PHE A CE2 1 
ATOM   409  C CZ  . PHE A 1 61  ? 43.914 -6.593  9.635   1.00 23.13  ? 78  PHE A CZ  1 
ATOM   410  N N   . VAL A 1 62  ? 42.839 0.198   7.226   1.00 22.69  ? 79  VAL A N   1 
ATOM   411  C CA  . VAL A 1 62  ? 43.075 1.488   6.593   1.00 21.84  ? 79  VAL A CA  1 
ATOM   412  C C   . VAL A 1 62  ? 44.517 1.867   6.863   1.00 25.21  ? 79  VAL A C   1 
ATOM   413  O O   . VAL A 1 62  ? 44.910 2.135   8.006   1.00 21.72  ? 79  VAL A O   1 
ATOM   414  C CB  . VAL A 1 62  ? 42.080 2.538   7.081   1.00 23.04  ? 79  VAL A CB  1 
ATOM   415  C CG1 . VAL A 1 62  ? 42.375 3.904   6.490   1.00 19.86  ? 79  VAL A CG1 1 
ATOM   416  C CG2 . VAL A 1 62  ? 40.666 2.101   6.738   1.00 25.91  ? 79  VAL A CG2 1 
ATOM   417  N N   . THR A 1 63  ? 45.318 1.864   5.801   1.00 23.22  ? 80  THR A N   1 
ATOM   418  C CA  . THR A 1 63  ? 46.762 1.960   5.906   1.00 26.07  ? 80  THR A CA  1 
ATOM   419  C C   . THR A 1 63  ? 47.247 3.342   5.500   1.00 25.56  ? 80  THR A C   1 
ATOM   420  O O   . THR A 1 63  ? 46.539 4.132   4.877   1.00 26.70  ? 80  THR A O   1 
ATOM   421  C CB  . THR A 1 63  ? 47.440 0.903   5.028   1.00 25.03  ? 80  THR A CB  1 
ATOM   422  O OG1 . THR A 1 63  ? 47.154 1.192   3.658   1.00 29.14  ? 80  THR A OG1 1 
ATOM   423  C CG2 . THR A 1 63  ? 46.917 -0.433  5.345   1.00 24.32  ? 80  THR A CG2 1 
ATOM   424  N N   . GLY A 1 64  ? 48.487 3.622   5.867   1.00 29.86  ? 81  GLY A N   1 
ATOM   425  C CA  . GLY A 1 64  ? 49.135 4.854   5.476   1.00 29.10  ? 81  GLY A CA  1 
ATOM   426  C C   . GLY A 1 64  ? 50.539 4.523   5.025   1.00 32.95  ? 81  GLY A C   1 
ATOM   427  O O   . GLY A 1 64  ? 50.726 3.593   4.239   1.00 32.52  ? 81  GLY A O   1 
ATOM   428  N N   . ARG A 1 65  ? 51.545 5.223   5.515   1.00 37.25  ? 82  ARG A N   1 
ATOM   429  C CA  . ARG A 1 65  ? 52.864 4.767   5.114   1.00 51.74  ? 82  ARG A CA  1 
ATOM   430  C C   . ARG A 1 65  ? 53.253 3.536   5.939   1.00 38.35  ? 82  ARG A C   1 
ATOM   431  O O   . ARG A 1 65  ? 52.651 3.210   6.967   1.00 47.96  ? 82  ARG A O   1 
ATOM   432  C CB  . ARG A 1 65  ? 53.916 5.878   5.213   1.00 64.90  ? 82  ARG A CB  1 
ATOM   433  C CG  . ARG A 1 65  ? 53.976 6.670   6.509   1.00 62.31  ? 82  ARG A CG  1 
ATOM   434  C CD  . ARG A 1 65  ? 55.083 7.768   6.422   1.00 70.47  ? 82  ARG A CD  1 
ATOM   435  N NE  . ARG A 1 65  ? 56.357 7.236   5.931   1.00 70.87  ? 82  ARG A NE  1 
ATOM   436  C CZ  . ARG A 1 65  ? 57.301 6.667   6.680   1.00 55.50  ? 82  ARG A CZ  1 
ATOM   437  N NH1 . ARG A 1 65  ? 57.220 6.636   8.004   1.00 55.09  ? 82  ARG A NH1 1 
ATOM   438  N NH2 . ARG A 1 65  ? 58.346 6.097   6.085   1.00 55.91  ? 82  ARG A NH2 1 
ATOM   439  N N   . ASN A 1 66  ? 54.222 2.802   5.420   1.00 49.07  ? 83  ASN A N   1 
ATOM   440  C CA  . ASN A 1 66  ? 54.619 1.537   6.018   1.00 44.21  ? 83  ASN A CA  1 
ATOM   441  C C   . ASN A 1 66  ? 53.456 0.550   6.019   1.00 34.52  ? 83  ASN A C   1 
ATOM   442  O O   . ASN A 1 66  ? 53.340 -0.304  6.898   1.00 39.44  ? 83  ASN A O   1 
ATOM   443  C CB  . ASN A 1 66  ? 55.179 1.758   7.430   1.00 45.34  ? 83  ASN A CB  1 
ATOM   444  C CG  . ASN A 1 66  ? 56.425 2.621   7.418   1.00 43.80  ? 83  ASN A CG  1 
ATOM   445  O OD1 . ASN A 1 66  ? 57.366 2.365   6.662   1.00 47.12  ? 83  ASN A OD1 1 
ATOM   446  N ND2 . ASN A 1 66  ? 56.417 3.669   8.214   1.00 38.66  ? 83  ASN A ND2 1 
ATOM   447  N N   . LYS A 1 67  ? 52.603 0.637   5.000   1.00 27.01  ? 84  LYS A N   1 
ATOM   448  C CA  . LYS A 1 67  ? 51.521 -0.334  4.858   1.00 26.67  ? 84  LYS A CA  1 
ATOM   449  C C   . LYS A 1 67  ? 52.059 -1.767  4.829   1.00 27.94  ? 84  LYS A C   1 
ATOM   450  O O   . LYS A 1 67  ? 51.365 -2.705  5.240   1.00 29.00  ? 84  LYS A O   1 
ATOM   451  C CB  . LYS A 1 67  ? 50.742 -0.011  3.585   1.00 34.28  ? 84  LYS A CB  1 
ATOM   452  C CG  . LYS A 1 67  ? 51.588 -0.225  2.319   1.00 27.60  ? 84  LYS A CG  1 
ATOM   453  C CD  . LYS A 1 67  ? 51.122 0.664   1.135   1.00 41.76  ? 84  LYS A CD  1 
ATOM   454  C CE  . LYS A 1 67  ? 51.727 0.144   -0.199  1.00 37.63  ? 84  LYS A CE  1 
ATOM   455  N NZ  . LYS A 1 67  ? 51.933 1.157   -1.320  1.00 47.04  ? 84  LYS A NZ  1 
ATOM   456  N N   . ARG A 1 68  ? 53.303 -1.942  4.372   1.00 25.76  ? 85  ARG A N   1 
ATOM   457  C CA  . ARG A 1 68  ? 53.945 -3.255  4.267   1.00 31.07  ? 85  ARG A CA  1 
ATOM   458  C C   . ARG A 1 68  ? 53.889 -4.037  5.568   1.00 25.80  ? 85  ARG A C   1 
ATOM   459  O O   . ARG A 1 68  ? 53.647 -5.250  5.573   1.00 27.35  ? 85  ARG A O   1 
ATOM   460  C CB  . ARG A 1 68  ? 55.433 -3.082  3.870   1.00 38.25  ? 85  ARG A CB  1 
ATOM   461  C CG  . ARG A 1 68  ? 56.286 -4.407  3.892   1.00 43.86  ? 85  ARG A CG  1 
ATOM   462  C CD  . ARG A 1 68  ? 57.800 -4.186  4.071   1.00 42.39  ? 85  ARG A CD  1 
ATOM   463  N NE  . ARG A 1 68  ? 58.045 -3.587  5.370   1.00 50.59  ? 85  ARG A NE  1 
ATOM   464  C CZ  . ARG A 1 68  ? 57.968 -4.231  6.532   1.00 45.66  ? 85  ARG A CZ  1 
ATOM   465  N NH1 . ARG A 1 68  ? 57.750 -5.550  6.598   1.00 46.45  ? 85  ARG A NH1 1 
ATOM   466  N NH2 . ARG A 1 68  ? 58.111 -3.536  7.655   1.00 46.72  ? 85  ARG A NH2 1 
ATOM   467  N N   . ALA A 1 69  ? 54.212 -3.373  6.675   1.00 25.40  ? 86  ALA A N   1 
ATOM   468  C CA  . ALA A 1 69  ? 54.279 -4.059  7.965   1.00 23.34  ? 86  ALA A CA  1 
ATOM   469  C C   . ALA A 1 69  ? 52.944 -4.683  8.327   1.00 23.34  ? 86  ALA A C   1 
ATOM   470  O O   . ALA A 1 69  ? 52.882 -5.835  8.783   1.00 30.01  ? 86  ALA A O   1 
ATOM   471  C CB  . ALA A 1 69  ? 54.754 -3.058  9.038   1.00 31.02  ? 86  ALA A CB  1 
ATOM   472  N N   . ILE A 1 70  ? 51.852 -3.965  8.076   1.00 22.11  ? 87  ILE A N   1 
ATOM   473  C CA  . ILE A 1 70  ? 50.523 -4.524  8.323   1.00 21.53  ? 87  ILE A CA  1 
ATOM   474  C C   . ILE A 1 70  ? 50.212 -5.649  7.352   1.00 22.72  ? 87  ILE A C   1 
ATOM   475  O O   . ILE A 1 70  ? 49.803 -6.742  7.746   1.00 22.97  ? 87  ILE A O   1 
ATOM   476  C CB  . ILE A 1 70  ? 49.471 -3.406  8.210   1.00 24.53  ? 87  ILE A CB  1 
ATOM   477  C CG1 . ILE A 1 70  ? 49.586 -2.488  9.418   1.00 28.30  ? 87  ILE A CG1 1 
ATOM   478  C CG2 . ILE A 1 70  ? 48.047 -4.024  8.081   1.00 23.42  ? 87  ILE A CG2 1 
ATOM   479  C CD1 . ILE A 1 70  ? 49.032 -3.099  10.670  1.00 31.45  ? 87  ILE A CD1 1 
ATOM   480  N N   . GLU A 1 71  ? 50.385 -5.391  6.055   1.00 23.38  ? 88  GLU A N   1 
ATOM   481  C CA  . GLU A 1 71  ? 50.033 -6.400  5.062   1.00 23.74  ? 88  GLU A CA  1 
ATOM   482  C C   . GLU A 1 71  ? 50.821 -7.670  5.276   1.00 23.90  ? 88  GLU A C   1 
ATOM   483  O O   . GLU A 1 71  ? 50.276 -8.776  5.215   1.00 24.52  ? 88  GLU A O   1 
ATOM   484  C CB  . GLU A 1 71  ? 50.294 -5.865  3.652   1.00 24.31  ? 88  GLU A CB  1 
ATOM   485  C CG  . GLU A 1 71  ? 49.413 -4.694  3.289   1.00 29.59  ? 88  GLU A CG  1 
ATOM   486  C CD  . GLU A 1 71  ? 49.750 -4.132  1.922   1.00 30.12  ? 88  GLU A CD  1 
ATOM   487  O OE1 . GLU A 1 71  ? 50.744 -4.598  1.318   1.00 33.63  ? 88  GLU A OE1 1 
ATOM   488  O OE2 . GLU A 1 71  ? 49.026 -3.242  1.474   1.00 30.21  ? 88  GLU A OE2 1 
ATOM   489  N N   . ASP A 1 72  ? 52.122 -7.538  5.501   1.00 24.26  ? 89  ASP A N   1 
ATOM   490  C CA  . ASP A 1 72  ? 52.911 -8.749  5.655   1.00 25.07  ? 89  ASP A CA  1 
ATOM   491  C C   . ASP A 1 72  ? 52.614 -9.445  6.970   1.00 25.26  ? 89  ASP A C   1 
ATOM   492  O O   . ASP A 1 72  ? 52.803 -10.672 7.082   1.00 24.59  ? 89  ASP A O   1 
ATOM   493  C CB  . ASP A 1 72  ? 54.405 -8.433  5.559   1.00 31.18  ? 89  ASP A CB  1 
ATOM   494  C CG  . ASP A 1 72  ? 54.825 -8.082  4.153   1.00 36.79  ? 89  ASP A CG  1 
ATOM   495  O OD1 . ASP A 1 72  ? 53.973 -8.241  3.241   1.00 29.20  ? 89  ASP A OD1 1 
ATOM   496  O OD2 . ASP A 1 72  ? 55.966 -7.592  3.991   1.00 32.95  ? 89  ASP A OD2 1 
ATOM   497  N N   . HIS A 1 73  ? 52.091 -8.712  7.954   1.00 23.27  ? 90  HIS A N   1 
ATOM   498  C CA  . HIS A 1 73  ? 51.761 -9.384  9.196   1.00 22.78  ? 90  HIS A CA  1 
ATOM   499  C C   . HIS A 1 73  ? 50.555 -10.293 9.021   1.00 24.88  ? 90  HIS A C   1 
ATOM   500  O O   . HIS A 1 73  ? 50.535 -11.415 9.541   1.00 24.65  ? 90  HIS A O   1 
ATOM   501  C CB  . HIS A 1 73  ? 51.514 -8.380  10.332  1.00 25.42  ? 90  HIS A CB  1 
ATOM   502  C CG  . HIS A 1 73  ? 51.353 -9.068  11.647  1.00 28.43  ? 90  HIS A CG  1 
ATOM   503  N ND1 . HIS A 1 73  ? 52.424 -9.605  12.325  1.00 25.80  ? 90  HIS A ND1 1 
ATOM   504  C CD2 . HIS A 1 73  ? 50.246 -9.436  12.334  1.00 27.05  ? 90  HIS A CD2 1 
ATOM   505  C CE1 . HIS A 1 73  ? 51.986 -10.236 13.398  1.00 29.59  ? 90  HIS A CE1 1 
ATOM   506  N NE2 . HIS A 1 73  ? 50.669 -10.145 13.429  1.00 27.64  ? 90  HIS A NE2 1 
ATOM   507  N N   . PHE A 1 74  ? 49.535 -9.826  8.306   1.00 22.59  ? 91  PHE A N   1 
ATOM   508  C CA  . PHE A 1 74  ? 48.301 -10.591 8.207   1.00 23.26  ? 91  PHE A CA  1 
ATOM   509  C C   . PHE A 1 74  ? 48.224 -11.472 6.975   1.00 27.93  ? 91  PHE A C   1 
ATOM   510  O O   . PHE A 1 74  ? 47.518 -12.485 7.007   1.00 26.55  ? 91  PHE A O   1 
ATOM   511  C CB  . PHE A 1 74  ? 47.112 -9.630  8.264   1.00 27.40  ? 91  PHE A CB  1 
ATOM   512  C CG  . PHE A 1 74  ? 46.873 -9.084  9.640   1.00 26.96  ? 91  PHE A CG  1 
ATOM   513  C CD1 . PHE A 1 74  ? 46.260 -9.863  10.608  1.00 27.67  ? 91  PHE A CD1 1 
ATOM   514  C CD2 . PHE A 1 74  ? 47.316 -7.812  9.985   1.00 24.33  ? 91  PHE A CD2 1 
ATOM   515  C CE1 . PHE A 1 74  ? 46.069 -9.360  11.888  1.00 27.69  ? 91  PHE A CE1 1 
ATOM   516  C CE2 . PHE A 1 74  ? 47.118 -7.317  11.253  1.00 27.77  ? 91  PHE A CE2 1 
ATOM   517  C CZ  . PHE A 1 74  ? 46.493 -8.105  12.205  1.00 26.83  ? 91  PHE A CZ  1 
ATOM   518  N N   . ASP A 1 75  ? 48.928 -11.136 5.898   1.00 24.73  ? 92  ASP A N   1 
ATOM   519  C CA  . ASP A 1 75  ? 48.910 -12.018 4.730   1.00 24.97  ? 92  ASP A CA  1 
ATOM   520  C C   . ASP A 1 75  ? 49.709 -13.288 5.005   1.00 32.29  ? 92  ASP A C   1 
ATOM   521  O O   . ASP A 1 75  ? 50.697 -13.272 5.741   1.00 34.51  ? 92  ASP A O   1 
ATOM   522  C CB  . ASP A 1 75  ? 49.505 -11.324 3.498   1.00 29.81  ? 92  ASP A CB  1 
ATOM   523  C CG  . ASP A 1 75  ? 48.693 -10.109 3.051   1.00 36.08  ? 92  ASP A CG  1 
ATOM   524  O OD1 . ASP A 1 75  ? 47.475 -10.042 3.347   1.00 29.75  ? 92  ASP A OD1 1 
ATOM   525  O OD2 . ASP A 1 75  ? 49.279 -9.232  2.384   1.00 39.43  ? 92  ASP A OD2 1 
ATOM   526  N N   . ALA A 1 76  ? 49.300 -14.386 4.379   1.00 29.54  ? 93  ALA A N   1 
ATOM   527  C CA  . ALA A 1 76  ? 50.007 -15.644 4.557   1.00 35.90  ? 93  ALA A CA  1 
ATOM   528  C C   . ALA A 1 76  ? 51.461 -15.510 4.146   1.00 32.16  ? 93  ALA A C   1 
ATOM   529  O O   . ALA A 1 76  ? 51.804 -14.786 3.220   1.00 38.80  ? 93  ALA A O   1 
ATOM   530  C CB  . ALA A 1 76  ? 49.360 -16.767 3.743   1.00 37.74  ? 93  ALA A CB  1 
ATOM   531  N N   . ALA A 1 77  ? 52.327 -16.254 4.822   1.00 36.39  ? 94  ALA A N   1 
ATOM   532  C CA  . ALA A 1 77  ? 53.751 -16.281 4.489   1.00 40.97  ? 94  ALA A CA  1 
ATOM   533  C C   . ALA A 1 77  ? 54.130 -17.732 4.203   1.00 45.23  ? 94  ALA A C   1 
ATOM   534  O O   . ALA A 1 77  ? 54.551 -18.473 5.104   1.00 48.15  ? 94  ALA A O   1 
ATOM   535  C CB  . ALA A 1 77  ? 54.581 -15.685 5.624   1.00 40.30  ? 94  ALA A CB  1 
ATOM   536  N N   . PRO A 1 78  ? 53.972 -18.188 2.969   1.00 44.59  ? 95  PRO A N   1 
ATOM   537  C CA  . PRO A 1 78  ? 54.235 -19.609 2.697   1.00 49.76  ? 95  PRO A CA  1 
ATOM   538  C C   . PRO A 1 78  ? 55.618 -20.047 3.123   1.00 52.77  ? 95  PRO A C   1 
ATOM   539  O O   . PRO A 1 78  ? 55.770 -21.113 3.730   1.00 58.21  ? 95  PRO A O   1 
ATOM   540  C CB  . PRO A 1 78  ? 54.064 -19.706 1.177   1.00 53.96  ? 95  PRO A CB  1 
ATOM   541  C CG  . PRO A 1 78  ? 53.266 -18.511 0.780   1.00 56.89  ? 95  PRO A CG  1 
ATOM   542  C CD  . PRO A 1 78  ? 53.637 -17.434 1.753   1.00 51.34  ? 95  PRO A CD  1 
ATOM   543  N N   . GLU A 1 79  ? 56.626 -19.214 2.869   1.00 55.74  ? 96  GLU A N   1 
ATOM   544  C CA  . GLU A 1 79  ? 58.004 -19.596 3.151   1.00 57.51  ? 96  GLU A CA  1 
ATOM   545  C C   . GLU A 1 79  ? 58.177 -19.932 4.620   1.00 64.55  ? 96  GLU A C   1 
ATOM   546  O O   . GLU A 1 79  ? 58.788 -20.949 4.969   1.00 63.33  ? 96  GLU A O   1 
ATOM   547  C CB  . GLU A 1 79  ? 58.943 -18.458 2.749   1.00 64.62  ? 96  GLU A CB  1 
ATOM   548  C CG  . GLU A 1 79  ? 60.372 -18.596 3.247   1.00 79.33  ? 96  GLU A CG  1 
ATOM   549  C CD  . GLU A 1 79  ? 61.235 -17.399 2.871   1.00 92.82  ? 96  GLU A CD  1 
ATOM   550  O OE1 . GLU A 1 79  ? 60.788 -16.586 2.032   1.00 93.31  ? 96  GLU A OE1 1 
ATOM   551  O OE2 . GLU A 1 79  ? 62.363 -17.280 3.401   1.00 97.71  ? 96  GLU A OE2 1 
ATOM   552  N N   . LEU A 1 80  ? 57.644 -19.076 5.498   1.00 59.62  ? 97  LEU A N   1 
ATOM   553  C CA  . LEU A 1 80  ? 57.768 -19.305 6.931   1.00 54.93  ? 97  LEU A CA  1 
ATOM   554  C C   . LEU A 1 80  ? 57.058 -20.580 7.341   1.00 54.26  ? 97  LEU A C   1 
ATOM   555  O O   . LEU A 1 80  ? 57.555 -21.326 8.188   1.00 63.36  ? 97  LEU A O   1 
ATOM   556  C CB  . LEU A 1 80  ? 57.215 -18.114 7.704   1.00 52.82  ? 97  LEU A CB  1 
ATOM   557  C CG  . LEU A 1 80  ? 57.345 -18.171 9.224   1.00 50.90  ? 97  LEU A CG  1 
ATOM   558  C CD1 . LEU A 1 80  ? 58.794 -18.028 9.676   1.00 54.39  ? 97  LEU A CD1 1 
ATOM   559  C CD2 . LEU A 1 80  ? 56.497 -17.061 9.847   1.00 48.31  ? 97  LEU A CD2 1 
ATOM   560  N N   . GLU A 1 81  ? 55.877 -20.829 6.780   1.00 51.70  ? 98  GLU A N   1 
ATOM   561  C CA  . GLU A 1 81  ? 55.133 -22.031 7.140   1.00 61.93  ? 98  GLU A CA  1 
ATOM   562  C C   . GLU A 1 81  ? 55.875 -23.295 6.709   1.00 65.96  ? 98  GLU A C   1 
ATOM   563  O O   . GLU A 1 81  ? 55.949 -24.262 7.474   1.00 66.34  ? 98  GLU A O   1 
ATOM   564  C CB  . GLU A 1 81  ? 53.728 -21.988 6.524   1.00 56.23  ? 98  GLU A CB  1 
ATOM   565  C CG  . GLU A 1 81  ? 52.852 -20.843 7.034   1.00 53.37  ? 98  GLU A CG  1 
ATOM   566  C CD  . GLU A 1 81  ? 51.400 -20.911 6.534   1.00 59.05  ? 98  GLU A CD  1 
ATOM   567  O OE1 . GLU A 1 81  ? 50.915 -22.014 6.205   1.00 66.46  ? 98  GLU A OE1 1 
ATOM   568  O OE2 . GLU A 1 81  ? 50.746 -19.847 6.442   1.00 48.59  ? 98  GLU A OE2 1 
ATOM   569  N N   . THR A 1 82  ? 56.435 -23.308 5.490   1.00 78.61  ? 99  THR A N   1 
ATOM   570  C CA  . THR A 1 82  ? 57.177 -24.486 5.039   1.00 75.14  ? 99  THR A CA  1 
ATOM   571  C C   . THR A 1 82  ? 58.421 -24.714 5.894   1.00 79.62  ? 99  THR A C   1 
ATOM   572  O O   . THR A 1 82  ? 58.707 -25.848 6.289   1.00 87.70  ? 99  THR A O   1 
ATOM   573  C CB  . THR A 1 82  ? 57.555 -24.361 3.560   1.00 81.33  ? 99  THR A CB  1 
ATOM   574  O OG1 . THR A 1 82  ? 58.433 -23.243 3.368   1.00 82.90  ? 99  THR A OG1 1 
ATOM   575  C CG2 . THR A 1 82  ? 56.302 -24.205 2.686   1.00 71.31  ? 99  THR A CG2 1 
ATOM   576  N N   . ASP A 1 83  ? 59.157 -23.648 6.226   1.00 70.61  ? 100 ASP A N   1 
ATOM   577  C CA  . ASP A 1 83  ? 60.324 -23.817 7.087   1.00 76.59  ? 100 ASP A CA  1 
ATOM   578  C C   . ASP A 1 83  ? 59.916 -24.359 8.453   1.00 85.07  ? 100 ASP A C   1 
ATOM   579  O O   . ASP A 1 83  ? 60.574 -25.257 8.995   1.00 90.93  ? 100 ASP A O   1 
ATOM   580  C CB  . ASP A 1 83  ? 61.077 -22.489 7.235   1.00 79.23  ? 100 ASP A CB  1 
ATOM   581  C CG  . ASP A 1 83  ? 62.133 -22.521 8.352   1.00 86.57  ? 100 ASP A CG  1 
ATOM   582  O OD1 . ASP A 1 83  ? 61.747 -22.518 9.547   1.00 78.11  ? 100 ASP A OD1 1 
ATOM   583  O OD2 . ASP A 1 83  ? 63.351 -22.548 8.035   1.00 82.52  ? 100 ASP A OD2 1 
ATOM   584  N N   . LEU A 1 84  ? 58.839 -23.819 9.032   1.00 75.85  ? 101 LEU A N   1 
ATOM   585  C CA  . LEU A 1 84  ? 58.386 -24.282 10.341  1.00 73.76  ? 101 LEU A CA  1 
ATOM   586  C C   . LEU A 1 84  ? 57.879 -25.715 10.268  1.00 80.03  ? 101 LEU A C   1 
ATOM   587  O O   . LEU A 1 84  ? 58.017 -26.480 11.230  1.00 78.28  ? 101 LEU A O   1 
ATOM   588  C CB  . LEU A 1 84  ? 57.278 -23.382 10.874  1.00 68.23  ? 101 LEU A CB  1 
ATOM   589  C CG  . LEU A 1 84  ? 57.639 -21.951 11.265  1.00 63.07  ? 101 LEU A CG  1 
ATOM   590  C CD1 . LEU A 1 84  ? 56.380 -21.233 11.732  1.00 57.61  ? 101 LEU A CD1 1 
ATOM   591  C CD2 . LEU A 1 84  ? 58.706 -21.936 12.332  1.00 66.75  ? 101 LEU A CD2 1 
ATOM   592  N N   . GLU A 1 85  ? 57.231 -26.070 9.154   1.00 81.46  ? 102 GLU A N   1 
ATOM   593  C CA  . GLU A 1 85  ? 56.817 -27.453 8.947   1.00 86.09  ? 102 GLU A CA  1 
ATOM   594  C C   . GLU A 1 85  ? 58.032 -28.367 8.985   1.00 87.86  ? 102 GLU A C   1 
ATOM   595  O O   . GLU A 1 85  ? 58.073 -29.338 9.747   1.00 84.10  ? 102 GLU A O   1 
ATOM   596  C CB  . GLU A 1 85  ? 56.069 -27.571 7.616   1.00 89.01  ? 102 GLU A CB  1 
ATOM   597  C CG  . GLU A 1 85  ? 55.525 -28.958 7.282   1.00 100.00 ? 102 GLU A CG  1 
ATOM   598  C CD  . GLU A 1 85  ? 54.511 -29.461 8.303   1.00 102.28 ? 102 GLU A CD  1 
ATOM   599  O OE1 . GLU A 1 85  ? 54.058 -28.651 9.133   1.00 101.53 ? 102 GLU A OE1 1 
ATOM   600  O OE2 . GLU A 1 85  ? 54.158 -30.661 8.271   1.00 101.01 ? 102 GLU A OE2 1 
ATOM   601  N N   . ALA A 1 86  ? 59.066 -28.024 8.213   1.00 90.00  ? 103 ALA A N   1 
ATOM   602  C CA  . ALA A 1 86  ? 60.290 -28.813 8.212   1.00 93.01  ? 103 ALA A CA  1 
ATOM   603  C C   . ALA A 1 86  ? 60.812 -29.005 9.630   1.00 92.28  ? 103 ALA A C   1 
ATOM   604  O O   . ALA A 1 86  ? 61.021 -30.136 10.082  1.00 98.46  ? 103 ALA A O   1 
ATOM   605  C CB  . ALA A 1 86  ? 61.345 -28.129 7.338   1.00 91.09  ? 103 ALA A CB  1 
ATOM   606  N N   . LYS A 1 87  ? 60.975 -27.909 10.367  1.00 89.21  ? 104 LYS A N   1 
ATOM   607  C CA  . LYS A 1 87  ? 61.474 -27.973 11.737  1.00 93.39  ? 104 LYS A CA  1 
ATOM   608  C C   . LYS A 1 87  ? 60.515 -28.699 12.672  1.00 89.02  ? 104 LYS A C   1 
ATOM   609  O O   . LYS A 1 87  ? 60.800 -28.826 13.872  1.00 87.75  ? 104 LYS A O   1 
ATOM   610  C CB  . LYS A 1 87  ? 61.703 -26.556 12.280  1.00 94.91  ? 104 LYS A CB  1 
ATOM   611  C CG  . LYS A 1 87  ? 62.640 -25.683 11.459  1.00 91.92  ? 104 LYS A CG  1 
ATOM   612  C CD  . LYS A 1 87  ? 64.015 -25.574 12.094  1.00 84.97  ? 104 LYS A CD  1 
ATOM   613  C CE  . LYS A 1 87  ? 64.672 -24.276 11.698  1.00 89.93  ? 104 LYS A CE  1 
ATOM   614  N NZ  . LYS A 1 87  ? 64.515 -24.029 10.235  1.00 102.37 ? 104 LYS A NZ  1 
ATOM   615  N N   . GLY A 1 88  ? 59.373 -29.151 12.164  1.00 76.09  ? 105 GLY A N   1 
ATOM   616  C CA  . GLY A 1 88  ? 58.411 -29.817 13.021  1.00 76.98  ? 105 GLY A CA  1 
ATOM   617  C C   . GLY A 1 88  ? 57.975 -28.978 14.201  1.00 83.96  ? 105 GLY A C   1 
ATOM   618  O O   . GLY A 1 88  ? 57.665 -29.521 15.267  1.00 82.03  ? 105 GLY A O   1 
ATOM   619  N N   . LYS A 1 89  ? 57.930 -27.659 14.040  1.00 94.35  ? 106 LYS A N   1 
ATOM   620  C CA  . LYS A 1 89  ? 57.509 -26.769 15.118  1.00 91.91  ? 106 LYS A CA  1 
ATOM   621  C C   . LYS A 1 89  ? 56.020 -26.474 14.940  1.00 85.35  ? 106 LYS A C   1 
ATOM   622  O O   . LYS A 1 89  ? 55.591 -25.368 14.621  1.00 85.79  ? 106 LYS A O   1 
ATOM   623  C CB  . LYS A 1 89  ? 58.369 -25.506 15.126  1.00 89.01  ? 106 LYS A CB  1 
ATOM   624  C CG  . LYS A 1 89  ? 59.883 -25.793 15.155  1.00 92.23  ? 106 LYS A CG  1 
ATOM   625  C CD  . LYS A 1 89  ? 60.361 -26.299 16.523  1.00 112.00 ? 106 LYS A CD  1 
ATOM   626  C CE  . LYS A 1 89  ? 60.085 -25.307 17.658  1.00 113.45 ? 106 LYS A CE  1 
ATOM   627  N NZ  . LYS A 1 89  ? 60.699 -25.739 18.946  1.00 119.41 ? 106 LYS A NZ  1 
ATOM   628  N N   . HIS A 1 90  ? 55.229 -27.521 15.175  1.00 81.97  ? 107 HIS A N   1 
ATOM   629  C CA  . HIS A 1 90  ? 53.825 -27.500 14.782  1.00 80.75  ? 107 HIS A CA  1 
ATOM   630  C C   . HIS A 1 90  ? 52.996 -26.544 15.623  1.00 77.11  ? 107 HIS A C   1 
ATOM   631  O O   . HIS A 1 90  ? 52.027 -25.965 15.117  1.00 70.31  ? 107 HIS A O   1 
ATOM   632  C CB  . HIS A 1 90  ? 53.252 -28.917 14.853  1.00 83.98  ? 107 HIS A CB  1 
ATOM   633  C CG  . HIS A 1 90  ? 53.765 -29.819 13.777  1.00 89.16  ? 107 HIS A CG  1 
ATOM   634  N ND1 . HIS A 1 90  ? 54.895 -30.594 13.921  1.00 94.13  ? 107 HIS A ND1 1 
ATOM   635  C CD2 . HIS A 1 90  ? 53.296 -30.066 12.531  1.00 92.90  ? 107 HIS A CD2 1 
ATOM   636  C CE1 . HIS A 1 90  ? 55.102 -31.277 12.809  1.00 93.49  ? 107 HIS A CE1 1 
ATOM   637  N NE2 . HIS A 1 90  ? 54.144 -30.976 11.951  1.00 98.70  ? 107 HIS A NE2 1 
ATOM   638  N N   . GLU A 1 91  ? 53.339 -26.365 16.896  1.00 74.34  ? 108 GLU A N   1 
ATOM   639  C CA  . GLU A 1 91  ? 52.620 -25.383 17.698  1.00 74.64  ? 108 GLU A CA  1 
ATOM   640  C C   . GLU A 1 91  ? 52.885 -23.970 17.185  1.00 67.79  ? 108 GLU A C   1 
ATOM   641  O O   . GLU A 1 91  ? 51.998 -23.110 17.226  1.00 58.03  ? 108 GLU A O   1 
ATOM   642  C CB  . GLU A 1 91  ? 53.000 -25.526 19.170  1.00 77.66  ? 108 GLU A CB  1 
ATOM   643  C CG  . GLU A 1 91  ? 52.955 -26.961 19.672  1.00 90.38  ? 108 GLU A CG  1 
ATOM   644  C CD  . GLU A 1 91  ? 53.377 -27.091 21.123  1.00 106.20 ? 108 GLU A CD  1 
ATOM   645  O OE1 . GLU A 1 91  ? 53.823 -26.081 21.709  1.00 104.72 ? 108 GLU A OE1 1 
ATOM   646  O OE2 . GLU A 1 91  ? 53.263 -28.208 21.676  1.00 104.77 ? 108 GLU A OE2 1 
ATOM   647  N N   . LEU A 1 92  ? 54.110 -23.707 16.729  1.00 67.00  ? 109 LEU A N   1 
ATOM   648  C CA  . LEU A 1 92  ? 54.410 -22.421 16.114  1.00 65.37  ? 109 LEU A CA  1 
ATOM   649  C C   . LEU A 1 92  ? 53.663 -22.246 14.797  1.00 63.32  ? 109 LEU A C   1 
ATOM   650  O O   . LEU A 1 92  ? 53.083 -21.186 14.543  1.00 56.05  ? 109 LEU A O   1 
ATOM   651  C CB  . LEU A 1 92  ? 55.912 -22.295 15.877  1.00 67.10  ? 109 LEU A CB  1 
ATOM   652  C CG  . LEU A 1 92  ? 56.791 -22.097 17.106  1.00 65.41  ? 109 LEU A CG  1 
ATOM   653  C CD1 . LEU A 1 92  ? 58.241 -22.029 16.688  1.00 67.53  ? 109 LEU A CD1 1 
ATOM   654  C CD2 . LEU A 1 92  ? 56.409 -20.851 17.837  1.00 52.99  ? 109 LEU A CD2 1 
ATOM   655  N N   . LEU A 1 93  ? 53.647 -23.282 13.953  1.00 66.98  ? 110 LEU A N   1 
ATOM   656  C CA  . LEU A 1 93  ? 52.963 -23.171 12.671  1.00 58.76  ? 110 LEU A CA  1 
ATOM   657  C C   . LEU A 1 93  ? 51.504 -22.790 12.869  1.00 58.12  ? 110 LEU A C   1 
ATOM   658  O O   . LEU A 1 93  ? 50.994 -21.890 12.193  1.00 56.02  ? 110 LEU A O   1 
ATOM   659  C CB  . LEU A 1 93  ? 53.064 -24.492 11.909  1.00 65.76  ? 110 LEU A CB  1 
ATOM   660  C CG  . LEU A 1 93  ? 52.434 -24.569 10.512  1.00 69.25  ? 110 LEU A CG  1 
ATOM   661  C CD1 . LEU A 1 93  ? 53.027 -23.558 9.527   1.00 63.14  ? 110 LEU A CD1 1 
ATOM   662  C CD2 . LEU A 1 93  ? 52.549 -25.987 9.967   1.00 77.93  ? 110 LEU A CD2 1 
ATOM   663  N N   . ALA A 1 94  ? 50.830 -23.442 13.820  1.00 48.67  ? 111 ALA A N   1 
ATOM   664  C CA  . ALA A 1 94  ? 49.425 -23.146 14.084  1.00 48.09  ? 111 ALA A CA  1 
ATOM   665  C C   . ALA A 1 94  ? 49.255 -21.718 14.566  1.00 51.46  ? 111 ALA A C   1 
ATOM   666  O O   . ALA A 1 94  ? 48.243 -21.064 14.279  1.00 47.36  ? 111 ALA A O   1 
ATOM   667  C CB  . ALA A 1 94  ? 48.872 -24.122 15.117  1.00 46.37  ? 111 ALA A CB  1 
ATOM   668  N N   . LEU A 1 95  ? 50.221 -21.242 15.350  1.00 53.91  ? 112 LEU A N   1 
ATOM   669  C CA  . LEU A 1 95  ? 50.213 -19.865 15.809  1.00 54.95  ? 112 LEU A CA  1 
ATOM   670  C C   . LEU A 1 95  ? 50.282 -18.903 14.625  1.00 48.13  ? 112 LEU A C   1 
ATOM   671  O O   . LEU A 1 95  ? 49.475 -17.974 14.511  1.00 47.87  ? 112 LEU A O   1 
ATOM   672  C CB  . LEU A 1 95  ? 51.392 -19.675 16.758  1.00 59.05  ? 112 LEU A CB  1 
ATOM   673  C CG  . LEU A 1 95  ? 51.550 -18.367 17.513  1.00 58.07  ? 112 LEU A CG  1 
ATOM   674  C CD1 . LEU A 1 95  ? 50.452 -18.258 18.529  1.00 64.09  ? 112 LEU A CD1 1 
ATOM   675  C CD2 . LEU A 1 95  ? 52.919 -18.319 18.193  1.00 59.99  ? 112 LEU A CD2 1 
ATOM   676  N N   . VAL A 1 96  ? 51.224 -19.126 13.715  1.00 44.76  ? 113 VAL A N   1 
ATOM   677  C CA  . VAL A 1 96  ? 51.332 -18.263 12.542  1.00 44.47  ? 113 VAL A CA  1 
ATOM   678  C C   . VAL A 1 96  ? 50.045 -18.298 11.723  1.00 47.13  ? 113 VAL A C   1 
ATOM   679  O O   . VAL A 1 96  ? 49.591 -17.263 11.225  1.00 42.82  ? 113 VAL A O   1 
ATOM   680  C CB  . VAL A 1 96  ? 52.547 -18.665 11.690  1.00 48.57  ? 113 VAL A CB  1 
ATOM   681  C CG1 . VAL A 1 96  ? 52.512 -17.931 10.352  1.00 48.41  ? 113 VAL A CG1 1 
ATOM   682  C CG2 . VAL A 1 96  ? 53.828 -18.365 12.425  1.00 47.06  ? 113 VAL A CG2 1 
ATOM   683  N N   . ARG A 1 97  ? 49.424 -19.480 11.588  1.00 48.46  ? 114 ARG A N   1 
ATOM   684  C CA  . ARG A 1 97  ? 48.235 -19.590 10.740  1.00 44.33  ? 114 ARG A CA  1 
ATOM   685  C C   . ARG A 1 97  ? 47.020 -18.928 11.361  1.00 47.32  ? 114 ARG A C   1 
ATOM   686  O O   . ARG A 1 97  ? 46.139 -18.461 10.628  1.00 47.89  ? 114 ARG A O   1 
ATOM   687  C CB  . ARG A 1 97  ? 47.933 -21.049 10.437  1.00 46.99  ? 114 ARG A CB  1 
ATOM   688  C CG  . ARG A 1 97  ? 48.948 -21.662 9.493   1.00 51.65  ? 114 ARG A CG  1 
ATOM   689  C CD  . ARG A 1 97  ? 48.688 -23.138 9.192   1.00 52.75  ? 114 ARG A CD  1 
ATOM   690  N NE  . ARG A 1 97  ? 49.519 -23.574 8.077   1.00 60.50  ? 114 ARG A NE  1 
ATOM   691  C CZ  . ARG A 1 97  ? 49.802 -24.839 7.795   1.00 70.69  ? 114 ARG A CZ  1 
ATOM   692  N NH1 . ARG A 1 97  ? 49.241 -25.836 8.459   1.00 68.77  ? 114 ARG A NH1 1 
ATOM   693  N NH2 . ARG A 1 97  ? 50.682 -25.111 6.831   1.00 64.53  ? 114 ARG A NH2 1 
ATOM   694  N N   . ASP A 1 98  ? 46.980 -18.829 12.694  1.00 45.39  ? 115 ASP A N   1 
ATOM   695  C CA  . ASP A 1 98  ? 45.883 -18.193 13.409  1.00 43.07  ? 115 ASP A CA  1 
ATOM   696  C C   . ASP A 1 98  ? 45.898 -16.670 13.336  1.00 41.18  ? 115 ASP A C   1 
ATOM   697  O O   . ASP A 1 98  ? 44.927 -16.031 13.771  1.00 40.64  ? 115 ASP A O   1 
ATOM   698  C CB  . ASP A 1 98  ? 45.925 -18.621 14.883  1.00 56.94  ? 115 ASP A CB  1 
ATOM   699  C CG  . ASP A 1 98  ? 44.645 -18.280 15.624  1.00 68.49  ? 115 ASP A CG  1 
ATOM   700  O OD1 . ASP A 1 98  ? 43.554 -18.699 15.152  1.00 67.88  ? 115 ASP A OD1 1 
ATOM   701  O OD2 . ASP A 1 98  ? 44.730 -17.579 16.663  1.00 66.41  ? 115 ASP A OD2 1 
ATOM   702  N N   . ILE A 1 99  ? 46.959 -16.060 12.822  1.00 37.64  ? 116 ILE A N   1 
ATOM   703  C CA  . ILE A 1 99  ? 46.966 -14.601 12.732  1.00 38.58  ? 116 ILE A CA  1 
ATOM   704  C C   . ILE A 1 99  ? 45.793 -14.119 11.899  1.00 40.08  ? 116 ILE A C   1 
ATOM   705  O O   . ILE A 1 99  ? 45.193 -13.075 12.188  1.00 33.84  ? 116 ILE A O   1 
ATOM   706  C CB  . ILE A 1 99  ? 48.306 -14.114 12.174  1.00 41.07  ? 116 ILE A CB  1 
ATOM   707  C CG1 . ILE A 1 99  ? 49.372 -14.447 13.191  1.00 36.94  ? 116 ILE A CG1 1 
ATOM   708  C CG2 . ILE A 1 99  ? 48.278 -12.627 11.884  1.00 34.33  ? 116 ILE A CG2 1 
ATOM   709  C CD1 . ILE A 1 99  ? 50.728 -14.163 12.715  1.00 37.03  ? 116 ILE A CD1 1 
ATOM   710  N N   . LEU A 1 100 ? 45.463 -14.860 10.842  1.00 37.70  ? 117 LEU A N   1 
ATOM   711  C CA  . LEU A 1 100 ? 44.280 -14.625 10.021  1.00 39.29  ? 117 LEU A CA  1 
ATOM   712  C C   . LEU A 1 100 ? 43.581 -15.969 9.895   1.00 44.52  ? 117 LEU A C   1 
ATOM   713  O O   . LEU A 1 100 ? 43.958 -16.793 9.055   1.00 40.39  ? 117 LEU A O   1 
ATOM   714  C CB  . LEU A 1 100 ? 44.639 -14.065 8.647   1.00 43.69  ? 117 LEU A CB  1 
ATOM   715  C CG  . LEU A 1 100 ? 43.397 -13.627 7.870   1.00 48.90  ? 117 LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 100 ? 42.840 -12.369 8.489   1.00 40.58  ? 117 LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 100 ? 43.644 -13.439 6.353   1.00 45.66  ? 117 LEU A CD2 1 
ATOM   718  N N   . PRO A 1 101 ? 42.599 -16.248 10.747  1.00 36.76  ? 118 PRO A N   1 
ATOM   719  C CA  . PRO A 1 101 ? 41.879 -17.524 10.667  1.00 34.46  ? 118 PRO A CA  1 
ATOM   720  C C   . PRO A 1 101 ? 41.214 -17.751 9.312   1.00 36.26  ? 118 PRO A C   1 
ATOM   721  O O   . PRO A 1 101 ? 40.889 -16.818 8.573   1.00 33.37  ? 118 PRO A O   1 
ATOM   722  C CB  . PRO A 1 101 ? 40.830 -17.406 11.774  1.00 37.50  ? 118 PRO A CB  1 
ATOM   723  C CG  . PRO A 1 101 ? 41.395 -16.461 12.730  1.00 40.98  ? 118 PRO A CG  1 
ATOM   724  C CD  . PRO A 1 101 ? 42.187 -15.456 11.910  1.00 39.64  ? 118 PRO A CD  1 
ATOM   725  N N   . ALA A 1 102 ? 40.951 -19.033 9.032   1.00 38.31  ? 119 ALA A N   1 
ATOM   726  C CA  . ALA A 1 102 ? 40.466 -19.469 7.725   1.00 41.11  ? 119 ALA A CA  1 
ATOM   727  C C   . ALA A 1 102 ? 39.097 -18.900 7.382   1.00 38.00  ? 119 ALA A C   1 
ATOM   728  O O   . ALA A 1 102 ? 38.818 -18.651 6.209   1.00 36.81  ? 119 ALA A O   1 
ATOM   729  C CB  . ALA A 1 102 ? 40.410 -20.992 7.685   1.00 42.06  ? 119 ALA A CB  1 
ATOM   730  N N   . HIS A 1 103 ? 38.226 -18.700 8.376   1.00 40.46  ? 120 HIS A N   1 
ATOM   731  C CA  . HIS A 1 103 ? 36.893 -18.163 8.110   1.00 38.85  ? 120 HIS A CA  1 
ATOM   732  C C   . HIS A 1 103 ? 36.897 -16.641 7.976   1.00 38.47  ? 120 HIS A C   1 
ATOM   733  O O   . HIS A 1 103 ? 35.830 -16.040 7.784   1.00 33.85  ? 120 HIS A O   1 
ATOM   734  C CB  . HIS A 1 103 ? 35.898 -18.615 9.194   1.00 35.78  ? 120 HIS A CB  1 
ATOM   735  C CG  . HIS A 1 103 ? 36.091 -17.990 10.554  1.00 37.79  ? 120 HIS A CG  1 
ATOM   736  N ND1 . HIS A 1 103 ? 37.182 -18.254 11.359  1.00 39.19  ? 120 HIS A ND1 1 
ATOM   737  C CD2 . HIS A 1 103 ? 35.298 -17.152 11.270  1.00 41.21  ? 120 HIS A CD2 1 
ATOM   738  C CE1 . HIS A 1 103 ? 37.063 -17.589 12.500  1.00 42.58  ? 120 HIS A CE1 1 
ATOM   739  N NE2 . HIS A 1 103 ? 35.929 -16.911 12.472  1.00 36.94  ? 120 HIS A NE2 1 
ATOM   740  N N   . VAL A 1 104 ? 38.072 -16.014 7.999   1.00 33.95  ? 121 VAL A N   1 
ATOM   741  C CA  . VAL A 1 104 ? 38.192 -14.561 8.057   1.00 32.22  ? 121 VAL A CA  1 
ATOM   742  C C   . VAL A 1 104 ? 38.938 -14.090 6.818   1.00 32.04  ? 121 VAL A C   1 
ATOM   743  O O   . VAL A 1 104 ? 39.865 -14.760 6.351   1.00 32.93  ? 121 VAL A O   1 
ATOM   744  C CB  . VAL A 1 104 ? 38.916 -14.122 9.342   1.00 31.52  ? 121 VAL A CB  1 
ATOM   745  C CG1 . VAL A 1 104 ? 39.177 -12.613 9.358   1.00 27.94  ? 121 VAL A CG1 1 
ATOM   746  C CG2 . VAL A 1 104 ? 38.099 -14.552 10.569  1.00 33.39  ? 121 VAL A CG2 1 
ATOM   747  N N   . ASN A 1 105 ? 38.519 -12.951 6.278   1.00 29.39  ? 122 ASN A N   1 
ATOM   748  C CA  . ASN A 1 105 ? 39.179 -12.313 5.153   1.00 29.24  ? 122 ASN A CA  1 
ATOM   749  C C   . ASN A 1 105 ? 39.547 -10.881 5.518   1.00 32.94  ? 122 ASN A C   1 
ATOM   750  O O   . ASN A 1 105 ? 38.987 -10.284 6.436   1.00 30.81  ? 122 ASN A O   1 
ATOM   751  C CB  . ASN A 1 105 ? 38.299 -12.320 3.909   1.00 32.39  ? 122 ASN A CB  1 
ATOM   752  C CG  . ASN A 1 105 ? 37.057 -11.495 4.080   1.00 31.02  ? 122 ASN A CG  1 
ATOM   753  O OD1 . ASN A 1 105 ? 37.088 -10.288 3.889   1.00 31.86  ? 122 ASN A OD1 1 
ATOM   754  N ND2 . ASN A 1 105 ? 35.955 -12.134 4.463   1.00 35.91  ? 122 ASN A ND2 1 
ATOM   755  N N   . CYS A 1 106 ? 40.527 -10.372 4.790   1.00 28.24  ? 123 CYS A N   1 
ATOM   756  C CA  . CYS A 1 106 ? 40.939 -8.973  5.015   1.00 29.97  ? 123 CYS A CA  1 
ATOM   757  C C   . CYS A 1 106 ? 41.156 -8.244  3.695   1.00 26.40  ? 123 CYS A C   1 
ATOM   758  O O   . CYS A 1 106 ? 41.380 -8.907  2.678   1.00 30.01  ? 123 CYS A O   1 
ATOM   759  C CB  . CYS A 1 106 ? 42.207 -8.871  5.855   1.00 35.47  ? 123 CYS A CB  1 
ATOM   760  S SG  . CYS A 1 106 ? 43.667 -9.674  5.163   1.00 38.90  ? 123 CYS A SG  1 
ATOM   761  N N   . LEU A 1 107 ? 40.966 -6.943  3.721   1.00 25.17  ? 124 LEU A N   1 
ATOM   762  C CA  . LEU A 1 107 ? 41.303 -6.105  2.595   1.00 28.21  ? 124 LEU A CA  1 
ATOM   763  C C   . LEU A 1 107 ? 41.972 -4.842  3.110   1.00 26.68  ? 124 LEU A C   1 
ATOM   764  O O   . LEU A 1 107 ? 41.915 -4.512  4.300   1.00 25.56  ? 124 LEU A O   1 
ATOM   765  C CB  . LEU A 1 107 ? 40.070 -5.804  1.748   1.00 34.47  ? 124 LEU A CB  1 
ATOM   766  C CG  . LEU A 1 107 ? 38.899 -5.072  2.360   1.00 28.64  ? 124 LEU A CG  1 
ATOM   767  C CD1 . LEU A 1 107 ? 39.080 -3.568  2.306   1.00 32.30  ? 124 LEU A CD1 1 
ATOM   768  C CD2 . LEU A 1 107 ? 37.676 -5.519  1.557   1.00 30.17  ? 124 LEU A CD2 1 
ATOM   769  N N   . TYR A 1 108 ? 42.665 -4.172  2.205   1.00 24.60  ? 125 TYR A N   1 
ATOM   770  C CA  . TYR A 1 108 ? 43.510 -3.037  2.534   1.00 23.21  ? 125 TYR A CA  1 
ATOM   771  C C   . TYR A 1 108 ? 43.083 -1.832  1.711   1.00 26.69  ? 125 TYR A C   1 
ATOM   772  O O   . TYR A 1 108 ? 42.934 -1.940  0.492   1.00 24.25  ? 125 TYR A O   1 
ATOM   773  C CB  . TYR A 1 108 ? 44.987 -3.384  2.261   1.00 23.39  ? 125 TYR A CB  1 
ATOM   774  C CG  . TYR A 1 108 ? 45.460 -4.601  2.983   1.00 26.28  ? 125 TYR A CG  1 
ATOM   775  C CD1 . TYR A 1 108 ? 45.864 -4.531  4.326   1.00 26.93  ? 125 TYR A CD1 1 
ATOM   776  C CD2 . TYR A 1 108 ? 45.486 -5.843  2.353   1.00 29.38  ? 125 TYR A CD2 1 
ATOM   777  C CE1 . TYR A 1 108 ? 46.285 -5.658  5.007   1.00 26.46  ? 125 TYR A CE1 1 
ATOM   778  C CE2 . TYR A 1 108 ? 45.910 -6.976  3.030   1.00 31.51  ? 125 TYR A CE2 1 
ATOM   779  C CZ  . TYR A 1 108 ? 46.284 -6.871  4.386   1.00 28.08  ? 125 TYR A CZ  1 
ATOM   780  O OH  . TYR A 1 108 ? 46.739 -7.969  5.084   1.00 28.61  ? 125 TYR A OH  1 
ATOM   781  N N   . ILE A 1 109 ? 42.935 -0.685  2.378   1.00 25.66  ? 126 ILE A N   1 
ATOM   782  C CA  . ILE A 1 109 ? 42.611 0.588   1.751   1.00 29.31  ? 126 ILE A CA  1 
ATOM   783  C C   . ILE A 1 109 ? 43.546 1.673   2.277   1.00 27.51  ? 126 ILE A C   1 
ATOM   784  O O   . ILE A 1 109 ? 43.731 1.812   3.492   1.00 28.68  ? 126 ILE A O   1 
ATOM   785  C CB  . ILE A 1 109 ? 41.157 1.004   2.051   1.00 33.47  ? 126 ILE A CB  1 
ATOM   786  C CG1 . ILE A 1 109 ? 40.217 -0.186  1.927   1.00 34.27  ? 126 ILE A CG1 1 
ATOM   787  C CG2 . ILE A 1 109 ? 40.735 2.117   1.119   1.00 33.43  ? 126 ILE A CG2 1 
ATOM   788  C CD1 . ILE A 1 109 ? 38.770 0.186   2.217   1.00 42.73  ? 126 ILE A CD1 1 
ATOM   789  N N   . ARG A 1 110 ? 44.033 2.514   1.381   1.00 32.31  ? 127 ARG A N   1 
ATOM   790  C CA  . ARG A 1 110 ? 44.908 3.621   1.751   1.00 29.49  ? 127 ARG A CA  1 
ATOM   791  C C   . ARG A 1 110 ? 44.087 4.858   2.051   1.00 34.74  ? 127 ARG A C   1 
ATOM   792  O O   . ARG A 1 110 ? 43.295 5.305   1.220   1.00 36.12  ? 127 ARG A O   1 
ATOM   793  C CB  . ARG A 1 110 ? 45.886 3.970   0.630   1.00 31.60  ? 127 ARG A CB  1 
ATOM   794  C CG  . ARG A 1 110 ? 46.329 2.793   -0.173  1.00 43.20  ? 127 ARG A CG  1 
ATOM   795  C CD  . ARG A 1 110 ? 47.005 1.761   0.684   1.00 43.21  ? 127 ARG A CD  1 
ATOM   796  N NE  . ARG A 1 110 ? 47.620 0.684   -0.103  1.00 37.52  ? 127 ARG A NE  1 
ATOM   797  C CZ  . ARG A 1 110 ? 47.924 -0.508  0.391   1.00 44.49  ? 127 ARG A CZ  1 
ATOM   798  N NH1 . ARG A 1 110 ? 47.629 -0.845  1.670   1.00 30.65  ? 127 ARG A NH1 1 
ATOM   799  N NH2 . ARG A 1 110 ? 48.572 -1.369  -0.389  1.00 37.80  ? 127 ARG A NH2 1 
ATOM   800  N N   . GLN A 1 111 ? 44.307 5.442   3.215   1.00 30.02  ? 128 GLN A N   1 
ATOM   801  C CA  . GLN A 1 111 ? 43.776 6.774   3.420   1.00 36.90  ? 128 GLN A CA  1 
ATOM   802  C C   . GLN A 1 111 ? 44.581 7.747   2.567   1.00 36.06  ? 128 GLN A C   1 
ATOM   803  O O   . GLN A 1 111 ? 45.785 7.575   2.362   1.00 37.52  ? 128 GLN A O   1 
ATOM   804  C CB  . GLN A 1 111 ? 43.825 7.164   4.886   1.00 31.85  ? 128 GLN A CB  1 
ATOM   805  C CG  . GLN A 1 111 ? 45.199 7.410   5.405   1.00 40.39  ? 128 GLN A CG  1 
ATOM   806  C CD  . GLN A 1 111 ? 45.162 7.884   6.852   1.00 49.50  ? 128 GLN A CD  1 
ATOM   807  O OE1 . GLN A 1 111 ? 44.118 7.801   7.534   1.00 36.90  ? 128 GLN A OE1 1 
ATOM   808  N NE2 . GLN A 1 111 ? 46.290 8.410   7.319   1.00 43.90  ? 128 GLN A NE2 1 
ATOM   809  N N   . SER A 1 112 ? 43.890 8.736   2.019   1.00 38.99  ? 129 SER A N   1 
ATOM   810  C CA  . SER A 1 112 ? 44.530 9.667   1.098   1.00 46.32  ? 129 SER A CA  1 
ATOM   811  C C   . SER A 1 112 ? 45.547 10.549  1.805   1.00 53.11  ? 129 SER A C   1 
ATOM   812  O O   . SER A 1 112 ? 46.569 10.915  1.217   1.00 56.70  ? 129 SER A O   1 
ATOM   813  C CB  . SER A 1 112 ? 43.461 10.523  0.439   1.00 49.62  ? 129 SER A CB  1 
ATOM   814  O OG  . SER A 1 112 ? 42.723 11.193  1.451   1.00 47.08  ? 129 SER A OG  1 
ATOM   815  N N   . ALA A 1 113 ? 45.276 10.907  3.052   1.00 45.98  ? 130 ALA A N   1 
ATOM   816  C CA  . ALA A 1 113 ? 46.120 11.786  3.843   1.00 50.20  ? 130 ALA A CA  1 
ATOM   817  C C   . ALA A 1 113 ? 45.772 11.561  5.305   1.00 47.96  ? 130 ALA A C   1 
ATOM   818  O O   . ALA A 1 113 ? 44.715 10.994  5.605   1.00 46.32  ? 130 ALA A O   1 
ATOM   819  C CB  . ALA A 1 113 ? 45.905 13.258  3.459   1.00 46.58  ? 130 ALA A CB  1 
ATOM   820  N N   . PRO A 1 114 ? 46.653 11.968  6.239   1.00 55.88  ? 131 PRO A N   1 
ATOM   821  C CA  . PRO A 1 114 ? 46.348 11.855  7.679   1.00 45.75  ? 131 PRO A CA  1 
ATOM   822  C C   . PRO A 1 114 ? 45.394 12.955  8.140   1.00 47.86  ? 131 PRO A C   1 
ATOM   823  O O   . PRO A 1 114 ? 45.766 13.998  8.666   1.00 51.77  ? 131 PRO A O   1 
ATOM   824  C CB  . PRO A 1 114 ? 47.728 11.980  8.322   1.00 54.25  ? 131 PRO A CB  1 
ATOM   825  C CG  . PRO A 1 114 ? 48.462 12.890  7.400   1.00 61.09  ? 131 PRO A CG  1 
ATOM   826  C CD  . PRO A 1 114 ? 48.000 12.529  6.013   1.00 60.52  ? 131 PRO A CD  1 
ATOM   827  N N   . LEU A 1 115 ? 44.106 12.715  7.924   1.00 43.68  ? 132 LEU A N   1 
ATOM   828  C CA  . LEU A 1 115 ? 43.064 13.687  8.195   1.00 42.55  ? 132 LEU A CA  1 
ATOM   829  C C   . LEU A 1 115 ? 42.229 13.309  9.414   1.00 41.56  ? 132 LEU A C   1 
ATOM   830  O O   . LEU A 1 115 ? 41.142 13.870  9.614   1.00 45.32  ? 132 LEU A O   1 
ATOM   831  C CB  . LEU A 1 115 ? 42.186 13.834  6.949   1.00 44.71  ? 132 LEU A CB  1 
ATOM   832  C CG  . LEU A 1 115 ? 42.894 14.405  5.710   1.00 45.29  ? 132 LEU A CG  1 
ATOM   833  C CD1 . LEU A 1 115 ? 42.003 14.298  4.478   1.00 41.95  ? 132 LEU A CD1 1 
ATOM   834  C CD2 . LEU A 1 115 ? 43.276 15.844  5.916   1.00 47.81  ? 132 LEU A CD2 1 
ATOM   835  N N   . GLY A 1 116 ? 42.701 12.366  10.219  1.00 43.85  ? 133 GLY A N   1 
ATOM   836  C CA  . GLY A 1 116 ? 42.036 12.000  11.457  1.00 40.28  ? 133 GLY A CA  1 
ATOM   837  C C   . GLY A 1 116 ? 41.155 10.772  11.320  1.00 37.35  ? 133 GLY A C   1 
ATOM   838  O O   . GLY A 1 116 ? 40.933 10.223  10.238  1.00 30.20  ? 133 GLY A O   1 
ATOM   839  N N   . LEU A 1 117 ? 40.599 10.376  12.468  1.00 33.29  ? 134 LEU A N   1 
ATOM   840  C CA  . LEU A 1 117 ? 39.858 9.127   12.563  1.00 30.04  ? 134 LEU A CA  1 
ATOM   841  C C   . LEU A 1 117 ? 38.607 9.163   11.722  1.00 27.48  ? 134 LEU A C   1 
ATOM   842  O O   . LEU A 1 117 ? 38.193 8.140   11.171  1.00 27.16  ? 134 LEU A O   1 
ATOM   843  C CB  . LEU A 1 117 ? 39.475 8.864   14.029  1.00 25.58  ? 134 LEU A CB  1 
ATOM   844  C CG  . LEU A 1 117 ? 38.676 7.602   14.293  1.00 24.91  ? 134 LEU A CG  1 
ATOM   845  C CD1 . LEU A 1 117 ? 39.418 6.351   13.764  1.00 29.81  ? 134 LEU A CD1 1 
ATOM   846  C CD2 . LEU A 1 117 ? 38.421 7.448   15.837  1.00 31.62  ? 134 LEU A CD2 1 
ATOM   847  N N   . GLY A 1 118 ? 37.936 10.307  11.692  1.00 32.54  ? 135 GLY A N   1 
ATOM   848  C CA  . GLY A 1 118 ? 36.732 10.410  10.902  1.00 27.15  ? 135 GLY A CA  1 
ATOM   849  C C   . GLY A 1 118 ? 37.030 10.179  9.428   1.00 30.14  ? 135 GLY A C   1 
ATOM   850  O O   . GLY A 1 118 ? 36.287 9.488   8.735   1.00 25.94  ? 135 GLY A O   1 
ATOM   851  N N   . HIS A 1 119 ? 38.143 10.726  8.947   1.00 28.70  ? 136 HIS A N   1 
ATOM   852  C CA  . HIS A 1 119 ? 38.529 10.472  7.561   1.00 34.17  ? 136 HIS A CA  1 
ATOM   853  C C   . HIS A 1 119 ? 38.901 9.010   7.345   1.00 27.68  ? 136 HIS A C   1 
ATOM   854  O O   . HIS A 1 119 ? 38.561 8.420   6.304   1.00 26.70  ? 136 HIS A O   1 
ATOM   855  C CB  . HIS A 1 119 ? 39.685 11.382  7.167   1.00 32.91  ? 136 HIS A CB  1 
ATOM   856  C CG  . HIS A 1 119 ? 40.135 11.197  5.749   1.00 37.31  ? 136 HIS A CG  1 
ATOM   857  N ND1 . HIS A 1 119 ? 39.377 11.598  4.667   1.00 35.15  ? 136 HIS A ND1 1 
ATOM   858  C CD2 . HIS A 1 119 ? 41.279 10.680  5.241   1.00 35.49  ? 136 HIS A CD2 1 
ATOM   859  C CE1 . HIS A 1 119 ? 40.032 11.323  3.551   1.00 37.28  ? 136 HIS A CE1 1 
ATOM   860  N NE2 . HIS A 1 119 ? 41.192 10.773  3.870   1.00 40.91  ? 136 HIS A NE2 1 
ATOM   861  N N   . ALA A 1 120 ? 39.608 8.413   8.310   1.00 30.42  ? 137 ALA A N   1 
ATOM   862  C CA  . ALA A 1 120 ? 39.970 7.008   8.177   1.00 27.91  ? 137 ALA A CA  1 
ATOM   863  C C   . ALA A 1 120 ? 38.720 6.149   8.108   1.00 26.61  ? 137 ALA A C   1 
ATOM   864  O O   . ALA A 1 120 ? 38.656 5.194   7.330   1.00 25.14  ? 137 ALA A O   1 
ATOM   865  C CB  . ALA A 1 120 ? 40.875 6.570   9.323   1.00 30.71  ? 137 ALA A CB  1 
ATOM   866  N N   . VAL A 1 121 ? 37.713 6.465   8.919   1.00 28.82  ? 138 VAL A N   1 
ATOM   867  C CA  . VAL A 1 121 ? 36.483 5.684   8.883   1.00 25.41  ? 138 VAL A CA  1 
ATOM   868  C C   . VAL A 1 121 ? 35.761 5.875   7.542   1.00 26.93  ? 138 VAL A C   1 
ATOM   869  O O   . VAL A 1 121 ? 35.285 4.910   6.925   1.00 27.07  ? 138 VAL A O   1 
ATOM   870  C CB  . VAL A 1 121 ? 35.596 6.051   10.083  1.00 24.90  ? 138 VAL A CB  1 
ATOM   871  C CG1 . VAL A 1 121 ? 34.214 5.475   9.928   1.00 27.33  ? 138 VAL A CG1 1 
ATOM   872  C CG2 . VAL A 1 121 ? 36.234 5.576   11.427  1.00 29.22  ? 138 VAL A CG2 1 
ATOM   873  N N   . LEU A 1 122 ? 35.638 7.123   7.077   1.00 26.20  ? 139 LEU A N   1 
ATOM   874  C CA  . LEU A 1 122 ? 35.029 7.357   5.771   1.00 33.65  ? 139 LEU A CA  1 
ATOM   875  C C   . LEU A 1 122 ? 35.778 6.637   4.651   1.00 31.40  ? 139 LEU A C   1 
ATOM   876  O O   . LEU A 1 122 ? 35.151 6.144   3.713   1.00 28.60  ? 139 LEU A O   1 
ATOM   877  C CB  . LEU A 1 122 ? 34.971 8.853   5.484   1.00 31.23  ? 139 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 122 ? 34.329 9.294   4.183   1.00 32.97  ? 139 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 122 ? 32.887 8.821   4.070   1.00 35.90  ? 139 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 122 ? 34.416 10.817  4.088   1.00 39.41  ? 139 LEU A CD2 1 
ATOM   881  N N   . THR A 1 123 ? 37.104 6.513   4.771   1.00 30.36  ? 140 THR A N   1 
ATOM   882  C CA  . THR A 1 123 ? 37.895 5.787   3.784   1.00 32.07  ? 140 THR A CA  1 
ATOM   883  C C   . THR A 1 123 ? 37.392 4.360   3.581   1.00 27.58  ? 140 THR A C   1 
ATOM   884  O O   . THR A 1 123 ? 37.558 3.788   2.497   1.00 32.46  ? 140 THR A O   1 
ATOM   885  C CB  . THR A 1 123 ? 39.369 5.790   4.212   1.00 29.70  ? 140 THR A CB  1 
ATOM   886  O OG1 . THR A 1 123 ? 39.914 7.117   4.086   1.00 29.42  ? 140 THR A OG1 1 
ATOM   887  C CG2 . THR A 1 123 ? 40.170 4.856   3.359   1.00 32.43  ? 140 THR A CG2 1 
ATOM   888  N N   . ALA A 1 124 ? 36.762 3.779   4.582   1.00 25.81  ? 141 ALA A N   1 
ATOM   889  C CA  . ALA A 1 124 ? 36.341 2.384   4.525   1.00 22.42  ? 141 ALA A CA  1 
ATOM   890  C C   . ALA A 1 124 ? 34.980 2.193   3.875   1.00 26.66  ? 141 ALA A C   1 
ATOM   891  O O   . ALA A 1 124 ? 34.602 1.051   3.594   1.00 32.05  ? 141 ALA A O   1 
ATOM   892  C CB  . ALA A 1 124 ? 36.326 1.785   5.963   1.00 27.16  ? 141 ALA A CB  1 
ATOM   893  N N   . ALA A 1 125 ? 34.255 3.274   3.609   1.00 25.80  ? 142 ALA A N   1 
ATOM   894  C CA  . ALA A 1 125 ? 32.899 3.161   3.080   1.00 32.97  ? 142 ALA A CA  1 
ATOM   895  C C   . ALA A 1 125 ? 32.793 2.287   1.836   1.00 32.69  ? 142 ALA A C   1 
ATOM   896  O O   . ALA A 1 125 ? 31.843 1.487   1.752   1.00 30.77  ? 142 ALA A O   1 
ATOM   897  C CB  . ALA A 1 125 ? 32.343 4.569   2.795   1.00 37.15  ? 142 ALA A CB  1 
ATOM   898  N N   . PRO A 1 126 ? 33.700 2.347   0.865   1.00 29.83  ? 143 PRO A N   1 
ATOM   899  C CA  . PRO A 1 126 ? 33.531 1.471   -0.308  1.00 33.14  ? 143 PRO A CA  1 
ATOM   900  C C   . PRO A 1 126 ? 33.555 -0.013  0.044   1.00 31.71  ? 143 PRO A C   1 
ATOM   901  O O   . PRO A 1 126 ? 32.926 -0.814  -0.653  1.00 38.47  ? 143 PRO A O   1 
ATOM   902  C CB  . PRO A 1 126 ? 34.704 1.869   -1.223  1.00 33.30  ? 143 PRO A CB  1 
ATOM   903  C CG  . PRO A 1 126 ? 35.111 3.249   -0.748  1.00 31.37  ? 143 PRO A CG  1 
ATOM   904  C CD  . PRO A 1 126 ? 34.841 3.255   0.735   1.00 28.64  ? 143 PRO A CD  1 
ATOM   905  N N   . ALA A 1 127 ? 34.232 -0.403  1.123   1.00 31.51  ? 144 ALA A N   1 
ATOM   906  C CA  . ALA A 1 127 ? 34.239 -1.798  1.551   1.00 31.71  ? 144 ALA A CA  1 
ATOM   907  C C   . ALA A 1 127 ? 33.066 -2.156  2.463   1.00 32.69  ? 144 ALA A C   1 
ATOM   908  O O   . ALA A 1 127 ? 32.669 -3.323  2.550   1.00 31.98  ? 144 ALA A O   1 
ATOM   909  C CB  . ALA A 1 127 ? 35.541 -2.112  2.290   1.00 32.96  ? 144 ALA A CB  1 
ATOM   910  N N   . VAL A 1 128 ? 32.513 -1.190  3.161   1.00 35.98  ? 145 VAL A N   1 
ATOM   911  C CA  . VAL A 1 128 ? 31.438 -1.484  4.094   1.00 29.22  ? 145 VAL A CA  1 
ATOM   912  C C   . VAL A 1 128 ? 30.078 -1.485  3.415   1.00 36.10  ? 145 VAL A C   1 
ATOM   913  O O   . VAL A 1 128 ? 29.199 -2.265  3.789   1.00 41.68  ? 145 VAL A O   1 
ATOM   914  C CB  . VAL A 1 128 ? 31.514 -0.465  5.242   1.00 29.60  ? 145 VAL A CB  1 
ATOM   915  C CG1 . VAL A 1 128 ? 30.231 -0.499  6.108   1.00 30.81  ? 145 VAL A CG1 1 
ATOM   916  C CG2 . VAL A 1 128 ? 32.772 -0.751  6.067   1.00 30.89  ? 145 VAL A CG2 1 
ATOM   917  N N   . GLY A 1 129 ? 29.854 -0.595  2.444   1.00 35.27  ? 146 GLY A N   1 
ATOM   918  C CA  . GLY A 1 129 ? 28.525 -0.525  1.875   1.00 36.99  ? 146 GLY A CA  1 
ATOM   919  C C   . GLY A 1 129 ? 27.532 0.034   2.886   1.00 38.70  ? 146 GLY A C   1 
ATOM   920  O O   . GLY A 1 129 ? 27.866 0.867   3.734   1.00 40.84  ? 146 GLY A O   1 
ATOM   921  N N   . ASN A 1 130 ? 26.286 -0.419  2.786   1.00 38.15  ? 147 ASN A N   1 
ATOM   922  C CA  . ASN A 1 130 ? 25.220 0.038   3.680   1.00 51.90  ? 147 ASN A CA  1 
ATOM   923  C C   . ASN A 1 130 ? 24.927 -0.967  4.797   1.00 53.37  ? 147 ASN A C   1 
ATOM   924  O O   . ASN A 1 130 ? 23.802 -1.427  4.954   1.00 66.81  ? 147 ASN A O   1 
ATOM   925  C CB  . ASN A 1 130 ? 23.939 0.316   2.893   1.00 57.05  ? 147 ASN A CB  1 
ATOM   926  C CG  . ASN A 1 130 ? 23.068 1.369   3.567   1.00 73.61  ? 147 ASN A CG  1 
ATOM   927  O OD1 . ASN A 1 130 ? 23.579 2.314   4.172   1.00 66.91  ? 147 ASN A OD1 1 
ATOM   928  N ND2 . ASN A 1 130 ? 21.752 1.169   3.529   1.00 93.72  ? 147 ASN A ND2 1 
ATOM   929  N N   . GLU A 1 131 ? 25.932 -1.339  5.569   1.00 42.02  ? 148 GLU A N   1 
ATOM   930  C CA  . GLU A 1 131 ? 25.670 -2.216  6.701   1.00 43.94  ? 148 GLU A CA  1 
ATOM   931  C C   . GLU A 1 131 ? 26.366 -1.689  7.951   1.00 34.99  ? 148 GLU A C   1 
ATOM   932  O O   . GLU A 1 131 ? 27.342 -0.941  7.855   1.00 32.06  ? 148 GLU A O   1 
ATOM   933  C CB  . GLU A 1 131 ? 26.075 -3.659  6.399   1.00 46.03  ? 148 GLU A CB  1 
ATOM   934  C CG  . GLU A 1 131 ? 27.504 -3.963  6.292   1.00 47.68  ? 148 GLU A CG  1 
ATOM   935  C CD  . GLU A 1 131 ? 27.691 -5.358  5.742   1.00 47.16  ? 148 GLU A CD  1 
ATOM   936  O OE1 . GLU A 1 131 ? 27.593 -5.540  4.507   1.00 46.62  ? 148 GLU A OE1 1 
ATOM   937  O OE2 . GLU A 1 131 ? 27.899 -6.283  6.548   1.00 40.60  ? 148 GLU A OE2 1 
ATOM   938  N N   . PRO A 1 132 ? 25.854 -2.028  9.126   1.00 34.49  ? 149 PRO A N   1 
ATOM   939  C CA  . PRO A 1 132 ? 26.521 -1.605  10.363  1.00 34.90  ? 149 PRO A CA  1 
ATOM   940  C C   . PRO A 1 132 ? 27.880 -2.269  10.487  1.00 28.12  ? 149 PRO A C   1 
ATOM   941  O O   . PRO A 1 132 ? 28.082 -3.396  10.029  1.00 32.86  ? 149 PRO A O   1 
ATOM   942  C CB  . PRO A 1 132 ? 25.554 -2.075  11.460  1.00 35.21  ? 149 PRO A CB  1 
ATOM   943  C CG  . PRO A 1 132 ? 24.938 -3.316  10.884  1.00 39.45  ? 149 PRO A CG  1 
ATOM   944  C CD  . PRO A 1 132 ? 24.768 -2.997  9.394   1.00 41.13  ? 149 PRO A CD  1 
ATOM   945  N N   . PHE A 1 133 ? 28.826 -1.553  11.098  1.00 29.32  ? 150 PHE A N   1 
ATOM   946  C CA  . PHE A 1 133 ? 30.194 -2.053  11.150  1.00 26.64  ? 150 PHE A CA  1 
ATOM   947  C C   . PHE A 1 133 ? 30.903 -1.622  12.416  1.00 28.81  ? 150 PHE A C   1 
ATOM   948  O O   . PHE A 1 133 ? 30.579 -0.607  13.032  1.00 31.02  ? 150 PHE A O   1 
ATOM   949  C CB  . PHE A 1 133 ? 31.003 -1.562  9.943   1.00 27.66  ? 150 PHE A CB  1 
ATOM   950  C CG  . PHE A 1 133 ? 31.138 -0.092  9.899   1.00 23.77  ? 150 PHE A CG  1 
ATOM   951  C CD1 . PHE A 1 133 ? 30.071 0.704   9.527   1.00 24.10  ? 150 PHE A CD1 1 
ATOM   952  C CD2 . PHE A 1 133 ? 32.314 0.511   10.248  1.00 20.08  ? 150 PHE A CD2 1 
ATOM   953  C CE1 . PHE A 1 133 ? 30.180 2.070   9.515   1.00 24.96  ? 150 PHE A CE1 1 
ATOM   954  C CE2 . PHE A 1 133 ? 32.429 1.907   10.240  1.00 24.27  ? 150 PHE A CE2 1 
ATOM   955  C CZ  . PHE A 1 133 ? 31.357 2.678   9.877   1.00 27.32  ? 150 PHE A CZ  1 
ATOM   956  N N   . ALA A 1 134 ? 31.951 -2.363  12.745  1.00 26.90  ? 151 ALA A N   1 
ATOM   957  C CA  . ALA A 1 134 ? 32.743 -2.088  13.921  1.00 23.34  ? 151 ALA A CA  1 
ATOM   958  C C   . ALA A 1 134 ? 33.945 -1.244  13.548  1.00 24.35  ? 151 ALA A C   1 
ATOM   959  O O   . ALA A 1 134 ? 34.448 -1.307  12.426  1.00 25.31  ? 151 ALA A O   1 
ATOM   960  C CB  . ALA A 1 134 ? 33.221 -3.393  14.571  1.00 28.40  ? 151 ALA A CB  1 
ATOM   961  N N   . VAL A 1 135 ? 34.395 -0.449  14.500  1.00 23.02  ? 152 VAL A N   1 
ATOM   962  C CA  . VAL A 1 135 ? 35.664 0.273   14.424  1.00 22.31  ? 152 VAL A CA  1 
ATOM   963  C C   . VAL A 1 135 ? 36.450 -0.051  15.672  1.00 27.53  ? 152 VAL A C   1 
ATOM   964  O O   . VAL A 1 135 ? 35.911 0.077   16.786  1.00 26.31  ? 152 VAL A O   1 
ATOM   965  C CB  . VAL A 1 135 ? 35.461 1.795   14.305  1.00 22.18  ? 152 VAL A CB  1 
ATOM   966  C CG1 . VAL A 1 135 ? 36.803 2.487   14.209  1.00 25.53  ? 152 VAL A CG1 1 
ATOM   967  C CG2 . VAL A 1 135 ? 34.614 2.119   13.084  1.00 26.13  ? 152 VAL A CG2 1 
ATOM   968  N N   . LEU A 1 136 ? 37.725 -0.440  15.506  1.00 23.24  ? 153 LEU A N   1 
ATOM   969  C CA  . LEU A 1 136 ? 38.580 -0.717  16.655  1.00 23.01  ? 153 LEU A CA  1 
ATOM   970  C C   . LEU A 1 136 ? 39.915 0.004   16.498  1.00 27.15  ? 153 LEU A C   1 
ATOM   971  O O   . LEU A 1 136 ? 40.598 -0.139  15.473  1.00 23.05  ? 153 LEU A O   1 
ATOM   972  C CB  . LEU A 1 136 ? 38.864 -2.208  16.856  1.00 22.64  ? 153 LEU A CB  1 
ATOM   973  C CG  . LEU A 1 136 ? 37.676 -3.126  17.039  1.00 19.43  ? 153 LEU A CG  1 
ATOM   974  C CD1 . LEU A 1 136 ? 37.100 -3.537  15.684  1.00 23.12  ? 153 LEU A CD1 1 
ATOM   975  C CD2 . LEU A 1 136 ? 38.085 -4.310  17.848  1.00 23.91  ? 153 LEU A CD2 1 
ATOM   976  N N   . LEU A 1 137 ? 40.282 0.758   17.520  1.00 18.70  ? 154 LEU A N   1 
ATOM   977  C CA  . LEU A 1 137 ? 41.551 1.470   17.587  1.00 20.28  ? 154 LEU A CA  1 
ATOM   978  C C   . LEU A 1 137 ? 42.505 0.643   18.433  1.00 25.71  ? 154 LEU A C   1 
ATOM   979  O O   . LEU A 1 137 ? 42.316 0.471   19.653  1.00 21.91  ? 154 LEU A O   1 
ATOM   980  C CB  . LEU A 1 137 ? 41.371 2.863   18.153  1.00 24.14  ? 154 LEU A CB  1 
ATOM   981  C CG  . LEU A 1 137 ? 40.130 3.634   17.722  1.00 26.08  ? 154 LEU A CG  1 
ATOM   982  C CD1 . LEU A 1 137 ? 40.199 4.978   18.426  1.00 27.60  ? 154 LEU A CD1 1 
ATOM   983  C CD2 . LEU A 1 137 ? 40.020 3.789   16.202  1.00 23.39  ? 154 LEU A CD2 1 
ATOM   984  N N   . ALA A 1 138 ? 43.520 0.102   17.779  1.00 21.81  ? 155 ALA A N   1 
ATOM   985  C CA  . ALA A 1 138 ? 44.362 -0.881  18.440  1.00 20.89  ? 155 ALA A CA  1 
ATOM   986  C C   . ALA A 1 138 ? 45.172 -0.283  19.583  1.00 23.91  ? 155 ALA A C   1 
ATOM   987  O O   . ALA A 1 138 ? 45.643 -1.046  20.438  1.00 24.32  ? 155 ALA A O   1 
ATOM   988  C CB  . ALA A 1 138 ? 45.289 -1.542  17.422  1.00 23.39  ? 155 ALA A CB  1 
ATOM   989  N N   . ASP A 1 139 ? 45.364 1.043   19.595  1.00 26.12  ? 156 ASP A N   1 
ATOM   990  C CA  . ASP A 1 139 ? 46.079 1.684   20.697  1.00 26.47  ? 156 ASP A CA  1 
ATOM   991  C C   . ASP A 1 139 ? 45.341 1.480   22.017  1.00 28.54  ? 156 ASP A C   1 
ATOM   992  O O   . ASP A 1 139 ? 45.950 1.521   23.095  1.00 26.75  ? 156 ASP A O   1 
ATOM   993  C CB  . ASP A 1 139 ? 46.264 3.187   20.436  1.00 29.96  ? 156 ASP A CB  1 
ATOM   994  C CG  . ASP A 1 139 ? 47.705 3.550   20.028  1.00 35.09  ? 156 ASP A CG  1 
ATOM   995  O OD1 . ASP A 1 139 ? 48.586 2.664   20.132  1.00 33.03  ? 156 ASP A OD1 1 
ATOM   996  O OD2 . ASP A 1 139 ? 47.970 4.720   19.635  1.00 33.41  ? 156 ASP A OD2 1 
ATOM   997  N N   . ASP A 1 140 ? 44.037 1.294   21.958  1.00 24.48  ? 157 ASP A N   1 
ATOM   998  C CA  . ASP A 1 140 ? 43.264 0.921   23.145  1.00 22.11  ? 157 ASP A CA  1 
ATOM   999  C C   . ASP A 1 140 ? 43.316 -0.584  23.244  1.00 21.98  ? 157 ASP A C   1 
ATOM   1000 O O   . ASP A 1 140 ? 42.526 -1.290  22.641  1.00 24.49  ? 157 ASP A O   1 
ATOM   1001 C CB  . ASP A 1 140 ? 41.831 1.434   23.066  1.00 22.61  ? 157 ASP A CB  1 
ATOM   1002 C CG  . ASP A 1 140 ? 41.732 2.904   23.422  1.00 31.01  ? 157 ASP A CG  1 
ATOM   1003 O OD1 . ASP A 1 140 ? 42.674 3.394   24.057  1.00 30.84  ? 157 ASP A OD1 1 
ATOM   1004 O OD2 . ASP A 1 140 ? 40.721 3.575   23.092  1.00 36.01  ? 157 ASP A OD2 1 
ATOM   1005 N N   . LEU A 1 141 ? 44.271 -1.071  24.031  1.00 25.75  ? 158 LEU A N   1 
ATOM   1006 C CA  . LEU A 1 141 ? 44.430 -2.488  24.280  1.00 24.39  ? 158 LEU A CA  1 
ATOM   1007 C C   . LEU A 1 141 ? 43.538 -2.886  25.444  1.00 26.95  ? 158 LEU A C   1 
ATOM   1008 O O   . LEU A 1 141 ? 43.718 -2.397  26.561  1.00 24.74  ? 158 LEU A O   1 
ATOM   1009 C CB  . LEU A 1 141 ? 45.886 -2.786  24.591  1.00 21.11  ? 158 LEU A CB  1 
ATOM   1010 C CG  . LEU A 1 141 ? 46.261 -4.246  24.838  1.00 31.92  ? 158 LEU A CG  1 
ATOM   1011 C CD1 . LEU A 1 141 ? 45.844 -5.153  23.803  1.00 33.33  ? 158 LEU A CD1 1 
ATOM   1012 C CD2 . LEU A 1 141 ? 47.767 -4.296  25.011  1.00 33.52  ? 158 LEU A CD2 1 
ATOM   1013 N N   . ILE A 1 142 ? 42.595 -3.778  25.191  1.00 27.16  ? 159 ILE A N   1 
ATOM   1014 C CA  . ILE A 1 142 ? 41.590 -4.123  26.180  1.00 24.94  ? 159 ILE A CA  1 
ATOM   1015 C C   . ILE A 1 142 ? 41.707 -5.596  26.507  1.00 27.76  ? 159 ILE A C   1 
ATOM   1016 O O   . ILE A 1 142 ? 41.649 -6.443  25.617  1.00 28.20  ? 159 ILE A O   1 
ATOM   1017 C CB  . ILE A 1 142 ? 40.170 -3.798  25.711  1.00 29.44  ? 159 ILE A CB  1 
ATOM   1018 C CG1 . ILE A 1 142 ? 40.030 -2.300  25.409  1.00 27.94  ? 159 ILE A CG1 1 
ATOM   1019 C CG2 . ILE A 1 142 ? 39.205 -4.256  26.806  1.00 32.64  ? 159 ILE A CG2 1 
ATOM   1020 C CD1 . ILE A 1 142 ? 38.670 -1.901  24.908  1.00 27.95  ? 159 ILE A CD1 1 
ATOM   1021 N N   . ASP A 1 143 ? 41.867 -5.897  27.791  1.00 25.71  ? 160 ASP A N   1 
ATOM   1022 C CA  . ASP A 1 143 ? 41.946 -7.256  28.295  1.00 27.85  ? 160 ASP A CA  1 
ATOM   1023 C C   . ASP A 1 143 ? 40.631 -7.520  29.012  1.00 31.50  ? 160 ASP A C   1 
ATOM   1024 O O   . ASP A 1 143 ? 40.306 -6.818  29.974  1.00 29.55  ? 160 ASP A O   1 
ATOM   1025 C CB  . ASP A 1 143 ? 43.152 -7.380  29.230  1.00 32.66  ? 160 ASP A CB  1 
ATOM   1026 C CG  . ASP A 1 143 ? 43.346 -8.764  29.791  1.00 42.99  ? 160 ASP A CG  1 
ATOM   1027 O OD1 . ASP A 1 143 ? 43.219 -9.741  29.019  1.00 39.79  ? 160 ASP A OD1 1 
ATOM   1028 O OD2 . ASP A 1 143 ? 43.701 -8.847  31.005  1.00 37.94  ? 160 ASP A OD2 1 
ATOM   1029 N N   . ALA A 1 144 ? 39.850 -8.474  28.501  1.00 31.44  ? 161 ALA A N   1 
ATOM   1030 C CA  . ALA A 1 144 ? 38.490 -8.702  28.975  1.00 28.25  ? 161 ALA A CA  1 
ATOM   1031 C C   . ALA A 1 144 ? 38.158 -10.176 28.875  1.00 32.61  ? 161 ALA A C   1 
ATOM   1032 O O   . ALA A 1 144 ? 38.588 -10.859 27.940  1.00 33.21  ? 161 ALA A O   1 
ATOM   1033 C CB  . ALA A 1 144 ? 37.474 -7.894  28.165  1.00 28.08  ? 161 ALA A CB  1 
ATOM   1034 N N   . ASP A 1 145 ? 37.347 -10.649 29.818  1.00 29.80  ? 162 ASP A N   1 
ATOM   1035 C CA  . ASP A 1 145 ? 36.925 -12.045 29.821  1.00 31.14  ? 162 ASP A CA  1 
ATOM   1036 C C   . ASP A 1 145 ? 36.003 -12.364 28.655  1.00 35.62  ? 162 ASP A C   1 
ATOM   1037 O O   . ASP A 1 145 ? 35.995 -13.500 28.170  1.00 31.40  ? 162 ASP A O   1 
ATOM   1038 C CB  . ASP A 1 145 ? 36.195 -12.420 31.123  1.00 31.83  ? 162 ASP A CB  1 
ATOM   1039 C CG  . ASP A 1 145 ? 37.097 -12.398 32.340  1.00 42.73  ? 162 ASP A CG  1 
ATOM   1040 O OD1 . ASP A 1 145 ? 38.340 -12.410 32.162  1.00 40.46  ? 162 ASP A OD1 1 
ATOM   1041 O OD2 . ASP A 1 145 ? 36.552 -12.383 33.479  1.00 46.78  ? 162 ASP A OD2 1 
ATOM   1042 N N   . THR A 1 146 ? 35.138 -11.420 28.277  1.00 32.49  ? 163 THR A N   1 
ATOM   1043 C CA  . THR A 1 146 ? 34.304 -11.508 27.090  1.00 31.12  ? 163 THR A CA  1 
ATOM   1044 C C   . THR A 1 146 ? 34.713 -10.401 26.138  1.00 30.43  ? 163 THR A C   1 
ATOM   1045 O O   . THR A 1 146 ? 34.970 -9.283  26.577  1.00 29.81  ? 163 THR A O   1 
ATOM   1046 C CB  . THR A 1 146 ? 32.796 -11.376 27.390  1.00 38.29  ? 163 THR A CB  1 
ATOM   1047 O OG1 . THR A 1 146 ? 32.528 -10.104 27.979  1.00 52.08  ? 163 THR A OG1 1 
ATOM   1048 C CG2 . THR A 1 146 ? 32.361 -12.413 28.349  1.00 33.83  ? 163 THR A CG2 1 
ATOM   1049 N N   . PRO A 1 147 ? 34.825 -10.676 24.844  1.00 28.92  ? 164 PRO A N   1 
ATOM   1050 C CA  . PRO A 1 147 ? 35.335 -9.639  23.933  1.00 27.16  ? 164 PRO A CA  1 
ATOM   1051 C C   . PRO A 1 147 ? 34.487 -8.380  24.016  1.00 23.59  ? 164 PRO A C   1 
ATOM   1052 O O   . PRO A 1 147 ? 33.259 -8.437  23.961  1.00 27.25  ? 164 PRO A O   1 
ATOM   1053 C CB  . PRO A 1 147 ? 35.242 -10.305 22.554  1.00 30.07  ? 164 PRO A CB  1 
ATOM   1054 C CG  . PRO A 1 147 ? 35.337 -11.754 22.826  1.00 30.15  ? 164 PRO A CG  1 
ATOM   1055 C CD  . PRO A 1 147 ? 34.695 -11.986 24.191  1.00 27.04  ? 164 PRO A CD  1 
ATOM   1056 N N   . VAL A 1 148 ? 35.151 -7.225  24.169  1.00 24.31  ? 165 VAL A N   1 
ATOM   1057 C CA  . VAL A 1 148 ? 34.398 -5.984  24.343  1.00 25.09  ? 165 VAL A CA  1 
ATOM   1058 C C   . VAL A 1 148 ? 33.557 -5.677  23.109  1.00 29.12  ? 165 VAL A C   1 
ATOM   1059 O O   . VAL A 1 148 ? 32.402 -5.209  23.212  1.00 23.67  ? 165 VAL A O   1 
ATOM   1060 C CB  . VAL A 1 148 ? 35.363 -4.839  24.710  1.00 26.21  ? 165 VAL A CB  1 
ATOM   1061 C CG1 . VAL A 1 148 ? 34.697 -3.499  24.484  1.00 28.64  ? 165 VAL A CG1 1 
ATOM   1062 C CG2 . VAL A 1 148 ? 35.766 -4.969  26.192  1.00 28.06  ? 165 VAL A CG2 1 
ATOM   1063 N N   . LEU A 1 149 ? 34.097 -5.946  21.919  1.00 25.39  ? 166 LEU A N   1 
ATOM   1064 C CA  . LEU A 1 149 ? 33.310 -5.678  20.722  1.00 26.44  ? 166 LEU A CA  1 
ATOM   1065 C C   . LEU A 1 149 ? 32.027 -6.491  20.727  1.00 23.61  ? 166 LEU A C   1 
ATOM   1066 O O   . LEU A 1 149 ? 30.974 -6.006  20.284  1.00 23.40  ? 166 LEU A O   1 
ATOM   1067 C CB  . LEU A 1 149 ? 34.122 -5.973  19.456  1.00 20.64  ? 166 LEU A CB  1 
ATOM   1068 C CG  . LEU A 1 149 ? 33.469 -5.393  18.199  1.00 26.48  ? 166 LEU A CG  1 
ATOM   1069 C CD1 . LEU A 1 149 ? 33.556 -3.862  18.151  1.00 24.31  ? 166 LEU A CD1 1 
ATOM   1070 C CD2 . LEU A 1 149 ? 34.057 -5.987  16.909  1.00 23.64  ? 166 LEU A CD2 1 
ATOM   1071 N N   . LYS A 1 150 ? 32.095 -7.728  21.227  1.00 23.35  ? 167 LYS A N   1 
ATOM   1072 C CA  . LYS A 1 150 ? 30.889 -8.553  21.337  1.00 27.27  ? 167 LYS A CA  1 
ATOM   1073 C C   . LYS A 1 150 ? 29.881 -7.927  22.287  1.00 29.26  ? 167 LYS A C   1 
ATOM   1074 O O   . LYS A 1 150 ? 28.672 -7.947  22.023  1.00 29.24  ? 167 LYS A O   1 
ATOM   1075 C CB  . LYS A 1 150 ? 31.243 -9.966  21.820  1.00 28.49  ? 167 LYS A CB  1 
ATOM   1076 C CG  . LYS A 1 150 ? 30.056 -10.950 21.890  1.00 32.08  ? 167 LYS A CG  1 
ATOM   1077 C CD  . LYS A 1 150 ? 29.449 -11.160 20.530  1.00 43.66  ? 167 LYS A CD  1 
ATOM   1078 C CE  . LYS A 1 150 ? 28.342 -12.212 20.552  1.00 54.30  ? 167 LYS A CE  1 
ATOM   1079 N NZ  . LYS A 1 150 ? 27.338 -11.945 19.468  1.00 56.52  ? 167 LYS A NZ  1 
ATOM   1080 N N   . GLN A 1 151 ? 30.359 -7.400  23.422  1.00 28.21  ? 168 GLN A N   1 
ATOM   1081 C CA  . GLN A 1 151 ? 29.453 -6.731  24.351  1.00 26.18  ? 168 GLN A CA  1 
ATOM   1082 C C   . GLN A 1 151 ? 28.752 -5.573  23.655  1.00 29.61  ? 168 GLN A C   1 
ATOM   1083 O O   . GLN A 1 151 ? 27.541 -5.370  23.831  1.00 26.72  ? 168 GLN A O   1 
ATOM   1084 C CB  . GLN A 1 151 ? 30.214 -6.234  25.591  1.00 27.06  ? 168 GLN A CB  1 
ATOM   1085 C CG  . GLN A 1 151 ? 31.038 -7.326  26.337  1.00 30.10  ? 168 GLN A CG  1 
ATOM   1086 C CD  . GLN A 1 151 ? 31.868 -6.757  27.475  1.00 30.30  ? 168 GLN A CD  1 
ATOM   1087 O OE1 . GLN A 1 151 ? 31.455 -5.831  28.164  1.00 28.92  ? 168 GLN A OE1 1 
ATOM   1088 N NE2 . GLN A 1 151 ? 33.043 -7.296  27.664  1.00 30.69  ? 168 GLN A NE2 1 
ATOM   1089 N N   . LEU A 1 152 ? 29.508 -4.784  22.882  1.00 25.87  ? 169 LEU A N   1 
ATOM   1090 C CA  . LEU A 1 152 ? 28.914 -3.664  22.144  1.00 31.25  ? 169 LEU A CA  1 
ATOM   1091 C C   . LEU A 1 152 ? 27.980 -4.135  21.034  1.00 27.47  ? 169 LEU A C   1 
ATOM   1092 O O   . LEU A 1 152 ? 26.904 -3.551  20.829  1.00 25.30  ? 169 LEU A O   1 
ATOM   1093 C CB  . LEU A 1 152 ? 30.003 -2.785  21.534  1.00 28.63  ? 169 LEU A CB  1 
ATOM   1094 C CG  . LEU A 1 152 ? 31.068 -2.230  22.470  1.00 28.26  ? 169 LEU A CG  1 
ATOM   1095 C CD1 . LEU A 1 152 ? 31.869 -1.156  21.724  1.00 27.95  ? 169 LEU A CD1 1 
ATOM   1096 C CD2 . LEU A 1 152 ? 30.468 -1.655  23.746  1.00 29.66  ? 169 LEU A CD2 1 
ATOM   1097 N N   . ILE A 1 153 ? 28.373 -5.172  20.292  1.00 26.42  ? 170 ILE A N   1 
ATOM   1098 C CA  . ILE A 1 153 ? 27.511 -5.667  19.210  1.00 27.27  ? 170 ILE A CA  1 
ATOM   1099 C C   . ILE A 1 153 ? 26.165 -6.152  19.759  1.00 32.70  ? 170 ILE A C   1 
ATOM   1100 O O   . ILE A 1 153 ? 25.112 -5.900  19.155  1.00 30.78  ? 170 ILE A O   1 
ATOM   1101 C CB  . ILE A 1 153 ? 28.216 -6.786  18.417  1.00 31.91  ? 170 ILE A CB  1 
ATOM   1102 C CG1 . ILE A 1 153 ? 29.252 -6.185  17.439  1.00 26.28  ? 170 ILE A CG1 1 
ATOM   1103 C CG2 . ILE A 1 153 ? 27.177 -7.634  17.693  1.00 28.68  ? 170 ILE A CG2 1 
ATOM   1104 C CD1 . ILE A 1 153 ? 30.293 -7.194  16.881  1.00 34.01  ? 170 ILE A CD1 1 
ATOM   1105 N N   . ASP A 1 154 ? 26.175 -6.888  20.885  1.00 31.53  ? 171 ASP A N   1 
ATOM   1106 C CA  . ASP A 1 154 ? 24.914 -7.400  21.430  1.00 31.62  ? 171 ASP A CA  1 
ATOM   1107 C C   . ASP A 1 154 ? 23.991 -6.263  21.845  1.00 30.20  ? 171 ASP A C   1 
ATOM   1108 O O   . ASP A 1 154 ? 22.776 -6.346  21.648  1.00 34.32  ? 171 ASP A O   1 
ATOM   1109 C CB  . ASP A 1 154 ? 25.157 -8.344  22.601  1.00 32.95  ? 171 ASP A CB  1 
ATOM   1110 C CG  . ASP A 1 154 ? 25.752 -9.672  22.159  1.00 40.03  ? 171 ASP A CG  1 
ATOM   1111 O OD1 . ASP A 1 154 ? 25.685 -9.984  20.958  1.00 40.94  ? 171 ASP A OD1 1 
ATOM   1112 O OD2 . ASP A 1 154 ? 26.274 -10.407 23.016  1.00 42.52  ? 171 ASP A OD2 1 
ATOM   1113 N N   . VAL A 1 155 ? 24.546 -5.191  22.409  1.00 25.74  ? 172 VAL A N   1 
ATOM   1114 C CA  . VAL A 1 155 ? 23.737 -4.005  22.681  1.00 32.44  ? 172 VAL A CA  1 
ATOM   1115 C C   . VAL A 1 155 ? 23.233 -3.384  21.385  1.00 33.79  ? 172 VAL A C   1 
ATOM   1116 O O   . VAL A 1 155 ? 22.093 -2.910  21.314  1.00 34.25  ? 172 VAL A O   1 
ATOM   1117 C CB  . VAL A 1 155 ? 24.535 -2.976  23.503  1.00 30.63  ? 172 VAL A CB  1 
ATOM   1118 C CG1 . VAL A 1 155 ? 23.685 -1.733  23.771  1.00 31.50  ? 172 VAL A CG1 1 
ATOM   1119 C CG2 . VAL A 1 155 ? 24.997 -3.588  24.814  1.00 31.05  ? 172 VAL A CG2 1 
ATOM   1120 N N   . ALA A 1 156 ? 24.096 -3.298  20.372  1.00 30.21  ? 173 ALA A N   1 
ATOM   1121 C CA  . ALA A 1 156 ? 23.689 -2.685  19.107  1.00 32.07  ? 173 ALA A CA  1 
ATOM   1122 C C   . ALA A 1 156 ? 22.524 -3.431  18.481  1.00 35.76  ? 173 ALA A C   1 
ATOM   1123 O O   . ALA A 1 156 ? 21.560 -2.816  18.029  1.00 35.28  ? 173 ALA A O   1 
ATOM   1124 C CB  . ALA A 1 156 ? 24.854 -2.651  18.117  1.00 34.39  ? 173 ALA A CB  1 
ATOM   1125 N N   . VAL A 1 157 ? 22.588 -4.760  18.467  1.00 35.71  ? 174 VAL A N   1 
ATOM   1126 C CA  . VAL A 1 157 ? 21.478 -5.543  17.942  1.00 38.11  ? 174 VAL A CA  1 
ATOM   1127 C C   . VAL A 1 157 ? 20.235 -5.359  18.806  1.00 40.24  ? 174 VAL A C   1 
ATOM   1128 O O   . VAL A 1 157 ? 19.126 -5.176  18.292  1.00 40.64  ? 174 VAL A O   1 
ATOM   1129 C CB  . VAL A 1 157 ? 21.866 -7.032  17.851  1.00 38.68  ? 174 VAL A CB  1 
ATOM   1130 C CG1 . VAL A 1 157 ? 20.649 -7.848  17.464  1.00 46.55  ? 174 VAL A CG1 1 
ATOM   1131 C CG2 . VAL A 1 157 ? 22.986 -7.234  16.873  1.00 37.37  ? 174 VAL A CG2 1 
ATOM   1132 N N   . ALA A 1 158 ? 20.392 -5.411  20.134  1.00 41.31  ? 175 ALA A N   1 
ATOM   1133 C CA  . ALA A 1 158 ? 19.225 -5.385  21.010  1.00 38.76  ? 175 ALA A CA  1 
ATOM   1134 C C   . ALA A 1 158 ? 18.512 -4.037  20.973  1.00 45.29  ? 175 ALA A C   1 
ATOM   1135 O O   . ALA A 1 158 ? 17.276 -3.987  20.989  1.00 41.83  ? 175 ALA A O   1 
ATOM   1136 C CB  . ALA A 1 158 ? 19.631 -5.715  22.448  1.00 38.72  ? 175 ALA A CB  1 
ATOM   1137 N N   . ARG A 1 159 ? 19.262 -2.934  20.988  1.00 38.64  ? 176 ARG A N   1 
ATOM   1138 C CA  . ARG A 1 159 ? 18.657 -1.615  21.069  1.00 38.28  ? 176 ARG A CA  1 
ATOM   1139 C C   . ARG A 1 159 ? 18.505 -0.947  19.716  1.00 42.33  ? 176 ARG A C   1 
ATOM   1140 O O   . ARG A 1 159 ? 17.962 0.160   19.645  1.00 42.02  ? 176 ARG A O   1 
ATOM   1141 C CB  . ARG A 1 159 ? 19.461 -0.709  22.005  1.00 38.62  ? 176 ARG A CB  1 
ATOM   1142 C CG  . ARG A 1 159 ? 19.708 -1.358  23.348  1.00 48.30  ? 176 ARG A CG  1 
ATOM   1143 C CD  . ARG A 1 159 ? 19.689 -0.362  24.448  1.00 47.72  ? 176 ARG A CD  1 
ATOM   1144 N NE  . ARG A 1 159 ? 19.717 -0.982  25.767  1.00 46.89  ? 176 ARG A NE  1 
ATOM   1145 C CZ  . ARG A 1 159 ? 18.686 -1.063  26.592  1.00 48.94  ? 176 ARG A CZ  1 
ATOM   1146 N NH1 . ARG A 1 159 ? 17.479 -0.670  26.230  1.00 49.22  ? 176 ARG A NH1 1 
ATOM   1147 N NH2 . ARG A 1 159 ? 18.882 -1.510  27.828  1.00 52.61  ? 176 ARG A NH2 1 
ATOM   1148 N N   . GLN A 1 160 ? 18.969 -1.589  18.645  1.00 40.93  ? 177 GLN A N   1 
ATOM   1149 C CA  . GLN A 1 160 ? 18.814 -1.094  17.274  1.00 46.95  ? 177 GLN A CA  1 
ATOM   1150 C C   . GLN A 1 160 ? 19.399 0.319   17.122  1.00 41.63  ? 177 GLN A C   1 
ATOM   1151 O O   . GLN A 1 160 ? 18.684 1.303   16.926  1.00 49.38  ? 177 GLN A O   1 
ATOM   1152 C CB  . GLN A 1 160 ? 17.330 -1.133  16.888  1.00 53.55  ? 177 GLN A CB  1 
ATOM   1153 C CG  . GLN A 1 160 ? 16.790 -2.540  16.630  1.00 59.94  ? 177 GLN A CG  1 
ATOM   1154 C CD  . GLN A 1 160 ? 15.279 -2.569  16.472  1.00 67.74  ? 177 GLN A CD  1 
ATOM   1155 O OE1 . GLN A 1 160 ? 14.549 -1.888  17.203  1.00 71.70  ? 177 GLN A OE1 1 
ATOM   1156 N NE2 . GLN A 1 160 ? 14.800 -3.363  15.522  1.00 72.28  ? 177 GLN A NE2 1 
ATOM   1157 N N   . GLY A 1 161 ? 20.721 0.407   17.273  1.00 35.35  ? 178 GLY A N   1 
ATOM   1158 C CA  . GLY A 1 161 ? 21.405 1.685   17.110  1.00 33.85  ? 178 GLY A CA  1 
ATOM   1159 C C   . GLY A 1 161 ? 22.914 1.535   17.168  1.00 29.55  ? 178 GLY A C   1 
ATOM   1160 O O   . GLY A 1 161 ? 23.439 0.450   17.392  1.00 34.69  ? 178 GLY A O   1 
ATOM   1161 N N   . SER A 1 162 ? 23.617 2.645   16.963  1.00 30.37  ? 179 SER A N   1 
ATOM   1162 C CA  . SER A 1 162 ? 25.064 2.646   17.130  1.00 29.41  ? 179 SER A CA  1 
ATOM   1163 C C   . SER A 1 162 ? 25.415 2.587   18.619  1.00 30.58  ? 179 SER A C   1 
ATOM   1164 O O   . SER A 1 162 ? 24.640 3.028   19.468  1.00 29.56  ? 179 SER A O   1 
ATOM   1165 C CB  . SER A 1 162 ? 25.654 3.904   16.511  1.00 28.64  ? 179 SER A CB  1 
ATOM   1166 O OG  . SER A 1 162 ? 25.382 3.999   15.114  1.00 29.93  ? 179 SER A OG  1 
ATOM   1167 N N   . VAL A 1 163 ? 26.609 2.056   18.932  1.00 27.71  ? 180 VAL A N   1 
ATOM   1168 C CA  . VAL A 1 163 ? 27.064 1.902   20.311  1.00 24.87  ? 180 VAL A CA  1 
ATOM   1169 C C   . VAL A 1 163 ? 28.519 2.313   20.401  1.00 24.12  ? 180 VAL A C   1 
ATOM   1170 O O   . VAL A 1 163 ? 29.354 1.814   19.644  1.00 28.20  ? 180 VAL A O   1 
ATOM   1171 C CB  . VAL A 1 163 ? 26.887 0.449   20.805  1.00 27.46  ? 180 VAL A CB  1 
ATOM   1172 C CG1 . VAL A 1 163 ? 27.408 0.271   22.287  1.00 27.54  ? 180 VAL A CG1 1 
ATOM   1173 C CG2 . VAL A 1 163 ? 25.433 0.050   20.684  1.00 28.15  ? 180 VAL A CG2 1 
ATOM   1174 N N   . LEU A 1 164 ? 28.821 3.209   21.330  1.00 25.37  ? 181 LEU A N   1 
ATOM   1175 C CA  . LEU A 1 164 ? 30.181 3.579   21.690  1.00 24.12  ? 181 LEU A CA  1 
ATOM   1176 C C   . LEU A 1 164 ? 30.601 2.875   22.983  1.00 26.67  ? 181 LEU A C   1 
ATOM   1177 O O   . LEU A 1 164 ? 29.904 2.956   23.999  1.00 25.69  ? 181 LEU A O   1 
ATOM   1178 C CB  . LEU A 1 164 ? 30.275 5.087   21.916  1.00 27.00  ? 181 LEU A CB  1 
ATOM   1179 C CG  . LEU A 1 164 ? 29.481 5.997   20.969  1.00 29.61  ? 181 LEU A CG  1 
ATOM   1180 C CD1 . LEU A 1 164 ? 29.716 7.455   21.321  1.00 27.25  ? 181 LEU A CD1 1 
ATOM   1181 C CD2 . LEU A 1 164 ? 29.824 5.765   19.509  1.00 29.29  ? 181 LEU A CD2 1 
ATOM   1182 N N   . GLY A 1 165 ? 31.774 2.254   22.985  1.00 24.52  ? 182 GLY A N   1 
ATOM   1183 C CA  . GLY A 1 165 ? 32.330 1.789   24.249  1.00 25.77  ? 182 GLY A CA  1 
ATOM   1184 C C   . GLY A 1 165 ? 32.793 2.975   25.085  1.00 27.12  ? 182 GLY A C   1 
ATOM   1185 O O   . GLY A 1 165 ? 33.376 3.929   24.564  1.00 23.72  ? 182 GLY A O   1 
ATOM   1186 N N   . VAL A 1 166 ? 32.476 2.949   26.402  1.00 23.46  ? 183 VAL A N   1 
ATOM   1187 C CA  . VAL A 1 166 ? 32.848 4.046   27.293  1.00 22.50  ? 183 VAL A CA  1 
ATOM   1188 C C   . VAL A 1 166 ? 33.379 3.540   28.626  1.00 26.83  ? 183 VAL A C   1 
ATOM   1189 O O   . VAL A 1 166 ? 33.114 2.412   29.039  1.00 29.85  ? 183 VAL A O   1 
ATOM   1190 C CB  . VAL A 1 166 ? 31.665 4.989   27.573  1.00 25.30  ? 183 VAL A CB  1 
ATOM   1191 C CG1 . VAL A 1 166 ? 31.298 5.755   26.318  1.00 28.76  ? 183 VAL A CG1 1 
ATOM   1192 C CG2 . VAL A 1 166 ? 30.474 4.194   28.131  1.00 26.48  ? 183 VAL A CG2 1 
ATOM   1193 N N   . GLN A 1 167 ? 34.110 4.414   29.319  1.00 27.87  ? 184 GLN A N   1 
ATOM   1194 C CA  . GLN A 1 167 ? 34.460 4.188   30.713  1.00 30.63  ? 184 GLN A CA  1 
ATOM   1195 C C   . GLN A 1 167 ? 34.650 5.532   31.394  1.00 29.02  ? 184 GLN A C   1 
ATOM   1196 O O   . GLN A 1 167 ? 34.893 6.553   30.736  1.00 23.78  ? 184 GLN A O   1 
ATOM   1197 C CB  . GLN A 1 167 ? 35.715 3.304   30.859  1.00 36.28  ? 184 GLN A CB  1 
ATOM   1198 C CG  . GLN A 1 167 ? 37.032 3.988   30.625  1.00 40.47  ? 184 GLN A CG  1 
ATOM   1199 C CD  . GLN A 1 167 ? 38.204 3.021   30.786  1.00 54.73  ? 184 GLN A CD  1 
ATOM   1200 O OE1 . GLN A 1 167 ? 38.043 1.790   30.673  1.00 63.22  ? 184 GLN A OE1 1 
ATOM   1201 N NE2 . GLN A 1 167 ? 39.377 3.562   31.102  1.00 53.38  ? 184 GLN A NE2 1 
ATOM   1202 N N   . GLU A 1 168 ? 34.482 5.521   32.726  1.00 27.37  ? 185 GLU A N   1 
ATOM   1203 C CA  . GLU A 1 168 ? 34.762 6.686   33.550  1.00 29.94  ? 185 GLU A CA  1 
ATOM   1204 C C   . GLU A 1 168 ? 36.265 6.951   33.574  1.00 28.08  ? 185 GLU A C   1 
ATOM   1205 O O   . GLU A 1 168 ? 37.078 6.025   33.620  1.00 28.72  ? 185 GLU A O   1 
ATOM   1206 C CB  . GLU A 1 168 ? 34.246 6.487   34.994  1.00 29.18  ? 185 GLU A CB  1 
ATOM   1207 C CG  . GLU A 1 168 ? 32.718 6.328   35.068  1.00 31.07  ? 185 GLU A CG  1 
ATOM   1208 C CD  . GLU A 1 168 ? 31.938 7.615   34.794  1.00 33.53  ? 185 GLU A CD  1 
ATOM   1209 O OE1 . GLU A 1 168 ? 32.442 8.721   35.096  1.00 34.81  ? 185 GLU A OE1 1 
ATOM   1210 O OE2 . GLU A 1 168 ? 30.789 7.521   34.295  1.00 34.33  ? 185 GLU A OE2 1 
ATOM   1211 N N   . VAL A 1 169 ? 36.629 8.221   33.528  1.00 25.39  ? 186 VAL A N   1 
ATOM   1212 C CA  . VAL A 1 169 ? 38.022 8.633   33.677  1.00 28.31  ? 186 VAL A CA  1 
ATOM   1213 C C   . VAL A 1 169 ? 38.094 9.712   34.751  1.00 32.12  ? 186 VAL A C   1 
ATOM   1214 O O   . VAL A 1 169 ? 37.088 10.344  35.101  1.00 32.95  ? 186 VAL A O   1 
ATOM   1215 C CB  . VAL A 1 169 ? 38.602 9.147   32.340  1.00 33.60  ? 186 VAL A CB  1 
ATOM   1216 C CG1 . VAL A 1 169 ? 38.497 8.041   31.296  1.00 31.54  ? 186 VAL A CG1 1 
ATOM   1217 C CG2 . VAL A 1 169 ? 37.866 10.397  31.891  1.00 32.09  ? 186 VAL A CG2 1 
ATOM   1218 N N   . PRO A 1 170 ? 39.273 9.941   35.302  1.00 31.51  ? 187 PRO A N   1 
ATOM   1219 C CA  . PRO A 1 170 ? 39.432 11.042  36.263  1.00 34.64  ? 187 PRO A CA  1 
ATOM   1220 C C   . PRO A 1 170 ? 39.087 12.363  35.608  1.00 38.74  ? 187 PRO A C   1 
ATOM   1221 O O   . PRO A 1 170 ? 39.469 12.614  34.466  1.00 39.47  ? 187 PRO A O   1 
ATOM   1222 C CB  . PRO A 1 170 ? 40.916 10.978  36.643  1.00 33.22  ? 187 PRO A CB  1 
ATOM   1223 C CG  . PRO A 1 170 ? 41.315 9.579   36.392  1.00 38.74  ? 187 PRO A CG  1 
ATOM   1224 C CD  . PRO A 1 170 ? 40.481 9.120   35.182  1.00 33.82  ? 187 PRO A CD  1 
ATOM   1225 N N   . ARG A 1 171 ? 38.382 13.228  36.346  1.00 37.20  ? 188 ARG A N   1 
ATOM   1226 C CA  . ARG A 1 171 ? 37.969 14.496  35.742  1.00 42.88  ? 188 ARG A CA  1 
ATOM   1227 C C   . ARG A 1 171 ? 39.165 15.266  35.212  1.00 50.59  ? 188 ARG A C   1 
ATOM   1228 O O   . ARG A 1 171 ? 39.055 15.967  34.203  1.00 45.12  ? 188 ARG A O   1 
ATOM   1229 C CB  . ARG A 1 171 ? 37.208 15.364  36.729  1.00 43.37  ? 188 ARG A CB  1 
ATOM   1230 C CG  . ARG A 1 171 ? 36.761 16.720  36.151  1.00 42.17  ? 188 ARG A CG  1 
ATOM   1231 C CD  . ARG A 1 171 ? 35.685 17.394  37.008  1.00 42.28  ? 188 ARG A CD  1 
ATOM   1232 N NE  . ARG A 1 171 ? 34.377 16.764  36.845  1.00 45.30  ? 188 ARG A NE  1 
ATOM   1233 C CZ  . ARG A 1 171 ? 33.481 17.102  35.920  1.00 51.68  ? 188 ARG A CZ  1 
ATOM   1234 N NH1 . ARG A 1 171 ? 33.706 18.087  35.054  1.00 41.99  ? 188 ARG A NH1 1 
ATOM   1235 N NH2 . ARG A 1 171 ? 32.331 16.432  35.852  1.00 49.62  ? 188 ARG A NH2 1 
ATOM   1236 N N   . GLU A 1 172 ? 40.316 15.116  35.862  1.00 51.94  ? 189 GLU A N   1 
ATOM   1237 C CA  . GLU A 1 172 ? 41.525 15.806  35.445  1.00 60.62  ? 189 GLU A CA  1 
ATOM   1238 C C   . GLU A 1 172 ? 41.995 15.363  34.071  1.00 51.40  ? 189 GLU A C   1 
ATOM   1239 O O   . GLU A 1 172 ? 42.775 16.078  33.435  1.00 62.68  ? 189 GLU A O   1 
ATOM   1240 C CB  . GLU A 1 172 ? 42.628 15.579  36.483  1.00 72.53  ? 189 GLU A CB  1 
ATOM   1241 C CG  . GLU A 1 172 ? 42.268 16.069  37.904  1.00 84.22  ? 189 GLU A CG  1 
ATOM   1242 C CD  . GLU A 1 172 ? 41.324 15.121  38.679  1.00 76.83  ? 189 GLU A CD  1 
ATOM   1243 O OE1 . GLU A 1 172 ? 41.462 13.880  38.544  1.00 61.53  ? 189 GLU A OE1 1 
ATOM   1244 O OE2 . GLU A 1 172 ? 40.442 15.625  39.418  1.00 69.61  ? 189 GLU A OE2 1 
ATOM   1245 N N   . ASP A 1 173 ? 41.543 14.205  33.599  1.00 49.34  ? 190 ASP A N   1 
ATOM   1246 C CA  . ASP A 1 173 ? 41.987 13.648  32.334  1.00 46.21  ? 190 ASP A CA  1 
ATOM   1247 C C   . ASP A 1 173 ? 41.039 13.925  31.168  1.00 44.36  ? 190 ASP A C   1 
ATOM   1248 O O   . ASP A 1 173 ? 41.285 13.419  30.066  1.00 46.67  ? 190 ASP A O   1 
ATOM   1249 C CB  . ASP A 1 173 ? 42.145 12.123  32.423  1.00 47.07  ? 190 ASP A CB  1 
ATOM   1250 C CG  . ASP A 1 173 ? 43.369 11.686  33.212  1.00 60.61  ? 190 ASP A CG  1 
ATOM   1251 O OD1 . ASP A 1 173 ? 44.026 12.542  33.854  1.00 58.81  ? 190 ASP A OD1 1 
ATOM   1252 O OD2 . ASP A 1 173 ? 43.678 10.471  33.137  1.00 58.10  ? 190 ASP A OD2 1 
ATOM   1253 N N   . THR A 1 174 ? 39.939 14.657  31.376  1.00 40.32  ? 191 THR A N   1 
ATOM   1254 C CA  . THR A 1 174 ? 38.931 14.726  30.323  1.00 40.19  ? 191 THR A CA  1 
ATOM   1255 C C   . THR A 1 174 ? 39.444 15.453  29.083  1.00 37.54  ? 191 THR A C   1 
ATOM   1256 O O   . THR A 1 174 ? 38.905 15.260  28.002  1.00 37.29  ? 191 THR A O   1 
ATOM   1257 C CB  . THR A 1 174 ? 37.656 15.412  30.811  1.00 37.08  ? 191 THR A CB  1 
ATOM   1258 O OG1 . THR A 1 174 ? 37.956 16.728  31.297  1.00 39.80  ? 191 THR A OG1 1 
ATOM   1259 C CG2 . THR A 1 174 ? 36.965 14.559  31.881  1.00 35.27  ? 191 THR A CG2 1 
ATOM   1260 N N   . ARG A 1 175 ? 40.488 16.258  29.230  1.00 38.12  ? 192 ARG A N   1 
ATOM   1261 C CA  . ARG A 1 175 ? 41.107 16.961  28.129  1.00 43.62  ? 192 ARG A CA  1 
ATOM   1262 C C   . ARG A 1 175 ? 41.736 16.004  27.126  1.00 42.58  ? 192 ARG A C   1 
ATOM   1263 O O   . ARG A 1 175 ? 42.121 16.436  26.037  1.00 46.21  ? 192 ARG A O   1 
ATOM   1264 C CB  . ARG A 1 175 ? 42.180 17.868  28.722  1.00 55.10  ? 192 ARG A CB  1 
ATOM   1265 C CG  . ARG A 1 175 ? 42.658 19.012  27.874  1.00 68.74  ? 192 ARG A CG  1 
ATOM   1266 C CD  . ARG A 1 175 ? 43.782 19.750  28.626  1.00 90.18  ? 192 ARG A CD  1 
ATOM   1267 N NE  . ARG A 1 175 ? 43.364 20.451  29.840  1.00 92.79  ? 192 ARG A NE  1 
ATOM   1268 C CZ  . ARG A 1 175 ? 43.675 20.081  31.082  1.00 82.52  ? 192 ARG A CZ  1 
ATOM   1269 N NH1 . ARG A 1 175 ? 44.355 18.971  31.335  1.00 74.73  ? 192 ARG A NH1 1 
ATOM   1270 N NH2 . ARG A 1 175 ? 43.309 20.855  32.099  1.00 76.21  ? 192 ARG A NH2 1 
ATOM   1271 N N   . LYS A 1 176 ? 41.887 14.729  27.484  1.00 41.03  ? 193 LYS A N   1 
ATOM   1272 C CA  . LYS A 1 176 ? 42.438 13.711  26.601  1.00 39.96  ? 193 LYS A CA  1 
ATOM   1273 C C   . LYS A 1 176 ? 41.403 13.042  25.709  1.00 42.93  ? 193 LYS A C   1 
ATOM   1274 O O   . LYS A 1 176 ? 41.791 12.339  24.776  1.00 40.86  ? 193 LYS A O   1 
ATOM   1275 C CB  . LYS A 1 176 ? 43.127 12.602  27.408  1.00 50.88  ? 193 LYS A CB  1 
ATOM   1276 C CG  . LYS A 1 176 ? 44.421 12.957  28.097  1.00 48.48  ? 193 LYS A CG  1 
ATOM   1277 C CD  . LYS A 1 176 ? 44.950 11.708  28.850  1.00 63.13  ? 193 LYS A CD  1 
ATOM   1278 C CE  . LYS A 1 176 ? 46.099 12.017  29.811  1.00 73.36  ? 193 LYS A CE  1 
ATOM   1279 N NZ  . LYS A 1 176 ? 46.502 10.819  30.621  1.00 77.98  ? 193 LYS A NZ  1 
ATOM   1280 N N   . TYR A 1 177 ? 40.105 13.207  25.975  1.00 41.08  ? 194 TYR A N   1 
ATOM   1281 C CA  . TYR A 1 177 ? 39.105 12.276  25.467  1.00 32.79  ? 194 TYR A CA  1 
ATOM   1282 C C   . TYR A 1 177 ? 37.901 12.967  24.860  1.00 31.87  ? 194 TYR A C   1 
ATOM   1283 O O   . TYR A 1 177 ? 37.618 14.127  25.136  1.00 36.71  ? 194 TYR A O   1 
ATOM   1284 C CB  . TYR A 1 177 ? 38.590 11.336  26.589  1.00 45.84  ? 194 TYR A CB  1 
ATOM   1285 C CG  . TYR A 1 177 ? 39.655 10.444  27.158  1.00 48.89  ? 194 TYR A CG  1 
ATOM   1286 C CD1 . TYR A 1 177 ? 40.192 9.431   26.380  1.00 52.70  ? 194 TYR A CD1 1 
ATOM   1287 C CD2 . TYR A 1 177 ? 40.105 10.586  28.467  1.00 50.59  ? 194 TYR A CD2 1 
ATOM   1288 C CE1 . TYR A 1 177 ? 41.168 8.607   26.869  1.00 57.94  ? 194 TYR A CE1 1 
ATOM   1289 C CE2 . TYR A 1 177 ? 41.086 9.748   28.971  1.00 55.55  ? 194 TYR A CE2 1 
ATOM   1290 C CZ  . TYR A 1 177 ? 41.604 8.765   28.163  1.00 55.76  ? 194 TYR A CZ  1 
ATOM   1291 O OH  . TYR A 1 177 ? 42.584 7.935   28.648  1.00 74.82  ? 194 TYR A OH  1 
ATOM   1292 N N   . GLY A 1 178 ? 37.164 12.212  24.050  1.00 30.15  ? 195 GLY A N   1 
ATOM   1293 C CA  . GLY A 1 178 ? 35.791 12.570  23.754  1.00 35.33  ? 195 GLY A CA  1 
ATOM   1294 C C   . GLY A 1 178 ? 34.890 12.143  24.907  1.00 28.86  ? 195 GLY A C   1 
ATOM   1295 O O   . GLY A 1 178 ? 34.989 11.014  25.398  1.00 26.16  ? 195 GLY A O   1 
ATOM   1296 N N   . ILE A 1 179 ? 33.995 13.036  25.316  1.00 30.88  ? 196 ILE A N   1 
ATOM   1297 C CA  . ILE A 1 179 ? 33.196 12.882  26.527  1.00 28.51  ? 196 ILE A CA  1 
ATOM   1298 C C   . ILE A 1 179 ? 31.736 12.842  26.130  1.00 27.53  ? 196 ILE A C   1 
ATOM   1299 O O   . ILE A 1 179 ? 31.273 13.714  25.388  1.00 26.74  ? 196 ILE A O   1 
ATOM   1300 C CB  . ILE A 1 179 ? 33.463 14.039  27.506  1.00 30.07  ? 196 ILE A CB  1 
ATOM   1301 C CG1 . ILE A 1 179 ? 34.925 14.023  27.953  1.00 32.67  ? 196 ILE A CG1 1 
ATOM   1302 C CG2 . ILE A 1 179 ? 32.542 13.949  28.666  1.00 29.02  ? 196 ILE A CG2 1 
ATOM   1303 C CD1 . ILE A 1 179 ? 35.313 12.748  28.805  1.00 33.97  ? 196 ILE A CD1 1 
ATOM   1304 N N   . VAL A 1 180 ? 31.013 11.836  26.614  1.00 24.73  ? 197 VAL A N   1 
ATOM   1305 C CA  A VAL A 1 180 ? 29.605 11.683  26.276  0.44 25.24  ? 197 VAL A CA  1 
ATOM   1306 C CA  B VAL A 1 180 ? 29.606 11.648  26.291  0.56 25.21  ? 197 VAL A CA  1 
ATOM   1307 C C   . VAL A 1 180 ? 28.732 12.209  27.406  1.00 26.73  ? 197 VAL A C   1 
ATOM   1308 O O   . VAL A 1 180 ? 28.980 11.957  28.593  1.00 26.71  ? 197 VAL A O   1 
ATOM   1309 C CB  A VAL A 1 180 ? 29.233 10.226  25.926  0.44 26.56  ? 197 VAL A CB  1 
ATOM   1310 C CB  B VAL A 1 180 ? 29.290 10.163  26.042  0.56 26.44  ? 197 VAL A CB  1 
ATOM   1311 C CG1 A VAL A 1 180 ? 29.877 9.833   24.591  0.44 32.36  ? 197 VAL A CG1 1 
ATOM   1312 C CG1 B VAL A 1 180 ? 27.805 9.964   25.895  0.56 30.26  ? 197 VAL A CG1 1 
ATOM   1313 C CG2 A VAL A 1 180 ? 29.641 9.291   26.979  0.44 30.46  ? 197 VAL A CG2 1 
ATOM   1314 C CG2 B VAL A 1 180 ? 30.013 9.702   24.780  0.56 32.62  ? 197 VAL A CG2 1 
ATOM   1315 N N   . ALA A 1 181 ? 27.705 12.950  27.019  1.00 29.97  ? 198 ALA A N   1 
ATOM   1316 C CA  . ALA A 1 181 ? 26.609 13.348  27.884  1.00 30.49  ? 198 ALA A CA  1 
ATOM   1317 C C   . ALA A 1 181 ? 25.462 12.422  27.512  1.00 30.86  ? 198 ALA A C   1 
ATOM   1318 O O   . ALA A 1 181 ? 25.074 12.356  26.343  1.00 26.64  ? 198 ALA A O   1 
ATOM   1319 C CB  . ALA A 1 181 ? 26.219 14.809  27.663  1.00 31.02  ? 198 ALA A CB  1 
ATOM   1320 N N   . SER A 1 182 ? 24.956 11.687  28.489  1.00 27.83  ? 199 SER A N   1 
ATOM   1321 C CA  . SER A 1 182 ? 24.044 10.593  28.223  1.00 30.06  ? 199 SER A CA  1 
ATOM   1322 C C   . SER A 1 182 ? 23.124 10.417  29.417  1.00 30.95  ? 199 SER A C   1 
ATOM   1323 O O   . SER A 1 182 ? 23.395 10.914  30.512  1.00 31.10  ? 199 SER A O   1 
ATOM   1324 C CB  . SER A 1 182 ? 24.799 9.278   27.962  1.00 29.71  ? 199 SER A CB  1 
ATOM   1325 O OG  . SER A 1 182 ? 25.718 8.943   29.007  1.00 28.81  ? 199 SER A OG  1 
ATOM   1326 N N   . GLN A 1 183 ? 22.037 9.696   29.187  1.00 31.80  ? 200 GLN A N   1 
ATOM   1327 C CA  . GLN A 1 183 ? 21.124 9.320   30.256  1.00 38.39  ? 200 GLN A CA  1 
ATOM   1328 C C   . GLN A 1 183 ? 21.038 7.803   30.322  1.00 33.70  ? 200 GLN A C   1 
ATOM   1329 O O   . GLN A 1 183 ? 20.990 7.137   29.280  1.00 32.87  ? 200 GLN A O   1 
ATOM   1330 C CB  . GLN A 1 183 ? 19.706 9.886   30.069  1.00 36.54  ? 200 GLN A CB  1 
ATOM   1331 C CG  . GLN A 1 183 ? 19.631 11.405  30.112  1.00 40.40  ? 200 GLN A CG  1 
ATOM   1332 C CD  . GLN A 1 183 ? 20.166 12.009  31.409  1.00 42.73  ? 200 GLN A CD  1 
ATOM   1333 O OE1 . GLN A 1 183 ? 20.122 11.388  32.468  1.00 45.75  ? 200 GLN A OE1 1 
ATOM   1334 N NE2 . GLN A 1 183 ? 20.698 13.225  31.316  1.00 44.90  ? 200 GLN A NE2 1 
ATOM   1335 N N   . PRO A 1 184 ? 21.036 7.239   31.524  1.00 29.54  ? 201 PRO A N   1 
ATOM   1336 C CA  . PRO A 1 184 ? 21.024 5.781   31.676  1.00 34.82  ? 201 PRO A CA  1 
ATOM   1337 C C   . PRO A 1 184 ? 19.768 5.139   31.111  1.00 34.48  ? 201 PRO A C   1 
ATOM   1338 O O   . PRO A 1 184 ? 18.658 5.633   31.311  1.00 33.31  ? 201 PRO A O   1 
ATOM   1339 C CB  . PRO A 1 184 ? 21.080 5.598   33.202  1.00 41.44  ? 201 PRO A CB  1 
ATOM   1340 C CG  . PRO A 1 184 ? 21.678 6.850   33.706  1.00 45.81  ? 201 PRO A CG  1 
ATOM   1341 C CD  . PRO A 1 184 ? 21.119 7.914   32.835  1.00 37.22  ? 201 PRO A CD  1 
ATOM   1342 N N   . VAL A 1 185 ? 19.946 3.977   30.486  1.00 32.37  ? 202 VAL A N   1 
ATOM   1343 C CA  . VAL A 1 185 ? 18.832 3.099   30.157  1.00 31.07  ? 202 VAL A CA  1 
ATOM   1344 C C   . VAL A 1 185 ? 18.875 1.815   30.981  1.00 39.80  ? 202 VAL A C   1 
ATOM   1345 O O   . VAL A 1 185 ? 17.824 1.214   31.234  1.00 37.99  ? 202 VAL A O   1 
ATOM   1346 C CB  . VAL A 1 185 ? 18.808 2.771   28.644  1.00 39.80  ? 202 VAL A CB  1 
ATOM   1347 C CG1 . VAL A 1 185 ? 17.625 1.920   28.339  1.00 43.83  ? 202 VAL A CG1 1 
ATOM   1348 C CG2 . VAL A 1 185 ? 18.749 4.038   27.829  1.00 41.29  ? 202 VAL A CG2 1 
ATOM   1349 N N   . ASP A 1 186 ? 20.054 1.399   31.424  1.00 36.66  ? 203 ASP A N   1 
ATOM   1350 C CA  . ASP A 1 186 ? 20.238 0.353   32.418  1.00 35.30  ? 203 ASP A CA  1 
ATOM   1351 C C   . ASP A 1 186 ? 21.607 0.611   33.053  1.00 33.64  ? 203 ASP A C   1 
ATOM   1352 O O   . ASP A 1 186 ? 22.185 1.692   32.886  1.00 32.00  ? 203 ASP A O   1 
ATOM   1353 C CB  . ASP A 1 186 ? 20.021 -1.035  31.787  1.00 34.99  ? 203 ASP A CB  1 
ATOM   1354 C CG  . ASP A 1 186 ? 21.072 -1.415  30.750  1.00 35.70  ? 203 ASP A CG  1 
ATOM   1355 O OD1 . ASP A 1 186 ? 22.244 -1.007  30.877  1.00 33.30  ? 203 ASP A OD1 1 
ATOM   1356 O OD2 . ASP A 1 186 ? 20.707 -2.141  29.792  1.00 39.30  ? 203 ASP A OD2 1 
ATOM   1357 N N   . ALA A 1 187 ? 22.102 -0.348  33.840  1.00 32.65  ? 204 ALA A N   1 
ATOM   1358 C CA  . ALA A 1 187 ? 23.298 -0.098  34.647  1.00 34.33  ? 204 ALA A CA  1 
ATOM   1359 C C   . ALA A 1 187 ? 24.545 0.106   33.796  1.00 29.60  ? 204 ALA A C   1 
ATOM   1360 O O   . ALA A 1 187 ? 25.529 0.680   34.290  1.00 31.02  ? 204 ALA A O   1 
ATOM   1361 C CB  . ALA A 1 187 ? 23.541 -1.232  35.663  1.00 30.79  ? 204 ALA A CB  1 
ATOM   1362 N N   . ARG A 1 188 ? 24.553 -0.391  32.564  1.00 31.08  ? 205 ARG A N   1 
ATOM   1363 C CA  . ARG A 1 188 ? 25.710 -0.263  31.692  1.00 32.34  ? 205 ARG A CA  1 
ATOM   1364 C C   . ARG A 1 188 ? 25.454 0.529   30.426  1.00 28.75  ? 205 ARG A C   1 
ATOM   1365 O O   . ARG A 1 188 ? 26.400 1.115   29.891  1.00 28.04  ? 205 ARG A O   1 
ATOM   1366 C CB  . ARG A 1 188 ? 26.230 -1.659  31.297  1.00 33.74  ? 205 ARG A CB  1 
ATOM   1367 C CG  . ARG A 1 188 ? 26.858 -2.429  32.455  1.00 34.94  ? 205 ARG A CG  1 
ATOM   1368 C CD  . ARG A 1 188 ? 27.502 -3.772  32.051  1.00 36.90  ? 205 ARG A CD  1 
ATOM   1369 N NE  . ARG A 1 188 ? 28.088 -4.456  33.202  1.00 37.99  ? 205 ARG A NE  1 
ATOM   1370 C CZ  . ARG A 1 188 ? 29.324 -4.272  33.658  1.00 43.50  ? 205 ARG A CZ  1 
ATOM   1371 N NH1 . ARG A 1 188 ? 30.181 -3.469  33.041  1.00 36.47  ? 205 ARG A NH1 1 
ATOM   1372 N NH2 . ARG A 1 188 ? 29.702 -4.891  34.783  1.00 42.86  ? 205 ARG A NH2 1 
ATOM   1373 N N   . THR A 1 189 ? 24.210 0.660   29.986  1.00 28.75  ? 206 THR A N   1 
ATOM   1374 C CA  . THR A 1 189 ? 23.915 1.263   28.697  1.00 32.02  ? 206 THR A CA  1 
ATOM   1375 C C   . THR A 1 189 ? 23.224 2.605   28.893  1.00 32.52  ? 206 THR A C   1 
ATOM   1376 O O   . THR A 1 189 ? 22.397 2.765   29.792  1.00 31.98  ? 206 THR A O   1 
ATOM   1377 C CB  . THR A 1 189 ? 23.054 0.329   27.850  1.00 30.49  ? 206 THR A CB  1 
ATOM   1378 O OG1 . THR A 1 189 ? 23.774 -0.886  27.674  1.00 27.76  ? 206 THR A OG1 1 
ATOM   1379 C CG2 . THR A 1 189 ? 22.788 0.932   26.498  1.00 34.65  ? 206 THR A CG2 1 
ATOM   1380 N N   . GLU A 1 190 ? 23.594 3.567   28.045  1.00 32.59  ? 207 GLU A N   1 
ATOM   1381 C CA  . GLU A 1 190 ? 23.120 4.939   28.122  1.00 32.83  ? 207 GLU A CA  1 
ATOM   1382 C C   . GLU A 1 190 ? 22.704 5.418   26.744  1.00 30.22  ? 207 GLU A C   1 
ATOM   1383 O O   . GLU A 1 190 ? 23.233 4.949   25.751  1.00 28.97  ? 207 GLU A O   1 
ATOM   1384 C CB  . GLU A 1 190 ? 24.231 5.825   28.709  1.00 30.24  ? 207 GLU A CB  1 
ATOM   1385 C CG  . GLU A 1 190 ? 24.716 5.255   30.029  1.00 39.31  ? 207 GLU A CG  1 
ATOM   1386 C CD  . GLU A 1 190 ? 24.659 6.256   31.166  1.00 42.54  ? 207 GLU A CD  1 
ATOM   1387 O OE1 . GLU A 1 190 ? 24.321 7.465   30.936  1.00 37.48  ? 207 GLU A OE1 1 
ATOM   1388 O OE2 . GLU A 1 190 ? 24.895 5.797   32.297  1.00 41.30  ? 207 GLU A OE2 1 
ATOM   1389 N N   . ARG A 1 191 ? 21.749 6.351   26.698  1.00 30.36  ? 208 ARG A N   1 
ATOM   1390 C CA  . ARG A 1 191 ? 21.353 7.010   25.463  1.00 32.98  ? 208 ARG A CA  1 
ATOM   1391 C C   . ARG A 1 191 ? 22.142 8.304   25.336  1.00 32.39  ? 208 ARG A C   1 
ATOM   1392 O O   . ARG A 1 191 ? 22.067 9.169   26.211  1.00 29.83  ? 208 ARG A O   1 
ATOM   1393 C CB  . ARG A 1 191 ? 19.852 7.298   25.435  1.00 40.38  ? 208 ARG A CB  1 
ATOM   1394 C CG  . ARG A 1 191 ? 19.392 7.854   24.096  1.00 43.65  ? 208 ARG A CG  1 
ATOM   1395 C CD  . ARG A 1 191 ? 17.896 8.123   24.073  1.00 59.64  ? 208 ARG A CD  1 
ATOM   1396 N NE  . ARG A 1 191 ? 17.162 7.039   24.719  1.00 60.98  ? 208 ARG A NE  1 
ATOM   1397 C CZ  . ARG A 1 191 ? 16.802 5.909   24.123  1.00 61.85  ? 208 ARG A CZ  1 
ATOM   1398 N NH1 . ARG A 1 191 ? 16.931 5.739   22.813  1.00 57.29  ? 208 ARG A NH1 1 
ATOM   1399 N NH2 . ARG A 1 191 ? 16.305 4.923   24.859  1.00 49.20  ? 208 ARG A NH2 1 
ATOM   1400 N N   . VAL A 1 192 ? 22.896 8.440   24.253  1.00 28.47  ? 209 VAL A N   1 
ATOM   1401 C CA  . VAL A 1 192 ? 23.757 9.607   24.078  1.00 28.94  ? 209 VAL A CA  1 
ATOM   1402 C C   . VAL A 1 192 ? 22.933 10.771  23.556  1.00 27.56  ? 209 VAL A C   1 
ATOM   1403 O O   . VAL A 1 192 ? 22.139 10.602  22.635  1.00 30.37  ? 209 VAL A O   1 
ATOM   1404 C CB  . VAL A 1 192 ? 24.914 9.293   23.123  1.00 31.47  ? 209 VAL A CB  1 
ATOM   1405 C CG1 . VAL A 1 192 ? 25.758 10.541  22.906  1.00 29.39  ? 209 VAL A CG1 1 
ATOM   1406 C CG2 . VAL A 1 192 ? 25.718 8.149   23.729  1.00 29.90  ? 209 VAL A CG2 1 
ATOM   1407 N N   . THR A 1 193 ? 23.124 11.948  24.153  1.00 29.94  ? 210 THR A N   1 
ATOM   1408 C CA  . THR A 1 193 ? 22.469 13.174  23.723  1.00 30.69  ? 210 THR A CA  1 
ATOM   1409 C C   . THR A 1 193 ? 23.447 14.220  23.230  1.00 29.42  ? 210 THR A C   1 
ATOM   1410 O O   . THR A 1 193 ? 23.085 15.030  22.389  1.00 28.17  ? 210 THR A O   1 
ATOM   1411 C CB  . THR A 1 193 ? 21.639 13.786  24.866  1.00 30.63  ? 210 THR A CB  1 
ATOM   1412 O OG1 . THR A 1 193 ? 22.503 14.186  25.939  1.00 29.94  ? 210 THR A OG1 1 
ATOM   1413 C CG2 . THR A 1 193 ? 20.617 12.776  25.414  1.00 29.31  ? 210 THR A CG2 1 
ATOM   1414 N N   . HIS A 1 194 ? 24.677 14.214  23.721  1.00 27.45  ? 211 HIS A N   1 
ATOM   1415 C CA  . HIS A 1 194 ? 25.680 15.197  23.328  1.00 25.18  ? 211 HIS A CA  1 
ATOM   1416 C C   . HIS A 1 194 ? 27.037 14.532  23.422  1.00 27.49  ? 211 HIS A C   1 
ATOM   1417 O O   . HIS A 1 194 ? 27.241 13.601  24.199  1.00 25.55  ? 211 HIS A O   1 
ATOM   1418 C CB  . HIS A 1 194 ? 25.693 16.458  24.240  1.00 29.31  ? 211 HIS A CB  1 
ATOM   1419 C CG  . HIS A 1 194 ? 24.362 17.144  24.375  1.00 34.15  ? 211 HIS A CG  1 
ATOM   1420 N ND1 . HIS A 1 194 ? 23.399 16.741  25.280  1.00 32.72  ? 211 HIS A ND1 1 
ATOM   1421 C CD2 . HIS A 1 194 ? 23.835 18.207  23.716  1.00 32.33  ? 211 HIS A CD2 1 
ATOM   1422 C CE1 . HIS A 1 194 ? 22.344 17.538  25.184  1.00 36.71  ? 211 HIS A CE1 1 
ATOM   1423 N NE2 . HIS A 1 194 ? 22.588 18.442  24.249  1.00 36.32  ? 211 HIS A NE2 1 
ATOM   1424 N N   . ILE A 1 195 ? 27.986 15.040  22.655  1.00 26.66  ? 212 ILE A N   1 
ATOM   1425 C CA  . ILE A 1 195 ? 29.357 14.573  22.776  1.00 25.72  ? 212 ILE A CA  1 
ATOM   1426 C C   . ILE A 1 195 ? 30.248 15.791  22.623  1.00 29.50  ? 212 ILE A C   1 
ATOM   1427 O O   . ILE A 1 195 ? 29.898 16.733  21.910  1.00 29.92  ? 212 ILE A O   1 
ATOM   1428 C CB  . ILE A 1 195 ? 29.617 13.467  21.739  1.00 31.76  ? 212 ILE A CB  1 
ATOM   1429 C CG1 . ILE A 1 195 ? 30.985 12.847  21.894  1.00 31.77  ? 212 ILE A CG1 1 
ATOM   1430 C CG2 . ILE A 1 195 ? 29.493 14.040  20.359  1.00 37.11  ? 212 ILE A CG2 1 
ATOM   1431 C CD1 . ILE A 1 195 ? 31.036 11.484  21.181  1.00 37.45  ? 212 ILE A CD1 1 
ATOM   1432 N N   . VAL A 1 196 ? 31.337 15.828  23.379  1.00 26.22  ? 213 VAL A N   1 
ATOM   1433 C CA  . VAL A 1 196 ? 32.223 16.981  23.374  1.00 30.47  ? 213 VAL A CA  1 
ATOM   1434 C C   . VAL A 1 196 ? 33.653 16.478  23.352  1.00 34.69  ? 213 VAL A C   1 
ATOM   1435 O O   . VAL A 1 196 ? 34.026 15.562  24.098  1.00 30.46  ? 213 VAL A O   1 
ATOM   1436 C CB  . VAL A 1 196 ? 31.965 17.926  24.564  1.00 33.53  ? 213 VAL A CB  1 
ATOM   1437 C CG1 . VAL A 1 196 ? 32.263 17.246  25.886  1.00 34.12  ? 213 VAL A CG1 1 
ATOM   1438 C CG2 . VAL A 1 196 ? 32.774 19.185  24.440  1.00 38.45  ? 213 VAL A CG2 1 
ATOM   1439 N N   . GLU A 1 197 ? 34.460 17.088  22.501  1.00 32.40  ? 214 GLU A N   1 
ATOM   1440 C CA  . GLU A 1 197 ? 35.835 16.659  22.292  1.00 33.18  ? 214 GLU A CA  1 
ATOM   1441 C C   . GLU A 1 197 ? 36.761 17.462  23.194  1.00 34.90  ? 214 GLU A C   1 
ATOM   1442 O O   . GLU A 1 197 ? 36.801 18.688  23.113  1.00 34.50  ? 214 GLU A O   1 
ATOM   1443 C CB  . GLU A 1 197 ? 36.202 16.834  20.816  1.00 37.19  ? 214 GLU A CB  1 
ATOM   1444 C CG  . GLU A 1 197 ? 37.567 16.305  20.404  1.00 42.33  ? 214 GLU A CG  1 
ATOM   1445 C CD  . GLU A 1 197 ? 37.715 14.809  20.608  1.00 50.34  ? 214 GLU A CD  1 
ATOM   1446 O OE1 . GLU A 1 197 ? 36.702 14.074  20.610  1.00 51.45  ? 214 GLU A OE1 1 
ATOM   1447 O OE2 . GLU A 1 197 ? 38.867 14.354  20.738  1.00 66.29  ? 214 GLU A OE2 1 
ATOM   1448 N N   . LYS A 1 198 ? 37.481 16.770  24.071  1.00 36.40  ? 215 LYS A N   1 
ATOM   1449 C CA  . LYS A 1 198 ? 38.545 17.354  24.876  1.00 39.83  ? 215 LYS A CA  1 
ATOM   1450 C C   . LYS A 1 198 ? 38.134 18.602  25.671  1.00 39.23  ? 215 LYS A C   1 
ATOM   1451 O O   . LYS A 1 198 ? 38.801 19.627  25.613  1.00 39.42  ? 215 LYS A O   1 
ATOM   1452 C CB  . LYS A 1 198 ? 39.738 17.674  23.985  1.00 43.95  ? 215 LYS A CB  1 
ATOM   1453 C CG  . LYS A 1 198 ? 40.370 16.432  23.368  1.00 44.61  ? 215 LYS A CG  1 
ATOM   1454 C CD  . LYS A 1 198 ? 41.612 16.754  22.549  1.00 55.74  ? 215 LYS A CD  1 
ATOM   1455 C CE  . LYS A 1 198 ? 42.356 15.487  22.117  1.00 63.20  ? 215 LYS A CE  1 
ATOM   1456 N NZ  . LYS A 1 198 ? 41.617 14.706  21.099  1.00 78.69  ? 215 LYS A NZ  1 
ATOM   1457 N N   . PRO A 1 199 ? 37.084 18.505  26.477  1.00 33.85  ? 216 PRO A N   1 
ATOM   1458 C CA  . PRO A 1 199 ? 36.673 19.656  27.284  1.00 37.20  ? 216 PRO A CA  1 
ATOM   1459 C C   . PRO A 1 199 ? 37.691 19.965  28.365  1.00 43.65  ? 216 PRO A C   1 
ATOM   1460 O O   . PRO A 1 199 ? 38.489 19.117  28.788  1.00 42.29  ? 216 PRO A O   1 
ATOM   1461 C CB  . PRO A 1 199 ? 35.351 19.199  27.899  1.00 38.25  ? 216 PRO A CB  1 
ATOM   1462 C CG  . PRO A 1 199 ? 35.585 17.711  28.109  1.00 36.60  ? 216 PRO A CG  1 
ATOM   1463 C CD  . PRO A 1 199 ? 36.345 17.287  26.849  1.00 34.49  ? 216 PRO A CD  1 
ATOM   1464 N N   . ALA A 1 200 ? 37.657 21.211  28.803  1.00 39.17  ? 217 ALA A N   1 
ATOM   1465 C CA  . ALA A 1 200 ? 38.350 21.584  30.019  1.00 41.60  ? 217 ALA A CA  1 
ATOM   1466 C C   . ALA A 1 200 ? 37.803 20.773  31.197  1.00 45.98  ? 217 ALA A C   1 
ATOM   1467 O O   . ALA A 1 200 ? 36.587 20.569  31.307  1.00 38.26  ? 217 ALA A O   1 
ATOM   1468 C CB  . ALA A 1 200 ? 38.168 23.080  30.273  1.00 44.42  ? 217 ALA A CB  1 
ATOM   1469 N N   . PRO A 1 201 ? 38.665 20.286  32.094  1.00 45.66  ? 218 PRO A N   1 
ATOM   1470 C CA  . PRO A 1 201 ? 38.152 19.457  33.202  1.00 43.42  ? 218 PRO A CA  1 
ATOM   1471 C C   . PRO A 1 201 ? 37.078 20.139  34.031  1.00 43.73  ? 218 PRO A C   1 
ATOM   1472 O O   . PRO A 1 201 ? 36.096 19.495  34.421  1.00 43.39  ? 218 PRO A O   1 
ATOM   1473 C CB  . PRO A 1 201 ? 39.419 19.161  34.015  1.00 51.03  ? 218 PRO A CB  1 
ATOM   1474 C CG  . PRO A 1 201 ? 40.522 19.155  32.954  1.00 55.44  ? 218 PRO A CG  1 
ATOM   1475 C CD  . PRO A 1 201 ? 40.137 20.239  31.990  1.00 46.02  ? 218 PRO A CD  1 
ATOM   1476 N N   . GLU A 1 202 ? 37.228 21.436  34.292  1.00 41.82  ? 219 GLU A N   1 
ATOM   1477 C CA  . GLU A 1 202 ? 36.239 22.181  35.058  1.00 47.28  ? 219 GLU A CA  1 
ATOM   1478 C C   . GLU A 1 202 ? 34.922 22.340  34.305  1.00 44.37  ? 219 GLU A C   1 
ATOM   1479 O O   . GLU A 1 202 ? 33.903 22.665  34.916  1.00 44.86  ? 219 GLU A O   1 
ATOM   1480 C CB  . GLU A 1 202 ? 36.807 23.557  35.429  1.00 60.31  ? 219 GLU A CB  1 
ATOM   1481 C CG  . GLU A 1 202 ? 38.155 23.527  36.193  1.00 68.47  ? 219 GLU A CG  1 
ATOM   1482 C CD  . GLU A 1 202 ? 39.392 23.240  35.308  1.00 74.85  ? 219 GLU A CD  1 
ATOM   1483 O OE1 . GLU A 1 202 ? 39.326 23.424  34.068  1.00 57.10  ? 219 GLU A OE1 1 
ATOM   1484 O OE2 . GLU A 1 202 ? 40.431 22.796  35.861  1.00 78.41  ? 219 GLU A OE2 1 
ATOM   1485 N N   . GLN A 1 203 ? 34.921 22.137  32.990  1.00 44.01  ? 220 GLN A N   1 
ATOM   1486 C CA  . GLN A 1 203 ? 33.727 22.331  32.174  1.00 43.09  ? 220 GLN A CA  1 
ATOM   1487 C C   . GLN A 1 203 ? 33.258 21.041  31.514  1.00 40.42  ? 220 GLN A C   1 
ATOM   1488 O O   . GLN A 1 203 ? 32.318 21.071  30.709  1.00 36.30  ? 220 GLN A O   1 
ATOM   1489 C CB  . GLN A 1 203 ? 34.006 23.401  31.127  1.00 37.00  ? 220 GLN A CB  1 
ATOM   1490 C CG  . GLN A 1 203 ? 34.319 24.770  31.741  1.00 39.78  ? 220 GLN A CG  1 
ATOM   1491 C CD  . GLN A 1 203 ? 34.798 25.736  30.687  1.00 42.25  ? 220 GLN A CD  1 
ATOM   1492 O OE1 . GLN A 1 203 ? 35.287 25.318  29.629  1.00 45.45  ? 220 GLN A OE1 1 
ATOM   1493 N NE2 . GLN A 1 203 ? 34.664 27.031  30.958  1.00 42.81  ? 220 GLN A NE2 1 
ATOM   1494 N N   . ALA A 1 204 ? 33.863 19.904  31.844  1.00 39.63  ? 221 ALA A N   1 
ATOM   1495 C CA  . ALA A 1 204 ? 33.475 18.662  31.174  1.00 40.71  ? 221 ALA A CA  1 
ATOM   1496 C C   . ALA A 1 204 ? 32.065 18.288  31.616  1.00 36.08  ? 221 ALA A C   1 
ATOM   1497 O O   . ALA A 1 204 ? 31.759 18.370  32.808  1.00 34.70  ? 221 ALA A O   1 
ATOM   1498 C CB  . ALA A 1 204 ? 34.462 17.548  31.491  1.00 33.84  ? 221 ALA A CB  1 
ATOM   1499 N N   . PRO A 1 205 ? 31.157 17.958  30.694  1.00 35.49  ? 222 PRO A N   1 
ATOM   1500 C CA  . PRO A 1 205 ? 29.783 17.661  31.123  1.00 36.03  ? 222 PRO A CA  1 
ATOM   1501 C C   . PRO A 1 205 ? 29.678 16.452  32.031  1.00 35.34  ? 222 PRO A C   1 
ATOM   1502 O O   . PRO A 1 205 ? 28.745 16.359  32.841  1.00 33.55  ? 222 PRO A O   1 
ATOM   1503 C CB  . PRO A 1 205 ? 29.050 17.440  29.795  1.00 34.92  ? 222 PRO A CB  1 
ATOM   1504 C CG  . PRO A 1 205 ? 30.101 16.980  28.879  1.00 38.13  ? 222 PRO A CG  1 
ATOM   1505 C CD  . PRO A 1 205 ? 31.317 17.766  29.238  1.00 32.90  ? 222 PRO A CD  1 
ATOM   1506 N N   . THR A 1 206 ? 30.583 15.503  31.865  1.00 30.68  ? 223 THR A N   1 
ATOM   1507 C CA  . THR A 1 206 ? 30.638 14.273  32.621  1.00 31.47  ? 223 THR A CA  1 
ATOM   1508 C C   . THR A 1 206 ? 32.086 13.839  32.604  1.00 29.57  ? 223 THR A C   1 
ATOM   1509 O O   . THR A 1 206 ? 32.944 14.531  32.051  1.00 30.82  ? 223 THR A O   1 
ATOM   1510 C CB  . THR A 1 206 ? 29.774 13.161  32.025  1.00 33.20  ? 223 THR A CB  1 
ATOM   1511 O OG1 . THR A 1 206 ? 30.439 12.605  30.878  1.00 31.07  ? 223 THR A OG1 1 
ATOM   1512 C CG2 . THR A 1 206 ? 28.410 13.706  31.606  1.00 32.22  ? 223 THR A CG2 1 
ATOM   1513 N N   . THR A 1 207 ? 32.355 12.674  33.187  1.00 29.24  ? 224 THR A N   1 
ATOM   1514 C CA  . THR A 1 207 ? 33.673 12.057  33.076  1.00 28.28  ? 224 THR A CA  1 
ATOM   1515 C C   . THR A 1 207 ? 33.559 10.721  32.360  1.00 27.71  ? 224 THR A C   1 
ATOM   1516 O O   . THR A 1 207 ? 34.344 9.809   32.609  1.00 28.85  ? 224 THR A O   1 
ATOM   1517 C CB  . THR A 1 207 ? 34.341 11.890  34.447  1.00 32.81  ? 224 THR A CB  1 
ATOM   1518 O OG1 . THR A 1 207 ? 33.515 11.121  35.323  1.00 31.43  ? 224 THR A OG1 1 
ATOM   1519 C CG2 . THR A 1 207 ? 34.588 13.240  35.082  1.00 31.72  ? 224 THR A CG2 1 
ATOM   1520 N N   . LEU A 1 208 ? 32.562 10.584  31.480  1.00 27.51  ? 225 LEU A N   1 
ATOM   1521 C CA  . LEU A 1 208 ? 32.348 9.352   30.726  1.00 30.35  ? 225 LEU A CA  1 
ATOM   1522 C C   . LEU A 1 208 ? 33.006 9.517   29.355  1.00 27.41  ? 225 LEU A C   1 
ATOM   1523 O O   . LEU A 1 208 ? 32.533 10.288  28.523  1.00 27.67  ? 225 LEU A O   1 
ATOM   1524 C CB  . LEU A 1 208 ? 30.855 9.050   30.605  1.00 29.17  ? 225 LEU A CB  1 
ATOM   1525 C CG  . LEU A 1 208 ? 30.507 7.661   30.038  1.00 28.29  ? 225 LEU A CG  1 
ATOM   1526 C CD1 . LEU A 1 208 ? 31.059 6.565   30.878  1.00 31.70  ? 225 LEU A CD1 1 
ATOM   1527 C CD2 . LEU A 1 208 ? 29.020 7.470   29.886  1.00 35.11  ? 225 LEU A CD2 1 
ATOM   1528 N N   . ALA A 1 209 ? 34.083 8.777   29.126  1.00 25.75  ? 226 ALA A N   1 
ATOM   1529 C CA  . ALA A 1 209 ? 34.930 8.930   27.962  1.00 27.65  ? 226 ALA A CA  1 
ATOM   1530 C C   . ALA A 1 209 ? 34.700 7.792   26.975  1.00 26.08  ? 226 ALA A C   1 
ATOM   1531 O O   . ALA A 1 209 ? 34.538 6.632   27.370  1.00 26.54  ? 226 ALA A O   1 
ATOM   1532 C CB  . ALA A 1 209 ? 36.412 8.966   28.369  1.00 24.11  ? 226 ALA A CB  1 
ATOM   1533 N N   . VAL A 1 210 ? 34.732 8.149   25.690  1.00 30.86  ? 227 VAL A N   1 
ATOM   1534 C CA  . VAL A 1 210 ? 34.681 7.186   24.593  1.00 22.84  ? 227 VAL A CA  1 
ATOM   1535 C C   . VAL A 1 210 ? 36.007 6.446   24.529  1.00 26.32  ? 227 VAL A C   1 
ATOM   1536 O O   . VAL A 1 210 ? 37.070 7.062   24.606  1.00 29.23  ? 227 VAL A O   1 
ATOM   1537 C CB  . VAL A 1 210 ? 34.399 7.912   23.271  1.00 28.02  ? 227 VAL A CB  1 
ATOM   1538 C CG1 . VAL A 1 210 ? 34.381 6.906   22.080  1.00 29.43  ? 227 VAL A CG1 1 
ATOM   1539 C CG2 . VAL A 1 210 ? 33.095 8.654   23.345  1.00 27.36  ? 227 VAL A CG2 1 
ATOM   1540 N N   . VAL A 1 211 ? 35.964 5.126   24.413  1.00 23.47  ? 228 VAL A N   1 
ATOM   1541 C CA  . VAL A 1 211 ? 37.174 4.354   24.139  1.00 26.52  ? 228 VAL A CA  1 
ATOM   1542 C C   . VAL A 1 211 ? 37.095 3.907   22.680  1.00 25.68  ? 228 VAL A C   1 
ATOM   1543 O O   . VAL A 1 211 ? 36.057 4.020   22.030  1.00 30.87  ? 228 VAL A O   1 
ATOM   1544 C CB  . VAL A 1 211 ? 37.344 3.155   25.095  1.00 29.11  ? 228 VAL A CB  1 
ATOM   1545 C CG1 . VAL A 1 211 ? 37.038 3.602   26.575  1.00 35.70  ? 228 VAL A CG1 1 
ATOM   1546 C CG2 . VAL A 1 211 ? 36.496 2.013   24.681  1.00 30.08  ? 228 VAL A CG2 1 
ATOM   1547 N N   . GLY A 1 212 ? 38.209 3.399   22.171  1.00 27.20  ? 229 GLY A N   1 
ATOM   1548 C CA  . GLY A 1 212 ? 38.314 3.030   20.758  1.00 25.88  ? 229 GLY A CA  1 
ATOM   1549 C C   . GLY A 1 212 ? 37.647 1.727   20.343  1.00 25.80  ? 229 GLY A C   1 
ATOM   1550 O O   . GLY A 1 212 ? 38.291 0.838   19.757  1.00 23.52  ? 229 GLY A O   1 
ATOM   1551 N N   . ARG A 1 213 ? 36.345 1.630   20.598  1.00 22.69  ? 230 ARG A N   1 
ATOM   1552 C CA  . ARG A 1 213 ? 35.522 0.504   20.193  1.00 26.41  ? 230 ARG A CA  1 
ATOM   1553 C C   . ARG A 1 213 ? 34.181 1.089   19.816  1.00 25.68  ? 230 ARG A C   1 
ATOM   1554 O O   . ARG A 1 213 ? 33.521 1.721   20.649  1.00 26.32  ? 230 ARG A O   1 
ATOM   1555 C CB  . ARG A 1 213 ? 35.346 -0.522  21.307  1.00 20.49  ? 230 ARG A CB  1 
ATOM   1556 C CG  . ARG A 1 213 ? 36.639 -1.224  21.734  1.00 22.93  ? 230 ARG A CG  1 
ATOM   1557 C CD  . ARG A 1 213 ? 37.164 -2.111  20.664  1.00 23.53  ? 230 ARG A CD  1 
ATOM   1558 N NE  . ARG A 1 213 ? 38.276 -2.921  21.157  1.00 20.57  ? 230 ARG A NE  1 
ATOM   1559 C CZ  . ARG A 1 213 ? 39.532 -2.526  21.268  1.00 20.37  ? 230 ARG A CZ  1 
ATOM   1560 N NH1 . ARG A 1 213 ? 39.930 -1.322  20.880  1.00 25.37  ? 230 ARG A NH1 1 
ATOM   1561 N NH2 . ARG A 1 213 ? 40.421 -3.357  21.797  1.00 23.27  ? 230 ARG A NH2 1 
ATOM   1562 N N   . TYR A 1 214 ? 33.779 0.878   18.575  1.00 21.81  ? 231 TYR A N   1 
ATOM   1563 C CA  . TYR A 1 214 ? 32.535 1.422   18.073  1.00 25.03  ? 231 TYR A CA  1 
ATOM   1564 C C   . TYR A 1 214 ? 31.795 0.372   17.263  1.00 25.86  ? 231 TYR A C   1 
ATOM   1565 O O   . TYR A 1 214 ? 32.397 -0.471  16.596  1.00 28.44  ? 231 TYR A O   1 
ATOM   1566 C CB  . TYR A 1 214 ? 32.747 2.641   17.172  1.00 25.08  ? 231 TYR A CB  1 
ATOM   1567 C CG  . TYR A 1 214 ? 33.675 3.719   17.655  1.00 24.43  ? 231 TYR A CG  1 
ATOM   1568 C CD1 . TYR A 1 214 ? 35.024 3.527   17.668  1.00 23.79  ? 231 TYR A CD1 1 
ATOM   1569 C CD2 . TYR A 1 214 ? 33.191 4.961   18.038  1.00 25.78  ? 231 TYR A CD2 1 
ATOM   1570 C CE1 . TYR A 1 214 ? 35.870 4.512   18.072  1.00 25.51  ? 231 TYR A CE1 1 
ATOM   1571 C CE2 . TYR A 1 214 ? 34.045 5.962   18.448  1.00 24.86  ? 231 TYR A CE2 1 
ATOM   1572 C CZ  . TYR A 1 214 ? 35.387 5.730   18.451  1.00 23.94  ? 231 TYR A CZ  1 
ATOM   1573 O OH  . TYR A 1 214 ? 36.262 6.716   18.861  1.00 33.51  ? 231 TYR A OH  1 
ATOM   1574 N N   . VAL A 1 215 ? 30.479 0.466   17.310  1.00 26.27  ? 232 VAL A N   1 
ATOM   1575 C CA  . VAL A 1 215 ? 29.587 -0.184  16.376  1.00 28.45  ? 232 VAL A CA  1 
ATOM   1576 C C   . VAL A 1 215 ? 28.736 0.926   15.812  1.00 26.83  ? 232 VAL A C   1 
ATOM   1577 O O   . VAL A 1 215 ? 28.001 1.573   16.553  1.00 28.38  ? 232 VAL A O   1 
ATOM   1578 C CB  . VAL A 1 215 ? 28.725 -1.265  17.034  1.00 29.01  ? 232 VAL A CB  1 
ATOM   1579 C CG1 . VAL A 1 215 ? 27.788 -1.880  16.006  1.00 29.10  ? 232 VAL A CG1 1 
ATOM   1580 C CG2 . VAL A 1 215 ? 29.612 -2.333  17.693  1.00 32.13  ? 232 VAL A CG2 1 
ATOM   1581 N N   . LEU A 1 216 ? 28.842 1.161   14.514  1.00 26.79  ? 233 LEU A N   1 
ATOM   1582 C CA  . LEU A 1 216 ? 28.225 2.318   13.880  1.00 27.69  ? 233 LEU A CA  1 
ATOM   1583 C C   . LEU A 1 216 ? 27.337 1.873   12.734  1.00 28.54  ? 233 LEU A C   1 
ATOM   1584 O O   . LEU A 1 216 ? 27.700 0.978   11.972  1.00 30.97  ? 233 LEU A O   1 
ATOM   1585 C CB  . LEU A 1 216 ? 29.302 3.268   13.312  1.00 30.64  ? 233 LEU A CB  1 
ATOM   1586 C CG  . LEU A 1 216 ? 30.320 3.766   14.329  1.00 27.35  ? 233 LEU A CG  1 
ATOM   1587 C CD1 . LEU A 1 216 ? 31.467 4.463   13.616  1.00 31.05  ? 233 LEU A CD1 1 
ATOM   1588 C CD2 . LEU A 1 216 ? 29.588 4.712   15.286  1.00 30.21  ? 233 LEU A CD2 1 
ATOM   1589 N N   . GLU A 1 217 ? 26.182 2.515   12.616  1.00 31.19  ? 234 GLU A N   1 
ATOM   1590 C CA  . GLU A 1 217 ? 25.331 2.321   11.469  1.00 32.75  ? 234 GLU A CA  1 
ATOM   1591 C C   . GLU A 1 217 ? 25.956 3.024   10.267  1.00 32.90  ? 234 GLU A C   1 
ATOM   1592 O O   . GLU A 1 217 ? 26.655 4.035   10.401  1.00 30.09  ? 234 GLU A O   1 
ATOM   1593 C CB  . GLU A 1 217 ? 23.926 2.866   11.753  1.00 31.66  ? 234 GLU A CB  1 
ATOM   1594 C CG  . GLU A 1 217 ? 23.162 2.066   12.815  1.00 39.91  ? 234 GLU A CG  1 
ATOM   1595 C CD  . GLU A 1 217 ? 21.731 2.508   13.003  1.00 48.90  ? 234 GLU A CD  1 
ATOM   1596 O OE1 . GLU A 1 217 ? 21.487 3.714   13.240  1.00 45.02  ? 234 GLU A OE1 1 
ATOM   1597 O OE2 . GLU A 1 217 ? 20.853 1.624   12.938  1.00 55.64  ? 234 GLU A OE2 1 
ATOM   1598 N N   . ALA A 1 218 ? 25.707 2.473   9.081   1.00 33.16  ? 235 ALA A N   1 
ATOM   1599 C CA  . ALA A 1 218 ? 26.326 3.031   7.899   1.00 31.48  ? 235 ALA A CA  1 
ATOM   1600 C C   . ALA A 1 218 ? 25.881 4.462   7.636   1.00 37.59  ? 235 ALA A C   1 
ATOM   1601 O O   . ALA A 1 218 ? 26.541 5.167   6.862   1.00 37.83  ? 235 ALA A O   1 
ATOM   1602 C CB  . ALA A 1 218 ? 26.045 2.128   6.692   1.00 39.21  ? 235 ALA A CB  1 
ATOM   1603 N N   . ALA A 1 219 ? 24.796 4.915   8.253   1.00 35.10  ? 236 ALA A N   1 
ATOM   1604 C CA  . ALA A 1 219 ? 24.389 6.311   8.098   1.00 35.86  ? 236 ALA A CA  1 
ATOM   1605 C C   . ALA A 1 219 ? 25.477 7.288   8.547   1.00 39.52  ? 236 ALA A C   1 
ATOM   1606 O O   . ALA A 1 219 ? 25.427 8.464   8.176   1.00 36.13  ? 236 ALA A O   1 
ATOM   1607 C CB  . ALA A 1 219 ? 23.103 6.583   8.890   1.00 42.92  ? 236 ALA A CB  1 
ATOM   1608 N N   . ILE A 1 220 ? 26.471 6.826   9.313   1.00 33.40  ? 237 ILE A N   1 
ATOM   1609 C CA  . ILE A 1 220 ? 27.557 7.711   9.736   1.00 34.34  ? 237 ILE A CA  1 
ATOM   1610 C C   . ILE A 1 220 ? 28.344 8.262   8.541   1.00 35.56  ? 237 ILE A C   1 
ATOM   1611 O O   . ILE A 1 220 ? 28.901 9.369   8.622   1.00 29.95  ? 237 ILE A O   1 
ATOM   1612 C CB  . ILE A 1 220 ? 28.476 6.966   10.720  1.00 33.56  ? 237 ILE A CB  1 
ATOM   1613 C CG1 . ILE A 1 220 ? 29.628 7.844   11.235  1.00 40.93  ? 237 ILE A CG1 1 
ATOM   1614 C CG2 . ILE A 1 220 ? 29.125 5.782   10.050  1.00 32.94  ? 237 ILE A CG2 1 
ATOM   1615 C CD1 . ILE A 1 220 ? 29.318 8.738   12.384  1.00 34.17  ? 237 ILE A CD1 1 
ATOM   1616 N N   . PHE A 1 221 ? 28.435 7.502   7.439   1.00 37.38  ? 238 PHE A N   1 
ATOM   1617 C CA  . PHE A 1 221 ? 29.301 7.910   6.331   1.00 38.05  ? 238 PHE A CA  1 
ATOM   1618 C C   . PHE A 1 221 ? 28.841 9.238   5.755   1.00 39.21  ? 238 PHE A C   1 
ATOM   1619 O O   . PHE A 1 221 ? 29.651 10.138  5.506   1.00 41.47  ? 238 PHE A O   1 
ATOM   1620 C CB  . PHE A 1 221 ? 29.329 6.841   5.229   1.00 36.35  ? 238 PHE A CB  1 
ATOM   1621 C CG  . PHE A 1 221 ? 30.059 5.585   5.620   1.00 33.14  ? 238 PHE A CG  1 
ATOM   1622 C CD1 . PHE A 1 221 ? 31.308 5.642   6.186   1.00 33.49  ? 238 PHE A CD1 1 
ATOM   1623 C CD2 . PHE A 1 221 ? 29.482 4.353   5.441   1.00 30.59  ? 238 PHE A CD2 1 
ATOM   1624 C CE1 . PHE A 1 221 ? 31.987 4.487   6.575   1.00 32.85  ? 238 PHE A CE1 1 
ATOM   1625 C CE2 . PHE A 1 221 ? 30.154 3.194   5.811   1.00 38.47  ? 238 PHE A CE2 1 
ATOM   1626 C CZ  . PHE A 1 221 ? 31.412 3.264   6.389   1.00 32.24  ? 238 PHE A CZ  1 
ATOM   1627 N N   . ASP A 1 222 ? 27.532 9.395   5.574   1.00 38.98  ? 239 ASP A N   1 
ATOM   1628 C CA  . ASP A 1 222 ? 27.020 10.651  5.033   1.00 46.51  ? 239 ASP A CA  1 
ATOM   1629 C C   . ASP A 1 222 ? 27.369 11.842  5.918   1.00 46.73  ? 239 ASP A C   1 
ATOM   1630 O O   . ASP A 1 222 ? 27.604 12.942  5.400   1.00 42.31  ? 239 ASP A O   1 
ATOM   1631 C CB  . ASP A 1 222 ? 25.512 10.544  4.829   1.00 47.43  ? 239 ASP A CB  1 
ATOM   1632 C CG  . ASP A 1 222 ? 25.148 9.763   3.569   1.00 63.57  ? 239 ASP A CG  1 
ATOM   1633 O OD1 . ASP A 1 222 ? 25.961 9.750   2.597   1.00 52.43  ? 239 ASP A OD1 1 
ATOM   1634 O OD2 . ASP A 1 222 ? 24.052 9.155   3.564   1.00 72.95  ? 239 ASP A OD2 1 
ATOM   1635 N N   . HIS A 1 223 ? 27.409 11.653  7.247   1.00 39.72  ? 240 HIS A N   1 
ATOM   1636 C CA  . HIS A 1 223 ? 27.750 12.752  8.151   1.00 37.31  ? 240 HIS A CA  1 
ATOM   1637 C C   . HIS A 1 223 ? 29.239 13.077  8.157   1.00 41.59  ? 240 HIS A C   1 
ATOM   1638 O O   . HIS A 1 223 ? 29.610 14.225  8.402   1.00 52.07  ? 240 HIS A O   1 
ATOM   1639 C CB  . HIS A 1 223 ? 27.272 12.429  9.567   1.00 42.23  ? 240 HIS A CB  1 
ATOM   1640 C CG  . HIS A 1 223 ? 25.789 12.304  9.665   1.00 39.34  ? 240 HIS A CG  1 
ATOM   1641 N ND1 . HIS A 1 223 ? 24.951 13.391  9.555   1.00 40.78  ? 240 HIS A ND1 1 
ATOM   1642 C CD2 . HIS A 1 223 ? 24.991 11.220  9.816   1.00 42.63  ? 240 HIS A CD2 1 
ATOM   1643 C CE1 . HIS A 1 223 ? 23.698 12.985  9.662   1.00 47.95  ? 240 HIS A CE1 1 
ATOM   1644 N NE2 . HIS A 1 223 ? 23.693 11.673  9.819   1.00 47.61  ? 240 HIS A NE2 1 
ATOM   1645 N N   . LEU A 1 224 ? 30.101 12.114  7.855   1.00 36.89  ? 241 LEU A N   1 
ATOM   1646 C CA  . LEU A 1 224 ? 31.529 12.388  7.728   1.00 37.74  ? 241 LEU A CA  1 
ATOM   1647 C C   . LEU A 1 224 ? 31.905 13.016  6.383   1.00 48.64  ? 241 LEU A C   1 
ATOM   1648 O O   . LEU A 1 224 ? 32.996 13.584  6.259   1.00 49.91  ? 241 LEU A O   1 
ATOM   1649 C CB  . LEU A 1 224 ? 32.318 11.096  7.893   1.00 35.00  ? 241 LEU A CB  1 
ATOM   1650 C CG  . LEU A 1 224 ? 32.221 10.473  9.288   1.00 31.42  ? 241 LEU A CG  1 
ATOM   1651 C CD1 . LEU A 1 224 ? 32.740 9.050   9.223   1.00 31.93  ? 241 LEU A CD1 1 
ATOM   1652 C CD2 . LEU A 1 224 ? 33.036 11.306  10.258  1.00 35.90  ? 241 LEU A CD2 1 
ATOM   1653 N N   . ARG A 1 225 ? 31.050 12.898  5.370   1.00 46.85  ? 242 ARG A N   1 
ATOM   1654 C CA  . ARG A 1 225 ? 31.319 13.583  4.106   1.00 52.92  ? 242 ARG A CA  1 
ATOM   1655 C C   . ARG A 1 225 ? 31.084 15.087  4.211   1.00 63.90  ? 242 ARG A C   1 
ATOM   1656 O O   . ARG A 1 225 ? 31.745 15.865  3.517   1.00 63.99  ? 242 ARG A O   1 
ATOM   1657 C CB  . ARG A 1 225 ? 30.452 12.997  3.001   1.00 48.04  ? 242 ARG A CB  1 
ATOM   1658 C CG  . ARG A 1 225 ? 30.747 11.563  2.703   1.00 46.62  ? 242 ARG A CG  1 
ATOM   1659 C CD  . ARG A 1 225 ? 30.123 11.085  1.389   1.00 48.08  ? 242 ARG A CD  1 
ATOM   1660 N NE  . ARG A 1 225 ? 30.544 9.715   1.101   1.00 49.39  ? 242 ARG A NE  1 
ATOM   1661 C CZ  . ARG A 1 225 ? 29.867 8.624   1.445   1.00 42.40  ? 242 ARG A CZ  1 
ATOM   1662 N NH1 . ARG A 1 225 ? 28.653 8.693   1.969   1.00 49.27  ? 242 ARG A NH1 1 
ATOM   1663 N NH2 . ARG A 1 225 ? 30.431 7.435   1.266   1.00 47.13  ? 242 ARG A NH2 1 
ATOM   1664 N N   . ALA A 1 226 ? 30.144 15.514  5.062   1.00 76.41  ? 243 ALA A N   1 
ATOM   1665 C CA  . ALA A 1 226 ? 29.936 16.943  5.289   1.00 90.13  ? 243 ALA A CA  1 
ATOM   1666 C C   . ALA A 1 226 ? 31.054 17.560  6.130   1.00 103.52 ? 243 ALA A C   1 
ATOM   1667 O O   . ALA A 1 226 ? 31.345 18.755  5.981   1.00 108.44 ? 243 ALA A O   1 
ATOM   1668 C CB  . ALA A 1 226 ? 28.583 17.177  5.966   1.00 76.27  ? 243 ALA A CB  1 
ATOM   1669 N N   . THR A 1 227 ? 31.688 16.767  7.002   1.00 100.85 ? 244 THR A N   1 
ATOM   1670 C CA  . THR A 1 227 ? 32.645 17.295  7.972   1.00 106.54 ? 244 THR A CA  1 
ATOM   1671 C C   . THR A 1 227 ? 33.882 17.889  7.302   1.00 116.33 ? 244 THR A C   1 
ATOM   1672 O O   . THR A 1 227 ? 34.392 17.358  6.310   1.00 121.52 ? 244 THR A O   1 
ATOM   1673 C CB  . THR A 1 227 ? 33.083 16.191  8.942   1.00 101.84 ? 244 THR A CB  1 
ATOM   1674 O OG1 . THR A 1 227 ? 31.938 15.476  9.417   1.00 88.56  ? 244 THR A OG1 1 
ATOM   1675 C CG2 . THR A 1 227 ? 33.829 16.790  10.132  1.00 102.52 ? 244 THR A CG2 1 
ATOM   1676 N N   . THR A 1 228 ? 34.381 18.983  7.882   1.00 94.05  ? 245 THR A N   1 
ATOM   1677 C CA  . THR A 1 228 ? 35.573 19.676  7.391   1.00 82.46  ? 245 THR A CA  1 
ATOM   1678 C C   . THR A 1 228 ? 36.817 19.308  8.199   1.00 81.28  ? 245 THR A C   1 
ATOM   1679 O O   . THR A 1 228 ? 37.692 20.147  8.427   1.00 76.80  ? 245 THR A O   1 
ATOM   1680 C CB  . THR A 1 228 ? 35.394 21.211  7.439   1.00 64.57  ? 245 THR A CB  1 
ATOM   1681 N N   . GLU A 1 234 ? 41.419 18.353  10.075  1.00 111.33 ? 251 GLU A N   1 
ATOM   1682 C CA  . GLU A 1 234 ? 41.116 16.989  10.489  1.00 96.07  ? 251 GLU A CA  1 
ATOM   1683 C C   . GLU A 1 234 ? 39.618 16.733  10.659  1.00 92.30  ? 251 GLU A C   1 
ATOM   1684 O O   . GLU A 1 234 ? 38.978 17.351  11.511  1.00 90.43  ? 251 GLU A O   1 
ATOM   1685 C CB  . GLU A 1 234 ? 41.817 16.673  11.817  1.00 97.95  ? 251 GLU A CB  1 
ATOM   1686 C CG  . GLU A 1 234 ? 43.320 16.456  11.715  1.00 105.17 ? 251 GLU A CG  1 
ATOM   1687 C CD  . GLU A 1 234 ? 43.886 15.786  12.952  1.00 104.52 ? 251 GLU A CD  1 
ATOM   1688 O OE1 . GLU A 1 234 ? 43.175 15.758  13.984  1.00 108.01 ? 251 GLU A OE1 1 
ATOM   1689 O OE2 . GLU A 1 234 ? 45.032 15.287  12.887  1.00 91.95  ? 251 GLU A OE2 1 
ATOM   1690 N N   . ILE A 1 235 ? 39.066 15.809  9.867   1.00 78.04  ? 252 ILE A N   1 
ATOM   1691 C CA  . ILE A 1 235 ? 37.690 15.377  10.087  1.00 70.43  ? 252 ILE A CA  1 
ATOM   1692 C C   . ILE A 1 235 ? 37.631 14.508  11.335  1.00 66.26  ? 252 ILE A C   1 
ATOM   1693 O O   . ILE A 1 235 ? 38.228 13.421  11.386  1.00 49.46  ? 252 ILE A O   1 
ATOM   1694 C CB  . ILE A 1 235 ? 37.129 14.598  8.894   1.00 67.70  ? 252 ILE A CB  1 
ATOM   1695 C CG1 . ILE A 1 235 ? 37.028 15.478  7.644   1.00 78.11  ? 252 ILE A CG1 1 
ATOM   1696 C CG2 . ILE A 1 235 ? 35.776 13.992  9.306   1.00 53.10  ? 252 ILE A CG2 1 
ATOM   1697 C CD1 . ILE A 1 235 ? 38.264 15.439  6.758   1.00 68.44  ? 252 ILE A CD1 1 
ATOM   1698 N N   . GLN A 1 236 ? 36.829 14.925  12.303  1.00 57.21  ? 253 GLN A N   1 
ATOM   1699 C CA  . GLN A 1 236 ? 36.750 14.212  13.562  1.00 54.91  ? 253 GLN A CA  1 
ATOM   1700 C C   . GLN A 1 236 ? 35.565 13.254  13.547  1.00 41.31  ? 253 GLN A C   1 
ATOM   1701 O O   . GLN A 1 236 ? 34.449 13.624  13.161  1.00 40.65  ? 253 GLN A O   1 
ATOM   1702 C CB  . GLN A 1 236 ? 36.632 15.188  14.724  1.00 60.01  ? 253 GLN A CB  1 
ATOM   1703 C CG  . GLN A 1 236 ? 37.890 15.990  14.963  1.00 72.19  ? 253 GLN A CG  1 
ATOM   1704 C CD  . GLN A 1 236 ? 38.158 16.162  16.445  1.00 71.19  ? 253 GLN A CD  1 
ATOM   1705 O OE1 . GLN A 1 236 ? 37.875 17.208  17.036  1.00 69.22  ? 253 GLN A OE1 1 
ATOM   1706 N NE2 . GLN A 1 236 ? 38.684 15.106  17.064  1.00 69.02  ? 253 GLN A NE2 1 
ATOM   1707 N N   . LEU A 1 237 ? 35.823 12.015  13.950  1.00 37.48  ? 254 LEU A N   1 
ATOM   1708 C CA  . LEU A 1 237 ? 34.736 11.064  14.088  1.00 35.41  ? 254 LEU A CA  1 
ATOM   1709 C C   . LEU A 1 237 ? 33.704 11.589  15.083  1.00 35.63  ? 254 LEU A C   1 
ATOM   1710 O O   . LEU A 1 237 ? 32.500 11.446  14.865  1.00 34.68  ? 254 LEU A O   1 
ATOM   1711 C CB  . LEU A 1 237 ? 35.301 9.725   14.527  1.00 34.01  ? 254 LEU A CB  1 
ATOM   1712 C CG  . LEU A 1 237 ? 34.318 8.568   14.709  1.00 32.44  ? 254 LEU A CG  1 
ATOM   1713 C CD1 . LEU A 1 237 ? 33.548 8.306   13.433  1.00 37.58  ? 254 LEU A CD1 1 
ATOM   1714 C CD2 . LEU A 1 237 ? 35.074 7.322   15.167  1.00 31.24  ? 254 LEU A CD2 1 
ATOM   1715 N N   . THR A 1 238 ? 34.161 12.265  16.142  1.00 33.09  ? 255 THR A N   1 
ATOM   1716 C CA  . THR A 1 238 ? 33.245 12.840  17.129  1.00 37.50  ? 255 THR A CA  1 
ATOM   1717 C C   . THR A 1 238 ? 32.238 13.770  16.472  1.00 37.48  ? 255 THR A C   1 
ATOM   1718 O O   . THR A 1 238 ? 31.067 13.808  16.864  1.00 34.13  ? 255 THR A O   1 
ATOM   1719 C CB  . THR A 1 238 ? 34.051 13.592  18.196  1.00 35.88  ? 255 THR A CB  1 
ATOM   1720 O OG1 . THR A 1 238 ? 34.796 12.653  18.988  1.00 48.73  ? 255 THR A OG1 1 
ATOM   1721 C CG2 . THR A 1 238 ? 33.163 14.355  19.123  1.00 45.70  ? 255 THR A CG2 1 
ATOM   1722 N N   . ASP A 1 239 ? 32.677 14.526  15.462  1.00 41.73  ? 256 ASP A N   1 
ATOM   1723 C CA  . ASP A 1 239 ? 31.756 15.372  14.706  1.00 42.15  ? 256 ASP A CA  1 
ATOM   1724 C C   . ASP A 1 239 ? 30.722 14.546  13.964  1.00 36.75  ? 256 ASP A C   1 
ATOM   1725 O O   . ASP A 1 239 ? 29.541 14.898  13.936  1.00 37.33  ? 256 ASP A O   1 
ATOM   1726 C CB  . ASP A 1 239 ? 32.517 16.243  13.709  1.00 54.36  ? 256 ASP A CB  1 
ATOM   1727 C CG  . ASP A 1 239 ? 33.478 17.195  14.382  1.00 59.80  ? 256 ASP A CG  1 
ATOM   1728 O OD1 . ASP A 1 239 ? 33.161 17.674  15.483  1.00 59.46  ? 256 ASP A OD1 1 
ATOM   1729 O OD2 . ASP A 1 239 ? 34.546 17.469  13.801  1.00 77.70  ? 256 ASP A OD2 1 
ATOM   1730 N N   . GLY A 1 240 ? 31.144 13.457  13.333  1.00 37.93  ? 257 GLY A N   1 
ATOM   1731 C CA  . GLY A 1 240 ? 30.179 12.619  12.650  1.00 38.31  ? 257 GLY A CA  1 
ATOM   1732 C C   . GLY A 1 240 ? 29.149 12.044  13.600  1.00 35.35  ? 257 GLY A C   1 
ATOM   1733 O O   . GLY A 1 240 ? 27.954 11.995  13.291  1.00 39.59  ? 257 GLY A O   1 
ATOM   1734 N N   . ILE A 1 241 ? 29.603 11.581  14.760  1.00 35.31  ? 258 ILE A N   1 
ATOM   1735 C CA  . ILE A 1 241 ? 28.684 10.993  15.718  1.00 32.02  ? 258 ILE A CA  1 
ATOM   1736 C C   . ILE A 1 241 ? 27.711 12.040  16.226  1.00 35.72  ? 258 ILE A C   1 
ATOM   1737 O O   . ILE A 1 241 ? 26.494 11.809  16.275  1.00 34.39  ? 258 ILE A O   1 
ATOM   1738 C CB  . ILE A 1 241 ? 29.461 10.335  16.866  1.00 37.66  ? 258 ILE A CB  1 
ATOM   1739 C CG1 . ILE A 1 241 ? 30.154 9.093   16.323  1.00 32.97  ? 258 ILE A CG1 1 
ATOM   1740 C CG2 . ILE A 1 241 ? 28.510 10.067  18.046  1.00 33.53  ? 258 ILE A CG2 1 
ATOM   1741 C CD1 . ILE A 1 241 ? 31.387 8.693   17.093  1.00 32.16  ? 258 ILE A CD1 1 
ATOM   1742 N N   . ALA A 1 242 ? 28.222 13.227  16.559  1.00 36.35  ? 259 ALA A N   1 
ATOM   1743 C CA  . ALA A 1 242 ? 27.342 14.307  16.998  1.00 37.27  ? 259 ALA A CA  1 
ATOM   1744 C C   . ALA A 1 242 ? 26.258 14.577  15.967  1.00 43.21  ? 259 ALA A C   1 
ATOM   1745 O O   . ALA A 1 242 ? 25.089 14.794  16.315  1.00 35.09  ? 259 ALA A O   1 
ATOM   1746 C CB  . ALA A 1 242 ? 28.156 15.581  17.231  1.00 39.11  ? 259 ALA A CB  1 
ATOM   1747 N N   . ALA A 1 243 ? 26.636 14.587  14.682  1.00 39.71  ? 260 ALA A N   1 
ATOM   1748 C CA  . ALA A 1 243 ? 25.655 14.821  13.634  1.00 35.68  ? 260 ALA A CA  1 
ATOM   1749 C C   . ALA A 1 243 ? 24.696 13.650  13.517  1.00 40.39  ? 260 ALA A C   1 
ATOM   1750 O O   . ALA A 1 243 ? 23.501 13.835  13.265  1.00 38.83  ? 260 ALA A O   1 
ATOM   1751 C CB  . ALA A 1 243 ? 26.364 15.084  12.308  1.00 36.51  ? 260 ALA A CB  1 
ATOM   1752 N N   . LEU A 1 244 ? 25.210 12.438  13.673  1.00 36.61  ? 261 LEU A N   1 
ATOM   1753 C CA  . LEU A 1 244 ? 24.361 11.256  13.617  1.00 43.33  ? 261 LEU A CA  1 
ATOM   1754 C C   . LEU A 1 244 ? 23.287 11.281  14.700  1.00 42.23  ? 261 LEU A C   1 
ATOM   1755 O O   . LEU A 1 244 ? 22.162 10.826  14.464  1.00 45.06  ? 261 LEU A O   1 
ATOM   1756 C CB  . LEU A 1 244 ? 25.240 10.019  13.745  1.00 36.86  ? 261 LEU A CB  1 
ATOM   1757 C CG  . LEU A 1 244 ? 24.566 8.662   13.655  1.00 36.34  ? 261 LEU A CG  1 
ATOM   1758 C CD1 . LEU A 1 244 ? 23.897 8.538   12.305  1.00 40.21  ? 261 LEU A CD1 1 
ATOM   1759 C CD2 . LEU A 1 244 ? 25.598 7.560   13.875  1.00 41.02  ? 261 LEU A CD2 1 
ATOM   1760 N N   . LEU A 1 245 ? 23.604 11.843  15.871  1.00 45.92  ? 262 LEU A N   1 
ATOM   1761 C CA  . LEU A 1 245 ? 22.651 11.913  16.980  1.00 43.32  ? 262 LEU A CA  1 
ATOM   1762 C C   . LEU A 1 245 ? 21.339 12.586  16.575  1.00 47.28  ? 262 LEU A C   1 
ATOM   1763 O O   . LEU A 1 245 ? 20.290 12.313  17.161  1.00 44.10  ? 262 LEU A O   1 
ATOM   1764 C CB  . LEU A 1 245 ? 23.283 12.676  18.152  1.00 41.59  ? 262 LEU A CB  1 
ATOM   1765 C CG  . LEU A 1 245 ? 24.326 11.991  19.023  1.00 38.66  ? 262 LEU A CG  1 
ATOM   1766 C CD1 . LEU A 1 245 ? 24.859 12.984  20.083  1.00 40.08  ? 262 LEU A CD1 1 
ATOM   1767 C CD2 . LEU A 1 245 ? 23.711 10.807  19.709  1.00 46.46  ? 262 LEU A CD2 1 
ATOM   1768 N N   . ARG A 1 246 ? 21.379 13.504  15.615  1.00 46.89  ? 263 ARG A N   1 
ATOM   1769 C CA  . ARG A 1 246 ? 20.155 14.175  15.198  1.00 56.26  ? 263 ARG A CA  1 
ATOM   1770 C C   . ARG A 1 246 ? 19.241 13.300  14.344  1.00 55.80  ? 263 ARG A C   1 
ATOM   1771 O O   . ARG A 1 246 ? 18.042 13.574  14.275  1.00 59.54  ? 263 ARG A O   1 
ATOM   1772 C CB  . ARG A 1 246 ? 20.515 15.435  14.414  1.00 55.10  ? 263 ARG A CB  1 
ATOM   1773 C CG  . ARG A 1 246 ? 21.433 16.318  15.204  1.00 58.70  ? 263 ARG A CG  1 
ATOM   1774 C CD  . ARG A 1 246 ? 21.790 17.585  14.487  1.00 63.69  ? 263 ARG A CD  1 
ATOM   1775 N NE  . ARG A 1 246 ? 22.609 18.412  15.362  1.00 83.71  ? 263 ARG A NE  1 
ATOM   1776 C CZ  . ARG A 1 246 ? 22.882 19.690  15.150  1.00 95.71  ? 263 ARG A CZ  1 
ATOM   1777 N NH1 . ARG A 1 246 ? 22.423 20.326  14.084  1.00 100.34 ? 263 ARG A NH1 1 
ATOM   1778 N NH2 . ARG A 1 246 ? 23.621 20.350  16.039  1.00 97.21  ? 263 ARG A NH2 1 
ATOM   1779 N N   . GLU A 1 247 ? 19.755 12.229  13.748  1.00 51.29  ? 264 GLU A N   1 
ATOM   1780 C CA  . GLU A 1 247 ? 18.991 11.385  12.836  1.00 49.89  ? 264 GLU A CA  1 
ATOM   1781 C C   . GLU A 1 247 ? 18.699 10.003  13.391  1.00 50.84  ? 264 GLU A C   1 
ATOM   1782 O O   . GLU A 1 247 ? 17.648 9.441   13.096  1.00 57.91  ? 264 GLU A O   1 
ATOM   1783 C CB  . GLU A 1 247 ? 19.754 11.238  11.499  1.00 53.92  ? 264 GLU A CB  1 
ATOM   1784 C CG  . GLU A 1 247 ? 19.080 10.339  10.423  1.00 67.08  ? 264 GLU A CG  1 
ATOM   1785 C CD  . GLU A 1 247 ? 20.065 9.788   9.355   1.00 70.21  ? 264 GLU A CD  1 
ATOM   1786 O OE1 . GLU A 1 247 ? 21.255 10.180  9.352   1.00 59.71  ? 264 GLU A OE1 1 
ATOM   1787 O OE2 . GLU A 1 247 ? 19.644 8.968   8.502   1.00 64.98  ? 264 GLU A OE2 1 
ATOM   1788 N N   . ARG A 1 248 ? 19.607 9.440   14.176  1.00 46.48  ? 265 ARG A N   1 
ATOM   1789 C CA  . ARG A 1 248 ? 19.530 8.052   14.590  1.00 46.43  ? 265 ARG A CA  1 
ATOM   1790 C C   . ARG A 1 248 ? 19.872 7.954   16.073  1.00 41.35  ? 265 ARG A C   1 
ATOM   1791 O O   . ARG A 1 248 ? 20.491 8.851   16.651  1.00 40.91  ? 265 ARG A O   1 
ATOM   1792 C CB  . ARG A 1 248 ? 20.500 7.200   13.765  1.00 49.20  ? 265 ARG A CB  1 
ATOM   1793 C CG  . ARG A 1 248 ? 20.448 7.464   12.242  1.00 58.85  ? 265 ARG A CG  1 
ATOM   1794 C CD  . ARG A 1 248 ? 19.262 6.814   11.598  1.00 66.11  ? 265 ARG A CD  1 
ATOM   1795 N NE  . ARG A 1 248 ? 19.395 5.362   11.634  1.00 71.25  ? 265 ARG A NE  1 
ATOM   1796 C CZ  . ARG A 1 248 ? 18.395 4.512   11.835  1.00 78.53  ? 265 ARG A CZ  1 
ATOM   1797 N NH1 . ARG A 1 248 ? 17.153 4.929   12.038  1.00 87.23  ? 265 ARG A NH1 1 
ATOM   1798 N NH2 . ARG A 1 248 ? 18.649 3.208   11.838  1.00 78.67  ? 265 ARG A NH2 1 
ATOM   1799 N N   . ASP A 1 249 ? 19.524 6.817   16.655  1.00 37.67  ? 266 ASP A N   1 
ATOM   1800 C CA  . ASP A 1 249 ? 19.827 6.528   18.055  1.00 36.16  ? 266 ASP A CA  1 
ATOM   1801 C C   . ASP A 1 249 ? 21.277 6.124   18.228  1.00 32.58  ? 266 ASP A C   1 
ATOM   1802 O O   . ASP A 1 249 ? 21.795 5.292   17.475  1.00 40.89  ? 266 ASP A O   1 
ATOM   1803 C CB  . ASP A 1 249 ? 18.934 5.404   18.556  1.00 45.55  ? 266 ASP A CB  1 
ATOM   1804 C CG  . ASP A 1 249 ? 17.506 5.804   18.606  1.00 52.25  ? 266 ASP A CG  1 
ATOM   1805 O OD1 . ASP A 1 249 ? 17.269 7.024   18.756  1.00 57.53  ? 266 ASP A OD1 1 
ATOM   1806 O OD2 . ASP A 1 249 ? 16.638 4.914   18.477  1.00 56.57  ? 266 ASP A OD2 1 
ATOM   1807 N N   . VAL A 1 250 ? 21.939 6.714   19.213  1.00 34.54  ? 267 VAL A N   1 
ATOM   1808 C CA  . VAL A 1 250 ? 23.302 6.347   19.562  1.00 25.91  ? 267 VAL A CA  1 
ATOM   1809 C C   . VAL A 1 250 ? 23.371 6.052   21.058  1.00 28.32  ? 267 VAL A C   1 
ATOM   1810 O O   . VAL A 1 250 ? 22.925 6.864   21.873  1.00 29.72  ? 267 VAL A O   1 
ATOM   1811 C CB  . VAL A 1 250 ? 24.288 7.457   19.190  1.00 25.63  ? 267 VAL A CB  1 
ATOM   1812 C CG1 . VAL A 1 250 ? 25.718 7.022   19.590  1.00 26.38  ? 267 VAL A CG1 1 
ATOM   1813 C CG2 . VAL A 1 250 ? 24.153 7.774   17.703  1.00 33.53  ? 267 VAL A CG2 1 
ATOM   1814 N N   . TYR A 1 251 ? 23.943 4.900   21.407  1.00 29.29  ? 268 TYR A N   1 
ATOM   1815 C CA  . TYR A 1 251 ? 24.072 4.438   22.783  1.00 29.41  ? 268 TYR A CA  1 
ATOM   1816 C C   . TYR A 1 251 ? 25.545 4.364   23.147  1.00 28.89  ? 268 TYR A C   1 
ATOM   1817 O O   . TYR A 1 251 ? 26.407 4.319   22.283  1.00 27.15  ? 268 TYR A O   1 
ATOM   1818 C CB  . TYR A 1 251 ? 23.426 3.057   22.968  1.00 28.59  ? 268 TYR A CB  1 
ATOM   1819 C CG  . TYR A 1 251 ? 21.965 3.071   22.655  1.00 33.76  ? 268 TYR A CG  1 
ATOM   1820 C CD1 . TYR A 1 251 ? 21.032 3.417   23.631  1.00 32.72  ? 268 TYR A CD1 1 
ATOM   1821 C CD2 . TYR A 1 251 ? 21.502 2.800   21.362  1.00 39.20  ? 268 TYR A CD2 1 
ATOM   1822 C CE1 . TYR A 1 251 ? 19.684 3.454   23.350  1.00 35.17  ? 268 TYR A CE1 1 
ATOM   1823 C CE2 . TYR A 1 251 ? 20.125 2.836   21.073  1.00 39.15  ? 268 TYR A CE2 1 
ATOM   1824 C CZ  . TYR A 1 251 ? 19.237 3.160   22.066  1.00 39.14  ? 268 TYR A CZ  1 
ATOM   1825 O OH  . TYR A 1 251 ? 17.887 3.201   21.797  1.00 43.05  ? 268 TYR A OH  1 
ATOM   1826 N N   . ALA A 1 252 ? 25.815 4.370   24.441  1.00 25.68  ? 269 ALA A N   1 
ATOM   1827 C CA  . ALA A 1 252 ? 27.141 4.169   24.992  1.00 29.02  ? 269 ALA A CA  1 
ATOM   1828 C C   . ALA A 1 252 ? 27.051 3.011   25.965  1.00 25.85  ? 269 ALA A C   1 
ATOM   1829 O O   . ALA A 1 252 ? 26.062 2.872   26.660  1.00 27.53  ? 269 ALA A O   1 
ATOM   1830 C CB  . ALA A 1 252 ? 27.649 5.422   25.703  1.00 25.90  ? 269 ALA A CB  1 
ATOM   1831 N N   . HIS A 1 253 ? 28.063 2.164   25.999  1.00 25.77  ? 270 HIS A N   1 
ATOM   1832 C CA  . HIS A 1 253 ? 28.003 0.981   26.844  1.00 26.33  ? 270 HIS A CA  1 
ATOM   1833 C C   . HIS A 1 253 ? 29.248 0.884   27.692  1.00 27.70  ? 270 HIS A C   1 
ATOM   1834 O O   . HIS A 1 253 ? 30.368 0.898   27.163  1.00 23.76  ? 270 HIS A O   1 
ATOM   1835 C CB  . HIS A 1 253 ? 27.850 -0.296  26.022  1.00 28.90  ? 270 HIS A CB  1 
ATOM   1836 C CG  . HIS A 1 253 ? 27.645 -1.516  26.860  1.00 32.12  ? 270 HIS A CG  1 
ATOM   1837 N ND1 . HIS A 1 253 ? 26.446 -1.808  27.483  1.00 25.45  ? 270 HIS A ND1 1 
ATOM   1838 C CD2 . HIS A 1 253 ? 28.478 -2.541  27.146  1.00 27.28  ? 270 HIS A CD2 1 
ATOM   1839 C CE1 . HIS A 1 253 ? 26.565 -2.951  28.132  1.00 27.48  ? 270 HIS A CE1 1 
ATOM   1840 N NE2 . HIS A 1 253 ? 27.785 -3.419  27.939  1.00 27.24  ? 270 HIS A NE2 1 
ATOM   1841 N N   . ARG A 1 254 ? 29.026 0.788   29.009  1.00 27.18  ? 271 ARG A N   1 
ATOM   1842 C CA  . ARG A 1 254 ? 30.060 0.601   30.023  1.00 28.68  ? 271 ARG A CA  1 
ATOM   1843 C C   . ARG A 1 254 ? 30.460 -0.864  29.952  1.00 30.01  ? 271 ARG A C   1 
ATOM   1844 O O   . ARG A 1 254 ? 29.873 -1.727  30.611  1.00 26.93  ? 271 ARG A O   1 
ATOM   1845 C CB  . ARG A 1 254 ? 29.511 0.981   31.401  1.00 27.53  ? 271 ARG A CB  1 
ATOM   1846 C CG  . ARG A 1 254 ? 29.014 2.406   31.483  1.00 22.93  ? 271 ARG A CG  1 
ATOM   1847 C CD  . ARG A 1 254 ? 28.328 2.659   32.817  1.00 28.27  ? 271 ARG A CD  1 
ATOM   1848 N NE  . ARG A 1 254 ? 27.641 3.947   32.910  1.00 27.83  ? 271 ARG A NE  1 
ATOM   1849 C CZ  . ARG A 1 254 ? 28.242 5.087   33.229  1.00 26.04  ? 271 ARG A CZ  1 
ATOM   1850 N NH1 . ARG A 1 254 ? 29.546 5.143   33.462  1.00 27.87  ? 271 ARG A NH1 1 
ATOM   1851 N NH2 . ARG A 1 254 ? 27.516 6.184   33.365  1.00 30.82  ? 271 ARG A NH2 1 
ATOM   1852 N N   . TYR A 1 255 ? 31.461 -1.154  29.132  1.00 28.14  ? 272 TYR A N   1 
ATOM   1853 C CA  . TYR A 1 255 ? 31.854 -2.537  28.915  1.00 28.11  ? 272 TYR A CA  1 
ATOM   1854 C C   . TYR A 1 255 ? 32.547 -3.075  30.153  1.00 26.31  ? 272 TYR A C   1 
ATOM   1855 O O   . TYR A 1 255 ? 33.076 -2.333  30.972  1.00 30.58  ? 272 TYR A O   1 
ATOM   1856 C CB  . TYR A 1 255 ? 32.786 -2.667  27.702  1.00 28.57  ? 272 TYR A CB  1 
ATOM   1857 C CG  . TYR A 1 255 ? 34.003 -1.800  27.880  1.00 27.96  ? 272 TYR A CG  1 
ATOM   1858 C CD1 . TYR A 1 255 ? 35.111 -2.246  28.588  1.00 27.62  ? 272 TYR A CD1 1 
ATOM   1859 C CD2 . TYR A 1 255 ? 34.024 -0.510  27.370  1.00 26.95  ? 272 TYR A CD2 1 
ATOM   1860 C CE1 . TYR A 1 255 ? 36.190 -1.428  28.767  1.00 26.23  ? 272 TYR A CE1 1 
ATOM   1861 C CE2 . TYR A 1 255 ? 35.073 0.303   27.560  1.00 27.28  ? 272 TYR A CE2 1 
ATOM   1862 C CZ  . TYR A 1 255 ? 36.165 -0.145  28.236  1.00 32.37  ? 272 TYR A CZ  1 
ATOM   1863 O OH  . TYR A 1 255 ? 37.216 0.727   28.397  1.00 41.00  ? 272 TYR A OH  1 
ATOM   1864 N N   . ASP A 1 256 ? 32.553 -4.395  30.267  1.00 26.11  ? 273 ASP A N   1 
ATOM   1865 C CA  . ASP A 1 256 ? 33.348 -5.082  31.264  1.00 26.68  ? 273 ASP A CA  1 
ATOM   1866 C C   . ASP A 1 256 ? 34.709 -5.406  30.664  1.00 32.74  ? 273 ASP A C   1 
ATOM   1867 O O   . ASP A 1 256 ? 34.803 -6.082  29.638  1.00 31.27  ? 273 ASP A O   1 
ATOM   1868 C CB  . ASP A 1 256 ? 32.670 -6.367  31.725  1.00 33.72  ? 273 ASP A CB  1 
ATOM   1869 C CG  . ASP A 1 256 ? 33.500 -7.086  32.778  1.00 38.32  ? 273 ASP A CG  1 
ATOM   1870 O OD1 . ASP A 1 256 ? 33.616 -6.536  33.868  1.00 35.91  ? 273 ASP A OD1 1 
ATOM   1871 O OD2 . ASP A 1 256 ? 34.095 -8.151  32.495  1.00 39.79  ? 273 ASP A OD2 1 
ATOM   1872 N N   . GLY A 1 257 ? 35.753 -4.922  31.289  1.00 34.45  ? 274 GLY A N   1 
ATOM   1873 C CA  . GLY A 1 257 ? 37.083 -5.138  30.768  1.00 32.94  ? 274 GLY A CA  1 
ATOM   1874 C C   . GLY A 1 257 ? 38.000 -4.023  31.200  1.00 28.66  ? 274 GLY A C   1 
ATOM   1875 O O   . GLY A 1 257 ? 37.581 -2.987  31.704  1.00 33.04  ? 274 GLY A O   1 
ATOM   1876 N N   . LYS A 1 258 ? 39.286 -4.283  31.057  1.00 28.04  ? 275 LYS A N   1 
ATOM   1877 C CA  . LYS A 1 258 ? 40.365 -3.380  31.439  1.00 29.17  ? 275 LYS A CA  1 
ATOM   1878 C C   . LYS A 1 258 ? 41.038 -2.847  30.169  1.00 30.74  ? 275 LYS A C   1 
ATOM   1879 O O   . LYS A 1 258 ? 41.610 -3.621  29.394  1.00 27.20  ? 275 LYS A O   1 
ATOM   1880 C CB  . LYS A 1 258 ? 41.381 -4.119  32.313  1.00 31.78  ? 275 LYS A CB  1 
ATOM   1881 C CG  . LYS A 1 258 ? 42.651 -3.348  32.556  1.00 35.40  ? 275 LYS A CG  1 
ATOM   1882 C CD  . LYS A 1 258 ? 42.469 -2.088  33.322  1.00 46.21  ? 275 LYS A CD  1 
ATOM   1883 C CE  . LYS A 1 258 ? 43.839 -1.438  33.582  1.00 49.07  ? 275 LYS A CE  1 
ATOM   1884 N NZ  . LYS A 1 258 ? 43.790 -0.467  34.708  1.00 50.29  ? 275 LYS A NZ  1 
ATOM   1885 N N   . ARG A 1 259 ? 40.981 -1.536  29.977  1.00 28.38  ? 276 ARG A N   1 
ATOM   1886 C CA  . ARG A 1 259 ? 41.595 -0.867  28.841  1.00 31.39  ? 276 ARG A CA  1 
ATOM   1887 C C   . ARG A 1 259 ? 42.948 -0.298  29.239  1.00 31.93  ? 276 ARG A C   1 
ATOM   1888 O O   . ARG A 1 259 ? 43.071 0.371   30.267  1.00 28.35  ? 276 ARG A O   1 
ATOM   1889 C CB  . ARG A 1 259 ? 40.732 0.276   28.316  1.00 34.62  ? 276 ARG A CB  1 
ATOM   1890 C CG  . ARG A 1 259 ? 41.464 1.109   27.275  1.00 39.26  ? 276 ARG A CG  1 
ATOM   1891 C CD  . ARG A 1 259 ? 40.667 2.278   26.886  1.00 48.46  ? 276 ARG A CD  1 
ATOM   1892 N NE  . ARG A 1 259 ? 40.769 3.319   27.884  1.00 54.51  ? 276 ARG A NE  1 
ATOM   1893 C CZ  . ARG A 1 259 ? 41.234 4.534   27.656  1.00 55.57  ? 276 ARG A CZ  1 
ATOM   1894 N NH1 . ARG A 1 259 ? 41.680 4.898   26.460  1.00 48.44  ? 276 ARG A NH1 1 
ATOM   1895 N NH2 . ARG A 1 259 ? 41.233 5.414   28.649  1.00 64.59  ? 276 ARG A NH2 1 
ATOM   1896 N N   . TYR A 1 260 ? 43.952 -0.574  28.429  1.00 26.91  ? 277 TYR A N   1 
ATOM   1897 C CA  . TYR A 1 260 ? 45.254 0.070   28.506  1.00 23.36  ? 277 TYR A CA  1 
ATOM   1898 C C   . TYR A 1 260 ? 45.391 1.047   27.337  1.00 26.56  ? 277 TYR A C   1 
ATOM   1899 O O   . TYR A 1 260 ? 45.330 0.640   26.173  1.00 26.44  ? 277 TYR A O   1 
ATOM   1900 C CB  . TYR A 1 260 ? 46.363 -0.983  28.472  1.00 21.82  ? 277 TYR A CB  1 
ATOM   1901 C CG  . TYR A 1 260 ? 46.281 -1.999  29.591  1.00 23.52  ? 277 TYR A CG  1 
ATOM   1902 C CD1 . TYR A 1 260 ? 46.899 -1.751  30.824  1.00 27.96  ? 277 TYR A CD1 1 
ATOM   1903 C CD2 . TYR A 1 260 ? 45.592 -3.194  29.434  1.00 25.93  ? 277 TYR A CD2 1 
ATOM   1904 C CE1 . TYR A 1 260 ? 46.833 -2.675  31.877  1.00 31.86  ? 277 TYR A CE1 1 
ATOM   1905 C CE2 . TYR A 1 260 ? 45.514 -4.134  30.483  1.00 26.31  ? 277 TYR A CE2 1 
ATOM   1906 C CZ  . TYR A 1 260 ? 46.135 -3.861  31.697  1.00 34.29  ? 277 TYR A CZ  1 
ATOM   1907 O OH  . TYR A 1 260 ? 46.054 -4.769  32.723  1.00 33.02  ? 277 TYR A OH  1 
ATOM   1908 N N   . ASP A 1 261 ? 45.571 2.332   27.639  1.00 26.86  ? 278 ASP A N   1 
ATOM   1909 C CA  . ASP A 1 261 ? 45.730 3.363   26.613  1.00 32.02  ? 278 ASP A CA  1 
ATOM   1910 C C   . ASP A 1 261 ? 47.199 3.388   26.231  1.00 29.62  ? 278 ASP A C   1 
ATOM   1911 O O   . ASP A 1 261 ? 48.029 3.959   26.936  1.00 24.89  ? 278 ASP A O   1 
ATOM   1912 C CB  . ASP A 1 261 ? 45.254 4.722   27.101  1.00 33.07  ? 278 ASP A CB  1 
ATOM   1913 C CG  . ASP A 1 261 ? 45.275 5.787   25.996  1.00 35.83  ? 278 ASP A CG  1 
ATOM   1914 O OD1 . ASP A 1 261 ? 46.031 5.636   25.013  1.00 29.70  ? 278 ASP A OD1 1 
ATOM   1915 O OD2 . ASP A 1 261 ? 44.547 6.788   26.121  1.00 35.30  ? 278 ASP A OD2 1 
ATOM   1916 N N   . CYS A 1 262 ? 47.529 2.743   25.133  1.00 27.23  ? 279 CYS A N   1 
ATOM   1917 C CA  . CYS A 1 262 ? 48.913 2.642   24.714  1.00 29.23  ? 279 CYS A CA  1 
ATOM   1918 C C   . CYS A 1 262 ? 49.348 3.806   23.845  1.00 32.10  ? 279 CYS A C   1 
ATOM   1919 O O   . CYS A 1 262 ? 50.417 3.737   23.253  1.00 33.57  ? 279 CYS A O   1 
ATOM   1920 C CB  . CYS A 1 262 ? 49.134 1.327   23.980  1.00 29.70  ? 279 CYS A CB  1 
ATOM   1921 S SG  . CYS A 1 262 ? 48.837 -0.157  25.001  1.00 26.58  ? 279 CYS A SG  1 
ATOM   1922 N N   . GLY A 1 263 ? 48.552 4.863   23.776  1.00 26.79  ? 280 GLY A N   1 
ATOM   1923 C CA  . GLY A 1 263 ? 48.875 6.064   23.035  1.00 33.83  ? 280 GLY A CA  1 
ATOM   1924 C C   . GLY A 1 263 ? 50.019 6.879   23.600  1.00 33.77  ? 280 GLY A C   1 
ATOM   1925 O O   . GLY A 1 263 ? 50.521 7.762   22.900  1.00 40.42  ? 280 GLY A O   1 
ATOM   1926 N N   . SER A 1 264 ? 50.447 6.612   24.828  1.00 30.57  ? 281 SER A N   1 
ATOM   1927 C CA  . SER A 1 264 ? 51.624 7.251   25.400  1.00 27.04  ? 281 SER A CA  1 
ATOM   1928 C C   . SER A 1 264 ? 52.674 6.191   25.698  1.00 26.93  ? 281 SER A C   1 
ATOM   1929 O O   . SER A 1 264 ? 52.376 5.005   25.825  1.00 27.88  ? 281 SER A O   1 
ATOM   1930 C CB  . SER A 1 264 ? 51.265 8.054   26.667  1.00 35.65  ? 281 SER A CB  1 
ATOM   1931 O OG  . SER A 1 264 ? 50.996 7.207   27.772  1.00 29.20  ? 281 SER A OG  1 
ATOM   1932 N N   . LYS A 1 265 ? 53.934 6.608   25.775  1.00 25.96  ? 282 LYS A N   1 
ATOM   1933 C CA  . LYS A 1 265 ? 54.954 5.634   26.147  1.00 31.03  ? 282 LYS A CA  1 
ATOM   1934 C C   . LYS A 1 265 ? 54.663 5.079   27.540  1.00 28.28  ? 282 LYS A C   1 
ATOM   1935 O O   . LYS A 1 265 ? 54.823 3.876   27.785  1.00 28.24  ? 282 LYS A O   1 
ATOM   1936 C CB  . LYS A 1 265 ? 56.368 6.232   26.099  1.00 29.68  ? 282 LYS A CB  1 
ATOM   1937 C CG  . LYS A 1 265 ? 56.919 6.447   24.727  1.00 44.63  ? 282 LYS A CG  1 
ATOM   1938 C CD  . LYS A 1 265 ? 58.338 7.055   24.723  1.00 45.99  ? 282 LYS A CD  1 
ATOM   1939 C CE  . LYS A 1 265 ? 58.638 7.941   25.890  1.00 43.61  ? 282 LYS A CE  1 
ATOM   1940 N NZ  . LYS A 1 265 ? 60.007 8.539   25.790  1.00 42.59  ? 282 LYS A NZ  1 
ATOM   1941 N N   . ALA A 1 266 ? 54.223 5.946   28.460  1.00 27.81  ? 283 ALA A N   1 
ATOM   1942 C CA  . ALA A 1 266 ? 53.896 5.479   29.801  1.00 28.20  ? 283 ALA A CA  1 
ATOM   1943 C C   . ALA A 1 266 ? 52.758 4.473   29.764  1.00 29.79  ? 283 ALA A C   1 
ATOM   1944 O O   . ALA A 1 266 ? 52.791 3.448   30.469  1.00 27.90  ? 283 ALA A O   1 
ATOM   1945 C CB  . ALA A 1 266 ? 53.515 6.668   30.690  1.00 31.91  ? 283 ALA A CB  1 
ATOM   1946 N N   . GLY A 1 267 ? 51.717 4.758   28.979  1.00 26.43  ? 284 GLY A N   1 
ATOM   1947 C CA  . GLY A 1 267 ? 50.586 3.841   28.946  1.00 27.58  ? 284 GLY A CA  1 
ATOM   1948 C C   . GLY A 1 267 ? 50.975 2.504   28.358  1.00 26.02  ? 284 GLY A C   1 
ATOM   1949 O O   . GLY A 1 267 ? 50.572 1.447   28.852  1.00 30.47  ? 284 GLY A O   1 
ATOM   1950 N N   . MET A 1 268 ? 51.778 2.537   27.295  1.00 27.71  ? 285 MET A N   1 
ATOM   1951 C CA  . MET A 1 268 ? 52.229 1.316   26.645  1.00 28.74  ? 285 MET A CA  1 
ATOM   1952 C C   . MET A 1 268 ? 53.136 0.511   27.553  1.00 24.42  ? 285 MET A C   1 
ATOM   1953 O O   . MET A 1 268 ? 53.064 -0.723  27.574  1.00 23.49  ? 285 MET A O   1 
ATOM   1954 C CB  . MET A 1 268 ? 52.959 1.660   25.342  1.00 28.26  ? 285 MET A CB  1 
ATOM   1955 C CG  . MET A 1 268 ? 53.653 0.461   24.768  1.00 34.21  ? 285 MET A CG  1 
ATOM   1956 S SD  . MET A 1 268 ? 52.700 -0.179  23.451  1.00 45.76  ? 285 MET A SD  1 
ATOM   1957 C CE  . MET A 1 268 ? 53.124 1.068   22.314  1.00 36.41  ? 285 MET A CE  1 
ATOM   1958 N N   . PHE A 1 269 ? 54.022 1.203   28.268  1.00 27.53  ? 286 PHE A N   1 
ATOM   1959 C CA  . PHE A 1 269 ? 54.893 0.559   29.240  1.00 27.14  ? 286 PHE A CA  1 
ATOM   1960 C C   . PHE A 1 269 ? 54.084 -0.186  30.291  1.00 24.13  ? 286 PHE A C   1 
ATOM   1961 O O   . PHE A 1 269 ? 54.392 -1.335  30.620  1.00 25.43  ? 286 PHE A O   1 
ATOM   1962 C CB  . PHE A 1 269 ? 55.773 1.623   29.892  1.00 31.62  ? 286 PHE A CB  1 
ATOM   1963 C CG  . PHE A 1 269 ? 56.706 1.086   30.897  1.00 23.36  ? 286 PHE A CG  1 
ATOM   1964 C CD1 . PHE A 1 269 ? 57.903 0.532   30.495  1.00 29.46  ? 286 PHE A CD1 1 
ATOM   1965 C CD2 . PHE A 1 269 ? 56.392 1.118   32.251  1.00 27.31  ? 286 PHE A CD2 1 
ATOM   1966 C CE1 . PHE A 1 269 ? 58.773 0.040   31.418  1.00 31.82  ? 286 PHE A CE1 1 
ATOM   1967 C CE2 . PHE A 1 269 ? 57.265 0.625   33.177  1.00 27.43  ? 286 PHE A CE2 1 
ATOM   1968 C CZ  . PHE A 1 269 ? 58.453 0.082   32.757  1.00 25.29  ? 286 PHE A CZ  1 
ATOM   1969 N N   A GLN A 1 270 ? 53.029 0.432   30.819  0.50 25.11  ? 287 GLN A N   1 
ATOM   1970 N N   B GLN A 1 270 ? 53.030 0.439   30.814  0.50 26.07  ? 287 GLN A N   1 
ATOM   1971 C CA  A GLN A 1 270 ? 52.276 -0.239  31.871  0.50 27.77  ? 287 GLN A CA  1 
ATOM   1972 C CA  B GLN A 1 270 ? 52.259 -0.221  31.860  0.50 27.93  ? 287 GLN A CA  1 
ATOM   1973 C C   A GLN A 1 270 ? 51.466 -1.404  31.313  0.50 27.12  ? 287 GLN A C   1 
ATOM   1974 C C   B GLN A 1 270 ? 51.491 -1.409  31.303  0.50 26.57  ? 287 GLN A C   1 
ATOM   1975 O O   A GLN A 1 270 ? 51.203 -2.371  32.030  0.50 25.20  ? 287 GLN A O   1 
ATOM   1976 O O   B GLN A 1 270 ? 51.285 -2.398  32.011  0.50 25.15  ? 287 GLN A O   1 
ATOM   1977 C CB  A GLN A 1 270 ? 51.363 0.747   32.603  0.50 27.87  ? 287 GLN A CB  1 
ATOM   1978 C CB  B GLN A 1 270 ? 51.303 0.764   32.534  0.50 28.11  ? 287 GLN A CB  1 
ATOM   1979 C CG  A GLN A 1 270 ? 52.093 1.859   33.368  0.50 31.85  ? 287 GLN A CG  1 
ATOM   1980 C CG  B GLN A 1 270 ? 50.584 0.184   33.747  0.50 32.34  ? 287 GLN A CG  1 
ATOM   1981 C CD  A GLN A 1 270 ? 53.092 1.364   34.428  0.50 29.27  ? 287 GLN A CD  1 
ATOM   1982 C CD  B GLN A 1 270 ? 51.506 -0.605  34.658  0.50 29.00  ? 287 GLN A CD  1 
ATOM   1983 O OE1 A GLN A 1 270 ? 53.021 0.229   34.904  0.50 31.74  ? 287 GLN A OE1 1 
ATOM   1984 O OE1 B GLN A 1 270 ? 52.590 -0.153  35.029  0.50 32.79  ? 287 GLN A OE1 1 
ATOM   1985 N NE2 A GLN A 1 270 ? 54.027 2.226   34.785  0.50 21.96  ? 287 GLN A NE2 1 
ATOM   1986 N NE2 B GLN A 1 270 ? 51.090 -1.799  34.991  0.50 22.53  ? 287 GLN A NE2 1 
ATOM   1987 N N   . ALA A 1 271 ? 51.062 -1.332  30.045  1.00 25.61  ? 288 ALA A N   1 
ATOM   1988 C CA  . ALA A 1 271 ? 50.449 -2.495  29.402  1.00 22.77  ? 288 ALA A CA  1 
ATOM   1989 C C   . ALA A 1 271 ? 51.437 -3.648  29.331  1.00 24.11  ? 288 ALA A C   1 
ATOM   1990 O O   . ALA A 1 271 ? 51.085 -4.793  29.603  1.00 27.19  ? 288 ALA A O   1 
ATOM   1991 C CB  . ALA A 1 271 ? 49.964 -2.144  27.989  1.00 28.17  ? 288 ALA A CB  1 
ATOM   1992 N N   . THR A 1 272 ? 52.687 -3.356  28.977  1.00 24.91  ? 289 THR A N   1 
ATOM   1993 C CA  . THR A 1 272 ? 53.703 -4.401  28.916  1.00 24.75  ? 289 THR A CA  1 
ATOM   1994 C C   . THR A 1 272 ? 53.915 -5.025  30.289  1.00 26.66  ? 289 THR A C   1 
ATOM   1995 O O   . THR A 1 272 ? 53.964 -6.258  30.444  1.00 25.84  ? 289 THR A O   1 
ATOM   1996 C CB  . THR A 1 272 ? 55.003 -3.791  28.361  1.00 28.11  ? 289 THR A CB  1 
ATOM   1997 O OG1 . THR A 1 272 ? 54.734 -3.281  27.053  1.00 30.96  ? 289 THR A OG1 1 
ATOM   1998 C CG2 . THR A 1 272 ? 56.111 -4.800  28.266  1.00 29.82  ? 289 THR A CG2 1 
ATOM   1999 N N   . VAL A 1 273 ? 54.028 -4.181  31.309  1.00 25.38  ? 290 VAL A N   1 
ATOM   2000 C CA  . VAL A 1 273 ? 54.216 -4.681  32.667  1.00 22.88  ? 290 VAL A CA  1 
ATOM   2001 C C   . VAL A 1 273 ? 53.027 -5.543  33.066  1.00 21.96  ? 290 VAL A C   1 
ATOM   2002 O O   . VAL A 1 273 ? 53.177 -6.696  33.485  1.00 26.33  ? 290 VAL A O   1 
ATOM   2003 C CB  . VAL A 1 273 ? 54.419 -3.488  33.621  1.00 23.82  ? 290 VAL A CB  1 
ATOM   2004 C CG1 . VAL A 1 273 ? 54.302 -3.899  35.107  1.00 27.23  ? 290 VAL A CG1 1 
ATOM   2005 C CG2 . VAL A 1 273 ? 55.778 -2.843  33.371  1.00 23.79  ? 290 VAL A CG2 1 
ATOM   2006 N N   . ALA A 1 274 ? 51.825 -5.008  32.899  1.00 23.39  ? 291 ALA A N   1 
ATOM   2007 C CA  . ALA A 1 274 ? 50.629 -5.681  33.403  1.00 24.76  ? 291 ALA A CA  1 
ATOM   2008 C C   . ALA A 1 274 ? 50.361 -6.969  32.650  1.00 26.67  ? 291 ALA A C   1 
ATOM   2009 O O   . ALA A 1 274 ? 50.122 -8.022  33.261  1.00 26.14  ? 291 ALA A O   1 
ATOM   2010 C CB  . ALA A 1 274 ? 49.413 -4.759  33.297  1.00 29.57  ? 291 ALA A CB  1 
ATOM   2011 N N   . LEU A 1 275 ? 50.394 -6.913  31.314  1.00 24.04  ? 292 LEU A N   1 
ATOM   2012 C CA  . LEU A 1 275 ? 50.129 -8.129  30.557  1.00 25.43  ? 292 LEU A CA  1 
ATOM   2013 C C   . LEU A 1 275 ? 51.326 -9.053  30.608  1.00 25.09  ? 292 LEU A C   1 
ATOM   2014 O O   . LEU A 1 275 ? 51.180 -10.278 30.539  1.00 27.00  ? 292 LEU A O   1 
ATOM   2015 C CB  . LEU A 1 275 ? 49.755 -7.768  29.118  1.00 30.40  ? 292 LEU A CB  1 
ATOM   2016 C CG  . LEU A 1 275 ? 48.449 -6.957  29.069  1.00 25.76  ? 292 LEU A CG  1 
ATOM   2017 C CD1 . LEU A 1 275 ? 48.186 -6.603  27.635  1.00 40.26  ? 292 LEU A CD1 1 
ATOM   2018 C CD2 . LEU A 1 275 ? 47.265 -7.661  29.620  1.00 35.09  ? 292 LEU A CD2 1 
ATOM   2019 N N   . GLY A 1 276 ? 52.527 -8.495  30.714  1.00 23.72  ? 293 GLY A N   1 
ATOM   2020 C CA  . GLY A 1 276 ? 53.680 -9.346  30.951  1.00 26.35  ? 293 GLY A CA  1 
ATOM   2021 C C   . GLY A 1 276 ? 53.532 -10.162 32.209  1.00 25.75  ? 293 GLY A C   1 
ATOM   2022 O O   . GLY A 1 276 ? 53.880 -11.342 32.241  1.00 29.35  ? 293 GLY A O   1 
ATOM   2023 N N   . ARG A 1 277 ? 53.010 -9.545  33.269  1.00 28.23  ? 294 ARG A N   1 
ATOM   2024 C CA  . ARG A 1 277 ? 52.819 -10.288 34.518  1.00 33.41  ? 294 ARG A CA  1 
ATOM   2025 C C   . ARG A 1 277 ? 51.740 -11.346 34.353  1.00 31.95  ? 294 ARG A C   1 
ATOM   2026 O O   . ARG A 1 277 ? 51.973 -12.531 34.603  1.00 36.03  ? 294 ARG A O   1 
ATOM   2027 C CB  . ARG A 1 277 ? 52.460 -9.316  35.646  1.00 29.90  ? 294 ARG A CB  1 
ATOM   2028 C CG  . ARG A 1 277 ? 52.258 -9.908  37.059  1.00 33.97  ? 294 ARG A CG  1 
ATOM   2029 C CD  . ARG A 1 277 ? 53.581 -10.161 37.719  1.00 35.58  ? 294 ARG A CD  1 
ATOM   2030 N NE  . ARG A 1 277 ? 53.498 -10.456 39.152  1.00 36.45  ? 294 ARG A NE  1 
ATOM   2031 C CZ  . ARG A 1 277 ? 53.706 -9.579  40.126  1.00 32.09  ? 294 ARG A CZ  1 
ATOM   2032 N NH1 . ARG A 1 277 ? 53.969 -8.306  39.874  1.00 36.56  ? 294 ARG A NH1 1 
ATOM   2033 N NH2 . ARG A 1 277 ? 53.693 -9.998  41.381  1.00 32.82  ? 294 ARG A NH2 1 
ATOM   2034 N N   . LYS A 1 278 ? 50.576 -10.941 33.856  1.00 30.17  ? 295 LYS A N   1 
ATOM   2035 C CA  . LYS A 1 278 ? 49.408 -11.812 33.885  1.00 35.29  ? 295 LYS A CA  1 
ATOM   2036 C C   . LYS A 1 278 ? 49.550 -12.972 32.906  1.00 40.05  ? 295 LYS A C   1 
ATOM   2037 O O   . LYS A 1 278 ? 49.186 -14.101 33.235  1.00 36.17  ? 295 LYS A O   1 
ATOM   2038 C CB  . LYS A 1 278 ? 48.147 -10.997 33.591  1.00 34.42  ? 295 LYS A CB  1 
ATOM   2039 C CG  . LYS A 1 278 ? 46.882 -11.835 33.413  1.00 40.79  ? 295 LYS A CG  1 
ATOM   2040 C CD  . LYS A 1 278 ? 45.670 -10.930 33.222  1.00 45.62  ? 295 LYS A CD  1 
ATOM   2041 C CE  . LYS A 1 278 ? 44.370 -11.695 33.020  1.00 46.60  ? 295 LYS A CE  1 
ATOM   2042 N NZ  . LYS A 1 278 ? 43.215 -10.773 32.825  1.00 37.67  ? 295 LYS A NZ  1 
ATOM   2043 N N   . TYR A 1 279 ? 50.050 -12.722 31.695  1.00 34.04  ? 296 TYR A N   1 
ATOM   2044 C CA  . TYR A 1 279 ? 50.057 -13.756 30.663  1.00 34.44  ? 296 TYR A CA  1 
ATOM   2045 C C   . TYR A 1 279 ? 51.425 -14.375 30.409  1.00 36.75  ? 296 TYR A C   1 
ATOM   2046 O O   . TYR A 1 279 ? 51.512 -15.339 29.644  1.00 36.73  ? 296 TYR A O   1 
ATOM   2047 C CB  . TYR A 1 279 ? 49.497 -13.201 29.342  1.00 35.80  ? 296 TYR A CB  1 
ATOM   2048 C CG  . TYR A 1 279 ? 48.017 -12.868 29.432  1.00 39.01  ? 296 TYR A CG  1 
ATOM   2049 C CD1 . TYR A 1 279 ? 47.085 -13.878 29.572  1.00 45.30  ? 296 TYR A CD1 1 
ATOM   2050 C CD2 . TYR A 1 279 ? 47.558 -11.554 29.398  1.00 37.43  ? 296 TYR A CD2 1 
ATOM   2051 C CE1 . TYR A 1 279 ? 45.752 -13.607 29.680  1.00 42.93  ? 296 TYR A CE1 1 
ATOM   2052 C CE2 . TYR A 1 279 ? 46.214 -11.271 29.508  1.00 42.03  ? 296 TYR A CE2 1 
ATOM   2053 C CZ  . TYR A 1 279 ? 45.311 -12.317 29.650  1.00 43.39  ? 296 TYR A CZ  1 
ATOM   2054 O OH  . TYR A 1 279 ? 43.955 -12.101 29.783  1.00 41.65  ? 296 TYR A OH  1 
ATOM   2055 N N   . HIS A 1 280 ? 52.484 -13.863 31.022  1.00 33.96  ? 297 HIS A N   1 
ATOM   2056 C CA  . HIS A 1 280 ? 53.816 -14.392 30.779  1.00 34.46  ? 297 HIS A CA  1 
ATOM   2057 C C   . HIS A 1 280 ? 54.626 -14.588 32.046  1.00 33.84  ? 297 HIS A C   1 
ATOM   2058 O O   . HIS A 1 280 ? 55.775 -15.029 31.953  1.00 32.72  ? 297 HIS A O   1 
ATOM   2059 C CB  . HIS A 1 280 ? 54.571 -13.462 29.813  1.00 34.96  ? 297 HIS A CB  1 
ATOM   2060 C CG  . HIS A 1 280 ? 53.830 -13.194 28.538  1.00 36.95  ? 297 HIS A CG  1 
ATOM   2061 N ND1 . HIS A 1 280 ? 53.994 -13.958 27.403  1.00 33.28  ? 297 HIS A ND1 1 
ATOM   2062 C CD2 . HIS A 1 280 ? 52.890 -12.269 28.231  1.00 34.33  ? 297 HIS A CD2 1 
ATOM   2063 C CE1 . HIS A 1 280 ? 53.215 -13.496 26.442  1.00 35.16  ? 297 HIS A CE1 1 
ATOM   2064 N NE2 . HIS A 1 280 ? 52.532 -12.475 26.919  1.00 37.97  ? 297 HIS A NE2 1 
ATOM   2065 N N   . GLY A 1 281 ? 54.089 -14.242 33.218  1.00 37.43  ? 298 GLY A N   1 
ATOM   2066 C CA  . GLY A 1 281 ? 54.826 -14.438 34.453  1.00 35.38  ? 298 GLY A CA  1 
ATOM   2067 C C   . GLY A 1 281 ? 56.055 -13.569 34.610  1.00 36.31  ? 298 GLY A C   1 
ATOM   2068 O O   . GLY A 1 281 ? 56.964 -13.944 35.338  1.00 42.46  ? 298 GLY A O   1 
ATOM   2069 N N   . LEU A 1 282 ? 56.122 -12.431 33.922  1.00 28.79  ? 299 LEU A N   1 
ATOM   2070 C CA  . LEU A 1 282 ? 57.268 -11.534 33.984  1.00 30.98  ? 299 LEU A CA  1 
ATOM   2071 C C   . LEU A 1 282 ? 57.087 -10.505 35.094  1.00 30.86  ? 299 LEU A C   1 
ATOM   2072 O O   . LEU A 1 282 ? 56.016 -9.901  35.208  1.00 32.26  ? 299 LEU A O   1 
ATOM   2073 C CB  . LEU A 1 282 ? 57.432 -10.832 32.632  1.00 32.77  ? 299 LEU A CB  1 
ATOM   2074 C CG  . LEU A 1 282 ? 57.504 -11.843 31.487  1.00 35.26  ? 299 LEU A CG  1 
ATOM   2075 C CD1 . LEU A 1 282 ? 57.398 -11.148 30.167  1.00 36.45  ? 299 LEU A CD1 1 
ATOM   2076 C CD2 . LEU A 1 282 ? 58.788 -12.625 31.572  1.00 36.85  ? 299 LEU A CD2 1 
ATOM   2077 N N   . ILE A 1 283 ? 58.134 -10.299 35.894  1.00 29.59  ? 300 ILE A N   1 
ATOM   2078 C CA  . ILE A 1 283 ? 58.083 -9.410  37.052  1.00 30.76  ? 300 ILE A CA  1 
ATOM   2079 C C   . ILE A 1 283 ? 59.257 -8.448  37.004  1.00 26.84  ? 300 ILE A C   1 
ATOM   2080 O O   . ILE A 1 283 ? 60.393 -8.902  36.874  1.00 26.57  ? 300 ILE A O   1 
ATOM   2081 C CB  . ILE A 1 283 ? 58.112 -10.205 38.377  1.00 36.25  ? 300 ILE A CB  1 
ATOM   2082 C CG1 . ILE A 1 283 ? 56.903 -11.134 38.440  1.00 38.75  ? 300 ILE A CG1 1 
ATOM   2083 C CG2 . ILE A 1 283 ? 58.169 -9.264  39.553  1.00 29.36  ? 300 ILE A CG2 1 
ATOM   2084 C CD1 . ILE A 1 283 ? 56.845 -11.975 39.673  1.00 45.48  ? 300 ILE A CD1 1 
ATOM   2085 N N   . PRO A 1 284 ? 59.057 -7.136  37.126  1.00 30.57  ? 301 PRO A N   1 
ATOM   2086 C CA  . PRO A 1 284 ? 60.212 -6.231  37.146  1.00 28.18  ? 301 PRO A CA  1 
ATOM   2087 C C   . PRO A 1 284 ? 61.112 -6.553  38.319  1.00 37.75  ? 301 PRO A C   1 
ATOM   2088 O O   . PRO A 1 284 ? 60.643 -6.749  39.439  1.00 38.08  ? 301 PRO A O   1 
ATOM   2089 C CB  . PRO A 1 284 ? 59.585 -4.848  37.289  1.00 30.01  ? 301 PRO A CB  1 
ATOM   2090 C CG  . PRO A 1 284 ? 58.178 -5.009  36.808  1.00 30.41  ? 301 PRO A CG  1 
ATOM   2091 C CD  . PRO A 1 284 ? 57.787 -6.401  37.219  1.00 28.24  ? 301 PRO A CD  1 
ATOM   2092 N N   . GLU A 1 285 ? 62.412 -6.511  38.088  1.00 36.12  ? 302 GLU A N   1 
ATOM   2093 C CA  . GLU A 1 285 ? 63.332 -6.563  39.208  1.00 48.93  ? 302 GLU A CA  1 
ATOM   2094 C C   . GLU A 1 285 ? 63.197 -5.199  39.898  1.00 48.11  ? 302 GLU A C   1 
ATOM   2095 O O   . GLU A 1 285 ? 63.075 -4.132  39.245  1.00 49.71  ? 302 GLU A O   1 
ATOM   2096 C CB  . GLU A 1 285 ? 64.759 -6.815  38.739  1.00 53.51  ? 302 GLU A CB  1 
ATOM   2097 C CG  . GLU A 1 285 ? 64.959 -8.180  38.099  1.00 56.05  ? 302 GLU A CG  1 
ATOM   2098 C CD  . GLU A 1 285 ? 66.320 -8.314  37.435  1.00 60.74  ? 302 GLU A CD  1 
ATOM   2099 O OE1 . GLU A 1 285 ? 67.222 -7.483  37.715  1.00 59.62  ? 302 GLU A OE1 1 
ATOM   2100 O OE2 . GLU A 1 285 ? 66.480 -9.260  36.634  1.00 58.52  ? 302 GLU A OE2 1 
ATOM   2101 O OXT . GLU A 1 285 ? 63.174 -5.140  41.109  1.00 46.53  ? 302 GLU A OXT 1 
ATOM   2102 N N   . HIS B 1 7   ? 16.682 -0.966  -11.111 1.00 86.75  ? 24  HIS B N   1 
ATOM   2103 C CA  . HIS B 1 7   ? 17.847 -0.033  -11.086 1.00 92.45  ? 24  HIS B CA  1 
ATOM   2104 C C   . HIS B 1 7   ? 19.180 -0.776  -10.991 1.00 88.66  ? 24  HIS B C   1 
ATOM   2105 O O   . HIS B 1 7   ? 19.575 -1.221  -9.917  1.00 92.93  ? 24  HIS B O   1 
ATOM   2106 C CB  . HIS B 1 7   ? 17.720 0.948   -9.916  1.00 76.48  ? 24  HIS B CB  1 
ATOM   2107 N N   . HIS B 1 8   ? 19.848 -0.920  -12.136 1.00 88.72  ? 25  HIS B N   1 
ATOM   2108 C CA  . HIS B 1 8   ? 21.235 -1.362  -12.196 1.00 80.75  ? 25  HIS B CA  1 
ATOM   2109 C C   . HIS B 1 8   ? 22.135 -0.143  -12.121 1.00 75.13  ? 25  HIS B C   1 
ATOM   2110 O O   . HIS B 1 8   ? 22.021 0.769   -12.948 1.00 77.00  ? 25  HIS B O   1 
ATOM   2111 C CB  . HIS B 1 8   ? 21.553 -2.109  -13.489 1.00 73.84  ? 25  HIS B CB  1 
ATOM   2112 C CG  . HIS B 1 8   ? 21.475 -3.595  -13.384 1.00 78.79  ? 25  HIS B CG  1 
ATOM   2113 N ND1 . HIS B 1 8   ? 22.401 -4.423  -13.985 1.00 64.36  ? 25  HIS B ND1 1 
ATOM   2114 C CD2 . HIS B 1 8   ? 20.591 -4.405  -12.757 1.00 85.55  ? 25  HIS B CD2 1 
ATOM   2115 C CE1 . HIS B 1 8   ? 22.082 -5.681  -13.743 1.00 67.88  ? 25  HIS B CE1 1 
ATOM   2116 N NE2 . HIS B 1 8   ? 20.991 -5.699  -12.996 1.00 86.30  ? 25  HIS B NE2 1 
ATOM   2117 N N   . VAL B 1 9   ? 23.030 -0.130  -11.149 1.00 57.37  ? 26  VAL B N   1 
ATOM   2118 C CA  . VAL B 1 9   ? 24.136 0.807   -11.150 1.00 52.92  ? 26  VAL B CA  1 
ATOM   2119 C C   . VAL B 1 9   ? 25.395 -0.006  -10.947 1.00 46.62  ? 26  VAL B C   1 
ATOM   2120 O O   . VAL B 1 9   ? 25.503 -0.745  -9.962  1.00 42.56  ? 26  VAL B O   1 
ATOM   2121 C CB  . VAL B 1 9   ? 24.007 1.875   -10.058 1.00 56.71  ? 26  VAL B CB  1 
ATOM   2122 C CG1 . VAL B 1 9   ? 25.135 2.882   -10.179 1.00 54.51  ? 26  VAL B CG1 1 
ATOM   2123 C CG2 . VAL B 1 9   ? 22.669 2.555   -10.164 1.00 60.28  ? 26  VAL B CG2 1 
ATOM   2124 N N   . VAL B 1 10  ? 26.342 0.132   -11.866 1.00 41.27  ? 27  VAL B N   1 
ATOM   2125 C CA  . VAL B 1 10  ? 27.604 -0.584  -11.805 1.00 35.96  ? 27  VAL B CA  1 
ATOM   2126 C C   . VAL B 1 10  ? 28.665 0.447   -11.493 1.00 34.84  ? 27  VAL B C   1 
ATOM   2127 O O   . VAL B 1 10  ? 29.019 1.262   -12.347 1.00 36.61  ? 27  VAL B O   1 
ATOM   2128 C CB  . VAL B 1 10  ? 27.923 -1.321  -13.110 1.00 36.69  ? 27  VAL B CB  1 
ATOM   2129 C CG1 . VAL B 1 10  ? 29.182 -2.168  -12.912 1.00 31.89  ? 27  VAL B CG1 1 
ATOM   2130 C CG2 . VAL B 1 10  ? 26.752 -2.172  -13.525 1.00 38.09  ? 27  VAL B CG2 1 
ATOM   2131 N N   . ARG B 1 11  ? 29.176 0.422   -10.284 1.00 31.56  ? 28  ARG B N   1 
ATOM   2132 C CA  . ARG B 1 11  ? 30.208 1.354   -9.894  1.00 29.32  ? 28  ARG B CA  1 
ATOM   2133 C C   . ARG B 1 11  ? 31.464 0.657   -9.397  1.00 29.60  ? 28  ARG B C   1 
ATOM   2134 O O   . ARG B 1 11  ? 32.477 1.327   -9.201  1.00 29.72  ? 28  ARG B O   1 
ATOM   2135 C CB  . ARG B 1 11  ? 29.691 2.310   -8.811  1.00 35.35  ? 28  ARG B CB  1 
ATOM   2136 C CG  . ARG B 1 11  ? 29.532 1.631   -7.477  1.00 42.04  ? 28  ARG B CG  1 
ATOM   2137 C CD  . ARG B 1 11  ? 28.862 2.524   -6.439  1.00 49.26  ? 28  ARG B CD  1 
ATOM   2138 N NE  . ARG B 1 11  ? 28.288 1.732   -5.356  1.00 53.60  ? 28  ARG B NE  1 
ATOM   2139 C CZ  . ARG B 1 11  ? 27.908 2.221   -4.182  1.00 61.90  ? 28  ARG B CZ  1 
ATOM   2140 N NH1 . ARG B 1 11  ? 28.021 3.511   -3.899  1.00 59.66  ? 28  ARG B NH1 1 
ATOM   2141 N NH2 . ARG B 1 11  ? 27.360 1.399   -3.286  1.00 60.61  ? 28  ARG B NH2 1 
ATOM   2142 N N   . LYS B 1 12  ? 31.449 -0.664  -9.252  1.00 32.17  ? 29  LYS B N   1 
ATOM   2143 C CA  . LYS B 1 12  ? 32.608 -1.426  -8.802  1.00 26.85  ? 29  LYS B CA  1 
ATOM   2144 C C   . LYS B 1 12  ? 33.182 -2.299  -9.917  1.00 25.19  ? 29  LYS B C   1 
ATOM   2145 O O   . LYS B 1 12  ? 32.434 -2.945  -10.648 1.00 24.82  ? 29  LYS B O   1 
ATOM   2146 C CB  . LYS B 1 12  ? 32.230 -2.346  -7.649  1.00 27.43  ? 29  LYS B CB  1 
ATOM   2147 C CG  . LYS B 1 12  ? 31.855 -1.628  -6.347  1.00 27.06  ? 29  LYS B CG  1 
ATOM   2148 C CD  . LYS B 1 12  ? 31.421 -2.641  -5.302  1.00 29.09  ? 29  LYS B CD  1 
ATOM   2149 C CE  . LYS B 1 12  ? 30.900 -1.936  -4.020  1.00 36.86  ? 29  LYS B CE  1 
ATOM   2150 N NZ  . LYS B 1 12  ? 31.979 -1.182  -3.332  1.00 36.46  ? 29  LYS B NZ  1 
ATOM   2151 N N   . ALA B 1 13  ? 34.507 -2.381  -9.995  1.00 26.54  ? 30  ALA B N   1 
ATOM   2152 C CA  . ALA B 1 13  ? 35.168 -3.275  -10.943 1.00 24.43  ? 30  ALA B CA  1 
ATOM   2153 C C   . ALA B 1 13  ? 36.306 -4.042  -10.275 1.00 22.65  ? 30  ALA B C   1 
ATOM   2154 O O   . ALA B 1 13  ? 37.075 -3.480  -9.486  1.00 29.14  ? 30  ALA B O   1 
ATOM   2155 C CB  . ALA B 1 13  ? 35.718 -2.508  -12.130 1.00 26.48  ? 30  ALA B CB  1 
ATOM   2156 N N   . VAL B 1 14  ? 36.422 -5.313  -10.636 1.00 23.95  ? 31  VAL B N   1 
ATOM   2157 C CA  . VAL B 1 14  ? 37.402 -6.241  -10.089 1.00 22.41  ? 31  VAL B CA  1 
ATOM   2158 C C   . VAL B 1 14  ? 38.462 -6.521  -11.150 1.00 25.27  ? 31  VAL B C   1 
ATOM   2159 O O   . VAL B 1 14  ? 38.132 -6.916  -12.277 1.00 24.27  ? 31  VAL B O   1 
ATOM   2160 C CB  . VAL B 1 14  ? 36.725 -7.557  -9.667  1.00 25.62  ? 31  VAL B CB  1 
ATOM   2161 C CG1 . VAL B 1 14  ? 37.782 -8.583  -9.279  1.00 24.59  ? 31  VAL B CG1 1 
ATOM   2162 C CG2 . VAL B 1 14  ? 35.743 -7.341  -8.510  1.00 27.53  ? 31  VAL B CG2 1 
ATOM   2163 N N   . PHE B 1 15  ? 39.731 -6.362  -10.777 1.00 21.87  ? 32  PHE B N   1 
ATOM   2164 C CA  . PHE B 1 15  ? 40.857 -6.629  -11.658 1.00 22.16  ? 32  PHE B CA  1 
ATOM   2165 C C   . PHE B 1 15  ? 41.717 -7.734  -11.082 1.00 23.94  ? 32  PHE B C   1 
ATOM   2166 O O   . PHE B 1 15  ? 42.437 -7.498  -10.098 1.00 25.58  ? 32  PHE B O   1 
ATOM   2167 C CB  . PHE B 1 15  ? 41.699 -5.374  -11.836 1.00 23.61  ? 32  PHE B CB  1 
ATOM   2168 C CG  . PHE B 1 15  ? 40.920 -4.196  -12.264 1.00 24.38  ? 32  PHE B CG  1 
ATOM   2169 C CD1 . PHE B 1 15  ? 40.246 -3.426  -11.341 1.00 22.08  ? 32  PHE B CD1 1 
ATOM   2170 C CD2 . PHE B 1 15  ? 40.852 -3.848  -13.596 1.00 27.13  ? 32  PHE B CD2 1 
ATOM   2171 C CE1 . PHE B 1 15  ? 39.517 -2.302  -11.749 1.00 27.06  ? 32  PHE B CE1 1 
ATOM   2172 C CE2 . PHE B 1 15  ? 40.132 -2.731  -14.008 1.00 22.75  ? 32  PHE B CE2 1 
ATOM   2173 C CZ  . PHE B 1 15  ? 39.465 -1.966  -13.085 1.00 25.66  ? 32  PHE B CZ  1 
ATOM   2174 N N   . PRO B 1 16  ? 41.694 -8.946  -11.623 1.00 26.14  ? 33  PRO B N   1 
ATOM   2175 C CA  . PRO B 1 16  ? 42.661 -9.952  -11.159 1.00 22.66  ? 33  PRO B CA  1 
ATOM   2176 C C   . PRO B 1 16  ? 44.050 -9.595  -11.663 1.00 27.34  ? 33  PRO B C   1 
ATOM   2177 O O   . PRO B 1 16  ? 44.279 -9.471  -12.875 1.00 22.48  ? 33  PRO B O   1 
ATOM   2178 C CB  . PRO B 1 16  ? 42.138 -11.263 -11.764 1.00 24.53  ? 33  PRO B CB  1 
ATOM   2179 C CG  . PRO B 1 16  ? 40.725 -10.958 -12.154 1.00 24.50  ? 33  PRO B CG  1 
ATOM   2180 C CD  . PRO B 1 16  ? 40.710 -9.526  -12.554 1.00 25.36  ? 33  PRO B CD  1 
ATOM   2181 N N   . VAL B 1 17  ? 44.964 -9.360  -10.729 1.00 22.92  ? 34  VAL B N   1 
ATOM   2182 C CA  . VAL B 1 17  ? 46.288 -8.856  -11.088 1.00 26.95  ? 34  VAL B CA  1 
ATOM   2183 C C   . VAL B 1 17  ? 47.352 -9.723  -10.448 1.00 27.23  ? 34  VAL B C   1 
ATOM   2184 O O   . VAL B 1 17  ? 48.372 -9.227  -9.959  1.00 31.40  ? 34  VAL B O   1 
ATOM   2185 C CB  . VAL B 1 17  ? 46.493 -7.384  -10.717 1.00 26.35  ? 34  VAL B CB  1 
ATOM   2186 C CG1 . VAL B 1 17  ? 45.725 -6.476  -11.681 1.00 25.11  ? 34  VAL B CG1 1 
ATOM   2187 C CG2 . VAL B 1 17  ? 46.068 -7.114  -9.293  1.00 25.88  ? 34  VAL B CG2 1 
ATOM   2188 N N   . ALA B 1 18  ? 47.089 -11.012 -10.373 1.00 27.47  ? 35  ALA B N   1 
ATOM   2189 C CA  . ALA B 1 18  ? 48.076 -11.950 -9.869  1.00 33.26  ? 35  ALA B CA  1 
ATOM   2190 C C   . ALA B 1 18  ? 48.645 -12.833 -10.978 1.00 37.03  ? 35  ALA B C   1 
ATOM   2191 O O   . ALA B 1 18  ? 49.131 -13.934 -10.707 1.00 30.95  ? 35  ALA B O   1 
ATOM   2192 C CB  . ALA B 1 18  ? 47.436 -12.769 -8.749  1.00 27.05  ? 35  ALA B CB  1 
ATOM   2193 N N   . GLY B 1 19  ? 48.577 -12.388 -12.246 1.00 36.14  ? 36  GLY B N   1 
ATOM   2194 C CA  . GLY B 1 19  ? 49.031 -13.243 -13.320 1.00 29.73  ? 36  GLY B CA  1 
ATOM   2195 C C   . GLY B 1 19  ? 50.482 -13.696 -13.211 1.00 33.00  ? 36  GLY B C   1 
ATOM   2196 O O   . GLY B 1 19  ? 51.402 -12.872 -13.081 1.00 30.07  ? 36  GLY B O   1 
ATOM   2197 N N   . MET B 1 20  ? 50.701 -15.014 -13.272 1.00 33.75  ? 37  MET B N   1 
ATOM   2198 C CA  . MET B 1 20  ? 52.062 -15.539 -13.211 1.00 36.56  ? 37  MET B CA  1 
ATOM   2199 C C   . MET B 1 20  ? 52.868 -15.169 -14.455 1.00 36.60  ? 37  MET B C   1 
ATOM   2200 O O   . MET B 1 20  ? 54.071 -14.898 -14.360 1.00 36.05  ? 37  MET B O   1 
ATOM   2201 C CB  . MET B 1 20  ? 52.014 -17.044 -13.038 1.00 38.51  ? 37  MET B CB  1 
ATOM   2202 C CG  . MET B 1 20  ? 51.426 -17.469 -11.694 1.00 43.29  ? 37  MET B CG  1 
ATOM   2203 S SD  . MET B 1 20  ? 51.698 -19.225 -11.384 1.00 70.58  ? 37  MET B SD  1 
ATOM   2204 C CE  . MET B 1 20  ? 53.487 -19.244 -11.221 1.00 64.95  ? 37  MET B CE  1 
ATOM   2205 N N   . GLY B 1 21  ? 52.225 -15.125 -15.622 1.00 38.47  ? 38  GLY B N   1 
ATOM   2206 C CA  . GLY B 1 21  ? 52.920 -14.730 -16.839 1.00 34.63  ? 38  GLY B CA  1 
ATOM   2207 C C   . GLY B 1 21  ? 54.169 -15.566 -17.031 1.00 35.98  ? 38  GLY B C   1 
ATOM   2208 O O   . GLY B 1 21  ? 55.256 -15.018 -17.214 1.00 37.43  ? 38  GLY B O   1 
ATOM   2209 N N   . THR B 1 22  ? 54.043 -16.892 -16.912 1.00 36.75  ? 39  THR B N   1 
ATOM   2210 C CA  . THR B 1 22  ? 55.214 -17.748 -17.059 1.00 38.54  ? 39  THR B CA  1 
ATOM   2211 C C   . THR B 1 22  ? 55.835 -17.569 -18.429 1.00 42.01  ? 39  THR B C   1 
ATOM   2212 O O   . THR B 1 22  ? 57.060 -17.653 -18.575 1.00 39.30  ? 39  THR B O   1 
ATOM   2213 C CB  . THR B 1 22  ? 54.844 -19.216 -16.854 1.00 45.00  ? 39  THR B CB  1 
ATOM   2214 O OG1 . THR B 1 22  ? 53.921 -19.614 -17.873 1.00 51.24  ? 39  THR B OG1 1 
ATOM   2215 C CG2 . THR B 1 22  ? 54.213 -19.418 -15.510 1.00 41.88  ? 39  THR B CG2 1 
ATOM   2216 N N   . ARG B 1 23  ? 55.003 -17.331 -19.445 1.00 39.60  ? 40  ARG B N   1 
ATOM   2217 C CA  . ARG B 1 23  ? 55.524 -17.105 -20.787 1.00 45.45  ? 40  ARG B CA  1 
ATOM   2218 C C   . ARG B 1 23  ? 56.377 -15.860 -20.854 1.00 37.07  ? 40  ARG B C   1 
ATOM   2219 O O   . ARG B 1 23  ? 57.059 -15.648 -21.862 1.00 43.58  ? 40  ARG B O   1 
ATOM   2220 C CB  . ARG B 1 23  ? 54.380 -16.996 -21.794 1.00 48.61  ? 40  ARG B CB  1 
ATOM   2221 C CG  . ARG B 1 23  ? 53.648 -18.299 -21.974 1.00 54.16  ? 40  ARG B CG  1 
ATOM   2222 C CD  . ARG B 1 23  ? 52.703 -18.252 -23.132 1.00 63.93  ? 40  ARG B CD  1 
ATOM   2223 N NE  . ARG B 1 23  ? 51.365 -17.802 -22.770 1.00 74.11  ? 40  ARG B NE  1 
ATOM   2224 C CZ  . ARG B 1 23  ? 50.265 -18.162 -23.422 1.00 78.90  ? 40  ARG B CZ  1 
ATOM   2225 N NH1 . ARG B 1 23  ? 50.287 -19.114 -24.347 1.00 63.11  ? 40  ARG B NH1 1 
ATOM   2226 N NH2 . ARG B 1 23  ? 49.114 -17.552 -23.142 1.00 79.77  ? 40  ARG B NH2 1 
ATOM   2227 N N   . PHE B 1 24  ? 56.261 -14.979 -19.854 1.00 34.76  ? 41  PHE B N   1 
ATOM   2228 C CA  . PHE B 1 24  ? 57.000 -13.723 -19.811 1.00 31.70  ? 41  PHE B CA  1 
ATOM   2229 C C   . PHE B 1 24  ? 58.070 -13.707 -18.725 1.00 34.83  ? 41  PHE B C   1 
ATOM   2230 O O   . PHE B 1 24  ? 58.613 -12.637 -18.420 1.00 29.22  ? 41  PHE B O   1 
ATOM   2231 C CB  . PHE B 1 24  ? 56.015 -12.562 -19.636 1.00 28.80  ? 41  PHE B CB  1 
ATOM   2232 C CG  . PHE B 1 24  ? 55.084 -12.416 -20.804 1.00 29.43  ? 41  PHE B CG  1 
ATOM   2233 C CD1 . PHE B 1 24  ? 53.988 -13.248 -20.939 1.00 33.09  ? 41  PHE B CD1 1 
ATOM   2234 C CD2 . PHE B 1 24  ? 55.330 -11.479 -21.799 1.00 32.95  ? 41  PHE B CD2 1 
ATOM   2235 C CE1 . PHE B 1 24  ? 53.127 -13.127 -22.043 1.00 31.14  ? 41  PHE B CE1 1 
ATOM   2236 C CE2 . PHE B 1 24  ? 54.469 -11.351 -22.870 1.00 33.37  ? 41  PHE B CE2 1 
ATOM   2237 C CZ  . PHE B 1 24  ? 53.358 -12.181 -22.979 1.00 31.48  ? 41  PHE B CZ  1 
ATOM   2238 N N   . LEU B 1 25  ? 58.358 -14.848 -18.106 1.00 29.79  ? 42  LEU B N   1 
ATOM   2239 C CA  . LEU B 1 25  ? 59.527 -14.929 -17.245 1.00 28.40  ? 42  LEU B CA  1 
ATOM   2240 C C   . LEU B 1 25  ? 60.781 -14.713 -18.087 1.00 33.69  ? 42  LEU B C   1 
ATOM   2241 O O   . LEU B 1 25  ? 60.838 -15.182 -19.231 1.00 33.61  ? 42  LEU B O   1 
ATOM   2242 C CB  . LEU B 1 25  ? 59.610 -16.272 -16.530 1.00 32.01  ? 42  LEU B CB  1 
ATOM   2243 C CG  . LEU B 1 25  ? 58.677 -16.409 -15.321 1.00 33.35  ? 42  LEU B CG  1 
ATOM   2244 C CD1 . LEU B 1 25  ? 58.572 -17.835 -14.833 1.00 37.36  ? 42  LEU B CD1 1 
ATOM   2245 C CD2 . LEU B 1 25  ? 59.166 -15.533 -14.222 1.00 28.03  ? 42  LEU B CD2 1 
ATOM   2246 N N   . PRO B 1 26  ? 61.821 -14.050 -17.549 1.00 27.98  ? 43  PRO B N   1 
ATOM   2247 C CA  . PRO B 1 26  ? 61.988 -13.556 -16.170 1.00 33.00  ? 43  PRO B CA  1 
ATOM   2248 C C   . PRO B 1 26  ? 61.386 -12.200 -15.834 1.00 27.20  ? 43  PRO B C   1 
ATOM   2249 O O   . PRO B 1 26  ? 61.468 -11.757 -14.682 1.00 24.74  ? 43  PRO B O   1 
ATOM   2250 C CB  . PRO B 1 26  ? 63.525 -13.486 -16.028 1.00 28.47  ? 43  PRO B CB  1 
ATOM   2251 C CG  . PRO B 1 26  ? 63.980 -13.167 -17.414 1.00 30.51  ? 43  PRO B CG  1 
ATOM   2252 C CD  . PRO B 1 26  ? 63.081 -13.979 -18.300 1.00 32.47  ? 43  PRO B CD  1 
ATOM   2253 N N   . ALA B 1 27  ? 60.794 -11.508 -16.804 1.00 28.18  ? 44  ALA B N   1 
ATOM   2254 C CA  . ALA B 1 27  ? 60.309 -10.163 -16.543 1.00 28.00  ? 44  ALA B CA  1 
ATOM   2255 C C   . ALA B 1 27  ? 59.250 -10.153 -15.457 1.00 24.58  ? 44  ALA B C   1 
ATOM   2256 O O   . ALA B 1 27  ? 59.108 -9.158  -14.735 1.00 28.15  ? 44  ALA B O   1 
ATOM   2257 C CB  . ALA B 1 27  ? 59.731 -9.553  -17.819 1.00 31.78  ? 44  ALA B CB  1 
ATOM   2258 N N   . THR B 1 28  ? 58.488 -11.225 -15.342 1.00 26.13  ? 45  THR B N   1 
ATOM   2259 C CA  . THR B 1 28  ? 57.454 -11.328 -14.321 1.00 29.44  ? 45  THR B CA  1 
ATOM   2260 C C   . THR B 1 28  ? 57.974 -11.954 -13.027 1.00 28.98  ? 45  THR B C   1 
ATOM   2261 O O   . THR B 1 28  ? 57.172 -12.344 -12.176 1.00 25.95  ? 45  THR B O   1 
ATOM   2262 C CB  . THR B 1 28  ? 56.279 -12.149 -14.854 1.00 29.05  ? 45  THR B CB  1 
ATOM   2263 O OG1 . THR B 1 28  ? 56.781 -13.369 -15.394 1.00 24.41  ? 45  THR B OG1 1 
ATOM   2264 C CG2 . THR B 1 28  ? 55.502 -11.402 -15.956 1.00 29.15  ? 45  THR B CG2 1 
ATOM   2265 N N   . LYS B 1 29  ? 59.295 -12.073 -12.848 1.00 23.76  ? 46  LYS B N   1 
ATOM   2266 C CA  . LYS B 1 29  ? 59.778 -12.591 -11.573 1.00 30.64  ? 46  LYS B CA  1 
ATOM   2267 C C   . LYS B 1 29  ? 59.314 -11.718 -10.409 1.00 30.71  ? 46  LYS B C   1 
ATOM   2268 O O   . LYS B 1 29  ? 58.893 -12.231 -9.376  1.00 30.62  ? 46  LYS B O   1 
ATOM   2269 C CB  . LYS B 1 29  ? 61.302 -12.674 -11.538 1.00 27.95  ? 46  LYS B CB  1 
ATOM   2270 C CG  . LYS B 1 29  ? 61.802 -13.207 -10.201 1.00 29.20  ? 46  LYS B CG  1 
ATOM   2271 C CD  . LYS B 1 29  ? 63.130 -13.812 -10.340 1.00 40.00  ? 46  LYS B CD  1 
ATOM   2272 C CE  . LYS B 1 29  ? 63.710 -14.358 -9.047  1.00 40.10  ? 46  LYS B CE  1 
ATOM   2273 N NZ  . LYS B 1 29  ? 63.747 -13.415 -8.013  1.00 33.68  ? 46  LYS B NZ  1 
ATOM   2274 N N   . ALA B 1 30  ? 59.401 -10.398 -10.561 1.00 31.49  ? 47  ALA B N   1 
ATOM   2275 C CA  . ALA B 1 30  ? 59.126 -9.457  -9.485  1.00 32.79  ? 47  ALA B CA  1 
ATOM   2276 C C   . ALA B 1 30  ? 57.925 -8.563  -9.748  1.00 30.23  ? 47  ALA B C   1 
ATOM   2277 O O   . ALA B 1 30  ? 57.702 -7.616  -8.987  1.00 30.10  ? 47  ALA B O   1 
ATOM   2278 C CB  . ALA B 1 30  ? 60.344 -8.558  -9.233  1.00 35.49  ? 47  ALA B CB  1 
ATOM   2279 N N   . MET B 1 31  ? 57.191 -8.772  -10.827 1.00 28.46  ? 48  MET B N   1 
ATOM   2280 C CA  . MET B 1 31  ? 55.940 -8.052  -11.015 1.00 25.83  ? 48  MET B CA  1 
ATOM   2281 C C   . MET B 1 31  ? 54.960 -9.012  -11.666 1.00 25.37  ? 48  MET B C   1 
ATOM   2282 O O   . MET B 1 31  ? 55.374 -9.932  -12.389 1.00 27.07  ? 48  MET B O   1 
ATOM   2283 C CB  . MET B 1 31  ? 56.131 -6.783  -11.856 1.00 29.96  ? 48  MET B CB  1 
ATOM   2284 C CG  . MET B 1 31  ? 56.660 -7.072  -13.248 1.00 31.14  ? 48  MET B CG  1 
ATOM   2285 S SD  . MET B 1 31  ? 57.323 -5.608  -14.023 1.00 34.54  ? 48  MET B SD  1 
ATOM   2286 C CE  . MET B 1 31  ? 58.793 -5.307  -13.043 1.00 46.30  ? 48  MET B CE  1 
ATOM   2287 N N   . PRO B 1 32  ? 53.669 -8.863  -11.393 1.00 23.88  ? 49  PRO B N   1 
ATOM   2288 C CA  . PRO B 1 32  ? 52.684 -9.691  -12.081 1.00 25.53  ? 49  PRO B CA  1 
ATOM   2289 C C   . PRO B 1 32  ? 52.577 -9.281  -13.546 1.00 26.78  ? 49  PRO B C   1 
ATOM   2290 O O   . PRO B 1 32  ? 52.975 -8.188  -13.959 1.00 21.75  ? 49  PRO B O   1 
ATOM   2291 C CB  . PRO B 1 32  ? 51.386 -9.424  -11.313 1.00 29.43  ? 49  PRO B CB  1 
ATOM   2292 C CG  . PRO B 1 32  ? 51.556 -8.068  -10.759 1.00 26.11  ? 49  PRO B CG  1 
ATOM   2293 C CD  . PRO B 1 32  ? 53.021 -7.902  -10.473 1.00 26.70  ? 49  PRO B CD  1 
ATOM   2294 N N   . LYS B 1 33  ? 52.035 -10.210 -14.336 1.00 25.10  ? 50  LYS B N   1 
ATOM   2295 C CA  . LYS B 1 33  ? 51.950 -10.024 -15.781 1.00 28.21  ? 50  LYS B CA  1 
ATOM   2296 C C   . LYS B 1 33  ? 51.259 -8.712  -16.123 1.00 25.48  ? 50  LYS B C   1 
ATOM   2297 O O   . LYS B 1 33  ? 51.697 -7.976  -17.018 1.00 28.64  ? 50  LYS B O   1 
ATOM   2298 C CB  . LYS B 1 33  ? 51.204 -11.221 -16.372 1.00 34.06  ? 50  LYS B CB  1 
ATOM   2299 C CG  . LYS B 1 33  ? 50.849 -11.112 -17.832 1.00 29.48  ? 50  LYS B CG  1 
ATOM   2300 C CD  . LYS B 1 33  ? 52.048 -10.791 -18.660 1.00 30.52  ? 50  LYS B CD  1 
ATOM   2301 C CE  . LYS B 1 33  ? 51.796 -11.060 -20.151 1.00 39.06  ? 50  LYS B CE  1 
ATOM   2302 N NZ  . LYS B 1 33  ? 50.456 -10.762 -20.636 1.00 33.81  ? 50  LYS B NZ  1 
ATOM   2303 N N   . GLU B 1 34  ? 50.214 -8.370  -15.372 1.00 26.07  ? 51  GLU B N   1 
ATOM   2304 C CA  . GLU B 1 34  ? 49.420 -7.184  -15.675 1.00 27.23  ? 51  GLU B CA  1 
ATOM   2305 C C   . GLU B 1 34  ? 50.170 -5.880  -15.420 1.00 21.77  ? 51  GLU B C   1 
ATOM   2306 O O   . GLU B 1 34  ? 49.684 -4.815  -15.822 1.00 26.70  ? 51  GLU B O   1 
ATOM   2307 C CB  . GLU B 1 34  ? 48.116 -7.224  -14.881 1.00 27.27  ? 51  GLU B CB  1 
ATOM   2308 C CG  . GLU B 1 34  ? 47.104 -8.348  -15.278 1.00 31.39  ? 51  GLU B CG  1 
ATOM   2309 C CD  . GLU B 1 34  ? 47.469 -9.755  -14.787 1.00 35.11  ? 51  GLU B CD  1 
ATOM   2310 O OE1 . GLU B 1 34  ? 48.342 -9.900  -13.892 1.00 32.25  ? 51  GLU B OE1 1 
ATOM   2311 O OE2 . GLU B 1 34  ? 46.856 -10.729 -15.276 1.00 33.50  ? 51  GLU B OE2 1 
ATOM   2312 N N   . MET B 1 35  ? 51.350 -5.926  -14.817 1.00 23.91  ? 52  MET B N   1 
ATOM   2313 C CA  . MET B 1 35  ? 52.180 -4.729  -14.705 1.00 26.07  ? 52  MET B CA  1 
ATOM   2314 C C   . MET B 1 35  ? 53.194 -4.578  -15.834 1.00 26.32  ? 52  MET B C   1 
ATOM   2315 O O   . MET B 1 35  ? 53.938 -3.598  -15.849 1.00 23.75  ? 52  MET B O   1 
ATOM   2316 C CB  . MET B 1 35  ? 52.936 -4.710  -13.352 1.00 24.85  ? 52  MET B CB  1 
ATOM   2317 C CG  . MET B 1 35  ? 52.111 -4.288  -12.175 1.00 24.77  ? 52  MET B CG  1 
ATOM   2318 S SD  . MET B 1 35  ? 51.479 -2.613  -12.354 1.00 26.01  ? 52  MET B SD  1 
ATOM   2319 C CE  . MET B 1 35  ? 52.971 -1.665  -12.425 1.00 20.65  ? 52  MET B CE  1 
ATOM   2320 N N   . LEU B 1 36  ? 53.294 -5.513  -16.747 1.00 25.49  ? 53  LEU B N   1 
ATOM   2321 C CA  . LEU B 1 36  ? 54.167 -5.257  -17.884 1.00 26.70  ? 53  LEU B CA  1 
ATOM   2322 C C   . LEU B 1 36  ? 53.619 -4.115  -18.728 1.00 23.19  ? 53  LEU B C   1 
ATOM   2323 O O   . LEU B 1 36  ? 52.405 -4.037  -18.963 1.00 23.78  ? 53  LEU B O   1 
ATOM   2324 C CB  . LEU B 1 36  ? 54.332 -6.486  -18.765 1.00 28.03  ? 53  LEU B CB  1 
ATOM   2325 C CG  . LEU B 1 36  ? 54.959 -7.681  -18.059 1.00 30.45  ? 53  LEU B CG  1 
ATOM   2326 C CD1 . LEU B 1 36  ? 55.244 -8.740  -19.056 1.00 32.84  ? 53  LEU B CD1 1 
ATOM   2327 C CD2 . LEU B 1 36  ? 56.205 -7.290  -17.287 1.00 32.49  ? 53  LEU B CD2 1 
ATOM   2328 N N   . PRO B 1 37  ? 54.479 -3.223  -19.198 1.00 23.11  ? 54  PRO B N   1 
ATOM   2329 C CA  . PRO B 1 37  ? 54.012 -2.109  -20.014 1.00 27.86  ? 54  PRO B CA  1 
ATOM   2330 C C   . PRO B 1 37  ? 53.859 -2.438  -21.487 1.00 31.06  ? 54  PRO B C   1 
ATOM   2331 O O   . PRO B 1 37  ? 54.523 -3.319  -22.059 1.00 26.65  ? 54  PRO B O   1 
ATOM   2332 C CB  . PRO B 1 37  ? 55.104 -1.054  -19.816 1.00 26.70  ? 54  PRO B CB  1 
ATOM   2333 C CG  . PRO B 1 37  ? 56.334 -1.852  -19.642 1.00 26.62  ? 54  PRO B CG  1 
ATOM   2334 C CD  . PRO B 1 37  ? 55.903 -3.072  -18.843 1.00 25.98  ? 54  PRO B CD  1 
ATOM   2335 N N   . VAL B 1 38  ? 52.937 -1.699  -22.092 1.00 24.70  ? 55  VAL B N   1 
ATOM   2336 C CA  . VAL B 1 38  ? 52.838 -1.573  -23.536 1.00 28.48  ? 55  VAL B CA  1 
ATOM   2337 C C   . VAL B 1 38  ? 53.267 -0.142  -23.818 1.00 33.29  ? 55  VAL B C   1 
ATOM   2338 O O   . VAL B 1 38  ? 52.550 0.802   -23.466 1.00 29.19  ? 55  VAL B O   1 
ATOM   2339 C CB  . VAL B 1 38  ? 51.428 -1.867  -24.047 1.00 24.12  ? 55  VAL B CB  1 
ATOM   2340 C CG1 . VAL B 1 38  ? 51.348 -1.670  -25.590 1.00 31.37  ? 55  VAL B CG1 1 
ATOM   2341 C CG2 . VAL B 1 38  ? 51.052 -3.305  -23.708 1.00 29.88  ? 55  VAL B CG2 1 
ATOM   2342 N N   . VAL B 1 39  ? 54.483 0.003   -24.352 1.00 30.87  ? 56  VAL B N   1 
ATOM   2343 C CA  . VAL B 1 39  ? 55.202 1.261   -24.534 1.00 31.48  ? 56  VAL B CA  1 
ATOM   2344 C C   . VAL B 1 39  ? 55.561 1.876   -23.191 1.00 33.20  ? 56  VAL B C   1 
ATOM   2345 O O   . VAL B 1 39  ? 56.634 1.600   -22.645 1.00 38.54  ? 56  VAL B O   1 
ATOM   2346 C CB  . VAL B 1 39  ? 54.425 2.259   -25.418 1.00 34.35  ? 56  VAL B CB  1 
ATOM   2347 C CG1 . VAL B 1 39  ? 55.228 3.563   -25.585 1.00 36.87  ? 56  VAL B CG1 1 
ATOM   2348 C CG2 . VAL B 1 39  ? 54.215 1.677   -26.797 1.00 32.24  ? 56  VAL B CG2 1 
ATOM   2349 N N   . ASP B 1 40  ? 54.697 2.738   -22.662 1.00 29.91  ? 57  ASP B N   1 
ATOM   2350 C CA  . ASP B 1 40  ? 54.994 3.470   -21.432 1.00 31.87  ? 57  ASP B CA  1 
ATOM   2351 C C   . ASP B 1 40  ? 53.932 3.264   -20.352 1.00 29.01  ? 57  ASP B C   1 
ATOM   2352 O O   . ASP B 1 40  ? 53.837 4.071   -19.420 1.00 27.33  ? 57  ASP B O   1 
ATOM   2353 C CB  . ASP B 1 40  ? 55.131 4.965   -21.732 1.00 32.91  ? 57  ASP B CB  1 
ATOM   2354 C CG  . ASP B 1 40  ? 53.844 5.573   -22.282 1.00 35.78  ? 57  ASP B CG  1 
ATOM   2355 O OD1 . ASP B 1 40  ? 52.830 4.836   -22.450 1.00 36.07  ? 57  ASP B OD1 1 
ATOM   2356 O OD2 . ASP B 1 40  ? 53.847 6.795   -22.542 1.00 43.76  ? 57  ASP B OD2 1 
ATOM   2357 N N   . LYS B 1 41  ? 53.115 2.214   -20.458 1.00 28.59  ? 58  LYS B N   1 
ATOM   2358 C CA  . LYS B 1 41  ? 51.928 2.083   -19.598 1.00 29.24  ? 58  LYS B CA  1 
ATOM   2359 C C   . LYS B 1 41  ? 51.642 0.627   -19.248 1.00 26.05  ? 58  LYS B C   1 
ATOM   2360 O O   . LYS B 1 41  ? 51.529 -0.201  -20.162 1.00 26.67  ? 58  LYS B O   1 
ATOM   2361 C CB  . LYS B 1 41  ? 50.721 2.701   -20.299 1.00 27.18  ? 58  LYS B CB  1 
ATOM   2362 C CG  . LYS B 1 41  ? 49.475 2.732   -19.450 1.00 29.05  ? 58  LYS B CG  1 
ATOM   2363 C CD  . LYS B 1 41  ? 48.303 3.417   -20.124 1.00 28.73  ? 58  LYS B CD  1 
ATOM   2364 C CE  . LYS B 1 41  ? 48.543 4.911   -20.263 1.00 32.52  ? 58  LYS B CE  1 
ATOM   2365 N NZ  . LYS B 1 41  ? 47.422 5.575   -21.015 1.00 33.71  ? 58  LYS B NZ  1 
ATOM   2366 N N   . PRO B 1 42  ? 51.505 0.286   -17.964 1.00 25.76  ? 59  PRO B N   1 
ATOM   2367 C CA  . PRO B 1 42  ? 51.209 -1.109  -17.599 1.00 21.24  ? 59  PRO B CA  1 
ATOM   2368 C C   . PRO B 1 42  ? 49.877 -1.534  -18.184 1.00 23.62  ? 59  PRO B C   1 
ATOM   2369 O O   . PRO B 1 42  ? 48.939 -0.741  -18.264 1.00 22.28  ? 59  PRO B O   1 
ATOM   2370 C CB  . PRO B 1 42  ? 51.159 -1.087  -16.052 1.00 26.24  ? 59  PRO B CB  1 
ATOM   2371 C CG  . PRO B 1 42  ? 51.807 0.147   -15.649 1.00 25.67  ? 59  PRO B CG  1 
ATOM   2372 C CD  . PRO B 1 42  ? 51.636 1.147   -16.777 1.00 27.74  ? 59  PRO B CD  1 
ATOM   2373 N N   . LEU B 1 43  ? 49.801 -2.799  -18.602 1.00 25.33  ? 60  LEU B N   1 
ATOM   2374 C CA  . LEU B 1 43  ? 48.528 -3.352  -19.054 1.00 21.45  ? 60  LEU B CA  1 
ATOM   2375 C C   . LEU B 1 43  ? 47.375 -2.968  -18.144 1.00 20.97  ? 60  LEU B C   1 
ATOM   2376 O O   . LEU B 1 43  ? 46.331 -2.515  -18.620 1.00 24.90  ? 60  LEU B O   1 
ATOM   2377 C CB  . LEU B 1 43  ? 48.610 -4.872  -19.151 1.00 26.35  ? 60  LEU B CB  1 
ATOM   2378 C CG  . LEU B 1 43  ? 49.418 -5.434  -20.319 1.00 29.92  ? 60  LEU B CG  1 
ATOM   2379 C CD1 . LEU B 1 43  ? 49.737 -6.908  -20.042 1.00 29.58  ? 60  LEU B CD1 1 
ATOM   2380 C CD2 . LEU B 1 43  ? 48.671 -5.260  -21.610 1.00 29.35  ? 60  LEU B CD2 1 
ATOM   2381 N N   . ILE B 1 44  ? 47.556 -3.120  -16.818 1.00 23.22  ? 61  ILE B N   1 
ATOM   2382 C CA  . ILE B 1 44  ? 46.458 -2.879  -15.885 1.00 22.87  ? 61  ILE B CA  1 
ATOM   2383 C C   . ILE B 1 44  ? 45.977 -1.444  -15.970 1.00 22.99  ? 61  ILE B C   1 
ATOM   2384 O O   . ILE B 1 44  ? 44.778 -1.158  -15.811 1.00 22.75  ? 61  ILE B O   1 
ATOM   2385 C CB  . ILE B 1 44  ? 46.886 -3.276  -14.438 1.00 22.57  ? 61  ILE B CB  1 
ATOM   2386 C CG1 . ILE B 1 44  ? 45.732 -3.078  -13.443 1.00 19.62  ? 61  ILE B CG1 1 
ATOM   2387 C CG2 . ILE B 1 44  ? 48.109 -2.482  -13.980 1.00 21.11  ? 61  ILE B CG2 1 
ATOM   2388 C CD1 . ILE B 1 44  ? 44.479 -3.833  -13.772 1.00 24.14  ? 61  ILE B CD1 1 
ATOM   2389 N N   . GLN B 1 45  ? 46.876 -0.508  -16.210 1.00 23.72  ? 62  GLN B N   1 
ATOM   2390 C CA  . GLN B 1 45  ? 46.419 0.875   -16.280 1.00 27.08  ? 62  GLN B CA  1 
ATOM   2391 C C   . GLN B 1 45  ? 45.523 1.138   -17.506 1.00 26.48  ? 62  GLN B C   1 
ATOM   2392 O O   . GLN B 1 45  ? 44.592 1.959   -17.413 1.00 25.35  ? 62  GLN B O   1 
ATOM   2393 C CB  . GLN B 1 45  ? 47.608 1.831   -16.245 1.00 27.48  ? 62  GLN B CB  1 
ATOM   2394 C CG  . GLN B 1 45  ? 47.154 3.282   -16.188 1.00 28.69  ? 62  GLN B CG  1 
ATOM   2395 C CD  . GLN B 1 45  ? 48.281 4.240   -15.969 1.00 32.29  ? 62  GLN B CD  1 
ATOM   2396 O OE1 . GLN B 1 45  ? 49.337 3.877   -15.414 1.00 27.94  ? 62  GLN B OE1 1 
ATOM   2397 N NE2 . GLN B 1 45  ? 48.093 5.483   -16.443 1.00 29.09  ? 62  GLN B NE2 1 
ATOM   2398 N N   . TYR B 1 46  ? 45.751 0.466   -18.656 1.00 23.66  ? 63  TYR B N   1 
ATOM   2399 C CA  . TYR B 1 46  ? 44.791 0.604   -19.747 1.00 25.45  ? 63  TYR B CA  1 
ATOM   2400 C C   . TYR B 1 46  ? 43.406 0.154   -19.295 1.00 24.78  ? 63  TYR B C   1 
ATOM   2401 O O   . TYR B 1 46  ? 42.385 0.794   -19.602 1.00 21.11  ? 63  TYR B O   1 
ATOM   2402 C CB  . TYR B 1 46  ? 45.187 -0.234  -20.988 1.00 25.44  ? 63  TYR B CB  1 
ATOM   2403 C CG  . TYR B 1 46  ? 46.393 0.255   -21.741 1.00 26.23  ? 63  TYR B CG  1 
ATOM   2404 C CD1 . TYR B 1 46  ? 47.654 -0.196  -21.414 1.00 24.05  ? 63  TYR B CD1 1 
ATOM   2405 C CD2 . TYR B 1 46  ? 46.267 1.150   -22.815 1.00 27.95  ? 63  TYR B CD2 1 
ATOM   2406 C CE1 . TYR B 1 46  ? 48.768 0.259   -22.097 1.00 26.37  ? 63  TYR B CE1 1 
ATOM   2407 C CE2 . TYR B 1 46  ? 47.382 1.592   -23.502 1.00 29.19  ? 63  TYR B CE2 1 
ATOM   2408 C CZ  . TYR B 1 46  ? 48.626 1.121   -23.138 1.00 28.41  ? 63  TYR B CZ  1 
ATOM   2409 O OH  . TYR B 1 46  ? 49.762 1.537   -23.789 1.00 30.84  ? 63  TYR B OH  1 
ATOM   2410 N N   . ALA B 1 47  ? 43.350 -0.973  -18.606 1.00 20.55  ? 64  ALA B N   1 
ATOM   2411 C CA  . ALA B 1 47  ? 42.058 -1.485  -18.181 1.00 22.27  ? 64  ALA B CA  1 
ATOM   2412 C C   . ALA B 1 47  ? 41.428 -0.596  -17.106 1.00 22.42  ? 64  ALA B C   1 
ATOM   2413 O O   . ALA B 1 47  ? 40.215 -0.356  -17.112 1.00 23.11  ? 64  ALA B O   1 
ATOM   2414 C CB  . ALA B 1 47  ? 42.234 -2.920  -17.703 1.00 20.88  ? 64  ALA B CB  1 
ATOM   2415 N N   . VAL B 1 48  ? 42.220 -0.082  -16.181 1.00 25.43  ? 65  VAL B N   1 
ATOM   2416 C CA  . VAL B 1 48  ? 41.646 0.826   -15.192 1.00 21.97  ? 65  VAL B CA  1 
ATOM   2417 C C   . VAL B 1 48  ? 41.116 2.080   -15.882 1.00 25.28  ? 65  VAL B C   1 
ATOM   2418 O O   . VAL B 1 48  ? 40.015 2.562   -15.579 1.00 22.37  ? 65  VAL B O   1 
ATOM   2419 C CB  . VAL B 1 48  ? 42.689 1.157   -14.111 1.00 25.72  ? 65  VAL B CB  1 
ATOM   2420 C CG1 . VAL B 1 48  ? 42.240 2.334   -13.253 1.00 28.60  ? 65  VAL B CG1 1 
ATOM   2421 C CG2 . VAL B 1 48  ? 42.944 -0.078  -13.233 1.00 29.07  ? 65  VAL B CG2 1 
ATOM   2422 N N   . GLU B 1 49  ? 41.866 2.604   -16.855 1.00 25.25  ? 66  GLU B N   1 
ATOM   2423 C CA  . GLU B 1 49  ? 41.409 3.816   -17.543 1.00 29.04  ? 66  GLU B CA  1 
ATOM   2424 C C   . GLU B 1 49  ? 40.093 3.571   -18.260 1.00 24.94  ? 66  GLU B C   1 
ATOM   2425 O O   . GLU B 1 49  ? 39.188 4.419   -18.225 1.00 28.17  ? 66  GLU B O   1 
ATOM   2426 C CB  . GLU B 1 49  ? 42.486 4.311   -18.506 1.00 28.80  ? 66  GLU B CB  1 
ATOM   2427 C CG  . GLU B 1 49  ? 43.612 4.971   -17.718 1.00 31.57  ? 66  GLU B CG  1 
ATOM   2428 C CD  . GLU B 1 49  ? 44.861 5.298   -18.529 1.00 34.01  ? 66  GLU B CD  1 
ATOM   2429 O OE1 . GLU B 1 49  ? 44.968 4.882   -19.702 1.00 33.89  ? 66  GLU B OE1 1 
ATOM   2430 O OE2 . GLU B 1 49  ? 45.741 5.989   -17.960 1.00 39.89  ? 66  GLU B OE2 1 
ATOM   2431 N N   . GLU B 1 50  ? 39.937 2.391   -18.855 1.00 26.99  ? 67  GLU B N   1 
ATOM   2432 C CA  . GLU B 1 50  ? 38.661 2.033   -19.466 1.00 25.84  ? 67  GLU B CA  1 
ATOM   2433 C C   . GLU B 1 50  ? 37.539 1.983   -18.433 1.00 30.52  ? 67  GLU B C   1 
ATOM   2434 O O   . GLU B 1 50  ? 36.442 2.515   -18.645 1.00 26.01  ? 67  GLU B O   1 
ATOM   2435 C CB  . GLU B 1 50  ? 38.802 0.684   -20.172 1.00 30.26  ? 67  GLU B CB  1 
ATOM   2436 C CG  . GLU B 1 50  ? 37.484 0.163   -20.784 1.00 32.51  ? 67  GLU B CG  1 
ATOM   2437 C CD  . GLU B 1 50  ? 37.623 -1.219  -21.395 1.00 32.24  ? 67  GLU B CD  1 
ATOM   2438 O OE1 . GLU B 1 50  ? 38.735 -1.536  -21.886 1.00 27.33  ? 67  GLU B OE1 1 
ATOM   2439 O OE2 . GLU B 1 50  ? 36.628 -1.986  -21.383 1.00 25.26  ? 67  GLU B OE2 1 
ATOM   2440 N N   . ALA B 1 51  ? 37.785 1.314   -17.313 1.00 26.98  ? 68  ALA B N   1 
ATOM   2441 C CA  . ALA B 1 51  ? 36.755 1.222   -16.283 1.00 26.77  ? 68  ALA B CA  1 
ATOM   2442 C C   . ALA B 1 51  ? 36.373 2.607   -15.765 1.00 30.19  ? 68  ALA B C   1 
ATOM   2443 O O   . ALA B 1 51  ? 35.189 2.908   -15.583 1.00 26.52  ? 68  ALA B O   1 
ATOM   2444 C CB  . ALA B 1 51  ? 37.238 0.337   -15.134 1.00 26.10  ? 68  ALA B CB  1 
ATOM   2445 N N   . VAL B 1 52  ? 37.360 3.469   -15.527 1.00 27.32  ? 69  VAL B N   1 
ATOM   2446 C CA  . VAL B 1 52  ? 37.043 4.803   -15.035 1.00 26.77  ? 69  VAL B CA  1 
ATOM   2447 C C   . VAL B 1 52  ? 36.258 5.581   -16.085 1.00 32.31  ? 69  VAL B C   1 
ATOM   2448 O O   . VAL B 1 52  ? 35.301 6.296   -15.767 1.00 30.60  ? 69  VAL B O   1 
ATOM   2449 C CB  . VAL B 1 52  ? 38.336 5.533   -14.627 1.00 26.71  ? 69  VAL B CB  1 
ATOM   2450 C CG1 . VAL B 1 52  ? 38.051 6.981   -14.296 1.00 34.64  ? 69  VAL B CG1 1 
ATOM   2451 C CG2 . VAL B 1 52  ? 38.999 4.848   -13.413 1.00 30.76  ? 69  VAL B CG2 1 
ATOM   2452 N N   . ALA B 1 53  ? 36.643 5.462   -17.354 1.00 29.41  ? 70  ALA B N   1 
ATOM   2453 C CA  . ALA B 1 53  ? 35.890 6.149   -18.403 1.00 28.48  ? 70  ALA B CA  1 
ATOM   2454 C C   . ALA B 1 53  ? 34.450 5.665   -18.492 1.00 35.01  ? 70  ALA B C   1 
ATOM   2455 O O   . ALA B 1 53  ? 33.581 6.406   -18.961 1.00 33.15  ? 70  ALA B O   1 
ATOM   2456 C CB  . ALA B 1 53  ? 36.591 5.963   -19.745 1.00 31.23  ? 70  ALA B CB  1 
ATOM   2457 N N   . ALA B 1 54  ? 34.174 4.443   -18.046 1.00 29.25  ? 71  ALA B N   1 
ATOM   2458 C CA  . ALA B 1 54  ? 32.832 3.881   -18.055 1.00 32.50  ? 71  ALA B CA  1 
ATOM   2459 C C   . ALA B 1 54  ? 32.048 4.146   -16.773 1.00 31.12  ? 71  ALA B C   1 
ATOM   2460 O O   . ALA B 1 54  ? 31.003 3.530   -16.567 1.00 32.37  ? 71  ALA B O   1 
ATOM   2461 C CB  . ALA B 1 54  ? 32.906 2.372   -18.288 1.00 31.97  ? 71  ALA B CB  1 
ATOM   2462 N N   . GLY B 1 55  ? 32.541 5.006   -15.893 1.00 33.31  ? 72  GLY B N   1 
ATOM   2463 C CA  . GLY B 1 55  ? 31.813 5.332   -14.686 1.00 35.68  ? 72  GLY B CA  1 
ATOM   2464 C C   . GLY B 1 55  ? 32.176 4.539   -13.451 1.00 32.27  ? 72  GLY B C   1 
ATOM   2465 O O   . GLY B 1 55  ? 31.545 4.728   -12.406 1.00 34.47  ? 72  GLY B O   1 
ATOM   2466 N N   . ILE B 1 56  ? 33.188 3.678   -13.513 1.00 32.46  ? 73  ILE B N   1 
ATOM   2467 C CA  . ILE B 1 56  ? 33.589 2.967   -12.315 1.00 29.09  ? 73  ILE B CA  1 
ATOM   2468 C C   . ILE B 1 56  ? 34.266 3.940   -11.368 1.00 28.74  ? 73  ILE B C   1 
ATOM   2469 O O   . ILE B 1 56  ? 35.123 4.733   -11.777 1.00 33.92  ? 73  ILE B O   1 
ATOM   2470 C CB  . ILE B 1 56  ? 34.527 1.801   -12.648 1.00 28.55  ? 73  ILE B CB  1 
ATOM   2471 C CG1 . ILE B 1 56  ? 33.836 0.812   -13.579 1.00 29.55  ? 73  ILE B CG1 1 
ATOM   2472 C CG2 . ILE B 1 56  ? 34.964 1.119   -11.373 1.00 31.23  ? 73  ILE B CG2 1 
ATOM   2473 C CD1 . ILE B 1 56  ? 32.558 0.235   -12.997 1.00 30.35  ? 73  ILE B CD1 1 
ATOM   2474 N N   . THR B 1 57  ? 33.898 3.864   -10.095 1.00 28.18  ? 74  THR B N   1 
ATOM   2475 C CA  . THR B 1 57  ? 34.531 4.638   -9.044  1.00 34.99  ? 74  THR B CA  1 
ATOM   2476 C C   . THR B 1 57  ? 35.248 3.792   -8.005  1.00 30.10  ? 74  THR B C   1 
ATOM   2477 O O   . THR B 1 57  ? 36.122 4.327   -7.319  1.00 31.06  ? 74  THR B O   1 
ATOM   2478 C CB  . THR B 1 57  ? 33.488 5.487   -8.318  1.00 34.73  ? 74  THR B CB  1 
ATOM   2479 O OG1 . THR B 1 57  ? 32.523 4.617   -7.732  1.00 32.83  ? 74  THR B OG1 1 
ATOM   2480 C CG2 . THR B 1 57  ? 32.777 6.392   -9.298  1.00 40.41  ? 74  THR B CG2 1 
ATOM   2481 N N   . ASP B 1 58  ? 34.921 2.497   -7.882  1.00 32.69  ? 75  ASP B N   1 
ATOM   2482 C CA  . ASP B 1 58  ? 35.518 1.596   -6.892  1.00 28.76  ? 75  ASP B CA  1 
ATOM   2483 C C   . ASP B 1 58  ? 36.313 0.505   -7.604  1.00 28.57  ? 75  ASP B C   1 
ATOM   2484 O O   . ASP B 1 58  ? 35.731 -0.395  -8.222  1.00 28.26  ? 75  ASP B O   1 
ATOM   2485 C CB  . ASP B 1 58  ? 34.457 0.942   -5.996  1.00 33.03  ? 75  ASP B CB  1 
ATOM   2486 C CG  . ASP B 1 58  ? 33.643 1.935   -5.185  1.00 38.94  ? 75  ASP B CG  1 
ATOM   2487 O OD1 . ASP B 1 58  ? 33.975 3.142   -5.176  1.00 38.56  ? 75  ASP B OD1 1 
ATOM   2488 O OD2 . ASP B 1 58  ? 32.660 1.483   -4.529  1.00 37.24  ? 75  ASP B OD2 1 
ATOM   2489 N N   . LEU B 1 59  ? 37.627 0.557   -7.480  1.00 25.55  ? 76  LEU B N   1 
ATOM   2490 C CA  . LEU B 1 59  ? 38.517 -0.431  -8.068  1.00 22.36  ? 76  LEU B CA  1 
ATOM   2491 C C   . LEU B 1 59  ? 38.910 -1.453  -7.015  1.00 27.00  ? 76  LEU B C   1 
ATOM   2492 O O   . LEU B 1 59  ? 39.276 -1.076  -5.902  1.00 27.38  ? 76  LEU B O   1 
ATOM   2493 C CB  . LEU B 1 59  ? 39.787 0.226   -8.606  1.00 25.06  ? 76  LEU B CB  1 
ATOM   2494 C CG  . LEU B 1 59  ? 39.639 1.489   -9.463  1.00 26.20  ? 76  LEU B CG  1 
ATOM   2495 C CD1 . LEU B 1 59  ? 41.009 2.071   -9.862  1.00 24.35  ? 76  LEU B CD1 1 
ATOM   2496 C CD2 . LEU B 1 59  ? 38.805 1.163   -10.664 1.00 26.86  ? 76  LEU B CD2 1 
ATOM   2497 N N   . ILE B 1 60  ? 38.871 -2.731  -7.380  1.00 22.53  ? 77  ILE B N   1 
ATOM   2498 C CA  . ILE B 1 60  ? 39.173 -3.845  -6.492  1.00 20.83  ? 77  ILE B CA  1 
ATOM   2499 C C   . ILE B 1 60  ? 40.240 -4.690  -7.175  1.00 24.12  ? 77  ILE B C   1 
ATOM   2500 O O   . ILE B 1 60  ? 39.984 -5.284  -8.237  1.00 24.87  ? 77  ILE B O   1 
ATOM   2501 C CB  . ILE B 1 60  ? 37.913 -4.685  -6.187  1.00 23.70  ? 77  ILE B CB  1 
ATOM   2502 C CG1 . ILE B 1 60  ? 36.836 -3.823  -5.542  1.00 27.56  ? 77  ILE B CG1 1 
ATOM   2503 C CG2 . ILE B 1 60  ? 38.242 -5.858  -5.305  1.00 23.39  ? 77  ILE B CG2 1 
ATOM   2504 C CD1 . ILE B 1 60  ? 35.472 -4.469  -5.562  1.00 27.10  ? 77  ILE B CD1 1 
ATOM   2505 N N   . PHE B 1 61  ? 41.440 -4.712  -6.596  1.00 19.37  ? 78  PHE B N   1 
ATOM   2506 C CA  . PHE B 1 61  ? 42.583 -5.421  -7.145  1.00 22.23  ? 78  PHE B CA  1 
ATOM   2507 C C   . PHE B 1 61  ? 42.757 -6.706  -6.362  1.00 23.08  ? 78  PHE B C   1 
ATOM   2508 O O   . PHE B 1 61  ? 42.854 -6.681  -5.129  1.00 27.29  ? 78  PHE B O   1 
ATOM   2509 C CB  . PHE B 1 61  ? 43.847 -4.569  -7.047  1.00 22.55  ? 78  PHE B CB  1 
ATOM   2510 C CG  . PHE B 1 61  ? 43.818 -3.324  -7.890  1.00 26.30  ? 78  PHE B CG  1 
ATOM   2511 C CD1 . PHE B 1 61  ? 43.908 -3.401  -9.286  1.00 21.74  ? 78  PHE B CD1 1 
ATOM   2512 C CD2 . PHE B 1 61  ? 43.727 -2.074  -7.303  1.00 22.45  ? 78  PHE B CD2 1 
ATOM   2513 C CE1 . PHE B 1 61  ? 43.887 -2.264  -10.061 1.00 23.58  ? 78  PHE B CE1 1 
ATOM   2514 C CE2 . PHE B 1 61  ? 43.718 -0.916  -8.078  1.00 22.95  ? 78  PHE B CE2 1 
ATOM   2515 C CZ  . PHE B 1 61  ? 43.792 -1.020  -9.480  1.00 23.44  ? 78  PHE B CZ  1 
ATOM   2516 N N   . VAL B 1 62  ? 42.712 -7.828  -7.056  1.00 21.05  ? 79  VAL B N   1 
ATOM   2517 C CA  . VAL B 1 62  ? 42.935 -9.118  -6.446  1.00 22.07  ? 79  VAL B CA  1 
ATOM   2518 C C   . VAL B 1 62  ? 44.371 -9.488  -6.760  1.00 26.23  ? 79  VAL B C   1 
ATOM   2519 O O   . VAL B 1 62  ? 44.727 -9.743  -7.923  1.00 24.46  ? 79  VAL B O   1 
ATOM   2520 C CB  . VAL B 1 62  ? 41.923 -10.159 -6.936  1.00 21.76  ? 79  VAL B CB  1 
ATOM   2521 C CG1 . VAL B 1 62  ? 42.205 -11.484 -6.292  1.00 23.19  ? 79  VAL B CG1 1 
ATOM   2522 C CG2 . VAL B 1 62  ? 40.510 -9.713  -6.581  1.00 25.73  ? 79  VAL B CG2 1 
ATOM   2523 N N   . THR B 1 63  ? 45.194 -9.517  -5.720  1.00 24.12  ? 80  THR B N   1 
ATOM   2524 C CA  . THR B 1 63  ? 46.640 -9.603  -5.842  1.00 25.77  ? 80  THR B CA  1 
ATOM   2525 C C   . THR B 1 63  ? 47.152 -10.990 -5.495  1.00 26.24  ? 80  THR B C   1 
ATOM   2526 O O   . THR B 1 63  ? 46.459 -11.815 -4.891  1.00 26.11  ? 80  THR B O   1 
ATOM   2527 C CB  . THR B 1 63  ? 47.346 -8.584  -4.933  1.00 25.82  ? 80  THR B CB  1 
ATOM   2528 O OG1 . THR B 1 63  ? 47.093 -8.905  -3.568  1.00 29.43  ? 80  THR B OG1 1 
ATOM   2529 C CG2 . THR B 1 63  ? 46.853 -7.194  -5.178  1.00 26.44  ? 80  THR B CG2 1 
ATOM   2530 N N   . GLY B 1 64  ? 48.396 -11.233 -5.893  1.00 27.36  ? 81  GLY B N   1 
ATOM   2531 C CA  . GLY B 1 64  ? 49.080 -12.456 -5.543  1.00 28.34  ? 81  GLY B CA  1 
ATOM   2532 C C   . GLY B 1 64  ? 50.494 -12.132 -5.123  1.00 34.62  ? 81  GLY B C   1 
ATOM   2533 O O   . GLY B 1 64  ? 50.734 -11.203 -4.353  1.00 35.61  ? 81  GLY B O   1 
ATOM   2534 N N   . ARG B 1 65  ? 51.461 -12.834 -5.670  1.00 42.11  ? 82  ARG B N   1 
ATOM   2535 C CA  . ARG B 1 65  ? 52.804 -12.411 -5.323  1.00 47.35  ? 82  ARG B CA  1 
ATOM   2536 C C   . ARG B 1 65  ? 53.185 -11.148 -6.102  1.00 33.35  ? 82  ARG B C   1 
ATOM   2537 O O   . ARG B 1 65  ? 52.559 -10.754 -7.101  1.00 36.74  ? 82  ARG B O   1 
ATOM   2538 C CB  . ARG B 1 65  ? 53.786 -13.571 -5.516  1.00 58.33  ? 82  ARG B CB  1 
ATOM   2539 C CG  . ARG B 1 65  ? 53.662 -14.348 -6.803  1.00 54.10  ? 82  ARG B CG  1 
ATOM   2540 C CD  . ARG B 1 65  ? 54.673 -15.511 -6.812  1.00 62.60  ? 82  ARG B CD  1 
ATOM   2541 N NE  . ARG B 1 65  ? 55.996 -15.036 -6.411  1.00 67.46  ? 82  ARG B NE  1 
ATOM   2542 C CZ  . ARG B 1 65  ? 56.890 -14.484 -7.228  1.00 63.86  ? 82  ARG B CZ  1 
ATOM   2543 N NH1 . ARG B 1 65  ? 56.698 -14.427 -8.545  1.00 60.75  ? 82  ARG B NH1 1 
ATOM   2544 N NH2 . ARG B 1 65  ? 57.992 -13.945 -6.708  1.00 55.28  ? 82  ARG B NH2 1 
ATOM   2545 N N   . ASN B 1 66  ? 54.160 -10.441 -5.559  1.00 38.97  ? 83  ASN B N   1 
ATOM   2546 C CA  . ASN B 1 66  ? 54.545 -9.154  -6.105  1.00 39.97  ? 83  ASN B CA  1 
ATOM   2547 C C   . ASN B 1 66  ? 53.367 -8.178  -6.059  1.00 35.65  ? 83  ASN B C   1 
ATOM   2548 O O   . ASN B 1 66  ? 53.215 -7.287  -6.913  1.00 28.36  ? 83  ASN B O   1 
ATOM   2549 C CB  . ASN B 1 66  ? 55.111 -9.346  -7.514  1.00 44.83  ? 83  ASN B CB  1 
ATOM   2550 C CG  . ASN B 1 66  ? 56.353 -10.233 -7.508  1.00 42.02  ? 83  ASN B CG  1 
ATOM   2551 O OD1 . ASN B 1 66  ? 57.279 -10.006 -6.731  1.00 46.66  ? 83  ASN B OD1 1 
ATOM   2552 N ND2 . ASN B 1 66  ? 56.348 -11.260 -8.328  1.00 41.91  ? 83  ASN B ND2 1 
ATOM   2553 N N   . LYS B 1 67  ? 52.547 -8.321  -5.016  1.00 29.85  ? 84  LYS B N   1 
ATOM   2554 C CA  . LYS B 1 67  ? 51.428 -7.405  -4.819  1.00 30.53  ? 84  LYS B CA  1 
ATOM   2555 C C   . LYS B 1 67  ? 51.872 -5.943  -4.776  1.00 32.56  ? 84  LYS B C   1 
ATOM   2556 O O   . LYS B 1 67  ? 51.097 -5.044  -5.116  1.00 28.91  ? 84  LYS B O   1 
ATOM   2557 C CB  . LYS B 1 67  ? 50.711 -7.762  -3.521  1.00 32.34  ? 84  LYS B CB  1 
ATOM   2558 C CG  . LYS B 1 67  ? 51.575 -7.516  -2.257  1.00 33.93  ? 84  LYS B CG  1 
ATOM   2559 C CD  . LYS B 1 67  ? 51.158 -8.408  -1.093  1.00 36.69  ? 84  LYS B CD  1 
ATOM   2560 C CE  . LYS B 1 67  ? 51.744 -7.873  0.202   1.00 38.16  ? 84  LYS B CE  1 
ATOM   2561 N NZ  . LYS B 1 67  ? 51.962 -8.958  1.230   1.00 48.85  ? 84  LYS B NZ  1 
ATOM   2562 N N   . ARG B 1 68  ? 53.092 -5.669  -4.345  1.00 28.21  ? 85  ARG B N   1 
ATOM   2563 C CA  A ARG B 1 68  ? 53.436 -4.268  -4.156  0.57 35.00  ? 85  ARG B CA  1 
ATOM   2564 C CA  B ARG B 1 68  ? 53.526 -4.290  -4.146  0.43 35.06  ? 85  ARG B CA  1 
ATOM   2565 C C   . ARG B 1 68  ? 53.743 -3.550  -5.457  1.00 24.92  ? 85  ARG B C   1 
ATOM   2566 O O   . ARG B 1 68  ? 53.664 -2.318  -5.488  1.00 21.46  ? 85  ARG B O   1 
ATOM   2567 C CB  A ARG B 1 68  ? 54.613 -4.123  -3.192  0.57 43.70  ? 85  ARG B CB  1 
ATOM   2568 C CB  B ARG B 1 68  ? 54.820 -4.256  -3.332  0.43 43.39  ? 85  ARG B CB  1 
ATOM   2569 C CG  A ARG B 1 68  ? 54.319 -4.733  -1.829  0.57 45.80  ? 85  ARG B CG  1 
ATOM   2570 C CG  B ARG B 1 68  ? 54.700 -4.807  -1.905  0.43 45.71  ? 85  ARG B CG  1 
ATOM   2571 C CD  A ARG B 1 68  ? 54.702 -3.850  -0.621  0.57 41.33  ? 85  ARG B CD  1 
ATOM   2572 C CD  B ARG B 1 68  ? 53.667 -4.057  -1.061  0.43 41.69  ? 85  ARG B CD  1 
ATOM   2573 N NE  A ARG B 1 68  ? 53.916 -4.303  0.511   0.57 38.86  ? 85  ARG B NE  1 
ATOM   2574 N NE  B ARG B 1 68  ? 54.290 -3.241  -0.025  0.43 39.02  ? 85  ARG B NE  1 
ATOM   2575 C CZ  A ARG B 1 68  ? 54.191 -5.369  1.249   0.57 43.29  ? 85  ARG B CZ  1 
ATOM   2576 C CZ  B ARG B 1 68  ? 54.713 -1.998  -0.214  0.43 39.25  ? 85  ARG B CZ  1 
ATOM   2577 N NH1 A ARG B 1 68  ? 55.336 -6.026  1.131   0.57 38.32  ? 85  ARG B NH1 1 
ATOM   2578 N NH1 B ARG B 1 68  ? 54.703 -1.443  -1.409  0.43 32.66  ? 85  ARG B NH1 1 
ATOM   2579 N NH2 A ARG B 1 68  ? 53.287 -5.795  2.121   0.57 42.18  ? 85  ARG B NH2 1 
ATOM   2580 N NH2 B ARG B 1 68  ? 55.126 -1.285  0.829   0.43 42.93  ? 85  ARG B NH2 1 
ATOM   2581 N N   . ALA B 1 69  ? 54.054 -4.272  -6.545  1.00 27.34  ? 86  ALA B N   1 
ATOM   2582 C CA  . ALA B 1 69  ? 54.168 -3.589  -7.832  1.00 25.54  ? 86  ALA B CA  1 
ATOM   2583 C C   . ALA B 1 69  ? 52.838 -2.952  -8.209  1.00 22.91  ? 86  ALA B C   1 
ATOM   2584 O O   . ALA B 1 69  ? 52.786 -1.835  -8.719  1.00 23.40  ? 86  ALA B O   1 
ATOM   2585 C CB  . ALA B 1 69  ? 54.633 -4.570  -8.922  1.00 30.07  ? 86  ALA B CB  1 
ATOM   2586 N N   . ILE B 1 70  ? 51.739 -3.656  -7.956  1.00 25.36  ? 87  ILE B N   1 
ATOM   2587 C CA  . ILE B 1 70  ? 50.420 -3.094  -8.216  1.00 22.81  ? 87  ILE B CA  1 
ATOM   2588 C C   . ILE B 1 70  ? 50.105 -1.974  -7.242  1.00 23.27  ? 87  ILE B C   1 
ATOM   2589 O O   . ILE B 1 70  ? 49.619 -0.907  -7.634  1.00 23.50  ? 87  ILE B O   1 
ATOM   2590 C CB  . ILE B 1 70  ? 49.367 -4.212  -8.124  1.00 27.47  ? 87  ILE B CB  1 
ATOM   2591 C CG1 . ILE B 1 70  ? 49.498 -5.125  -9.323  1.00 31.28  ? 87  ILE B CG1 1 
ATOM   2592 C CG2 . ILE B 1 70  ? 47.973 -3.597  -8.086  1.00 28.42  ? 87  ILE B CG2 1 
ATOM   2593 C CD1 . ILE B 1 70  ? 48.888 -4.489  -10.587 1.00 29.44  ? 87  ILE B CD1 1 
ATOM   2594 N N   . GLU B 1 71  ? 50.299 -2.228  -5.938  1.00 22.54  ? 88  GLU B N   1 
ATOM   2595 C CA  . GLU B 1 71  ? 49.950 -1.233  -4.937  1.00 23.86  ? 88  GLU B CA  1 
ATOM   2596 C C   . GLU B 1 71  ? 50.741 0.042   -5.146  1.00 24.81  ? 88  GLU B C   1 
ATOM   2597 O O   . GLU B 1 71  ? 50.185 1.149   -5.062  1.00 22.58  ? 88  GLU B O   1 
ATOM   2598 C CB  . GLU B 1 71  ? 50.205 -1.767  -3.514  1.00 27.72  ? 88  GLU B CB  1 
ATOM   2599 C CG  . GLU B 1 71  ? 49.345 -3.008  -3.178  1.00 29.84  ? 88  GLU B CG  1 
ATOM   2600 C CD  . GLU B 1 71  ? 49.626 -3.587  -1.789  1.00 32.10  ? 88  GLU B CD  1 
ATOM   2601 O OE1 . GLU B 1 71  ? 50.516 -3.065  -1.089  1.00 36.32  ? 88  GLU B OE1 1 
ATOM   2602 O OE2 . GLU B 1 71  ? 48.949 -4.560  -1.396  1.00 30.66  ? 88  GLU B OE2 1 
ATOM   2603 N N   . ASP B 1 72  ? 52.049 -0.091  -5.399  1.00 22.52  ? 89  ASP B N   1 
ATOM   2604 C CA  . ASP B 1 72  ? 52.865 1.109   -5.520  1.00 24.11  ? 89  ASP B CA  1 
ATOM   2605 C C   . ASP B 1 72  ? 52.593 1.839   -6.816  1.00 22.14  ? 89  ASP B C   1 
ATOM   2606 O O   . ASP B 1 72  ? 52.898 3.036   -6.923  1.00 26.09  ? 89  ASP B O   1 
ATOM   2607 C CB  . ASP B 1 72  ? 54.337 0.772   -5.387  1.00 24.60  ? 89  ASP B CB  1 
ATOM   2608 C CG  . ASP B 1 72  ? 54.712 0.389   -3.948  1.00 31.90  ? 89  ASP B CG  1 
ATOM   2609 O OD1 . ASP B 1 72  ? 53.850 0.533   -3.065  1.00 31.75  ? 89  ASP B OD1 1 
ATOM   2610 O OD2 . ASP B 1 72  ? 55.839 -0.091  -3.724  1.00 31.86  ? 89  ASP B OD2 1 
ATOM   2611 N N   . HIS B 1 73  ? 52.027 1.146   -7.801  1.00 24.49  ? 90  HIS B N   1 
ATOM   2612 C CA  . HIS B 1 73  ? 51.637 1.827   -9.011  1.00 22.15  ? 90  HIS B CA  1 
ATOM   2613 C C   . HIS B 1 73  ? 50.407 2.703   -8.789  1.00 21.90  ? 90  HIS B C   1 
ATOM   2614 O O   . HIS B 1 73  ? 50.367 3.847   -9.251  1.00 25.44  ? 90  HIS B O   1 
ATOM   2615 C CB  . HIS B 1 73  ? 51.403 0.815   -10.134 1.00 25.43  ? 90  HIS B CB  1 
ATOM   2616 C CG  . HIS B 1 73  ? 51.188 1.491   -11.439 1.00 24.06  ? 90  HIS B CG  1 
ATOM   2617 N ND1 . HIS B 1 73  ? 52.214 2.071   -12.159 1.00 21.48  ? 90  HIS B ND1 1 
ATOM   2618 C CD2 . HIS B 1 73  ? 50.047 1.803   -12.081 1.00 18.65  ? 90  HIS B CD2 1 
ATOM   2619 C CE1 . HIS B 1 73  ? 51.704 2.687   -13.208 1.00 26.45  ? 90  HIS B CE1 1 
ATOM   2620 N NE2 . HIS B 1 73  ? 50.392 2.538   -13.180 1.00 22.08  ? 90  HIS B NE2 1 
ATOM   2621 N N   . PHE B 1 74  ? 49.394 2.204   -8.080  1.00 22.36  ? 91  PHE B N   1 
ATOM   2622 C CA  . PHE B 1 74  ? 48.153 2.963   -7.974  1.00 23.91  ? 91  PHE B CA  1 
ATOM   2623 C C   . PHE B 1 74  ? 48.082 3.842   -6.725  1.00 27.75  ? 91  PHE B C   1 
ATOM   2624 O O   . PHE B 1 74  ? 47.392 4.871   -6.752  1.00 26.34  ? 91  PHE B O   1 
ATOM   2625 C CB  . PHE B 1 74  ? 46.964 1.989   -8.063  1.00 23.96  ? 91  PHE B CB  1 
ATOM   2626 C CG  . PHE B 1 74  ? 46.730 1.460   -9.464  1.00 22.38  ? 91  PHE B CG  1 
ATOM   2627 C CD1 . PHE B 1 74  ? 46.110 2.255   -10.415 1.00 27.40  ? 91  PHE B CD1 1 
ATOM   2628 C CD2 . PHE B 1 74  ? 47.157 0.192   -9.841  1.00 25.99  ? 91  PHE B CD2 1 
ATOM   2629 C CE1 . PHE B 1 74  ? 45.926 1.816   -11.724 1.00 29.16  ? 91  PHE B CE1 1 
ATOM   2630 C CE2 . PHE B 1 74  ? 46.959 -0.261  -11.158 1.00 26.38  ? 91  PHE B CE2 1 
ATOM   2631 C CZ  . PHE B 1 74  ? 46.325 0.557   -12.093 1.00 26.37  ? 91  PHE B CZ  1 
ATOM   2632 N N   . ASP B 1 75  ? 48.795 3.510   -5.642  1.00 27.93  ? 92  ASP B N   1 
ATOM   2633 C CA  . ASP B 1 75  ? 48.806 4.391   -4.470  1.00 25.05  ? 92  ASP B CA  1 
ATOM   2634 C C   . ASP B 1 75  ? 49.607 5.652   -4.745  1.00 31.49  ? 92  ASP B C   1 
ATOM   2635 O O   . ASP B 1 75  ? 50.575 5.645   -5.512  1.00 33.88  ? 92  ASP B O   1 
ATOM   2636 C CB  . ASP B 1 75  ? 49.405 3.674   -3.258  1.00 28.90  ? 92  ASP B CB  1 
ATOM   2637 C CG  . ASP B 1 75  ? 48.589 2.465   -2.849  1.00 36.60  ? 92  ASP B CG  1 
ATOM   2638 O OD1 . ASP B 1 75  ? 47.370 2.404   -3.126  1.00 34.80  ? 92  ASP B OD1 1 
ATOM   2639 O OD2 . ASP B 1 75  ? 49.178 1.559   -2.261  1.00 37.55  ? 92  ASP B OD2 1 
ATOM   2640 N N   . ALA B 1 76  ? 49.192 6.744   -4.122  1.00 26.62  ? 93  ALA B N   1 
ATOM   2641 C CA  . ALA B 1 76  ? 49.913 7.998   -4.266  1.00 30.20  ? 93  ALA B CA  1 
ATOM   2642 C C   . ALA B 1 76  ? 51.371 7.847   -3.844  1.00 28.26  ? 93  ALA B C   1 
ATOM   2643 O O   . ALA B 1 76  ? 51.717 7.038   -2.989  1.00 37.09  ? 93  ALA B O   1 
ATOM   2644 C CB  . ALA B 1 76  ? 49.252 9.091   -3.426  1.00 34.65  ? 93  ALA B CB  1 
ATOM   2645 N N   . ALA B 1 77  ? 52.248 8.600   -4.493  1.00 32.06  ? 94  ALA B N   1 
ATOM   2646 C CA  . ALA B 1 77  ? 53.659 8.609   -4.129  1.00 35.05  ? 94  ALA B CA  1 
ATOM   2647 C C   . ALA B 1 77  ? 54.034 10.064  -3.902  1.00 41.65  ? 94  ALA B C   1 
ATOM   2648 O O   . ALA B 1 77  ? 54.485 10.753  -4.819  1.00 36.32  ? 94  ALA B O   1 
ATOM   2649 C CB  . ALA B 1 77  ? 54.517 7.935   -5.187  1.00 34.27  ? 94  ALA B CB  1 
ATOM   2650 N N   . PRO B 1 78  ? 53.840 10.563  -2.693  1.00 43.08  ? 95  PRO B N   1 
ATOM   2651 C CA  . PRO B 1 78  ? 54.097 11.984  -2.432  1.00 45.53  ? 95  PRO B CA  1 
ATOM   2652 C C   . PRO B 1 78  ? 55.490 12.408  -2.823  1.00 48.29  ? 95  PRO B C   1 
ATOM   2653 O O   . PRO B 1 78  ? 55.680 13.519  -3.328  1.00 46.98  ? 95  PRO B O   1 
ATOM   2654 C CB  . PRO B 1 78  ? 53.869 12.106  -0.918  1.00 47.89  ? 95  PRO B CB  1 
ATOM   2655 C CG  . PRO B 1 78  ? 53.036 10.938  -0.554  1.00 52.26  ? 95  PRO B CG  1 
ATOM   2656 C CD  . PRO B 1 78  ? 53.413 9.838   -1.486  1.00 51.30  ? 95  PRO B CD  1 
ATOM   2657 N N   . GLU B 1 79  ? 56.481 11.551  -2.591  1.00 50.15  ? 96  GLU B N   1 
ATOM   2658 C CA  . GLU B 1 79  ? 57.859 11.928  -2.885  1.00 53.01  ? 96  GLU B CA  1 
ATOM   2659 C C   . GLU B 1 79  ? 58.021 12.267  -4.365  1.00 56.76  ? 96  GLU B C   1 
ATOM   2660 O O   . GLU B 1 79  ? 58.611 13.296  -4.713  1.00 51.32  ? 96  GLU B O   1 
ATOM   2661 C CB  . GLU B 1 79  ? 58.794 10.796  -2.446  1.00 58.24  ? 96  GLU B CB  1 
ATOM   2662 C CG  . GLU B 1 79  ? 60.234 10.890  -2.944  1.00 78.54  ? 96  GLU B CG  1 
ATOM   2663 C CD  . GLU B 1 79  ? 61.073 9.689   -2.509  1.00 89.99  ? 96  GLU B CD  1 
ATOM   2664 O OE1 . GLU B 1 79  ? 60.612 8.939   -1.610  1.00 86.07  ? 96  GLU B OE1 1 
ATOM   2665 O OE2 . GLU B 1 79  ? 62.175 9.483   -3.081  1.00 86.01  ? 96  GLU B OE2 1 
ATOM   2666 N N   . LEU B 1 80  ? 57.490 11.419  -5.255  1.00 46.92  ? 97  LEU B N   1 
ATOM   2667 C CA  . LEU B 1 80  ? 57.577 11.699  -6.684  1.00 43.32  ? 97  LEU B CA  1 
ATOM   2668 C C   . LEU B 1 80  ? 56.823 12.967  -7.048  1.00 47.79  ? 97  LEU B C   1 
ATOM   2669 O O   . LEU B 1 80  ? 57.298 13.769  -7.863  1.00 47.30  ? 97  LEU B O   1 
ATOM   2670 C CB  . LEU B 1 80  ? 57.008 10.533  -7.497  1.00 45.27  ? 97  LEU B CB  1 
ATOM   2671 C CG  . LEU B 1 80  ? 57.053 10.665  -9.029  1.00 42.33  ? 97  LEU B CG  1 
ATOM   2672 C CD1 . LEU B 1 80  ? 58.484 10.535  -9.569  1.00 43.65  ? 97  LEU B CD1 1 
ATOM   2673 C CD2 . LEU B 1 80  ? 56.132 9.643   -9.700  1.00 39.88  ? 97  LEU B CD2 1 
ATOM   2674 N N   . GLU B 1 81  ? 55.621 13.138  -6.497  1.00 42.76  ? 98  GLU B N   1 
ATOM   2675 C CA  . GLU B 1 81  ? 54.835 14.324  -6.807  1.00 43.66  ? 98  GLU B CA  1 
ATOM   2676 C C   . GLU B 1 81  ? 55.526 15.584  -6.291  1.00 58.95  ? 98  GLU B C   1 
ATOM   2677 O O   . GLU B 1 81  ? 55.568 16.607  -6.986  1.00 53.26  ? 98  GLU B O   1 
ATOM   2678 C CB  . GLU B 1 81  ? 53.437 14.194  -6.215  1.00 44.61  ? 98  GLU B CB  1 
ATOM   2679 C CG  . GLU B 1 81  ? 52.609 13.061  -6.784  1.00 42.67  ? 98  GLU B CG  1 
ATOM   2680 C CD  . GLU B 1 81  ? 51.184 13.100  -6.265  1.00 47.19  ? 98  GLU B CD  1 
ATOM   2681 O OE1 . GLU B 1 81  ? 50.745 14.195  -5.862  1.00 52.26  ? 98  GLU B OE1 1 
ATOM   2682 O OE2 . GLU B 1 81  ? 50.500 12.055  -6.255  1.00 48.11  ? 98  GLU B OE2 1 
ATOM   2683 N N   . THR B 1 82  ? 56.085 15.522  -5.073  1.00 53.30  ? 99  THR B N   1 
ATOM   2684 C CA  . THR B 1 82  ? 56.788 16.673  -4.511  1.00 59.26  ? 99  THR B CA  1 
ATOM   2685 C C   . THR B 1 82  ? 58.001 17.037  -5.355  1.00 61.76  ? 99  THR B C   1 
ATOM   2686 O O   . THR B 1 82  ? 58.261 18.218  -5.601  1.00 69.67  ? 99  THR B O   1 
ATOM   2687 C CB  . THR B 1 82  ? 57.229 16.381  -3.071  1.00 63.86  ? 99  THR B CB  1 
ATOM   2688 O OG1 . THR B 1 82  ? 56.084 16.256  -2.211  1.00 62.06  ? 99  THR B OG1 1 
ATOM   2689 C CG2 . THR B 1 82  ? 58.144 17.491  -2.551  1.00 64.01  ? 99  THR B CG2 1 
ATOM   2690 N N   . ASP B 1 83  ? 58.762 16.034  -5.797  1.00 62.87  ? 100 ASP B N   1 
ATOM   2691 C CA  . ASP B 1 83  ? 59.924 16.288  -6.644  1.00 64.44  ? 100 ASP B CA  1 
ATOM   2692 C C   . ASP B 1 83  ? 59.520 16.874  -7.993  1.00 66.91  ? 100 ASP B C   1 
ATOM   2693 O O   . ASP B 1 83  ? 60.133 17.836  -8.471  1.00 70.77  ? 100 ASP B O   1 
ATOM   2694 C CB  . ASP B 1 83  ? 60.711 14.990  -6.833  1.00 67.43  ? 100 ASP B CB  1 
ATOM   2695 C CG  . ASP B 1 83  ? 61.768 15.084  -7.937  1.00 78.55  ? 100 ASP B CG  1 
ATOM   2696 O OD1 . ASP B 1 83  ? 62.187 16.201  -8.312  1.00 87.42  ? 100 ASP B OD1 1 
ATOM   2697 O OD2 . ASP B 1 83  ? 62.182 14.022  -8.439  1.00 72.38  ? 100 ASP B OD2 1 
ATOM   2698 N N   . LEU B 1 84  ? 58.496 16.308  -8.629  1.00 55.21  ? 101 LEU B N   1 
ATOM   2699 C CA  . LEU B 1 84  ? 58.109 16.805  -9.948  1.00 59.60  ? 101 LEU B CA  1 
ATOM   2700 C C   . LEU B 1 84  ? 57.571 18.225  -9.865  1.00 61.75  ? 101 LEU B C   1 
ATOM   2701 O O   . LEU B 1 84  ? 57.803 19.039  -10.769 1.00 60.33  ? 101 LEU B O   1 
ATOM   2702 C CB  . LEU B 1 84  ? 57.065 15.891  -10.594 1.00 53.34  ? 101 LEU B CB  1 
ATOM   2703 C CG  . LEU B 1 84  ? 57.485 14.496  -11.071 1.00 53.20  ? 101 LEU B CG  1 
ATOM   2704 C CD1 . LEU B 1 84  ? 56.281 13.715  -11.640 1.00 39.34  ? 101 LEU B CD1 1 
ATOM   2705 C CD2 . LEU B 1 84  ? 58.565 14.615  -12.117 1.00 51.18  ? 101 LEU B CD2 1 
ATOM   2706 N N   . GLU B 1 85  ? 56.837 18.533  -8.795  1.00 63.80  ? 102 GLU B N   1 
ATOM   2707 C CA  . GLU B 1 85  ? 56.380 19.901  -8.579  1.00 71.71  ? 102 GLU B CA  1 
ATOM   2708 C C   . GLU B 1 85  ? 57.561 20.850  -8.513  1.00 69.70  ? 102 GLU B C   1 
ATOM   2709 O O   . GLU B 1 85  ? 57.608 21.849  -9.236  1.00 72.68  ? 102 GLU B O   1 
ATOM   2710 C CB  . GLU B 1 85  ? 55.543 19.979  -7.297  1.00 76.55  ? 102 GLU B CB  1 
ATOM   2711 C CG  . GLU B 1 85  ? 55.032 21.373  -6.932  1.00 82.79  ? 102 GLU B CG  1 
ATOM   2712 C CD  . GLU B 1 85  ? 54.158 22.001  -8.003  1.00 96.56  ? 102 GLU B CD  1 
ATOM   2713 O OE1 . GLU B 1 85  ? 53.733 21.284  -8.933  1.00 99.06  ? 102 GLU B OE1 1 
ATOM   2714 O OE2 . GLU B 1 85  ? 53.909 23.225  -7.923  1.00 99.59  ? 102 GLU B OE2 1 
ATOM   2715 N N   . ALA B 1 86  ? 58.553 20.520  -7.685  1.00 75.22  ? 103 ALA B N   1 
ATOM   2716 C CA  . ALA B 1 86  ? 59.730 21.370  -7.560  1.00 86.28  ? 103 ALA B CA  1 
ATOM   2717 C C   . ALA B 1 86  ? 60.353 21.650  -8.920  1.00 81.48  ? 103 ALA B C   1 
ATOM   2718 O O   . ALA B 1 86  ? 60.545 22.807  -9.307  1.00 89.43  ? 103 ALA B O   1 
ATOM   2719 C CB  . ALA B 1 86  ? 60.748 20.703  -6.634  1.00 85.91  ? 103 ALA B CB  1 
ATOM   2720 N N   . LYS B 1 87  ? 60.649 20.600  -9.672  1.00 68.75  ? 104 LYS B N   1 
ATOM   2721 C CA  . LYS B 1 87  ? 61.234 20.752  -10.997 1.00 72.91  ? 104 LYS B CA  1 
ATOM   2722 C C   . LYS B 1 87  ? 60.276 21.384  -12.004 1.00 71.37  ? 104 LYS B C   1 
ATOM   2723 O O   . LYS B 1 87  ? 60.626 21.487  -13.187 1.00 70.01  ? 104 LYS B O   1 
ATOM   2724 C CB  . LYS B 1 87  ? 61.732 19.387  -11.482 1.00 76.47  ? 104 LYS B CB  1 
ATOM   2725 C CG  . LYS B 1 87  ? 62.746 18.763  -10.516 1.00 75.11  ? 104 LYS B CG  1 
ATOM   2726 C CD  . LYS B 1 87  ? 63.219 17.394  -10.959 1.00 73.79  ? 104 LYS B CD  1 
ATOM   2727 C CE  . LYS B 1 87  ? 64.042 17.473  -12.223 1.00 71.46  ? 104 LYS B CE  1 
ATOM   2728 N NZ  . LYS B 1 87  ? 64.585 16.139  -12.595 1.00 77.09  ? 104 LYS B NZ  1 
ATOM   2729 N N   . GLY B 1 88  ? 59.077 21.775  -11.579 1.00 62.03  ? 105 GLY B N   1 
ATOM   2730 C CA  . GLY B 1 88  ? 58.118 22.393  -12.478 1.00 63.37  ? 105 GLY B CA  1 
ATOM   2731 C C   . GLY B 1 88  ? 57.681 21.536  -13.642 1.00 64.96  ? 105 GLY B C   1 
ATOM   2732 O O   . GLY B 1 88  ? 57.414 22.062  -14.725 1.00 60.76  ? 105 GLY B O   1 
ATOM   2733 N N   . LYS B 1 89  ? 57.581 20.226  -13.444 1.00 73.92  ? 106 LYS B N   1 
ATOM   2734 C CA  . LYS B 1 89  ? 57.142 19.315  -14.498 1.00 68.27  ? 106 LYS B CA  1 
ATOM   2735 C C   . LYS B 1 89  ? 55.648 19.035  -14.342 1.00 62.95  ? 106 LYS B C   1 
ATOM   2736 O O   . LYS B 1 89  ? 55.218 17.948  -13.965 1.00 57.98  ? 106 LYS B O   1 
ATOM   2737 C CB  . LYS B 1 89  ? 57.956 18.033  -14.441 1.00 72.15  ? 106 LYS B CB  1 
ATOM   2738 C CG  . LYS B 1 89  ? 59.469 18.231  -14.429 1.00 79.29  ? 106 LYS B CG  1 
ATOM   2739 C CD  . LYS B 1 89  ? 60.031 18.665  -15.782 1.00 91.22  ? 106 LYS B CD  1 
ATOM   2740 C CE  . LYS B 1 89  ? 59.619 17.688  -16.887 1.00 93.68  ? 106 LYS B CE  1 
ATOM   2741 N NZ  . LYS B 1 89  ? 60.345 17.875  -18.174 1.00 100.32 ? 106 LYS B NZ  1 
ATOM   2742 N N   . HIS B 1 90  ? 54.843 20.057  -14.627 1.00 64.13  ? 107 HIS B N   1 
ATOM   2743 C CA  . HIS B 1 90  ? 53.436 19.994  -14.237 1.00 63.78  ? 107 HIS B CA  1 
ATOM   2744 C C   . HIS B 1 90  ? 52.647 19.025  -15.105 1.00 58.27  ? 107 HIS B C   1 
ATOM   2745 O O   . HIS B 1 90  ? 51.653 18.449  -14.647 1.00 52.50  ? 107 HIS B O   1 
ATOM   2746 C CB  . HIS B 1 90  ? 52.819 21.386  -14.290 1.00 67.47  ? 107 HIS B CB  1 
ATOM   2747 C CG  . HIS B 1 90  ? 53.437 22.338  -13.317 1.00 74.15  ? 107 HIS B CG  1 
ATOM   2748 N ND1 . HIS B 1 90  ? 54.474 23.176  -13.663 1.00 77.66  ? 107 HIS B ND1 1 
ATOM   2749 C CD2 . HIS B 1 90  ? 53.222 22.531  -11.995 1.00 78.01  ? 107 HIS B CD2 1 
ATOM   2750 C CE1 . HIS B 1 90  ? 54.839 23.880  -12.608 1.00 74.86  ? 107 HIS B CE1 1 
ATOM   2751 N NE2 . HIS B 1 90  ? 54.097 23.505  -11.582 1.00 81.47  ? 107 HIS B NE2 1 
ATOM   2752 N N   . GLU B 1 91  ? 53.033 18.863  -16.366 1.00 56.05  ? 108 GLU B N   1 
ATOM   2753 C CA  . GLU B 1 91  ? 52.345 17.892  -17.199 1.00 56.68  ? 108 GLU B CA  1 
ATOM   2754 C C   . GLU B 1 91  ? 52.618 16.482  -16.702 1.00 51.26  ? 108 GLU B C   1 
ATOM   2755 O O   . GLU B 1 91  ? 51.718 15.636  -16.679 1.00 49.72  ? 108 GLU B O   1 
ATOM   2756 C CB  . GLU B 1 91  ? 52.787 18.035  -18.651 1.00 60.90  ? 108 GLU B CB  1 
ATOM   2757 C CG  . GLU B 1 91  ? 52.875 19.476  -19.138 1.00 77.46  ? 108 GLU B CG  1 
ATOM   2758 C CD  . GLU B 1 91  ? 53.370 19.572  -20.573 1.00 96.46  ? 108 GLU B CD  1 
ATOM   2759 O OE1 . GLU B 1 91  ? 53.742 18.521  -21.143 1.00 91.76  ? 108 GLU B OE1 1 
ATOM   2760 O OE2 . GLU B 1 91  ? 53.406 20.697  -21.121 1.00 96.80  ? 108 GLU B OE2 1 
ATOM   2761 N N   . LEU B 1 92  ? 53.859 16.218  -16.297 1.00 48.77  ? 109 LEU B N   1 
ATOM   2762 C CA  . LEU B 1 92  ? 54.195 14.927  -15.711 1.00 50.12  ? 109 LEU B CA  1 
ATOM   2763 C C   . LEU B 1 92  ? 53.471 14.724  -14.385 1.00 47.58  ? 109 LEU B C   1 
ATOM   2764 O O   . LEU B 1 92  ? 52.958 13.639  -14.103 1.00 44.99  ? 109 LEU B O   1 
ATOM   2765 C CB  . LEU B 1 92  ? 55.703 14.821  -15.498 1.00 46.33  ? 109 LEU B CB  1 
ATOM   2766 C CG  . LEU B 1 92  ? 56.574 14.628  -16.740 1.00 57.75  ? 109 LEU B CG  1 
ATOM   2767 C CD1 . LEU B 1 92  ? 58.036 14.581  -16.353 1.00 52.81  ? 109 LEU B CD1 1 
ATOM   2768 C CD2 . LEU B 1 92  ? 56.182 13.357  -17.467 1.00 51.54  ? 109 LEU B CD2 1 
ATOM   2769 N N   . LEU B 1 93  ? 53.435 15.753  -13.549 1.00 44.78  ? 110 LEU B N   1 
ATOM   2770 C CA  . LEU B 1 93  ? 52.744 15.617  -12.283 1.00 44.76  ? 110 LEU B CA  1 
ATOM   2771 C C   . LEU B 1 93  ? 51.292 15.241  -12.515 1.00 45.71  ? 110 LEU B C   1 
ATOM   2772 O O   . LEU B 1 93  ? 50.745 14.376  -11.821 1.00 39.70  ? 110 LEU B O   1 
ATOM   2773 C CB  . LEU B 1 93  ? 52.881 16.915  -11.500 1.00 48.63  ? 110 LEU B CB  1 
ATOM   2774 C CG  . LEU B 1 93  ? 52.251 16.907  -10.117 1.00 46.80  ? 110 LEU B CG  1 
ATOM   2775 C CD1 . LEU B 1 93  ? 52.770 15.756  -9.275  1.00 47.67  ? 110 LEU B CD1 1 
ATOM   2776 C CD2 . LEU B 1 93  ? 52.580 18.236  -9.440  1.00 58.50  ? 110 LEU B CD2 1 
ATOM   2777 N N   . ALA B 1 94  ? 50.655 15.873  -13.503 1.00 43.96  ? 111 ALA B N   1 
ATOM   2778 C CA  . ALA B 1 94  ? 49.259 15.570  -13.794 1.00 45.85  ? 111 ALA B CA  1 
ATOM   2779 C C   . ALA B 1 94  ? 49.092 14.134  -14.243 1.00 41.22  ? 111 ALA B C   1 
ATOM   2780 O O   . ALA B 1 94  ? 48.116 13.466  -13.883 1.00 44.76  ? 111 ALA B O   1 
ATOM   2781 C CB  . ALA B 1 94  ? 48.731 16.516  -14.869 1.00 46.04  ? 111 ALA B CB  1 
ATOM   2782 N N   . LEU B 1 95  ? 50.035 13.645  -15.038 1.00 44.86  ? 112 LEU B N   1 
ATOM   2783 C CA  . LEU B 1 95  ? 49.986 12.266  -15.491 1.00 48.03  ? 112 LEU B CA  1 
ATOM   2784 C C   . LEU B 1 95  ? 50.050 11.306  -14.312 1.00 42.22  ? 112 LEU B C   1 
ATOM   2785 O O   . LEU B 1 95  ? 49.209 10.410  -14.175 1.00 42.27  ? 112 LEU B O   1 
ATOM   2786 C CB  . LEU B 1 95  ? 51.145 12.036  -16.453 1.00 47.42  ? 112 LEU B CB  1 
ATOM   2787 C CG  . LEU B 1 95  ? 51.262 10.713  -17.188 1.00 51.07  ? 112 LEU B CG  1 
ATOM   2788 C CD1 . LEU B 1 95  ? 50.158 10.553  -18.213 1.00 61.80  ? 112 LEU B CD1 1 
ATOM   2789 C CD2 . LEU B 1 95  ? 52.630 10.697  -17.866 1.00 56.09  ? 112 LEU B CD2 1 
ATOM   2790 N N   . VAL B 1 96  ? 51.020 11.513  -13.424 1.00 39.94  ? 113 VAL B N   1 
ATOM   2791 C CA  . VAL B 1 96  ? 51.157 10.663  -12.248 1.00 42.18  ? 113 VAL B CA  1 
ATOM   2792 C C   . VAL B 1 96  ? 49.885 10.707  -11.405 1.00 40.26  ? 113 VAL B C   1 
ATOM   2793 O O   . VAL B 1 96  ? 49.415 9.677   -10.916 1.00 35.67  ? 113 VAL B O   1 
ATOM   2794 C CB  . VAL B 1 96  ? 52.390 11.094  -11.438 1.00 38.91  ? 113 VAL B CB  1 
ATOM   2795 C CG1 . VAL B 1 96  ? 52.437 10.373  -10.141 1.00 38.71  ? 113 VAL B CG1 1 
ATOM   2796 C CG2 . VAL B 1 96  ? 53.644 10.829  -12.225 1.00 44.05  ? 113 VAL B CG2 1 
ATOM   2797 N N   . ARG B 1 97  ? 49.279 11.891  -11.261 1.00 39.33  ? 114 ARG B N   1 
ATOM   2798 C CA  . ARG B 1 97  ? 48.080 11.995  -10.430 1.00 42.96  ? 114 ARG B CA  1 
ATOM   2799 C C   . ARG B 1 97  ? 46.875 11.365  -11.105 1.00 41.31  ? 114 ARG B C   1 
ATOM   2800 O O   . ARG B 1 97  ? 45.955 10.928  -10.419 1.00 37.27  ? 114 ARG B O   1 
ATOM   2801 C CB  . ARG B 1 97  ? 47.800 13.454  -10.080 1.00 36.95  ? 114 ARG B CB  1 
ATOM   2802 C CG  . ARG B 1 97  ? 48.845 14.016  -9.118  1.00 40.53  ? 114 ARG B CG  1 
ATOM   2803 C CD  . ARG B 1 97  ? 48.635 15.485  -8.766  1.00 50.01  ? 114 ARG B CD  1 
ATOM   2804 N NE  . ARG B 1 97  ? 49.448 15.887  -7.622  1.00 50.65  ? 114 ARG B NE  1 
ATOM   2805 C CZ  . ARG B 1 97  ? 49.744 17.144  -7.301  1.00 63.82  ? 114 ARG B CZ  1 
ATOM   2806 N NH1 . ARG B 1 97  ? 49.232 18.171  -7.969  1.00 51.15  ? 114 ARG B NH1 1 
ATOM   2807 N NH2 . ARG B 1 97  ? 50.549 17.378  -6.263  1.00 54.29  ? 114 ARG B NH2 1 
ATOM   2808 N N   . ASP B 1 98  ? 46.847 11.300  -12.436 1.00 40.57  ? 115 ASP B N   1 
ATOM   2809 C CA  . ASP B 1 98  ? 45.710 10.657  -13.090 1.00 41.87  ? 115 ASP B CA  1 
ATOM   2810 C C   . ASP B 1 98  ? 45.768 9.129   -13.049 1.00 42.34  ? 115 ASP B C   1 
ATOM   2811 O O   . ASP B 1 98  ? 44.784 8.459   -13.410 1.00 40.57  ? 115 ASP B O   1 
ATOM   2812 C CB  . ASP B 1 98  ? 45.573 11.120  -14.542 1.00 53.22  ? 115 ASP B CB  1 
ATOM   2813 C CG  . ASP B 1 98  ? 44.198 10.787  -15.113 1.00 66.23  ? 115 ASP B CG  1 
ATOM   2814 O OD1 . ASP B 1 98  ? 43.175 11.206  -14.488 1.00 59.46  ? 115 ASP B OD1 1 
ATOM   2815 O OD2 . ASP B 1 98  ? 44.143 10.070  -16.145 1.00 64.06  ? 115 ASP B OD2 1 
ATOM   2816 N N   . ILE B 1 99  ? 46.869 8.541   -12.600 1.00 36.61  ? 116 ILE B N   1 
ATOM   2817 C CA  . ILE B 1 99  ? 46.892 7.089   -12.512 1.00 34.15  ? 116 ILE B CA  1 
ATOM   2818 C C   . ILE B 1 99  ? 45.717 6.606   -11.669 1.00 38.99  ? 116 ILE B C   1 
ATOM   2819 O O   . ILE B 1 99  ? 45.091 5.583   -11.982 1.00 38.71  ? 116 ILE B O   1 
ATOM   2820 C CB  . ILE B 1 99  ? 48.235 6.619   -11.939 1.00 34.32  ? 116 ILE B CB  1 
ATOM   2821 C CG1 . ILE B 1 99  ? 49.359 6.990   -12.893 1.00 38.60  ? 116 ILE B CG1 1 
ATOM   2822 C CG2 . ILE B 1 99  ? 48.214 5.132   -11.709 1.00 34.53  ? 116 ILE B CG2 1 
ATOM   2823 C CD1 . ILE B 1 99  ? 50.732 6.695   -12.329 1.00 35.84  ? 116 ILE B CD1 1 
ATOM   2824 N N   . LEU B 1 100 ? 45.394 7.344   -10.594 1.00 36.11  ? 117 LEU B N   1 
ATOM   2825 C CA  . LEU B 1 100 ? 44.216 7.107   -9.753  1.00 38.85  ? 117 LEU B CA  1 
ATOM   2826 C C   . LEU B 1 100 ? 43.509 8.446   -9.586  1.00 40.47  ? 117 LEU B C   1 
ATOM   2827 O O   . LEU B 1 100 ? 43.824 9.205   -8.659  1.00 37.63  ? 117 LEU B O   1 
ATOM   2828 C CB  . LEU B 1 100 ? 44.598 6.529   -8.383  1.00 36.70  ? 117 LEU B CB  1 
ATOM   2829 C CG  . LEU B 1 100 ? 43.445 6.033   -7.495  1.00 41.59  ? 117 LEU B CG  1 
ATOM   2830 C CD1 . LEU B 1 100 ? 42.886 4.757   -8.094  1.00 38.98  ? 117 LEU B CD1 1 
ATOM   2831 C CD2 . LEU B 1 100 ? 43.873 5.790   -6.031  1.00 42.63  ? 117 LEU B CD2 1 
ATOM   2832 N N   . PRO B 1 101 ? 42.527 8.754   -10.441 1.00 37.40  ? 118 PRO B N   1 
ATOM   2833 C CA  . PRO B 1 101 ? 41.801 10.030  -10.330 1.00 33.73  ? 118 PRO B CA  1 
ATOM   2834 C C   . PRO B 1 101 ? 41.161 10.232  -8.959  1.00 34.49  ? 118 PRO B C   1 
ATOM   2835 O O   . PRO B 1 101 ? 40.846 9.284   -8.243  1.00 33.48  ? 118 PRO B O   1 
ATOM   2836 C CB  . PRO B 1 101 ? 40.720 9.912   -11.416 1.00 34.38  ? 118 PRO B CB  1 
ATOM   2837 C CG  . PRO B 1 101 ? 41.282 8.971   -12.400 1.00 42.76  ? 118 PRO B CG  1 
ATOM   2838 C CD  . PRO B 1 101 ? 42.096 7.981   -11.615 1.00 37.72  ? 118 PRO B CD  1 
ATOM   2839 N N   . ALA B 1 102 ? 40.907 11.508  -8.634  1.00 38.11  ? 119 ALA B N   1 
ATOM   2840 C CA  . ALA B 1 102 ? 40.459 11.891  -7.296  1.00 44.26  ? 119 ALA B CA  1 
ATOM   2841 C C   . ALA B 1 102 ? 39.104 11.296  -6.931  1.00 42.26  ? 119 ALA B C   1 
ATOM   2842 O O   . ALA B 1 102 ? 38.867 10.981  -5.766  1.00 39.09  ? 119 ALA B O   1 
ATOM   2843 C CB  . ALA B 1 102 ? 40.386 13.412  -7.195  1.00 48.46  ? 119 ALA B CB  1 
ATOM   2844 N N   . HIS B 1 103 ? 38.209 11.127  -7.897  1.00 38.67  ? 120 HIS B N   1 
ATOM   2845 C CA  . HIS B 1 103 ? 36.869 10.606  -7.624  1.00 40.99  ? 120 HIS B CA  1 
ATOM   2846 C C   . HIS B 1 103 ? 36.825 9.081   -7.547  1.00 35.56  ? 120 HIS B C   1 
ATOM   2847 O O   . HIS B 1 103 ? 35.733 8.511   -7.439  1.00 34.98  ? 120 HIS B O   1 
ATOM   2848 C CB  . HIS B 1 103 ? 35.891 11.116  -8.693  1.00 36.85  ? 120 HIS B CB  1 
ATOM   2849 C CG  . HIS B 1 103 ? 36.102 10.519  -10.051 1.00 33.76  ? 120 HIS B CG  1 
ATOM   2850 N ND1 . HIS B 1 103 ? 37.230 10.764  -10.807 1.00 41.03  ? 120 HIS B ND1 1 
ATOM   2851 C CD2 . HIS B 1 103 ? 35.329 9.688   -10.792 1.00 40.16  ? 120 HIS B CD2 1 
ATOM   2852 C CE1 . HIS B 1 103 ? 37.150 10.099  -11.949 1.00 38.37  ? 120 HIS B CE1 1 
ATOM   2853 N NE2 . HIS B 1 103 ? 36.006 9.439   -11.968 1.00 40.21  ? 120 HIS B NE2 1 
ATOM   2854 N N   . VAL B 1 104 ? 37.985 8.423   -7.595  1.00 33.52  ? 121 VAL B N   1 
ATOM   2855 C CA  . VAL B 1 104 ? 38.107 6.973   -7.672  1.00 29.54  ? 121 VAL B CA  1 
ATOM   2856 C C   . VAL B 1 104 ? 38.897 6.472   -6.466  1.00 31.00  ? 121 VAL B C   1 
ATOM   2857 O O   . VAL B 1 104 ? 39.887 7.087   -6.061  1.00 31.60  ? 121 VAL B O   1 
ATOM   2858 C CB  . VAL B 1 104 ? 38.816 6.553   -8.983  1.00 32.91  ? 121 VAL B CB  1 
ATOM   2859 C CG1 . VAL B 1 104 ? 39.114 5.052   -8.990  1.00 29.84  ? 121 VAL B CG1 1 
ATOM   2860 C CG2 . VAL B 1 104 ? 37.988 6.949   -10.212 1.00 31.70  ? 121 VAL B CG2 1 
ATOM   2861 N N   . ASN B 1 105 ? 38.498 5.329   -5.936  1.00 29.36  ? 122 ASN B N   1 
ATOM   2862 C CA  . ASN B 1 105 ? 39.185 4.681   -4.833  1.00 28.96  ? 122 ASN B CA  1 
ATOM   2863 C C   . ASN B 1 105 ? 39.579 3.277   -5.252  1.00 26.80  ? 122 ASN B C   1 
ATOM   2864 O O   . ASN B 1 105 ? 39.014 2.711   -6.191  1.00 30.11  ? 122 ASN B O   1 
ATOM   2865 C CB  . ASN B 1 105 ? 38.290 4.635   -3.582  1.00 28.96  ? 122 ASN B CB  1 
ATOM   2866 C CG  . ASN B 1 105 ? 37.033 3.838   -3.807  1.00 28.62  ? 122 ASN B CG  1 
ATOM   2867 O OD1 . ASN B 1 105 ? 37.039 2.617   -3.711  1.00 27.34  ? 122 ASN B OD1 1 
ATOM   2868 N ND2 . ASN B 1 105 ? 35.947 4.526   -4.151  1.00 32.72  ? 122 ASN B ND2 1 
ATOM   2869 N N   . CYS B 1 106 ? 40.557 2.745   -4.536  1.00 26.42  ? 123 CYS B N   1 
ATOM   2870 C CA  . CYS B 1 106 ? 41.014 1.370   -4.817  1.00 29.23  ? 123 CYS B CA  1 
ATOM   2871 C C   . CYS B 1 106 ? 41.204 0.599   -3.511  1.00 25.59  ? 123 CYS B C   1 
ATOM   2872 O O   . CYS B 1 106 ? 41.438 1.235   -2.479  1.00 30.74  ? 123 CYS B O   1 
ATOM   2873 C CB  . CYS B 1 106 ? 42.293 1.363   -5.650  1.00 37.19  ? 123 CYS B CB  1 
ATOM   2874 S SG  . CYS B 1 106 ? 43.766 2.008   -4.835  1.00 43.38  ? 123 CYS B SG  1 
ATOM   2875 N N   . LEU B 1 107 ? 40.983 -0.702  -3.552  1.00 22.36  ? 124 LEU B N   1 
ATOM   2876 C CA  . LEU B 1 107 ? 41.303 -1.537  -2.417  1.00 26.47  ? 124 LEU B CA  1 
ATOM   2877 C C   . LEU B 1 107 ? 41.962 -2.797  -2.927  1.00 26.66  ? 124 LEU B C   1 
ATOM   2878 O O   . LEU B 1 107 ? 41.826 -3.159  -4.097  1.00 24.79  ? 124 LEU B O   1 
ATOM   2879 C CB  . LEU B 1 107 ? 40.067 -1.858  -1.585  1.00 29.09  ? 124 LEU B CB  1 
ATOM   2880 C CG  . LEU B 1 107 ? 38.904 -2.611  -2.170  1.00 30.35  ? 124 LEU B CG  1 
ATOM   2881 C CD1 . LEU B 1 107 ? 39.125 -4.106  -2.099  1.00 35.07  ? 124 LEU B CD1 1 
ATOM   2882 C CD2 . LEU B 1 107 ? 37.708 -2.219  -1.313  1.00 26.31  ? 124 LEU B CD2 1 
ATOM   2883 N N   . TYR B 1 108 ? 42.669 -3.468  -2.018  1.00 24.88  ? 125 TYR B N   1 
ATOM   2884 C CA  . TYR B 1 108 ? 43.493 -4.613  -2.347  1.00 25.92  ? 125 TYR B CA  1 
ATOM   2885 C C   . TYR B 1 108 ? 43.064 -5.823  -1.546  1.00 25.75  ? 125 TYR B C   1 
ATOM   2886 O O   . TYR B 1 108 ? 42.880 -5.739  -0.325  1.00 24.65  ? 125 TYR B O   1 
ATOM   2887 C CB  . TYR B 1 108 ? 44.948 -4.283  -2.061  1.00 22.70  ? 125 TYR B CB  1 
ATOM   2888 C CG  . TYR B 1 108 ? 45.402 -3.068  -2.806  1.00 23.83  ? 125 TYR B CG  1 
ATOM   2889 C CD1 . TYR B 1 108 ? 45.776 -3.158  -4.150  1.00 23.78  ? 125 TYR B CD1 1 
ATOM   2890 C CD2 . TYR B 1 108 ? 45.470 -1.838  -2.189  1.00 26.47  ? 125 TYR B CD2 1 
ATOM   2891 C CE1 . TYR B 1 108 ? 46.179 -2.049  -4.845  1.00 21.39  ? 125 TYR B CE1 1 
ATOM   2892 C CE2 . TYR B 1 108 ? 45.885 -0.705  -2.883  1.00 26.69  ? 125 TYR B CE2 1 
ATOM   2893 C CZ  . TYR B 1 108 ? 46.250 -0.827  -4.212  1.00 28.47  ? 125 TYR B CZ  1 
ATOM   2894 O OH  . TYR B 1 108 ? 46.665 0.293   -4.888  1.00 31.51  ? 125 TYR B OH  1 
ATOM   2895 N N   . ILE B 1 109 ? 42.915 -6.942  -2.234  1.00 21.45  ? 126 ILE B N   1 
ATOM   2896 C CA  . ILE B 1 109 ? 42.583 -8.222  -1.621  1.00 23.08  ? 126 ILE B CA  1 
ATOM   2897 C C   . ILE B 1 109 ? 43.517 -9.295  -2.153  1.00 27.51  ? 126 ILE B C   1 
ATOM   2898 O O   . ILE B 1 109 ? 43.677 -9.417  -3.376  1.00 25.41  ? 126 ILE B O   1 
ATOM   2899 C CB  . ILE B 1 109 ? 41.132 -8.640  -1.928  1.00 28.72  ? 126 ILE B CB  1 
ATOM   2900 C CG1 . ILE B 1 109 ? 40.193 -7.448  -1.761  1.00 33.48  ? 126 ILE B CG1 1 
ATOM   2901 C CG2 . ILE B 1 109 ? 40.733 -9.786  -1.010  1.00 31.62  ? 126 ILE B CG2 1 
ATOM   2902 C CD1 . ILE B 1 109 ? 38.733 -7.806  -2.000  1.00 39.42  ? 126 ILE B CD1 1 
ATOM   2903 N N   . ARG B 1 110 ? 44.028 -10.140 -1.259  1.00 25.71  ? 127 ARG B N   1 
ATOM   2904 C CA  . ARG B 1 110 ? 44.910 -11.237 -1.643  1.00 35.39  ? 127 ARG B CA  1 
ATOM   2905 C C   . ARG B 1 110 ? 44.098 -12.476 -1.967  1.00 33.67  ? 127 ARG B C   1 
ATOM   2906 O O   . ARG B 1 110 ? 43.303 -12.929 -1.148  1.00 30.59  ? 127 ARG B O   1 
ATOM   2907 C CB  . ARG B 1 110 ? 45.900 -11.613 -0.544  1.00 34.28  ? 127 ARG B CB  1 
ATOM   2908 C CG  . ARG B 1 110 ? 46.384 -10.477 0.281   1.00 39.92  ? 127 ARG B CG  1 
ATOM   2909 C CD  . ARG B 1 110 ? 47.045 -9.470  -0.562  1.00 41.17  ? 127 ARG B CD  1 
ATOM   2910 N NE  . ARG B 1 110 ? 47.659 -8.431  0.260   1.00 35.20  ? 127 ARG B NE  1 
ATOM   2911 C CZ  . ARG B 1 110 ? 47.959 -7.231  -0.199  1.00 36.94  ? 127 ARG B CZ  1 
ATOM   2912 N NH1 . ARG B 1 110 ? 47.669 -6.873  -1.468  1.00 31.14  ? 127 ARG B NH1 1 
ATOM   2913 N NH2 . ARG B 1 110 ? 48.577 -6.376  0.614   1.00 34.80  ? 127 ARG B NH2 1 
ATOM   2914 N N   . GLN B 1 111 ? 44.326 -13.048 -3.131  1.00 29.61  ? 128 GLN B N   1 
ATOM   2915 C CA  . GLN B 1 111 ? 43.779 -14.374 -3.379  1.00 33.40  ? 128 GLN B CA  1 
ATOM   2916 C C   . GLN B 1 111 ? 44.560 -15.404 -2.562  1.00 35.35  ? 128 GLN B C   1 
ATOM   2917 O O   . GLN B 1 111 ? 45.760 -15.263 -2.334  1.00 36.72  ? 128 GLN B O   1 
ATOM   2918 C CB  . GLN B 1 111 ? 43.817 -14.697 -4.874  1.00 29.56  ? 128 GLN B CB  1 
ATOM   2919 C CG  . GLN B 1 111 ? 45.194 -14.935 -5.406  1.00 34.93  ? 128 GLN B CG  1 
ATOM   2920 C CD  . GLN B 1 111 ? 45.158 -15.344 -6.874  1.00 41.12  ? 128 GLN B CD  1 
ATOM   2921 O OE1 . GLN B 1 111 ? 44.123 -15.232 -7.554  1.00 30.01  ? 128 GLN B OE1 1 
ATOM   2922 N NE2 . GLN B 1 111 ? 46.277 -15.864 -7.349  1.00 34.04  ? 128 GLN B NE2 1 
ATOM   2923 N N   . SER B 1 112 ? 43.859 -16.415 -2.060  1.00 35.50  ? 129 SER B N   1 
ATOM   2924 C CA  . SER B 1 112 ? 44.519 -17.377 -1.184  1.00 43.79  ? 129 SER B CA  1 
ATOM   2925 C C   . SER B 1 112 ? 45.545 -18.225 -1.929  1.00 47.31  ? 129 SER B C   1 
ATOM   2926 O O   . SER B 1 112 ? 46.547 -18.645 -1.338  1.00 46.65  ? 129 SER B O   1 
ATOM   2927 C CB  . SER B 1 112 ? 43.486 -18.296 -0.540  1.00 47.28  ? 129 SER B CB  1 
ATOM   2928 O OG  . SER B 1 112 ? 42.781 -19.012 -1.533  1.00 44.61  ? 129 SER B OG  1 
ATOM   2929 N N   . ALA B 1 113 ? 45.280 -18.544 -3.193  1.00 43.67  ? 130 ALA B N   1 
ATOM   2930 C CA  . ALA B 1 113 ? 46.149 -19.385 -4.008  1.00 46.29  ? 130 ALA B CA  1 
ATOM   2931 C C   . ALA B 1 113 ? 45.754 -19.187 -5.464  1.00 42.16  ? 130 ALA B C   1 
ATOM   2932 O O   . ALA B 1 113 ? 44.649 -18.713 -5.740  1.00 37.20  ? 130 ALA B O   1 
ATOM   2933 C CB  . ALA B 1 113 ? 46.029 -20.867 -3.609  1.00 46.50  ? 130 ALA B CB  1 
ATOM   2934 N N   . PRO B 1 114 ? 46.629 -19.550 -6.416  1.00 51.59  ? 131 PRO B N   1 
ATOM   2935 C CA  . PRO B 1 114 ? 46.284 -19.432 -7.856  1.00 52.99  ? 131 PRO B CA  1 
ATOM   2936 C C   . PRO B 1 114 ? 45.340 -20.546 -8.297  1.00 53.07  ? 131 PRO B C   1 
ATOM   2937 O O   . PRO B 1 114 ? 45.718 -21.611 -8.771  1.00 62.30  ? 131 PRO B O   1 
ATOM   2938 C CB  . PRO B 1 114 ? 47.652 -19.510 -8.535  1.00 57.88  ? 131 PRO B CB  1 
ATOM   2939 C CG  . PRO B 1 114 ? 48.454 -20.382 -7.621  1.00 60.88  ? 131 PRO B CG  1 
ATOM   2940 C CD  . PRO B 1 114 ? 48.010 -20.034 -6.223  1.00 60.25  ? 131 PRO B CD  1 
ATOM   2941 N N   . LEU B 1 115 ? 44.058 -20.304 -8.054  1.00 45.94  ? 132 LEU B N   1 
ATOM   2942 C CA  . LEU B 1 115 ? 42.996 -21.254 -8.326  1.00 46.87  ? 132 LEU B CA  1 
ATOM   2943 C C   . LEU B 1 115 ? 42.109 -20.833 -9.496  1.00 43.64  ? 132 LEU B C   1 
ATOM   2944 O O   . LEU B 1 115 ? 40.990 -21.335 -9.622  1.00 49.80  ? 132 LEU B O   1 
ATOM   2945 C CB  . LEU B 1 115 ? 42.154 -21.444 -7.071  1.00 46.04  ? 132 LEU B CB  1 
ATOM   2946 C CG  . LEU B 1 115 ? 42.851 -22.123 -5.897  1.00 49.19  ? 132 LEU B CG  1 
ATOM   2947 C CD1 . LEU B 1 115 ? 41.976 -22.022 -4.690  1.00 40.88  ? 132 LEU B CD1 1 
ATOM   2948 C CD2 . LEU B 1 115 ? 43.095 -23.578 -6.238  1.00 54.67  ? 132 LEU B CD2 1 
ATOM   2949 N N   . GLY B 1 116 ? 42.557 -19.884 -10.311 1.00 43.73  ? 133 GLY B N   1 
ATOM   2950 C CA  . GLY B 1 116 ? 41.830 -19.489 -11.506 1.00 41.13  ? 133 GLY B CA  1 
ATOM   2951 C C   . GLY B 1 116 ? 40.973 -18.250 -11.308 1.00 34.58  ? 133 GLY B C   1 
ATOM   2952 O O   . GLY B 1 116 ? 40.808 -17.709 -10.207 1.00 37.52  ? 133 GLY B O   1 
ATOM   2953 N N   . LEU B 1 117 ? 40.380 -17.837 -12.426 1.00 30.88  ? 134 LEU B N   1 
ATOM   2954 C CA  . LEU B 1 117 ? 39.630 -16.592 -12.488 1.00 31.29  ? 134 LEU B CA  1 
ATOM   2955 C C   . LEU B 1 117 ? 38.390 -16.641 -11.611 1.00 30.30  ? 134 LEU B C   1 
ATOM   2956 O O   . LEU B 1 117 ? 37.996 -15.630 -11.022 1.00 27.77  ? 134 LEU B O   1 
ATOM   2957 C CB  . LEU B 1 117 ? 39.248 -16.303 -13.944 1.00 33.39  ? 134 LEU B CB  1 
ATOM   2958 C CG  . LEU B 1 117 ? 38.448 -15.031 -14.225 1.00 30.95  ? 134 LEU B CG  1 
ATOM   2959 C CD1 . LEU B 1 117 ? 39.233 -13.834 -13.706 1.00 29.66  ? 134 LEU B CD1 1 
ATOM   2960 C CD2 . LEU B 1 117 ? 38.154 -14.885 -15.766 1.00 31.61  ? 134 LEU B CD2 1 
ATOM   2961 N N   . GLY B 1 118 ? 37.720 -17.784 -11.573 1.00 32.31  ? 135 GLY B N   1 
ATOM   2962 C CA  . GLY B 1 118 ? 36.530 -17.896 -10.763 1.00 31.25  ? 135 GLY B CA  1 
ATOM   2963 C C   . GLY B 1 118 ? 36.841 -17.695 -9.292  1.00 36.67  ? 135 GLY B C   1 
ATOM   2964 O O   . GLY B 1 118 ? 36.098 -17.016 -8.581  1.00 28.48  ? 135 GLY B O   1 
ATOM   2965 N N   . HIS B 1 119 ? 37.962 -18.263 -8.830  1.00 28.96  ? 136 HIS B N   1 
ATOM   2966 C CA  . HIS B 1 119 ? 38.407 -18.040 -7.465  1.00 33.24  ? 136 HIS B CA  1 
ATOM   2967 C C   . HIS B 1 119 ? 38.796 -16.584 -7.255  1.00 29.56  ? 136 HIS B C   1 
ATOM   2968 O O   . HIS B 1 119 ? 38.496 -16.006 -6.215  1.00 27.90  ? 136 HIS B O   1 
ATOM   2969 C CB  . HIS B 1 119 ? 39.590 -18.951 -7.150  1.00 35.55  ? 136 HIS B CB  1 
ATOM   2970 C CG  . HIS B 1 119 ? 40.070 -18.846 -5.736  1.00 36.16  ? 136 HIS B CG  1 
ATOM   2971 N ND1 . HIS B 1 119 ? 39.363 -19.371 -4.677  1.00 39.66  ? 136 HIS B ND1 1 
ATOM   2972 C CD2 . HIS B 1 119 ? 41.175 -18.271 -5.204  1.00 33.40  ? 136 HIS B CD2 1 
ATOM   2973 C CE1 . HIS B 1 119 ? 40.016 -19.131 -3.555  1.00 40.34  ? 136 HIS B CE1 1 
ATOM   2974 N NE2 . HIS B 1 119 ? 41.121 -18.470 -3.849  1.00 39.25  ? 136 HIS B NE2 1 
ATOM   2975 N N   . ALA B 1 120 ? 39.457 -15.971 -8.242  1.00 30.82  ? 137 ALA B N   1 
ATOM   2976 C CA  . ALA B 1 120 ? 39.832 -14.572 -8.111  1.00 28.50  ? 137 ALA B CA  1 
ATOM   2977 C C   . ALA B 1 120 ? 38.596 -13.703 -7.982  1.00 27.35  ? 137 ALA B C   1 
ATOM   2978 O O   . ALA B 1 120 ? 38.548 -12.788 -7.153  1.00 28.33  ? 137 ALA B O   1 
ATOM   2979 C CB  . ALA B 1 120 ? 40.659 -14.133 -9.313  1.00 29.29  ? 137 ALA B CB  1 
ATOM   2980 N N   . VAL B 1 121 ? 37.573 -13.990 -8.774  1.00 26.86  ? 138 VAL B N   1 
ATOM   2981 C CA  . VAL B 1 121 ? 36.351 -13.198 -8.689  1.00 29.70  ? 138 VAL B CA  1 
ATOM   2982 C C   . VAL B 1 121 ? 35.684 -13.392 -7.327  1.00 27.72  ? 138 VAL B C   1 
ATOM   2983 O O   . VAL B 1 121 ? 35.284 -12.426 -6.671  1.00 32.36  ? 138 VAL B O   1 
ATOM   2984 C CB  . VAL B 1 121 ? 35.401 -13.563 -9.836  1.00 26.38  ? 138 VAL B CB  1 
ATOM   2985 C CG1 . VAL B 1 121 ? 34.026 -12.989 -9.562  1.00 28.80  ? 138 VAL B CG1 1 
ATOM   2986 C CG2 . VAL B 1 121 ? 35.939 -13.050 -11.170 1.00 30.02  ? 138 VAL B CG2 1 
ATOM   2987 N N   . LEU B 1 122 ? 35.565 -14.643 -6.874  1.00 29.56  ? 139 LEU B N   1 
ATOM   2988 C CA  . LEU B 1 122 ? 34.973 -14.899 -5.562  1.00 30.38  ? 139 LEU B CA  1 
ATOM   2989 C C   . LEU B 1 122 ? 35.744 -14.216 -4.426  1.00 31.87  ? 139 LEU B C   1 
ATOM   2990 O O   . LEU B 1 122 ? 35.127 -13.726 -3.476  1.00 27.25  ? 139 LEU B O   1 
ATOM   2991 C CB  . LEU B 1 122 ? 34.887 -16.407 -5.346  1.00 34.25  ? 139 LEU B CB  1 
ATOM   2992 C CG  . LEU B 1 122 ? 34.244 -16.907 -4.050  1.00 38.54  ? 139 LEU B CG  1 
ATOM   2993 C CD1 . LEU B 1 122 ? 32.816 -16.408 -3.846  1.00 32.59  ? 139 LEU B CD1 1 
ATOM   2994 C CD2 . LEU B 1 122 ? 34.263 -18.415 -4.110  1.00 38.95  ? 139 LEU B CD2 1 
ATOM   2995 N N   . THR B 1 123 ? 37.078 -14.107 -4.543  1.00 30.84  ? 140 THR B N   1 
ATOM   2996 C CA  . THR B 1 123 ? 37.880 -13.398 -3.549  1.00 31.26  ? 140 THR B CA  1 
ATOM   2997 C C   . THR B 1 123 ? 37.390 -11.972 -3.317  1.00 30.45  ? 140 THR B C   1 
ATOM   2998 O O   . THR B 1 123 ? 37.574 -11.402 -2.222  1.00 29.86  ? 140 THR B O   1 
ATOM   2999 C CB  . THR B 1 123 ? 39.339 -13.382 -4.003  1.00 29.40  ? 140 THR B CB  1 
ATOM   3000 O OG1 . THR B 1 123 ? 39.851 -14.718 -3.955  1.00 32.27  ? 140 THR B OG1 1 
ATOM   3001 C CG2 . THR B 1 123 ? 40.168 -12.504 -3.123  1.00 31.22  ? 140 THR B CG2 1 
ATOM   3002 N N   . ALA B 1 124 ? 36.758 -11.389 -4.307  1.00 26.18  ? 141 ALA B N   1 
ATOM   3003 C CA  . ALA B 1 124 ? 36.311 -10.007 -4.239  1.00 27.78  ? 141 ALA B CA  1 
ATOM   3004 C C   . ALA B 1 124 ? 34.950 -9.832  -3.565  1.00 26.62  ? 141 ALA B C   1 
ATOM   3005 O O   . ALA B 1 124 ? 34.570 -8.695  -3.264  1.00 29.31  ? 141 ALA B O   1 
ATOM   3006 C CB  . ALA B 1 124 ? 36.255 -9.430  -5.667  1.00 27.08  ? 141 ALA B CB  1 
ATOM   3007 N N   . ALA B 1 125 ? 34.232 -10.914 -3.273  1.00 30.30  ? 142 ALA B N   1 
ATOM   3008 C CA  . ALA B 1 125 ? 32.892 -10.775 -2.708  1.00 34.08  ? 142 ALA B CA  1 
ATOM   3009 C C   . ALA B 1 125 ? 32.820 -9.857  -1.483  1.00 30.22  ? 142 ALA B C   1 
ATOM   3010 O O   . ALA B 1 125 ? 31.883 -9.045  -1.417  1.00 30.97  ? 142 ALA B O   1 
ATOM   3011 C CB  . ALA B 1 125 ? 32.329 -12.168 -2.370  1.00 34.83  ? 142 ALA B CB  1 
ATOM   3012 N N   . PRO B 1 126 ? 33.742 -9.887  -0.519  1.00 30.01  ? 143 PRO B N   1 
ATOM   3013 C CA  . PRO B 1 126 ? 33.593 -8.977  0.639   1.00 35.76  ? 143 PRO B CA  1 
ATOM   3014 C C   . PRO B 1 126 ? 33.617 -7.497  0.257   1.00 34.12  ? 143 PRO B C   1 
ATOM   3015 O O   . PRO B 1 126 ? 33.104 -6.664  1.015   1.00 34.82  ? 143 PRO B O   1 
ATOM   3016 C CB  . PRO B 1 126 ? 34.778 -9.349  1.548   1.00 31.52  ? 143 PRO B CB  1 
ATOM   3017 C CG  . PRO B 1 126 ? 35.168 -10.705 1.138   1.00 31.34  ? 143 PRO B CG  1 
ATOM   3018 C CD  . PRO B 1 126 ? 34.893 -10.788 -0.349  1.00 25.92  ? 143 PRO B CD  1 
ATOM   3019 N N   . ALA B 1 127 ? 34.230 -7.136  -0.869  1.00 32.14  ? 144 ALA B N   1 
ATOM   3020 C CA  . ALA B 1 127 ? 34.251 -5.743  -1.313  1.00 31.90  ? 144 ALA B CA  1 
ATOM   3021 C C   . ALA B 1 127 ? 33.054 -5.376  -2.187  1.00 36.51  ? 144 ALA B C   1 
ATOM   3022 O O   . ALA B 1 127 ? 32.661 -4.197  -2.249  1.00 37.64  ? 144 ALA B O   1 
ATOM   3023 C CB  . ALA B 1 127 ? 35.535 -5.445  -2.107  1.00 34.37  ? 144 ALA B CB  1 
ATOM   3024 N N   . VAL B 1 128 ? 32.471 -6.351  -2.870  1.00 35.16  ? 145 VAL B N   1 
ATOM   3025 C CA  . VAL B 1 128 ? 31.367 -6.068  -3.785  1.00 35.24  ? 145 VAL B CA  1 
ATOM   3026 C C   . VAL B 1 128 ? 30.026 -6.047  -3.059  1.00 35.88  ? 145 VAL B C   1 
ATOM   3027 O O   . VAL B 1 128 ? 29.158 -5.224  -3.362  1.00 38.06  ? 145 VAL B O   1 
ATOM   3028 C CB  . VAL B 1 128 ? 31.370 -7.110  -4.910  1.00 32.04  ? 145 VAL B CB  1 
ATOM   3029 C CG1 . VAL B 1 128 ? 30.057 -7.042  -5.715  1.00 32.01  ? 145 VAL B CG1 1 
ATOM   3030 C CG2 . VAL B 1 128 ? 32.579 -6.908  -5.807  1.00 36.75  ? 145 VAL B CG2 1 
ATOM   3031 N N   . GLY B 1 129 ? 29.828 -6.932  -2.093  1.00 37.80  ? 146 GLY B N   1 
ATOM   3032 C CA  . GLY B 1 129 ? 28.514 -6.964  -1.481  1.00 43.19  ? 146 GLY B CA  1 
ATOM   3033 C C   . GLY B 1 129 ? 27.482 -7.525  -2.449  1.00 40.57  ? 146 GLY B C   1 
ATOM   3034 O O   . GLY B 1 129 ? 27.759 -8.432  -3.237  1.00 44.65  ? 146 GLY B O   1 
ATOM   3035 N N   . ASN B 1 130 ? 26.261 -7.021  -2.333  1.00 41.39  ? 147 ASN B N   1 
ATOM   3036 C CA  . ASN B 1 130 ? 25.144 -7.426  -3.193  1.00 57.66  ? 147 ASN B CA  1 
ATOM   3037 C C   . ASN B 1 130 ? 24.908 -6.385  -4.293  1.00 55.85  ? 147 ASN B C   1 
ATOM   3038 O O   . ASN B 1 130 ? 23.810 -5.872  -4.484  1.00 61.39  ? 147 ASN B O   1 
ATOM   3039 C CB  . ASN B 1 130 ? 23.891 -7.638  -2.336  1.00 50.34  ? 147 ASN B CB  1 
ATOM   3040 C CG  . ASN B 1 130 ? 22.972 -8.704  -2.896  1.00 67.53  ? 147 ASN B CG  1 
ATOM   3041 O OD1 . ASN B 1 130 ? 23.422 -9.652  -3.539  1.00 66.11  ? 147 ASN B OD1 1 
ATOM   3042 N ND2 . ASN B 1 130 ? 21.682 -8.595  -2.591  1.00 93.27  ? 147 ASN B ND2 1 
ATOM   3043 N N   . GLU B 1 131 ? 25.955 -6.097  -5.050  1.00 50.07  ? 148 GLU B N   1 
ATOM   3044 C CA  . GLU B 1 131 ? 25.866 -5.142  -6.142  1.00 48.02  ? 148 GLU B CA  1 
ATOM   3045 C C   . GLU B 1 131 ? 26.368 -5.802  -7.411  1.00 37.96  ? 148 GLU B C   1 
ATOM   3046 O O   . GLU B 1 131 ? 27.272 -6.637  -7.352  1.00 31.68  ? 148 GLU B O   1 
ATOM   3047 C CB  . GLU B 1 131 ? 26.748 -3.897  -5.940  1.00 39.46  ? 148 GLU B CB  1 
ATOM   3048 C CG  . GLU B 1 131 ? 26.521 -3.042  -4.725  1.00 47.72  ? 148 GLU B CG  1 
ATOM   3049 C CD  . GLU B 1 131 ? 27.391 -1.800  -4.760  1.00 47.41  ? 148 GLU B CD  1 
ATOM   3050 O OE1 . GLU B 1 131 ? 27.884 -1.412  -5.865  1.00 38.94  ? 148 GLU B OE1 1 
ATOM   3051 O OE2 . GLU B 1 131 ? 27.590 -1.210  -3.677  1.00 49.81  ? 148 GLU B OE2 1 
ATOM   3052 N N   . PRO B 1 132 ? 25.844 -5.412  -8.566  1.00 36.32  ? 149 PRO B N   1 
ATOM   3053 C CA  . PRO B 1 132 ? 26.454 -5.847  -9.825  1.00 31.75  ? 149 PRO B CA  1 
ATOM   3054 C C   . PRO B 1 132 ? 27.819 -5.204  -9.946  1.00 30.09  ? 149 PRO B C   1 
ATOM   3055 O O   . PRO B 1 132 ? 28.033 -4.089  -9.471  1.00 31.20  ? 149 PRO B O   1 
ATOM   3056 C CB  . PRO B 1 132 ? 25.477 -5.331  -10.894 1.00 35.30  ? 149 PRO B CB  1 
ATOM   3057 C CG  . PRO B 1 132 ? 24.889 -4.092  -10.268 1.00 41.60  ? 149 PRO B CG  1 
ATOM   3058 C CD  . PRO B 1 132 ? 24.761 -4.433  -8.789  1.00 39.17  ? 149 PRO B CD  1 
ATOM   3059 N N   . PHE B 1 133 ? 28.750 -5.921  -10.580 1.00 30.04  ? 150 PHE B N   1 
ATOM   3060 C CA  . PHE B 1 133 ? 30.133 -5.469  -10.648 1.00 27.95  ? 150 PHE B CA  1 
ATOM   3061 C C   . PHE B 1 133 ? 30.749 -5.877  -11.988 1.00 29.46  ? 150 PHE B C   1 
ATOM   3062 O O   . PHE B 1 133 ? 30.277 -6.783  -12.673 1.00 27.00  ? 150 PHE B O   1 
ATOM   3063 C CB  . PHE B 1 133 ? 30.960 -6.047  -9.475  1.00 25.56  ? 150 PHE B CB  1 
ATOM   3064 C CG  . PHE B 1 133 ? 31.061 -7.530  -9.499  1.00 26.18  ? 150 PHE B CG  1 
ATOM   3065 C CD1 . PHE B 1 133 ? 30.001 -8.322  -9.118  1.00 26.23  ? 150 PHE B CD1 1 
ATOM   3066 C CD2 . PHE B 1 133 ? 32.212 -8.156  -9.920  1.00 26.32  ? 150 PHE B CD2 1 
ATOM   3067 C CE1 . PHE B 1 133 ? 30.108 -9.714  -9.173  1.00 24.73  ? 150 PHE B CE1 1 
ATOM   3068 C CE2 . PHE B 1 133 ? 32.303 -9.535  -9.966  1.00 26.33  ? 150 PHE B CE2 1 
ATOM   3069 C CZ  . PHE B 1 133 ? 31.257 -10.304 -9.607  1.00 28.11  ? 150 PHE B CZ  1 
ATOM   3070 N N   . ALA B 1 134 ? 31.809 -5.186  -12.359 1.00 24.55  ? 151 ALA B N   1 
ATOM   3071 C CA  . ALA B 1 134 ? 32.544 -5.477  -13.575 1.00 26.55  ? 151 ALA B CA  1 
ATOM   3072 C C   . ALA B 1 134 ? 33.764 -6.309  -13.242 1.00 23.17  ? 151 ALA B C   1 
ATOM   3073 O O   . ALA B 1 134 ? 34.266 -6.259  -12.119 1.00 26.11  ? 151 ALA B O   1 
ATOM   3074 C CB  . ALA B 1 134 ? 32.988 -4.200  -14.273 1.00 23.50  ? 151 ALA B CB  1 
ATOM   3075 N N   . VAL B 1 135 ? 34.214 -7.087  -14.228 1.00 25.12  ? 152 VAL B N   1 
ATOM   3076 C CA  . VAL B 1 135 ? 35.483 -7.803  -14.208 1.00 23.63  ? 152 VAL B CA  1 
ATOM   3077 C C   . VAL B 1 135 ? 36.265 -7.467  -15.473 1.00 28.62  ? 152 VAL B C   1 
ATOM   3078 O O   . VAL B 1 135 ? 35.730 -7.583  -16.583 1.00 25.52  ? 152 VAL B O   1 
ATOM   3079 C CB  . VAL B 1 135 ? 35.258 -9.320  -14.099 1.00 23.26  ? 152 VAL B CB  1 
ATOM   3080 C CG1 . VAL B 1 135 ? 36.602 -10.041 -14.026 1.00 25.80  ? 152 VAL B CG1 1 
ATOM   3081 C CG2 . VAL B 1 135 ? 34.421 -9.653  -12.821 1.00 22.39  ? 152 VAL B CG2 1 
ATOM   3082 N N   . LEU B 1 136 ? 37.535 -7.072  -15.316 1.00 24.27  ? 153 LEU B N   1 
ATOM   3083 C CA  . LEU B 1 136 ? 38.388 -6.753  -16.458 1.00 23.08  ? 153 LEU B CA  1 
ATOM   3084 C C   . LEU B 1 136 ? 39.707 -7.495  -16.338 1.00 22.95  ? 153 LEU B C   1 
ATOM   3085 O O   . LEU B 1 136 ? 40.383 -7.417  -15.303 1.00 25.10  ? 153 LEU B O   1 
ATOM   3086 C CB  . LEU B 1 136 ? 38.665 -5.247  -16.595 1.00 22.10  ? 153 LEU B CB  1 
ATOM   3087 C CG  . LEU B 1 136 ? 37.454 -4.339  -16.811 1.00 25.96  ? 153 LEU B CG  1 
ATOM   3088 C CD1 . LEU B 1 136 ? 36.794 -3.957  -15.481 1.00 27.11  ? 153 LEU B CD1 1 
ATOM   3089 C CD2 . LEU B 1 136 ? 37.864 -3.113  -17.616 1.00 27.72  ? 153 LEU B CD2 1 
ATOM   3090 N N   . LEU B 1 137 ? 40.056 -8.220  -17.394 1.00 24.77  ? 154 LEU B N   1 
ATOM   3091 C CA  . LEU B 1 137 ? 41.312 -8.956  -17.483 1.00 22.93  ? 154 LEU B CA  1 
ATOM   3092 C C   . LEU B 1 137 ? 42.284 -8.116  -18.296 1.00 24.58  ? 154 LEU B C   1 
ATOM   3093 O O   . LEU B 1 137 ? 42.096 -7.918  -19.504 1.00 26.30  ? 154 LEU B O   1 
ATOM   3094 C CB  . LEU B 1 137 ? 41.094 -10.332 -18.100 1.00 25.64  ? 154 LEU B CB  1 
ATOM   3095 C CG  . LEU B 1 137 ? 39.843 -11.073 -17.632 1.00 24.83  ? 154 LEU B CG  1 
ATOM   3096 C CD1 . LEU B 1 137 ? 39.835 -12.443 -18.320 1.00 30.02  ? 154 LEU B CD1 1 
ATOM   3097 C CD2 . LEU B 1 137 ? 39.815 -11.205 -16.083 1.00 28.55  ? 154 LEU B CD2 1 
ATOM   3098 N N   . ALA B 1 138 ? 43.313 -7.596  -17.631 1.00 25.62  ? 155 ALA B N   1 
ATOM   3099 C CA  . ALA B 1 138 ? 44.136 -6.591  -18.293 1.00 24.88  ? 155 ALA B CA  1 
ATOM   3100 C C   . ALA B 1 138 ? 44.894 -7.172  -19.486 1.00 26.62  ? 155 ALA B C   1 
ATOM   3101 O O   . ALA B 1 138 ? 45.311 -6.408  -20.362 1.00 25.00  ? 155 ALA B O   1 
ATOM   3102 C CB  . ALA B 1 138 ? 45.091 -5.957  -17.281 1.00 22.72  ? 155 ALA B CB  1 
ATOM   3103 N N   . ASP B 1 139 ? 45.067 -8.500  -19.535 1.00 24.08  ? 156 ASP B N   1 
ATOM   3104 C CA  . ASP B 1 139 ? 45.733 -9.149  -20.665 1.00 29.71  ? 156 ASP B CA  1 
ATOM   3105 C C   . ASP B 1 139 ? 44.976 -8.928  -21.975 1.00 30.14  ? 156 ASP B C   1 
ATOM   3106 O O   . ASP B 1 139 ? 45.579 -8.964  -23.062 1.00 30.98  ? 156 ASP B O   1 
ATOM   3107 C CB  . ASP B 1 139 ? 45.886 -10.650 -20.386 1.00 27.71  ? 156 ASP B CB  1 
ATOM   3108 C CG  . ASP B 1 139 ? 47.311 -11.038 -19.980 1.00 34.82  ? 156 ASP B CG  1 
ATOM   3109 O OD1 . ASP B 1 139 ? 48.206 -10.174 -20.061 1.00 35.05  ? 156 ASP B OD1 1 
ATOM   3110 O OD2 . ASP B 1 139 ? 47.550 -12.213 -19.621 1.00 36.46  ? 156 ASP B OD2 1 
ATOM   3111 N N   . ASP B 1 140 ? 43.668 -8.714  -21.899 1.00 25.17  ? 157 ASP B N   1 
ATOM   3112 C CA  . ASP B 1 140 ? 42.894 -8.294  -23.053 1.00 26.90  ? 157 ASP B CA  1 
ATOM   3113 C C   . ASP B 1 140 ? 42.960 -6.781  -23.111 1.00 30.72  ? 157 ASP B C   1 
ATOM   3114 O O   . ASP B 1 140 ? 42.200 -6.080  -22.438 1.00 24.38  ? 157 ASP B O   1 
ATOM   3115 C CB  . ASP B 1 140 ? 41.459 -8.785  -22.990 1.00 29.69  ? 157 ASP B CB  1 
ATOM   3116 C CG  . ASP B 1 140 ? 41.332 -10.245 -23.384 1.00 33.91  ? 157 ASP B CG  1 
ATOM   3117 O OD1 . ASP B 1 140 ? 42.249 -10.779 -24.041 1.00 35.39  ? 157 ASP B OD1 1 
ATOM   3118 O OD2 . ASP B 1 140 ? 40.323 -10.876 -23.009 1.00 39.75  ? 157 ASP B OD2 1 
ATOM   3119 N N   . LEU B 1 141 ? 43.888 -6.271  -23.907 1.00 26.35  ? 158 LEU B N   1 
ATOM   3120 C CA  . LEU B 1 141 ? 44.029 -4.838  -24.064 1.00 25.00  ? 158 LEU B CA  1 
ATOM   3121 C C   . LEU B 1 141 ? 43.122 -4.439  -25.214 1.00 30.58  ? 158 LEU B C   1 
ATOM   3122 O O   . LEU B 1 141 ? 43.275 -4.942  -26.341 1.00 27.13  ? 158 LEU B O   1 
ATOM   3123 C CB  . LEU B 1 141 ? 45.481 -4.458  -24.313 1.00 25.91  ? 158 LEU B CB  1 
ATOM   3124 C CG  . LEU B 1 141 ? 45.858 -2.987  -24.126 1.00 27.46  ? 158 LEU B CG  1 
ATOM   3125 C CD1 . LEU B 1 141 ? 47.312 -2.907  -24.505 1.00 35.60  ? 158 LEU B CD1 1 
ATOM   3126 C CD2 . LEU B 1 141 ? 45.028 -2.058  -24.930 1.00 36.22  ? 158 LEU B CD2 1 
ATOM   3127 N N   . ILE B 1 142 ? 42.159 -3.574  -24.936 1.00 29.40  ? 159 ILE B N   1 
ATOM   3128 C CA  . ILE B 1 142 ? 41.160 -3.212  -25.921 1.00 29.84  ? 159 ILE B CA  1 
ATOM   3129 C C   . ILE B 1 142 ? 41.243 -1.726  -26.207 1.00 30.14  ? 159 ILE B C   1 
ATOM   3130 O O   . ILE B 1 142 ? 41.119 -0.905  -25.301 1.00 31.11  ? 159 ILE B O   1 
ATOM   3131 C CB  . ILE B 1 142 ? 39.746 -3.591  -25.478 1.00 30.07  ? 159 ILE B CB  1 
ATOM   3132 C CG1 . ILE B 1 142 ? 39.646 -5.107  -25.290 1.00 31.77  ? 159 ILE B CG1 1 
ATOM   3133 C CG2 . ILE B 1 142 ? 38.767 -3.066  -26.533 1.00 37.84  ? 159 ILE B CG2 1 
ATOM   3134 C CD1 . ILE B 1 142 ? 38.283 -5.570  -24.823 1.00 34.32  ? 159 ILE B CD1 1 
ATOM   3135 N N   . ASP B 1 143 ? 41.431 -1.389  -27.474 1.00 26.72  ? 160 ASP B N   1 
ATOM   3136 C CA  . ASP B 1 143 ? 41.507 -0.009  -27.948 1.00 28.21  ? 160 ASP B CA  1 
ATOM   3137 C C   . ASP B 1 143 ? 40.210 0.277   -28.681 1.00 34.47  ? 160 ASP B C   1 
ATOM   3138 O O   . ASP B 1 143 ? 39.932 -0.358  -29.702 1.00 36.83  ? 160 ASP B O   1 
ATOM   3139 C CB  . ASP B 1 143 ? 42.721 0.158   -28.871 1.00 33.82  ? 160 ASP B CB  1 
ATOM   3140 C CG  . ASP B 1 143 ? 42.926 1.588   -29.352 1.00 32.91  ? 160 ASP B CG  1 
ATOM   3141 O OD1 . ASP B 1 143 ? 42.814 2.526   -28.537 1.00 35.58  ? 160 ASP B OD1 1 
ATOM   3142 O OD2 . ASP B 1 143 ? 43.269 1.765   -30.543 1.00 31.76  ? 160 ASP B OD2 1 
ATOM   3143 N N   . ALA B 1 144 ? 39.414 1.215   -28.155 1.00 32.14  ? 161 ALA B N   1 
ATOM   3144 C CA  . ALA B 1 144 ? 38.051 1.412   -28.636 1.00 32.93  ? 161 ALA B CA  1 
ATOM   3145 C C   . ALA B 1 144 ? 37.655 2.875   -28.568 1.00 37.45  ? 161 ALA B C   1 
ATOM   3146 O O   . ALA B 1 144 ? 38.086 3.596   -27.682 1.00 35.21  ? 161 ALA B O   1 
ATOM   3147 C CB  . ALA B 1 144 ? 37.057 0.596   -27.815 1.00 30.57  ? 161 ALA B CB  1 
ATOM   3148 N N   . ASP B 1 145 ? 36.814 3.303   -29.508 1.00 34.56  ? 162 ASP B N   1 
ATOM   3149 C CA  . ASP B 1 145 ? 36.355 4.686   -29.499 1.00 37.70  ? 162 ASP B CA  1 
ATOM   3150 C C   . ASP B 1 145 ? 35.465 4.946   -28.289 1.00 40.19  ? 162 ASP B C   1 
ATOM   3151 O O   . ASP B 1 145 ? 35.520 6.020   -27.687 1.00 41.34  ? 162 ASP B O   1 
ATOM   3152 C CB  . ASP B 1 145 ? 35.615 5.000   -30.800 1.00 43.57  ? 162 ASP B CB  1 
ATOM   3153 C CG  . ASP B 1 145 ? 36.531 4.959   -32.030 1.00 52.65  ? 162 ASP B CG  1 
ATOM   3154 O OD1 . ASP B 1 145 ? 37.774 5.058   -31.875 1.00 52.29  ? 162 ASP B OD1 1 
ATOM   3155 O OD2 . ASP B 1 145 ? 36.002 4.820   -33.160 1.00 54.61  ? 162 ASP B OD2 1 
ATOM   3156 N N   . THR B 1 146 ? 34.630 3.983   -27.935 1.00 35.94  ? 163 THR B N   1 
ATOM   3157 C CA  A THR B 1 146 ? 33.813 4.035   -26.732 0.65 36.34  ? 163 THR B CA  1 
ATOM   3158 C CA  B THR B 1 146 ? 33.816 4.035   -26.734 0.35 36.29  ? 163 THR B CA  1 
ATOM   3159 C C   . THR B 1 146 ? 34.277 2.938   -25.789 1.00 30.18  ? 163 THR B C   1 
ATOM   3160 O O   . THR B 1 146 ? 34.453 1.797   -26.229 1.00 31.35  ? 163 THR B O   1 
ATOM   3161 C CB  A THR B 1 146 ? 32.321 3.851   -27.075 0.65 35.13  ? 163 THR B CB  1 
ATOM   3162 C CB  B THR B 1 146 ? 32.325 3.855   -27.072 0.35 35.18  ? 163 THR B CB  1 
ATOM   3163 O OG1 A THR B 1 146 ? 31.844 5.015   -27.756 0.65 40.06  ? 163 THR B OG1 1 
ATOM   3164 O OG1 B THR B 1 146 ? 32.112 2.596   -27.720 0.35 33.70  ? 163 THR B OG1 1 
ATOM   3165 C CG2 A THR B 1 146 ? 31.488 3.628   -25.831 0.65 36.82  ? 163 THR B CG2 1 
ATOM   3166 C CG2 B THR B 1 146 ? 31.858 4.954   -27.999 0.35 39.64  ? 163 THR B CG2 1 
ATOM   3167 N N   . PRO B 1 147 ? 34.524 3.233   -24.513 1.00 32.10  ? 164 PRO B N   1 
ATOM   3168 C CA  . PRO B 1 147 ? 35.043 2.196   -23.617 1.00 33.24  ? 164 PRO B CA  1 
ATOM   3169 C C   . PRO B 1 147 ? 34.176 0.953   -23.661 1.00 29.12  ? 164 PRO B C   1 
ATOM   3170 O O   . PRO B 1 147 ? 32.942 1.012   -23.487 1.00 29.98  ? 164 PRO B O   1 
ATOM   3171 C CB  . PRO B 1 147 ? 34.997 2.866   -22.243 1.00 32.85  ? 164 PRO B CB  1 
ATOM   3172 C CG  . PRO B 1 147 ? 35.121 4.307   -22.536 1.00 35.43  ? 164 PRO B CG  1 
ATOM   3173 C CD  . PRO B 1 147 ? 34.461 4.538   -23.844 1.00 29.90  ? 164 PRO B CD  1 
ATOM   3174 N N   . VAL B 1 148 ? 34.828 -0.191  -23.847 1.00 25.30  ? 165 VAL B N   1 
ATOM   3175 C CA  . VAL B 1 148 ? 34.060 -1.419  -24.022 1.00 29.44  ? 165 VAL B CA  1 
ATOM   3176 C C   . VAL B 1 148 ? 33.238 -1.713  -22.770 1.00 28.04  ? 165 VAL B C   1 
ATOM   3177 O O   . VAL B 1 148 ? 32.073 -2.140  -22.852 1.00 29.06  ? 165 VAL B O   1 
ATOM   3178 C CB  . VAL B 1 148 ? 35.002 -2.571  -24.410 1.00 28.82  ? 165 VAL B CB  1 
ATOM   3179 C CG1 . VAL B 1 148 ? 34.325 -3.914  -24.198 1.00 34.91  ? 165 VAL B CG1 1 
ATOM   3180 C CG2 . VAL B 1 148 ? 35.426 -2.427  -25.897 1.00 30.64  ? 165 VAL B CG2 1 
ATOM   3181 N N   . LEU B 1 149 ? 33.813 -1.475  -21.583 1.00 27.79  ? 166 LEU B N   1 
ATOM   3182 C CA  . LEU B 1 149 ? 33.041 -1.695  -20.365 1.00 29.80  ? 166 LEU B CA  1 
ATOM   3183 C C   . LEU B 1 149 ? 31.794 -0.824  -20.349 1.00 30.41  ? 166 LEU B C   1 
ATOM   3184 O O   . LEU B 1 149 ? 30.742 -1.245  -19.843 1.00 28.91  ? 166 LEU B O   1 
ATOM   3185 C CB  . LEU B 1 149 ? 33.883 -1.433  -19.114 1.00 27.15  ? 166 LEU B CB  1 
ATOM   3186 C CG  . LEU B 1 149 ? 33.248 -2.028  -17.837 1.00 27.31  ? 166 LEU B CG  1 
ATOM   3187 C CD1 . LEU B 1 149 ? 33.293 -3.559  -17.820 1.00 24.23  ? 166 LEU B CD1 1 
ATOM   3188 C CD2 . LEU B 1 149 ? 33.878 -1.482  -16.580 1.00 29.57  ? 166 LEU B CD2 1 
ATOM   3189 N N   . LYS B 1 150 ? 31.885 0.396   -20.892 1.00 27.02  ? 167 LYS B N   1 
ATOM   3190 C CA  . LYS B 1 150 ? 30.686 1.228   -20.983 1.00 32.51  ? 167 LYS B CA  1 
ATOM   3191 C C   . LYS B 1 150 ? 29.651 0.577   -21.886 1.00 32.25  ? 167 LYS B C   1 
ATOM   3192 O O   . LYS B 1 150 ? 28.460 0.546   -21.556 1.00 31.25  ? 167 LYS B O   1 
ATOM   3193 C CB  . LYS B 1 150 ? 31.022 2.637   -21.497 1.00 32.03  ? 167 LYS B CB  1 
ATOM   3194 C CG  . LYS B 1 150 ? 29.831 3.602   -21.505 1.00 35.93  ? 167 LYS B CG  1 
ATOM   3195 C CD  . LYS B 1 150 ? 29.196 3.758   -20.105 1.00 46.78  ? 167 LYS B CD  1 
ATOM   3196 C CE  . LYS B 1 150 ? 28.098 4.864   -20.065 1.00 54.64  ? 167 LYS B CE  1 
ATOM   3197 N NZ  . LYS B 1 150 ? 27.018 4.580   -19.049 1.00 56.56  ? 167 LYS B NZ  1 
ATOM   3198 N N   . GLN B 1 151 ? 30.087 0.033   -23.029 1.00 32.64  ? 168 GLN B N   1 
ATOM   3199 C CA  . GLN B 1 151 ? 29.138 -0.645  -23.905 1.00 30.64  ? 168 GLN B CA  1 
ATOM   3200 C C   . GLN B 1 151 ? 28.442 -1.779  -23.160 1.00 33.43  ? 168 GLN B C   1 
ATOM   3201 O O   . GLN B 1 151 ? 27.218 -1.897  -23.224 1.00 33.71  ? 168 GLN B O   1 
ATOM   3202 C CB  . GLN B 1 151 ? 29.847 -1.160  -25.152 1.00 29.29  ? 168 GLN B CB  1 
ATOM   3203 C CG  . GLN B 1 151 ? 30.656 -0.076  -25.935 1.00 32.32  ? 168 GLN B CG  1 
ATOM   3204 C CD  . GLN B 1 151 ? 31.488 -0.657  -27.059 1.00 33.63  ? 168 GLN B CD  1 
ATOM   3205 O OE1 . GLN B 1 151 ? 31.089 -1.624  -27.711 1.00 32.05  ? 168 GLN B OE1 1 
ATOM   3206 N NE2 . GLN B 1 151 ? 32.665 -0.090  -27.271 1.00 31.96  ? 168 GLN B NE2 1 
ATOM   3207 N N   . LEU B 1 152 ? 29.201 -2.581  -22.391 1.00 27.86  ? 169 LEU B N   1 
ATOM   3208 C CA  . LEU B 1 152 ? 28.617 -3.710  -21.655 1.00 30.61  ? 169 LEU B CA  1 
ATOM   3209 C C   . LEU B 1 152 ? 27.685 -3.256  -20.526 1.00 33.59  ? 169 LEU B C   1 
ATOM   3210 O O   . LEU B 1 152 ? 26.634 -3.870  -20.301 1.00 30.92  ? 169 LEU B O   1 
ATOM   3211 C CB  . LEU B 1 152 ? 29.729 -4.593  -21.077 1.00 30.67  ? 169 LEU B CB  1 
ATOM   3212 C CG  . LEU B 1 152 ? 30.784 -5.072  -22.082 1.00 29.29  ? 169 LEU B CG  1 
ATOM   3213 C CD1 . LEU B 1 152 ? 31.603 -6.168  -21.412 1.00 31.77  ? 169 LEU B CD1 1 
ATOM   3214 C CD2 . LEU B 1 152 ? 30.163 -5.572  -23.356 1.00 31.20  ? 169 LEU B CD2 1 
ATOM   3215 N N   . ILE B 1 153 ? 28.073 -2.206  -19.789 1.00 34.19  ? 170 ILE B N   1 
ATOM   3216 C CA  . ILE B 1 153 ? 27.260 -1.706  -18.685 1.00 34.69  ? 170 ILE B CA  1 
ATOM   3217 C C   . ILE B 1 153 ? 25.915 -1.201  -19.193 1.00 38.22  ? 170 ILE B C   1 
ATOM   3218 O O   . ILE B 1 153 ? 24.873 -1.465  -18.584 1.00 35.85  ? 170 ILE B O   1 
ATOM   3219 C CB  . ILE B 1 153 ? 28.022 -0.609  -17.915 1.00 30.18  ? 170 ILE B CB  1 
ATOM   3220 C CG1 . ILE B 1 153 ? 29.078 -1.265  -17.020 1.00 32.06  ? 170 ILE B CG1 1 
ATOM   3221 C CG2 . ILE B 1 153 ? 27.050 0.245   -17.114 1.00 37.29  ? 170 ILE B CG2 1 
ATOM   3222 C CD1 . ILE B 1 153 ? 30.136 -0.314  -16.493 1.00 35.71  ? 170 ILE B CD1 1 
ATOM   3223 N N   . ASP B 1 154 ? 25.911 -0.460  -20.308 1.00 33.96  ? 171 ASP B N   1 
ATOM   3224 C CA  . ASP B 1 154 ? 24.645 0.060   -20.820 1.00 35.53  ? 171 ASP B CA  1 
ATOM   3225 C C   . ASP B 1 154 ? 23.691 -1.069  -21.219 1.00 35.00  ? 171 ASP B C   1 
ATOM   3226 O O   . ASP B 1 154 ? 22.479 -0.953  -21.028 1.00 37.81  ? 171 ASP B O   1 
ATOM   3227 C CB  . ASP B 1 154 ? 24.892 1.004   -21.995 1.00 41.20  ? 171 ASP B CB  1 
ATOM   3228 C CG  . ASP B 1 154 ? 25.528 2.323   -21.563 1.00 41.20  ? 171 ASP B CG  1 
ATOM   3229 O OD1 . ASP B 1 154 ? 25.501 2.642   -20.358 1.00 44.81  ? 171 ASP B OD1 1 
ATOM   3230 O OD2 . ASP B 1 154 ? 26.040 3.044   -22.442 1.00 47.10  ? 171 ASP B OD2 1 
ATOM   3231 N N   . VAL B 1 155 ? 24.206 -2.159  -21.788 1.00 33.47  ? 172 VAL B N   1 
ATOM   3232 C CA  . VAL B 1 155 ? 23.348 -3.321  -22.032 1.00 37.11  ? 172 VAL B CA  1 
ATOM   3233 C C   . VAL B 1 155 ? 22.870 -3.916  -20.707 1.00 36.94  ? 172 VAL B C   1 
ATOM   3234 O O   . VAL B 1 155 ? 21.691 -4.256  -20.543 1.00 35.38  ? 172 VAL B O   1 
ATOM   3235 C CB  . VAL B 1 155 ? 24.090 -4.373  -22.880 1.00 37.17  ? 172 VAL B CB  1 
ATOM   3236 C CG1 . VAL B 1 155 ? 23.177 -5.582  -23.142 1.00 39.41  ? 172 VAL B CG1 1 
ATOM   3237 C CG2 . VAL B 1 155 ? 24.577 -3.759  -24.208 1.00 38.13  ? 172 VAL B CG2 1 
ATOM   3238 N N   . ALA B 1 156 ? 23.773 -4.031  -19.738 1.00 33.74  ? 173 ALA B N   1 
ATOM   3239 C CA  . ALA B 1 156 ? 23.409 -4.651  -18.469 1.00 35.62  ? 173 ALA B CA  1 
ATOM   3240 C C   . ALA B 1 156 ? 22.286 -3.889  -17.790 1.00 43.23  ? 173 ALA B C   1 
ATOM   3241 O O   . ALA B 1 156 ? 21.354 -4.494  -17.242 1.00 43.17  ? 173 ALA B O   1 
ATOM   3242 C CB  . ALA B 1 156 ? 24.631 -4.715  -17.560 1.00 36.60  ? 173 ALA B CB  1 
ATOM   3243 N N   . VAL B 1 157 ? 22.382 -2.560  -17.790 1.00 40.98  ? 174 VAL B N   1 
ATOM   3244 C CA  . VAL B 1 157 ? 21.344 -1.715  -17.215 1.00 46.06  ? 174 VAL B CA  1 
ATOM   3245 C C   . VAL B 1 157 ? 20.036 -1.841  -17.996 1.00 49.32  ? 174 VAL B C   1 
ATOM   3246 O O   . VAL B 1 157 ? 18.954 -1.952  -17.408 1.00 48.40  ? 174 VAL B O   1 
ATOM   3247 C CB  . VAL B 1 157 ? 21.832 -0.256  -17.170 1.00 50.95  ? 174 VAL B CB  1 
ATOM   3248 C CG1 . VAL B 1 157 ? 20.693 0.686   -16.756 1.00 55.16  ? 174 VAL B CG1 1 
ATOM   3249 C CG2 . VAL B 1 157 ? 22.984 -0.130  -16.213 1.00 46.45  ? 174 VAL B CG2 1 
ATOM   3250 N N   . ALA B 1 158 ? 20.108 -1.805  -19.330 1.00 41.60  ? 175 ALA B N   1 
ATOM   3251 C CA  . ALA B 1 158 ? 18.881 -1.788  -20.124 1.00 46.92  ? 175 ALA B CA  1 
ATOM   3252 C C   . ALA B 1 158 ? 18.130 -3.109  -20.037 1.00 49.76  ? 175 ALA B C   1 
ATOM   3253 O O   . ALA B 1 158 ? 16.900 -3.119  -19.926 1.00 57.50  ? 175 ALA B O   1 
ATOM   3254 C CB  . ALA B 1 158 ? 19.190 -1.474  -21.587 1.00 37.05  ? 175 ALA B CB  1 
ATOM   3255 N N   . ARG B 1 159 ? 18.841 -4.231  -20.111 1.00 51.25  ? 176 ARG B N   1 
ATOM   3256 C CA  . ARG B 1 159 ? 18.213 -5.548  -20.169 1.00 48.16  ? 176 ARG B CA  1 
ATOM   3257 C C   . ARG B 1 159 ? 18.146 -6.251  -18.817 1.00 46.27  ? 176 ARG B C   1 
ATOM   3258 O O   . ARG B 1 159 ? 17.575 -7.340  -18.734 1.00 49.40  ? 176 ARG B O   1 
ATOM   3259 C CB  . ARG B 1 159 ? 18.967 -6.410  -21.180 1.00 43.69  ? 176 ARG B CB  1 
ATOM   3260 C CG  . ARG B 1 159 ? 19.091 -5.745  -22.529 1.00 46.60  ? 176 ARG B CG  1 
ATOM   3261 C CD  . ARG B 1 159 ? 19.219 -6.753  -23.652 1.00 50.01  ? 176 ARG B CD  1 
ATOM   3262 N NE  . ARG B 1 159 ? 19.108 -6.139  -24.968 1.00 49.35  ? 176 ARG B NE  1 
ATOM   3263 C CZ  . ARG B 1 159 ? 18.035 -6.230  -25.741 1.00 52.55  ? 176 ARG B CZ  1 
ATOM   3264 N NH1 . ARG B 1 159 ? 16.930 -6.824  -25.322 1.00 49.91  ? 176 ARG B NH1 1 
ATOM   3265 N NH2 . ARG B 1 159 ? 18.062 -5.689  -26.951 1.00 54.59  ? 176 ARG B NH2 1 
ATOM   3266 N N   . GLN B 1 160 ? 18.702 -5.653  -17.761 1.00 44.53  ? 177 GLN B N   1 
ATOM   3267 C CA  . GLN B 1 160 ? 18.639 -6.191  -16.399 1.00 53.82  ? 177 GLN B CA  1 
ATOM   3268 C C   . GLN B 1 160 ? 19.207 -7.615  -16.337 1.00 51.05  ? 177 GLN B C   1 
ATOM   3269 O O   . GLN B 1 160 ? 18.498 -8.600  -16.133 1.00 45.40  ? 177 GLN B O   1 
ATOM   3270 C CB  . GLN B 1 160 ? 17.204 -6.140  -15.855 1.00 57.60  ? 177 GLN B CB  1 
ATOM   3271 C CG  . GLN B 1 160 ? 16.740 -4.755  -15.425 1.00 62.91  ? 177 GLN B CG  1 
ATOM   3272 C CD  . GLN B 1 160 ? 15.247 -4.712  -15.067 1.00 79.45  ? 177 GLN B CD  1 
ATOM   3273 O OE1 . GLN B 1 160 ? 14.411 -5.306  -15.755 1.00 72.10  ? 177 GLN B OE1 1 
ATOM   3274 N NE2 . GLN B 1 160 ? 14.917 -4.024  -13.973 1.00 79.93  ? 177 GLN B NE2 1 
ATOM   3275 N N   . GLY B 1 161 ? 20.512 -7.705  -16.566 1.00 44.43  ? 178 GLY B N   1 
ATOM   3276 C CA  . GLY B 1 161 ? 21.156 -9.004  -16.468 1.00 38.65  ? 178 GLY B CA  1 
ATOM   3277 C C   . GLY B 1 161 ? 22.661 -8.865  -16.544 1.00 34.31  ? 178 GLY B C   1 
ATOM   3278 O O   . GLY B 1 161 ? 23.198 -7.771  -16.711 1.00 34.94  ? 178 GLY B O   1 
ATOM   3279 N N   . SER B 1 162 ? 23.341 -9.994  -16.395 1.00 28.90  ? 179 SER B N   1 
ATOM   3280 C CA  . SER B 1 162 ? 24.783 -10.010 -16.573 1.00 33.13  ? 179 SER B CA  1 
ATOM   3281 C C   . SER B 1 162 ? 25.116 -9.904  -18.060 1.00 32.17  ? 179 SER B C   1 
ATOM   3282 O O   . SER B 1 162 ? 24.292 -10.231 -18.912 1.00 30.34  ? 179 SER B O   1 
ATOM   3283 C CB  . SER B 1 162 ? 25.373 -11.295 -15.998 1.00 30.06  ? 179 SER B CB  1 
ATOM   3284 O OG  . SER B 1 162 ? 25.135 -11.396 -14.624 1.00 31.01  ? 179 SER B OG  1 
ATOM   3285 N N   . VAL B 1 163 ? 26.324 -9.419  -18.373 1.00 29.24  ? 180 VAL B N   1 
ATOM   3286 C CA  . VAL B 1 163 ? 26.736 -9.260  -19.768 1.00 26.75  ? 180 VAL B CA  1 
ATOM   3287 C C   . VAL B 1 163 ? 28.183 -9.696  -19.938 1.00 28.89  ? 180 VAL B C   1 
ATOM   3288 O O   . VAL B 1 163 ? 29.081 -9.202  -19.248 1.00 30.36  ? 180 VAL B O   1 
ATOM   3289 C CB  . VAL B 1 163 ? 26.553 -7.816  -20.283 1.00 29.77  ? 180 VAL B CB  1 
ATOM   3290 C CG1 . VAL B 1 163 ? 27.021 -7.702  -21.748 1.00 28.76  ? 180 VAL B CG1 1 
ATOM   3291 C CG2 . VAL B 1 163 ? 25.069 -7.381  -20.166 1.00 35.83  ? 180 VAL B CG2 1 
ATOM   3292 N N   . LEU B 1 164 ? 28.409 -10.581 -20.903 1.00 27.38  ? 181 LEU B N   1 
ATOM   3293 C CA  . LEU B 1 164 ? 29.742 -10.990 -21.309 1.00 24.04  ? 181 LEU B CA  1 
ATOM   3294 C C   . LEU B 1 164 ? 30.132 -10.268 -22.593 1.00 28.45  ? 181 LEU B C   1 
ATOM   3295 O O   . LEU B 1 164 ? 29.393 -10.310 -23.570 1.00 28.76  ? 181 LEU B O   1 
ATOM   3296 C CB  . LEU B 1 164 ? 29.788 -12.496 -21.551 1.00 29.68  ? 181 LEU B CB  1 
ATOM   3297 C CG  . LEU B 1 164 ? 29.031 -13.440 -20.609 1.00 33.42  ? 181 LEU B CG  1 
ATOM   3298 C CD1 . LEU B 1 164 ? 29.290 -14.880 -21.012 1.00 33.30  ? 181 LEU B CD1 1 
ATOM   3299 C CD2 . LEU B 1 164 ? 29.402 -13.235 -19.160 1.00 31.39  ? 181 LEU B CD2 1 
ATOM   3300 N N   . GLY B 1 165 ? 31.308 -9.651  -22.612 1.00 25.07  ? 182 GLY B N   1 
ATOM   3301 C CA  . GLY B 1 165 ? 31.829 -9.162  -23.879 1.00 29.46  ? 182 GLY B CA  1 
ATOM   3302 C C   . GLY B 1 165 ? 32.259 -10.329 -24.752 1.00 32.21  ? 182 GLY B C   1 
ATOM   3303 O O   . GLY B 1 165 ? 32.950 -11.246 -24.287 1.00 32.12  ? 182 GLY B O   1 
ATOM   3304 N N   . VAL B 1 166 ? 31.855 -10.304 -26.031 1.00 29.54  ? 183 VAL B N   1 
ATOM   3305 C CA  . VAL B 1 166 ? 32.200 -11.379 -26.949 1.00 26.09  ? 183 VAL B CA  1 
ATOM   3306 C C   . VAL B 1 166 ? 32.703 -10.776 -28.247 1.00 33.17  ? 183 VAL B C   1 
ATOM   3307 O O   . VAL B 1 166 ? 32.422 -9.622  -28.568 1.00 31.46  ? 183 VAL B O   1 
ATOM   3308 C CB  . VAL B 1 166 ? 31.019 -12.300 -27.245 1.00 29.80  ? 183 VAL B CB  1 
ATOM   3309 C CG1 . VAL B 1 166 ? 30.662 -13.068 -25.993 1.00 32.51  ? 183 VAL B CG1 1 
ATOM   3310 C CG2 . VAL B 1 166 ? 29.841 -11.510 -27.759 1.00 29.93  ? 183 VAL B CG2 1 
ATOM   3311 N N   . GLN B 1 167 ? 33.419 -11.597 -29.012 1.00 34.63  ? 184 GLN B N   1 
ATOM   3312 C CA  . GLN B 1 167 ? 33.740 -11.245 -30.386 1.00 32.99  ? 184 GLN B CA  1 
ATOM   3313 C C   . GLN B 1 167 ? 33.840 -12.507 -31.214 1.00 35.25  ? 184 GLN B C   1 
ATOM   3314 O O   . GLN B 1 167 ? 34.156 -13.589 -30.700 1.00 32.58  ? 184 GLN B O   1 
ATOM   3315 C CB  . GLN B 1 167 ? 35.050 -10.439 -30.494 1.00 38.13  ? 184 GLN B CB  1 
ATOM   3316 C CG  . GLN B 1 167 ? 36.358 -11.240 -30.331 1.00 43.05  ? 184 GLN B CG  1 
ATOM   3317 C CD  . GLN B 1 167 ? 37.638 -10.379 -30.525 1.00 55.94  ? 184 GLN B CD  1 
ATOM   3318 O OE1 . GLN B 1 167 ? 37.597 -9.134  -30.477 1.00 61.91  ? 184 GLN B OE1 1 
ATOM   3319 N NE2 . GLN B 1 167 ? 38.783 -11.051 -30.685 1.00 49.84  ? 184 GLN B NE2 1 
ATOM   3320 N N   . GLU B 1 168 ? 33.565 -12.344 -32.510 1.00 35.60  ? 185 GLU B N   1 
ATOM   3321 C CA  . GLU B 1 168 ? 33.741 -13.429 -33.454 1.00 33.70  ? 185 GLU B CA  1 
ATOM   3322 C C   . GLU B 1 168 ? 35.220 -13.750 -33.594 1.00 38.62  ? 185 GLU B C   1 
ATOM   3323 O O   . GLU B 1 168 ? 36.057 -12.853 -33.700 1.00 37.32  ? 185 GLU B O   1 
ATOM   3324 C CB  . GLU B 1 168 ? 33.152 -13.053 -34.818 1.00 41.09  ? 185 GLU B CB  1 
ATOM   3325 C CG  . GLU B 1 168 ? 31.636 -12.968 -34.869 1.00 42.77  ? 185 GLU B CG  1 
ATOM   3326 C CD  . GLU B 1 168 ? 30.999 -14.348 -34.836 1.00 47.98  ? 185 GLU B CD  1 
ATOM   3327 O OE1 . GLU B 1 168 ? 31.667 -15.292 -35.320 1.00 45.26  ? 185 GLU B OE1 1 
ATOM   3328 O OE2 . GLU B 1 168 ? 29.859 -14.500 -34.327 1.00 50.22  ? 185 GLU B OE2 1 
ATOM   3329 N N   . VAL B 1 169 ? 35.538 -15.041 -33.581 1.00 36.34  ? 186 VAL B N   1 
ATOM   3330 C CA  . VAL B 1 169 ? 36.902 -15.501 -33.827 1.00 36.43  ? 186 VAL B CA  1 
ATOM   3331 C C   . VAL B 1 169 ? 36.837 -16.557 -34.921 1.00 38.77  ? 186 VAL B C   1 
ATOM   3332 O O   . VAL B 1 169 ? 35.773 -17.154 -35.172 1.00 35.14  ? 186 VAL B O   1 
ATOM   3333 C CB  . VAL B 1 169 ? 37.569 -16.051 -32.545 1.00 40.34  ? 186 VAL B CB  1 
ATOM   3334 C CG1 . VAL B 1 169 ? 37.649 -14.963 -31.492 1.00 35.27  ? 186 VAL B CG1 1 
ATOM   3335 C CG2 . VAL B 1 169 ? 36.823 -17.290 -32.028 1.00 40.21  ? 186 VAL B CG2 1 
ATOM   3336 N N   . PRO B 1 170 ? 37.947 -16.784 -35.622 1.00 38.93  ? 187 PRO B N   1 
ATOM   3337 C CA  . PRO B 1 170 ? 37.959 -17.850 -36.632 1.00 44.03  ? 187 PRO B CA  1 
ATOM   3338 C C   . PRO B 1 170 ? 37.663 -19.194 -35.992 1.00 39.24  ? 187 PRO B C   1 
ATOM   3339 O O   . PRO B 1 170 ? 38.149 -19.494 -34.906 1.00 44.86  ? 187 PRO B O   1 
ATOM   3340 C CB  . PRO B 1 170 ? 39.380 -17.791 -37.208 1.00 45.87  ? 187 PRO B CB  1 
ATOM   3341 C CG  . PRO B 1 170 ? 40.173 -16.959 -36.278 1.00 50.94  ? 187 PRO B CG  1 
ATOM   3342 C CD  . PRO B 1 170 ? 39.227 -16.053 -35.554 1.00 45.95  ? 187 PRO B CD  1 
ATOM   3343 N N   . ARG B 1 171 ? 36.874 -20.020 -36.687 1.00 37.37  ? 188 ARG B N   1 
ATOM   3344 C CA  . ARG B 1 171 ? 36.495 -21.306 -36.105 1.00 41.25  ? 188 ARG B CA  1 
ATOM   3345 C C   . ARG B 1 171 ? 37.720 -22.129 -35.722 1.00 46.05  ? 188 ARG B C   1 
ATOM   3346 O O   . ARG B 1 171 ? 37.692 -22.866 -34.728 1.00 42.01  ? 188 ARG B O   1 
ATOM   3347 C CB  . ARG B 1 171 ? 35.601 -22.088 -37.067 1.00 46.03  ? 188 ARG B CB  1 
ATOM   3348 C CG  . ARG B 1 171 ? 35.175 -23.447 -36.509 1.00 38.76  ? 188 ARG B CG  1 
ATOM   3349 C CD  . ARG B 1 171 ? 34.009 -24.028 -37.286 1.00 35.10  ? 188 ARG B CD  1 
ATOM   3350 N NE  . ARG B 1 171 ? 32.757 -23.370 -36.930 1.00 36.44  ? 188 ARG B NE  1 
ATOM   3351 C CZ  . ARG B 1 171 ? 31.971 -23.753 -35.925 1.00 42.88  ? 188 ARG B CZ  1 
ATOM   3352 N NH1 . ARG B 1 171 ? 32.272 -24.793 -35.161 1.00 36.05  ? 188 ARG B NH1 1 
ATOM   3353 N NH2 . ARG B 1 171 ? 30.844 -23.089 -35.687 1.00 43.55  ? 188 ARG B NH2 1 
ATOM   3354 N N   . GLU B 1 172 ? 38.819 -21.972 -36.460 1.00 43.87  ? 189 GLU B N   1 
ATOM   3355 C CA  . GLU B 1 172 ? 40.045 -22.704 -36.167 1.00 47.74  ? 189 GLU B CA  1 
ATOM   3356 C C   . GLU B 1 172 ? 40.615 -22.369 -34.799 1.00 43.90  ? 189 GLU B C   1 
ATOM   3357 O O   . GLU B 1 172 ? 41.410 -23.145 -34.263 1.00 52.98  ? 189 GLU B O   1 
ATOM   3358 C CB  . GLU B 1 172 ? 41.107 -22.388 -37.237 1.00 50.64  ? 189 GLU B CB  1 
ATOM   3359 C CG  . GLU B 1 172 ? 40.716 -22.790 -38.657 1.00 71.28  ? 189 GLU B CG  1 
ATOM   3360 C CD  . GLU B 1 172 ? 39.675 -21.868 -39.304 1.00 65.20  ? 189 GLU B CD  1 
ATOM   3361 O OE1 . GLU B 1 172 ? 39.712 -20.641 -39.068 1.00 58.97  ? 189 GLU B OE1 1 
ATOM   3362 O OE2 . GLU B 1 172 ? 38.802 -22.390 -40.039 1.00 63.78  ? 189 GLU B OE2 1 
ATOM   3363 N N   . ASP B 1 173 ? 40.246 -21.233 -34.226 1.00 46.92  ? 190 ASP B N   1 
ATOM   3364 C CA  . ASP B 1 173 ? 40.817 -20.785 -32.966 1.00 44.77  ? 190 ASP B CA  1 
ATOM   3365 C C   . ASP B 1 173 ? 39.945 -21.082 -31.749 1.00 44.04  ? 190 ASP B C   1 
ATOM   3366 O O   . ASP B 1 173 ? 40.329 -20.718 -30.639 1.00 41.49  ? 190 ASP B O   1 
ATOM   3367 C CB  . ASP B 1 173 ? 41.085 -19.274 -33.018 1.00 47.24  ? 190 ASP B CB  1 
ATOM   3368 C CG  . ASP B 1 173 ? 42.312 -18.903 -33.863 1.00 57.73  ? 190 ASP B CG  1 
ATOM   3369 O OD1 . ASP B 1 173 ? 42.933 -19.788 -34.492 1.00 57.20  ? 190 ASP B OD1 1 
ATOM   3370 O OD2 . ASP B 1 173 ? 42.626 -17.696 -33.928 1.00 61.40  ? 190 ASP B OD2 1 
ATOM   3371 N N   . THR B 1 174 ? 38.789 -21.730 -31.910 1.00 44.38  ? 191 THR B N   1 
ATOM   3372 C CA  . THR B 1 174 ? 37.859 -21.810 -30.789 1.00 38.07  ? 191 THR B CA  1 
ATOM   3373 C C   . THR B 1 174 ? 38.394 -22.622 -29.616 1.00 40.91  ? 191 THR B C   1 
ATOM   3374 O O   . THR B 1 174 ? 37.880 -22.486 -28.503 1.00 38.63  ? 191 THR B O   1 
ATOM   3375 C CB  . THR B 1 174 ? 36.529 -22.417 -31.224 1.00 36.68  ? 191 THR B CB  1 
ATOM   3376 O OG1 . THR B 1 174 ? 36.760 -23.697 -31.815 1.00 37.82  ? 191 THR B OG1 1 
ATOM   3377 C CG2 . THR B 1 174 ? 35.832 -21.499 -32.179 1.00 37.23  ? 191 THR B CG2 1 
ATOM   3378 N N   . ARG B 1 175 ? 39.389 -23.480 -29.827 1.00 45.22  ? 192 ARG B N   1 
ATOM   3379 C CA  . ARG B 1 175 ? 39.931 -24.183 -28.677 1.00 46.01  ? 192 ARG B CA  1 
ATOM   3380 C C   . ARG B 1 175 ? 40.643 -23.258 -27.705 1.00 49.73  ? 192 ARG B C   1 
ATOM   3381 O O   . ARG B 1 175 ? 40.987 -23.698 -26.603 1.00 53.89  ? 192 ARG B O   1 
ATOM   3382 C CB  . ARG B 1 175 ? 40.851 -25.321 -29.109 1.00 55.23  ? 192 ARG B CB  1 
ATOM   3383 C CG  . ARG B 1 175 ? 41.189 -26.231 -27.927 1.00 63.49  ? 192 ARG B CG  1 
ATOM   3384 C CD  . ARG B 1 175 ? 41.948 -27.494 -28.304 1.00 75.75  ? 192 ARG B CD  1 
ATOM   3385 N NE  . ARG B 1 175 ? 41.081 -28.492 -28.926 1.00 75.42  ? 192 ARG B NE  1 
ATOM   3386 C CZ  . ARG B 1 175 ? 41.103 -28.847 -30.203 1.00 64.99  ? 192 ARG B CZ  1 
ATOM   3387 N NH1 . ARG B 1 175 ? 41.906 -28.259 -31.075 1.00 81.83  ? 192 ARG B NH1 1 
ATOM   3388 N NH2 . ARG B 1 175 ? 40.290 -29.813 -30.615 1.00 67.50  ? 192 ARG B NH2 1 
ATOM   3389 N N   . LYS B 1 176 ? 40.880 -22.004 -28.074 1.00 42.45  ? 193 LYS B N   1 
ATOM   3390 C CA  . LYS B 1 176 ? 41.516 -21.083 -27.150 1.00 41.92  ? 193 LYS B CA  1 
ATOM   3391 C C   . LYS B 1 176 ? 40.529 -20.461 -26.174 1.00 44.25  ? 193 LYS B C   1 
ATOM   3392 O O   . LYS B 1 176 ? 40.956 -19.897 -25.165 1.00 46.35  ? 193 LYS B O   1 
ATOM   3393 C CB  . LYS B 1 176 ? 42.214 -19.944 -27.917 1.00 44.61  ? 193 LYS B CB  1 
ATOM   3394 C CG  . LYS B 1 176 ? 43.446 -20.349 -28.713 1.00 53.37  ? 193 LYS B CG  1 
ATOM   3395 C CD  . LYS B 1 176 ? 44.033 -19.154 -29.517 1.00 65.97  ? 193 LYS B CD  1 
ATOM   3396 C CE  . LYS B 1 176 ? 45.076 -19.609 -30.566 1.00 70.17  ? 193 LYS B CE  1 
ATOM   3397 N NZ  . LYS B 1 176 ? 45.567 -18.510 -31.473 1.00 73.78  ? 193 LYS B NZ  1 
ATOM   3398 N N   . TYR B 1 177 ? 39.229 -20.575 -26.416 1.00 39.62  ? 194 TYR B N   1 
ATOM   3399 C CA  . TYR B 1 177 ? 38.288 -19.640 -25.839 1.00 34.81  ? 194 TYR B CA  1 
ATOM   3400 C C   . TYR B 1 177 ? 37.128 -20.361 -25.174 1.00 36.65  ? 194 TYR B C   1 
ATOM   3401 O O   . TYR B 1 177 ? 36.848 -21.533 -25.442 1.00 36.57  ? 194 TYR B O   1 
ATOM   3402 C CB  . TYR B 1 177 ? 37.704 -18.711 -26.909 1.00 39.70  ? 194 TYR B CB  1 
ATOM   3403 C CG  . TYR B 1 177 ? 38.711 -17.897 -27.699 1.00 43.61  ? 194 TYR B CG  1 
ATOM   3404 C CD1 . TYR B 1 177 ? 39.396 -16.836 -27.134 1.00 45.34  ? 194 TYR B CD1 1 
ATOM   3405 C CD2 . TYR B 1 177 ? 38.961 -18.199 -29.024 1.00 38.01  ? 194 TYR B CD2 1 
ATOM   3406 C CE1 . TYR B 1 177 ? 40.323 -16.095 -27.889 1.00 40.20  ? 194 TYR B CE1 1 
ATOM   3407 C CE2 . TYR B 1 177 ? 39.886 -17.461 -29.780 1.00 47.06  ? 194 TYR B CE2 1 
ATOM   3408 C CZ  . TYR B 1 177 ? 40.557 -16.418 -29.198 1.00 43.23  ? 194 TYR B CZ  1 
ATOM   3409 O OH  . TYR B 1 177 ? 41.467 -15.699 -29.944 1.00 52.44  ? 194 TYR B OH  1 
ATOM   3410 N N   . GLY B 1 178 ? 36.454 -19.628 -24.292 1.00 39.93  ? 195 GLY B N   1 
ATOM   3411 C CA  . GLY B 1 178 ? 35.103 -19.980 -23.915 1.00 37.38  ? 195 GLY B CA  1 
ATOM   3412 C C   . GLY B 1 178 ? 34.181 -19.480 -25.008 1.00 33.62  ? 195 GLY B C   1 
ATOM   3413 O O   . GLY B 1 178 ? 34.336 -18.352 -25.493 1.00 31.24  ? 195 GLY B O   1 
ATOM   3414 N N   . ILE B 1 179 ? 33.243 -20.334 -25.429 1.00 31.84  ? 196 ILE B N   1 
ATOM   3415 C CA  . ILE B 1 179 ? 32.387 -20.068 -26.581 1.00 29.55  ? 196 ILE B CA  1 
ATOM   3416 C C   . ILE B 1 179 ? 30.949 -20.065 -26.081 1.00 28.85  ? 196 ILE B C   1 
ATOM   3417 O O   . ILE B 1 179 ? 30.545 -20.976 -25.353 1.00 29.64  ? 196 ILE B O   1 
ATOM   3418 C CB  . ILE B 1 179 ? 32.603 -21.109 -27.703 1.00 28.25  ? 196 ILE B CB  1 
ATOM   3419 C CG1 . ILE B 1 179 ? 34.049 -21.056 -28.206 1.00 33.49  ? 196 ILE B CG1 1 
ATOM   3420 C CG2 . ILE B 1 179 ? 31.625 -20.908 -28.835 1.00 32.82  ? 196 ILE B CG2 1 
ATOM   3421 C CD1 . ILE B 1 179 ? 34.433 -19.735 -28.867 1.00 32.40  ? 196 ILE B CD1 1 
ATOM   3422 N N   . VAL B 1 180 ? 30.175 -19.059 -26.488 1.00 32.26  ? 197 VAL B N   1 
ATOM   3423 C CA  . VAL B 1 180 ? 28.786 -18.911 -26.050 1.00 31.67  ? 197 VAL B CA  1 
ATOM   3424 C C   . VAL B 1 180 ? 27.847 -19.432 -27.125 1.00 32.89  ? 197 VAL B C   1 
ATOM   3425 O O   . VAL B 1 180 ? 28.064 -19.208 -28.318 1.00 32.92  ? 197 VAL B O   1 
ATOM   3426 C CB  . VAL B 1 180 ? 28.444 -17.445 -25.696 1.00 32.30  ? 197 VAL B CB  1 
ATOM   3427 C CG1 . VAL B 1 180 ? 29.304 -16.971 -24.528 1.00 37.28  ? 197 VAL B CG1 1 
ATOM   3428 C CG2 . VAL B 1 180 ? 28.627 -16.521 -26.874 1.00 42.80  ? 197 VAL B CG2 1 
ATOM   3429 N N   . ALA B 1 181 ? 26.827 -20.163 -26.700 1.00 33.20  ? 198 ALA B N   1 
ATOM   3430 C CA  . ALA B 1 181 ? 25.666 -20.481 -27.520 1.00 33.04  ? 198 ALA B CA  1 
ATOM   3431 C C   . ALA B 1 181 ? 24.557 -19.526 -27.094 1.00 39.65  ? 198 ALA B C   1 
ATOM   3432 O O   . ALA B 1 181 ? 24.225 -19.445 -25.899 1.00 33.30  ? 198 ALA B O   1 
ATOM   3433 C CB  . ALA B 1 181 ? 25.238 -21.935 -27.323 1.00 35.68  ? 198 ALA B CB  1 
ATOM   3434 N N   . SER B 1 182 ? 24.015 -18.782 -28.046 1.00 32.26  ? 199 SER B N   1 
ATOM   3435 C CA  . SER B 1 182 ? 23.138 -17.671 -27.704 1.00 43.11  ? 199 SER B CA  1 
ATOM   3436 C C   . SER B 1 182 ? 22.115 -17.457 -28.801 1.00 43.59  ? 199 SER B C   1 
ATOM   3437 O O   . SER B 1 182 ? 22.301 -17.891 -29.936 1.00 41.75  ? 199 SER B O   1 
ATOM   3438 C CB  . SER B 1 182 ? 23.915 -16.364 -27.499 1.00 36.01  ? 199 SER B CB  1 
ATOM   3439 O OG  . SER B 1 182 ? 24.743 -16.076 -28.592 1.00 44.19  ? 199 SER B OG  1 
ATOM   3440 N N   . GLN B 1 183 ? 21.060 -16.714 -28.458 1.00 48.51  ? 200 GLN B N   1 
ATOM   3441 C CA  . GLN B 1 183 ? 20.016 -16.330 -29.396 1.00 56.37  ? 200 GLN B CA  1 
ATOM   3442 C C   . GLN B 1 183 ? 19.903 -14.809 -29.493 1.00 54.88  ? 200 GLN B C   1 
ATOM   3443 O O   . GLN B 1 183 ? 19.871 -14.125 -28.459 1.00 46.25  ? 200 GLN B O   1 
ATOM   3444 C CB  . GLN B 1 183 ? 18.664 -16.941 -28.956 1.00 56.69  ? 200 GLN B CB  1 
ATOM   3445 C CG  . GLN B 1 183 ? 18.627 -18.478 -28.985 1.00 61.31  ? 200 GLN B CG  1 
ATOM   3446 C CD  . GLN B 1 183 ? 18.938 -19.051 -30.372 1.00 65.24  ? 200 GLN B CD  1 
ATOM   3447 O OE1 . GLN B 1 183 ? 18.709 -18.396 -31.388 1.00 62.31  ? 200 GLN B OE1 1 
ATOM   3448 N NE2 . GLN B 1 183 ? 19.451 -20.279 -30.413 1.00 66.43  ? 200 GLN B NE2 1 
ATOM   3449 N N   . PRO B 1 184 ? 19.804 -14.244 -30.698 1.00 55.19  ? 201 PRO B N   1 
ATOM   3450 C CA  . PRO B 1 184 ? 19.771 -12.781 -30.819 1.00 52.39  ? 201 PRO B CA  1 
ATOM   3451 C C   . PRO B 1 184 ? 18.580 -12.135 -30.133 1.00 52.92  ? 201 PRO B C   1 
ATOM   3452 O O   . PRO B 1 184 ? 17.462 -12.657 -30.138 1.00 54.25  ? 201 PRO B O   1 
ATOM   3453 C CB  . PRO B 1 184 ? 19.719 -12.560 -32.334 1.00 52.91  ? 201 PRO B CB  1 
ATOM   3454 C CG  . PRO B 1 184 ? 20.376 -13.775 -32.895 1.00 56.16  ? 201 PRO B CG  1 
ATOM   3455 C CD  . PRO B 1 184 ? 19.900 -14.888 -32.017 1.00 55.37  ? 201 PRO B CD  1 
ATOM   3456 N N   . VAL B 1 185 ? 18.850 -10.995 -29.509 1.00 52.06  ? 202 VAL B N   1 
ATOM   3457 C CA  . VAL B 1 185 ? 17.806 -10.084 -29.063 1.00 48.75  ? 202 VAL B CA  1 
ATOM   3458 C C   . VAL B 1 185 ? 17.857 -8.748  -29.784 1.00 49.04  ? 202 VAL B C   1 
ATOM   3459 O O   . VAL B 1 185 ? 16.843 -8.042  -29.804 1.00 52.66  ? 202 VAL B O   1 
ATOM   3460 C CB  . VAL B 1 185 ? 17.875 -9.862  -27.541 1.00 46.12  ? 202 VAL B CB  1 
ATOM   3461 C CG1 . VAL B 1 185 ? 17.573 -11.150 -26.815 1.00 49.84  ? 202 VAL B CG1 1 
ATOM   3462 C CG2 . VAL B 1 185 ? 19.238 -9.334  -27.135 1.00 50.07  ? 202 VAL B CG2 1 
ATOM   3463 N N   . ASP B 1 186 ? 19.008 -8.353  -30.315 1.00 49.67  ? 203 ASP B N   1 
ATOM   3464 C CA  . ASP B 1 186 ? 19.151 -7.220  -31.216 1.00 49.92  ? 203 ASP B CA  1 
ATOM   3465 C C   . ASP B 1 186 ? 20.440 -7.443  -32.002 1.00 45.22  ? 203 ASP B C   1 
ATOM   3466 O O   . ASP B 1 186 ? 21.021 -8.535  -31.978 1.00 48.78  ? 203 ASP B O   1 
ATOM   3467 C CB  . ASP B 1 186 ? 19.108 -5.883  -30.462 1.00 44.67  ? 203 ASP B CB  1 
ATOM   3468 C CG  . ASP B 1 186 ? 20.326 -5.628  -29.585 1.00 47.46  ? 203 ASP B CG  1 
ATOM   3469 O OD1 . ASP B 1 186 ? 21.462 -6.063  -29.902 1.00 43.25  ? 203 ASP B OD1 1 
ATOM   3470 O OD2 . ASP B 1 186 ? 20.134 -4.927  -28.571 1.00 51.27  ? 203 ASP B OD2 1 
ATOM   3471 N N   . ALA B 1 187 ? 20.876 -6.409  -32.716 1.00 48.13  ? 204 ALA B N   1 
ATOM   3472 C CA  . ALA B 1 187 ? 21.939 -6.587  -33.699 1.00 50.09  ? 204 ALA B CA  1 
ATOM   3473 C C   . ALA B 1 187 ? 23.278 -6.940  -33.058 1.00 50.35  ? 204 ALA B C   1 
ATOM   3474 O O   . ALA B 1 187 ? 24.098 -7.632  -33.678 1.00 42.92  ? 204 ALA B O   1 
ATOM   3475 C CB  . ALA B 1 187 ? 22.077 -5.311  -34.528 1.00 49.76  ? 204 ALA B CB  1 
ATOM   3476 N N   . ARG B 1 188 ? 23.522 -6.506  -31.822 1.00 47.08  ? 205 ARG B N   1 
ATOM   3477 C CA  . ARG B 1 188 ? 24.792 -6.794  -31.171 1.00 46.78  ? 205 ARG B CA  1 
ATOM   3478 C C   . ARG B 1 188 ? 24.666 -7.642  -29.921 1.00 42.02  ? 205 ARG B C   1 
ATOM   3479 O O   . ARG B 1 188 ? 25.689 -8.157  -29.454 1.00 41.46  ? 205 ARG B O   1 
ATOM   3480 C CB  . ARG B 1 188 ? 25.548 -5.502  -30.804 1.00 43.87  ? 205 ARG B CB  1 
ATOM   3481 C CG  . ARG B 1 188 ? 26.161 -4.741  -32.000 1.00 49.00  ? 205 ARG B CG  1 
ATOM   3482 C CD  . ARG B 1 188 ? 27.067 -3.583  -31.532 1.00 58.59  ? 205 ARG B CD  1 
ATOM   3483 N NE  . ARG B 1 188 ? 27.685 -2.864  -32.643 1.00 67.57  ? 205 ARG B NE  1 
ATOM   3484 C CZ  . ARG B 1 188 ? 28.836 -3.197  -33.218 1.00 71.10  ? 205 ARG B CZ  1 
ATOM   3485 N NH1 . ARG B 1 188 ? 29.566 -4.215  -32.779 1.00 58.45  ? 205 ARG B NH1 1 
ATOM   3486 N NH2 . ARG B 1 188 ? 29.272 -2.485  -34.255 1.00 76.50  ? 205 ARG B NH2 1 
ATOM   3487 N N   . THR B 1 189 ? 23.469 -7.779  -29.355 1.00 38.04  ? 206 THR B N   1 
ATOM   3488 C CA  . THR B 1 189 ? 23.265 -8.438  -28.069 1.00 36.71  ? 206 THR B CA  1 
ATOM   3489 C C   . THR B 1 189 ? 22.521 -9.744  -28.282 1.00 41.92  ? 206 THR B C   1 
ATOM   3490 O O   . THR B 1 189 ? 21.647 -9.834  -29.145 1.00 43.55  ? 206 THR B O   1 
ATOM   3491 C CB  . THR B 1 189 ? 22.498 -7.527  -27.116 1.00 37.72  ? 206 THR B CB  1 
ATOM   3492 O OG1 . THR B 1 189 ? 23.253 -6.318  -26.915 1.00 39.29  ? 206 THR B OG1 1 
ATOM   3493 C CG2 . THR B 1 189 ? 22.243 -8.222  -25.757 1.00 36.32  ? 206 THR B CG2 1 
ATOM   3494 N N   . GLU B 1 190 ? 22.903 -10.763 -27.520 1.00 39.64  ? 207 GLU B N   1 
ATOM   3495 C CA  . GLU B 1 190 ? 22.305 -12.086 -27.607 1.00 44.79  ? 207 GLU B CA  1 
ATOM   3496 C C   . GLU B 1 190 ? 22.038 -12.585 -26.195 1.00 44.32  ? 207 GLU B C   1 
ATOM   3497 O O   . GLU B 1 190 ? 22.705 -12.172 -25.244 1.00 37.00  ? 207 GLU B O   1 
ATOM   3498 C CB  . GLU B 1 190 ? 23.239 -13.050 -28.321 1.00 49.40  ? 207 GLU B CB  1 
ATOM   3499 C CG  . GLU B 1 190 ? 23.764 -12.511 -29.638 1.00 48.21  ? 207 GLU B CG  1 
ATOM   3500 C CD  . GLU B 1 190 ? 23.691 -13.522 -30.762 1.00 55.99  ? 207 GLU B CD  1 
ATOM   3501 O OE1 . GLU B 1 190 ? 23.276 -14.685 -30.512 1.00 51.12  ? 207 GLU B OE1 1 
ATOM   3502 O OE2 . GLU B 1 190 ? 24.069 -13.148 -31.893 1.00 60.43  ? 207 GLU B OE2 1 
ATOM   3503 N N   . ARG B 1 191 ? 21.065 -13.486 -26.062 1.00 39.05  ? 208 ARG B N   1 
ATOM   3504 C CA  . ARG B 1 191 ? 20.805 -14.148 -24.789 1.00 43.46  ? 208 ARG B CA  1 
ATOM   3505 C C   . ARG B 1 191 ? 21.580 -15.458 -24.752 1.00 37.28  ? 208 ARG B C   1 
ATOM   3506 O O   . ARG B 1 191 ? 21.434 -16.286 -25.657 1.00 39.85  ? 208 ARG B O   1 
ATOM   3507 C CB  . ARG B 1 191 ? 19.321 -14.441 -24.573 1.00 49.58  ? 208 ARG B CB  1 
ATOM   3508 C CG  . ARG B 1 191 ? 19.042 -15.001 -23.170 1.00 41.90  ? 208 ARG B CG  1 
ATOM   3509 C CD  . ARG B 1 191 ? 17.580 -15.378 -22.962 1.00 60.97  ? 208 ARG B CD  1 
ATOM   3510 N NE  . ARG B 1 191 ? 16.717 -14.368 -23.557 1.00 73.48  ? 208 ARG B NE  1 
ATOM   3511 C CZ  . ARG B 1 191 ? 16.314 -13.257 -22.953 1.00 71.60  ? 208 ARG B CZ  1 
ATOM   3512 N NH1 . ARG B 1 191 ? 16.494 -13.067 -21.650 1.00 69.65  ? 208 ARG B NH1 1 
ATOM   3513 N NH2 . ARG B 1 191 ? 15.726 -12.308 -23.676 1.00 64.86  ? 208 ARG B NH2 1 
ATOM   3514 N N   . VAL B 1 192 ? 22.406 -15.635 -23.726 1.00 30.98  ? 209 VAL B N   1 
ATOM   3515 C CA  . VAL B 1 192 ? 23.238 -16.828 -23.609 1.00 35.88  ? 209 VAL B CA  1 
ATOM   3516 C C   . VAL B 1 192 ? 22.401 -17.973 -23.050 1.00 37.39  ? 209 VAL B C   1 
ATOM   3517 O O   . VAL B 1 192 ? 21.717 -17.818 -22.036 1.00 33.93  ? 209 VAL B O   1 
ATOM   3518 C CB  . VAL B 1 192 ? 24.452 -16.570 -22.707 1.00 33.78  ? 209 VAL B CB  1 
ATOM   3519 C CG1 . VAL B 1 192 ? 25.288 -17.820 -22.617 1.00 32.93  ? 209 VAL B CG1 1 
ATOM   3520 C CG2 . VAL B 1 192 ? 25.275 -15.422 -23.236 1.00 34.25  ? 209 VAL B CG2 1 
ATOM   3521 N N   . THR B 1 193 ? 22.511 -19.139 -23.676 1.00 33.00  ? 210 THR B N   1 
ATOM   3522 C CA  . THR B 1 193 ? 21.856 -20.357 -23.229 1.00 35.82  ? 210 THR B CA  1 
ATOM   3523 C C   . THR B 1 193 ? 22.843 -21.416 -22.767 1.00 35.42  ? 210 THR B C   1 
ATOM   3524 O O   . THR B 1 193 ? 22.475 -22.280 -21.985 1.00 34.69  ? 210 THR B O   1 
ATOM   3525 C CB  . THR B 1 193 ? 20.989 -20.952 -24.359 1.00 41.51  ? 210 THR B CB  1 
ATOM   3526 O OG1 . THR B 1 193 ? 21.821 -21.325 -25.473 1.00 39.03  ? 210 THR B OG1 1 
ATOM   3527 C CG2 . THR B 1 193 ? 19.946 -19.949 -24.835 1.00 38.15  ? 210 THR B CG2 1 
ATOM   3528 N N   . HIS B 1 194 ? 24.059 -21.420 -23.296 1.00 33.85  ? 211 HIS B N   1 
ATOM   3529 C CA  . HIS B 1 194 ? 25.057 -22.413 -22.939 1.00 31.04  ? 211 HIS B CA  1 
ATOM   3530 C C   . HIS B 1 194 ? 26.409 -21.754 -23.108 1.00 33.92  ? 211 HIS B C   1 
ATOM   3531 O O   . HIS B 1 194 ? 26.556 -20.774 -23.843 1.00 30.92  ? 211 HIS B O   1 
ATOM   3532 C CB  . HIS B 1 194 ? 25.026 -23.686 -23.812 1.00 40.42  ? 211 HIS B CB  1 
ATOM   3533 C CG  . HIS B 1 194 ? 23.685 -24.351 -23.908 1.00 43.19  ? 211 HIS B CG  1 
ATOM   3534 N ND1 . HIS B 1 194 ? 22.723 -23.958 -24.815 1.00 41.47  ? 211 HIS B ND1 1 
ATOM   3535 C CD2 . HIS B 1 194 ? 23.161 -25.409 -23.239 1.00 44.62  ? 211 HIS B CD2 1 
ATOM   3536 C CE1 . HIS B 1 194 ? 21.663 -24.740 -24.697 1.00 42.26  ? 211 HIS B CE1 1 
ATOM   3537 N NE2 . HIS B 1 194 ? 21.904 -25.628 -23.746 1.00 41.58  ? 211 HIS B NE2 1 
ATOM   3538 N N   . ILE B 1 195 ? 27.399 -22.308 -22.440 1.00 27.76  ? 212 ILE B N   1 
ATOM   3539 C CA  . ILE B 1 195 ? 28.767 -21.860 -22.608 1.00 27.60  ? 212 ILE B CA  1 
ATOM   3540 C C   . ILE B 1 195 ? 29.652 -23.093 -22.586 1.00 30.63  ? 212 ILE B C   1 
ATOM   3541 O O   . ILE B 1 195 ? 29.371 -24.048 -21.860 1.00 29.99  ? 212 ILE B O   1 
ATOM   3542 C CB  . ILE B 1 195 ? 29.123 -20.826 -21.529 1.00 28.19  ? 212 ILE B CB  1 
ATOM   3543 C CG1 . ILE B 1 195 ? 30.502 -20.272 -21.769 1.00 28.99  ? 212 ILE B CG1 1 
ATOM   3544 C CG2 . ILE B 1 195 ? 29.046 -21.445 -20.152 1.00 39.95  ? 212 ILE B CG2 1 
ATOM   3545 C CD1 . ILE B 1 195 ? 30.691 -18.913 -21.108 1.00 43.68  ? 212 ILE B CD1 1 
ATOM   3546 N N   . VAL B 1 196 ? 30.684 -23.114 -23.433 1.00 27.92  ? 213 VAL B N   1 
ATOM   3547 C CA  . VAL B 1 196 ? 31.537 -24.292 -23.561 1.00 27.91  ? 213 VAL B CA  1 
ATOM   3548 C C   . VAL B 1 196 ? 32.976 -23.841 -23.565 1.00 28.92  ? 213 VAL B C   1 
ATOM   3549 O O   . VAL B 1 196 ? 33.351 -22.940 -24.318 1.00 28.06  ? 213 VAL B O   1 
ATOM   3550 C CB  . VAL B 1 196 ? 31.204 -25.120 -24.823 1.00 33.55  ? 213 VAL B CB  1 
ATOM   3551 C CG1 . VAL B 1 196 ? 31.422 -24.341 -26.088 1.00 33.74  ? 213 VAL B CG1 1 
ATOM   3552 C CG2 . VAL B 1 196 ? 32.068 -26.378 -24.883 1.00 39.62  ? 213 VAL B CG2 1 
ATOM   3553 N N   . GLU B 1 197 ? 33.791 -24.497 -22.752 1.00 33.80  ? 214 GLU B N   1 
ATOM   3554 C CA  . GLU B 1 197 ? 35.174 -24.091 -22.568 1.00 39.09  ? 214 GLU B CA  1 
ATOM   3555 C C   . GLU B 1 197 ? 36.058 -24.895 -23.519 1.00 35.52  ? 214 GLU B C   1 
ATOM   3556 O O   . GLU B 1 197 ? 36.070 -26.128 -23.477 1.00 32.20  ? 214 GLU B O   1 
ATOM   3557 C CB  . GLU B 1 197 ? 35.603 -24.280 -21.107 1.00 38.85  ? 214 GLU B CB  1 
ATOM   3558 C CG  . GLU B 1 197 ? 36.954 -23.657 -20.845 1.00 54.61  ? 214 GLU B CG  1 
ATOM   3559 C CD  . GLU B 1 197 ? 36.902 -22.146 -20.991 1.00 50.05  ? 214 GLU B CD  1 
ATOM   3560 O OE1 . GLU B 1 197 ? 35.831 -21.563 -20.700 1.00 49.00  ? 214 GLU B OE1 1 
ATOM   3561 O OE2 . GLU B 1 197 ? 37.893 -21.552 -21.448 1.00 53.99  ? 214 GLU B OE2 1 
ATOM   3562 N N   . LYS B 1 198 ? 36.762 -24.188 -24.392 1.00 33.47  ? 215 LYS B N   1 
ATOM   3563 C CA  . LYS B 1 198 ? 37.746 -24.766 -25.299 1.00 40.32  ? 215 LYS B CA  1 
ATOM   3564 C C   . LYS B 1 198 ? 37.212 -25.910 -26.163 1.00 38.32  ? 215 LYS B C   1 
ATOM   3565 O O   . LYS B 1 198 ? 37.778 -27.014 -26.164 1.00 39.71  ? 215 LYS B O   1 
ATOM   3566 C CB  . LYS B 1 198 ? 38.963 -25.214 -24.501 1.00 46.70  ? 215 LYS B CB  1 
ATOM   3567 C CG  . LYS B 1 198 ? 39.674 -24.049 -23.801 1.00 47.07  ? 215 LYS B CG  1 
ATOM   3568 C CD  . LYS B 1 198 ? 40.955 -24.492 -23.125 1.00 55.64  ? 215 LYS B CD  1 
ATOM   3569 C CE  . LYS B 1 198 ? 41.708 -23.295 -22.559 1.00 64.73  ? 215 LYS B CE  1 
ATOM   3570 N NZ  . LYS B 1 198 ? 40.970 -22.715 -21.396 1.00 60.32  ? 215 LYS B NZ  1 
ATOM   3571 N N   . PRO B 1 199 ? 36.143 -25.690 -26.923 1.00 31.85  ? 216 PRO B N   1 
ATOM   3572 C CA  . PRO B 1 199 ? 35.637 -26.764 -27.785 1.00 32.27  ? 216 PRO B CA  1 
ATOM   3573 C C   . PRO B 1 199 ? 36.600 -27.055 -28.914 1.00 33.30  ? 216 PRO B C   1 
ATOM   3574 O O   . PRO B 1 199 ? 37.343 -26.183 -29.375 1.00 38.11  ? 216 PRO B O   1 
ATOM   3575 C CB  . PRO B 1 199 ? 34.325 -26.195 -28.332 1.00 33.21  ? 216 PRO B CB  1 
ATOM   3576 C CG  . PRO B 1 199 ? 34.627 -24.716 -28.423 1.00 31.42  ? 216 PRO B CG  1 
ATOM   3577 C CD  . PRO B 1 199 ? 35.441 -24.420 -27.178 1.00 32.98  ? 216 PRO B CD  1 
ATOM   3578 N N   . ALA B 1 200 ? 36.557 -28.288 -29.389 1.00 39.71  ? 217 ALA B N   1 
ATOM   3579 C CA  . ALA B 1 200 ? 37.223 -28.582 -30.648 1.00 38.58  ? 217 ALA B CA  1 
ATOM   3580 C C   . ALA B 1 200 ? 36.599 -27.737 -31.764 1.00 40.27  ? 217 ALA B C   1 
ATOM   3581 O O   . ALA B 1 200 ? 35.371 -27.554 -31.808 1.00 37.88  ? 217 ALA B O   1 
ATOM   3582 C CB  . ALA B 1 200 ? 37.130 -30.073 -30.978 1.00 38.44  ? 217 ALA B CB  1 
ATOM   3583 N N   . PRO B 1 201 ? 37.398 -27.228 -32.695 1.00 49.31  ? 218 PRO B N   1 
ATOM   3584 C CA  . PRO B 1 201 ? 36.841 -26.320 -33.716 1.00 36.54  ? 218 PRO B CA  1 
ATOM   3585 C C   . PRO B 1 201 ? 35.673 -26.895 -34.480 1.00 40.69  ? 218 PRO B C   1 
ATOM   3586 O O   . PRO B 1 201 ? 34.685 -26.189 -34.713 1.00 39.30  ? 218 PRO B O   1 
ATOM   3587 C CB  . PRO B 1 201 ? 38.043 -26.063 -34.627 1.00 41.39  ? 218 PRO B CB  1 
ATOM   3588 C CG  . PRO B 1 201 ? 39.226 -26.217 -33.731 1.00 45.89  ? 218 PRO B CG  1 
ATOM   3589 C CD  . PRO B 1 201 ? 38.864 -27.333 -32.785 1.00 54.68  ? 218 PRO B CD  1 
ATOM   3590 N N   . GLU B 1 202 ? 35.738 -28.179 -34.835 1.00 39.80  ? 219 GLU B N   1 
ATOM   3591 C CA  . GLU B 1 202 ? 34.661 -28.830 -35.559 1.00 40.47  ? 219 GLU B CA  1 
ATOM   3592 C C   . GLU B 1 202 ? 33.394 -28.938 -34.732 1.00 41.65  ? 219 GLU B C   1 
ATOM   3593 O O   . GLU B 1 202 ? 32.317 -29.182 -35.290 1.00 39.99  ? 219 GLU B O   1 
ATOM   3594 C CB  . GLU B 1 202 ? 35.085 -30.244 -35.964 1.00 45.94  ? 219 GLU B CB  1 
ATOM   3595 C CG  . GLU B 1 202 ? 36.381 -30.353 -36.786 1.00 58.93  ? 219 GLU B CG  1 
ATOM   3596 C CD  . GLU B 1 202 ? 37.652 -30.159 -35.951 1.00 70.61  ? 219 GLU B CD  1 
ATOM   3597 O OE1 . GLU B 1 202 ? 37.582 -30.258 -34.702 1.00 48.47  ? 219 GLU B OE1 1 
ATOM   3598 O OE2 . GLU B 1 202 ? 38.726 -29.911 -36.553 1.00 76.17  ? 219 GLU B OE2 1 
ATOM   3599 N N   . GLN B 1 203 ? 33.504 -28.785 -33.420 1.00 38.70  ? 220 GLN B N   1 
ATOM   3600 C CA  . GLN B 1 203 ? 32.394 -29.008 -32.506 1.00 39.37  ? 220 GLN B CA  1 
ATOM   3601 C C   . GLN B 1 203 ? 31.957 -27.746 -31.785 1.00 37.54  ? 220 GLN B C   1 
ATOM   3602 O O   . GLN B 1 203 ? 31.132 -27.831 -30.870 1.00 37.49  ? 220 GLN B O   1 
ATOM   3603 C CB  . GLN B 1 203 ? 32.789 -30.072 -31.468 1.00 34.84  ? 220 GLN B CB  1 
ATOM   3604 C CG  . GLN B 1 203 ? 33.074 -31.397 -32.124 1.00 35.56  ? 220 GLN B CG  1 
ATOM   3605 C CD  . GLN B 1 203 ? 33.561 -32.478 -31.199 1.00 35.96  ? 220 GLN B CD  1 
ATOM   3606 O OE1 . GLN B 1 203 ? 34.091 -32.225 -30.103 1.00 34.90  ? 220 GLN B OE1 1 
ATOM   3607 N NE2 . GLN B 1 203 ? 33.368 -33.711 -31.634 1.00 37.64  ? 220 GLN B NE2 1 
ATOM   3608 N N   . ALA B 1 204 ? 32.508 -26.600 -32.135 1.00 37.58  ? 221 ALA B N   1 
ATOM   3609 C CA  . ALA B 1 204 ? 32.159 -25.376 -31.428 1.00 34.04  ? 221 ALA B CA  1 
ATOM   3610 C C   . ALA B 1 204 ? 30.742 -24.961 -31.791 1.00 34.95  ? 221 ALA B C   1 
ATOM   3611 O O   . ALA B 1 204 ? 30.400 -24.909 -32.983 1.00 34.76  ? 221 ALA B O   1 
ATOM   3612 C CB  . ALA B 1 204 ? 33.129 -24.262 -31.765 1.00 39.10  ? 221 ALA B CB  1 
ATOM   3613 N N   . PRO B 1 205 ? 29.889 -24.675 -30.814 1.00 33.11  ? 222 PRO B N   1 
ATOM   3614 C CA  . PRO B 1 205 ? 28.497 -24.338 -31.146 1.00 35.84  ? 222 PRO B CA  1 
ATOM   3615 C C   . PRO B 1 205 ? 28.398 -23.062 -31.941 1.00 35.97  ? 222 PRO B C   1 
ATOM   3616 O O   . PRO B 1 205 ? 27.479 -22.916 -32.746 1.00 33.23  ? 222 PRO B O   1 
ATOM   3617 C CB  . PRO B 1 205 ? 27.828 -24.216 -29.765 1.00 37.52  ? 222 PRO B CB  1 
ATOM   3618 C CG  . PRO B 1 205 ? 28.909 -23.814 -28.899 1.00 35.96  ? 222 PRO B CG  1 
ATOM   3619 C CD  . PRO B 1 205 ? 30.129 -24.566 -29.366 1.00 35.88  ? 222 PRO B CD  1 
ATOM   3620 N N   . THR B 1 206 ? 29.321 -22.134 -31.734 1.00 32.65  ? 223 THR B N   1 
ATOM   3621 C CA  . THR B 1 206 ? 29.377 -20.897 -32.487 1.00 35.28  ? 223 THR B CA  1 
ATOM   3622 C C   . THR B 1 206 ? 30.842 -20.509 -32.557 1.00 29.46  ? 223 THR B C   1 
ATOM   3623 O O   . THR B 1 206 ? 31.709 -21.252 -32.086 1.00 35.54  ? 223 THR B O   1 
ATOM   3624 C CB  . THR B 1 206 ? 28.572 -19.767 -31.835 1.00 35.78  ? 223 THR B CB  1 
ATOM   3625 O OG1 . THR B 1 206 ? 29.324 -19.254 -30.738 1.00 31.61  ? 223 THR B OG1 1 
ATOM   3626 C CG2 . THR B 1 206 ? 27.215 -20.245 -31.358 1.00 39.20  ? 223 THR B CG2 1 
ATOM   3627 N N   . THR B 1 207 ? 31.119 -19.333 -33.122 1.00 32.72  ? 224 THR B N   1 
ATOM   3628 C CA  . THR B 1 207 ? 32.448 -18.733 -33.101 1.00 31.64  ? 224 THR B CA  1 
ATOM   3629 C C   . THR B 1 207 ? 32.425 -17.432 -32.303 1.00 35.11  ? 224 THR B C   1 
ATOM   3630 O O   . THR B 1 207 ? 33.247 -16.549 -32.503 1.00 32.59  ? 224 THR B O   1 
ATOM   3631 C CB  . THR B 1 207 ? 32.979 -18.502 -34.524 1.00 37.78  ? 224 THR B CB  1 
ATOM   3632 O OG1 . THR B 1 207 ? 32.029 -17.745 -35.303 1.00 35.09  ? 224 THR B OG1 1 
ATOM   3633 C CG2 . THR B 1 207 ? 33.271 -19.842 -35.222 1.00 35.29  ? 224 THR B CG2 1 
ATOM   3634 N N   . LEU B 1 208 ? 31.498 -17.314 -31.367 1.00 32.23  ? 225 LEU B N   1 
ATOM   3635 C CA  . LEU B 1 208 ? 31.379 -16.122 -30.532 1.00 34.24  ? 225 LEU B CA  1 
ATOM   3636 C C   . LEU B 1 208 ? 32.106 -16.404 -29.216 1.00 34.96  ? 225 LEU B C   1 
ATOM   3637 O O   . LEU B 1 208 ? 31.637 -17.203 -28.399 1.00 35.86  ? 225 LEU B O   1 
ATOM   3638 C CB  . LEU B 1 208 ? 29.895 -15.811 -30.350 1.00 40.79  ? 225 LEU B CB  1 
ATOM   3639 C CG  . LEU B 1 208 ? 29.455 -14.439 -29.854 1.00 50.16  ? 225 LEU B CG  1 
ATOM   3640 C CD1 . LEU B 1 208 ? 29.963 -13.367 -30.818 1.00 45.53  ? 225 LEU B CD1 1 
ATOM   3641 C CD2 . LEU B 1 208 ? 27.933 -14.386 -29.759 1.00 48.50  ? 225 LEU B CD2 1 
ATOM   3642 N N   . ALA B 1 209 ? 33.256 -15.757 -29.009 1.00 31.35  ? 226 ALA B N   1 
ATOM   3643 C CA  . ALA B 1 209 ? 34.122 -16.056 -27.881 1.00 35.37  ? 226 ALA B CA  1 
ATOM   3644 C C   . ALA B 1 209 ? 34.027 -14.991 -26.793 1.00 31.32  ? 226 ALA B C   1 
ATOM   3645 O O   . ALA B 1 209 ? 33.910 -13.795 -27.075 1.00 29.10  ? 226 ALA B O   1 
ATOM   3646 C CB  . ALA B 1 209 ? 35.577 -16.170 -28.308 1.00 34.88  ? 226 ALA B CB  1 
ATOM   3647 N N   . VAL B 1 210 ? 34.112 -15.444 -25.545 1.00 30.82  ? 227 VAL B N   1 
ATOM   3648 C CA  . VAL B 1 210 ? 34.166 -14.538 -24.396 1.00 32.57  ? 227 VAL B CA  1 
ATOM   3649 C C   . VAL B 1 210 ? 35.537 -13.885 -24.311 1.00 31.46  ? 227 VAL B C   1 
ATOM   3650 O O   . VAL B 1 210 ? 36.564 -14.572 -24.246 1.00 37.30  ? 227 VAL B O   1 
ATOM   3651 C CB  . VAL B 1 210 ? 33.860 -15.309 -23.109 1.00 31.26  ? 227 VAL B CB  1 
ATOM   3652 C CG1 . VAL B 1 210 ? 33.912 -14.363 -21.919 1.00 30.25  ? 227 VAL B CG1 1 
ATOM   3653 C CG2 . VAL B 1 210 ? 32.500 -15.959 -23.190 1.00 33.01  ? 227 VAL B CG2 1 
ATOM   3654 N N   . VAL B 1 211 ? 35.561 -12.562 -24.208 1.00 26.94  ? 228 VAL B N   1 
ATOM   3655 C CA  . VAL B 1 211 ? 36.794 -11.833 -23.939 1.00 26.24  ? 228 VAL B CA  1 
ATOM   3656 C C   . VAL B 1 211 ? 36.784 -11.364 -22.481 1.00 34.06  ? 228 VAL B C   1 
ATOM   3657 O O   . VAL B 1 211 ? 35.804 -11.541 -21.751 1.00 36.40  ? 228 VAL B O   1 
ATOM   3658 C CB  . VAL B 1 211 ? 36.995 -10.657 -24.897 1.00 35.69  ? 228 VAL B CB  1 
ATOM   3659 C CG1 . VAL B 1 211 ? 36.725 -11.130 -26.346 1.00 38.08  ? 228 VAL B CG1 1 
ATOM   3660 C CG2 . VAL B 1 211 ? 36.127 -9.496  -24.465 1.00 32.31  ? 228 VAL B CG2 1 
ATOM   3661 N N   . GLY B 1 212 ? 37.912 -10.812 -22.047 1.00 29.09  ? 229 GLY B N   1 
ATOM   3662 C CA  . GLY B 1 212 ? 38.076 -10.440 -20.651 1.00 30.72  ? 229 GLY B CA  1 
ATOM   3663 C C   . GLY B 1 212 ? 37.381 -9.168  -20.194 1.00 25.38  ? 229 GLY B C   1 
ATOM   3664 O O   . GLY B 1 212 ? 38.015 -8.265  -19.647 1.00 28.86  ? 229 GLY B O   1 
ATOM   3665 N N   . ARG B 1 213 ? 36.071 -9.104  -20.397 1.00 26.46  ? 230 ARG B N   1 
ATOM   3666 C CA  . ARG B 1 213 ? 35.261 -7.988  -19.934 1.00 26.55  ? 230 ARG B CA  1 
ATOM   3667 C C   . ARG B 1 213 ? 33.927 -8.583  -19.539 1.00 25.45  ? 230 ARG B C   1 
ATOM   3668 O O   . ARG B 1 213 ? 33.287 -9.221  -20.372 1.00 26.91  ? 230 ARG B O   1 
ATOM   3669 C CB  . ARG B 1 213 ? 35.065 -6.933  -21.020 1.00 23.99  ? 230 ARG B CB  1 
ATOM   3670 C CG  . ARG B 1 213 ? 36.316 -6.213  -21.476 1.00 24.07  ? 230 ARG B CG  1 
ATOM   3671 C CD  . ARG B 1 213 ? 36.844 -5.330  -20.410 1.00 25.93  ? 230 ARG B CD  1 
ATOM   3672 N NE  . ARG B 1 213 ? 37.913 -4.496  -20.931 1.00 23.93  ? 230 ARG B NE  1 
ATOM   3673 C CZ  . ARG B 1 213 ? 39.159 -4.907  -21.109 1.00 27.33  ? 230 ARG B CZ  1 
ATOM   3674 N NH1 . ARG B 1 213 ? 39.533 -6.138  -20.801 1.00 26.55  ? 230 ARG B NH1 1 
ATOM   3675 N NH2 . ARG B 1 213 ? 40.056 -4.057  -21.593 1.00 30.29  ? 230 ARG B NH2 1 
ATOM   3676 N N   . TYR B 1 214 ? 33.534 -8.413  -18.284 1.00 25.31  ? 231 TYR B N   1 
ATOM   3677 C CA  . TYR B 1 214 ? 32.273 -8.943  -17.784 1.00 27.94  ? 231 TYR B CA  1 
ATOM   3678 C C   . TYR B 1 214 ? 31.563 -7.893  -16.934 1.00 24.43  ? 231 TYR B C   1 
ATOM   3679 O O   . TYR B 1 214 ? 32.212 -7.074  -16.283 1.00 26.43  ? 231 TYR B O   1 
ATOM   3680 C CB  . TYR B 1 214 ? 32.473 -10.178 -16.923 1.00 26.80  ? 231 TYR B CB  1 
ATOM   3681 C CG  . TYR B 1 214 ? 33.409 -11.242 -17.454 1.00 24.88  ? 231 TYR B CG  1 
ATOM   3682 C CD1 . TYR B 1 214 ? 34.765 -11.051 -17.443 1.00 26.09  ? 231 TYR B CD1 1 
ATOM   3683 C CD2 . TYR B 1 214 ? 32.922 -12.473 -17.887 1.00 29.71  ? 231 TYR B CD2 1 
ATOM   3684 C CE1 . TYR B 1 214 ? 35.637 -12.027 -17.907 1.00 28.18  ? 231 TYR B CE1 1 
ATOM   3685 C CE2 . TYR B 1 214 ? 33.777 -13.464 -18.336 1.00 30.76  ? 231 TYR B CE2 1 
ATOM   3686 C CZ  . TYR B 1 214 ? 35.136 -13.235 -18.348 1.00 27.51  ? 231 TYR B CZ  1 
ATOM   3687 O OH  . TYR B 1 214 ? 35.998 -14.217 -18.780 1.00 31.49  ? 231 TYR B OH  1 
ATOM   3688 N N   . VAL B 1 215 ? 30.226 -7.940  -16.954 1.00 27.26  ? 232 VAL B N   1 
ATOM   3689 C CA  . VAL B 1 215 ? 29.354 -7.279  -15.984 1.00 25.77  ? 232 VAL B CA  1 
ATOM   3690 C C   . VAL B 1 215 ? 28.501 -8.385  -15.386 1.00 29.89  ? 232 VAL B C   1 
ATOM   3691 O O   . VAL B 1 215 ? 27.738 -9.043  -16.103 1.00 28.58  ? 232 VAL B O   1 
ATOM   3692 C CB  . VAL B 1 215 ? 28.461 -6.199  -16.607 1.00 27.17  ? 232 VAL B CB  1 
ATOM   3693 C CG1 . VAL B 1 215 ? 27.621 -5.533  -15.544 1.00 30.35  ? 232 VAL B CG1 1 
ATOM   3694 C CG2 . VAL B 1 215 ? 29.288 -5.141  -17.353 1.00 34.50  ? 232 VAL B CG2 1 
ATOM   3695 N N   . LEU B 1 216 ? 28.640 -8.607  -14.084 1.00 27.13  ? 233 LEU B N   1 
ATOM   3696 C CA  . LEU B 1 216 ? 28.049 -9.762  -13.434 1.00 35.50  ? 233 LEU B CA  1 
ATOM   3697 C C   . LEU B 1 216 ? 27.194 -9.328  -12.257 1.00 30.51  ? 233 LEU B C   1 
ATOM   3698 O O   . LEU B 1 216 ? 27.607 -8.484  -11.454 1.00 29.74  ? 233 LEU B O   1 
ATOM   3699 C CB  . LEU B 1 216 ? 29.144 -10.706 -12.927 1.00 30.10  ? 233 LEU B CB  1 
ATOM   3700 C CG  . LEU B 1 216 ? 30.153 -11.205 -13.956 1.00 31.20  ? 233 LEU B CG  1 
ATOM   3701 C CD1 . LEU B 1 216 ? 31.318 -11.935 -13.246 1.00 31.80  ? 233 LEU B CD1 1 
ATOM   3702 C CD2 . LEU B 1 216 ? 29.438 -12.089 -14.944 1.00 29.96  ? 233 LEU B CD2 1 
ATOM   3703 N N   . GLU B 1 217 ? 26.025 -9.946  -12.138 1.00 29.14  ? 234 GLU B N   1 
ATOM   3704 C CA  . GLU B 1 217 ? 25.212 -9.773  -10.952 1.00 35.33  ? 234 GLU B CA  1 
ATOM   3705 C C   . GLU B 1 217 ? 25.850 -10.506 -9.782  1.00 34.46  ? 234 GLU B C   1 
ATOM   3706 O O   . GLU B 1 217 ? 26.550 -11.517 -9.951  1.00 30.30  ? 234 GLU B O   1 
ATOM   3707 C CB  . GLU B 1 217 ? 23.783 -10.272 -11.203 1.00 35.80  ? 234 GLU B CB  1 
ATOM   3708 C CG  . GLU B 1 217 ? 23.020 -9.354  -12.149 1.00 40.05  ? 234 GLU B CG  1 
ATOM   3709 C CD  . GLU B 1 217 ? 21.541 -9.721  -12.344 1.00 50.75  ? 234 GLU B CD  1 
ATOM   3710 O OE1 . GLU B 1 217 ? 21.225 -10.869 -12.732 1.00 44.79  ? 234 GLU B OE1 1 
ATOM   3711 O OE2 . GLU B 1 217 ? 20.697 -8.834  -12.097 1.00 54.09  ? 234 GLU B OE2 1 
ATOM   3712 N N   . ALA B 1 218 ? 25.622 -9.965  -8.586  1.00 30.83  ? 235 ALA B N   1 
ATOM   3713 C CA  . ALA B 1 218 ? 26.249 -10.515 -7.393  1.00 33.02  ? 235 ALA B CA  1 
ATOM   3714 C C   . ALA B 1 218 ? 25.804 -11.945 -7.128  1.00 33.26  ? 235 ALA B C   1 
ATOM   3715 O O   . ALA B 1 218 ? 26.494 -12.670 -6.415  1.00 33.77  ? 235 ALA B O   1 
ATOM   3716 C CB  . ALA B 1 218 ? 25.954 -9.622  -6.169  1.00 36.87  ? 235 ALA B CB  1 
ATOM   3717 N N   . ALA B 1 219 ? 24.707 -12.385 -7.725  1.00 34.40  ? 236 ALA B N   1 
ATOM   3718 C CA  . ALA B 1 219 ? 24.299 -13.775 -7.588  1.00 38.50  ? 236 ALA B CA  1 
ATOM   3719 C C   . ALA B 1 219 ? 25.349 -14.758 -8.090  1.00 36.21  ? 236 ALA B C   1 
ATOM   3720 O O   . ALA B 1 219 ? 25.266 -15.949 -7.772  1.00 38.22  ? 236 ALA B O   1 
ATOM   3721 C CB  . ALA B 1 219 ? 22.980 -13.996 -8.323  1.00 36.52  ? 236 ALA B CB  1 
ATOM   3722 N N   . ILE B 1 220 ? 26.330 -14.306 -8.868  1.00 36.42  ? 237 ILE B N   1 
ATOM   3723 C CA  . ILE B 1 220 ? 27.376 -15.218 -9.325  1.00 34.27  ? 237 ILE B CA  1 
ATOM   3724 C C   . ILE B 1 220 ? 28.170 -15.785 -8.155  1.00 36.15  ? 237 ILE B C   1 
ATOM   3725 O O   . ILE B 1 220 ? 28.714 -16.888 -8.251  1.00 34.16  ? 237 ILE B O   1 
ATOM   3726 C CB  . ILE B 1 220 ? 28.296 -14.499 -10.322 1.00 33.40  ? 237 ILE B CB  1 
ATOM   3727 C CG1 . ILE B 1 220 ? 29.386 -15.421 -10.881 1.00 43.19  ? 237 ILE B CG1 1 
ATOM   3728 C CG2 . ILE B 1 220 ? 29.030 -13.378 -9.652  1.00 33.47  ? 237 ILE B CG2 1 
ATOM   3729 C CD1 . ILE B 1 220 ? 28.958 -16.271 -11.985 1.00 38.22  ? 237 ILE B CD1 1 
ATOM   3730 N N   . PHE B 1 221 ? 28.295 -15.028 -7.055  1.00 35.84  ? 238 PHE B N   1 
ATOM   3731 C CA  . PHE B 1 221 ? 29.169 -15.439 -5.962  1.00 36.31  ? 238 PHE B CA  1 
ATOM   3732 C C   . PHE B 1 221 ? 28.711 -16.769 -5.373  1.00 41.08  ? 238 PHE B C   1 
ATOM   3733 O O   . PHE B 1 221 ? 29.528 -17.669 -5.138  1.00 34.20  ? 238 PHE B O   1 
ATOM   3734 C CB  . PHE B 1 221 ? 29.193 -14.353 -4.883  1.00 36.19  ? 238 PHE B CB  1 
ATOM   3735 C CG  . PHE B 1 221 ? 29.904 -13.102 -5.301  1.00 37.07  ? 238 PHE B CG  1 
ATOM   3736 C CD1 . PHE B 1 221 ? 31.161 -13.162 -5.893  1.00 35.46  ? 238 PHE B CD1 1 
ATOM   3737 C CD2 . PHE B 1 221 ? 29.332 -11.863 -5.085  1.00 36.22  ? 238 PHE B CD2 1 
ATOM   3738 C CE1 . PHE B 1 221 ? 31.836 -11.998 -6.273  1.00 33.58  ? 238 PHE B CE1 1 
ATOM   3739 C CE2 . PHE B 1 221 ? 30.003 -10.702 -5.451  1.00 35.40  ? 238 PHE B CE2 1 
ATOM   3740 C CZ  . PHE B 1 221 ? 31.255 -10.774 -6.056  1.00 31.36  ? 238 PHE B CZ  1 
ATOM   3741 N N   . ASP B 1 222 ? 27.402 -16.926 -5.170  1.00 44.59  ? 239 ASP B N   1 
ATOM   3742 C CA  . ASP B 1 222 ? 26.888 -18.185 -4.638  1.00 46.11  ? 239 ASP B CA  1 
ATOM   3743 C C   . ASP B 1 222 ? 27.210 -19.356 -5.562  1.00 47.58  ? 239 ASP B C   1 
ATOM   3744 O O   . ASP B 1 222 ? 27.495 -20.467 -5.093  1.00 44.30  ? 239 ASP B O   1 
ATOM   3745 C CB  . ASP B 1 222 ? 25.376 -18.085 -4.412  1.00 54.33  ? 239 ASP B CB  1 
ATOM   3746 C CG  . ASP B 1 222 ? 25.011 -17.330 -3.130  1.00 66.14  ? 239 ASP B CG  1 
ATOM   3747 O OD1 . ASP B 1 222 ? 25.825 -17.287 -2.165  1.00 52.94  ? 239 ASP B OD1 1 
ATOM   3748 O OD2 . ASP B 1 222 ? 23.878 -16.804 -3.081  1.00 73.26  ? 239 ASP B OD2 1 
ATOM   3749 N N   . HIS B 1 223 ? 27.193 -19.125 -6.882  1.00 42.74  ? 240 HIS B N   1 
ATOM   3750 C CA  . HIS B 1 223 ? 27.480 -20.206 -7.818  1.00 43.49  ? 240 HIS B CA  1 
ATOM   3751 C C   . HIS B 1 223 ? 28.963 -20.550 -7.860  1.00 43.85  ? 240 HIS B C   1 
ATOM   3752 O O   . HIS B 1 223 ? 29.314 -21.690 -8.168  1.00 48.63  ? 240 HIS B O   1 
ATOM   3753 C CB  . HIS B 1 223 ? 26.954 -19.841 -9.204  1.00 42.68  ? 240 HIS B CB  1 
ATOM   3754 C CG  . HIS B 1 223 ? 25.462 -19.739 -9.264  1.00 41.77  ? 240 HIS B CG  1 
ATOM   3755 N ND1 . HIS B 1 223 ? 24.639 -20.847 -9.204  1.00 46.06  ? 240 HIS B ND1 1 
ATOM   3756 C CD2 . HIS B 1 223 ? 24.642 -18.663 -9.328  1.00 40.92  ? 240 HIS B CD2 1 
ATOM   3757 C CE1 . HIS B 1 223 ? 23.378 -20.457 -9.250  1.00 45.37  ? 240 HIS B CE1 1 
ATOM   3758 N NE2 . HIS B 1 223 ? 23.350 -19.137 -9.319  1.00 45.84  ? 240 HIS B NE2 1 
ATOM   3759 N N   . LEU B 1 224 ? 29.844 -19.607 -7.538  1.00 38.15  ? 241 LEU B N   1 
ATOM   3760 C CA  . LEU B 1 224 ? 31.265 -19.923 -7.451  1.00 38.80  ? 241 LEU B CA  1 
ATOM   3761 C C   . LEU B 1 224 ? 31.661 -20.574 -6.120  1.00 48.48  ? 241 LEU B C   1 
ATOM   3762 O O   . LEU B 1 224 ? 32.723 -21.199 -6.058  1.00 50.61  ? 241 LEU B O   1 
ATOM   3763 C CB  . LEU B 1 224 ? 32.088 -18.648 -7.643  1.00 33.15  ? 241 LEU B CB  1 
ATOM   3764 C CG  . LEU B 1 224 ? 31.967 -17.967 -9.011  1.00 36.71  ? 241 LEU B CG  1 
ATOM   3765 C CD1 . LEU B 1 224 ? 32.579 -16.569 -8.918  1.00 36.05  ? 241 LEU B CD1 1 
ATOM   3766 C CD2 . LEU B 1 224 ? 32.662 -18.792 -10.056 1.00 30.11  ? 241 LEU B CD2 1 
ATOM   3767 N N   . ARG B 1 225 ? 30.868 -20.410 -5.048  1.00 44.00  ? 242 ARG B N   1 
ATOM   3768 C CA  . ARG B 1 225 ? 31.130 -21.130 -3.796  1.00 49.57  ? 242 ARG B CA  1 
ATOM   3769 C C   . ARG B 1 225 ? 30.727 -22.600 -3.883  1.00 56.24  ? 242 ARG B C   1 
ATOM   3770 O O   . ARG B 1 225 ? 31.312 -23.439 -3.196  1.00 61.39  ? 242 ARG B O   1 
ATOM   3771 C CB  . ARG B 1 225 ? 30.383 -20.494 -2.625  1.00 48.27  ? 242 ARG B CB  1 
ATOM   3772 C CG  . ARG B 1 225 ? 30.782 -19.098 -2.333  1.00 48.18  ? 242 ARG B CG  1 
ATOM   3773 C CD  . ARG B 1 225 ? 30.265 -18.601 -1.008  1.00 45.36  ? 242 ARG B CD  1 
ATOM   3774 N NE  . ARG B 1 225 ? 30.703 -17.233 -0.753  1.00 49.75  ? 242 ARG B NE  1 
ATOM   3775 C CZ  . ARG B 1 225 ? 29.994 -16.154 -1.061  1.00 47.93  ? 242 ARG B CZ  1 
ATOM   3776 N NH1 . ARG B 1 225 ? 28.756 -16.248 -1.525  1.00 44.64  ? 242 ARG B NH1 1 
ATOM   3777 N NH2 . ARG B 1 225 ? 30.535 -14.951 -0.887  1.00 45.11  ? 242 ARG B NH2 1 
ATOM   3778 N N   . ALA B 1 226 ? 29.718 -22.921 -4.702  1.00 75.44  ? 243 ALA B N   1 
ATOM   3779 C CA  . ALA B 1 226 ? 29.329 -24.313 -4.921  1.00 80.49  ? 243 ALA B CA  1 
ATOM   3780 C C   . ALA B 1 226 ? 30.355 -25.066 -5.767  1.00 87.98  ? 243 ALA B C   1 
ATOM   3781 O O   . ALA B 1 226 ? 30.508 -26.285 -5.614  1.00 98.81  ? 243 ALA B O   1 
ATOM   3782 C CB  . ALA B 1 226 ? 27.950 -24.364 -5.593  1.00 68.79  ? 243 ALA B CB  1 
ATOM   3783 N N   . THR B 1 227 ? 31.075 -24.357 -6.639  1.00 91.06  ? 244 THR B N   1 
ATOM   3784 C CA  . THR B 1 227 ? 31.973 -24.962 -7.629  1.00 91.06  ? 244 THR B CA  1 
ATOM   3785 C C   . THR B 1 227 ? 33.147 -25.714 -7.025  1.00 98.51  ? 244 THR B C   1 
ATOM   3786 O O   . THR B 1 227 ? 34.272 -25.600 -7.515  1.00 91.78  ? 244 THR B O   1 
ATOM   3787 C CB  . THR B 1 227 ? 32.560 -23.885 -8.582  1.00 81.06  ? 244 THR B CB  1 
ATOM   3788 N N   . GLU B 1 234 ? 41.521 -25.759 -10.496 1.00 110.66 ? 251 GLU B N   1 
ATOM   3789 C CA  . GLU B 1 234 ? 41.192 -24.341 -10.612 1.00 91.24  ? 251 GLU B CA  1 
ATOM   3790 C C   . GLU B 1 234 ? 39.699 -24.117 -10.888 1.00 92.06  ? 251 GLU B C   1 
ATOM   3791 O O   . GLU B 1 234 ? 39.154 -24.651 -11.851 1.00 89.08  ? 251 GLU B O   1 
ATOM   3792 C CB  . GLU B 1 234 ? 42.024 -23.673 -11.716 1.00 91.84  ? 251 GLU B CB  1 
ATOM   3793 C CG  . GLU B 1 234 ? 43.503 -23.458 -11.357 1.00 92.83  ? 251 GLU B CG  1 
ATOM   3794 C CD  . GLU B 1 234 ? 44.199 -22.435 -12.268 1.00 90.22  ? 251 GLU B CD  1 
ATOM   3795 O OE1 . GLU B 1 234 ? 43.639 -22.117 -13.345 1.00 84.61  ? 251 GLU B OE1 1 
ATOM   3796 O OE2 . GLU B 1 234 ? 45.289 -21.930 -11.890 1.00 76.11  ? 251 GLU B OE2 1 
ATOM   3797 N N   . ILE B 1 235 ? 39.047 -23.336 -10.025 1.00 87.56  ? 252 ILE B N   1 
ATOM   3798 C CA  . ILE B 1 235 ? 37.657 -22.948 -10.246 1.00 75.94  ? 252 ILE B CA  1 
ATOM   3799 C C   . ILE B 1 235 ? 37.574 -21.980 -11.421 1.00 78.03  ? 252 ILE B C   1 
ATOM   3800 O O   . ILE B 1 235 ? 38.181 -20.899 -11.413 1.00 63.62  ? 252 ILE B O   1 
ATOM   3801 C CB  . ILE B 1 235 ? 37.042 -22.322 -8.988  1.00 75.40  ? 252 ILE B CB  1 
ATOM   3802 C CG1 . ILE B 1 235 ? 36.977 -23.363 -7.863  1.00 86.78  ? 252 ILE B CG1 1 
ATOM   3803 C CG2 . ILE B 1 235 ? 35.659 -21.759 -9.340  1.00 53.93  ? 252 ILE B CG2 1 
ATOM   3804 C CD1 . ILE B 1 235 ? 38.240 -23.420 -7.003  1.00 74.11  ? 252 ILE B CD1 1 
ATOM   3805 N N   . GLN B 1 236 ? 36.773 -22.344 -12.409 1.00 66.25  ? 253 GLN B N   1 
ATOM   3806 C CA  . GLN B 1 236 ? 36.641 -21.592 -13.642 1.00 63.15  ? 253 GLN B CA  1 
ATOM   3807 C C   . GLN B 1 236 ? 35.452 -20.651 -13.534 1.00 52.85  ? 253 GLN B C   1 
ATOM   3808 O O   . GLN B 1 236 ? 34.384 -21.025 -13.038 1.00 45.09  ? 253 GLN B O   1 
ATOM   3809 C CB  . GLN B 1 236 ? 36.483 -22.546 -14.831 1.00 70.77  ? 253 GLN B CB  1 
ATOM   3810 C CG  . GLN B 1 236 ? 37.780 -23.242 -15.272 1.00 77.60  ? 253 GLN B CG  1 
ATOM   3811 C CD  . GLN B 1 236 ? 37.653 -24.000 -16.583 1.00 86.04  ? 253 GLN B CD  1 
ATOM   3812 O OE1 . GLN B 1 236 ? 36.541 -24.257 -17.068 1.00 82.06  ? 253 GLN B OE1 1 
ATOM   3813 N NE2 . GLN B 1 236 ? 38.797 -24.358 -17.170 1.00 83.31  ? 253 GLN B NE2 1 
ATOM   3814 N N   . LEU B 1 237 ? 35.647 -19.407 -13.963 1.00 45.06  ? 254 LEU B N   1 
ATOM   3815 C CA  . LEU B 1 237 ? 34.520 -18.486 -13.966 1.00 41.72  ? 254 LEU B CA  1 
ATOM   3816 C C   . LEU B 1 237 ? 33.393 -19.007 -14.857 1.00 42.11  ? 254 LEU B C   1 
ATOM   3817 O O   . LEU B 1 237 ? 32.212 -18.872 -14.507 1.00 40.55  ? 254 LEU B O   1 
ATOM   3818 C CB  . LEU B 1 237 ? 34.983 -17.105 -14.402 1.00 38.29  ? 254 LEU B CB  1 
ATOM   3819 C CG  . LEU B 1 237 ? 33.912 -16.012 -14.476 1.00 38.64  ? 254 LEU B CG  1 
ATOM   3820 C CD1 . LEU B 1 237 ? 33.213 -15.855 -13.161 1.00 32.53  ? 254 LEU B CD1 1 
ATOM   3821 C CD2 . LEU B 1 237 ? 34.561 -14.698 -14.875 1.00 38.73  ? 254 LEU B CD2 1 
ATOM   3822 N N   . THR B 1 238 ? 33.743 -19.649 -15.987 1.00 39.09  ? 255 THR B N   1 
ATOM   3823 C CA  . THR B 1 238 ? 32.734 -20.204 -16.899 1.00 44.40  ? 255 THR B CA  1 
ATOM   3824 C C   . THR B 1 238 ? 31.772 -21.141 -16.176 1.00 42.49  ? 255 THR B C   1 
ATOM   3825 O O   . THR B 1 238 ? 30.586 -21.212 -16.524 1.00 38.56  ? 255 THR B O   1 
ATOM   3826 C CB  . THR B 1 238 ? 33.411 -20.943 -18.065 1.00 42.17  ? 255 THR B CB  1 
ATOM   3827 O OG1 . THR B 1 238 ? 34.044 -20.005 -18.945 1.00 52.05  ? 255 THR B OG1 1 
ATOM   3828 C CG2 . THR B 1 238 ? 32.418 -21.706 -18.886 1.00 53.80  ? 255 THR B CG2 1 
ATOM   3829 N N   . ASP B 1 239 ? 32.266 -21.888 -15.185 1.00 48.08  ? 256 ASP B N   1 
ATOM   3830 C CA  . ASP B 1 239 ? 31.381 -22.753 -14.409 1.00 48.20  ? 256 ASP B CA  1 
ATOM   3831 C C   . ASP B 1 239 ? 30.354 -21.933 -13.653 1.00 40.57  ? 256 ASP B C   1 
ATOM   3832 O O   . ASP B 1 239 ? 29.159 -22.264 -13.646 1.00 42.94  ? 256 ASP B O   1 
ATOM   3833 C CB  . ASP B 1 239 ? 32.180 -23.606 -13.429 1.00 55.50  ? 256 ASP B CB  1 
ATOM   3834 C CG  . ASP B 1 239 ? 33.189 -24.496 -14.116 1.00 69.95  ? 256 ASP B CG  1 
ATOM   3835 O OD1 . ASP B 1 239 ? 32.927 -24.960 -15.246 1.00 65.48  ? 256 ASP B OD1 1 
ATOM   3836 O OD2 . ASP B 1 239 ? 34.259 -24.727 -13.515 1.00 84.83  ? 256 ASP B OD2 1 
ATOM   3837 N N   . GLY B 1 240 ? 30.791 -20.841 -13.036 1.00 40.33  ? 257 GLY B N   1 
ATOM   3838 C CA  . GLY B 1 240 ? 29.845 -19.987 -12.344 1.00 41.57  ? 257 GLY B CA  1 
ATOM   3839 C C   . GLY B 1 240 ? 28.809 -19.415 -13.292 1.00 37.02  ? 257 GLY B C   1 
ATOM   3840 O O   . GLY B 1 240 ? 27.607 -19.446 -13.020 1.00 36.01  ? 257 GLY B O   1 
ATOM   3841 N N   . ILE B 1 241 ? 29.258 -18.929 -14.443 1.00 38.80  ? 258 ILE B N   1 
ATOM   3842 C CA  . ILE B 1 241 ? 28.314 -18.324 -15.373 1.00 38.38  ? 258 ILE B CA  1 
ATOM   3843 C C   . ILE B 1 241 ? 27.328 -19.367 -15.877 1.00 35.38  ? 258 ILE B C   1 
ATOM   3844 O O   . ILE B 1 241 ? 26.114 -19.120 -15.930 1.00 39.59  ? 258 ILE B O   1 
ATOM   3845 C CB  . ILE B 1 241 ? 29.065 -17.639 -16.527 1.00 42.31  ? 258 ILE B CB  1 
ATOM   3846 C CG1 . ILE B 1 241 ? 29.821 -16.420 -15.983 1.00 37.29  ? 258 ILE B CG1 1 
ATOM   3847 C CG2 . ILE B 1 241 ? 28.083 -17.251 -17.649 1.00 31.00  ? 258 ILE B CG2 1 
ATOM   3848 C CD1 . ILE B 1 241 ? 31.022 -16.018 -16.854 1.00 40.29  ? 258 ILE B CD1 1 
ATOM   3849 N N   . ALA B 1 242 ? 27.825 -20.555 -16.240 1.00 39.81  ? 259 ALA B N   1 
ATOM   3850 C CA  . ALA B 1 242 ? 26.931 -21.625 -16.674 1.00 40.75  ? 259 ALA B CA  1 
ATOM   3851 C C   . ALA B 1 242 ? 25.897 -21.939 -15.603 1.00 45.16  ? 259 ALA B C   1 
ATOM   3852 O O   . ALA B 1 242 ? 24.728 -22.166 -15.914 1.00 40.50  ? 259 ALA B O   1 
ATOM   3853 C CB  . ALA B 1 242 ? 27.724 -22.887 -17.010 1.00 40.69  ? 259 ALA B CB  1 
ATOM   3854 N N   . ALA B 1 243 ? 26.318 -21.992 -14.336 1.00 43.58  ? 260 ALA B N   1 
ATOM   3855 C CA  . ALA B 1 243 ? 25.356 -22.214 -13.261 1.00 43.27  ? 260 ALA B CA  1 
ATOM   3856 C C   . ALA B 1 243 ? 24.416 -21.022 -13.113 1.00 43.31  ? 260 ALA B C   1 
ATOM   3857 O O   . ALA B 1 243 ? 23.205 -21.188 -12.955 1.00 39.62  ? 260 ALA B O   1 
ATOM   3858 C CB  . ALA B 1 243 ? 26.100 -22.464 -11.951 1.00 43.64  ? 260 ALA B CB  1 
ATOM   3859 N N   . LEU B 1 244 ? 24.953 -19.811 -13.218 1.00 41.05  ? 261 LEU B N   1 
ATOM   3860 C CA  . LEU B 1 244 ? 24.118 -18.621 -13.127 1.00 42.03  ? 261 LEU B CA  1 
ATOM   3861 C C   . LEU B 1 244 ? 23.032 -18.598 -14.192 1.00 48.26  ? 261 LEU B C   1 
ATOM   3862 O O   . LEU B 1 244 ? 21.936 -18.088 -13.939 1.00 45.56  ? 261 LEU B O   1 
ATOM   3863 C CB  . LEU B 1 244 ? 24.988 -17.379 -13.267 1.00 38.76  ? 261 LEU B CB  1 
ATOM   3864 C CG  . LEU B 1 244 ? 24.273 -16.041 -13.121 1.00 41.75  ? 261 LEU B CG  1 
ATOM   3865 C CD1 . LEU B 1 244 ? 23.672 -15.926 -11.730 1.00 47.33  ? 261 LEU B CD1 1 
ATOM   3866 C CD2 . LEU B 1 244 ? 25.241 -14.917 -13.391 1.00 46.61  ? 261 LEU B CD2 1 
ATOM   3867 N N   . LEU B 1 245 ? 23.320 -19.137 -15.389 1.00 53.45  ? 262 LEU B N   1 
ATOM   3868 C CA  . LEU B 1 245 ? 22.345 -19.157 -16.473 1.00 56.19  ? 262 LEU B CA  1 
ATOM   3869 C C   . LEU B 1 245 ? 21.037 -19.799 -16.046 1.00 53.44  ? 262 LEU B C   1 
ATOM   3870 O O   . LEU B 1 245 ? 19.970 -19.404 -16.516 1.00 57.70  ? 262 LEU B O   1 
ATOM   3871 C CB  . LEU B 1 245 ? 22.902 -19.941 -17.669 1.00 47.82  ? 262 LEU B CB  1 
ATOM   3872 C CG  . LEU B 1 245 ? 23.908 -19.282 -18.598 1.00 50.27  ? 262 LEU B CG  1 
ATOM   3873 C CD1 . LEU B 1 245 ? 24.414 -20.278 -19.614 1.00 49.95  ? 262 LEU B CD1 1 
ATOM   3874 C CD2 . LEU B 1 245 ? 23.239 -18.150 -19.328 1.00 54.90  ? 262 LEU B CD2 1 
ATOM   3875 N N   . ARG B 1 246 ? 21.096 -20.775 -15.145 1.00 53.65  ? 263 ARG B N   1 
ATOM   3876 C CA  . ARG B 1 246 ? 19.895 -21.491 -14.745 1.00 57.03  ? 263 ARG B CA  1 
ATOM   3877 C C   . ARG B 1 246 ? 19.007 -20.672 -13.820 1.00 58.60  ? 263 ARG B C   1 
ATOM   3878 O O   . ARG B 1 246 ? 17.857 -21.055 -13.597 1.00 68.61  ? 263 ARG B O   1 
ATOM   3879 C CB  . ARG B 1 246 ? 20.286 -22.811 -14.080 1.00 63.11  ? 263 ARG B CB  1 
ATOM   3880 C CG  . ARG B 1 246 ? 21.248 -23.584 -14.937 1.00 64.26  ? 263 ARG B CG  1 
ATOM   3881 C CD  . ARG B 1 246 ? 21.598 -24.937 -14.386 1.00 74.84  ? 263 ARG B CD  1 
ATOM   3882 N NE  . ARG B 1 246 ? 22.510 -25.606 -15.306 1.00 87.05  ? 263 ARG B NE  1 
ATOM   3883 C CZ  . ARG B 1 246 ? 22.782 -26.901 -15.297 1.00 93.02  ? 263 ARG B CZ  1 
ATOM   3884 N NH1 . ARG B 1 246 ? 22.208 -27.721 -14.430 1.00 89.06  ? 263 ARG B NH1 1 
ATOM   3885 N NH2 . ARG B 1 246 ? 23.648 -27.387 -16.184 1.00 91.49  ? 263 ARG B NH2 1 
ATOM   3886 N N   . GLU B 1 247 ? 19.518 -19.597 -13.237 1.00 61.23  ? 264 GLU B N   1 
ATOM   3887 C CA  . GLU B 1 247 ? 18.746 -18.771 -12.319 1.00 59.71  ? 264 GLU B CA  1 
ATOM   3888 C C   . GLU B 1 247 ? 18.436 -17.397 -12.877 1.00 56.23  ? 264 GLU B C   1 
ATOM   3889 O O   . GLU B 1 247 ? 17.336 -16.893 -12.668 1.00 59.11  ? 264 GLU B O   1 
ATOM   3890 C CB  . GLU B 1 247 ? 19.497 -18.618 -10.980 1.00 63.73  ? 264 GLU B CB  1 
ATOM   3891 C CG  . GLU B 1 247 ? 18.794 -17.713 -9.937  1.00 76.15  ? 264 GLU B CG  1 
ATOM   3892 C CD  . GLU B 1 247 ? 19.725 -17.182 -8.835  1.00 76.61  ? 264 GLU B CD  1 
ATOM   3893 O OE1 . GLU B 1 247 ? 20.894 -17.630 -8.755  1.00 69.56  ? 264 GLU B OE1 1 
ATOM   3894 O OE2 . GLU B 1 247 ? 19.282 -16.294 -8.061  1.00 69.78  ? 264 GLU B OE2 1 
ATOM   3895 N N   . ARG B 1 248 ? 19.351 -16.805 -13.641 1.00 49.25  ? 265 ARG B N   1 
ATOM   3896 C CA  . ARG B 1 248 ? 19.252 -15.404 -14.000 1.00 49.99  ? 265 ARG B CA  1 
ATOM   3897 C C   . ARG B 1 248 ? 19.560 -15.216 -15.481 1.00 45.63  ? 265 ARG B C   1 
ATOM   3898 O O   . ARG B 1 248 ? 20.063 -16.115 -16.161 1.00 42.96  ? 265 ARG B O   1 
ATOM   3899 C CB  . ARG B 1 248 ? 20.207 -14.547 -13.156 1.00 52.27  ? 265 ARG B CB  1 
ATOM   3900 C CG  . ARG B 1 248 ? 20.204 -14.826 -11.652 1.00 57.12  ? 265 ARG B CG  1 
ATOM   3901 C CD  . ARG B 1 248 ? 18.943 -14.324 -11.012 1.00 66.19  ? 265 ARG B CD  1 
ATOM   3902 N NE  . ARG B 1 248 ? 18.790 -12.880 -11.136 1.00 64.88  ? 265 ARG B NE  1 
ATOM   3903 C CZ  . ARG B 1 248 ? 19.459 -11.975 -10.434 1.00 66.95  ? 265 ARG B CZ  1 
ATOM   3904 N NH1 . ARG B 1 248 ? 20.362 -12.321 -9.530  1.00 69.13  ? 265 ARG B NH1 1 
ATOM   3905 N NH2 . ARG B 1 248 ? 19.200 -10.686 -10.632 1.00 69.31  ? 265 ARG B NH2 1 
ATOM   3906 N N   . ASP B 1 249 ? 19.238 -14.032 -15.979 1.00 42.21  ? 266 ASP B N   1 
ATOM   3907 C CA  . ASP B 1 249 ? 19.502 -13.704 -17.372 1.00 46.36  ? 266 ASP B CA  1 
ATOM   3908 C C   . ASP B 1 249 ? 20.967 -13.347 -17.582 1.00 42.42  ? 266 ASP B C   1 
ATOM   3909 O O   . ASP B 1 249 ? 21.542 -12.540 -16.840 1.00 39.66  ? 266 ASP B O   1 
ATOM   3910 C CB  . ASP B 1 249 ? 18.636 -12.540 -17.832 1.00 51.65  ? 266 ASP B CB  1 
ATOM   3911 C CG  . ASP B 1 249 ? 17.180 -12.883 -17.833 1.00 53.68  ? 266 ASP B CG  1 
ATOM   3912 O OD1 . ASP B 1 249 ? 16.875 -14.083 -17.931 1.00 56.74  ? 266 ASP B OD1 1 
ATOM   3913 O OD2 . ASP B 1 249 ? 16.350 -11.957 -17.770 1.00 66.57  ? 266 ASP B OD2 1 
ATOM   3914 N N   . VAL B 1 250 ? 21.562 -13.936 -18.612 1.00 39.63  ? 267 VAL B N   1 
ATOM   3915 C CA  . VAL B 1 250 ? 22.929 -13.624 -19.009 1.00 38.75  ? 267 VAL B CA  1 
ATOM   3916 C C   . VAL B 1 250 ? 22.939 -13.331 -20.502 1.00 33.77  ? 267 VAL B C   1 
ATOM   3917 O O   . VAL B 1 250 ? 22.430 -14.124 -21.297 1.00 32.61  ? 267 VAL B O   1 
ATOM   3918 C CB  . VAL B 1 250 ? 23.897 -14.769 -18.663 1.00 33.45  ? 267 VAL B CB  1 
ATOM   3919 C CG1 . VAL B 1 250 ? 25.297 -14.397 -19.085 1.00 30.53  ? 267 VAL B CG1 1 
ATOM   3920 C CG2 . VAL B 1 250 ? 23.817 -15.098 -17.161 1.00 40.23  ? 267 VAL B CG2 1 
ATOM   3921 N N   . TYR B 1 251 ? 23.524 -12.197 -20.873 1.00 33.01  ? 268 TYR B N   1 
ATOM   3922 C CA  . TYR B 1 251 ? 23.592 -11.742 -22.253 1.00 34.87  ? 268 TYR B CA  1 
ATOM   3923 C C   . TYR B 1 251 ? 25.046 -11.705 -22.692 1.00 33.01  ? 268 TYR B C   1 
ATOM   3924 O O   . TYR B 1 251 ? 25.955 -11.694 -21.869 1.00 30.69  ? 268 TYR B O   1 
ATOM   3925 C CB  . TYR B 1 251 ? 22.953 -10.353 -22.423 1.00 38.03  ? 268 TYR B CB  1 
ATOM   3926 C CG  . TYR B 1 251 ? 21.499 -10.338 -22.025 1.00 40.60  ? 268 TYR B CG  1 
ATOM   3927 C CD1 . TYR B 1 251 ? 20.499 -10.728 -22.921 1.00 41.82  ? 268 TYR B CD1 1 
ATOM   3928 C CD2 . TYR B 1 251 ? 21.128 -9.955  -20.743 1.00 41.88  ? 268 TYR B CD2 1 
ATOM   3929 C CE1 . TYR B 1 251 ? 19.161 -10.740 -22.533 1.00 41.87  ? 268 TYR B CE1 1 
ATOM   3930 C CE2 . TYR B 1 251 ? 19.801 -9.960  -20.350 1.00 47.18  ? 268 TYR B CE2 1 
ATOM   3931 C CZ  . TYR B 1 251 ? 18.823 -10.350 -21.239 1.00 45.77  ? 268 TYR B CZ  1 
ATOM   3932 O OH  . TYR B 1 251 ? 17.519 -10.340 -20.804 1.00 53.70  ? 268 TYR B OH  1 
ATOM   3933 N N   . ALA B 1 252 ? 25.246 -11.730 -24.005 1.00 39.25  ? 269 ALA B N   1 
ATOM   3934 C CA  . ALA B 1 252 ? 26.554 -11.605 -24.626 1.00 38.59  ? 269 ALA B CA  1 
ATOM   3935 C C   . ALA B 1 252 ? 26.485 -10.430 -25.586 1.00 30.51  ? 269 ALA B C   1 
ATOM   3936 O O   . ALA B 1 252 ? 25.491 -10.266 -26.277 1.00 34.47  ? 269 ALA B O   1 
ATOM   3937 C CB  . ALA B 1 252 ? 26.918 -12.889 -25.383 1.00 37.77  ? 269 ALA B CB  1 
ATOM   3938 N N   . HIS B 1 253 ? 27.513 -9.587  -25.618 1.00 31.56  ? 270 HIS B N   1 
ATOM   3939 C CA  . HIS B 1 253 ? 27.448 -8.388  -26.454 1.00 31.66  ? 270 HIS B CA  1 
ATOM   3940 C C   . HIS B 1 253 ? 28.698 -8.259  -27.304 1.00 34.86  ? 270 HIS B C   1 
ATOM   3941 O O   . HIS B 1 253 ? 29.807 -8.198  -26.762 1.00 30.02  ? 270 HIS B O   1 
ATOM   3942 C CB  . HIS B 1 253 ? 27.295 -7.128  -25.606 1.00 38.12  ? 270 HIS B CB  1 
ATOM   3943 C CG  . HIS B 1 253 ? 27.147 -5.873  -26.408 1.00 36.83  ? 270 HIS B CG  1 
ATOM   3944 N ND1 . HIS B 1 253 ? 25.971 -5.520  -27.041 1.00 31.15  ? 270 HIS B ND1 1 
ATOM   3945 C CD2 . HIS B 1 253 ? 28.030 -4.882  -26.674 1.00 39.04  ? 270 HIS B CD2 1 
ATOM   3946 C CE1 . HIS B 1 253 ? 26.137 -4.358  -27.647 1.00 38.87  ? 270 HIS B CE1 1 
ATOM   3947 N NE2 . HIS B 1 253 ? 27.379 -3.953  -27.447 1.00 38.58  ? 270 HIS B NE2 1 
ATOM   3948 N N   . ARG B 1 254 ? 28.506 -8.156  -28.621 1.00 34.69  ? 271 ARG B N   1 
ATOM   3949 C CA  . ARG B 1 254 ? 29.590 -7.941  -29.574 1.00 38.34  ? 271 ARG B CA  1 
ATOM   3950 C C   . ARG B 1 254 ? 29.987 -6.484  -29.517 1.00 39.81  ? 271 ARG B C   1 
ATOM   3951 O O   . ARG B 1 254 ? 29.398 -5.635  -30.189 1.00 41.87  ? 271 ARG B O   1 
ATOM   3952 C CB  . ARG B 1 254 ? 29.197 -8.315  -31.003 1.00 36.08  ? 271 ARG B CB  1 
ATOM   3953 C CG  . ARG B 1 254 ? 28.976 -9.781  -31.270 1.00 40.97  ? 271 ARG B CG  1 
ATOM   3954 C CD  . ARG B 1 254 ? 28.492 -10.022 -32.712 1.00 54.73  ? 271 ARG B CD  1 
ATOM   3955 N NE  . ARG B 1 254 ? 27.055 -9.807  -32.780 1.00 53.65  ? 271 ARG B NE  1 
ATOM   3956 C CZ  . ARG B 1 254 ? 26.155 -10.767 -32.620 1.00 62.48  ? 271 ARG B CZ  1 
ATOM   3957 N NH1 . ARG B 1 254 ? 26.518 -12.033 -32.449 1.00 57.21  ? 271 ARG B NH1 1 
ATOM   3958 N NH2 . ARG B 1 254 ? 24.860 -10.445 -32.584 1.00 62.74  ? 271 ARG B NH2 1 
ATOM   3959 N N   . TYR B 1 255 ? 31.001 -6.203  -28.716 1.00 37.12  ? 272 TYR B N   1 
ATOM   3960 C CA  . TYR B 1 255 ? 31.464 -4.845  -28.539 1.00 33.75  ? 272 TYR B CA  1 
ATOM   3961 C C   . TYR B 1 255 ? 32.164 -4.381  -29.803 1.00 39.85  ? 272 TYR B C   1 
ATOM   3962 O O   . TYR B 1 255 ? 32.614 -5.180  -30.633 1.00 36.07  ? 272 TYR B O   1 
ATOM   3963 C CB  . TYR B 1 255 ? 32.435 -4.725  -27.342 1.00 35.97  ? 272 TYR B CB  1 
ATOM   3964 C CG  . TYR B 1 255 ? 33.639 -5.590  -27.526 1.00 35.88  ? 272 TYR B CG  1 
ATOM   3965 C CD1 . TYR B 1 255 ? 34.741 -5.133  -28.243 1.00 38.02  ? 272 TYR B CD1 1 
ATOM   3966 C CD2 . TYR B 1 255 ? 33.659 -6.896  -27.051 1.00 41.01  ? 272 TYR B CD2 1 
ATOM   3967 C CE1 . TYR B 1 255 ? 35.827 -5.947  -28.479 1.00 38.42  ? 272 TYR B CE1 1 
ATOM   3968 C CE2 . TYR B 1 255 ? 34.753 -7.714  -27.265 1.00 41.13  ? 272 TYR B CE2 1 
ATOM   3969 C CZ  . TYR B 1 255 ? 35.831 -7.236  -27.977 1.00 42.22  ? 272 TYR B CZ  1 
ATOM   3970 O OH  . TYR B 1 255 ? 36.914 -8.055  -28.197 1.00 46.93  ? 272 TYR B OH  1 
ATOM   3971 N N   . ASP B 1 256 ? 32.214 -3.065  -29.939 1.00 37.65  ? 273 ASP B N   1 
ATOM   3972 C CA  . ASP B 1 256 ? 33.000 -2.379  -30.947 1.00 36.31  ? 273 ASP B CA  1 
ATOM   3973 C C   . ASP B 1 256 ? 34.359 -2.035  -30.344 1.00 37.23  ? 273 ASP B C   1 
ATOM   3974 O O   . ASP B 1 256 ? 34.439 -1.389  -29.292 1.00 36.81  ? 273 ASP B O   1 
ATOM   3975 C CB  . ASP B 1 256 ? 32.260 -1.122  -31.395 1.00 43.93  ? 273 ASP B CB  1 
ATOM   3976 C CG  . ASP B 1 256 ? 32.989 -0.362  -32.475 1.00 52.90  ? 273 ASP B CG  1 
ATOM   3977 O OD1 . ASP B 1 256 ? 34.208 -0.553  -32.644 1.00 55.66  ? 273 ASP B OD1 1 
ATOM   3978 O OD2 . ASP B 1 256 ? 32.330 0.444   -33.153 1.00 67.39  ? 273 ASP B OD2 1 
ATOM   3979 N N   . GLY B 1 257 ? 35.419 -2.476  -30.980 1.00 35.82  ? 274 GLY B N   1 
ATOM   3980 C CA  . GLY B 1 257 ? 36.744 -2.185  -30.467 1.00 43.71  ? 274 GLY B CA  1 
ATOM   3981 C C   . GLY B 1 257 ? 37.735 -3.226  -30.915 1.00 37.57  ? 274 GLY B C   1 
ATOM   3982 O O   . GLY B 1 257 ? 37.385 -4.344  -31.281 1.00 38.80  ? 274 GLY B O   1 
ATOM   3983 N N   . LYS B 1 258 ? 39.009 -2.862  -30.825 1.00 35.53  ? 275 LYS B N   1 
ATOM   3984 C CA  . LYS B 1 258 ? 40.093 -3.707  -31.296 1.00 39.41  ? 275 LYS B CA  1 
ATOM   3985 C C   . LYS B 1 258 ? 40.768 -4.322  -30.077 1.00 37.56  ? 275 LYS B C   1 
ATOM   3986 O O   . LYS B 1 258 ? 41.345 -3.611  -29.240 1.00 34.89  ? 275 LYS B O   1 
ATOM   3987 C CB  . LYS B 1 258 ? 41.086 -2.897  -32.132 1.00 41.58  ? 275 LYS B CB  1 
ATOM   3988 C CG  . LYS B 1 258 ? 42.254 -3.684  -32.680 1.00 45.32  ? 275 LYS B CG  1 
ATOM   3989 C CD  . LYS B 1 258 ? 41.749 -4.769  -33.615 1.00 53.28  ? 275 LYS B CD  1 
ATOM   3990 C CE  . LYS B 1 258 ? 42.856 -5.388  -34.467 1.00 67.44  ? 275 LYS B CE  1 
ATOM   3991 N NZ  . LYS B 1 258 ? 42.299 -6.138  -35.678 1.00 82.84  ? 275 LYS B NZ  1 
ATOM   3992 N N   . ARG B 1 259 ? 40.704 -5.643  -29.985 1.00 32.05  ? 276 ARG B N   1 
ATOM   3993 C CA  . ARG B 1 259 ? 41.242 -6.389  -28.860 1.00 33.93  ? 276 ARG B CA  1 
ATOM   3994 C C   . ARG B 1 259 ? 42.627 -6.916  -29.200 1.00 33.59  ? 276 ARG B C   1 
ATOM   3995 O O   . ARG B 1 259 ? 42.806 -7.586  -30.219 1.00 36.30  ? 276 ARG B O   1 
ATOM   3996 C CB  . ARG B 1 259 ? 40.314 -7.551  -28.526 1.00 36.64  ? 276 ARG B CB  1 
ATOM   3997 C CG  . ARG B 1 259 ? 40.881 -8.541  -27.485 1.00 38.60  ? 276 ARG B CG  1 
ATOM   3998 C CD  . ARG B 1 259 ? 39.984 -9.751  -27.340 1.00 43.74  ? 276 ARG B CD  1 
ATOM   3999 N NE  . ARG B 1 259 ? 40.648 -10.768 -26.545 1.00 47.82  ? 276 ARG B NE  1 
ATOM   4000 C CZ  . ARG B 1 259 ? 41.196 -11.872 -27.027 1.00 48.17  ? 276 ARG B CZ  1 
ATOM   4001 N NH1 . ARG B 1 259 ? 41.150 -12.163 -28.318 1.00 48.70  ? 276 ARG B NH1 1 
ATOM   4002 N NH2 . ARG B 1 259 ? 41.790 -12.714 -26.185 1.00 49.52  ? 276 ARG B NH2 1 
ATOM   4003 N N   . TYR B 1 260 ? 43.593 -6.649  -28.333 1.00 28.80  ? 277 TYR B N   1 
ATOM   4004 C CA  . TYR B 1 260 ? 44.916 -7.247  -28.429 1.00 27.85  ? 277 TYR B CA  1 
ATOM   4005 C C   . TYR B 1 260 ? 45.056 -8.290  -27.342 1.00 26.14  ? 277 TYR B C   1 
ATOM   4006 O O   . TYR B 1 260 ? 44.959 -7.980  -26.142 1.00 28.09  ? 277 TYR B O   1 
ATOM   4007 C CB  . TYR B 1 260 ? 46.021 -6.199  -28.315 1.00 26.00  ? 277 TYR B CB  1 
ATOM   4008 C CG  . TYR B 1 260 ? 45.936 -5.147  -29.357 1.00 30.69  ? 277 TYR B CG  1 
ATOM   4009 C CD1 . TYR B 1 260 ? 45.145 -4.028  -29.172 1.00 30.80  ? 277 TYR B CD1 1 
ATOM   4010 C CD2 . TYR B 1 260 ? 46.634 -5.269  -30.556 1.00 32.23  ? 277 TYR B CD2 1 
ATOM   4011 C CE1 . TYR B 1 260 ? 45.050 -3.061  -30.143 1.00 31.97  ? 277 TYR B CE1 1 
ATOM   4012 C CE2 . TYR B 1 260 ? 46.567 -4.291  -31.506 1.00 32.19  ? 277 TYR B CE2 1 
ATOM   4013 C CZ  . TYR B 1 260 ? 45.764 -3.200  -31.309 1.00 34.06  ? 277 TYR B CZ  1 
ATOM   4014 O OH  . TYR B 1 260 ? 45.663 -2.248  -32.273 1.00 35.77  ? 277 TYR B OH  1 
ATOM   4015 N N   . ASP B 1 261 ? 45.288 -9.521  -27.750 1.00 30.97  ? 278 ASP B N   1 
ATOM   4016 C CA  . ASP B 1 261 ? 45.451 -10.609 -26.793 1.00 34.30  ? 278 ASP B CA  1 
ATOM   4017 C C   . ASP B 1 261 ? 46.897 -10.593 -26.325 1.00 31.49  ? 278 ASP B C   1 
ATOM   4018 O O   . ASP B 1 261 ? 47.778 -11.202 -26.927 1.00 31.18  ? 278 ASP B O   1 
ATOM   4019 C CB  . ASP B 1 261 ? 45.085 -11.951 -27.428 1.00 34.49  ? 278 ASP B CB  1 
ATOM   4020 C CG  . ASP B 1 261 ? 45.076 -13.089 -26.404 1.00 39.15  ? 278 ASP B CG  1 
ATOM   4021 O OD1 . ASP B 1 261 ? 45.734 -12.933 -25.356 1.00 35.71  ? 278 ASP B OD1 1 
ATOM   4022 O OD2 . ASP B 1 261 ? 44.397 -14.117 -26.630 1.00 44.12  ? 278 ASP B OD2 1 
ATOM   4023 N N   . CYS B 1 262 ? 47.160 -9.935  -25.208 1.00 25.59  ? 279 CYS B N   1 
ATOM   4024 C CA  . CYS B 1 262 ? 48.543 -9.846  -24.742 1.00 28.45  ? 279 CYS B CA  1 
ATOM   4025 C C   . CYS B 1 262 ? 48.957 -11.048 -23.890 1.00 30.47  ? 279 CYS B C   1 
ATOM   4026 O O   . CYS B 1 262 ? 50.040 -11.042 -23.304 1.00 30.54  ? 279 CYS B O   1 
ATOM   4027 C CB  . CYS B 1 262 ? 48.763 -8.541  -23.983 1.00 24.86  ? 279 CYS B CB  1 
ATOM   4028 S SG  . CYS B 1 262 ? 48.531 -7.038  -24.976 1.00 27.86  ? 279 CYS B SG  1 
ATOM   4029 N N   . GLY B 1 263 ? 48.146 -12.093 -23.851 1.00 30.06  ? 280 GLY B N   1 
ATOM   4030 C CA  . GLY B 1 263 ? 48.549 -13.298 -23.156 1.00 36.32  ? 280 GLY B CA  1 
ATOM   4031 C C   . GLY B 1 263 ? 49.692 -14.052 -23.815 1.00 34.17  ? 280 GLY B C   1 
ATOM   4032 O O   . GLY B 1 263 ? 50.238 -14.966 -23.196 1.00 36.39  ? 280 GLY B O   1 
ATOM   4033 N N   . SER B 1 264 ? 50.055 -13.716 -25.050 1.00 32.56  ? 281 SER B N   1 
ATOM   4034 C CA  . SER B 1 264 ? 51.208 -14.322 -25.697 1.00 30.30  ? 281 SER B CA  1 
ATOM   4035 C C   . SER B 1 264 ? 52.254 -13.258 -26.025 1.00 29.52  ? 281 SER B C   1 
ATOM   4036 O O   . SER B 1 264 ? 51.947 -12.076 -26.188 1.00 32.94  ? 281 SER B O   1 
ATOM   4037 C CB  . SER B 1 264 ? 50.822 -15.072 -26.991 1.00 31.95  ? 281 SER B CB  1 
ATOM   4038 O OG  . SER B 1 264 ? 50.562 -14.168 -28.054 1.00 29.99  ? 281 SER B OG  1 
ATOM   4039 N N   . LYS B 1 265 ? 53.498 -13.712 -26.174 1.00 27.43  ? 282 LYS B N   1 
ATOM   4040 C CA  . LYS B 1 265 ? 54.572 -12.807 -26.562 1.00 31.63  ? 282 LYS B CA  1 
ATOM   4041 C C   . LYS B 1 265 ? 54.271 -12.155 -27.904 1.00 33.30  ? 282 LYS B C   1 
ATOM   4042 O O   . LYS B 1 265 ? 54.511 -10.958 -28.089 1.00 27.22  ? 282 LYS B O   1 
ATOM   4043 C CB  . LYS B 1 265 ? 55.888 -13.591 -26.631 1.00 37.64  ? 282 LYS B CB  1 
ATOM   4044 C CG  . LYS B 1 265 ? 56.411 -13.986 -25.253 1.00 45.29  ? 282 LYS B CG  1 
ATOM   4045 C CD  . LYS B 1 265 ? 57.575 -14.992 -25.287 1.00 55.94  ? 282 LYS B CD  1 
ATOM   4046 C CE  . LYS B 1 265 ? 58.686 -14.603 -26.198 1.00 45.81  ? 282 LYS B CE  1 
ATOM   4047 N NZ  . LYS B 1 265 ? 59.545 -15.792 -26.563 1.00 50.96  ? 282 LYS B NZ  1 
ATOM   4048 N N   . ALA B 1 266 ? 53.753 -12.932 -28.860 1.00 31.46  ? 283 ALA B N   1 
ATOM   4049 C CA  . ALA B 1 266 ? 53.417 -12.374 -30.164 1.00 28.48  ? 283 ALA B CA  1 
ATOM   4050 C C   . ALA B 1 266 ? 52.285 -11.359 -30.064 1.00 32.38  ? 283 ALA B C   1 
ATOM   4051 O O   . ALA B 1 266 ? 52.326 -10.303 -30.713 1.00 29.65  ? 283 ALA B O   1 
ATOM   4052 C CB  . ALA B 1 266 ? 53.055 -13.502 -31.120 1.00 29.26  ? 283 ALA B CB  1 
ATOM   4053 N N   . GLY B 1 267 ? 51.246 -11.673 -29.294 1.00 27.97  ? 284 GLY B N   1 
ATOM   4054 C CA  . GLY B 1 267 ? 50.142 -10.737 -29.167 1.00 26.51  ? 284 GLY B CA  1 
ATOM   4055 C C   . GLY B 1 267 ? 50.572 -9.460  -28.479 1.00 27.63  ? 284 GLY B C   1 
ATOM   4056 O O   . GLY B 1 267 ? 50.190 -8.361  -28.883 1.00 28.09  ? 284 GLY B O   1 
ATOM   4057 N N   . MET B 1 268 ? 51.397 -9.585  -27.439 1.00 25.69  ? 285 MET B N   1 
ATOM   4058 C CA  . MET B 1 268 ? 51.892 -8.403  -26.749 1.00 31.11  ? 285 MET B CA  1 
ATOM   4059 C C   . MET B 1 268 ? 52.782 -7.569  -27.665 1.00 25.42  ? 285 MET B C   1 
ATOM   4060 O O   . MET B 1 268 ? 52.735 -6.328  -27.632 1.00 25.20  ? 285 MET B O   1 
ATOM   4061 C CB  . MET B 1 268 ? 52.649 -8.824  -25.488 1.00 27.41  ? 285 MET B CB  1 
ATOM   4062 C CG  . MET B 1 268 ? 53.355 -7.675  -24.795 1.00 33.97  ? 285 MET B CG  1 
ATOM   4063 S SD  . MET B 1 268 ? 52.532 -7.214  -23.275 1.00 45.92  ? 285 MET B SD  1 
ATOM   4064 C CE  . MET B 1 268 ? 53.085 -8.574  -22.345 1.00 39.53  ? 285 MET B CE  1 
ATOM   4065 N N   . PHE B 1 269 ? 53.627 -8.231  -28.457 1.00 27.71  ? 286 PHE B N   1 
ATOM   4066 C CA  . PHE B 1 269 ? 54.461 -7.533  -29.442 1.00 27.75  ? 286 PHE B CA  1 
ATOM   4067 C C   . PHE B 1 269 ? 53.622 -6.755  -30.454 1.00 27.19  ? 286 PHE B C   1 
ATOM   4068 O O   . PHE B 1 269 ? 53.917 -5.587  -30.756 1.00 26.86  ? 286 PHE B O   1 
ATOM   4069 C CB  . PHE B 1 269 ? 55.370 -8.553  -30.138 1.00 31.44  ? 286 PHE B CB  1 
ATOM   4070 C CG  . PHE B 1 269 ? 56.294 -7.954  -31.168 1.00 30.67  ? 286 PHE B CG  1 
ATOM   4071 C CD1 . PHE B 1 269 ? 57.498 -7.403  -30.789 1.00 34.16  ? 286 PHE B CD1 1 
ATOM   4072 C CD2 . PHE B 1 269 ? 55.946 -7.940  -32.502 1.00 29.59  ? 286 PHE B CD2 1 
ATOM   4073 C CE1 . PHE B 1 269 ? 58.367 -6.858  -31.731 1.00 36.53  ? 286 PHE B CE1 1 
ATOM   4074 C CE2 . PHE B 1 269 ? 56.811 -7.377  -33.467 1.00 32.21  ? 286 PHE B CE2 1 
ATOM   4075 C CZ  . PHE B 1 269 ? 58.016 -6.832  -33.068 1.00 29.11  ? 286 PHE B CZ  1 
ATOM   4076 N N   . GLN B 1 270 ? 52.550 -7.354  -30.971 1.00 26.93  ? 287 GLN B N   1 
ATOM   4077 C CA  . GLN B 1 270 ? 51.739 -6.611  -31.933 1.00 32.98  ? 287 GLN B CA  1 
ATOM   4078 C C   . GLN B 1 270 ? 50.992 -5.450  -31.294 1.00 26.73  ? 287 GLN B C   1 
ATOM   4079 O O   . GLN B 1 270 ? 50.748 -4.426  -31.957 1.00 25.84  ? 287 GLN B O   1 
ATOM   4080 C CB  . GLN B 1 270 ? 50.753 -7.535  -32.633 1.00 34.76  ? 287 GLN B CB  1 
ATOM   4081 C CG  . GLN B 1 270 ? 51.401 -8.488  -33.620 1.00 43.82  ? 287 GLN B CG  1 
ATOM   4082 C CD  . GLN B 1 270 ? 52.348 -7.832  -34.674 1.00 48.62  ? 287 GLN B CD  1 
ATOM   4083 O OE1 . GLN B 1 270 ? 52.181 -6.651  -35.114 1.00 37.87  ? 287 GLN B OE1 1 
ATOM   4084 N NE2 . GLN B 1 270 ? 53.350 -8.627  -35.095 1.00 32.20  ? 287 GLN B NE2 1 
ATOM   4085 N N   . ALA B 1 271 ? 50.601 -5.585  -30.023 1.00 28.12  ? 288 ALA B N   1 
ATOM   4086 C CA  . ALA B 1 271 ? 50.054 -4.442  -29.298 1.00 29.97  ? 288 ALA B CA  1 
ATOM   4087 C C   . ALA B 1 271 ? 51.088 -3.317  -29.167 1.00 27.07  ? 288 ALA B C   1 
ATOM   4088 O O   . ALA B 1 271 ? 50.775 -2.136  -29.359 1.00 25.28  ? 288 ALA B O   1 
ATOM   4089 C CB  . ALA B 1 271 ? 49.569 -4.907  -27.915 1.00 31.52  ? 288 ALA B CB  1 
ATOM   4090 N N   . THR B 1 272 ? 52.330 -3.659  -28.852 1.00 24.56  ? 289 THR B N   1 
ATOM   4091 C CA  . THR B 1 272 ? 53.357 -2.626  -28.780 1.00 24.48  ? 289 THR B CA  1 
ATOM   4092 C C   . THR B 1 272 ? 53.530 -1.937  -30.133 1.00 26.52  ? 289 THR B C   1 
ATOM   4093 O O   . THR B 1 272 ? 53.619 -0.707  -30.207 1.00 26.03  ? 289 THR B O   1 
ATOM   4094 C CB  . THR B 1 272 ? 54.672 -3.246  -28.301 1.00 24.79  ? 289 THR B CB  1 
ATOM   4095 O OG1 . THR B 1 272 ? 54.484 -3.799  -27.005 1.00 33.99  ? 289 THR B OG1 1 
ATOM   4096 C CG2 . THR B 1 272 ? 55.810 -2.211  -28.297 1.00 29.69  ? 289 THR B CG2 1 
ATOM   4097 N N   . VAL B 1 273 ? 53.562 -2.712  -31.219 1.00 26.16  ? 290 VAL B N   1 
ATOM   4098 C CA  . VAL B 1 273 ? 53.716 -2.112  -32.540 1.00 26.03  ? 290 VAL B CA  1 
ATOM   4099 C C   . VAL B 1 273 ? 52.525 -1.210  -32.844 1.00 25.60  ? 290 VAL B C   1 
ATOM   4100 O O   . VAL B 1 273 ? 52.678 -0.045  -33.208 1.00 28.13  ? 290 VAL B O   1 
ATOM   4101 C CB  . VAL B 1 273 ? 53.894 -3.215  -33.603 1.00 28.27  ? 290 VAL B CB  1 
ATOM   4102 C CG1 . VAL B 1 273 ? 53.760 -2.656  -35.010 1.00 28.08  ? 290 VAL B CG1 1 
ATOM   4103 C CG2 . VAL B 1 273 ? 55.230 -3.899  -33.447 1.00 27.38  ? 290 VAL B CG2 1 
ATOM   4104 N N   . ALA B 1 274 ? 51.320 -1.737  -32.684 1.00 28.08  ? 291 ALA B N   1 
ATOM   4105 C CA  . ALA B 1 274 ? 50.127 -1.023  -33.133 1.00 27.65  ? 291 ALA B CA  1 
ATOM   4106 C C   . ALA B 1 274 ? 49.860 0.218   -32.295 1.00 27.03  ? 291 ALA B C   1 
ATOM   4107 O O   . ALA B 1 274 ? 49.540 1.284   -32.823 1.00 25.21  ? 291 ALA B O   1 
ATOM   4108 C CB  . ALA B 1 274 ? 48.919 -1.963  -33.079 1.00 30.62  ? 291 ALA B CB  1 
ATOM   4109 N N   . LEU B 1 275 ? 49.896 0.079   -30.984 1.00 25.02  ? 292 LEU B N   1 
ATOM   4110 C CA  . LEU B 1 275 ? 49.661 1.230   -30.118 1.00 23.08  ? 292 LEU B CA  1 
ATOM   4111 C C   . LEU B 1 275 ? 50.857 2.160   -30.054 1.00 24.56  ? 292 LEU B C   1 
ATOM   4112 O O   . LEU B 1 275 ? 50.684 3.379   -29.949 1.00 26.45  ? 292 LEU B O   1 
ATOM   4113 C CB  . LEU B 1 275 ? 49.262 0.767   -28.724 1.00 25.77  ? 292 LEU B CB  1 
ATOM   4114 C CG  . LEU B 1 275 ? 47.852 0.206   -28.633 1.00 28.88  ? 292 LEU B CG  1 
ATOM   4115 C CD1 . LEU B 1 275 ? 47.634 -0.956  -29.457 1.00 43.52  ? 292 LEU B CD1 1 
ATOM   4116 C CD2 . LEU B 1 275 ? 47.657 -0.181  -27.150 1.00 39.02  ? 292 LEU B CD2 1 
ATOM   4117 N N   . GLY B 1 276 ? 52.070 1.637   -30.168 1.00 25.40  ? 293 GLY B N   1 
ATOM   4118 C CA  . GLY B 1 276 ? 53.203 2.532   -30.327 1.00 28.86  ? 293 GLY B CA  1 
ATOM   4119 C C   . GLY B 1 276 ? 53.044 3.411   -31.556 1.00 31.41  ? 293 GLY B C   1 
ATOM   4120 O O   . GLY B 1 276 ? 53.326 4.608   -31.518 1.00 26.32  ? 293 GLY B O   1 
ATOM   4121 N N   . ARG B 1 277 ? 52.543 2.838   -32.650 1.00 27.31  ? 294 ARG B N   1 
ATOM   4122 C CA  . ARG B 1 277 ? 52.290 3.646   -33.838 1.00 32.28  ? 294 ARG B CA  1 
ATOM   4123 C C   . ARG B 1 277 ? 51.196 4.666   -33.565 1.00 29.18  ? 294 ARG B C   1 
ATOM   4124 O O   . ARG B 1 277 ? 51.371 5.864   -33.801 1.00 28.18  ? 294 ARG B O   1 
ATOM   4125 C CB  . ARG B 1 277 ? 51.889 2.751   -35.021 1.00 27.16  ? 294 ARG B CB  1 
ATOM   4126 C CG  . ARG B 1 277 ? 51.573 3.536   -36.343 1.00 28.55  ? 294 ARG B CG  1 
ATOM   4127 C CD  . ARG B 1 277 ? 52.836 3.960   -37.004 1.00 28.30  ? 294 ARG B CD  1 
ATOM   4128 N NE  . ARG B 1 277 ? 52.570 4.478   -38.341 1.00 32.32  ? 294 ARG B NE  1 
ATOM   4129 C CZ  . ARG B 1 277 ? 52.548 3.744   -39.450 1.00 32.38  ? 294 ARG B CZ  1 
ATOM   4130 N NH1 . ARG B 1 277 ? 52.745 2.422   -39.428 1.00 29.81  ? 294 ARG B NH1 1 
ATOM   4131 N NH2 . ARG B 1 277 ? 52.246 4.329   -40.592 1.00 31.28  ? 294 ARG B NH2 1 
ATOM   4132 N N   . LYS B 1 278 ? 50.070 4.212   -33.030 1.00 33.33  ? 295 LYS B N   1 
ATOM   4133 C CA  . LYS B 1 278 ? 48.893 5.065   -32.986 1.00 34.59  ? 295 LYS B CA  1 
ATOM   4134 C C   . LYS B 1 278 ? 49.049 6.193   -31.981 1.00 30.96  ? 295 LYS B C   1 
ATOM   4135 O O   . LYS B 1 278 ? 48.712 7.338   -32.289 1.00 30.11  ? 295 LYS B O   1 
ATOM   4136 C CB  . LYS B 1 278 ? 47.657 4.219   -32.668 1.00 33.05  ? 295 LYS B CB  1 
ATOM   4137 C CG  . LYS B 1 278 ? 46.393 5.031   -32.443 1.00 37.92  ? 295 LYS B CG  1 
ATOM   4138 C CD  . LYS B 1 278 ? 45.174 4.101   -32.345 1.00 36.69  ? 295 LYS B CD  1 
ATOM   4139 C CE  . LYS B 1 278 ? 43.896 4.887   -32.131 1.00 39.40  ? 295 LYS B CE  1 
ATOM   4140 N NZ  . LYS B 1 278 ? 42.719 3.986   -32.077 1.00 38.84  ? 295 LYS B NZ  1 
ATOM   4141 N N   . TYR B 1 279 ? 49.560 5.905   -30.770 1.00 29.05  ? 296 TYR B N   1 
ATOM   4142 C CA  . TYR B 1 279 ? 49.581 6.894   -29.710 1.00 27.46  ? 296 TYR B CA  1 
ATOM   4143 C C   . TYR B 1 279 ? 50.950 7.513   -29.481 1.00 31.99  ? 296 TYR B C   1 
ATOM   4144 O O   . TYR B 1 279 ? 51.050 8.496   -28.748 1.00 31.29  ? 296 TYR B O   1 
ATOM   4145 C CB  . TYR B 1 279 ? 49.081 6.278   -28.377 1.00 27.98  ? 296 TYR B CB  1 
ATOM   4146 C CG  . TYR B 1 279 ? 47.633 5.891   -28.458 1.00 31.17  ? 296 TYR B CG  1 
ATOM   4147 C CD1 . TYR B 1 279 ? 46.657 6.864   -28.582 1.00 38.38  ? 296 TYR B CD1 1 
ATOM   4148 C CD2 . TYR B 1 279 ? 47.239 4.561   -28.444 1.00 33.03  ? 296 TYR B CD2 1 
ATOM   4149 C CE1 . TYR B 1 279 ? 45.334 6.527   -28.679 1.00 35.90  ? 296 TYR B CE1 1 
ATOM   4150 C CE2 . TYR B 1 279 ? 45.912 4.212   -28.559 1.00 33.01  ? 296 TYR B CE2 1 
ATOM   4151 C CZ  . TYR B 1 279 ? 44.966 5.205   -28.668 1.00 33.98  ? 296 TYR B CZ  1 
ATOM   4152 O OH  . TYR B 1 279 ? 43.632 4.892   -28.775 1.00 33.87  ? 296 TYR B OH  1 
ATOM   4153 N N   . HIS B 1 280 ? 51.984 7.015   -30.133 1.00 29.97  ? 297 HIS B N   1 
ATOM   4154 C CA  . HIS B 1 280 ? 53.335 7.483   -29.897 1.00 32.35  ? 297 HIS B CA  1 
ATOM   4155 C C   . HIS B 1 280 ? 54.123 7.763   -31.181 1.00 33.86  ? 297 HIS B C   1 
ATOM   4156 O O   . HIS B 1 280 ? 55.272 8.225   -31.099 1.00 29.49  ? 297 HIS B O   1 
ATOM   4157 C CB  . HIS B 1 280 ? 54.084 6.443   -29.059 1.00 29.76  ? 297 HIS B CB  1 
ATOM   4158 C CG  . HIS B 1 280 ? 53.398 6.095   -27.776 1.00 31.44  ? 297 HIS B CG  1 
ATOM   4159 N ND1 . HIS B 1 280 ? 53.625 6.792   -26.611 1.00 32.24  ? 297 HIS B ND1 1 
ATOM   4160 C CD2 . HIS B 1 280 ? 52.491 5.136   -27.471 1.00 32.09  ? 297 HIS B CD2 1 
ATOM   4161 C CE1 . HIS B 1 280 ? 52.896 6.275   -25.638 1.00 29.90  ? 297 HIS B CE1 1 
ATOM   4162 N NE2 . HIS B 1 280 ? 52.194 5.272   -26.131 1.00 30.87  ? 297 HIS B NE2 1 
ATOM   4163 N N   . GLY B 1 281 ? 53.551 7.501   -32.353 1.00 31.47  ? 298 GLY B N   1 
ATOM   4164 C CA  . GLY B 1 281 ? 54.263 7.771   -33.580 1.00 34.06  ? 298 GLY B CA  1 
ATOM   4165 C C   . GLY B 1 281 ? 55.479 6.909   -33.823 1.00 30.17  ? 298 GLY B C   1 
ATOM   4166 O O   . GLY B 1 281 ? 56.307 7.262   -34.662 1.00 32.44  ? 298 GLY B O   1 
ATOM   4167 N N   . LEU B 1 282 ? 55.556 5.739   -33.181 1.00 28.80  ? 299 LEU B N   1 
ATOM   4168 C CA  . LEU B 1 282 ? 56.690 4.839   -33.303 1.00 30.07  ? 299 LEU B CA  1 
ATOM   4169 C C   . LEU B 1 282 ? 56.481 3.902   -34.478 1.00 31.46  ? 299 LEU B C   1 
ATOM   4170 O O   . LEU B 1 282 ? 55.410 3.297   -34.628 1.00 29.05  ? 299 LEU B O   1 
ATOM   4171 C CB  . LEU B 1 282 ? 56.873 4.030   -32.024 1.00 30.42  ? 299 LEU B CB  1 
ATOM   4172 C CG  . LEU B 1 282 ? 57.048 4.877   -30.767 1.00 31.77  ? 299 LEU B CG  1 
ATOM   4173 C CD1 . LEU B 1 282 ? 56.951 4.019   -29.494 1.00 33.53  ? 299 LEU B CD1 1 
ATOM   4174 C CD2 . LEU B 1 282 ? 58.399 5.614   -30.868 1.00 30.68  ? 299 LEU B CD2 1 
ATOM   4175 N N   . ILE B 1 283 ? 57.525 3.759   -35.281 1.00 28.70  ? 300 ILE B N   1 
ATOM   4176 C CA  . ILE B 1 283 ? 57.458 3.034   -36.536 1.00 28.61  ? 300 ILE B CA  1 
ATOM   4177 C C   . ILE B 1 283 ? 58.632 2.067   -36.603 1.00 29.82  ? 300 ILE B C   1 
ATOM   4178 O O   . ILE B 1 283 ? 59.785 2.494   -36.441 1.00 29.78  ? 300 ILE B O   1 
ATOM   4179 C CB  . ILE B 1 283 ? 57.490 4.006   -37.727 1.00 32.73  ? 300 ILE B CB  1 
ATOM   4180 C CG1 . ILE B 1 283 ? 56.326 4.994   -37.669 1.00 30.65  ? 300 ILE B CG1 1 
ATOM   4181 C CG2 . ILE B 1 283 ? 57.457 3.217   -39.068 1.00 33.51  ? 300 ILE B CG2 1 
ATOM   4182 C CD1 . ILE B 1 283 ? 56.380 6.034   -38.755 1.00 36.85  ? 300 ILE B CD1 1 
ATOM   4183 N N   . PRO B 1 284 ? 58.408 0.793   -36.900 1.00 28.56  ? 301 PRO B N   1 
ATOM   4184 C CA  . PRO B 1 284 ? 59.538 -0.129  -37.024 1.00 33.36  ? 301 PRO B CA  1 
ATOM   4185 C C   . PRO B 1 284 ? 60.506 0.296   -38.109 1.00 39.89  ? 301 PRO B C   1 
ATOM   4186 O O   . PRO B 1 284 ? 60.116 0.805   -39.169 1.00 39.78  ? 301 PRO B O   1 
ATOM   4187 C CB  . PRO B 1 284 ? 58.872 -1.464  -37.365 1.00 32.71  ? 301 PRO B CB  1 
ATOM   4188 C CG  . PRO B 1 284 ? 57.491 -1.345  -36.809 1.00 35.04  ? 301 PRO B CG  1 
ATOM   4189 C CD  . PRO B 1 284 ? 57.114 0.092   -37.009 1.00 35.83  ? 301 PRO B CD  1 
ATOM   4190 N N   . GLU B 1 285 ? 61.788 0.148   -37.814 1.00 41.10  ? 302 GLU B N   1 
ATOM   4191 C CA  . GLU B 1 285 ? 62.788 0.237   -38.861 1.00 52.02  ? 302 GLU B CA  1 
ATOM   4192 C C   . GLU B 1 285 ? 62.852 -1.124  -39.545 1.00 60.02  ? 302 GLU B C   1 
ATOM   4193 O O   . GLU B 1 285 ? 62.815 -2.202  -38.880 1.00 52.35  ? 302 GLU B O   1 
ATOM   4194 C CB  . GLU B 1 285 ? 64.142 0.646   -38.320 1.00 51.67  ? 302 GLU B CB  1 
ATOM   4195 C CG  . GLU B 1 285 ? 64.150 2.047   -37.767 1.00 56.37  ? 302 GLU B CG  1 
ATOM   4196 C CD  . GLU B 1 285 ? 65.468 2.376   -37.082 1.00 67.45  ? 302 GLU B CD  1 
ATOM   4197 O OE1 . GLU B 1 285 ? 66.467 1.661   -37.359 1.00 69.63  ? 302 GLU B OE1 1 
ATOM   4198 O OE2 . GLU B 1 285 ? 65.490 3.315   -36.245 1.00 58.64  ? 302 GLU B OE2 1 
ATOM   4199 O OXT . GLU B 1 285 ? 62.944 -1.147  -40.767 1.00 56.24  ? 302 GLU B OXT 1 
HETATM 4200 N N   . GLY C 2 .   ? 38.710 11.669  19.469  1.00 69.19  ? 401 GLY A N   1 
HETATM 4201 C CA  . GLY C 2 .   ? 38.956 10.948  18.186  1.00 64.15  ? 401 GLY A CA  1 
HETATM 4202 C C   . GLY C 2 .   ? 38.055 11.445  17.069  1.00 61.88  ? 401 GLY A C   1 
HETATM 4203 O O   . GLY C 2 .   ? 38.525 11.869  16.011  1.00 63.03  ? 401 GLY A O   1 
HETATM 4204 O OXT . GLY C 2 .   ? 36.825 11.443  17.192  1.00 59.93  ? 401 GLY A OXT 1 
HETATM 4205 N N   . GLY D 2 .   ? 49.565 9.377   20.460  1.00 59.25  ? 402 GLY A N   1 
HETATM 4206 C CA  . GLY D 2 .   ? 49.687 9.482   19.012  1.00 58.77  ? 402 GLY A CA  1 
HETATM 4207 C C   . GLY D 2 .   ? 51.083 9.769   18.459  1.00 58.67  ? 402 GLY A C   1 
HETATM 4208 O O   . GLY D 2 .   ? 52.123 9.405   19.039  1.00 58.73  ? 402 GLY A O   1 
HETATM 4209 O OXT . GLY D 2 .   ? 51.214 10.373  17.379  1.00 58.54  ? 402 GLY A OXT 1 
HETATM 4210 C C1  . GOL E 3 .   ? 32.386 -16.884 15.626  1.00 62.84  ? 403 GOL A C1  1 
HETATM 4211 O O1  . GOL E 3 .   ? 31.257 -16.559 16.411  1.00 63.80  ? 403 GOL A O1  1 
HETATM 4212 C C2  . GOL E 3 .   ? 33.486 -17.382 16.557  1.00 60.85  ? 403 GOL A C2  1 
HETATM 4213 O O2  . GOL E 3 .   ? 33.274 -16.754 17.801  1.00 56.47  ? 403 GOL A O2  1 
HETATM 4214 C C3  . GOL E 3 .   ? 34.893 -17.116 16.015  1.00 61.41  ? 403 GOL A C3  1 
HETATM 4215 O O3  . GOL E 3 .   ? 35.368 -18.306 15.407  1.00 62.54  ? 403 GOL A O3  1 
HETATM 4216 C C1  . GOL F 3 .   ? 19.996 3.052   35.269  1.00 57.16  ? 404 GOL A C1  1 
HETATM 4217 O O1  . GOL F 3 .   ? 20.805 2.553   36.338  1.00 48.03  ? 404 GOL A O1  1 
HETATM 4218 C C2  . GOL F 3 .   ? 18.511 2.745   35.430  1.00 57.15  ? 404 GOL A C2  1 
HETATM 4219 O O2  . GOL F 3 .   ? 18.369 1.355   35.653  1.00 64.79  ? 404 GOL A O2  1 
HETATM 4220 C C3  . GOL F 3 .   ? 17.706 3.164   34.199  1.00 51.37  ? 404 GOL A C3  1 
HETATM 4221 O O3  . GOL F 3 .   ? 16.973 4.351   34.464  1.00 51.25  ? 404 GOL A O3  1 
HETATM 4222 N N   . GLY G 2 .   ? 38.519 -19.466 -19.384 1.00 72.36  ? 401 GLY B N   1 
HETATM 4223 C CA  . GLY G 2 .   ? 38.480 -18.400 -18.400 1.00 67.82  ? 401 GLY B CA  1 
HETATM 4224 C C   . GLY G 2 .   ? 37.675 -18.807 -17.179 1.00 67.64  ? 401 GLY B C   1 
HETATM 4225 O O   . GLY G 2 .   ? 36.449 -18.701 -17.169 1.00 65.31  ? 401 GLY B O   1 
HETATM 4226 O OXT . GLY G 2 .   ? 38.224 -19.249 -16.167 1.00 70.95  ? 401 GLY B OXT 1 
HETATM 4227 N N   . GLY H 2 .   ? 49.374 -16.288 -20.361 1.00 77.70  ? 402 GLY B N   1 
HETATM 4228 C CA  . GLY H 2 .   ? 49.605 -16.761 -19.005 1.00 77.45  ? 402 GLY B CA  1 
HETATM 4229 C C   . GLY H 2 .   ? 51.052 -17.082 -18.675 1.00 67.78  ? 402 GLY B C   1 
HETATM 4230 O O   . GLY H 2 .   ? 51.338 -17.608 -17.582 1.00 64.59  ? 402 GLY B O   1 
HETATM 4231 O OXT . GLY H 2 .   ? 51.976 -16.839 -19.475 1.00 64.41  ? 402 GLY B OXT 1 
HETATM 4232 C C1  . GOL I 3 .   ? 34.877 11.466  -15.312 1.00 66.38  ? 403 GOL B C1  1 
HETATM 4233 O O1  . GOL I 3 .   ? 34.979 11.851  -13.947 1.00 57.52  ? 403 GOL B O1  1 
HETATM 4234 C C2  . GOL I 3 .   ? 34.347 10.044  -15.429 1.00 59.79  ? 403 GOL B C2  1 
HETATM 4235 O O2  . GOL I 3 .   ? 35.427 9.159   -15.196 1.00 65.85  ? 403 GOL B O2  1 
HETATM 4236 C C3  . GOL I 3 .   ? 33.734 9.714   -16.788 1.00 56.61  ? 403 GOL B C3  1 
HETATM 4237 O O3  . GOL I 3 .   ? 32.408 9.283   -16.540 1.00 61.98  ? 403 GOL B O3  1 
HETATM 4238 O O   . HOH J 4 .   ? 65.821 8.259   8.709   1.00 36.70  ? 501 HOH A O   1 
HETATM 4239 O O   . HOH J 4 .   ? 42.809 9.718   7.828   1.00 38.32  ? 502 HOH A O   1 
HETATM 4240 O O   . HOH J 4 .   ? 45.259 -15.060 16.452  1.00 42.35  ? 503 HOH A O   1 
HETATM 4241 O O   . HOH J 4 .   ? 17.197 2.452   19.211  1.00 44.36  ? 504 HOH A O   1 
HETATM 4242 O O   . HOH J 4 .   ? 20.750 15.382  21.688  1.00 43.11  ? 505 HOH A O   1 
HETATM 4243 O O   . HOH J 4 .   ? 39.941 17.969  8.096   1.00 66.32  ? 506 HOH A O   1 
HETATM 4244 O O   . HOH J 4 .   ? 48.810 3.291   2.653   1.00 38.14  ? 507 HOH A O   1 
HETATM 4245 O O   . HOH J 4 .   ? 45.384 -11.426 3.263   1.00 41.30  ? 508 HOH A O   1 
HETATM 4246 O O   . HOH J 4 .   ? 54.117 4.050   33.034  1.00 36.11  ? 509 HOH A O   1 
HETATM 4247 O O   . HOH J 4 .   ? 27.026 10.698  30.280  1.00 29.26  ? 510 HOH A O   1 
HETATM 4248 O O   . HOH J 4 .   ? 50.031 -16.253 8.941   1.00 44.63  ? 511 HOH A O   1 
HETATM 4249 O O   . HOH J 4 .   ? 58.382 -1.287  6.385   1.00 44.63  ? 512 HOH A O   1 
HETATM 4250 O O   . HOH J 4 .   ? 55.819 7.332   12.062  1.00 42.88  ? 513 HOH A O   1 
HETATM 4251 O O   . HOH J 4 .   ? 43.316 -10.188 1.635   1.00 37.91  ? 514 HOH A O   1 
HETATM 4252 O O   . HOH J 4 .   ? 28.764 -5.516  29.012  1.00 30.66  ? 515 HOH A O   1 
HETATM 4253 O O   . HOH J 4 .   ? 36.522 -8.638  31.876  1.00 31.00  ? 516 HOH A O   1 
HETATM 4254 O O   . HOH J 4 .   ? 44.617 -6.888  32.696  1.00 34.92  ? 517 HOH A O   1 
HETATM 4255 O O   . HOH J 4 .   ? 35.477 9.152   18.726  1.00 40.12  ? 518 HOH A O   1 
HETATM 4256 O O   . HOH J 4 .   ? 35.736 -15.189 5.336   1.00 37.29  ? 519 HOH A O   1 
HETATM 4257 O O   . HOH J 4 .   ? 56.724 -2.502  21.614  1.00 32.88  ? 520 HOH A O   1 
HETATM 4258 O O   . HOH J 4 .   ? 46.333 6.698   20.118  1.00 40.53  ? 521 HOH A O   1 
HETATM 4259 O O   . HOH J 4 .   ? 23.008 5.116   14.847  1.00 32.40  ? 522 HOH A O   1 
HETATM 4260 O O   . HOH J 4 .   ? 53.567 -12.155 5.060   1.00 34.56  ? 523 HOH A O   1 
HETATM 4261 O O   . HOH J 4 .   ? 21.650 -8.688  21.280  1.00 37.08  ? 524 HOH A O   1 
HETATM 4262 O O   . HOH J 4 .   ? 40.043 -14.390 18.165  1.00 33.65  ? 525 HOH A O   1 
HETATM 4263 O O   . HOH J 4 .   ? 48.480 6.510   27.451  1.00 35.77  ? 526 HOH A O   1 
HETATM 4264 O O   . HOH J 4 .   ? 46.411 -3.784  35.140  1.00 29.96  ? 527 HOH A O   1 
HETATM 4265 O O   . HOH J 4 .   ? 37.784 -12.100 25.753  1.00 36.32  ? 528 HOH A O   1 
HETATM 4266 O O   . HOH J 4 .   ? 34.333 -9.231  30.084  1.00 39.47  ? 529 HOH A O   1 
HETATM 4267 O O   . HOH J 4 .   ? 28.465 8.801   34.425  1.00 33.22  ? 530 HOH A O   1 
HETATM 4268 O O   . HOH J 4 .   ? 41.472 -7.068  23.041  1.00 28.04  ? 531 HOH A O   1 
HETATM 4269 O O   . HOH J 4 .   ? 21.008 5.096   37.085  1.00 41.72  ? 532 HOH A O   1 
HETATM 4270 O O   . HOH J 4 .   ? 55.010 -8.997  12.437  1.00 29.52  ? 533 HOH A O   1 
HETATM 4271 O O   . HOH J 4 .   ? 28.919 -5.760  8.953   1.00 28.31  ? 534 HOH A O   1 
HETATM 4272 O O   . HOH J 4 .   ? 34.598 -6.080  3.635   1.00 34.88  ? 535 HOH A O   1 
HETATM 4273 O O   . HOH J 4 .   ? 38.419 -9.702  1.643   1.00 34.61  ? 536 HOH A O   1 
HETATM 4274 O O   . HOH J 4 .   ? 56.198 -5.121  25.128  1.00 32.32  ? 537 HOH A O   1 
HETATM 4275 O O   . HOH J 4 .   ? 44.969 11.208  11.065  1.00 45.59  ? 538 HOH A O   1 
HETATM 4276 O O   . HOH J 4 .   ? 43.212 -0.176  14.866  1.00 19.89  ? 539 HOH A O   1 
HETATM 4277 O O   . HOH J 4 .   ? 24.536 3.006   32.680  1.00 27.23  ? 540 HOH A O   1 
HETATM 4278 O O   . HOH J 4 .   ? 64.908 -3.875  42.749  1.00 40.01  ? 541 HOH A O   1 
HETATM 4279 O O   . HOH J 4 .   ? 51.550 -17.298 7.195   1.00 37.71  ? 542 HOH A O   1 
HETATM 4280 O O   . HOH J 4 .   ? 32.378 -4.428  35.040  1.00 44.19  ? 543 HOH A O   1 
HETATM 4281 O O   . HOH J 4 .   ? 40.966 8.105   1.783   1.00 39.77  ? 544 HOH A O   1 
HETATM 4282 O O   . HOH J 4 .   ? 41.009 11.859  14.901  1.00 43.88  ? 545 HOH A O   1 
HETATM 4283 O O   . HOH J 4 .   ? 35.849 9.857   37.474  1.00 32.06  ? 546 HOH A O   1 
HETATM 4284 O O   . HOH J 4 .   ? 24.715 9.063   33.105  1.00 36.93  ? 547 HOH A O   1 
HETATM 4285 O O   . HOH J 4 .   ? 33.227 8.598   37.701  1.00 38.89  ? 548 HOH A O   1 
HETATM 4286 O O   . HOH J 4 .   ? 23.668 0.680   8.795   1.00 38.70  ? 549 HOH A O   1 
HETATM 4287 O O   . HOH J 4 .   ? 48.046 5.262   16.933  1.00 27.63  ? 550 HOH A O   1 
HETATM 4288 O O   . HOH J 4 .   ? 21.804 -2.768  27.370  1.00 44.77  ? 551 HOH A O   1 
HETATM 4289 O O   . HOH J 4 .   ? 36.883 -7.607  4.386   1.00 30.40  ? 552 HOH A O   1 
HETATM 4290 O O   . HOH J 4 .   ? 60.952 1.348   12.223  1.00 28.69  ? 553 HOH A O   1 
HETATM 4291 O O   . HOH J 4 .   ? 55.240 -7.193  35.210  1.00 27.70  ? 554 HOH A O   1 
HETATM 4292 O O   . HOH J 4 .   ? 32.735 -1.781  33.631  1.00 38.98  ? 555 HOH A O   1 
HETATM 4293 O O   . HOH J 4 .   ? 43.416 3.277   15.199  1.00 31.63  ? 556 HOH A O   1 
HETATM 4294 O O   . HOH J 4 .   ? 41.971 -16.461 5.939   1.00 45.62  ? 557 HOH A O   1 
HETATM 4295 O O   . HOH J 4 .   ? 44.839 -3.650  20.716  1.00 25.10  ? 558 HOH A O   1 
HETATM 4296 O O   . HOH J 4 .   ? 40.461 -7.924  32.476  1.00 37.64  ? 559 HOH A O   1 
HETATM 4297 O O   . HOH J 4 .   ? 40.444 -10.791 31.468  1.00 38.87  ? 560 HOH A O   1 
HETATM 4298 O O   . HOH J 4 .   ? 40.345 6.142   22.179  1.00 39.92  ? 561 HOH A O   1 
HETATM 4299 O O   . HOH J 4 .   ? 49.889 7.120   16.236  1.00 42.42  ? 562 HOH A O   1 
HETATM 4300 O O   . HOH J 4 .   ? 33.478 18.721  20.495  1.00 40.93  ? 563 HOH A O   1 
HETATM 4301 O O   . HOH J 4 .   ? 38.354 4.614   -0.027  1.00 31.98  ? 564 HOH A O   1 
HETATM 4302 O O   . HOH J 4 .   ? 42.406 -9.649  22.257  1.00 27.45  ? 565 HOH A O   1 
HETATM 4303 O O   . HOH J 4 .   ? 64.746 -3.083  37.286  1.00 32.10  ? 566 HOH A O   1 
HETATM 4304 O O   . HOH J 4 .   ? 26.248 -6.753  25.873  1.00 33.89  ? 567 HOH A O   1 
HETATM 4305 O O   . HOH J 4 .   ? 20.896 8.871   20.841  1.00 28.30  ? 568 HOH A O   1 
HETATM 4306 O O   . HOH J 4 .   ? 34.017 3.316   34.369  1.00 33.36  ? 569 HOH A O   1 
HETATM 4307 O O   . HOH J 4 .   ? 48.196 1.654   30.298  1.00 32.18  ? 570 HOH A O   1 
HETATM 4308 O O   . HOH J 4 .   ? 34.730 -14.595 13.551  1.00 32.01  ? 571 HOH A O   1 
HETATM 4309 O O   . HOH J 4 .   ? 27.778 15.050  35.115  1.00 37.13  ? 572 HOH A O   1 
HETATM 4310 O O   . HOH J 4 .   ? 25.770 7.278   5.069   1.00 42.73  ? 573 HOH A O   1 
HETATM 4311 O O   . HOH J 4 .   ? 42.728 -4.840  22.368  1.00 26.84  ? 574 HOH A O   1 
HETATM 4312 O O   . HOH J 4 .   ? 35.140 7.227   1.126   1.00 37.24  ? 575 HOH A O   1 
HETATM 4313 O O   . HOH J 4 .   ? 26.076 -9.138  14.708  1.00 40.05  ? 576 HOH A O   1 
HETATM 4314 O O   . HOH J 4 .   ? 30.562 10.961  34.523  1.00 43.08  ? 577 HOH A O   1 
HETATM 4315 O O   . HOH J 4 .   ? 35.328 -4.296  34.032  1.00 46.96  ? 578 HOH A O   1 
HETATM 4316 O O   . HOH J 4 .   ? 52.809 -15.795 21.020  1.00 39.89  ? 579 HOH A O   1 
HETATM 4317 O O   . HOH J 4 .   ? 32.833 6.821   -0.128  1.00 42.14  ? 580 HOH A O   1 
HETATM 4318 O O   . HOH J 4 .   ? 38.134 -7.243  24.605  1.00 27.57  ? 581 HOH A O   1 
HETATM 4319 O O   . HOH J 4 .   ? 33.612 0.492   31.106  1.00 33.55  ? 582 HOH A O   1 
HETATM 4320 O O   . HOH J 4 .   ? 50.007 1.738   7.507   1.00 31.05  ? 583 HOH A O   1 
HETATM 4321 O O   . HOH J 4 .   ? 37.619 12.803  39.077  1.00 41.87  ? 584 HOH A O   1 
HETATM 4322 O O   . HOH J 4 .   ? 32.353 12.412  37.618  1.00 51.82  ? 585 HOH A O   1 
HETATM 4323 O O   . HOH J 4 .   ? 32.873 21.377  27.894  1.00 39.82  ? 586 HOH A O   1 
HETATM 4324 O O   . HOH J 4 .   ? 21.202 -3.042  34.367  1.00 37.30  ? 587 HOH A O   1 
HETATM 4325 O O   . HOH J 4 .   ? 31.443 2.954   33.513  1.00 33.94  ? 588 HOH A O   1 
HETATM 4326 O O   . HOH J 4 .   ? 46.580 -17.361 7.950   1.00 50.45  ? 589 HOH A O   1 
HETATM 4327 O O   . HOH J 4 .   ? 25.397 -14.064 19.871  1.00 50.16  ? 590 HOH A O   1 
HETATM 4328 O O   . HOH J 4 .   ? 45.086 3.031   17.431  1.00 28.72  ? 591 HOH A O   1 
HETATM 4329 O O   . HOH J 4 .   ? 26.908 16.806  20.612  1.00 31.69  ? 592 HOH A O   1 
HETATM 4330 O O   . HOH J 4 .   ? 26.831 6.484   2.507   1.00 46.87  ? 593 HOH A O   1 
HETATM 4331 O O   . HOH J 4 .   ? 54.146 -6.577  37.523  1.00 27.81  ? 594 HOH A O   1 
HETATM 4332 O O   . HOH J 4 .   ? 18.577 5.766   36.459  1.00 48.23  ? 595 HOH A O   1 
HETATM 4333 O O   . HOH J 4 .   ? 46.210 3.182   30.371  1.00 30.34  ? 596 HOH A O   1 
HETATM 4334 O O   . HOH J 4 .   ? 21.847 0.686   38.360  1.00 36.54  ? 597 HOH A O   1 
HETATM 4335 O O   . HOH J 4 .   ? 44.407 7.641   10.470  1.00 41.99  ? 598 HOH A O   1 
HETATM 4336 O O   . HOH J 4 .   ? 45.164 5.259   11.589  1.00 31.43  ? 599 HOH A O   1 
HETATM 4337 O O   . HOH J 4 .   ? 54.656 4.550   10.422  1.00 41.18  ? 600 HOH A O   1 
HETATM 4338 O O   . HOH J 4 .   ? 48.969 -7.732  35.975  1.00 40.53  ? 601 HOH A O   1 
HETATM 4339 O O   . HOH J 4 .   ? 56.739 2.147   26.327  1.00 36.53  ? 602 HOH A O   1 
HETATM 4340 O O   . HOH J 4 .   ? 54.462 8.903   28.236  1.00 29.85  ? 603 HOH A O   1 
HETATM 4341 O O   . HOH J 4 .   ? 45.762 5.448   14.215  1.00 32.50  ? 604 HOH A O   1 
HETATM 4342 O O   . HOH J 4 .   ? 48.106 -1.652  35.056  1.00 37.77  ? 605 HOH A O   1 
HETATM 4343 O O   . HOH J 4 .   ? 52.430 6.153   10.377  1.00 44.83  ? 606 HOH A O   1 
HETATM 4344 O O   . HOH J 4 .   ? 44.708 -9.882  26.423  1.00 43.88  ? 607 HOH A O   1 
HETATM 4345 O O   . HOH J 4 .   ? 43.086 -8.984  24.873  1.00 44.84  ? 608 HOH A O   1 
HETATM 4346 O O   . HOH J 4 .   ? 49.957 8.584   30.252  1.00 49.94  ? 609 HOH A O   1 
HETATM 4347 O O   . HOH J 4 .   ? 41.994 -12.476 3.189   1.00 40.44  ? 610 HOH A O   1 
HETATM 4348 O O   . HOH J 4 .   ? 61.438 -1.591  39.011  1.00 42.22  ? 611 HOH A O   1 
HETATM 4349 O O   . HOH J 4 .   ? 40.825 5.799   -0.468  1.00 41.26  ? 612 HOH A O   1 
HETATM 4350 O O   . HOH J 4 .   ? 40.994 -9.720  25.982  1.00 32.76  ? 613 HOH A O   1 
HETATM 4351 O O   . HOH J 4 .   ? 46.212 -12.307 23.896  1.00 46.31  ? 614 HOH A O   1 
HETATM 4352 O O   . HOH J 4 .   ? 38.260 6.867   21.168  1.00 40.78  ? 615 HOH A O   1 
HETATM 4353 O O   . HOH J 4 .   ? 28.239 18.874  23.347  1.00 37.53  ? 616 HOH A O   1 
HETATM 4354 O O   . HOH J 4 .   ? 50.745 6.564   19.836  1.00 39.05  ? 617 HOH A O   1 
HETATM 4355 O O   . HOH J 4 .   ? 41.704 -13.857 31.030  1.00 53.72  ? 618 HOH A O   1 
HETATM 4356 O O   . HOH J 4 .   ? 40.931 -19.304 4.007   1.00 55.15  ? 619 HOH A O   1 
HETATM 4357 O O   . HOH J 4 .   ? 18.728 4.065   15.408  1.00 50.62  ? 620 HOH A O   1 
HETATM 4358 O O   . HOH J 4 .   ? 22.447 2.798   8.481   1.00 39.18  ? 621 HOH A O   1 
HETATM 4359 O O   . HOH J 4 .   ? 56.824 -0.954  26.294  1.00 38.09  ? 622 HOH A O   1 
HETATM 4360 O O   . HOH J 4 .   ? 54.546 9.728   25.205  1.00 28.54  ? 623 HOH A O   1 
HETATM 4361 O O   . HOH J 4 .   ? 19.298 14.449  28.635  1.00 40.67  ? 624 HOH A O   1 
HETATM 4362 O O   . HOH J 4 .   ? 51.331 -6.338  40.287  1.00 47.27  ? 625 HOH A O   1 
HETATM 4363 O O   . HOH J 4 .   ? 43.837 18.691  35.191  1.00 53.36  ? 626 HOH A O   1 
HETATM 4364 O O   . HOH J 4 .   ? 28.658 4.560   1.723   1.00 43.80  ? 627 HOH A O   1 
HETATM 4365 O O   . HOH J 4 .   ? 18.881 11.585  22.180  1.00 44.82  ? 628 HOH A O   1 
HETATM 4366 O O   . HOH J 4 .   ? 37.848 -16.311 17.793  1.00 35.80  ? 629 HOH A O   1 
HETATM 4367 O O   . HOH J 4 .   ? 20.135 3.918   39.497  1.00 39.80  ? 630 HOH A O   1 
HETATM 4368 O O   . HOH J 4 .   ? 40.195 -11.154 22.429  1.00 37.58  ? 631 HOH A O   1 
HETATM 4369 O O   . HOH J 4 .   ? 38.956 -9.783  24.610  1.00 40.57  ? 632 HOH A O   1 
HETATM 4370 O O   . HOH J 4 .   ? 42.715 7.517   12.531  1.00 33.53  ? 633 HOH A O   1 
HETATM 4371 O O   . HOH J 4 .   ? 50.445 -8.525  41.585  1.00 46.04  ? 634 HOH A O   1 
HETATM 4372 O O   . HOH J 4 .   ? 19.945 -1.212  37.596  1.00 43.72  ? 635 HOH A O   1 
HETATM 4373 O O   . HOH J 4 .   ? 21.334 -4.373  25.787  1.00 45.93  ? 636 HOH A O   1 
HETATM 4374 O O   . HOH J 4 .   ? 48.669 -10.085 37.026  1.00 42.86  ? 637 HOH A O   1 
HETATM 4375 O O   . HOH J 4 .   ? 68.230 -5.059  34.907  1.00 35.83  ? 638 HOH A O   1 
HETATM 4376 O O   . HOH J 4 .   ? 44.276 5.468   18.436  1.00 35.15  ? 639 HOH A O   1 
HETATM 4377 O O   . HOH J 4 .   ? 39.608 -18.029 15.242  1.00 48.08  ? 640 HOH A O   1 
HETATM 4378 O O   . HOH J 4 .   ? 67.174 -3.492  38.577  1.00 36.49  ? 641 HOH A O   1 
HETATM 4379 O O   . HOH J 4 .   ? 51.482 -6.026  37.192  1.00 37.29  ? 642 HOH A O   1 
HETATM 4380 O O   . HOH J 4 .   ? 49.420 -9.806  39.788  1.00 48.15  ? 643 HOH A O   1 
HETATM 4381 O O   . HOH J 4 .   ? 37.854 -14.105 24.240  1.00 50.02  ? 644 HOH A O   1 
HETATM 4382 O O   . HOH J 4 .   ? 46.756 8.121   14.683  1.00 43.67  ? 645 HOH A O   1 
HETATM 4383 O O   . HOH J 4 .   ? 43.265 5.868   14.827  1.00 32.70  ? 646 HOH A O   1 
HETATM 4384 O O   . HOH J 4 .   ? 68.756 -7.401  33.188  1.00 36.47  ? 647 HOH A O   1 
HETATM 4385 O O   . HOH J 4 .   ? 27.041 9.239   37.016  1.00 40.91  ? 648 HOH A O   1 
HETATM 4386 O O   . HOH J 4 .   ? 42.735 7.391   16.723  1.00 41.46  ? 649 HOH A O   1 
HETATM 4387 O O   . HOH K 4 .   ? 50.540 -5.011  -34.924 1.00 32.42  ? 501 HOH B O   1 
HETATM 4388 O O   . HOH K 4 .   ? 47.932 -14.137 -2.506  1.00 38.65  ? 502 HOH B O   1 
HETATM 4389 O O   . HOH K 4 .   ? 28.763 -1.869  -8.603  1.00 28.91  ? 503 HOH B O   1 
HETATM 4390 O O   . HOH K 4 .   ? 55.609 -14.667 -12.395 1.00 41.45  ? 504 HOH B O   1 
HETATM 4391 O O   . HOH K 4 .   ? 49.968 3.799   -24.860 1.00 43.12  ? 505 HOH B O   1 
HETATM 4392 O O   . HOH K 4 .   ? 32.757 -14.777 0.385   1.00 45.81  ? 506 HOH B O   1 
HETATM 4393 O O   . HOH K 4 .   ? 28.368 -1.765  -28.360 1.00 42.59  ? 507 HOH B O   1 
HETATM 4394 O O   . HOH K 4 .   ? 39.793 -28.609 -26.240 1.00 56.94  ? 508 HOH B O   1 
HETATM 4395 O O   . HOH K 4 .   ? 51.502 9.788   -6.949  1.00 33.87  ? 509 HOH B O   1 
HETATM 4396 O O   . HOH K 4 .   ? 56.582 -4.822  -21.691 1.00 35.47  ? 510 HOH B O   1 
HETATM 4397 O O   . HOH K 4 .   ? 64.444 -3.338  -37.235 1.00 44.31  ? 511 HOH B O   1 
HETATM 4398 O O   . HOH K 4 .   ? 35.249 -16.695 -18.655 1.00 35.78  ? 512 HOH B O   1 
HETATM 4399 O O   . HOH K 4 .   ? 44.492 4.902   -14.410 1.00 39.19  ? 513 HOH B O   1 
HETATM 4400 O O   . HOH K 4 .   ? 44.997 7.546   -16.015 1.00 44.24  ? 514 HOH B O   1 
HETATM 4401 O O   . HOH K 4 .   ? 22.809 -12.533 -14.378 1.00 32.90  ? 515 HOH B O   1 
HETATM 4402 O O   . HOH K 4 .   ? 44.493 -3.932  -20.558 1.00 25.88  ? 516 HOH B O   1 
HETATM 4403 O O   . HOH K 4 .   ? 44.247 -0.011  -32.234 1.00 35.47  ? 517 HOH B O   1 
HETATM 4404 O O   . HOH K 4 .   ? 34.625 7.019   -13.025 1.00 30.67  ? 518 HOH B O   1 
HETATM 4405 O O   . HOH K 4 .   ? 45.288 4.052   -3.121  1.00 35.27  ? 519 HOH B O   1 
HETATM 4406 O O   . HOH K 4 .   ? 41.331 -24.158 -31.801 1.00 47.63  ? 520 HOH B O   1 
HETATM 4407 O O   . HOH K 4 .   ? 35.926 -33.590 -28.737 1.00 32.86  ? 521 HOH B O   1 
HETATM 4408 O O   . HOH K 4 .   ? 65.445 -1.524  -41.605 1.00 41.64  ? 522 HOH B O   1 
HETATM 4409 O O   . HOH K 4 .   ? 21.079 -4.733  -26.084 1.00 43.64  ? 523 HOH B O   1 
HETATM 4410 O O   . HOH K 4 .   ? 63.163 1.346   -41.697 1.00 50.31  ? 524 HOH B O   1 
HETATM 4411 O O   . HOH K 4 .   ? 21.325 1.394   -20.483 1.00 42.84  ? 525 HOH B O   1 
HETATM 4412 O O   . HOH K 4 .   ? 47.671 -12.731 -17.000 1.00 33.09  ? 526 HOH B O   1 
HETATM 4413 O O   . HOH K 4 .   ? 47.839 11.712  -6.224  1.00 43.83  ? 527 HOH B O   1 
HETATM 4414 O O   . HOH K 4 .   ? 34.644 -1.513  -3.373  1.00 33.79  ? 528 HOH B O   1 
HETATM 4415 O O   . HOH K 4 .   ? 53.475 4.430   -4.690  1.00 32.50  ? 529 HOH B O   1 
HETATM 4416 O O   . HOH K 4 .   ? 55.004 -7.413  -3.593  1.00 43.93  ? 530 HOH B O   1 
HETATM 4417 O O   . HOH K 4 .   ? 54.735 0.707   -34.960 1.00 28.09  ? 531 HOH B O   1 
HETATM 4418 O O   . HOH K 4 .   ? 43.281 2.886   -1.405  1.00 40.35  ? 532 HOH B O   1 
HETATM 4419 O O   . HOH K 4 .   ? 39.377 -6.850  -32.009 1.00 45.59  ? 533 HOH B O   1 
HETATM 4420 O O   . HOH K 4 .   ? 49.757 -9.400  -7.640  1.00 29.60  ? 534 HOH B O   1 
HETATM 4421 O O   . HOH K 4 .   ? 42.592 -17.417 -8.042  1.00 38.96  ? 535 HOH B O   1 
HETATM 4422 O O   . HOH K 4 .   ? 39.789 7.047   -17.926 1.00 33.16  ? 536 HOH B O   1 
HETATM 4423 O O   . HOH K 4 .   ? 49.654 -14.679 -16.380 1.00 37.82  ? 537 HOH B O   1 
HETATM 4424 O O   . HOH K 4 .   ? 33.018 -7.866  -30.737 1.00 36.03  ? 538 HOH B O   1 
HETATM 4425 O O   . HOH K 4 .   ? 50.461 -13.800 -20.080 1.00 38.98  ? 539 HOH B O   1 
HETATM 4426 O O   . HOH K 4 .   ? 37.458 -17.055 -23.530 1.00 40.41  ? 540 HOH B O   1 
HETATM 4427 O O   . HOH K 4 .   ? 53.563 -10.685 -33.306 1.00 39.98  ? 541 HOH B O   1 
HETATM 4428 O O   . HOH K 4 .   ? 45.822 -3.364  -34.772 1.00 38.60  ? 542 HOH B O   1 
HETATM 4429 O O   . HOH K 4 .   ? 41.132 -0.402  -22.588 1.00 35.95  ? 543 HOH B O   1 
HETATM 4430 O O   . HOH K 4 .   ? 22.807 -14.584 -4.292  1.00 56.88  ? 544 HOH B O   1 
HETATM 4431 O O   . HOH K 4 .   ? 42.121 2.354   -21.850 1.00 33.87  ? 545 HOH B O   1 
HETATM 4432 O O   . HOH K 4 .   ? 43.727 4.146   -22.042 1.00 35.00  ? 546 HOH B O   1 
HETATM 4433 O O   . HOH K 4 .   ? 56.258 -9.380  -26.652 1.00 37.50  ? 547 HOH B O   1 
HETATM 4434 O O   . HOH K 4 .   ? 26.069 -0.741  -25.452 1.00 46.82  ? 548 HOH B O   1 
HETATM 4435 O O   . HOH K 4 .   ? 26.012 1.774   -14.065 1.00 36.86  ? 549 HOH B O   1 
HETATM 4436 O O   . HOH K 4 .   ? 45.514 -12.930 -14.277 1.00 36.77  ? 550 HOH B O   1 
HETATM 4437 O O   . HOH K 4 .   ? 55.894 9.181   -36.610 1.00 35.77  ? 551 HOH B O   1 
HETATM 4438 O O   . HOH K 4 .   ? 38.419 -12.296 0.257   1.00 33.55  ? 552 HOH B O   1 
HETATM 4439 O O   . HOH K 4 .   ? 40.939 -16.038 -1.773  1.00 39.62  ? 553 HOH B O   1 
HETATM 4440 O O   . HOH K 4 .   ? 37.561 -0.301  -24.320 1.00 29.32  ? 554 HOH B O   1 
HETATM 4441 O O   . HOH K 4 .   ? 23.713 -7.987  -8.188  1.00 40.23  ? 555 HOH B O   1 
HETATM 4442 O O   . HOH K 4 .   ? 34.946 -14.613 -0.850  1.00 41.69  ? 556 HOH B O   1 
HETATM 4443 O O   . HOH K 4 .   ? 33.012 -26.454 -20.941 1.00 39.20  ? 557 HOH B O   1 
HETATM 4444 O O   . HOH K 4 .   ? 43.116 -10.540 -15.167 1.00 31.14  ? 558 HOH B O   1 
HETATM 4445 O O   . HOH K 4 .   ? 36.967 -0.114  -4.267  1.00 33.32  ? 559 HOH B O   1 
HETATM 4446 O O   . HOH K 4 .   ? 56.079 -2.197  -24.981 1.00 30.51  ? 560 HOH B O   1 
HETATM 4447 O O   . HOH K 4 .   ? 33.957 1.769   -29.664 1.00 40.58  ? 561 HOH B O   1 
HETATM 4448 O O   . HOH K 4 .   ? 23.258 -16.592 -32.576 1.00 48.89  ? 562 HOH B O   1 
HETATM 4449 O O   . HOH K 4 .   ? 53.713 -15.742 -28.807 1.00 32.38  ? 563 HOH B O   1 
HETATM 4450 O O   . HOH K 4 .   ? 43.996 -14.898 -10.348 1.00 39.75  ? 564 HOH B O   1 
HETATM 4451 O O   . HOH K 4 .   ? 56.334 8.799   -1.992  1.00 53.52  ? 565 HOH B O   1 
HETATM 4452 O O   . HOH K 4 .   ? 43.154 -7.336  -14.747 1.00 24.30  ? 566 HOH B O   1 
HETATM 4453 O O   . HOH K 4 .   ? 26.393 -24.030 -20.435 1.00 35.25  ? 567 HOH B O   1 
HETATM 4454 O O   . HOH K 4 .   ? 44.865 -10.546 -17.282 1.00 31.70  ? 568 HOH B O   1 
HETATM 4455 O O   . HOH K 4 .   ? 35.527 7.250   -4.809  1.00 38.30  ? 569 HOH B O   1 
HETATM 4456 O O   . HOH K 4 .   ? 35.514 -19.379 -39.089 1.00 45.50  ? 570 HOH B O   1 
HETATM 4457 O O   . HOH K 4 .   ? 60.907 -4.284  -38.580 1.00 40.59  ? 571 HOH B O   1 
HETATM 4458 O O   . HOH K 4 .   ? 58.033 0.270   -41.035 1.00 30.22  ? 572 HOH B O   1 
HETATM 4459 O O   . HOH K 4 .   ? 40.586 10.188  -15.123 1.00 48.34  ? 573 HOH B O   1 
HETATM 4460 O O   . HOH K 4 .   ? 48.077 1.588   -35.258 1.00 32.56  ? 574 HOH B O   1 
HETATM 4461 O O   . HOH K 4 .   ? 56.599 9.309   -28.810 1.00 45.20  ? 575 HOH B O   1 
HETATM 4462 O O   . HOH K 4 .   ? 31.728 -28.474 -28.144 1.00 35.60  ? 576 HOH B O   1 
HETATM 4463 O O   . HOH K 4 .   ? 29.004 -17.226 -34.124 1.00 36.77  ? 577 HOH B O   1 
HETATM 4464 O O   . HOH K 4 .   ? 45.978 -10.296 -30.421 1.00 34.14  ? 578 HOH B O   1 
HETATM 4465 O O   . HOH K 4 .   ? 61.215 3.891   -38.497 1.00 37.41  ? 579 HOH B O   1 
HETATM 4466 O O   . HOH K 4 .   ? 45.734 14.840  -13.057 1.00 49.29  ? 580 HOH B O   1 
HETATM 4467 O O   . HOH K 4 .   ? 49.157 8.157   -16.295 1.00 37.67  ? 581 HOH B O   1 
HETATM 4468 O O   . HOH K 4 .   ? 34.227 -29.967 -28.297 1.00 34.87  ? 582 HOH B O   1 
HETATM 4469 O O   . HOH K 4 .   ? 39.828 -31.487 -33.335 1.00 54.77  ? 583 HOH B O   1 
HETATM 4470 O O   . HOH K 4 .   ? 42.512 -2.564  -21.998 1.00 34.16  ? 584 HOH B O   1 
HETATM 4471 O O   . HOH K 4 .   ? 36.171 1.343   -31.648 1.00 43.03  ? 585 HOH B O   1 
HETATM 4472 O O   . HOH K 4 .   ? 45.072 -12.751 -11.559 1.00 28.79  ? 586 HOH B O   1 
HETATM 4473 O O   . HOH K 4 .   ? 40.869 -19.377 -14.935 1.00 37.50  ? 587 HOH B O   1 
HETATM 4474 O O   . HOH K 4 .   ? 29.803 5.516   -7.148  1.00 51.64  ? 588 HOH B O   1 
HETATM 4475 O O   . HOH K 4 .   ? 20.291 -16.102 -20.129 1.00 33.82  ? 589 HOH B O   1 
HETATM 4476 O O   . HOH K 4 .   ? 27.154 -13.806 -1.828  1.00 43.49  ? 590 HOH B O   1 
HETATM 4477 O O   . HOH K 4 .   ? 59.827 5.444   -34.565 1.00 31.27  ? 591 HOH B O   1 
HETATM 4478 O O   . HOH K 4 .   ? 31.994 -34.538 -34.103 1.00 36.76  ? 592 HOH B O   1 
HETATM 4479 O O   . HOH K 4 .   ? 22.376 -10.608 -8.042  1.00 41.64  ? 593 HOH B O   1 
HETATM 4480 O O   . HOH K 4 .   ? 30.285 -7.436  1.414   1.00 45.33  ? 594 HOH B O   1 
HETATM 4481 O O   . HOH K 4 .   ? 45.037 -18.468 -11.101 1.00 45.39  ? 595 HOH B O   1 
HETATM 4482 O O   . HOH K 4 .   ? 53.489 0.422   -37.369 1.00 30.64  ? 596 HOH B O   1 
HETATM 4483 O O   . HOH K 4 .   ? 22.209 -1.786  -8.641  1.00 48.75  ? 597 HOH B O   1 
HETATM 4484 O O   . HOH K 4 .   ? 54.394 -12.059 -10.437 1.00 39.18  ? 598 HOH B O   1 
HETATM 4485 O O   . HOH K 4 .   ? 23.000 -3.660  -29.022 1.00 43.81  ? 599 HOH B O   1 
HETATM 4486 O O   . HOH K 4 .   ? 40.526 2.200   -25.524 1.00 40.92  ? 600 HOH B O   1 
HETATM 4487 O O   . HOH K 4 .   ? 39.796 1.062   -32.371 1.00 47.37  ? 601 HOH B O   1 
HETATM 4488 O O   . HOH K 4 .   ? 48.400 -16.909 -13.829 1.00 39.44  ? 602 HOH B O   1 
HETATM 4489 O O   . HOH K 4 .   ? 42.052 4.834   -2.918  1.00 40.29  ? 603 HOH B O   1 
HETATM 4490 O O   . HOH K 4 .   ? 42.201 9.082   -5.524  1.00 48.01  ? 604 HOH B O   1 
HETATM 4491 O O   . HOH K 4 .   ? 63.505 -0.215  -43.636 1.00 47.00  ? 605 HOH B O   1 
HETATM 4492 O O   . HOH K 4 .   ? 48.406 -16.510 -5.164  1.00 43.71  ? 606 HOH B O   1 
HETATM 4493 O O   . HOH K 4 .   ? 40.748 -13.385 0.606   1.00 42.26  ? 607 HOH B O   1 
HETATM 4494 O O   . HOH K 4 .   ? 27.473 -26.140 -23.294 1.00 35.15  ? 608 HOH B O   1 
HETATM 4495 O O   . HOH K 4 .   ? 38.051 -14.307 -21.230 1.00 40.12  ? 609 HOH B O   1 
HETATM 4496 O O   . HOH K 4 .   ? 56.220 -6.466  -26.640 1.00 39.56  ? 610 HOH B O   1 
HETATM 4497 O O   . HOH K 4 .   ? 27.951 2.700   -25.013 1.00 46.78  ? 611 HOH B O   1 
HETATM 4498 O O   . HOH K 4 .   ? 41.462 7.544   -3.248  1.00 49.41  ? 612 HOH B O   1 
HETATM 4499 O O   . HOH K 4 .   ? 22.017 -6.457  -9.982  1.00 51.97  ? 613 HOH B O   1 
HETATM 4500 O O   . HOH K 4 .   ? 54.189 -16.895 -25.819 1.00 28.71  ? 614 HOH B O   1 
HETATM 4501 O O   . HOH K 4 .   ? 39.639 3.869   -21.900 1.00 37.93  ? 615 HOH B O   1 
HETATM 4502 O O   . HOH K 4 .   ? 41.531 7.858   -15.981 1.00 48.08  ? 616 HOH B O   1 
HETATM 4503 O O   . HOH K 4 .   ? 61.592 10.843  -7.261  1.00 64.95  ? 617 HOH B O   1 
HETATM 4504 O O   . HOH K 4 .   ? 37.807 8.812   -17.741 1.00 43.39  ? 618 HOH B O   1 
HETATM 4505 O O   . HOH K 4 .   ? 42.572 -15.046 -12.496 1.00 31.83  ? 619 HOH B O   1 
HETATM 4506 O O   . HOH K 4 .   ? 57.924 -3.843  0.000   0.50 45.21  ? 620 HOH B O   1 
HETATM 4507 O O   . HOH K 4 .   ? 40.433 -16.325 -19.474 1.00 52.95  ? 621 HOH B O   1 
HETATM 4508 O O   . HOH K 4 .   ? 51.023 -0.673  -36.620 1.00 27.84  ? 622 HOH B O   1 
HETATM 4509 O O   . HOH K 4 .   ? 43.967 -13.045 -18.419 1.00 33.39  ? 623 HOH B O   1 
HETATM 4510 O O   . HOH K 4 .   ? 61.126 6.069   -37.268 1.00 38.57  ? 624 HOH B O   1 
HETATM 4511 O O   . HOH K 4 .   ? 45.597 0.908   -34.587 1.00 33.83  ? 625 HOH B O   1 
HETATM 4512 O O   . HOH K 4 .   ? 30.842 -36.817 -32.845 1.00 35.38  ? 626 HOH B O   1 
HETATM 4513 O O   . HOH K 4 .   ? 43.017 -13.233 -14.650 1.00 34.26  ? 627 HOH B O   1 
HETATM 4514 O O   . HOH K 4 .   ? 45.183 4.165   -24.685 1.00 46.54  ? 628 HOH B O   1 
HETATM 4515 O O   . HOH K 4 .   ? 46.410 -15.739 -14.570 1.00 44.48  ? 629 HOH B O   1 
HETATM 4516 O O   . HOH K 4 .   ? 29.292 -28.212 -26.375 1.00 42.05  ? 630 HOH B O   1 
HETATM 4517 O O   . HOH K 4 .   ? 42.375 -14.896 -16.778 1.00 41.50  ? 631 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . HIS A 8   ? 0.9210 1.0095 0.9173 -0.0196 0.0601  -0.0622 25  HIS A N   
2    C CA  . HIS A 8   ? 0.8169 0.8952 0.8102 -0.0193 0.0578  -0.0566 25  HIS A CA  
3    C C   . HIS A 8   ? 0.7342 0.8074 0.7343 -0.0231 0.0566  -0.0549 25  HIS A C   
4    O O   . HIS A 8   ? 0.7131 0.7836 0.7160 -0.0287 0.0577  -0.0533 25  HIS A O   
5    C CB  . HIS A 8   ? 0.8086 0.8794 0.7940 -0.0217 0.0577  -0.0515 25  HIS A CB  
6    C CG  . HIS A 8   ? 0.8724 0.9431 0.8508 -0.0171 0.0576  -0.0511 25  HIS A CG  
7    N ND1 . HIS A 8   ? 0.7301 0.7926 0.7031 -0.0170 0.0563  -0.0466 25  HIS A ND1 
8    C CD2 . HIS A 8   ? 0.9918 1.0698 0.9682 -0.0125 0.0591  -0.0546 25  HIS A CD2 
9    C CE1 . HIS A 8   ? 0.7693 0.8336 0.7382 -0.0126 0.0570  -0.0476 25  HIS A CE1 
10   N NE2 . HIS A 8   ? 0.9261 0.9995 0.8966 -0.0098 0.0587  -0.0521 25  HIS A NE2 
11   N N   . VAL A 9   ? 0.6130 0.6847 0.6160 -0.0201 0.0546  -0.0546 26  VAL A N   
12   C CA  . VAL A 9   ? 0.5465 0.6110 0.5543 -0.0232 0.0529  -0.0517 26  VAL A CA  
13   C C   . VAL A 9   ? 0.5581 0.6161 0.5611 -0.0198 0.0504  -0.0475 26  VAL A C   
14   O O   . VAL A 9   ? 0.4729 0.5352 0.4752 -0.0142 0.0498  -0.0494 26  VAL A O   
15   C CB  . VAL A 9   ? 0.5776 0.6483 0.5965 -0.0235 0.0530  -0.0569 26  VAL A CB  
16   C CG1 . VAL A 9   ? 0.7249 0.8050 0.7450 -0.0168 0.0522  -0.0617 26  VAL A CG1 
17   C CG2 . VAL A 9   ? 0.6171 0.6797 0.6410 -0.0264 0.0512  -0.0536 26  VAL A CG2 
18   N N   . VAL A 10  ? 0.4208 0.4688 0.4206 -0.0230 0.0492  -0.0419 27  VAL A N   
19   C CA  . VAL A 10  ? 0.4281 0.4694 0.4234 -0.0204 0.0469  -0.0380 27  VAL A CA  
20   C C   . VAL A 10  ? 0.4207 0.4568 0.4214 -0.0222 0.0449  -0.0359 27  VAL A C   
21   O O   . VAL A 10  ? 0.4229 0.4534 0.4247 -0.0269 0.0448  -0.0326 27  VAL A O   
22   C CB  . VAL A 10  ? 0.4186 0.4538 0.4056 -0.0221 0.0470  -0.0338 27  VAL A CB  
23   C CG1 . VAL A 10  ? 0.3572 0.3868 0.3407 -0.0189 0.0450  -0.0310 27  VAL A CG1 
24   C CG2 . VAL A 10  ? 0.4608 0.5016 0.4436 -0.0213 0.0492  -0.0362 27  VAL A CG2 
25   N N   . ARG A 11  ? 0.3781 0.4166 0.3824 -0.0182 0.0434  -0.0378 28  ARG A N   
26   C CA  . ARG A 11  ? 0.3936 0.4277 0.4034 -0.0194 0.0413  -0.0364 28  ARG A CA  
27   C C   . ARG A 11  ? 0.3421 0.3721 0.3491 -0.0155 0.0390  -0.0338 28  ARG A C   
28   O O   . ARG A 11  ? 0.3434 0.3692 0.3541 -0.0163 0.0369  -0.0322 28  ARG A O   
29   C CB  . ARG A 11  ? 0.3908 0.4332 0.4106 -0.0190 0.0417  -0.0422 28  ARG A CB  
30   C CG  . ARG A 11  ? 0.4994 0.5512 0.5207 -0.0127 0.0414  -0.0466 28  ARG A CG  
31   C CD  . ARG A 11  ? 0.6598 0.7216 0.6911 -0.0130 0.0422  -0.0535 28  ARG A CD  
32   N NE  . ARG A 11  ? 0.7278 0.7980 0.7639 -0.0077 0.0408  -0.0575 28  ARG A NE  
33   C CZ  . ARG A 11  ? 0.7328 0.8135 0.7671 -0.0015 0.0414  -0.0607 28  ARG A CZ  
34   N NH1 . ARG A 11  ? 0.6929 0.7760 0.7206 0.0003  0.0434  -0.0602 28  ARG A NH1 
35   N NH2 . ARG A 11  ? 0.8213 0.9111 0.8609 0.0033  0.0401  -0.0644 28  ARG A NH2 
36   N N   . LYS A 12  ? 0.3592 0.3901 0.3603 -0.0114 0.0394  -0.0331 29  LYS A N   
37   C CA  . LYS A 12  ? 0.3113 0.3383 0.3102 -0.0077 0.0378  -0.0304 29  LYS A CA  
38   C C   . LYS A 12  ? 0.3239 0.3428 0.3157 -0.0090 0.0377  -0.0263 29  LYS A C   
39   O O   . LYS A 12  ? 0.3071 0.3269 0.2946 -0.0097 0.0394  -0.0267 29  LYS A O   
40   C CB  . LYS A 12  ? 0.3918 0.4271 0.3911 -0.0010 0.0389  -0.0329 29  LYS A CB  
41   C CG  . LYS A 12  ? 0.3999 0.4452 0.4064 0.0016  0.0387  -0.0376 29  LYS A CG  
42   C CD  . LYS A 12  ? 0.4396 0.4946 0.4456 0.0089  0.0401  -0.0395 29  LYS A CD  
43   C CE  . LYS A 12  ? 0.4089 0.4765 0.4220 0.0119  0.0400  -0.0451 29  LYS A CE  
44   N NZ  . LYS A 12  ? 0.4258 0.4919 0.4438 0.0123  0.0374  -0.0446 29  LYS A NZ  
45   N N   . ALA A 13  ? 0.2992 0.3109 0.2901 -0.0091 0.0356  -0.0228 30  ALA A N   
46   C CA  . ALA A 13  ? 0.3126 0.3176 0.2979 -0.0099 0.0353  -0.0197 30  ALA A CA  
47   C C   . ALA A 13  ? 0.2998 0.3018 0.2853 -0.0057 0.0344  -0.0181 30  ALA A C   
48   O O   . ALA A 13  ? 0.3106 0.3127 0.3001 -0.0042 0.0327  -0.0177 30  ALA A O   
49   C CB  . ALA A 13  ? 0.2947 0.2932 0.2782 -0.0151 0.0338  -0.0166 30  ALA A CB  
50   N N   . VAL A 14  ? 0.3009 0.3008 0.2829 -0.0040 0.0356  -0.0174 31  VAL A N   
51   C CA  . VAL A 14  ? 0.2812 0.2780 0.2640 -0.0001 0.0355  -0.0158 31  VAL A CA  
52   C C   . VAL A 14  ? 0.3022 0.2909 0.2822 -0.0030 0.0341  -0.0136 31  VAL A C   
53   O O   . VAL A 14  ? 0.2778 0.2652 0.2542 -0.0057 0.0347  -0.0141 31  VAL A O   
54   C CB  . VAL A 14  ? 0.3093 0.3099 0.2916 0.0046  0.0386  -0.0169 31  VAL A CB  
55   C CG1 . VAL A 14  ? 0.2887 0.2848 0.2724 0.0082  0.0392  -0.0146 31  VAL A CG1 
56   C CG2 . VAL A 14  ? 0.3439 0.3537 0.3289 0.0083  0.0399  -0.0191 31  VAL A CG2 
57   N N   . PHE A 15  ? 0.2914 0.2758 0.2735 -0.0023 0.0322  -0.0115 32  PHE A N   
58   C CA  . PHE A 15  ? 0.2895 0.2670 0.2697 -0.0046 0.0306  -0.0098 32  PHE A CA  
59   C C   . PHE A 15  ? 0.3328 0.3074 0.3154 -0.0009 0.0314  -0.0089 32  PHE A C   
60   O O   . PHE A 15  ? 0.3336 0.3076 0.3194 0.0015  0.0303  -0.0074 32  PHE A O   
61   C CB  . PHE A 15  ? 0.3002 0.2746 0.2810 -0.0077 0.0275  -0.0079 32  PHE A CB  
62   C CG  . PHE A 15  ? 0.2773 0.2541 0.2575 -0.0113 0.0271  -0.0081 32  PHE A CG  
63   C CD1 . PHE A 15  ? 0.2845 0.2660 0.2685 -0.0105 0.0274  -0.0094 32  PHE A CD1 
64   C CD2 . PHE A 15  ? 0.2956 0.2705 0.2718 -0.0155 0.0267  -0.0070 32  PHE A CD2 
65   C CE1 . PHE A 15  ? 0.3067 0.2899 0.2915 -0.0140 0.0275  -0.0098 32  PHE A CE1 
66   C CE2 . PHE A 15  ? 0.2712 0.2481 0.2474 -0.0187 0.0269  -0.0065 32  PHE A CE2 
67   C CZ  . PHE A 15  ? 0.2975 0.2781 0.2785 -0.0181 0.0274  -0.0079 32  PHE A CZ  
68   N N   . PRO A 16  ? 0.3212 0.2941 0.3030 -0.0002 0.0333  -0.0099 33  PRO A N   
69   C CA  . PRO A 16  ? 0.3402 0.3092 0.3253 0.0029  0.0344  -0.0088 33  PRO A CA  
70   C C   . PRO A 16  ? 0.3992 0.3626 0.3842 0.0000  0.0315  -0.0078 33  PRO A C   
71   O O   . PRO A 16  ? 0.3357 0.2973 0.3176 -0.0038 0.0303  -0.0089 33  PRO A O   
72   C CB  . PRO A 16  ? 0.3028 0.2716 0.2878 0.0036  0.0374  -0.0109 33  PRO A CB  
73   C CG  . PRO A 16  ? 0.3212 0.2956 0.3028 0.0026  0.0383  -0.0128 33  PRO A CG  
74   C CD  . PRO A 16  ? 0.3518 0.3268 0.3304 -0.0015 0.0352  -0.0122 33  PRO A CD  
75   N N   . VAL A 17  ? 0.3062 0.2679 0.2944 0.0021  0.0304  -0.0056 34  VAL A N   
76   C CA  . VAL A 17  ? 0.3285 0.2854 0.3168 -0.0002 0.0274  -0.0045 34  VAL A CA  
77   C C   . VAL A 17  ? 0.4006 0.3543 0.3936 0.0029  0.0284  -0.0032 34  VAL A C   
78   O O   . VAL A 17  ? 0.4051 0.3570 0.3998 0.0034  0.0263  -0.0013 34  VAL A O   
79   C CB  . VAL A 17  ? 0.3182 0.2761 0.3057 -0.0019 0.0243  -0.0030 34  VAL A CB  
80   C CG1 . VAL A 17  ? 0.3399 0.2995 0.3232 -0.0061 0.0234  -0.0038 34  VAL A CG1 
81   C CG2 . VAL A 17  ? 0.3611 0.3236 0.3520 0.0020  0.0250  -0.0023 34  VAL A CG2 
82   N N   . ALA A 18  ? 0.3839 0.3373 0.3796 0.0056  0.0320  -0.0039 35  ALA A N   
83   C CA  . ALA A 18  ? 0.4244 0.3741 0.4256 0.0084  0.0338  -0.0027 35  ALA A CA  
84   C C   . ALA A 18  ? 0.5649 0.5102 0.5674 0.0058  0.0345  -0.0055 35  ALA A C   
85   O O   . ALA A 18  ? 0.4809 0.4234 0.4894 0.0081  0.0375  -0.0054 35  ALA A O   
86   C CB  . ALA A 18  ? 0.3918 0.3446 0.3969 0.0141  0.0379  -0.0009 35  ALA A CB  
87   N N   . GLY A 19  ? 0.4845 0.4299 0.4824 0.0012  0.0322  -0.0081 36  GLY A N   
88   C CA  . GLY A 19  ? 0.4755 0.4188 0.4750 -0.0010 0.0328  -0.0118 36  GLY A CA  
89   C C   . GLY A 19  ? 0.5235 0.4622 0.5281 -0.0009 0.0325  -0.0120 36  GLY A C   
90   O O   . GLY A 19  ? 0.4533 0.3907 0.4562 -0.0024 0.0291  -0.0106 36  GLY A O   
91   N N   . MET A 20  ? 0.5498 0.4862 0.5612 0.0007  0.0361  -0.0140 37  MET A N   
92   C CA  . MET A 20  ? 0.4684 0.4005 0.4861 0.0007  0.0364  -0.0145 37  MET A CA  
93   C C   . MET A 20  ? 0.6021 0.5344 0.6173 -0.0037 0.0329  -0.0184 37  MET A C   
94   O O   . MET A 20  ? 0.5391 0.4689 0.5563 -0.0044 0.0311  -0.0180 37  MET A O   
95   C CB  . MET A 20  ? 0.5292 0.4586 0.5559 0.0032  0.0415  -0.0160 37  MET A CB  
96   C CG  . MET A 20  ? 0.6585 0.5876 0.6889 0.0085  0.0452  -0.0109 37  MET A CG  
97   S SD  . MET A 20  ? 0.9566 0.8812 0.9998 0.0119  0.0519  -0.0113 37  MET A SD  
98   C CE  . MET A 20  ? 0.5790 0.4988 0.6284 0.0100  0.0507  -0.0120 37  MET A CE  
99   N N   . GLY A 21  ? 0.5126 0.4486 0.5236 -0.0063 0.0321  -0.0222 38  GLY A N   
100  C CA  . GLY A 21  ? 0.4839 0.4221 0.4917 -0.0099 0.0288  -0.0257 38  GLY A CA  
101  C C   . GLY A 21  ? 0.5059 0.4414 0.5214 -0.0102 0.0296  -0.0292 38  GLY A C   
102  O O   . GLY A 21  ? 0.4663 0.4018 0.4805 -0.0119 0.0264  -0.0296 38  GLY A O   
103  N N   . THR A 22  ? 0.4484 0.3817 0.4725 -0.0086 0.0340  -0.0319 39  THR A N   
104  C CA  . THR A 22  ? 0.4881 0.4187 0.5214 -0.0090 0.0354  -0.0359 39  THR A CA  
105  C C   . THR A 22  ? 0.4521 0.3875 0.4834 -0.0126 0.0324  -0.0422 39  THR A C   
106  O O   . THR A 22  ? 0.4240 0.3586 0.4594 -0.0137 0.0313  -0.0448 39  THR A O   
107  C CB  . THR A 22  ? 0.5571 0.4850 0.6007 -0.0070 0.0411  -0.0383 39  THR A CB  
108  O OG1 . THR A 22  ? 0.5731 0.5056 0.6148 -0.0083 0.0418  -0.0433 39  THR A OG1 
109  C CG2 . THR A 22  ? 0.6236 0.5479 0.6689 -0.0027 0.0444  -0.0315 39  THR A CG2 
110  N N   . ARG A 23  ? 0.4856 0.4269 0.5103 -0.0141 0.0310  -0.0446 40  ARG A N   
111  C CA  . ARG A 23  ? 0.4965 0.4446 0.5181 -0.0170 0.0280  -0.0505 40  ARG A CA  
112  C C   . ARG A 23  ? 0.4350 0.3841 0.4499 -0.0182 0.0233  -0.0471 40  ARG A C   
113  O O   . ARG A 23  ? 0.4928 0.4473 0.5067 -0.0199 0.0208  -0.0516 40  ARG A O   
114  C CB  . ARG A 23  ? 0.6164 0.5711 0.6317 -0.0179 0.0277  -0.0525 40  ARG A CB  
115  C CG  . ARG A 23  ? 0.7243 0.6819 0.7468 -0.0181 0.0310  -0.0603 40  ARG A CG  
116  C CD  . ARG A 23  ? 0.8358 0.7929 0.8573 -0.0167 0.0339  -0.0587 40  ARG A CD  
117  N NE  . ARG A 23  ? 0.9259 0.8902 0.9371 -0.0180 0.0316  -0.0581 40  ARG A NE  
118  C CZ  . ARG A 23  ? 1.0135 0.9837 1.0244 -0.0186 0.0327  -0.0632 40  ARG A CZ  
119  N NH1 . ARG A 23  ? 0.9455 0.9185 0.9646 -0.0191 0.0344  -0.0714 40  ARG A NH1 
120  N NH2 . ARG A 23  ? 0.8725 0.8463 0.8754 -0.0187 0.0323  -0.0604 40  ARG A NH2 
121  N N   . PHE A 24  ? 0.4373 0.3821 0.4482 -0.0170 0.0222  -0.0398 41  PHE A N   
122  C CA  . PHE A 24  ? 0.3945 0.3398 0.3995 -0.0179 0.0179  -0.0361 41  PHE A CA  
123  C C   . PHE A 24  ? 0.4623 0.4016 0.4721 -0.0166 0.0177  -0.0333 41  PHE A C   
124  O O   . PHE A 24  ? 0.4463 0.3851 0.4517 -0.0170 0.0143  -0.0296 41  PHE A O   
125  C CB  . PHE A 24  ? 0.3549 0.3012 0.3511 -0.0179 0.0163  -0.0302 41  PHE A CB  
126  C CG  . PHE A 24  ? 0.4128 0.3661 0.4029 -0.0194 0.0158  -0.0323 41  PHE A CG  
127  C CD1 . PHE A 24  ? 0.4030 0.3580 0.3947 -0.0190 0.0188  -0.0351 41  PHE A CD1 
128  C CD2 . PHE A 24  ? 0.4638 0.4224 0.4469 -0.0211 0.0123  -0.0314 41  PHE A CD2 
129  C CE1 . PHE A 24  ? 0.4162 0.3785 0.4020 -0.0205 0.0183  -0.0372 41  PHE A CE1 
130  C CE2 . PHE A 24  ? 0.4514 0.4173 0.4289 -0.0222 0.0120  -0.0328 41  PHE A CE2 
131  C CZ  . PHE A 24  ? 0.4260 0.3938 0.4049 -0.0220 0.0149  -0.0358 41  PHE A CZ  
132  N N   . LEU A 25  ? 0.3373 0.2722 0.3566 -0.0151 0.0214  -0.0349 42  LEU A N   
133  C CA  . LEU A 25  ? 0.4087 0.3390 0.4333 -0.0141 0.0212  -0.0330 42  LEU A CA  
134  C C   . LEU A 25  ? 0.4264 0.3598 0.4508 -0.0164 0.0180  -0.0375 42  LEU A C   
135  O O   . LEU A 25  ? 0.4323 0.3709 0.4573 -0.0182 0.0179  -0.0439 42  LEU A O   
136  C CB  . LEU A 25  ? 0.3699 0.2955 0.4059 -0.0121 0.0263  -0.0342 42  LEU A CB  
137  C CG  . LEU A 25  ? 0.3916 0.3141 0.4281 -0.0088 0.0294  -0.0284 42  LEU A CG  
138  C CD1 . LEU A 25  ? 0.4291 0.3483 0.4767 -0.0067 0.0352  -0.0300 42  LEU A CD1 
139  C CD2 . LEU A 25  ? 0.3486 0.2687 0.3828 -0.0069 0.0275  -0.0217 42  LEU A CD2 
140  N N   . PRO A 26  ? 0.4018 0.3331 0.4256 -0.0163 0.0155  -0.0347 43  PRO A N   
141  C CA  . PRO A 26  ? 0.3894 0.3156 0.4135 -0.0141 0.0153  -0.0280 43  PRO A CA  
142  C C   . PRO A 26  ? 0.3514 0.2782 0.3664 -0.0138 0.0124  -0.0221 43  PRO A C   
143  O O   . PRO A 26  ? 0.3133 0.2370 0.3286 -0.0118 0.0123  -0.0172 43  PRO A O   
144  C CB  . PRO A 26  ? 0.4446 0.3696 0.4723 -0.0148 0.0134  -0.0293 43  PRO A CB  
145  C CG  . PRO A 26  ? 0.4231 0.3542 0.4462 -0.0174 0.0101  -0.0343 43  PRO A CG  
146  C CD  . PRO A 26  ? 0.3676 0.3024 0.3920 -0.0181 0.0127  -0.0393 43  PRO A CD  
147  N N   . ALA A 27  ? 0.3150 0.2463 0.3222 -0.0155 0.0102  -0.0224 44  ALA A N   
148  C CA  . ALA A 27  ? 0.3235 0.2551 0.3235 -0.0154 0.0076  -0.0170 44  ALA A CA  
149  C C   . ALA A 27  ? 0.3538 0.2831 0.3544 -0.0133 0.0099  -0.0131 44  ALA A C   
150  O O   . ALA A 27  ? 0.3515 0.2800 0.3493 -0.0126 0.0082  -0.0087 44  ALA A O   
151  C CB  . ALA A 27  ? 0.3528 0.2898 0.3453 -0.0175 0.0056  -0.0178 44  ALA A CB  
152  N N   . THR A 28  ? 0.2821 0.2113 0.2865 -0.0121 0.0138  -0.0151 45  THR A N   
153  C CA  . THR A 28  ? 0.3286 0.2569 0.3339 -0.0096 0.0164  -0.0119 45  THR A CA  
154  C C   . THR A 28  ? 0.3700 0.2947 0.3826 -0.0063 0.0188  -0.0097 45  THR A C   
155  O O   . THR A 28  ? 0.3248 0.2495 0.3398 -0.0034 0.0219  -0.0076 45  THR A O   
156  C CB  . THR A 28  ? 0.3432 0.2738 0.3487 -0.0096 0.0195  -0.0147 45  THR A CB  
157  O OG1 . THR A 28  ? 0.3115 0.2413 0.3231 -0.0101 0.0217  -0.0197 45  THR A OG1 
158  C CG2 . THR A 28  ? 0.3704 0.3053 0.3681 -0.0122 0.0174  -0.0155 45  THR A CG2 
159  N N   . LYS A 29  ? 0.3110 0.2332 0.3273 -0.0065 0.0177  -0.0100 46  LYS A N   
160  C CA  . LYS A 29  ? 0.3356 0.2550 0.3585 -0.0031 0.0200  -0.0070 46  LYS A CA  
161  C C   . LYS A 29  ? 0.3817 0.3024 0.4018 -0.0006 0.0189  -0.0019 46  LYS A C   
162  O O   . LYS A 29  ? 0.3933 0.3143 0.4173 0.0032  0.0220  0.0009  46  LYS A O   
163  C CB  . LYS A 29  ? 0.3638 0.2808 0.3909 -0.0039 0.0187  -0.0081 46  LYS A CB  
164  C CG  . LYS A 29  ? 0.4031 0.3179 0.4362 -0.0001 0.0209  -0.0038 46  LYS A CG  
165  C CD  . LYS A 29  ? 0.4397 0.3515 0.4807 -0.0001 0.0225  -0.0053 46  LYS A CD  
166  C CE  . LYS A 29  ? 0.3874 0.2981 0.4335 0.0042  0.0246  0.0002  46  LYS A CE  
167  N NZ  . LYS A 29  ? 0.4205 0.3291 0.4700 0.0031  0.0229  -0.0005 46  LYS A NZ  
168  N N   . ALA A 30  ? 0.3721 0.2942 0.3861 -0.0023 0.0146  -0.0007 47  ALA A N   
169  C CA  . ALA A 30  ? 0.4018 0.3256 0.4143 -0.0002 0.0131  0.0031  47  ALA A CA  
170  C C   . ALA A 30  ? 0.3953 0.3223 0.4022 -0.0013 0.0119  0.0035  47  ALA A C   
171  O O   . ALA A 30  ? 0.3789 0.3079 0.3849 -0.0001 0.0104  0.0057  47  ALA A O   
172  C CB  . ALA A 30  ? 0.4880 0.4106 0.5000 -0.0010 0.0091  0.0044  47  ALA A CB  
173  N N   . MET A 31  ? 0.4191 0.3470 0.4227 -0.0037 0.0126  0.0010  48  MET A N   
174  C CA  . MET A 31  ? 0.3474 0.2784 0.3465 -0.0046 0.0124  0.0015  48  MET A CA  
175  C C   . MET A 31  ? 0.3687 0.3010 0.3672 -0.0049 0.0155  -0.0011 48  MET A C   
176  O O   . MET A 31  ? 0.3282 0.2591 0.3286 -0.0058 0.0168  -0.0039 48  MET A O   
177  C CB  . MET A 31  ? 0.4091 0.3404 0.4030 -0.0080 0.0086  0.0020  48  MET A CB  
178  C CG  . MET A 31  ? 0.4104 0.3414 0.4016 -0.0109 0.0077  -0.0005 48  MET A CG  
179  S SD  . MET A 31  ? 0.4843 0.4154 0.4704 -0.0137 0.0032  0.0014  48  MET A SD  
180  C CE  . MET A 31  ? 0.5808 0.5085 0.5712 -0.0122 0.0011  0.0025  48  MET A CE  
181  N N   . PRO A 32  ? 0.3735 0.3090 0.3705 -0.0039 0.0171  -0.0006 49  PRO A N   
182  C CA  . PRO A 32  ? 0.3583 0.2954 0.3544 -0.0044 0.0199  -0.0032 49  PRO A CA  
183  C C   . PRO A 32  ? 0.3434 0.2816 0.3342 -0.0084 0.0180  -0.0053 49  PRO A C   
184  O O   . PRO A 32  ? 0.3283 0.2666 0.3155 -0.0107 0.0148  -0.0039 49  PRO A O   
185  C CB  . PRO A 32  ? 0.4058 0.3465 0.4011 -0.0021 0.0215  -0.0019 49  PRO A CB  
186  C CG  . PRO A 32  ? 0.3988 0.3406 0.3928 -0.0026 0.0186  0.0003  49  PRO A CG  
187  C CD  . PRO A 32  ? 0.3693 0.3076 0.3655 -0.0025 0.0163  0.0016  49  PRO A CD  
188  N N   . LYS A 33  ? 0.3516 0.2911 0.3424 -0.0090 0.0202  -0.0085 50  LYS A N   
189  C CA  . LYS A 33  ? 0.3702 0.3123 0.3565 -0.0123 0.0189  -0.0111 50  LYS A CA  
190  C C   . LYS A 33  ? 0.3503 0.2953 0.3306 -0.0143 0.0169  -0.0086 50  LYS A C   
191  O O   . LYS A 33  ? 0.3758 0.3221 0.3521 -0.0167 0.0144  -0.0081 50  LYS A O   
192  C CB  . LYS A 33  ? 0.4036 0.3477 0.3916 -0.0120 0.0222  -0.0151 50  LYS A CB  
193  C CG  . LYS A 33  ? 0.4149 0.3636 0.3981 -0.0149 0.0212  -0.0181 50  LYS A CG  
194  C CD  . LYS A 33  ? 0.3956 0.3449 0.3776 -0.0169 0.0182  -0.0193 50  LYS A CD  
195  C CE  . LYS A 33  ? 0.5129 0.4683 0.4915 -0.0189 0.0178  -0.0235 50  LYS A CE  
196  N NZ  . LYS A 33  ? 0.4953 0.4550 0.4689 -0.0198 0.0186  -0.0229 50  LYS A NZ  
197  N N   . GLU A 34  ? 0.3253 0.2714 0.3054 -0.0130 0.0182  -0.0069 51  GLU A N   
198  C CA  . GLU A 34  ? 0.3429 0.2916 0.3187 -0.0150 0.0171  -0.0049 51  GLU A CA  
199  C C   . GLU A 34  ? 0.4047 0.3515 0.3801 -0.0160 0.0140  -0.0016 51  GLU A C   
200  O O   . GLU A 34  ? 0.3832 0.3316 0.3559 -0.0180 0.0131  0.0003  51  GLU A O   
201  C CB  . GLU A 34  ? 0.3294 0.2806 0.3063 -0.0132 0.0195  -0.0049 51  GLU A CB  
202  C CG  . GLU A 34  ? 0.3504 0.3041 0.3270 -0.0124 0.0226  -0.0079 51  GLU A CG  
203  C CD  . GLU A 34  ? 0.4855 0.4370 0.4670 -0.0093 0.0250  -0.0096 51  GLU A CD  
204  O OE1 . GLU A 34  ? 0.4710 0.4197 0.4566 -0.0070 0.0249  -0.0080 51  GLU A OE1 
205  O OE2 . GLU A 34  ? 0.4636 0.4166 0.4453 -0.0092 0.0273  -0.0125 51  GLU A OE2 
206  N N   . MET A 35  ? 0.3494 0.2927 0.3277 -0.0148 0.0125  -0.0008 52  MET A N   
207  C CA  . MET A 35  ? 0.3469 0.2884 0.3248 -0.0159 0.0093  0.0021  52  MET A CA  
208  C C   . MET A 35  ? 0.3217 0.2627 0.2965 -0.0180 0.0070  0.0021  52  MET A C   
209  O O   . MET A 35  ? 0.3763 0.3161 0.3502 -0.0190 0.0045  0.0048  52  MET A O   
210  C CB  . MET A 35  ? 0.3493 0.2883 0.3320 -0.0133 0.0086  0.0031  52  MET A CB  
211  C CG  . MET A 35  ? 0.3302 0.2711 0.3157 -0.0112 0.0096  0.0038  52  MET A CG  
212  S SD  . MET A 35  ? 0.3452 0.2877 0.3295 -0.0137 0.0081  0.0057  52  MET A SD  
213  C CE  . MET A 35  ? 0.3917 0.3303 0.3763 -0.0150 0.0043  0.0081  52  MET A CE  
214  N N   . LEU A 36  ? 0.3293 0.2720 0.3028 -0.0185 0.0079  -0.0010 53  LEU A N   
215  C CA  . LEU A 36  ? 0.3770 0.3214 0.3472 -0.0202 0.0057  -0.0013 53  LEU A CA  
216  C C   . LEU A 36  ? 0.3767 0.3243 0.3417 -0.0222 0.0048  0.0018  53  LEU A C   
217  O O   . LEU A 36  ? 0.3766 0.3268 0.3399 -0.0228 0.0068  0.0018  53  LEU A O   
218  C CB  . LEU A 36  ? 0.3597 0.3069 0.3301 -0.0204 0.0069  -0.0063 53  LEU A CB  
219  C CG  . LEU A 36  ? 0.3960 0.3398 0.3729 -0.0186 0.0084  -0.0093 53  LEU A CG  
220  C CD1 . LEU A 36  ? 0.4826 0.4293 0.4610 -0.0192 0.0094  -0.0149 53  LEU A CD1 
221  C CD2 . LEU A 36  ? 0.4479 0.3876 0.4273 -0.0178 0.0062  -0.0072 53  LEU A CD2 
222  N N   . PRO A 37  ? 0.3362 0.2839 0.2989 -0.0230 0.0022  0.0046  54  PRO A N   
223  C CA  . PRO A 37  ? 0.4190 0.3695 0.3775 -0.0246 0.0018  0.0086  54  PRO A CA  
224  C C   . PRO A 37  ? 0.3851 0.3423 0.3385 -0.0254 0.0020  0.0073  54  PRO A C   
225  O O   . PRO A 37  ? 0.3416 0.3017 0.2945 -0.0250 0.0014  0.0033  54  PRO A O   
226  C CB  . PRO A 37  ? 0.3565 0.3041 0.3155 -0.0245 -0.0010 0.0124  54  PRO A CB  
227  C CG  . PRO A 37  ? 0.4057 0.3521 0.3663 -0.0234 -0.0025 0.0092  54  PRO A CG  
228  C CD  . PRO A 37  ? 0.3981 0.3428 0.3626 -0.0223 -0.0003 0.0050  54  PRO A CD  
229  N N   . VAL A 38  ? 0.3654 0.3259 0.3156 -0.0265 0.0031  0.0106  55  VAL A N   
230  C CA  . VAL A 38  ? 0.4160 0.3841 0.3608 -0.0270 0.0030  0.0114  55  VAL A CA  
231  C C   . VAL A 38  ? 0.4738 0.4414 0.4168 -0.0273 0.0017  0.0181  55  VAL A C   
232  O O   . VAL A 38  ? 0.4391 0.4043 0.3833 -0.0282 0.0029  0.0226  55  VAL A O   
233  C CB  . VAL A 38  ? 0.3909 0.3635 0.3336 -0.0278 0.0057  0.0102  55  VAL A CB  
234  C CG1 . VAL A 38  ? 0.3689 0.3507 0.3056 -0.0281 0.0057  0.0117  55  VAL A CG1 
235  C CG2 . VAL A 38  ? 0.3640 0.3366 0.3091 -0.0272 0.0071  0.0035  55  VAL A CG2 
236  N N   . VAL A 39  ? 0.4254 0.3951 0.3664 -0.0264 -0.0008 0.0186  56  VAL A N   
237  C CA  . VAL A 39  ? 0.4219 0.3906 0.3620 -0.0260 -0.0024 0.0248  56  VAL A CA  
238  C C   . VAL A 39  ? 0.4613 0.4209 0.4069 -0.0262 -0.0032 0.0267  56  VAL A C   
239  O O   . VAL A 39  ? 0.5120 0.4682 0.4596 -0.0253 -0.0053 0.0249  56  VAL A O   
240  C CB  . VAL A 39  ? 0.4391 0.4124 0.3756 -0.0265 -0.0007 0.0309  56  VAL A CB  
241  C CG1 . VAL A 39  ? 0.5468 0.5192 0.4828 -0.0257 -0.0021 0.0377  56  VAL A CG1 
242  C CG2 . VAL A 39  ? 0.5525 0.5361 0.4836 -0.0260 -0.0002 0.0284  56  VAL A CG2 
243  N N   . ASP A 40  ? 0.4416 0.3977 0.3901 -0.0272 -0.0014 0.0301  57  ASP A N   
244  C CA  . ASP A 40  ? 0.4295 0.3784 0.3837 -0.0273 -0.0023 0.0318  57  ASP A CA  
245  C C   . ASP A 40  ? 0.4383 0.3841 0.3972 -0.0279 -0.0004 0.0292  57  ASP A C   
246  O O   . ASP A 40  ? 0.4024 0.3438 0.3666 -0.0280 -0.0006 0.0306  57  ASP A O   
247  C CB  . ASP A 40  ? 0.4816 0.4292 0.4366 -0.0277 -0.0022 0.0388  57  ASP A CB  
248  C CG  . ASP A 40  ? 0.4828 0.4331 0.4374 -0.0292 0.0010  0.0423  57  ASP A CG  
249  O OD1 . ASP A 40  ? 0.4628 0.4163 0.4157 -0.0299 0.0029  0.0391  57  ASP A OD1 
250  O OD2 . ASP A 40  ? 0.5340 0.4827 0.4906 -0.0297 0.0017  0.0483  57  ASP A OD2 
251  N N   . LYS A 41  ? 0.4143 0.3630 0.3718 -0.0279 0.0014  0.0252  58  LYS A N   
252  C CA  . LYS A 41  ? 0.4260 0.3734 0.3872 -0.0283 0.0036  0.0233  58  LYS A CA  
253  C C   . LYS A 41  ? 0.3869 0.3355 0.3479 -0.0271 0.0046  0.0177  58  LYS A C   
254  O O   . LYS A 41  ? 0.3611 0.3137 0.3182 -0.0272 0.0051  0.0155  58  LYS A O   
255  C CB  . LYS A 41  ? 0.4460 0.3967 0.4060 -0.0301 0.0061  0.0261  58  LYS A CB  
256  C CG  . LYS A 41  ? 0.3941 0.3444 0.3581 -0.0305 0.0084  0.0240  58  LYS A CG  
257  C CD  . LYS A 41  ? 0.4322 0.3854 0.3960 -0.0324 0.0110  0.0266  58  LYS A CD  
258  C CE  . LYS A 41  ? 0.5001 0.4507 0.4674 -0.0338 0.0112  0.0321  58  LYS A CE  
259  N NZ  . LYS A 41  ? 0.6210 0.5747 0.5886 -0.0357 0.0144  0.0349  58  LYS A NZ  
260  N N   . PRO A 42  ? 0.3772 0.3230 0.3429 -0.0258 0.0049  0.0153  59  PRO A N   
261  C CA  . PRO A 42  ? 0.3397 0.2864 0.3058 -0.0242 0.0063  0.0108  59  PRO A CA  
262  C C   . PRO A 42  ? 0.3009 0.2518 0.2647 -0.0250 0.0090  0.0091  59  PRO A C   
263  O O   . PRO A 42  ? 0.3111 0.2634 0.2751 -0.0262 0.0102  0.0109  59  PRO A O   
264  C CB  . PRO A 42  ? 0.3728 0.3168 0.3444 -0.0223 0.0064  0.0100  59  PRO A CB  
265  C CG  . PRO A 42  ? 0.4026 0.3440 0.3767 -0.0229 0.0042  0.0132  59  PRO A CG  
266  C CD  . PRO A 42  ? 0.4469 0.3893 0.4179 -0.0253 0.0041  0.0166  59  PRO A CD  
267  N N   . LEU A 43  ? 0.3501 0.3029 0.3124 -0.0242 0.0100  0.0054  60  LEU A N   
268  C CA  . LEU A 43  ? 0.3154 0.2722 0.2759 -0.0247 0.0126  0.0034  60  LEU A CA  
269  C C   . LEU A 43  ? 0.3528 0.3096 0.3160 -0.0242 0.0144  0.0037  60  LEU A C   
270  O O   . LEU A 43  ? 0.3107 0.2707 0.2722 -0.0258 0.0158  0.0046  60  LEU A O   
271  C CB  . LEU A 43  ? 0.3173 0.2752 0.2784 -0.0233 0.0138  -0.0013 60  LEU A CB  
272  C CG  . LEU A 43  ? 0.3996 0.3602 0.3580 -0.0240 0.0127  -0.0034 60  LEU A CG  
273  C CD1 . LEU A 43  ? 0.3856 0.3451 0.3475 -0.0225 0.0138  -0.0084 60  LEU A CD1 
274  C CD2 . LEU A 43  ? 0.3643 0.3315 0.3175 -0.0257 0.0134  -0.0034 60  LEU A CD2 
275  N N   . ILE A 44  ? 0.3185 0.2727 0.2863 -0.0220 0.0145  0.0030  61  ILE A N   
276  C CA  . ILE A 44  ? 0.2771 0.2331 0.2478 -0.0210 0.0162  0.0024  61  ILE A CA  
277  C C   . ILE A 44  ? 0.2823 0.2390 0.2539 -0.0233 0.0158  0.0050  61  ILE A C   
278  O O   . ILE A 44  ? 0.2788 0.2385 0.2515 -0.0238 0.0177  0.0041  61  ILE A O   
279  C CB  . ILE A 44  ? 0.3037 0.2581 0.2793 -0.0177 0.0161  0.0014  61  ILE A CB  
280  C CG1 . ILE A 44  ? 0.3206 0.2788 0.2991 -0.0161 0.0180  0.0001  61  ILE A CG1 
281  C CG2 . ILE A 44  ? 0.3232 0.2740 0.3011 -0.0177 0.0133  0.0037  61  ILE A CG2 
282  C CD1 . ILE A 44  ? 0.3195 0.2815 0.2957 -0.0158 0.0208  -0.0022 61  ILE A CD1 
283  N N   . GLN A 45  ? 0.3130 0.2668 0.2848 -0.0247 0.0136  0.0082  62  GLN A N   
284  C CA  . GLN A 45  ? 0.3065 0.2603 0.2806 -0.0268 0.0138  0.0108  62  GLN A CA  
285  C C   . GLN A 45  ? 0.3467 0.3039 0.3173 -0.0293 0.0157  0.0123  62  GLN A C   
286  O O   . GLN A 45  ? 0.3395 0.2982 0.3129 -0.0307 0.0174  0.0129  62  GLN A O   
287  C CB  . GLN A 45  ? 0.3648 0.3147 0.3406 -0.0275 0.0113  0.0143  62  GLN A CB  
288  C CG  . GLN A 45  ? 0.3676 0.3169 0.3479 -0.0295 0.0119  0.0168  62  GLN A CG  
289  C CD  . GLN A 45  ? 0.4848 0.4300 0.4683 -0.0298 0.0096  0.0200  62  GLN A CD  
290  O OE1 . GLN A 45  ? 0.4008 0.3435 0.3844 -0.0281 0.0072  0.0194  62  GLN A OE1 
291  N NE2 . GLN A 45  ? 0.4299 0.3741 0.4162 -0.0320 0.0105  0.0236  62  GLN A NE2 
292  N N   . TYR A 46  ? 0.3241 0.2831 0.2890 -0.0297 0.0156  0.0127  63  TYR A N   
293  C CA  . TYR A 46  ? 0.3180 0.2814 0.2792 -0.0316 0.0176  0.0139  63  TYR A CA  
294  C C   . TYR A 46  ? 0.3158 0.2823 0.2781 -0.0314 0.0202  0.0104  63  TYR A C   
295  O O   . TYR A 46  ? 0.3288 0.2978 0.2918 -0.0332 0.0221  0.0117  63  TYR A O   
296  C CB  . TYR A 46  ? 0.3852 0.3518 0.3402 -0.0315 0.0170  0.0133  63  TYR A CB  
297  C CG  . TYR A 46  ? 0.3590 0.3250 0.3115 -0.0317 0.0147  0.0168  63  TYR A CG  
298  C CD1 . TYR A 46  ? 0.4094 0.3784 0.3590 -0.0332 0.0151  0.0218  63  TYR A CD1 
299  C CD2 . TYR A 46  ? 0.3462 0.3093 0.2991 -0.0302 0.0123  0.0152  63  TYR A CD2 
300  C CE1 . TYR A 46  ? 0.3739 0.3434 0.3208 -0.0328 0.0131  0.0251  63  TYR A CE1 
301  C CE2 . TYR A 46  ? 0.4053 0.3686 0.3558 -0.0302 0.0102  0.0179  63  TYR A CE2 
302  C CZ  . TYR A 46  ? 0.4402 0.4070 0.3875 -0.0313 0.0105  0.0229  63  TYR A CZ  
303  O OH  . TYR A 46  ? 0.4428 0.4107 0.3874 -0.0307 0.0083  0.0257  63  TYR A OH  
304  N N   . ALA A 47  ? 0.3195 0.2860 0.2826 -0.0290 0.0204  0.0063  64  ALA A N   
305  C CA  . ALA A 47  ? 0.3101 0.2801 0.2740 -0.0282 0.0229  0.0030  64  ALA A CA  
306  C C   . ALA A 47  ? 0.2953 0.2657 0.2648 -0.0281 0.0237  0.0027  64  ALA A C   
307  O O   . ALA A 47  ? 0.3087 0.2830 0.2790 -0.0291 0.0259  0.0015  64  ALA A O   
308  C CB  . ALA A 47  ? 0.2946 0.2644 0.2583 -0.0252 0.0233  -0.0007 64  ALA A CB  
309  N N   . VAL A 48  ? 0.3389 0.3061 0.3128 -0.0271 0.0220  0.0034  65  VAL A N   
310  C CA  . VAL A 48  ? 0.3260 0.2945 0.3061 -0.0271 0.0225  0.0024  65  VAL A CA  
311  C C   . VAL A 48  ? 0.3265 0.2954 0.3085 -0.0307 0.0236  0.0051  65  VAL A C   
312  O O   . VAL A 48  ? 0.3407 0.3130 0.3268 -0.0316 0.0255  0.0032  65  VAL A O   
313  C CB  . VAL A 48  ? 0.3393 0.3047 0.3238 -0.0252 0.0202  0.0026  65  VAL A CB  
314  C CG1 . VAL A 48  ? 0.3112 0.2781 0.3031 -0.0260 0.0203  0.0017  65  VAL A CG1 
315  C CG2 . VAL A 48  ? 0.3600 0.3264 0.3444 -0.0211 0.0201  -0.0001 65  VAL A CG2 
316  N N   . GLU A 49  ? 0.3550 0.3207 0.3346 -0.0327 0.0226  0.0096  66  GLU A N   
317  C CA  . GLU A 49  ? 0.3847 0.3505 0.3666 -0.0359 0.0241  0.0132  66  GLU A CA  
318  C C   . GLU A 49  ? 0.3394 0.3102 0.3185 -0.0374 0.0270  0.0125  66  GLU A C   
319  O O   . GLU A 49  ? 0.3391 0.3116 0.3229 -0.0394 0.0293  0.0127  66  GLU A O   
320  C CB  . GLU A 49  ? 0.3683 0.3307 0.3474 -0.0369 0.0226  0.0187  66  GLU A CB  
321  C CG  . GLU A 49  ? 0.4566 0.4140 0.4404 -0.0362 0.0201  0.0199  66  GLU A CG  
322  C CD  . GLU A 49  ? 0.4981 0.4525 0.4784 -0.0365 0.0182  0.0250  66  GLU A CD  
323  O OE1 . GLU A 49  ? 0.5240 0.4808 0.4976 -0.0367 0.0185  0.0272  66  GLU A OE1 
324  O OE2 . GLU A 49  ? 0.5300 0.4802 0.5144 -0.0361 0.0164  0.0266  66  GLU A OE2 
325  N N   . GLU A 50  ? 0.3142 0.2876 0.2865 -0.0363 0.0271  0.0111  67  GLU A N   
326  C CA  . GLU A 50  ? 0.3435 0.3221 0.3131 -0.0374 0.0297  0.0097  67  GLU A CA  
327  C C   . GLU A 50  ? 0.3262 0.3077 0.3005 -0.0367 0.0315  0.0051  67  GLU A C   
328  O O   . GLU A 50  ? 0.3249 0.3099 0.3015 -0.0387 0.0340  0.0049  67  GLU A O   
329  C CB  . GLU A 50  ? 0.2960 0.2769 0.2584 -0.0360 0.0293  0.0079  67  GLU A CB  
330  C CG  . GLU A 50  ? 0.3706 0.3574 0.3299 -0.0366 0.0318  0.0057  67  GLU A CG  
331  C CD  . GLU A 50  ? 0.4084 0.3977 0.3618 -0.0350 0.0313  0.0030  67  GLU A CD  
332  O OE1 . GLU A 50  ? 0.3753 0.3630 0.3258 -0.0346 0.0293  0.0042  67  GLU A OE1 
333  O OE2 . GLU A 50  ? 0.3650 0.3581 0.3172 -0.0343 0.0330  -0.0007 67  GLU A OE2 
334  N N   . ALA A 51  ? 0.3769 0.3579 0.3530 -0.0336 0.0304  0.0014  68  ALA A N   
335  C CA  . ALA A 51  ? 0.3107 0.2962 0.2911 -0.0321 0.0319  -0.0031 68  ALA A CA  
336  C C   . ALA A 51  ? 0.3462 0.3325 0.3345 -0.0342 0.0328  -0.0033 68  ALA A C   
337  O O   . ALA A 51  ? 0.3013 0.2923 0.2925 -0.0353 0.0352  -0.0058 68  ALA A O   
338  C CB  . ALA A 51  ? 0.3640 0.3492 0.3453 -0.0279 0.0306  -0.0060 68  ALA A CB  
339  N N   . VAL A 52  ? 0.3465 0.3282 0.3389 -0.0350 0.0311  -0.0007 69  VAL A N   
340  C CA  . VAL A 52  ? 0.3649 0.3468 0.3665 -0.0370 0.0320  -0.0013 69  VAL A CA  
341  C C   . VAL A 52  ? 0.3616 0.3440 0.3643 -0.0410 0.0347  0.0018  69  VAL A C   
342  O O   . VAL A 52  ? 0.3749 0.3606 0.3846 -0.0427 0.0371  -0.0007 69  VAL A O   
343  C CB  . VAL A 52  ? 0.3444 0.3208 0.3499 -0.0368 0.0294  0.0010  69  VAL A CB  
344  C CG1 . VAL A 52  ? 0.3859 0.3619 0.4018 -0.0393 0.0306  0.0008  69  VAL A CG1 
345  C CG2 . VAL A 52  ? 0.4033 0.3805 0.4091 -0.0328 0.0271  -0.0024 69  VAL A CG2 
346  N N   . ALA A 53  ? 0.3398 0.3195 0.3360 -0.0423 0.0347  0.0072  70  ALA A N   
347  C CA  . ALA A 53  ? 0.3322 0.3132 0.3287 -0.0456 0.0376  0.0111  70  ALA A CA  
348  C C   . ALA A 53  ? 0.4124 0.3997 0.4076 -0.0461 0.0402  0.0073  70  ALA A C   
349  O O   . ALA A 53  ? 0.4204 0.4097 0.4194 -0.0490 0.0433  0.0088  70  ALA A O   
350  C CB  . ALA A 53  ? 0.4033 0.3824 0.3919 -0.0461 0.0369  0.0173  70  ALA A CB  
351  N N   . ALA A 54  ? 0.3987 0.3588 0.3946 -0.0577 0.0054  0.0161  71  ALA A N   
352  C CA  . ALA A 54  ? 0.3642 0.3400 0.3640 -0.0615 0.0061  0.0171  71  ALA A CA  
353  C C   . ALA A 54  ? 0.4275 0.4124 0.4328 -0.0680 0.0044  0.0106  71  ALA A C   
354  O O   . ALA A 54  ? 0.3750 0.3749 0.3854 -0.0706 0.0038  0.0105  71  ALA A O   
355  C CB  . ALA A 54  ? 0.3617 0.3492 0.3600 -0.0547 0.0044  0.0194  71  ALA A CB  
356  N N   . GLY A 55  ? 0.3982 0.3745 0.4028 -0.0703 0.0032  0.0046  72  GLY A N   
357  C CA  . GLY A 55  ? 0.4437 0.4267 0.4520 -0.0764 0.0007  -0.0026 72  GLY A CA  
358  C C   . GLY A 55  ? 0.4070 0.3983 0.4105 -0.0724 -0.0029 -0.0075 72  GLY A C   
359  O O   . GLY A 55  ? 0.4089 0.4061 0.4132 -0.0766 -0.0062 -0.0139 72  GLY A O   
360  N N   . ILE A 56  ? 0.3903 0.3814 0.3887 -0.0645 -0.0024 -0.0048 73  ILE A N   
361  C CA  . ILE A 56  ? 0.3921 0.3893 0.3849 -0.0607 -0.0044 -0.0084 73  ILE A CA  
362  C C   . ILE A 56  ? 0.3702 0.3564 0.3582 -0.0617 -0.0039 -0.0156 73  ILE A C   
363  O O   . ILE A 56  ? 0.4178 0.3901 0.4064 -0.0607 -0.0012 -0.0160 73  ILE A O   
364  C CB  . ILE A 56  ? 0.3318 0.3306 0.3227 -0.0525 -0.0031 -0.0034 73  ILE A CB  
365  C CG1 . ILE A 56  ? 0.3510 0.3599 0.3458 -0.0508 -0.0038 0.0028  73  ILE A CG1 
366  C CG2 . ILE A 56  ? 0.3354 0.3390 0.3201 -0.0490 -0.0037 -0.0061 73  ILE A CG2 
367  C CD1 . ILE A 56  ? 0.3359 0.3605 0.3326 -0.0530 -0.0069 0.0022  73  ILE A CD1 
368  N N   . THR A 57  ? 0.4195 0.4117 0.4020 -0.0629 -0.0067 -0.0216 74  THR A N   
369  C CA  . THR A 57  ? 0.4046 0.3873 0.3801 -0.0629 -0.0060 -0.0294 74  THR A CA  
370  C C   . THR A 57  ? 0.3905 0.3765 0.3558 -0.0565 -0.0046 -0.0304 74  THR A C   
371  O O   . THR A 57  ? 0.3913 0.3679 0.3501 -0.0545 -0.0018 -0.0359 74  THR A O   
372  C CB  . THR A 57  ? 0.4298 0.4140 0.4053 -0.0703 -0.0106 -0.0374 74  THR A CB  
373  O OG1 . THR A 57  ? 0.4032 0.4032 0.3767 -0.0706 -0.0156 -0.0375 74  THR A OG1 
374  C CG2 . THR A 57  ? 0.4927 0.4719 0.4797 -0.0778 -0.0106 -0.0366 74  THR A CG2 
375  N N   . ASP A 58  ? 0.3859 0.3841 0.3493 -0.0530 -0.0060 -0.0254 75  ASP A N   
376  C CA  . ASP A 58  ? 0.4070 0.4079 0.3602 -0.0470 -0.0040 -0.0250 75  ASP A CA  
377  C C   . ASP A 58  ? 0.3855 0.3878 0.3439 -0.0412 -0.0002 -0.0168 75  ASP A C   
378  O O   . ASP A 58  ? 0.3925 0.4037 0.3562 -0.0405 -0.0026 -0.0111 75  ASP A O   
379  C CB  . ASP A 58  ? 0.4489 0.4620 0.3943 -0.0473 -0.0096 -0.0261 75  ASP A CB  
380  C CG  . ASP A 58  ? 0.5274 0.5403 0.4685 -0.0531 -0.0151 -0.0351 75  ASP A CG  
381  O OD1 . ASP A 58  ? 0.5141 0.5160 0.4568 -0.0567 -0.0136 -0.0410 75  ASP A OD1 
382  O OD2 . ASP A 58  ? 0.5219 0.5457 0.4591 -0.0539 -0.0215 -0.0364 75  ASP A OD2 
383  N N   . LEU A 59  ? 0.3288 0.3227 0.2871 -0.0370 0.0055  -0.0168 76  LEU A N   
384  C CA  . LEU A 59  ? 0.3095 0.3043 0.2745 -0.0317 0.0088  -0.0102 76  LEU A CA  
385  C C   . LEU A 59  ? 0.3311 0.3304 0.2881 -0.0273 0.0120  -0.0082 76  LEU A C   
386  O O   . LEU A 59  ? 0.3607 0.3562 0.3073 -0.0265 0.0154  -0.0128 76  LEU A O   
387  C CB  . LEU A 59  ? 0.3146 0.2983 0.2874 -0.0295 0.0130  -0.0112 76  LEU A CB  
388  C CG  . LEU A 59  ? 0.3811 0.3559 0.3586 -0.0334 0.0109  -0.0138 76  LEU A CG  
389  C CD1 . LEU A 59  ? 0.3606 0.3245 0.3454 -0.0296 0.0147  -0.0148 76  LEU A CD1 
390  C CD2 . LEU A 59  ? 0.3352 0.3144 0.3181 -0.0356 0.0066  -0.0086 76  LEU A CD2 
391  N N   . ILE A 60  ? 0.3551 0.3615 0.3165 -0.0243 0.0115  -0.0014 77  ILE A N   
392  C CA  . ILE A 60  ? 0.3244 0.3345 0.2795 -0.0200 0.0148  0.0026  77  ILE A CA  
393  C C   . ILE A 60  ? 0.3300 0.3384 0.2979 -0.0161 0.0189  0.0080  77  ILE A C   
394  O O   . ILE A 60  ? 0.2930 0.3049 0.2706 -0.0156 0.0153  0.0119  77  ILE A O   
395  C CB  . ILE A 60  ? 0.3496 0.3701 0.2985 -0.0201 0.0090  0.0057  77  ILE A CB  
396  C CG1 . ILE A 60  ? 0.3363 0.3591 0.2748 -0.0242 0.0039  -0.0006 77  ILE A CG1 
397  C CG2 . ILE A 60  ? 0.2917 0.3144 0.2336 -0.0152 0.0126  0.0113  77  ILE A CG2 
398  C CD1 . ILE A 60  ? 0.3643 0.3987 0.3017 -0.0251 -0.0036 0.0015  77  ILE A CD1 
399  N N   . PHE A 61  ? 0.3060 0.3091 0.2748 -0.0133 0.0263  0.0076  78  PHE A N   
400  C CA  . PHE A 61  ? 0.2662 0.2677 0.2496 -0.0098 0.0306  0.0117  78  PHE A CA  
401  C C   . PHE A 61  ? 0.2994 0.3045 0.2791 -0.0068 0.0351  0.0176  78  PHE A C   
402  O O   . PHE A 61  ? 0.3107 0.3142 0.2778 -0.0058 0.0410  0.0170  78  PHE A O   
403  C CB  . PHE A 61  ? 0.2926 0.2863 0.2826 -0.0087 0.0370  0.0074  78  PHE A CB  
404  C CG  . PHE A 61  ? 0.2633 0.2514 0.2582 -0.0109 0.0329  0.0025  78  PHE A CG  
405  C CD1 . PHE A 61  ? 0.3211 0.3085 0.3288 -0.0105 0.0276  0.0047  78  PHE A CD1 
406  C CD2 . PHE A 61  ? 0.2979 0.2801 0.2840 -0.0130 0.0342  -0.0042 78  PHE A CD2 
407  C CE1 . PHE A 61  ? 0.2804 0.2611 0.2910 -0.0121 0.0241  0.0013  78  PHE A CE1 
408  C CE2 . PHE A 61  ? 0.3303 0.3056 0.3214 -0.0150 0.0306  -0.0080 78  PHE A CE2 
409  C CZ  . PHE A 61  ? 0.3005 0.2750 0.3034 -0.0145 0.0258  -0.0046 78  PHE A CZ  
410  N N   . VAL A 62  ? 0.2878 0.2966 0.2779 -0.0051 0.0329  0.0233  79  VAL A N   
411  C CA  . VAL A 62  ? 0.2765 0.2873 0.2661 -0.0023 0.0373  0.0299  79  VAL A CA  
412  C C   . VAL A 62  ? 0.3144 0.3216 0.3218 -0.0003 0.0440  0.0316  79  VAL A C   
413  O O   . VAL A 62  ? 0.2646 0.2720 0.2888 0.0001  0.0401  0.0318  79  VAL A O   
414  C CB  . VAL A 62  ? 0.2895 0.3064 0.2794 -0.0015 0.0304  0.0347  79  VAL A CB  
415  C CG1 . VAL A 62  ? 0.2489 0.2661 0.2397 0.0016  0.0349  0.0422  79  VAL A CG1 
416  C CG2 . VAL A 62  ? 0.3293 0.3511 0.3039 -0.0036 0.0239  0.0324  79  VAL A CG2 
417  N N   . THR A 63  ? 0.2913 0.2955 0.2954 0.0010  0.0541  0.0325  80  THR A N   
418  C CA  . THR A 63  ? 0.3221 0.3235 0.3448 0.0024  0.0620  0.0327  80  THR A CA  
419  C C   . THR A 63  ? 0.3129 0.3152 0.3430 0.0042  0.0685  0.0406  80  THR A C   
420  O O   . THR A 63  ? 0.3315 0.3349 0.3481 0.0049  0.0687  0.0462  80  THR A O   
421  C CB  . THR A 63  ? 0.3124 0.3096 0.3289 0.0027  0.0708  0.0277  80  THR A CB  
422  O OG1 . THR A 63  ? 0.3716 0.3680 0.3677 0.0038  0.0779  0.0306  80  THR A OG1 
423  C CG2 . THR A 63  ? 0.3068 0.3017 0.3156 0.0008  0.0645  0.0202  80  THR A CG2 
424  N N   . GLY A 64  ? 0.3600 0.3614 0.4130 0.0049  0.0736  0.0411  81  GLY A N   
425  C CA  . GLY A 64  ? 0.3467 0.3479 0.4109 0.0059  0.0815  0.0483  81  GLY A CA  
426  C C   . GLY A 64  ? 0.3909 0.3907 0.4702 0.0065  0.0936  0.0469  81  GLY A C   
427  O O   . GLY A 64  ? 0.3902 0.3880 0.4575 0.0069  0.1004  0.0432  81  GLY A O   
428  N N   . ARG A 65  ? 0.4359 0.4368 0.5427 0.0065  0.0964  0.0489  82  ARG A N   
429  C CA  . ARG A 65  ? 0.6138 0.6148 0.7373 0.0071  0.1079  0.0465  82  ARG A CA  
430  C C   . ARG A 65  ? 0.4408 0.4421 0.5744 0.0076  0.1010  0.0373  82  ARG A C   
431  O O   . ARG A 65  ? 0.5629 0.5643 0.6949 0.0073  0.0876  0.0339  82  ARG A O   
432  C CB  . ARG A 65  ? 0.7703 0.7729 0.9227 0.0066  0.1148  0.0515  82  ARG A CB  
433  C CG  . ARG A 65  ? 0.7294 0.7339 0.9041 0.0059  0.1028  0.0513  82  ARG A CG  
434  C CD  . ARG A 65  ? 0.8223 0.8280 1.0272 0.0048  0.1113  0.0561  82  ARG A CD  
435  N NE  . ARG A 65  ? 0.8203 0.8283 1.0440 0.0049  0.1238  0.0537  82  ARG A NE  
436  C CZ  . ARG A 65  ? 0.6156 0.6273 0.8660 0.0056  0.1199  0.0466  82  ARG A CZ  
437  N NH1 . ARG A 65  ? 0.6060 0.6187 0.8683 0.0062  0.1037  0.0414  82  ARG A NH1 
438  N NH2 . ARG A 65  ? 0.6152 0.6294 0.8796 0.0064  0.1325  0.0444  82  ARG A NH2 
439  N N   . ASN A 66  ? 0.5738 0.5749 0.7159 0.0088  0.1111  0.0336  83  ASN A N   
440  C CA  . ASN A 66  ? 0.5100 0.5100 0.6597 0.0101  0.1060  0.0252  83  ASN A CA  
441  C C   . ASN A 66  ? 0.3979 0.3940 0.5197 0.0094  0.0983  0.0211  83  ASN A C   
442  O O   . ASN A 66  ? 0.4599 0.4541 0.5847 0.0097  0.0886  0.0158  83  ASN A O   
443  C CB  . ASN A 66  ? 0.5142 0.5166 0.6918 0.0106  0.0949  0.0229  83  ASN A CB  
444  C CG  . ASN A 66  ? 0.4826 0.4894 0.6922 0.0109  0.1022  0.0254  83  ASN A CG  
445  O OD1 . ASN A 66  ? 0.5202 0.5286 0.7414 0.0118  0.1154  0.0246  83  ASN A OD1 
446  N ND2 . ASN A 66  ? 0.4120 0.4207 0.6363 0.0100  0.0944  0.0283  83  ASN A ND2 
447  N N   . LYS A 67  ? 0.3124 0.3070 0.4069 0.0086  0.1026  0.0237  84  LYS A N   
448  C CA  . LYS A 67  ? 0.3175 0.3089 0.3869 0.0076  0.0961  0.0191  84  LYS A CA  
449  C C   . LYS A 67  ? 0.3342 0.3214 0.4060 0.0087  0.0980  0.0106  84  LYS A C   
450  O O   . LYS A 67  ? 0.3522 0.3360 0.4137 0.0074  0.0894  0.0057  84  LYS A O   
451  C CB  . LYS A 67  ? 0.4235 0.4140 0.4651 0.0073  0.1017  0.0226  84  LYS A CB  
452  C CG  . LYS A 67  ? 0.3414 0.3295 0.3779 0.0096  0.1178  0.0220  84  LYS A CG  
453  C CD  . LYS A 67  ? 0.5284 0.5159 0.5425 0.0103  0.1253  0.0294  84  LYS A CD  
454  C CE  . LYS A 67  ? 0.4822 0.4656 0.4819 0.0129  0.1407  0.0270  84  LYS A CE  
455  N NZ  . LYS A 67  ? 0.6059 0.5881 0.5932 0.0147  0.1539  0.0361  84  LYS A NZ  
456  N N   . ARG A 68  ? 0.3016 0.2887 0.3886 0.0111  0.1095  0.0089  85  ARG A N   
457  C CA  . ARG A 68  ? 0.3686 0.3516 0.4602 0.0132  0.1128  0.0007  85  ARG A CA  
458  C C   . ARG A 68  ? 0.2990 0.2794 0.4019 0.0131  0.0997  -0.0036 85  ARG A C   
459  O O   . ARG A 68  ? 0.3238 0.2981 0.4174 0.0133  0.0968  -0.0100 85  ARG A O   
460  C CB  . ARG A 68  ? 0.4506 0.4364 0.5663 0.0162  0.1264  0.0005  85  ARG A CB  
461  C CG  . ARG A 68  ? 0.5191 0.5013 0.6462 0.0194  0.1298  -0.0083 85  ARG A CG  
462  C CD  . ARG A 68  ? 0.4869 0.4744 0.6495 0.0224  0.1380  -0.0087 85  ARG A CD  
463  N NE  . ARG A 68  ? 0.5812 0.5729 0.7679 0.0218  0.1260  -0.0061 85  ARG A NE  
464  C CZ  . ARG A 68  ? 0.5171 0.5060 0.7116 0.0227  0.1118  -0.0098 85  ARG A CZ  
465  N NH1 . ARG A 68  ? 0.5332 0.5148 0.7169 0.0242  0.1082  -0.0163 85  ARG A NH1 
466  N NH2 . ARG A 68  ? 0.5235 0.5159 0.7358 0.0223  0.1009  -0.0070 85  ARG A NH2 
467  N N   . ALA A 69  ? 0.2858 0.2698 0.4094 0.0133  0.0920  -0.0005 86  ALA A N   
468  C CA  . ALA A 69  ? 0.2572 0.2382 0.3914 0.0142  0.0796  -0.0039 86  ALA A CA  
469  C C   . ALA A 69  ? 0.2666 0.2427 0.3774 0.0114  0.0700  -0.0050 86  ALA A C   
470  O O   . ALA A 69  ? 0.3539 0.3234 0.4628 0.0119  0.0650  -0.0098 86  ALA A O   
471  C CB  . ALA A 69  ? 0.3453 0.3311 0.5023 0.0150  0.0724  -0.0002 86  ALA A CB  
472  N N   . ILE A 70  ? 0.2558 0.2348 0.3493 0.0084  0.0680  -0.0007 87  ILE A N   
473  C CA  . ILE A 70  ? 0.2564 0.2324 0.3293 0.0053  0.0599  -0.0018 87  ILE A CA  
474  C C   . ILE A 70  ? 0.2790 0.2496 0.3348 0.0043  0.0646  -0.0076 87  ILE A C   
475  O O   . ILE A 70  ? 0.2860 0.2504 0.3364 0.0029  0.0592  -0.0120 87  ILE A O   
476  C CB  . ILE A 70  ? 0.2964 0.2782 0.3574 0.0030  0.0569  0.0041  87  ILE A CB  
477  C CG1 . ILE A 70  ? 0.3379 0.3231 0.4141 0.0038  0.0494  0.0083  87  ILE A CG1 
478  C CG2 . ILE A 70  ? 0.2902 0.2705 0.3291 -0.0006 0.0511  0.0022  87  ILE A CG2 
479  C CD1 . ILE A 70  ? 0.3794 0.3613 0.4541 0.0031  0.0384  0.0067  87  ILE A CD1 
480  N N   . GLU A 71  ? 0.2900 0.2621 0.3362 0.0050  0.0750  -0.0078 88  GLU A N   
481  C CA  . GLU A 71  ? 0.3028 0.2693 0.3299 0.0043  0.0790  -0.0142 88  GLU A CA  
482  C C   . GLU A 71  ? 0.3039 0.2630 0.3411 0.0063  0.0807  -0.0214 88  GLU A C   
483  O O   . GLU A 71  ? 0.3178 0.2700 0.3440 0.0046  0.0768  -0.0273 88  GLU A O   
484  C CB  . GLU A 71  ? 0.3134 0.2819 0.3284 0.0060  0.0911  -0.0130 88  GLU A CB  
485  C CG  . GLU A 71  ? 0.3829 0.3571 0.3842 0.0045  0.0893  -0.0058 88  GLU A CG  
486  C CD  . GLU A 71  ? 0.3938 0.3685 0.3820 0.0069  0.1018  -0.0033 88  GLU A CD  
487  O OE1 . GLU A 71  ? 0.4380 0.4095 0.4301 0.0097  0.1131  -0.0070 88  GLU A OE1 
488  O OE2 . GLU A 71  ? 0.3986 0.3765 0.3726 0.0063  0.1007  0.0025  88  GLU A OE2 
489  N N   . ASP A 72  ? 0.3006 0.2608 0.3602 0.0102  0.0863  -0.0212 89  ASP A N   
490  C CA  . ASP A 72  ? 0.3097 0.2629 0.3799 0.0131  0.0880  -0.0282 89  ASP A CA  
491  C C   . ASP A 72  ? 0.3117 0.2595 0.3884 0.0122  0.0753  -0.0290 89  ASP A C   
492  O O   . ASP A 72  ? 0.3061 0.2449 0.3834 0.0134  0.0740  -0.0350 89  ASP A O   
493  C CB  . ASP A 72  ? 0.3774 0.3345 0.4728 0.0178  0.0972  -0.0281 89  ASP A CB  
494  C CG  . ASP A 72  ? 0.4501 0.4099 0.5380 0.0193  0.1127  -0.0286 89  ASP A CG  
495  O OD1 . ASP A 72  ? 0.3639 0.3209 0.4246 0.0173  0.1152  -0.0302 89  ASP A OD1 
496  O OD2 . ASP A 72  ? 0.3926 0.3576 0.5016 0.0223  0.1220  -0.0271 89  ASP A OD2 
497  N N   . HIS A 73  ? 0.2843 0.2360 0.3637 0.0102  0.0660  -0.0229 90  HIS A N   
498  C CA  . HIS A 73  ? 0.2793 0.2249 0.3614 0.0096  0.0548  -0.0230 90  HIS A CA  
499  C C   . HIS A 73  ? 0.3150 0.2539 0.3763 0.0051  0.0510  -0.0260 90  HIS A C   
500  O O   . HIS A 73  ? 0.3150 0.2443 0.3771 0.0051  0.0467  -0.0292 90  HIS A O   
501  C CB  . HIS A 73  ? 0.3086 0.2596 0.3976 0.0092  0.0462  -0.0164 90  HIS A CB  
502  C CG  . HIS A 73  ? 0.3482 0.2921 0.4400 0.0098  0.0357  -0.0160 90  HIS A CG  
503  N ND1 . HIS A 73  ? 0.3108 0.2496 0.4199 0.0146  0.0328  -0.0179 90  HIS A ND1 
504  C CD2 . HIS A 73  ? 0.3365 0.2763 0.4148 0.0063  0.0283  -0.0142 90  HIS A CD2 
505  C CE1 . HIS A 73  ? 0.3631 0.2941 0.4672 0.0144  0.0236  -0.0166 90  HIS A CE1 
506  N NE2 . HIS A 73  ? 0.3443 0.2758 0.4300 0.0092  0.0215  -0.0142 90  HIS A NE2 
507  N N   . PHE A 74  ? 0.2904 0.2340 0.3340 0.0012  0.0521  -0.0248 91  PHE A N   
508  C CA  . PHE A 74  ? 0.3060 0.2451 0.3326 -0.0038 0.0473  -0.0276 91  PHE A CA  
509  C C   . PHE A 74  ? 0.3714 0.3048 0.3852 -0.0045 0.0532  -0.0356 91  PHE A C   
510  O O   . PHE A 74  ? 0.3591 0.2851 0.3645 -0.0081 0.0490  -0.0401 91  PHE A O   
511  C CB  . PHE A 74  ? 0.3590 0.3069 0.3750 -0.0076 0.0428  -0.0224 91  PHE A CB  
512  C CG  . PHE A 74  ? 0.3496 0.3003 0.3743 -0.0078 0.0351  -0.0162 91  PHE A CG  
513  C CD1 . PHE A 74  ? 0.3611 0.3058 0.3844 -0.0104 0.0282  -0.0161 91  PHE A CD1 
514  C CD2 . PHE A 74  ? 0.3105 0.2688 0.3450 -0.0050 0.0353  -0.0106 91  PHE A CD2 
515  C CE1 . PHE A 74  ? 0.3589 0.3054 0.3879 -0.0099 0.0219  -0.0105 91  PHE A CE1 
516  C CE2 . PHE A 74  ? 0.3514 0.3114 0.3925 -0.0046 0.0280  -0.0060 91  PHE A CE2 
517  C CZ  . PHE A 74  ? 0.3427 0.2969 0.3800 -0.0068 0.0214  -0.0060 91  PHE A CZ  
518  N N   . ASP A 75  ? 0.3306 0.2666 0.3425 -0.0012 0.0630  -0.0377 92  ASP A N   
519  C CA  . ASP A 75  ? 0.3405 0.2699 0.3384 -0.0010 0.0688  -0.0463 92  ASP A CA  
520  C C   . ASP A 75  ? 0.4331 0.3515 0.4421 0.0017  0.0702  -0.0529 92  ASP A C   
521  O O   . ASP A 75  ? 0.4547 0.3726 0.4838 0.0056  0.0708  -0.0507 92  ASP A O   
522  C CB  . ASP A 75  ? 0.4023 0.3367 0.3936 0.0026  0.0804  -0.0464 92  ASP A CB  
523  C CG  . ASP A 75  ? 0.4833 0.4269 0.4608 0.0005  0.0794  -0.0399 92  ASP A CG  
524  O OD1 . ASP A 75  ? 0.4057 0.3513 0.3735 -0.0039 0.0699  -0.0385 92  ASP A OD1 
525  O OD2 . ASP A 75  ? 0.5243 0.4728 0.5012 0.0036  0.0885  -0.0361 92  ASP A OD2 
526  N N   . ALA A 76  ? 0.4056 0.3149 0.4019 0.0000  0.0703  -0.0614 93  ALA A N   
527  C CA  . ALA A 76  ? 0.4871 0.3842 0.4927 0.0028  0.0718  -0.0683 93  ALA A CA  
528  C C   . ALA A 76  ? 0.4347 0.3333 0.4541 0.0100  0.0827  -0.0701 93  ALA A C   
529  O O   . ALA A 76  ? 0.5183 0.4239 0.5320 0.0122  0.0920  -0.0697 93  ALA A O   
530  C CB  . ALA A 76  ? 0.5194 0.4063 0.5081 0.0000  0.0714  -0.0785 93  ALA A CB  
531  N N   . ALA A 77  ? 0.4845 0.3759 0.5224 0.0139  0.0819  -0.0721 94  ALA A N   
532  C CA  . ALA A 77  ? 0.5362 0.4290 0.5914 0.0211  0.0921  -0.0749 94  ALA A CA  
533  C C   . ALA A 77  ? 0.5946 0.4733 0.6508 0.0242  0.0943  -0.0850 94  ALA A C   
534  O O   . ALA A 77  ? 0.6290 0.4998 0.7007 0.0266  0.0885  -0.0853 94  ALA A O   
535  C CB  . ALA A 77  ? 0.5171 0.4161 0.5982 0.0243  0.0883  -0.0676 94  ALA A CB  
536  N N   . PRO A 78  ? 0.5936 0.4680 0.6326 0.0245  0.1021  -0.0936 95  PRO A N   
537  C CA  . PRO A 78  ? 0.6640 0.5236 0.7029 0.0272  0.1034  -0.1043 95  PRO A CA  
538  C C   . PRO A 78  ? 0.6942 0.5511 0.7597 0.0350  0.1078  -0.1060 95  PRO A C   
539  O O   . PRO A 78  ? 0.7642 0.6087 0.8387 0.0367  0.1020  -0.1094 95  PRO A O   
540  C CB  . PRO A 78  ? 0.7251 0.5837 0.7414 0.0279  0.1135  -0.1130 95  PRO A CB  
541  C CG  . PRO A 78  ? 0.7640 0.6342 0.7632 0.0234  0.1129  -0.1064 95  PRO A CG  
542  C CD  . PRO A 78  ? 0.6834 0.5652 0.7020 0.0235  0.1103  -0.0943 95  PRO A CD  
543  N N   . GLU A 79  ? 0.7229 0.5917 0.8031 0.0398  0.1175  -0.1031 96  GLU A N   
544  C CA  . GLU A 79  ? 0.7362 0.6046 0.8444 0.0478  0.1226  -0.1056 96  GLU A CA  
545  C C   . GLU A 79  ? 0.8204 0.6843 0.9480 0.0487  0.1092  -0.1005 96  GLU A C   
546  O O   . GLU A 79  ? 0.8037 0.6573 0.9451 0.0539  0.1073  -0.1054 96  GLU A O   
547  C CB  . GLU A 79  ? 0.8160 0.7001 0.9391 0.0512  0.1343  -0.1015 96  GLU A CB  
548  C CG  . GLU A 79  ? 0.9893 0.8773 1.1477 0.0588  0.1377  -0.1021 96  GLU A CG  
549  C CD  . GLU A 79  ? 1.1490 1.0535 1.3243 0.0609  0.1494  -0.0974 96  GLU A CD  
550  O OE1 . GLU A 79  ? 1.1594 1.0701 1.3159 0.0573  0.1575  -0.0946 96  GLU A OE1 
551  O OE2 . GLU A 79  ? 1.1978 1.1088 1.4058 0.0661  0.1505  -0.0965 96  GLU A OE2 
552  N N   . LEU A 80  ? 0.7555 0.6264 0.8832 0.0442  0.0996  -0.0906 97  LEU A N   
553  C CA  . LEU A 80  ? 0.6926 0.5592 0.8351 0.0454  0.0866  -0.0851 97  LEU A CA  
554  C C   . LEU A 80  ? 0.6939 0.5427 0.8250 0.0432  0.0783  -0.0881 97  LEU A C   
555  O O   . LEU A 80  ? 0.8076 0.6469 0.9528 0.0476  0.0716  -0.0878 97  LEU A O   
556  C CB  . LEU A 80  ? 0.6631 0.5400 0.8037 0.0408  0.0788  -0.0747 97  LEU A CB  
557  C CG  . LEU A 80  ? 0.6356 0.5092 0.7891 0.0424  0.0652  -0.0683 97  LEU A CG  
558  C CD1 . LEU A 80  ? 0.6679 0.5466 0.8521 0.0506  0.0654  -0.0685 97  LEU A CD1 
559  C CD2 . LEU A 80  ? 0.6031 0.4851 0.7472 0.0368  0.0582  -0.0595 97  LEU A CD2 
560  N N   . GLU A 81  ? 0.6714 0.5154 0.7777 0.0362  0.0780  -0.0907 98  GLU A N   
561  C CA  . GLU A 81  ? 0.8099 0.6368 0.9064 0.0329  0.0706  -0.0935 98  GLU A CA  
562  C C   . GLU A 81  ? 0.8629 0.6759 0.9672 0.0390  0.0753  -0.1036 98  GLU A C   
563  O O   . GLU A 81  ? 0.8704 0.6688 0.9814 0.0407  0.0683  -0.1034 98  GLU A O   
564  C CB  . GLU A 81  ? 0.7464 0.5728 0.8172 0.0240  0.0695  -0.0954 98  GLU A CB  
565  C CG  . GLU A 81  ? 0.7086 0.5473 0.7718 0.0180  0.0637  -0.0855 98  GLU A CG  
566  C CD  . GLU A 81  ? 0.7884 0.6263 0.8289 0.0093  0.0608  -0.0874 98  GLU A CD  
567  O OE1 . GLU A 81  ? 0.8893 0.7141 0.9217 0.0064  0.0594  -0.0948 98  GLU A OE1 
568  O OE2 . GLU A 81  ? 0.6546 0.5052 0.6865 0.0054  0.0597  -0.0820 98  GLU A OE2 
569  N N   . THR A 82  ? 1.0226 0.8390 1.1253 0.0427  0.0876  -0.1122 99  THR A N   
570  C CA  . THR A 82  ? 0.9803 0.7837 1.0908 0.0493  0.0930  -0.1227 99  THR A CA  
571  C C   . THR A 82  ? 1.0275 0.8301 1.1676 0.0580  0.0909  -0.1201 99  THR A C   
572  O O   . THR A 82  ? 1.1324 0.9193 1.2806 0.0620  0.0868  -0.1239 99  THR A O   
573  C CB  . THR A 82  ? 1.0600 0.8684 1.1617 0.0522  0.1078  -0.1323 99  THR A CB  
574  O OG1 . THR A 82  ? 1.0694 0.8954 1.1850 0.0563  0.1165  -0.1278 99  THR A OG1 
575  C CG2 . THR A 82  ? 0.9436 0.7516 1.0143 0.0443  0.1082  -0.1358 99  THR A CG2 
576  N N   . ASP A 83  ? 0.9022 0.7211 1.0594 0.0611  0.0927  -0.1135 100 ASP A N   
577  C CA  . ASP A 83  ? 0.9679 0.7873 1.1548 0.0695  0.0887  -0.1112 100 ASP A CA  
578  C C   . ASP A 83  ? 1.0792 0.8862 1.2669 0.0685  0.0729  -0.1044 100 ASP A C   
579  O O   . ASP A 83  ? 1.1521 0.9476 1.3551 0.0754  0.0683  -0.1062 100 ASP A O   
580  C CB  . ASP A 83  ? 0.9883 0.8282 1.1938 0.0716  0.0921  -0.1053 100 ASP A CB  
581  C CG  . ASP A 83  ? 1.0704 0.9122 1.3066 0.0792  0.0837  -0.1015 100 ASP A CG  
582  O OD1 . ASP A 83  ? 0.9654 0.8021 1.2002 0.0777  0.0694  -0.0940 100 ASP A OD1 
583  O OD2 . ASP A 83  ? 1.0083 0.8570 1.2701 0.0869  0.0914  -0.1061 100 ASP A OD2 
584  N N   . LEU A 84  ? 0.9673 0.7761 1.1385 0.0605  0.0649  -0.0962 101 LEU A N   
585  C CA  . LEU A 84  ? 0.9456 0.7424 1.1146 0.0593  0.0511  -0.0888 101 LEU A CA  
586  C C   . LEU A 84  ? 1.0357 0.8107 1.1943 0.0579  0.0491  -0.0938 101 LEU A C   
587  O O   . LEU A 84  ? 1.0164 0.7770 1.1807 0.0611  0.0403  -0.0901 101 LEU A O   
588  C CB  . LEU A 84  ? 0.8786 0.6827 1.0312 0.0508  0.0450  -0.0798 101 LEU A CB  
589  C CG  . LEU A 84  ? 0.8037 0.6267 0.9660 0.0516  0.0436  -0.0730 101 LEU A CG  
590  C CD1 . LEU A 84  ? 0.7395 0.5668 0.8826 0.0430  0.0379  -0.0653 101 LEU A CD1 
591  C CD2 . LEU A 84  ? 0.8426 0.6655 1.0280 0.0600  0.0355  -0.0692 101 LEU A CD2 
592  N N   . GLU A 85  ? 1.0605 0.8320 1.2026 0.0528  0.0566  -0.1020 102 GLU A N   
593  C CA  . GLU A 85  ? 1.1289 0.8791 1.2631 0.0514  0.0555  -0.1087 102 GLU A CA  
594  C C   . GLU A 85  ? 1.1480 0.8876 1.3026 0.0621  0.0574  -0.1146 102 GLU A C   
595  O O   . GLU A 85  ? 1.1049 0.8264 1.2641 0.0646  0.0499  -0.1125 102 GLU A O   
596  C CB  . GLU A 85  ? 1.1722 0.9228 1.2868 0.0453  0.0634  -0.1184 102 GLU A CB  
597  C CG  . GLU A 85  ? 1.3218 1.0507 1.4272 0.0425  0.0622  -0.1270 102 GLU A CG  
598  C CD  . GLU A 85  ? 1.3572 1.0732 1.4558 0.0352  0.0514  -0.1192 102 GLU A CD  
599  O OE1 . GLU A 85  ? 1.3452 1.0708 1.4415 0.0313  0.0456  -0.1078 102 GLU A OE1 
600  O OE2 . GLU A 85  ? 1.3488 1.0447 1.4444 0.0332  0.0492  -0.1244 102 GLU A OE2 
601  N N   . ALA A 86  ? 1.1669 0.9177 1.3350 0.0691  0.0675  -0.1211 103 ALA A N   
602  C CA  . ALA A 86  ? 1.2000 0.9432 1.3907 0.0802  0.0701  -0.1271 103 ALA A CA  
603  C C   . ALA A 86  ? 1.1869 0.9254 1.3940 0.0856  0.0574  -0.1175 103 ALA A C   
604  O O   . ALA A 86  ? 1.2700 0.9937 1.4774 0.0889  0.0509  -0.1166 103 ALA A O   
605  C CB  . ALA A 86  ? 1.1647 0.9259 1.3705 0.0865  0.0832  -0.1328 103 ALA A CB  
606  N N   . LYS A 87  ? 1.1405 0.8935 1.3557 0.0855  0.0521  -0.1084 104 LYS A N   
607  C CA  . LYS A 87  ? 1.1902 0.9418 1.4165 0.0904  0.0386  -0.0984 104 LYS A CA  
608  C C   . LYS A 87  ? 1.1472 0.8785 1.3565 0.0860  0.0278  -0.0915 104 LYS A C   
609  O O   . LYS A 87  ? 1.1314 0.8591 1.3437 0.0897  0.0162  -0.0822 104 LYS A O   
610  C CB  . LYS A 87  ? 1.1997 0.9700 1.4363 0.0904  0.0353  -0.0914 104 LYS A CB  
611  C CG  . LYS A 87  ? 1.1486 0.9403 1.4038 0.0938  0.0462  -0.0962 104 LYS A CG  
612  C CD  . LYS A 87  ? 1.0484 0.8519 1.3283 0.1019  0.0400  -0.0930 104 LYS A CD  
613  C CE  . LYS A 87  ? 1.0974 0.9241 1.3954 0.1023  0.0471  -0.0932 104 LYS A CE  
614  N NZ  . LYS A 87  ? 1.2546 1.0866 1.5483 0.0997  0.0653  -0.1015 104 LYS A NZ  
615  N N   . GLY A 88  ? 0.9940 0.7134 1.1838 0.0775  0.0313  -0.0950 105 GLY A N   
616  C CA  . GLY A 88  ? 1.0165 0.7176 1.1908 0.0720  0.0224  -0.0877 105 GLY A CA  
617  C C   . GLY A 88  ? 1.1048 0.8128 1.2726 0.0690  0.0130  -0.0746 105 GLY A C   
618  O O   . GLY A 88  ? 1.0873 0.7798 1.2495 0.0693  0.0039  -0.0664 105 GLY A O   
619  N N   . LYS A 89  ? 1.2291 0.9592 1.3966 0.0664  0.0152  -0.0724 106 LYS A N   
620  C CA  . LYS A 89  ? 1.1979 0.9354 1.3588 0.0637  0.0067  -0.0611 106 LYS A CA  
621  C C   . LYS A 89  ? 1.1221 0.8614 1.2595 0.0514  0.0085  -0.0581 106 LYS A C   
622  O O   . LYS A 89  ? 1.1238 0.8805 1.2552 0.0464  0.0115  -0.0569 106 LYS A O   
623  C CB  . LYS A 89  ? 1.1484 0.9080 1.3254 0.0684  0.0071  -0.0604 106 LYS A CB  
624  C CG  . LYS A 89  ? 1.1797 0.9402 1.3844 0.0804  0.0063  -0.0649 106 LYS A CG  
625  C CD  . LYS A 89  ? 1.4321 1.1806 1.6427 0.0880  -0.0075 -0.0576 106 LYS A CD  
626  C CE  . LYS A 89  ? 1.4499 1.2055 1.6553 0.0870  -0.0179 -0.0477 106 LYS A CE  
627  N NZ  . LYS A 89  ? 1.5273 1.2761 1.7336 0.0944  -0.0309 -0.0405 106 LYS A NZ  
628  N N   . HIS A 90  ? 1.0897 0.8097 1.2149 0.0467  0.0065  -0.0569 107 HIS A N   
629  C CA  . HIS A 90  ? 1.0806 0.8008 1.1869 0.0348  0.0095  -0.0569 107 HIS A CA  
630  C C   . HIS A 90  ? 1.0349 0.7650 1.1299 0.0293  0.0048  -0.0464 107 HIS A C   
631  O O   . HIS A 90  ? 0.9490 0.6899 1.0327 0.0207  0.0083  -0.0472 107 HIS A O   
632  C CB  . HIS A 90  ? 1.1317 0.8278 1.2314 0.0311  0.0087  -0.0584 107 HIS A CB  
633  C CG  . HIS A 90  ? 1.1979 0.8850 1.3047 0.0342  0.0149  -0.0711 107 HIS A CG  
634  N ND1 . HIS A 90  ? 1.2599 0.9347 1.3820 0.0446  0.0138  -0.0742 107 HIS A ND1 
635  C CD2 . HIS A 90  ? 1.2472 0.9354 1.3473 0.0287  0.0221  -0.0821 107 HIS A CD2 
636  C CE1 . HIS A 90  ? 1.2530 0.9217 1.3776 0.0454  0.0208  -0.0867 107 HIS A CE1 
637  N NE2 . HIS A 90  ? 1.3211 0.9975 1.4316 0.0358  0.0258  -0.0918 107 HIS A NE2 
638  N N   . GLU A 91  ? 1.0002 0.7267 1.0975 0.0344  -0.0034 -0.0369 108 GLU A N   
639  C CA  . GLU A 91  ? 1.0043 0.7410 1.0908 0.0302  -0.0075 -0.0277 108 GLU A CA  
640  C C   . GLU A 91  ? 0.9077 0.6685 0.9995 0.0305  -0.0046 -0.0300 108 GLU A C   
641  O O   . GLU A 91  ? 0.7838 0.5563 0.8649 0.0240  -0.0039 -0.0265 108 GLU A O   
642  C CB  . GLU A 91  ? 1.0462 0.7725 1.1321 0.0368  -0.0173 -0.0177 108 GLU A CB  
643  C CG  . GLU A 91  ? 1.2170 0.9174 1.2995 0.0384  -0.0200 -0.0148 108 GLU A CG  
644  C CD  . GLU A 91  ? 1.4222 1.1114 1.5016 0.0461  -0.0302 -0.0043 108 GLU A CD  
645  O OE1 . GLU A 91  ? 1.3983 1.1003 1.4801 0.0510  -0.0358 -0.0009 108 GLU A OE1 
646  O OE2 . GLU A 91  ? 1.4135 1.0801 1.4873 0.0474  -0.0328 0.0004  108 GLU A OE2 
647  N N   . LEU A 92  ? 0.8894 0.6577 0.9987 0.0383  -0.0028 -0.0355 109 LEU A N   
648  C CA  . LEU A 92  ? 0.8594 0.6493 0.9752 0.0382  0.0017  -0.0379 109 LEU A CA  
649  C C   . LEU A 92  ? 0.8342 0.6315 0.9400 0.0305  0.0113  -0.0443 109 LEU A C   
650  O O   . LEU A 92  ? 0.7396 0.5516 0.8384 0.0257  0.0132  -0.0422 109 LEU A O   
651  C CB  . LEU A 92  ? 0.8715 0.6671 1.0108 0.0479  0.0029  -0.0426 109 LEU A CB  
652  C CG  . LEU A 92  ? 0.8462 0.6405 0.9987 0.0565  -0.0079 -0.0371 109 LEU A CG  
653  C CD1 . LEU A 92  ? 0.8618 0.6633 1.0409 0.0653  -0.0054 -0.0433 109 LEU A CD1 
654  C CD2 . LEU A 92  ? 0.6867 0.4932 0.8336 0.0542  -0.0134 -0.0301 109 LEU A CD2 
655  N N   . LEU A 93  ? 0.8847 0.6714 0.9889 0.0296  0.0167  -0.0523 110 LEU A N   
656  C CA  . LEU A 93  ? 0.7823 0.5749 0.8753 0.0231  0.0248  -0.0593 110 LEU A CA  
657  C C   . LEU A 93  ? 0.7788 0.5752 0.8543 0.0132  0.0221  -0.0544 110 LEU A C   
658  O O   . LEU A 93  ? 0.7499 0.5606 0.8179 0.0090  0.0258  -0.0553 110 LEU A O   
659  C CB  . LEU A 93  ? 0.8764 0.6535 0.9686 0.0235  0.0291  -0.0689 110 LEU A CB  
660  C CG  . LEU A 93  ? 0.9238 0.7042 1.0032 0.0178  0.0367  -0.0783 110 LEU A CG  
661  C CD1 . LEU A 93  ? 0.8397 0.6377 0.9217 0.0210  0.0451  -0.0821 110 LEU A CD1 
662  C CD2 . LEU A 93  ? 1.0399 0.8018 1.1191 0.0188  0.0391  -0.0880 110 LEU A CD2 
663  N N   . ALA A 94  ? 0.6655 0.4490 0.7349 0.0098  0.0160  -0.0486 111 ALA A N   
664  C CA  . ALA A 94  ? 0.6617 0.4487 0.7169 0.0004  0.0140  -0.0437 111 ALA A CA  
665  C C   . ALA A 94  ? 0.6990 0.5036 0.7528 0.0004  0.0118  -0.0367 111 ALA A C   
666  O O   . ALA A 94  ? 0.6466 0.4620 0.6907 -0.0063 0.0128  -0.0355 111 ALA A O   
667  C CB  . ALA A 94  ? 0.6472 0.4164 0.6981 -0.0025 0.0090  -0.0377 111 ALA A CB  
668  N N   . LEU A 95  ? 0.7259 0.5328 0.7898 0.0082  0.0079  -0.0321 112 LEU A N   
669  C CA  . LEU A 95  ? 0.7335 0.5563 0.7981 0.0092  0.0054  -0.0264 112 LEU A CA  
670  C C   . LEU A 95  ? 0.6411 0.4806 0.7071 0.0078  0.0122  -0.0312 112 LEU A C   
671  O O   . LEU A 95  ? 0.6365 0.4879 0.6944 0.0031  0.0125  -0.0284 112 LEU A O   
672  C CB  . LEU A 95  ? 0.7818 0.6025 0.8595 0.0184  -0.0006 -0.0228 112 LEU A CB  
673  C CG  . LEU A 95  ? 0.7642 0.5976 0.8445 0.0209  -0.0056 -0.0170 112 LEU A CG  
674  C CD1 . LEU A 95  ? 0.8469 0.6768 0.9116 0.0166  -0.0105 -0.0092 112 LEU A CD1 
675  C CD2 . LEU A 95  ? 0.7836 0.6150 0.8808 0.0308  -0.0117 -0.0164 112 LEU A CD2 
676  N N   . VAL A 96  ? 0.5949 0.4350 0.6707 0.0122  0.0181  -0.0384 113 VAL A N   
677  C CA  . VAL A 96  ? 0.5866 0.4410 0.6619 0.0113  0.0258  -0.0424 113 VAL A CA  
678  C C   . VAL A 96  ? 0.6256 0.4823 0.6829 0.0031  0.0285  -0.0451 113 VAL A C   
679  O O   . VAL A 96  ? 0.5687 0.4387 0.6197 0.0004  0.0308  -0.0435 113 VAL A O   
680  C CB  . VAL A 96  ? 0.6349 0.4878 0.7228 0.0176  0.0331  -0.0500 113 VAL A CB  
681  C CG1 . VAL A 96  ? 0.6306 0.4956 0.7130 0.0160  0.0427  -0.0542 113 VAL A CG1 
682  C CG2 . VAL A 96  ? 0.6078 0.4632 0.7169 0.0257  0.0302  -0.0474 113 VAL A CG2 
683  N N   . ARG A 97  ? 0.6494 0.4930 0.6988 -0.0010 0.0275  -0.0490 114 ARG A N   
684  C CA  . ARG A 97  ? 0.6014 0.4473 0.6357 -0.0087 0.0292  -0.0531 114 ARG A CA  
685  C C   . ARG A 97  ? 0.6393 0.4930 0.6656 -0.0151 0.0241  -0.0459 114 ARG A C   
686  O O   . ARG A 97  ? 0.6468 0.5097 0.6630 -0.0201 0.0252  -0.0478 114 ARG A O   
687  C CB  . ARG A 97  ? 0.6419 0.4711 0.6725 -0.0117 0.0292  -0.0602 114 ARG A CB  
688  C CG  . ARG A 97  ? 0.7014 0.5244 0.7367 -0.0059 0.0357  -0.0698 114 ARG A CG  
689  C CD  . ARG A 97  ? 0.7224 0.5271 0.7547 -0.0084 0.0354  -0.0777 114 ARG A CD  
690  N NE  . ARG A 97  ? 0.8213 0.6224 0.8549 -0.0031 0.0428  -0.0884 114 ARG A NE  
691  C CZ  . ARG A 97  ? 0.9553 0.7396 0.9911 -0.0016 0.0440  -0.0966 114 ARG A CZ  
692  N NH1 . ARG A 97  ? 0.9359 0.7046 0.9723 -0.0058 0.0382  -0.0955 114 ARG A NH1 
693  N NH2 . ARG A 97  ? 0.8771 0.6597 0.9150 0.0047  0.0517  -0.1060 114 ARG A NH2 
694  N N   . ASP A 98  ? 0.6144 0.4653 0.6449 -0.0142 0.0187  -0.0376 115 ASP A N   
695  C CA  . ASP A 98  ? 0.5848 0.4429 0.6086 -0.0193 0.0147  -0.0305 115 ASP A CA  
696  C C   . ASP A 98  ? 0.5550 0.4305 0.5790 -0.0176 0.0150  -0.0267 115 ASP A C   
697  O O   . ASP A 98  ? 0.5475 0.4309 0.5657 -0.0216 0.0123  -0.0217 115 ASP A O   
698  C CB  . ASP A 98  ? 0.7633 0.6109 0.7894 -0.0178 0.0094  -0.0229 115 ASP A CB  
699  C CG  . ASP A 98  ? 0.9109 0.7628 0.9287 -0.0240 0.0068  -0.0163 115 ASP A CG  
700  O OD1 . ASP A 98  ? 0.9050 0.7572 0.9170 -0.0318 0.0081  -0.0189 115 ASP A OD1 
701  O OD2 . ASP A 98  ? 0.8832 0.7388 0.9011 -0.0209 0.0033  -0.0091 115 ASP A OD2 
702  N N   . ILE A 99  ? 0.5057 0.3873 0.5373 -0.0117 0.0185  -0.0287 116 ILE A N   
703  C CA  . ILE A 99  ? 0.5121 0.4089 0.5448 -0.0105 0.0191  -0.0247 116 ILE A CA  
704  C C   . ILE A 99  ? 0.5322 0.4384 0.5523 -0.0164 0.0206  -0.0258 116 ILE A C   
705  O O   . ILE A 99  ? 0.4505 0.3673 0.4680 -0.0177 0.0184  -0.0207 116 ILE A O   
706  C CB  . ILE A 99  ? 0.5383 0.4394 0.5827 -0.0040 0.0242  -0.0271 116 ILE A CB  
707  C CG1 . ILE A 99  ? 0.4836 0.3776 0.5425 0.0021  0.0203  -0.0252 116 ILE A CG1 
708  C CG2 . ILE A 99  ? 0.4478 0.3636 0.4931 -0.0035 0.0261  -0.0234 116 ILE A CG2 
709  C CD1 . ILE A 99  ? 0.4783 0.3759 0.5527 0.0083  0.0252  -0.0282 116 ILE A CD1 
710  N N   . LEU A 100 ? 0.5059 0.4082 0.5183 -0.0195 0.0238  -0.0330 117 LEU A N   
711  C CA  . LEU A 100 ? 0.5278 0.4374 0.5276 -0.0252 0.0236  -0.0353 117 LEU A CA  
712  C C   . LEU A 100 ? 0.5993 0.4979 0.5944 -0.0308 0.0216  -0.0409 117 LEU A C   
713  O O   . LEU A 100 ? 0.5505 0.4411 0.5429 -0.0302 0.0248  -0.0490 117 LEU A O   
714  C CB  . LEU A 100 ? 0.5835 0.4998 0.5769 -0.0228 0.0295  -0.0395 117 LEU A CB  
715  C CG  . LEU A 100 ? 0.6511 0.5763 0.6307 -0.0276 0.0274  -0.0408 117 LEU A CG  
716  C CD1 . LEU A 100 ? 0.5411 0.4784 0.5225 -0.0281 0.0240  -0.0323 117 LEU A CD1 
717  C CD2 . LEU A 100 ? 0.6132 0.5408 0.5810 -0.0255 0.0331  -0.0467 117 LEU A CD2 
718  N N   . PRO A 101 ? 0.5016 0.3988 0.4965 -0.0362 0.0168  -0.0370 118 PRO A N   
719  C CA  . PRO A 101 ? 0.4768 0.3633 0.4694 -0.0426 0.0151  -0.0419 118 PRO A CA  
720  C C   . PRO A 101 ? 0.5015 0.3914 0.4849 -0.0468 0.0153  -0.0509 118 PRO A C   
721  O O   . PRO A 101 ? 0.4629 0.3657 0.4394 -0.0463 0.0154  -0.0514 118 PRO A O   
722  C CB  . PRO A 101 ? 0.5137 0.4031 0.5080 -0.0478 0.0112  -0.0345 118 PRO A CB  
723  C CG  . PRO A 101 ? 0.5548 0.4492 0.5530 -0.0422 0.0107  -0.0261 118 PRO A CG  
724  C CD  . PRO A 101 ? 0.5347 0.4388 0.5326 -0.0364 0.0134  -0.0278 118 PRO A CD  
725  N N   . ALA A 102 ? 0.5318 0.4090 0.5148 -0.0510 0.0145  -0.0580 119 ALA A N   
726  C CA  . ALA A 102 ? 0.5704 0.4474 0.5443 -0.0543 0.0140  -0.0688 119 ALA A CA  
727  C C   . ALA A 102 ? 0.5281 0.4190 0.4968 -0.0605 0.0091  -0.0688 119 ALA A C   
728  O O   . ALA A 102 ? 0.5146 0.4114 0.4726 -0.0605 0.0081  -0.0756 119 ALA A O   
729  C CB  . ALA A 102 ? 0.5873 0.4464 0.5642 -0.0581 0.0132  -0.0762 119 ALA A CB  
730  N N   . HIS A 103 ? 0.5552 0.4513 0.5308 -0.0655 0.0059  -0.0614 120 HIS A N   
731  C CA  . HIS A 103 ? 0.5307 0.4411 0.5043 -0.0712 0.0011  -0.0614 120 HIS A CA  
732  C C   . HIS A 103 ? 0.5218 0.4488 0.4910 -0.0663 0.0011  -0.0554 120 HIS A C   
733  O O   . HIS A 103 ? 0.4593 0.3995 0.4274 -0.0697 -0.0031 -0.0545 120 HIS A O   
734  C CB  . HIS A 103 ? 0.4885 0.3982 0.4728 -0.0788 -0.0011 -0.0564 120 HIS A CB  
735  C CG  . HIS A 103 ? 0.5112 0.4236 0.5010 -0.0760 0.0010  -0.0445 120 HIS A CG  
736  N ND1 . HIS A 103 ? 0.5322 0.4326 0.5242 -0.0707 0.0042  -0.0397 120 HIS A ND1 
737  C CD2 . HIS A 103 ? 0.5491 0.4743 0.5423 -0.0776 -0.0001 -0.0370 120 HIS A CD2 
738  C CE1 . HIS A 103 ? 0.5726 0.4779 0.5674 -0.0691 0.0046  -0.0299 120 HIS A CE1 
739  N NE2 . HIS A 103 ? 0.4959 0.4161 0.4914 -0.0732 0.0025  -0.0282 120 HIS A NE2 
740  N N   . VAL A 104 ? 0.4654 0.3917 0.4328 -0.0585 0.0057  -0.0518 121 VAL A N   
741  C CA  . VAL A 104 ? 0.4397 0.3794 0.4053 -0.0538 0.0064  -0.0448 121 VAL A CA  
742  C C   . VAL A 104 ? 0.4402 0.3816 0.3955 -0.0482 0.0102  -0.0488 121 VAL A C   
743  O O   . VAL A 104 ? 0.4556 0.3865 0.4089 -0.0453 0.0146  -0.0542 121 VAL A O   
744  C CB  . VAL A 104 ? 0.4283 0.3662 0.4031 -0.0497 0.0084  -0.0359 121 VAL A CB  
745  C CG1 . VAL A 104 ? 0.3791 0.3293 0.3533 -0.0445 0.0094  -0.0296 121 VAL A CG1 
746  C CG2 . VAL A 104 ? 0.4503 0.3862 0.4321 -0.0549 0.0056  -0.0312 121 VAL A CG2 
747  N N   . ASN A 105 ? 0.4047 0.3589 0.3531 -0.0465 0.0089  -0.0460 122 ASN A N   
748  C CA  . ASN A 105 ? 0.4058 0.3622 0.3429 -0.0409 0.0134  -0.0475 122 ASN A CA  
749  C C   . ASN A 105 ? 0.4483 0.4140 0.3891 -0.0362 0.0157  -0.0378 122 ASN A C   
750  O O   . ASN A 105 ? 0.4164 0.3891 0.3650 -0.0376 0.0120  -0.0314 122 ASN A O   
751  C CB  . ASN A 105 ? 0.4492 0.4104 0.3709 -0.0429 0.0093  -0.0539 122 ASN A CB  
752  C CG  . ASN A 105 ? 0.4273 0.4022 0.3493 -0.0456 0.0023  -0.0493 122 ASN A CG  
753  O OD1 . ASN A 105 ? 0.4363 0.4199 0.3545 -0.0415 0.0031  -0.0430 122 ASN A OD1 
754  N ND2 . ASN A 105 ? 0.4865 0.4635 0.4146 -0.0525 -0.0043 -0.0524 122 ASN A ND2 
755  N N   . CYS A 106 ? 0.3905 0.3555 0.3269 -0.0305 0.0226  -0.0370 123 CYS A N   
756  C CA  . CYS A 106 ? 0.4085 0.3816 0.3485 -0.0264 0.0249  -0.0282 123 CYS A CA  
757  C C   . CYS A 106 ? 0.3674 0.3435 0.2923 -0.0227 0.0296  -0.0283 123 CYS A C   
758  O O   . CYS A 106 ? 0.4192 0.3897 0.3312 -0.0220 0.0326  -0.0354 123 CYS A O   
759  C CB  . CYS A 106 ? 0.4743 0.4433 0.4300 -0.0227 0.0296  -0.0241 123 CYS A CB  
760  S SG  . CYS A 106 ? 0.5206 0.4790 0.4784 -0.0189 0.0384  -0.0301 123 CYS A SG  
761  N N   . LEU A 107 ? 0.3489 0.3333 0.2741 -0.0202 0.0297  -0.0204 124 LEU A N   
762  C CA  . LEU A 107 ? 0.3910 0.3773 0.3034 -0.0159 0.0355  -0.0176 124 LEU A CA  
763  C C   . LEU A 107 ? 0.3663 0.3566 0.2909 -0.0124 0.0397  -0.0082 124 LEU A C   
764  O O   . LEU A 107 ? 0.3460 0.3392 0.2861 -0.0134 0.0358  -0.0043 124 LEU A O   
765  C CB  . LEU A 107 ? 0.4744 0.4666 0.3688 -0.0168 0.0289  -0.0185 124 LEU A CB  
766  C CG  . LEU A 107 ? 0.3955 0.3979 0.2947 -0.0189 0.0198  -0.0135 124 LEU A CG  
767  C CD1 . LEU A 107 ? 0.4399 0.4477 0.3398 -0.0144 0.0223  -0.0037 124 LEU A CD1 
768  C CD2 . LEU A 107 ? 0.4187 0.4247 0.3029 -0.0215 0.0115  -0.0196 124 LEU A CD2 
769  N N   . TYR A 108 ? 0.3427 0.3321 0.2600 -0.0083 0.0482  -0.0049 125 TYR A N   
770  C CA  . TYR A 108 ? 0.3200 0.3115 0.2504 -0.0052 0.0541  0.0033  125 TYR A CA  
771  C C   . TYR A 108 ? 0.3672 0.3628 0.2842 -0.0027 0.0555  0.0104  125 TYR A C   
772  O O   . TYR A 108 ? 0.3440 0.3373 0.2402 -0.0009 0.0590  0.0088  125 TYR A O   
773  C CB  . TYR A 108 ? 0.3215 0.3069 0.2603 -0.0025 0.0657  0.0014  125 TYR A CB  
774  C CG  . TYR A 108 ? 0.3557 0.3359 0.3068 -0.0040 0.0643  -0.0055 125 TYR A CG  
775  C CD1 . TYR A 108 ? 0.3565 0.3374 0.3295 -0.0045 0.0603  -0.0034 125 TYR A CD1 
776  C CD2 . TYR A 108 ? 0.4008 0.3744 0.3412 -0.0046 0.0662  -0.0144 125 TYR A CD2 
777  C CE1 . TYR A 108 ? 0.3491 0.3241 0.3321 -0.0052 0.0583  -0.0090 125 TYR A CE1 
778  C CE2 . TYR A 108 ? 0.4260 0.3934 0.3780 -0.0056 0.0646  -0.0203 125 TYR A CE2 
779  C CZ  . TYR A 108 ? 0.3752 0.3434 0.3485 -0.0059 0.0604  -0.0170 125 TYR A CZ  
780  O OH  . TYR A 108 ? 0.3807 0.3417 0.3648 -0.0062 0.0585  -0.0218 125 TYR A OH  
781  N N   . ILE A 109 ? 0.3487 0.3494 0.2770 -0.0019 0.0527  0.0181  126 ILE A N   
782  C CA  . ILE A 109 ? 0.3970 0.4005 0.3161 0.0009  0.0540  0.0263  126 ILE A CA  
783  C C   . ILE A 109 ? 0.3678 0.3713 0.3061 0.0028  0.0600  0.0338  126 ILE A C   
784  O O   . ILE A 109 ? 0.3754 0.3808 0.3335 0.0016  0.0557  0.0339  126 ILE A O   
785  C CB  . ILE A 109 ? 0.4490 0.4598 0.3629 -0.0001 0.0421  0.0279  126 ILE A CB  
786  C CG1 . ILE A 109 ? 0.4620 0.4742 0.3658 -0.0036 0.0343  0.0192  126 ILE A CG1 
787  C CG2 . ILE A 109 ? 0.4530 0.4652 0.3519 0.0036  0.0429  0.0354  126 ILE A CG2 
788  C CD1 . ILE A 109 ? 0.5670 0.5879 0.4687 -0.0048 0.0229  0.0204  126 ILE A CD1 
789  N N   . ARG A 110 ? 0.4317 0.4327 0.3631 0.0059  0.0689  0.0404  127 ARG A N   
790  C CA  . ARG A 110 ? 0.3899 0.3903 0.3402 0.0072  0.0751  0.0479  127 ARG A CA  
791  C C   . ARG A 110 ? 0.4550 0.4590 0.4058 0.0083  0.0683  0.0553  127 ARG A C   
792  O O   . ARG A 110 ? 0.4790 0.4834 0.4101 0.0104  0.0666  0.0593  127 ARG A O   
793  C CB  . ARG A 110 ? 0.4203 0.4157 0.3648 0.0097  0.0900  0.0525  127 ARG A CB  
794  C CG  . ARG A 110 ? 0.5728 0.5642 0.5044 0.0100  0.0972  0.0455  127 ARG A CG  
795  C CD  . ARG A 110 ? 0.5664 0.5578 0.5175 0.0080  0.0963  0.0373  127 ARG A CD  
796  N NE  . ARG A 110 ? 0.4990 0.4857 0.4408 0.0090  0.1051  0.0304  127 ARG A NE  
797  C CZ  . ARG A 110 ? 0.5850 0.5701 0.5354 0.0077  0.1028  0.0216  127 ARG A CZ  
798  N NH1 . ARG A 110 ? 0.4037 0.3911 0.3697 0.0051  0.0917  0.0187  127 ARG A NH1 
799  N NH2 . ARG A 110 ? 0.5044 0.4847 0.4473 0.0093  0.1123  0.0157  127 ARG A NH2 
800  N N   . GLN A 111 ? 0.3872 0.3933 0.3603 0.0077  0.0643  0.0569  128 GLN A N   
801  C CA  . GLN A 111 ? 0.4727 0.4805 0.4487 0.0095  0.0604  0.0644  128 GLN A CA  
802  C C   . GLN A 111 ? 0.4636 0.4663 0.4401 0.0117  0.0720  0.0731  128 GLN A C   
803  O O   . GLN A 111 ? 0.4797 0.4790 0.4668 0.0111  0.0825  0.0730  128 GLN A O   
804  C CB  . GLN A 111 ? 0.4003 0.4109 0.3989 0.0086  0.0532  0.0631  128 GLN A CB  
805  C CG  . GLN A 111 ? 0.5016 0.5091 0.5238 0.0081  0.0593  0.0632  128 GLN A CG  
806  C CD  . GLN A 111 ? 0.6099 0.6195 0.6515 0.0080  0.0505  0.0615  128 GLN A CD  
807  O OE1 . GLN A 111 ? 0.4507 0.4641 0.4871 0.0080  0.0408  0.0593  128 GLN A OE1 
808  N NE2 . GLN A 111 ? 0.5322 0.5394 0.5963 0.0081  0.0541  0.0624  128 GLN A NE2 
809  N N   . SER A 112 ? 0.5051 0.5069 0.4696 0.0143  0.0706  0.0809  129 SER A N   
810  C CA  . SER A 112 ? 0.6012 0.5966 0.5623 0.0165  0.0822  0.0906  129 SER A CA  
811  C C   . SER A 112 ? 0.6782 0.6713 0.6685 0.0154  0.0872  0.0944  129 SER A C   
812  O O   . SER A 112 ? 0.7233 0.7114 0.7196 0.0154  0.1003  0.0997  129 SER A O   
813  C CB  . SER A 112 ? 0.6499 0.6443 0.5912 0.0202  0.0775  0.0982  129 SER A CB  
814  O OG  . SER A 112 ? 0.6119 0.6106 0.5662 0.0206  0.0663  0.0986  129 SER A OG  
815  N N   . ALA A 113 ? 0.5806 0.5772 0.5892 0.0146  0.0772  0.0917  130 ALA A N   
816  C CA  . ALA A 113 ? 0.6252 0.6198 0.6622 0.0137  0.0790  0.0940  130 ALA A CA  
817  C C   . ALA A 113 ? 0.5904 0.5900 0.6417 0.0127  0.0663  0.0864  130 ALA A C   
818  O O   . ALA A 113 ? 0.5725 0.5767 0.6106 0.0130  0.0571  0.0820  130 ALA A O   
819  C CB  . ALA A 113 ? 0.5810 0.5704 0.6183 0.0160  0.0813  0.1047  130 ALA A CB  
820  N N   . PRO A 114 ? 0.6821 0.6808 0.7603 0.0115  0.0656  0.0843  131 PRO A N   
821  C CA  . PRO A 114 ? 0.5488 0.5509 0.6386 0.0115  0.0535  0.0774  131 PRO A CA  
822  C C   . PRO A 114 ? 0.5759 0.5780 0.6647 0.0139  0.0455  0.0807  131 PRO A C   
823  O O   . PRO A 114 ? 0.6206 0.6195 0.7271 0.0146  0.0441  0.0826  131 PRO A O   
824  C CB  . PRO A 114 ? 0.6476 0.6479 0.7656 0.0100  0.0561  0.0745  131 PRO A CB  
825  C CG  . PRO A 114 ? 0.7330 0.7287 0.8593 0.0095  0.0679  0.0828  131 PRO A CG  
826  C CD  . PRO A 114 ? 0.7350 0.7296 0.8347 0.0103  0.0762  0.0880  131 PRO A CD  
827  N N   . LEU A 115 ? 0.5285 0.5344 0.5968 0.0153  0.0399  0.0808  132 LEU A N   
828  C CA  . LEU A 115 ? 0.5149 0.5219 0.5799 0.0184  0.0330  0.0841  132 LEU A CA  
829  C C   . LEU A 115 ? 0.5002 0.5130 0.5659 0.0189  0.0221  0.0769  132 LEU A C   
830  O O   . LEU A 115 ? 0.5487 0.5646 0.6088 0.0216  0.0160  0.0783  132 LEU A O   
831  C CB  . LEU A 115 ? 0.5497 0.5571 0.5919 0.0204  0.0349  0.0905  132 LEU A CB  
832  C CG  . LEU A 115 ? 0.5609 0.5610 0.5989 0.0210  0.0463  0.0996  132 LEU A CG  
833  C CD1 . LEU A 115 ? 0.5275 0.5281 0.5382 0.0235  0.0469  0.1046  132 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.5895 0.5830 0.6439 0.0226  0.0483  0.1062  132 LEU A CD2 
835  N N   . GLY A 116 ? 0.5266 0.5409 0.5987 0.0166  0.0199  0.0696  133 GLY A N   
836  C CA  . GLY A 116 ? 0.4798 0.4982 0.5526 0.0171  0.0109  0.0634  133 GLY A CA  
837  C C   . GLY A 116 ? 0.4462 0.4704 0.5026 0.0153  0.0087  0.0599  133 GLY A C   
838  O O   . GLY A 116 ? 0.3597 0.3851 0.4028 0.0139  0.0126  0.0616  133 GLY A O   
839  N N   . LEU A 117 ? 0.3934 0.4208 0.4505 0.0153  0.0020  0.0548  134 LEU A N   
840  C CA  . LEU A 117 ? 0.3547 0.3867 0.4000 0.0127  -0.0001 0.0508  134 LEU A CA  
841  C C   . LEU A 117 ? 0.3245 0.3631 0.3564 0.0128  -0.0012 0.0533  134 LEU A C   
842  O O   . LEU A 117 ? 0.3231 0.3645 0.3443 0.0099  -0.0006 0.0512  134 LEU A O   
843  C CB  . LEU A 117 ? 0.2965 0.3300 0.3453 0.0133  -0.0061 0.0462  134 LEU A CB  
844  C CG  . LEU A 117 ? 0.2900 0.3276 0.3289 0.0102  -0.0078 0.0426  134 LEU A CG  
845  C CD1 . LEU A 117 ? 0.3546 0.3880 0.3901 0.0066  -0.0038 0.0403  134 LEU A CD1 
846  C CD2 . LEU A 117 ? 0.3741 0.4114 0.4159 0.0114  -0.0124 0.0391  134 LEU A CD2 
847  N N   . GLY A 118 ? 0.3873 0.4286 0.4205 0.0164  -0.0039 0.0571  135 GLY A N   
848  C CA  . GLY A 118 ? 0.3205 0.3687 0.3423 0.0173  -0.0063 0.0595  135 GLY A CA  
849  C C   . GLY A 118 ? 0.3632 0.4088 0.3731 0.0165  -0.0016 0.0630  135 GLY A C   
850  O O   . GLY A 118 ? 0.3126 0.3631 0.3100 0.0150  -0.0034 0.0615  135 GLY A O   
851  N N   . HIS A 119 ? 0.3464 0.3840 0.3601 0.0174  0.0048  0.0672  136 HIS A N   
852  C CA  . HIS A 119 ? 0.4211 0.4553 0.4219 0.0169  0.0110  0.0706  136 HIS A CA  
853  C C   . HIS A 119 ? 0.3412 0.3750 0.3356 0.0128  0.0137  0.0645  136 HIS A C   
854  O O   . HIS A 119 ? 0.3339 0.3687 0.3120 0.0121  0.0148  0.0640  136 HIS A O   
855  C CB  . HIS A 119 ? 0.4053 0.4310 0.4140 0.0183  0.0189  0.0768  136 HIS A CB  
856  C CG  . HIS A 119 ? 0.4675 0.4886 0.4616 0.0184  0.0271  0.0811  136 HIS A CG  
857  N ND1 . HIS A 119 ? 0.4461 0.4675 0.4219 0.0214  0.0264  0.0867  136 HIS A ND1 
858  C CD2 . HIS A 119 ? 0.4459 0.4619 0.4406 0.0164  0.0365  0.0807  136 HIS A CD2 
859  C CE1 . HIS A 119 ? 0.4790 0.4950 0.4425 0.0212  0.0352  0.0896  136 HIS A CE1 
860  N NE2 . HIS A 119 ? 0.5220 0.5349 0.4974 0.0182  0.0421  0.0860  136 HIS A NE2 
861  N N   . ALA A 120 ? 0.3725 0.4044 0.3791 0.0105  0.0142  0.0595  137 ALA A N   
862  C CA  . ALA A 120 ? 0.3426 0.3733 0.3446 0.0070  0.0164  0.0536  137 ALA A CA  
863  C C   . ALA A 120 ? 0.3279 0.3649 0.3181 0.0047  0.0103  0.0494  137 ALA A C   
864  O O   . ALA A 120 ? 0.3135 0.3497 0.2921 0.0025  0.0121  0.0461  137 ALA A O   
865  C CB  . ALA A 120 ? 0.3741 0.4013 0.3915 0.0057  0.0164  0.0495  137 ALA A CB  
866  N N   . VAL A 121 ? 0.3526 0.3959 0.3466 0.0052  0.0035  0.0490  138 VAL A N   
867  C CA  . VAL A 121 ? 0.3096 0.3602 0.2958 0.0026  -0.0019 0.0451  138 VAL A CA  
868  C C   . VAL A 121 ? 0.3324 0.3867 0.3040 0.0038  -0.0036 0.0471  138 VAL A C   
869  O O   . VAL A 121 ? 0.3368 0.3933 0.2983 0.0009  -0.0054 0.0427  138 VAL A O   
870  C CB  . VAL A 121 ? 0.2980 0.3551 0.2931 0.0033  -0.0075 0.0445  138 VAL A CB  
871  C CG1 . VAL A 121 ? 0.3273 0.3939 0.3172 0.0008  -0.0127 0.0416  138 VAL A CG1 
872  C CG2 . VAL A 121 ? 0.3508 0.4034 0.3559 0.0019  -0.0068 0.0414  138 VAL A CG2 
873  N N   . LEU A 122 ? 0.3236 0.3782 0.2936 0.0084  -0.0037 0.0537  139 LEU A N   
874  C CA  . LEU A 122 ? 0.4226 0.4794 0.3765 0.0106  -0.0057 0.0565  139 LEU A CA  
875  C C   . LEU A 122 ? 0.4013 0.4511 0.3406 0.0094  0.0004  0.0551  139 LEU A C   
876  O O   . LEU A 122 ? 0.3701 0.4225 0.2939 0.0092  -0.0029 0.0528  139 LEU A O   
877  C CB  . LEU A 122 ? 0.3923 0.4475 0.3468 0.0163  -0.0056 0.0649  139 LEU A CB  
878  C CG  . LEU A 122 ? 0.4197 0.4762 0.3568 0.0201  -0.0084 0.0695  139 LEU A CG  
879  C CD1 . LEU A 122 ? 0.4545 0.5224 0.3870 0.0195  -0.0186 0.0649  139 LEU A CD1 
880  C CD2 . LEU A 122 ? 0.5014 0.5541 0.4420 0.0257  -0.0075 0.0788  139 LEU A CD2 
881  N N   . THR A 123 ? 0.3889 0.4306 0.3340 0.0086  0.0090  0.0556  140 THR A N   
882  C CA  . THR A 123 ? 0.4168 0.4519 0.3497 0.0077  0.0163  0.0537  140 THR A CA  
883  C C   . THR A 123 ? 0.3621 0.3994 0.2863 0.0038  0.0125  0.0448  140 THR A C   
884  O O   . THR A 123 ? 0.4307 0.4643 0.3384 0.0039  0.0155  0.0423  140 THR A O   
885  C CB  . THR A 123 ? 0.3846 0.4126 0.3314 0.0071  0.0254  0.0543  140 THR A CB  
886  O OG1 . THR A 123 ? 0.3801 0.4046 0.3331 0.0105  0.0302  0.0628  140 THR A OG1 
887  C CG2 . THR A 123 ? 0.4244 0.4465 0.3613 0.0060  0.0332  0.0506  140 THR A CG2 
888  N N   . ALA A 124 ? 0.3346 0.3771 0.2689 0.0004  0.0063  0.0399  141 ALA A N   
889  C CA  . ALA A 124 ? 0.2929 0.3364 0.2226 -0.0042 0.0032  0.0315  141 ALA A CA  
890  C C   . ALA A 124 ? 0.3477 0.3990 0.2662 -0.0050 -0.0054 0.0288  141 ALA A C   
891  O O   . ALA A 124 ? 0.4178 0.4693 0.3308 -0.0089 -0.0083 0.0214  141 ALA A O   
892  C CB  . ALA A 124 ? 0.3472 0.3915 0.2934 -0.0079 0.0013  0.0282  141 ALA A CB  
893  N N   . ALA A 125 ? 0.3357 0.3930 0.2514 -0.0011 -0.0100 0.0344  142 ALA A N   
894  C CA  . ALA A 125 ? 0.4259 0.4925 0.3342 -0.0013 -0.0197 0.0317  142 ALA A CA  
895  C C   . ALA A 125 ? 0.4298 0.4934 0.3187 -0.0024 -0.0214 0.0258  142 ALA A C   
896  O O   . ALA A 125 ? 0.4034 0.4735 0.2921 -0.0062 -0.0292 0.0187  142 ALA A O   
897  C CB  . ALA A 125 ? 0.4779 0.5494 0.3842 0.0047  -0.0236 0.0397  142 ALA A CB  
898  N N   . PRO A 126 ? 0.4022 0.4564 0.2748 0.0006  -0.0144 0.0275  143 PRO A N   
899  C CA  . PRO A 126 ? 0.4520 0.5031 0.3041 0.0000  -0.0167 0.0206  143 PRO A CA  
900  C C   . PRO A 126 ? 0.4326 0.4819 0.2904 -0.0066 -0.0173 0.0100  143 PRO A C   
901  O O   . PRO A 126 ? 0.5216 0.5721 0.3681 -0.0086 -0.0238 0.0021  143 PRO A O   
902  C CB  . PRO A 126 ? 0.4631 0.5032 0.2989 0.0046  -0.0057 0.0254  143 PRO A CB  
903  C CG  . PRO A 126 ? 0.4353 0.4752 0.2815 0.0084  -0.0011 0.0366  143 PRO A CG  
904  C CD  . PRO A 126 ? 0.3900 0.4363 0.2619 0.0047  -0.0043 0.0358  143 PRO A CD  
905  N N   . ALA A 127 ? 0.4254 0.4714 0.3006 -0.0098 -0.0116 0.0096  144 ALA A N   
906  C CA  . ALA A 127 ? 0.4267 0.4697 0.3084 -0.0159 -0.0123 0.0006  144 ALA A CA  
907  C C   . ALA A 127 ? 0.4308 0.4834 0.3277 -0.0210 -0.0207 -0.0021 144 ALA A C   
908  O O   . ALA A 127 ? 0.4214 0.4730 0.3208 -0.0265 -0.0239 -0.0101 144 ALA A O   
909  C CB  . ALA A 127 ? 0.4417 0.4760 0.3345 -0.0164 -0.0026 0.0016  144 ALA A CB  
910  N N   . VAL A 128 ? 0.4661 0.5272 0.3739 -0.0194 -0.0236 0.0042  145 VAL A N   
911  C CA  . VAL A 128 ? 0.3721 0.4427 0.2955 -0.0239 -0.0296 0.0022  145 VAL A CA  
912  C C   . VAL A 128 ? 0.4568 0.5386 0.3764 -0.0248 -0.0401 -0.0014 145 VAL A C   
913  O O   . VAL A 128 ? 0.5219 0.6099 0.4518 -0.0307 -0.0451 -0.0069 145 VAL A O   
914  C CB  . VAL A 128 ? 0.3710 0.4454 0.3084 -0.0213 -0.0273 0.0099  145 VAL A CB  
915  C CG1 . VAL A 128 ? 0.3774 0.4639 0.3295 -0.0245 -0.0332 0.0090  145 VAL A CG1 
916  C CG2 . VAL A 128 ? 0.3886 0.4525 0.3325 -0.0217 -0.0190 0.0112  145 VAL A CG2 
917  N N   . GLY A 129 ? 0.4497 0.5344 0.3560 -0.0190 -0.0437 0.0021  146 GLY A N   
918  C CA  . GLY A 129 ? 0.4680 0.5646 0.3729 -0.0191 -0.0552 -0.0012 146 GLY A CA  
919  C C   . GLY A 129 ? 0.4783 0.5883 0.4040 -0.0198 -0.0593 0.0020  146 GLY A C   
920  O O   . GLY A 129 ? 0.5023 0.6123 0.4371 -0.0169 -0.0542 0.0090  146 GLY A O   
921  N N   . ASN A 130 ? 0.4645 0.5864 0.3985 -0.0235 -0.0686 -0.0039 147 ASN A N   
922  C CA  . ASN A 130 ? 0.6268 0.7633 0.5818 -0.0243 -0.0723 -0.0019 147 ASN A CA  
923  C C   . ASN A 130 ? 0.6386 0.7772 0.6122 -0.0328 -0.0688 -0.0060 147 ASN A C   
924  O O   . ASN A 130 ? 0.8000 0.9506 0.7877 -0.0376 -0.0747 -0.0108 147 ASN A O   
925  C CB  . ASN A 130 ? 0.6870 0.8377 0.6430 -0.0224 -0.0851 -0.0048 147 ASN A CB  
926  C CG  . ASN A 130 ? 0.8863 1.0510 0.8594 -0.0185 -0.0879 0.0006  147 ASN A CG  
927  O OD1 . ASN A 130 ? 0.8022 0.9633 0.7769 -0.0137 -0.0816 0.0084  147 ASN A OD1 
928  N ND2 . ASN A 130 ? 1.1307 1.3116 1.1188 -0.0210 -0.0972 -0.0042 147 ASN A ND2 
929  N N   . GLU A 131 ? 0.4985 0.6254 0.4728 -0.0347 -0.0591 -0.0042 148 GLU A N   
930  C CA  . GLU A 131 ? 0.5173 0.6448 0.5074 -0.0419 -0.0552 -0.0064 148 GLU A CA  
931  C C   . GLU A 131 ? 0.4039 0.5261 0.3996 -0.0393 -0.0466 0.0004  148 GLU A C   
932  O O   . GLU A 131 ? 0.3724 0.4868 0.3591 -0.0335 -0.0428 0.0053  148 GLU A O   
933  C CB  . GLU A 131 ? 0.5488 0.6658 0.5344 -0.0486 -0.0538 -0.0137 148 GLU A CB  
934  C CG  . GLU A 131 ? 0.5794 0.6797 0.5524 -0.0468 -0.0466 -0.0129 148 GLU A CG  
935  C CD  . GLU A 131 ? 0.5776 0.6690 0.5454 -0.0528 -0.0473 -0.0216 148 GLU A CD  
936  O OE1 . GLU A 131 ? 0.5753 0.6660 0.5299 -0.0518 -0.0527 -0.0271 148 GLU A OE1 
937  O OE2 . GLU A 131 ? 0.4940 0.5785 0.4703 -0.0582 -0.0428 -0.0231 148 GLU A OE2 
938  N N   . PRO A 132 ? 0.3911 0.5176 0.4017 -0.0434 -0.0435 0.0009  149 PRO A N   
939  C CA  . PRO A 132 ? 0.3974 0.5177 0.4111 -0.0407 -0.0361 0.0066  149 PRO A CA  
940  C C   . PRO A 132 ? 0.3202 0.4234 0.3249 -0.0415 -0.0305 0.0063  149 PRO A C   
941  O O   . PRO A 132 ? 0.3838 0.4802 0.3847 -0.0465 -0.0306 0.0012  149 PRO A O   
942  C CB  . PRO A 132 ? 0.3934 0.5217 0.4228 -0.0459 -0.0340 0.0062  149 PRO A CB  
943  C CG  . PRO A 132 ? 0.4451 0.5754 0.4784 -0.0541 -0.0374 -0.0006 149 PRO A CG  
944  C CD  . PRO A 132 ? 0.4679 0.6026 0.4922 -0.0514 -0.0458 -0.0042 149 PRO A CD  
945  N N   . PHE A 133 ? 0.3384 0.4347 0.3409 -0.0362 -0.0261 0.0114  150 PHE A N   
946  C CA  . PHE A 133 ? 0.3118 0.3929 0.3074 -0.0358 -0.0214 0.0112  150 PHE A CA  
947  C C   . PHE A 133 ? 0.3400 0.4151 0.3395 -0.0325 -0.0171 0.0157  150 PHE A C   
948  O O   . PHE A 133 ? 0.3643 0.4456 0.3686 -0.0285 -0.0176 0.0194  150 PHE A O   
949  C CB  . PHE A 133 ? 0.3301 0.4067 0.3143 -0.0315 -0.0216 0.0115  150 PHE A CB  
950  C CG  . PHE A 133 ? 0.2795 0.3601 0.2636 -0.0248 -0.0219 0.0173  150 PHE A CG  
951  C CD1 . PHE A 133 ? 0.2791 0.3718 0.2648 -0.0226 -0.0272 0.0188  150 PHE A CD1 
952  C CD2 . PHE A 133 ? 0.2355 0.3078 0.2196 -0.0205 -0.0175 0.0211  150 PHE A CD2 
953  C CE1 . PHE A 133 ? 0.2890 0.3841 0.2751 -0.0161 -0.0276 0.0244  150 PHE A CE1 
954  C CE2 . PHE A 133 ? 0.2872 0.3623 0.2728 -0.0146 -0.0178 0.0265  150 PHE A CE2 
955  C CZ  . PHE A 133 ? 0.3221 0.4079 0.3081 -0.0124 -0.0227 0.0283  150 PHE A CZ  
956  N N   . ALA A 134 ? 0.3208 0.3832 0.3179 -0.0334 -0.0136 0.0148  151 ALA A N   
957  C CA  . ALA A 134 ? 0.2773 0.3324 0.2771 -0.0301 -0.0107 0.0182  151 ALA A CA  
958  C C   . ALA A 134 ? 0.2925 0.3425 0.2903 -0.0244 -0.0096 0.0202  151 ALA A C   
959  O O   . ALA A 134 ? 0.3072 0.3548 0.2998 -0.0240 -0.0087 0.0187  151 ALA A O   
960  C CB  . ALA A 134 ? 0.3452 0.3890 0.3448 -0.0338 -0.0082 0.0165  151 ALA A CB  
961  N N   . VAL A 135 ? 0.2747 0.3230 0.2768 -0.0200 -0.0093 0.0235  152 VAL A N   
962  C CA  . VAL A 135 ? 0.2672 0.3093 0.2712 -0.0151 -0.0079 0.0252  152 VAL A CA  
963  C C   . VAL A 135 ? 0.3351 0.3684 0.3426 -0.0136 -0.0077 0.0253  152 VAL A C   
964  O O   . VAL A 135 ? 0.3188 0.3536 0.3271 -0.0129 -0.0091 0.0264  152 VAL A O   
965  C CB  . VAL A 135 ? 0.2624 0.3109 0.2693 -0.0103 -0.0094 0.0288  152 VAL A CB  
966  C CG1 . VAL A 135 ? 0.3057 0.3473 0.3169 -0.0063 -0.0075 0.0305  152 VAL A CG1 
967  C CG2 . VAL A 135 ? 0.3113 0.3682 0.3132 -0.0110 -0.0107 0.0293  152 VAL A CG2 
968  N N   . LEU A 136 ? 0.2831 0.3073 0.2925 -0.0125 -0.0059 0.0241  153 LEU A N   
969  C CA  . LEU A 136 ? 0.2818 0.2974 0.2950 -0.0101 -0.0071 0.0240  153 LEU A CA  
970  C C   . LEU A 136 ? 0.3328 0.3447 0.3542 -0.0058 -0.0067 0.0244  153 LEU A C   
971  O O   . LEU A 136 ? 0.2808 0.2910 0.3040 -0.0062 -0.0032 0.0234  153 LEU A O   
972  C CB  . LEU A 136 ? 0.2811 0.2878 0.2914 -0.0133 -0.0061 0.0217  153 LEU A CB  
973  C CG  . LEU A 136 ? 0.2418 0.2500 0.2463 -0.0187 -0.0057 0.0212  153 LEU A CG  
974  C CD1 . LEU A 136 ? 0.2880 0.3011 0.2894 -0.0232 -0.0042 0.0184  153 LEU A CD1 
975  C CD2 . LEU A 136 ? 0.3030 0.2997 0.3058 -0.0198 -0.0057 0.0208  153 LEU A CD2 
976  N N   . LEU A 137 ? 0.2245 0.2349 0.2512 -0.0016 -0.0101 0.0254  154 LEU A N   
977  C CA  . LEU A 137 ? 0.2419 0.2489 0.2797 0.0023  -0.0109 0.0252  154 LEU A CA  
978  C C   . LEU A 137 ? 0.3126 0.3105 0.3539 0.0039  -0.0136 0.0230  154 LEU A C   
979  O O   . LEU A 137 ? 0.2669 0.2611 0.3043 0.0058  -0.0181 0.0229  154 LEU A O   
980  C CB  . LEU A 137 ? 0.2881 0.2986 0.3305 0.0060  -0.0142 0.0268  154 LEU A CB  
981  C CG  . LEU A 137 ? 0.3115 0.3308 0.3488 0.0054  -0.0134 0.0292  154 LEU A CG  
982  C CD1 . LEU A 137 ? 0.3282 0.3484 0.3721 0.0100  -0.0170 0.0298  154 LEU A CD1 
983  C CD2 . LEU A 137 ? 0.2765 0.2998 0.3123 0.0033  -0.0088 0.0310  154 LEU A CD2 
984  N N   . ALA A 138 ? 0.2622 0.2562 0.3102 0.0037  -0.0106 0.0213  155 ALA A N   
985  C CA  . ALA A 138 ? 0.2524 0.2377 0.3036 0.0052  -0.0132 0.0191  155 ALA A CA  
986  C C   . ALA A 138 ? 0.2888 0.2707 0.3490 0.0104  -0.0200 0.0184  155 ALA A C   
987  O O   . ALA A 138 ? 0.2968 0.2711 0.3563 0.0126  -0.0244 0.0172  155 ALA A O   
988  C CB  . ALA A 138 ? 0.2827 0.2653 0.3407 0.0044  -0.0079 0.0169  155 ALA A CB  
989  N N   . ASP A 139 ? 0.3123 0.2991 0.3810 0.0125  -0.0213 0.0190  156 ASP A N   
990  C CA  . ASP A 139 ? 0.3149 0.2985 0.3924 0.0174  -0.0290 0.0172  156 ASP A CA  
991  C C   . ASP A 139 ? 0.3470 0.3269 0.4104 0.0195  -0.0350 0.0174  156 ASP A C   
992  O O   . ASP A 139 ? 0.3257 0.2998 0.3910 0.0241  -0.0425 0.0153  156 ASP A O   
993  C CB  . ASP A 139 ? 0.3534 0.3424 0.4424 0.0187  -0.0291 0.0177  156 ASP A CB  
994  C CG  . ASP A 139 ? 0.4113 0.3999 0.5221 0.0200  -0.0283 0.0159  156 ASP A CG  
995  O OD1 . ASP A 139 ? 0.3843 0.3689 0.5018 0.0209  -0.0293 0.0136  156 ASP A OD1 
996  O OD2 . ASP A 139 ? 0.3848 0.3771 0.5075 0.0201  -0.0267 0.0169  156 ASP A OD2 
997  N N   . ASP A 140 ? 0.2993 0.2824 0.3484 0.0166  -0.0317 0.0197  157 ASP A N   
998  C CA  . ASP A 140 ? 0.2755 0.2548 0.3099 0.0179  -0.0349 0.0206  157 ASP A CA  
999  C C   . ASP A 140 ? 0.2787 0.2506 0.3058 0.0157  -0.0334 0.0213  157 ASP A C   
1000 O O   . ASP A 140 ? 0.3119 0.2858 0.3327 0.0106  -0.0279 0.0228  157 ASP A O   
1001 C CB  . ASP A 140 ? 0.2820 0.2693 0.3077 0.0158  -0.0315 0.0227  157 ASP A CB  
1002 C CG  . ASP A 140 ? 0.3854 0.3770 0.4157 0.0197  -0.0347 0.0218  157 ASP A CG  
1003 O OD1 . ASP A 140 ? 0.3827 0.3694 0.4197 0.0242  -0.0407 0.0192  157 ASP A OD1 
1004 O OD2 . ASP A 140 ? 0.4469 0.4464 0.4749 0.0186  -0.0318 0.0232  157 ASP A OD2 
1005 N N   . LEU A 141 ? 0.3290 0.2917 0.3576 0.0198  -0.0392 0.0200  158 LEU A N   
1006 C CA  . LEU A 141 ? 0.3172 0.2704 0.3390 0.0189  -0.0389 0.0211  158 LEU A CA  
1007 C C   . LEU A 141 ? 0.3575 0.3052 0.3611 0.0197  -0.0401 0.0242  158 LEU A C   
1008 O O   . LEU A 141 ? 0.3328 0.2767 0.3305 0.0252  -0.0464 0.0240  158 LEU A O   
1009 C CB  . LEU A 141 ? 0.2745 0.2204 0.3071 0.0239  -0.0452 0.0185  158 LEU A CB  
1010 C CG  . LEU A 141 ? 0.4169 0.3514 0.4447 0.0243  -0.0459 0.0195  158 LEU A CG  
1011 C CD1 . LEU A 141 ? 0.4348 0.3696 0.4618 0.0183  -0.0379 0.0200  158 LEU A CD1 
1012 C CD2 . LEU A 141 ? 0.4333 0.3637 0.4767 0.0299  -0.0526 0.0161  158 LEU A CD2 
1013 N N   . ILE A 142 ? 0.3635 0.3103 0.3581 0.0142  -0.0340 0.0269  159 ILE A N   
1014 C CA  . ILE A 142 ? 0.3420 0.2851 0.3204 0.0137  -0.0325 0.0307  159 ILE A CA  
1015 C C   . ILE A 142 ? 0.3846 0.3149 0.3553 0.0121  -0.0314 0.0335  159 ILE A C   
1016 O O   . ILE A 142 ? 0.3888 0.3181 0.3644 0.0069  -0.0272 0.0330  159 ILE A O   
1017 C CB  . ILE A 142 ? 0.3961 0.3505 0.3719 0.0080  -0.0256 0.0321  159 ILE A CB  
1018 C CG1 . ILE A 142 ? 0.3708 0.3369 0.3539 0.0103  -0.0269 0.0298  159 ILE A CG1 
1019 C CG2 . ILE A 142 ? 0.4433 0.3933 0.4037 0.0075  -0.0228 0.0363  159 ILE A CG2 
1020 C CD1 . ILE A 142 ? 0.3671 0.3452 0.3496 0.0058  -0.0213 0.0309  159 ILE A CD1 
1021 N N   . ASP A 143 ? 0.3666 0.2859 0.3244 0.0170  -0.0355 0.0363  160 ASP A N   
1022 C CA  . ASP A 143 ? 0.4018 0.3065 0.3498 0.0166  -0.0348 0.0403  160 ASP A CA  
1023 C C   . ASP A 143 ? 0.4538 0.3573 0.3859 0.0134  -0.0284 0.0457  160 ASP A C   
1024 O O   . ASP A 143 ? 0.4325 0.3367 0.3534 0.0178  -0.0300 0.0470  160 ASP A O   
1025 C CB  . ASP A 143 ? 0.4681 0.3607 0.4123 0.0254  -0.0446 0.0402  160 ASP A CB  
1026 C CG  . ASP A 143 ? 0.6081 0.4837 0.5416 0.0262  -0.0450 0.0450  160 ASP A CG  
1027 O OD1 . ASP A 143 ? 0.5667 0.4392 0.5059 0.0205  -0.0398 0.0455  160 ASP A OD1 
1028 O OD2 . ASP A 143 ? 0.5526 0.4171 0.4718 0.0334  -0.0515 0.0478  160 ASP A OD2 
1029 N N   . ALA A 144 ? 0.4532 0.3557 0.3856 0.0055  -0.0209 0.0481  161 ALA A N   
1030 C CA  . ALA A 144 ? 0.4155 0.3199 0.3379 0.0007  -0.0129 0.0529  161 ALA A CA  
1031 C C   . ALA A 144 ? 0.4753 0.3685 0.3954 -0.0055 -0.0077 0.0569  161 ALA A C   
1032 O O   . ALA A 144 ? 0.4803 0.3709 0.4108 -0.0090 -0.0080 0.0539  161 ALA A O   
1033 C CB  . ALA A 144 ? 0.4039 0.3271 0.3360 -0.0046 -0.0081 0.0501  161 ALA A CB  
1034 N N   . ASP A 145 ? 0.4464 0.3329 0.3529 -0.0071 -0.0019 0.0635  162 ASP A N   
1035 C CA  . ASP A 145 ? 0.4680 0.3427 0.3723 -0.0137 0.0041  0.0682  162 ASP A CA  
1036 C C   . ASP A 145 ? 0.5160 0.4020 0.4355 -0.0243 0.0103  0.0650  162 ASP A C   
1037 O O   . ASP A 145 ? 0.4637 0.3410 0.3883 -0.0300 0.0125  0.0653  162 ASP A O   
1038 C CB  . ASP A 145 ? 0.4861 0.3512 0.3722 -0.0133 0.0105  0.0770  162 ASP A CB  
1039 C CG  . ASP A 145 ? 0.6357 0.4852 0.5028 -0.0027 0.0039  0.0810  162 ASP A CG  
1040 O OD1 . ASP A 145 ? 0.6078 0.4511 0.4783 0.0033  -0.0058 0.0775  162 ASP A OD1 
1041 O OD2 . ASP A 145 ? 0.6951 0.5385 0.5438 -0.0003 0.0086  0.0876  162 ASP A OD2 
1042 N N   . THR A 146 ? 0.4678 0.3725 0.3940 -0.0269 0.0131  0.0623  163 THR A N   
1043 C CA  . THR A 146 ? 0.4410 0.3591 0.3822 -0.0357 0.0166  0.0580  163 THR A CA  
1044 C C   . THR A 146 ? 0.4245 0.3567 0.3751 -0.0328 0.0111  0.0512  163 THR A C   
1045 O O   . THR A 146 ? 0.4159 0.3538 0.3628 -0.0260 0.0079  0.0508  163 THR A O   
1046 C CB  . THR A 146 ? 0.5275 0.4568 0.4707 -0.0418 0.0249  0.0610  163 THR A CB  
1047 O OG1 . THR A 146 ? 0.7001 0.6402 0.6384 -0.0359 0.0246  0.0613  163 THR A OG1 
1048 C CG2 . THR A 146 ? 0.4787 0.3941 0.4127 -0.0451 0.0319  0.0686  163 THR A CG2 
1049 N N   . PRO A 147 ? 0.4001 0.3368 0.3618 -0.0372 0.0098  0.0457  164 PRO A N   
1050 C CA  . PRO A 147 ? 0.3717 0.3196 0.3405 -0.0337 0.0052  0.0403  164 PRO A CA  
1051 C C   . PRO A 147 ? 0.3204 0.2849 0.2910 -0.0326 0.0061  0.0403  164 PRO A C   
1052 O O   . PRO A 147 ? 0.3626 0.3364 0.3365 -0.0382 0.0106  0.0412  164 PRO A O   
1053 C CB  . PRO A 147 ? 0.4050 0.3550 0.3826 -0.0401 0.0057  0.0350  164 PRO A CB  
1054 C CG  . PRO A 147 ? 0.4120 0.3462 0.3872 -0.0441 0.0080  0.0368  164 PRO A CG  
1055 C CD  . PRO A 147 ? 0.3773 0.3060 0.3440 -0.0445 0.0121  0.0442  164 PRO A CD  
1056 N N   . VAL A 148 ? 0.3285 0.2968 0.2984 -0.0253 0.0017  0.0392  165 VAL A N   
1057 C CA  . VAL A 148 ? 0.3332 0.3155 0.3045 -0.0232 0.0022  0.0392  165 VAL A CA  
1058 C C   . VAL A 148 ? 0.3759 0.3732 0.3574 -0.0283 0.0033  0.0361  165 VAL A C   
1059 O O   . VAL A 148 ? 0.3018 0.3112 0.2863 -0.0302 0.0061  0.0368  165 VAL A O   
1060 C CB  . VAL A 148 ? 0.3481 0.3297 0.3181 -0.0145 -0.0034 0.0380  165 VAL A CB  
1061 C CG1 . VAL A 148 ? 0.3723 0.3687 0.3470 -0.0125 -0.0036 0.0368  165 VAL A CG1 
1062 C CG2 . VAL A 148 ? 0.3796 0.3493 0.3371 -0.0089 -0.0048 0.0413  165 VAL A CG2 
1063 N N   . LEU A 149 ? 0.3270 0.3239 0.3137 -0.0303 0.0012  0.0323  166 LEU A N   
1064 C CA  . LEU A 149 ? 0.3336 0.3437 0.3273 -0.0346 0.0013  0.0292  166 LEU A CA  
1065 C C   . LEU A 149 ? 0.2950 0.3099 0.2921 -0.0424 0.0050  0.0295  166 LEU A C   
1066 O O   . LEU A 149 ? 0.2855 0.3148 0.2888 -0.0448 0.0051  0.0284  166 LEU A O   
1067 C CB  . LEU A 149 ? 0.2605 0.2674 0.2563 -0.0353 -0.0008 0.0251  166 LEU A CB  
1068 C CG  . LEU A 149 ? 0.3287 0.3490 0.3286 -0.0372 -0.0022 0.0221  166 LEU A CG  
1069 C CD1 . LEU A 149 ? 0.2978 0.3269 0.2990 -0.0310 -0.0042 0.0237  166 LEU A CD1 
1070 C CD2 . LEU A 149 ? 0.2943 0.3104 0.2934 -0.0393 -0.0029 0.0176  166 LEU A CD2 
1071 N N   . LYS A 150 ? 0.2967 0.2995 0.2909 -0.0464 0.0079  0.0311  167 LYS A N   
1072 C CA  . LYS A 150 ? 0.3435 0.3497 0.3429 -0.0546 0.0123  0.0319  167 LYS A CA  
1073 C C   . LYS A 150 ? 0.3651 0.3812 0.3653 -0.0539 0.0164  0.0359  167 LYS A C   
1074 O O   . LYS A 150 ? 0.3574 0.3863 0.3673 -0.0594 0.0188  0.0350  167 LYS A O   
1075 C CB  . LYS A 150 ? 0.3662 0.3548 0.3616 -0.0584 0.0152  0.0340  167 LYS A CB  
1076 C CG  . LYS A 150 ? 0.4087 0.3989 0.4114 -0.0682 0.0203  0.0348  167 LYS A CG  
1077 C CD  . LYS A 150 ? 0.5482 0.5489 0.5619 -0.0745 0.0173  0.0279  167 LYS A CD  
1078 C CE  . LYS A 150 ? 0.6793 0.6807 0.7032 -0.0850 0.0216  0.0276  167 LYS A CE  
1079 N NZ  . LYS A 150 ? 0.6972 0.7166 0.7338 -0.0900 0.0180  0.0213  167 LYS A NZ  
1080 N N   . GLN A 151 ? 0.3571 0.3672 0.3477 -0.0469 0.0173  0.0400  168 GLN A N   
1081 C CA  . GLN A 151 ? 0.3286 0.3477 0.3184 -0.0450 0.0219  0.0433  168 GLN A CA  
1082 C C   . GLN A 151 ? 0.3625 0.4006 0.3621 -0.0436 0.0195  0.0400  168 GLN A C   
1083 O O   . GLN A 151 ? 0.3189 0.3700 0.3263 -0.0465 0.0238  0.0406  168 GLN A O   
1084 C CB  . GLN A 151 ? 0.3479 0.3567 0.3235 -0.0364 0.0214  0.0467  168 GLN A CB  
1085 C CG  . GLN A 151 ? 0.3972 0.3855 0.3611 -0.0359 0.0222  0.0505  168 GLN A CG  
1086 C CD  . GLN A 151 ? 0.4077 0.3863 0.3571 -0.0263 0.0193  0.0528  168 GLN A CD  
1087 O OE1 . GLN A 151 ? 0.3896 0.3747 0.3344 -0.0216 0.0207  0.0535  168 GLN A OE1 
1088 N NE2 . GLN A 151 ? 0.4202 0.3832 0.3627 -0.0231 0.0147  0.0534  168 GLN A NE2 
1089 N N   . LEU A 152 ? 0.3144 0.3543 0.3143 -0.0390 0.0131  0.0368  169 LEU A N   
1090 C CA  . LEU A 152 ? 0.3743 0.4305 0.3825 -0.0370 0.0102  0.0343  169 LEU A CA  
1091 C C   . LEU A 152 ? 0.3191 0.3865 0.3382 -0.0444 0.0094  0.0312  169 LEU A C   
1092 O O   . LEU A 152 ? 0.2833 0.3664 0.3115 -0.0449 0.0095  0.0304  169 LEU A O   
1093 C CB  . LEU A 152 ? 0.3429 0.3964 0.3485 -0.0308 0.0044  0.0325  169 LEU A CB  
1094 C CG  . LEU A 152 ? 0.3446 0.3875 0.3418 -0.0233 0.0029  0.0342  169 LEU A CG  
1095 C CD1 . LEU A 152 ? 0.3391 0.3837 0.3390 -0.0181 -0.0022 0.0323  169 LEU A CD1 
1096 C CD2 . LEU A 152 ? 0.3626 0.4083 0.3560 -0.0193 0.0060  0.0365  169 LEU A CD2 
1097 N N   . ILE A 153 ? 0.3084 0.3682 0.3273 -0.0496 0.0080  0.0287  170 ILE A N   
1098 C CA  . ILE A 153 ? 0.3127 0.3822 0.3411 -0.0567 0.0060  0.0244  170 ILE A CA  
1099 C C   . ILE A 153 ? 0.3749 0.4535 0.4140 -0.0631 0.0109  0.0256  170 ILE A C   
1100 O O   . ILE A 153 ? 0.3413 0.4359 0.3922 -0.0661 0.0088  0.0228  170 ILE A O   
1101 C CB  . ILE A 153 ? 0.3766 0.4340 0.4017 -0.0610 0.0040  0.0208  170 ILE A CB  
1102 C CG1 . ILE A 153 ? 0.3085 0.3631 0.3270 -0.0555 -0.0009 0.0183  170 ILE A CG1 
1103 C CG2 . ILE A 153 ? 0.3300 0.3945 0.3652 -0.0700 0.0030  0.0164  170 ILE A CG2 
1104 C CD1 . ILE A 153 ? 0.4134 0.4528 0.4262 -0.0573 -0.0014 0.0152  170 ILE A CD1 
1105 N N   . ASP A 154 ? 0.3646 0.4332 0.4003 -0.0655 0.0177  0.0299  171 ASP A N   
1106 C CA  . ASP A 154 ? 0.3593 0.4360 0.4063 -0.0723 0.0242  0.0317  171 ASP A CA  
1107 C C   . ASP A 154 ? 0.3330 0.4273 0.3872 -0.0683 0.0263  0.0330  171 ASP A C   
1108 O O   . ASP A 154 ? 0.3748 0.4843 0.4448 -0.0735 0.0282  0.0315  171 ASP A O   
1109 C CB  . ASP A 154 ? 0.3839 0.4447 0.4232 -0.0746 0.0320  0.0374  171 ASP A CB  
1110 C CG  . ASP A 154 ? 0.4797 0.5245 0.5168 -0.0805 0.0308  0.0358  171 ASP A CG  
1111 O OD1 . ASP A 154 ? 0.4875 0.5361 0.5318 -0.0847 0.0252  0.0296  171 ASP A OD1 
1112 O OD2 . ASP A 154 ? 0.5200 0.5480 0.5475 -0.0806 0.0353  0.0407  171 ASP A OD2 
1113 N N   . VAL A 155 ? 0.2804 0.3730 0.3245 -0.0589 0.0257  0.0351  172 VAL A N   
1114 C CA  . VAL A 155 ? 0.3575 0.4664 0.4085 -0.0539 0.0267  0.0353  172 VAL A CA  
1115 C C   . VAL A 155 ? 0.3656 0.4900 0.4282 -0.0539 0.0190  0.0305  172 VAL A C   
1116 O O   . VAL A 155 ? 0.3610 0.5029 0.4375 -0.0543 0.0199  0.0295  172 VAL A O   
1117 C CB  . VAL A 155 ? 0.3416 0.4434 0.3788 -0.0436 0.0265  0.0375  172 VAL A CB  
1118 C CG1 . VAL A 155 ? 0.3448 0.4627 0.3895 -0.0380 0.0276  0.0370  172 VAL A CG1 
1119 C CG2 . VAL A 155 ? 0.3566 0.4429 0.3802 -0.0428 0.0331  0.0422  172 VAL A CG2 
1120 N N   . ALA A 156 ? 0.3244 0.4427 0.3809 -0.0524 0.0116  0.0278  173 ALA A N   
1121 C CA  . ALA A 156 ? 0.3412 0.4723 0.4049 -0.0514 0.0039  0.0240  173 ALA A CA  
1122 C C   . ALA A 156 ? 0.3787 0.5222 0.4578 -0.0599 0.0025  0.0203  173 ALA A C   
1123 O O   . ALA A 156 ? 0.3628 0.5235 0.4540 -0.0589 -0.0010 0.0184  173 ALA A O   
1124 C CB  . ALA A 156 ? 0.3778 0.4984 0.4306 -0.0491 -0.0022 0.0221  173 ALA A CB  
1125 N N   . VAL A 157 ? 0.3806 0.5155 0.4606 -0.0681 0.0050  0.0191  174 VAL A N   
1126 C CA  . VAL A 157 ? 0.4018 0.5478 0.4984 -0.0771 0.0036  0.0150  174 VAL A CA  
1127 C C   . VAL A 157 ? 0.4183 0.5793 0.5314 -0.0792 0.0104  0.0173  174 VAL A C   
1128 O O   . VAL A 157 ? 0.4113 0.5907 0.5422 -0.0819 0.0069  0.0138  174 VAL A O   
1129 C CB  . VAL A 157 ? 0.4148 0.5458 0.5091 -0.0856 0.0056  0.0133  174 VAL A CB  
1130 C CG1 . VAL A 157 ? 0.5039 0.6464 0.6182 -0.0957 0.0049  0.0090  174 VAL A CG1 
1131 C CG2 . VAL A 157 ? 0.4070 0.5255 0.4874 -0.0835 -0.0009 0.0098  174 VAL A CG2 
1132 N N   . ALA A 158 ? 0.4362 0.5898 0.5437 -0.0777 0.0203  0.0231  175 ALA A N   
1133 C CA  . ALA A 158 ? 0.3946 0.5611 0.5171 -0.0804 0.0291  0.0257  175 ALA A CA  
1134 C C   . ALA A 158 ? 0.4678 0.6534 0.5995 -0.0731 0.0270  0.0248  175 ALA A C   
1135 O O   . ALA A 158 ? 0.4109 0.6150 0.5636 -0.0765 0.0293  0.0234  175 ALA A O   
1136 C CB  . ALA A 158 ? 0.4030 0.5553 0.5130 -0.0793 0.0404  0.0324  175 ALA A CB  
1137 N N   . ARG A 159 ? 0.3897 0.5710 0.5076 -0.0630 0.0231  0.0258  176 ARG A N   
1138 C CA  . ARG A 159 ? 0.3775 0.5743 0.5028 -0.0551 0.0216  0.0255  176 ARG A CA  
1139 C C   . ARG A 159 ? 0.4236 0.6305 0.5544 -0.0521 0.0096  0.0214  176 ARG A C   
1140 O O   . ARG A 159 ? 0.4127 0.6327 0.5511 -0.0453 0.0070  0.0210  176 ARG A O   
1141 C CB  . ARG A 159 ? 0.3909 0.5771 0.4992 -0.0453 0.0250  0.0290  176 ARG A CB  
1142 C CG  . ARG A 159 ? 0.5210 0.6949 0.6193 -0.0470 0.0359  0.0334  176 ARG A CG  
1143 C CD  . ARG A 159 ? 0.5159 0.6902 0.6070 -0.0379 0.0414  0.0355  176 ARG A CD  
1144 N NE  . ARG A 159 ? 0.5121 0.6764 0.5931 -0.0392 0.0526  0.0400  176 ARG A NE  
1145 C CZ  . ARG A 159 ? 0.5319 0.7062 0.6215 -0.0406 0.0635  0.0419  176 ARG A CZ  
1146 N NH1 . ARG A 159 ? 0.5207 0.7167 0.6328 -0.0418 0.0647  0.0394  176 ARG A NH1 
1147 N NH2 . ARG A 159 ? 0.5873 0.7494 0.6622 -0.0400 0.0736  0.0467  176 ARG A NH2 
1148 N N   . GLN A 160 ? 0.4095 0.6100 0.5358 -0.0566 0.0022  0.0183  177 GLN A N   
1149 C CA  . GLN A 160 ? 0.4821 0.6910 0.6108 -0.0542 -0.0094 0.0144  177 GLN A CA  
1150 C C   . GLN A 160 ? 0.4189 0.6257 0.5370 -0.0431 -0.0133 0.0169  177 GLN A C   
1151 O O   . GLN A 160 ? 0.5092 0.7301 0.6369 -0.0374 -0.0169 0.0167  177 GLN A O   
1152 C CB  . GLN A 160 ? 0.5501 0.7815 0.7029 -0.0580 -0.0128 0.0108  177 GLN A CB  
1153 C CG  . GLN A 160 ? 0.6263 0.8598 0.7914 -0.0699 -0.0123 0.0068  177 GLN A CG  
1154 C CD  . GLN A 160 ? 0.7078 0.9651 0.9009 -0.0740 -0.0142 0.0033  177 GLN A CD  
1155 O OE1 . GLN A 160 ? 0.7493 1.0198 0.9553 -0.0702 -0.0087 0.0055  177 GLN A OE1 
1156 N NE2 . GLN A 160 ? 0.7599 1.0230 0.9636 -0.0815 -0.0222 -0.0029 177 GLN A NE2 
1157 N N   . GLY A 161 ? 0.3517 0.5402 0.4512 -0.0399 -0.0122 0.0192  178 GLY A N   
1158 C CA  . GLY A 161 ? 0.3373 0.5215 0.4273 -0.0303 -0.0155 0.0216  178 GLY A CA  
1159 C C   . GLY A 161 ? 0.2953 0.4596 0.3677 -0.0287 -0.0144 0.0233  178 GLY A C   
1160 O O   . GLY A 161 ? 0.3659 0.5193 0.4327 -0.0344 -0.0112 0.0228  178 GLY A O   
1161 N N   . SER A 162 ? 0.3098 0.4692 0.3749 -0.0210 -0.0172 0.0253  179 SER A N   
1162 C CA  . SER A 162 ? 0.3080 0.4498 0.3597 -0.0188 -0.0159 0.0270  179 SER A CA  
1163 C C   . SER A 162 ? 0.3264 0.4605 0.3750 -0.0173 -0.0095 0.0287  179 SER A C   
1164 O O   . SER A 162 ? 0.3088 0.4509 0.3636 -0.0148 -0.0062 0.0293  179 SER A O   
1165 C CB  . SER A 162 ? 0.3004 0.4398 0.3478 -0.0114 -0.0202 0.0289  179 SER A CB  
1166 O OG  . SER A 162 ? 0.3153 0.4601 0.3619 -0.0119 -0.0261 0.0281  179 SER A OG  
1167 N N   . VAL A 163 ? 0.2986 0.4169 0.3372 -0.0180 -0.0079 0.0293  180 VAL A N   
1168 C CA  . VAL A 163 ? 0.2678 0.3766 0.3005 -0.0161 -0.0032 0.0308  180 VAL A CA  
1169 C C   . VAL A 163 ? 0.2658 0.3606 0.2900 -0.0114 -0.0055 0.0314  180 VAL A C   
1170 O O   . VAL A 163 ? 0.3212 0.4084 0.3420 -0.0137 -0.0074 0.0307  180 VAL A O   
1171 C CB  . VAL A 163 ? 0.3031 0.4066 0.3338 -0.0234 0.0017  0.0310  180 VAL A CB  
1172 C CG1 . VAL A 163 ? 0.3112 0.4029 0.3323 -0.0205 0.0063  0.0335  180 VAL A CG1 
1173 C CG2 . VAL A 163 ? 0.3029 0.4213 0.3454 -0.0289 0.0042  0.0302  180 VAL A CG2 
1174 N N   . LEU A 164 ? 0.2836 0.3751 0.3053 -0.0048 -0.0053 0.0321  181 LEU A N   
1175 C CA  . LEU A 164 ? 0.2741 0.3524 0.2898 -0.0003 -0.0077 0.0321  181 LEU A CA  
1176 C C   . LEU A 164 ? 0.3129 0.3805 0.3198 0.0000  -0.0051 0.0326  181 LEU A C   
1177 O O   . LEU A 164 ? 0.3007 0.3708 0.3046 0.0017  -0.0015 0.0331  181 LEU A O   
1178 C CB  . LEU A 164 ? 0.3088 0.3893 0.3276 0.0073  -0.0104 0.0319  181 LEU A CB  
1179 C CG  . LEU A 164 ? 0.3351 0.4279 0.3622 0.0089  -0.0124 0.0324  181 LEU A CG  
1180 C CD1 . LEU A 164 ? 0.3046 0.3961 0.3345 0.0168  -0.0149 0.0322  181 LEU A CD1 
1181 C CD2 . LEU A 164 ? 0.3306 0.4237 0.3587 0.0056  -0.0148 0.0332  181 LEU A CD2 
1182 N N   . GLY A 165 ? 0.2915 0.3465 0.2936 -0.0008 -0.0068 0.0324  182 GLY A N   
1183 C CA  . GLY A 165 ? 0.3145 0.3577 0.3070 0.0015  -0.0062 0.0331  182 GLY A CA  
1184 C C   . GLY A 165 ? 0.3335 0.3734 0.3234 0.0097  -0.0097 0.0316  182 GLY A C   
1185 O O   . GLY A 165 ? 0.2880 0.3287 0.2845 0.0130  -0.0138 0.0301  182 GLY A O   
1186 N N   . VAL A 166 ? 0.2917 0.3280 0.2718 0.0131  -0.0077 0.0321  183 VAL A N   
1187 C CA  . VAL A 166 ? 0.2821 0.3146 0.2581 0.0212  -0.0114 0.0296  183 VAL A CA  
1188 C C   . VAL A 166 ? 0.3464 0.3658 0.3071 0.0248  -0.0125 0.0298  183 VAL A C   
1189 O O   . VAL A 166 ? 0.3891 0.4038 0.3411 0.0214  -0.0081 0.0329  183 VAL A O   
1190 C CB  . VAL A 166 ? 0.3130 0.3569 0.2914 0.0243  -0.0081 0.0287  183 VAL A CB  
1191 C CG1 . VAL A 166 ? 0.3482 0.4034 0.3410 0.0231  -0.0095 0.0283  183 VAL A CG1 
1192 C CG2 . VAL A 166 ? 0.3279 0.3772 0.3009 0.0209  0.0003  0.0314  183 VAL A CG2 
1193 N N   . GLN A 167 ? 0.3631 0.3759 0.3201 0.0322  -0.0186 0.0263  184 GLN A N   
1194 C CA  . GLN A 167 ? 0.4076 0.4087 0.3475 0.0376  -0.0206 0.0256  184 GLN A CA  
1195 C C   . GLN A 167 ? 0.3882 0.3881 0.3262 0.0459  -0.0259 0.0204  184 GLN A C   
1196 O O   . GLN A 167 ? 0.3155 0.3205 0.2675 0.0471  -0.0297 0.0175  184 GLN A O   
1197 C CB  . GLN A 167 ? 0.4850 0.4728 0.4207 0.0374  -0.0263 0.0263  184 GLN A CB  
1198 C CG  . GLN A 167 ? 0.5364 0.5195 0.4819 0.0412  -0.0360 0.0219  184 GLN A CG  
1199 C CD  . GLN A 167 ? 0.7218 0.6930 0.6648 0.0412  -0.0412 0.0225  184 GLN A CD  
1200 O OE1 . GLN A 167 ? 0.8323 0.7999 0.7700 0.0368  -0.0369 0.0268  184 GLN A OE1 
1201 N NE2 . GLN A 167 ? 0.7052 0.6701 0.6530 0.0465  -0.0508 0.0181  184 GLN A NE2 
1202 N N   . GLU A 168 ? 0.3759 0.3685 0.2954 0.0517  -0.0256 0.0194  185 GLU A N   
1203 C CA  . GLU A 168 ? 0.4116 0.4001 0.3258 0.0604  -0.0317 0.0133  185 GLU A CA  
1204 C C   . GLU A 168 ? 0.3898 0.3683 0.3090 0.0635  -0.0437 0.0091  185 GLU A C   
1205 O O   . GLU A 168 ? 0.4017 0.3719 0.3176 0.0619  -0.0472 0.0111  185 GLU A O   
1206 C CB  . GLU A 168 ? 0.4124 0.3942 0.3021 0.0662  -0.0281 0.0132  185 GLU A CB  
1207 C CG  . GLU A 168 ? 0.4336 0.4265 0.3206 0.0637  -0.0150 0.0168  185 GLU A CG  
1208 C CD  . GLU A 168 ? 0.4567 0.4618 0.3554 0.0666  -0.0130 0.0127  185 GLU A CD  
1209 O OE1 . GLU A 168 ? 0.4739 0.4751 0.3736 0.0735  -0.0206 0.0062  185 GLU A OE1 
1210 O OE2 . GLU A 168 ? 0.4594 0.4779 0.3671 0.0623  -0.0039 0.0156  185 GLU A OE2 
1211 N N   . VAL A 169 ? 0.3521 0.3315 0.2811 0.0679  -0.0500 0.0032  186 VAL A N   
1212 C CA  . VAL A 169 ? 0.3897 0.3602 0.3257 0.0713  -0.0619 -0.0019 186 VAL A CA  
1213 C C   . VAL A 169 ? 0.4427 0.4075 0.3701 0.0802  -0.0685 -0.0095 186 VAL A C   
1214 O O   . VAL A 169 ? 0.4539 0.4233 0.3749 0.0833  -0.0633 -0.0110 186 VAL A O   
1215 C CB  . VAL A 169 ? 0.4462 0.4227 0.4079 0.0666  -0.0636 -0.0018 186 VAL A CB  
1216 C CG1 . VAL A 169 ? 0.4166 0.3980 0.3839 0.0585  -0.0569 0.0049  186 VAL A CG1 
1217 C CG2 . VAL A 169 ? 0.4207 0.4057 0.3927 0.0677  -0.0607 -0.0035 186 VAL A CG2 
1218 N N   . PRO A 170 ? 0.4383 0.3930 0.3660 0.0848  -0.0804 -0.0151 187 PRO A N   
1219 C CA  . PRO A 170 ? 0.4821 0.4306 0.4033 0.0933  -0.0884 -0.0240 187 PRO A CA  
1220 C C   . PRO A 170 ? 0.5252 0.4812 0.4654 0.0930  -0.0872 -0.0272 187 PRO A C   
1221 O O   . PRO A 170 ? 0.5250 0.4865 0.4881 0.0874  -0.0867 -0.0249 187 PRO A O   
1222 C CB  . PRO A 170 ? 0.4660 0.4043 0.3920 0.0962  -0.1026 -0.0291 187 PRO A CB  
1223 C CG  . PRO A 170 ? 0.5377 0.4739 0.4602 0.0918  -0.1008 -0.0223 187 PRO A CG  
1224 C CD  . PRO A 170 ? 0.4683 0.4162 0.4006 0.0830  -0.0874 -0.0141 187 PRO A CD  
1225 N N   . ARG A 171 ? 0.5094 0.4645 0.4395 0.0995  -0.0866 -0.0325 188 ARG A N   
1226 C CA  . ARG A 171 ? 0.5734 0.5348 0.5212 0.0998  -0.0851 -0.0352 188 ARG A CA  
1227 C C   . ARG A 171 ? 0.6643 0.6218 0.6359 0.0987  -0.0951 -0.0394 188 ARG A C   
1228 O O   . ARG A 171 ? 0.5863 0.5498 0.5784 0.0952  -0.0923 -0.0373 188 ARG A O   
1229 C CB  . ARG A 171 ? 0.5850 0.5440 0.5189 0.1084  -0.0847 -0.0421 188 ARG A CB  
1230 C CG  . ARG A 171 ? 0.5619 0.5261 0.5144 0.1097  -0.0836 -0.0451 188 ARG A CG  
1231 C CD  . ARG A 171 ? 0.5679 0.5327 0.5060 0.1176  -0.0791 -0.0504 188 ARG A CD  
1232 N NE  . ARG A 171 ? 0.6049 0.5814 0.5349 0.1154  -0.0654 -0.0433 188 ARG A NE  
1233 C CZ  . ARG A 171 ? 0.6765 0.6653 0.6217 0.1123  -0.0577 -0.0387 188 ARG A CZ  
1234 N NH1 . ARG A 171 ? 0.5458 0.5363 0.5132 0.1113  -0.0615 -0.0395 188 ARG A NH1 
1235 N NH2 . ARG A 171 ? 0.6490 0.6488 0.5877 0.1100  -0.0460 -0.0328 188 ARG A NH2 
1236 N N   . GLU A 172 ? 0.6854 0.6329 0.6551 0.1015  -0.1066 -0.0449 189 GLU A N   
1237 C CA  . GLU A 172 ? 0.7883 0.7322 0.7827 0.1002  -0.1163 -0.0494 189 GLU A CA  
1238 C C   . GLU A 172 ? 0.6620 0.6128 0.6780 0.0913  -0.1114 -0.0416 189 GLU A C   
1239 O O   . GLU A 172 ? 0.7969 0.7474 0.8374 0.0888  -0.1152 -0.0433 189 GLU A O   
1240 C CB  . GLU A 172 ? 0.9453 0.8780 0.9325 0.1052  -0.1303 -0.0570 189 GLU A CB  
1241 C CG  . GLU A 172 ? 1.1043 1.0282 1.0674 0.1151  -0.1366 -0.0661 189 GLU A CG  
1242 C CD  . GLU A 172 ? 1.0222 0.9452 0.9517 0.1184  -0.1289 -0.0618 189 GLU A CD  
1243 O OE1 . GLU A 172 ? 0.8308 0.7545 0.7526 0.1147  -0.1255 -0.0544 189 GLU A OE1 
1244 O OE2 . GLU A 172 ? 0.9374 0.8588 0.8488 0.1246  -0.1256 -0.0657 189 GLU A OE2 
1245 N N   . ASP A 173 ? 0.6368 0.5933 0.6445 0.0864  -0.1025 -0.0332 190 ASP A N   
1246 C CA  . ASP A 173 ? 0.5897 0.5519 0.6142 0.0786  -0.0977 -0.0263 190 ASP A CA  
1247 C C   . ASP A 173 ? 0.5603 0.5329 0.5922 0.0737  -0.0867 -0.0197 190 ASP A C   
1248 O O   . ASP A 173 ? 0.5844 0.5619 0.6270 0.0674  -0.0816 -0.0137 190 ASP A O   
1249 C CB  . ASP A 173 ? 0.6050 0.5664 0.6170 0.0759  -0.0953 -0.0215 190 ASP A CB  
1250 C CG  . ASP A 173 ? 0.7801 0.7319 0.7908 0.0794  -0.1068 -0.0263 190 ASP A CG  
1251 O OD1 . ASP A 173 ? 0.7573 0.7031 0.7740 0.0844  -0.1174 -0.0344 190 ASP A OD1 
1252 O OD2 . ASP A 173 ? 0.7509 0.7011 0.7557 0.0770  -0.1055 -0.0221 190 ASP A OD2 
1253 N N   . THR A 174 ? 0.5100 0.4862 0.5357 0.0770  -0.0829 -0.0206 191 THR A N   
1254 C CA  . THR A 174 ? 0.5034 0.4902 0.5336 0.0728  -0.0731 -0.0138 191 THR A CA  
1255 C C   . THR A 174 ? 0.4616 0.4504 0.5144 0.0691  -0.0725 -0.0109 191 THR A C   
1256 O O   . THR A 174 ? 0.4545 0.4511 0.5113 0.0646  -0.0653 -0.0043 191 THR A O   
1257 C CB  . THR A 174 ? 0.4656 0.4564 0.4868 0.0778  -0.0694 -0.0157 191 THR A CB  
1258 O OG1 . THR A 174 ? 0.4998 0.4843 0.5283 0.0838  -0.0763 -0.0230 191 THR A OG1 
1259 C CG2 . THR A 174 ? 0.4506 0.4412 0.4482 0.0805  -0.0663 -0.0163 191 THR A CG2 
1260 N N   . ARG A 175 ? 0.4665 0.4480 0.5339 0.0708  -0.0801 -0.0158 192 ARG A N   
1261 C CA  . ARG A 175 ? 0.5287 0.5104 0.6183 0.0671  -0.0790 -0.0128 192 ARG A CA  
1262 C C   . ARG A 175 ? 0.5123 0.4974 0.6083 0.0603  -0.0744 -0.0066 192 ARG A C   
1263 O O   . ARG A 175 ? 0.5526 0.5390 0.6642 0.0566  -0.0707 -0.0021 192 ARG A O   
1264 C CB  . ARG A 175 ? 0.6723 0.6446 0.7765 0.0702  -0.0889 -0.0206 192 ARG A CB  
1265 C CG  . ARG A 175 ? 0.8378 0.8082 0.9658 0.0681  -0.0883 -0.0189 192 ARG A CG  
1266 C CD  . ARG A 175 ? 1.1074 1.0683 1.2507 0.0707  -0.0994 -0.0281 192 ARG A CD  
1267 N NE  . ARG A 175 ? 1.1457 1.1005 1.2793 0.0781  -0.1070 -0.0374 192 ARG A NE  
1268 C CZ  . ARG A 175 ? 1.0216 0.9712 1.1425 0.0828  -0.1160 -0.0457 192 ARG A CZ  
1269 N NH1 . ARG A 175 ? 0.9246 0.8744 1.0405 0.0812  -0.1190 -0.0455 192 ARG A NH1 
1270 N NH2 . ARG A 175 ? 0.9467 0.8900 1.0591 0.0899  -0.1226 -0.0545 192 ARG A NH2 
1271 N N   . LYS A 176 ? 0.4965 0.4818 0.5805 0.0589  -0.0743 -0.0062 193 LYS A N   
1272 C CA  . LYS A 176 ? 0.4807 0.4686 0.5689 0.0530  -0.0698 -0.0011 193 LYS A CA  
1273 C C   . LYS A 176 ? 0.5188 0.5150 0.5974 0.0488  -0.0604 0.0058  193 LYS A C   
1274 O O   . LYS A 176 ? 0.4904 0.4889 0.5732 0.0439  -0.0558 0.0100  193 LYS A O   
1275 C CB  . LYS A 176 ? 0.6233 0.6062 0.7038 0.0538  -0.0748 -0.0041 193 LYS A CB  
1276 C CG  . LYS A 176 ? 0.5912 0.5666 0.6841 0.0569  -0.0852 -0.0108 193 LYS A CG  
1277 C CD  . LYS A 176 ? 0.7820 0.7527 0.8640 0.0583  -0.0900 -0.0125 193 LYS A CD  
1278 C CE  . LYS A 176 ? 0.9114 0.8744 1.0016 0.0631  -0.1030 -0.0205 193 LYS A CE  
1279 N NZ  . LYS A 176 ? 0.9764 0.9338 1.0527 0.0657  -0.1085 -0.0216 193 LYS A NZ  
1280 N N   . TYR A 177 ? 0.4978 0.4990 0.5642 0.0508  -0.0575 0.0067  194 TYR A N   
1281 C CA  . TYR A 177 ? 0.3939 0.4028 0.4491 0.0470  -0.0504 0.0116  194 TYR A CA  
1282 C C   . TYR A 177 ? 0.3794 0.3967 0.4349 0.0474  -0.0461 0.0147  194 TYR A C   
1283 O O   . TYR A 177 ? 0.4393 0.4560 0.4995 0.0520  -0.0484 0.0126  194 TYR A O   
1284 C CB  . TYR A 177 ? 0.5656 0.5732 0.6029 0.0484  -0.0506 0.0098  194 TYR A CB  
1285 C CG  . TYR A 177 ? 0.6081 0.6074 0.6421 0.0482  -0.0550 0.0078  194 TYR A CG  
1286 C CD1 . TYR A 177 ? 0.6551 0.6546 0.6926 0.0429  -0.0522 0.0111  194 TYR A CD1 
1287 C CD2 . TYR A 177 ? 0.6348 0.6259 0.6616 0.0539  -0.0623 0.0024  194 TYR A CD2 
1288 C CE1 . TYR A 177 ? 0.7245 0.7165 0.7605 0.0433  -0.0564 0.0094  194 TYR A CE1 
1289 C CE2 . TYR A 177 ? 0.7011 0.6844 0.7250 0.0543  -0.0673 0.0008  194 TYR A CE2 
1290 C CZ  . TYR A 177 ? 0.7018 0.6858 0.7312 0.0490  -0.0643 0.0045  194 TYR A CZ  
1291 O OH  . TYR A 177 ? 0.9462 0.9226 0.9742 0.0501  -0.0696 0.0030  194 TYR A OH  
1292 N N   . GLY A 178 ? 0.3565 0.3818 0.4072 0.0429  -0.0403 0.0194  195 GLY A N   
1293 C CA  . GLY A 178 ? 0.4198 0.4546 0.4678 0.0438  -0.0369 0.0216  195 GLY A CA  
1294 C C   . GLY A 178 ? 0.3409 0.3786 0.3769 0.0460  -0.0358 0.0189  195 GLY A C   
1295 O O   . GLY A 178 ? 0.3106 0.3461 0.3373 0.0435  -0.0344 0.0187  195 GLY A O   
1296 N N   . ILE A 179 ? 0.3648 0.4071 0.4013 0.0510  -0.0355 0.0173  196 ILE A N   
1297 C CA  . ILE A 179 ? 0.3378 0.3819 0.3635 0.0546  -0.0336 0.0141  196 ILE A CA  
1298 C C   . ILE A 179 ? 0.3204 0.3782 0.3475 0.0537  -0.0281 0.0167  196 ILE A C   
1299 O O   . ILE A 179 ? 0.3051 0.3688 0.3420 0.0555  -0.0287 0.0182  196 ILE A O   
1300 C CB  . ILE A 179 ? 0.3600 0.3969 0.3857 0.0624  -0.0384 0.0081  196 ILE A CB  
1301 C CG1 . ILE A 179 ? 0.3972 0.4212 0.4231 0.0632  -0.0451 0.0047  196 ILE A CG1 
1302 C CG2 . ILE A 179 ? 0.3499 0.3894 0.3633 0.0668  -0.0350 0.0051  196 ILE A CG2 
1303 C CD1 . ILE A 179 ? 0.4204 0.4388 0.4314 0.0617  -0.0453 0.0040  196 ILE A CD1 
1304 N N   . VAL A 180 ? 0.2861 0.3489 0.3045 0.0510  -0.0230 0.0175  197 VAL A N   
1305 C CA  A VAL A 180 ? 0.2865 0.3638 0.3087 0.0494  -0.0176 0.0196  197 VAL A CA  
1306 C CA  B VAL A 180 ? 0.2862 0.3635 0.3082 0.0493  -0.0175 0.0196  197 VAL A CA  
1307 C C   . VAL A 180 ? 0.3055 0.3866 0.3237 0.0557  -0.0141 0.0162  197 VAL A C   
1308 O O   . VAL A 180 ? 0.3119 0.3854 0.3176 0.0585  -0.0128 0.0135  197 VAL A O   
1309 C CB  A VAL A 180 ? 0.3026 0.3849 0.3216 0.0413  -0.0131 0.0229  197 VAL A CB  
1310 C CB  B VAL A 180 ? 0.3019 0.3831 0.3196 0.0414  -0.0129 0.0228  197 VAL A CB  
1311 C CG1 A VAL A 180 ? 0.3748 0.4558 0.3990 0.0358  -0.0159 0.0258  197 VAL A CG1 
1312 C CG1 B VAL A 180 ? 0.3432 0.4399 0.3665 0.0396  -0.0074 0.0240  197 VAL A CG1 
1313 C CG2 A VAL A 180 ? 0.3595 0.4328 0.3652 0.0401  -0.0108 0.0223  197 VAL A CG2 
1314 C CG2 B VAL A 180 ? 0.3794 0.4584 0.4017 0.0357  -0.0158 0.0255  197 VAL A CG2 
1315 N N   . ALA A 181 ? 0.3392 0.4320 0.3676 0.0586  -0.0126 0.0163  198 ALA A N   
1316 C CA  . ALA A 181 ? 0.3433 0.4440 0.3711 0.0639  -0.0073 0.0135  198 ALA A CA  
1317 C C   . ALA A 181 ? 0.3412 0.4569 0.3743 0.0579  -0.0008 0.0168  198 ALA A C   
1318 O O   . ALA A 181 ? 0.2809 0.4058 0.3254 0.0541  -0.0027 0.0197  198 ALA A O   
1319 C CB  . ALA A 181 ? 0.3453 0.4495 0.3840 0.0715  -0.0104 0.0111  198 ALA A CB  
1320 N N   . SER A 182 ? 0.3051 0.4226 0.3297 0.0568  0.0068  0.0165  199 SER A N   
1321 C CA  . SER A 182 ? 0.3278 0.4571 0.3574 0.0493  0.0134  0.0198  199 SER A CA  
1322 C C   . SER A 182 ? 0.3387 0.4735 0.3636 0.0519  0.0235  0.0186  199 SER A C   
1323 O O   . SER A 182 ? 0.3478 0.4739 0.3600 0.0590  0.0251  0.0154  199 SER A O   
1324 C CB  . SER A 182 ? 0.3289 0.4495 0.3506 0.0409  0.0128  0.0230  199 SER A CB  
1325 O OG  . SER A 182 ? 0.3288 0.4332 0.3326 0.0430  0.0130  0.0223  199 SER A OG  
1326 N N   . GLN A 183 ? 0.3413 0.4905 0.3765 0.0461  0.0304  0.0210  200 GLN A N   
1327 C CA  . GLN A 183 ? 0.4237 0.5791 0.4558 0.0468  0.0422  0.0211  200 GLN A CA  
1328 C C   . GLN A 183 ? 0.3661 0.5199 0.3943 0.0367  0.0482  0.0257  200 GLN A C   
1329 O O   . GLN A 183 ? 0.3504 0.5092 0.3892 0.0287  0.0447  0.0279  200 GLN A O   
1330 C CB  . GLN A 183 ? 0.3866 0.5630 0.4388 0.0492  0.0472  0.0196  200 GLN A CB  
1331 C CG  . GLN A 183 ? 0.4333 0.6115 0.4903 0.0600  0.0426  0.0149  200 GLN A CG  
1332 C CD  . GLN A 183 ? 0.4739 0.6381 0.5114 0.0689  0.0450  0.0111  200 GLN A CD  
1333 O OE1 . GLN A 183 ? 0.5191 0.6777 0.5414 0.0686  0.0536  0.0117  200 GLN A OE1 
1334 N NE2 . GLN A 183 ? 0.5039 0.6611 0.5411 0.0768  0.0369  0.0070  200 GLN A NE2 
1335 N N   . PRO A 184 ? 0.3215 0.4673 0.3335 0.0373  0.0571  0.0274  201 PRO A N   
1336 C CA  . PRO A 184 ? 0.3917 0.5329 0.3985 0.0280  0.0632  0.0325  201 PRO A CA  
1337 C C   . PRO A 184 ? 0.3738 0.5337 0.4025 0.0196  0.0700  0.0346  201 PRO A C   
1338 O O   . PRO A 184 ? 0.3491 0.5252 0.3913 0.0221  0.0768  0.0330  201 PRO A O   
1339 C CB  . PRO A 184 ? 0.4867 0.6169 0.4711 0.0328  0.0725  0.0338  201 PRO A CB  
1340 C CG  . PRO A 184 ? 0.5483 0.6709 0.5215 0.0442  0.0663  0.0285  201 PRO A CG  
1341 C CD  . PRO A 184 ? 0.4269 0.5651 0.4221 0.0470  0.0616  0.0245  201 PRO A CD  
1342 N N   . VAL A 185 ? 0.3468 0.5040 0.3791 0.0096  0.0688  0.0377  202 VAL A N   
1343 C CA  . VAL A 185 ? 0.3194 0.4910 0.3702 0.0001  0.0763  0.0399  202 VAL A CA  
1344 C C   . VAL A 185 ? 0.4376 0.5980 0.4765 -0.0062 0.0866  0.0454  202 VAL A C   
1345 O O   . VAL A 185 ? 0.4068 0.5782 0.4583 -0.0123 0.0976  0.0479  202 VAL A O   
1346 C CB  . VAL A 185 ? 0.4216 0.6010 0.4896 -0.0070 0.0664  0.0384  202 VAL A CB  
1347 C CG1 . VAL A 185 ? 0.4604 0.6553 0.5495 -0.0166 0.0731  0.0395  202 VAL A CG1 
1348 C CG2 . VAL A 185 ? 0.4339 0.6231 0.5120 -0.0003 0.0567  0.0342  202 VAL A CG2 
1349 N N   . ASP A 186 ? 0.4127 0.5517 0.4286 -0.0048 0.0834  0.0477  203 ASP A N   
1350 C CA  . ASP A 186 ? 0.4062 0.5305 0.4047 -0.0079 0.0927  0.0536  203 ASP A CA  
1351 C C   . ASP A 186 ? 0.4014 0.5041 0.3728 0.0001  0.0858  0.0535  203 ASP A C   
1352 O O   . ASP A 186 ? 0.3819 0.4837 0.3503 0.0080  0.0766  0.0486  203 ASP A O   
1353 C CB  . ASP A 186 ? 0.3987 0.5224 0.4085 -0.0205 0.0948  0.0571  203 ASP A CB  
1354 C CG  . ASP A 186 ? 0.4111 0.5252 0.4202 -0.0237 0.0818  0.0553  203 ASP A CG  
1355 O OD1 . ASP A 186 ? 0.3908 0.4910 0.3834 -0.0170 0.0735  0.0540  203 ASP A OD1 
1356 O OD2 . ASP A 186 ? 0.4488 0.5696 0.4748 -0.0330 0.0799  0.0547  203 ASP A OD2 
1357 N N   . ALA A 187 ? 0.4012 0.4862 0.3530 -0.0015 0.0903  0.0589  204 ALA A N   
1358 C CA  . ALA A 187 ? 0.4381 0.5032 0.3632 0.0071  0.0843  0.0588  204 ALA A CA  
1359 C C   . ALA A 187 ? 0.3801 0.4377 0.3067 0.0082  0.0690  0.0551  204 ALA A C   
1360 O O   . ALA A 187 ? 0.4074 0.4530 0.3182 0.0165  0.0613  0.0525  204 ALA A O   
1361 C CB  . ALA A 187 ? 0.4065 0.4536 0.3096 0.0055  0.0920  0.0662  204 ALA A CB  
1362 N N   . ARG A 188 ? 0.3910 0.4545 0.3354 0.0000  0.0646  0.0546  205 ARG A N   
1363 C CA  . ARG A 188 ? 0.4085 0.4654 0.3550 0.0006  0.0519  0.0515  205 ARG A CA  
1364 C C   . ARG A 188 ? 0.3510 0.4235 0.3179 -0.0005 0.0456  0.0468  205 ARG A C   
1365 O O   . ARG A 188 ? 0.3435 0.4116 0.3103 0.0032  0.0358  0.0436  205 ARG A O   
1366 C CB  . ARG A 188 ? 0.4304 0.4759 0.3756 -0.0073 0.0511  0.0551  205 ARG A CB  
1367 C CG  . ARG A 188 ? 0.4599 0.4853 0.3823 -0.0048 0.0538  0.0601  205 ARG A CG  
1368 C CD  . ARG A 188 ? 0.4895 0.5016 0.4108 -0.0115 0.0518  0.0633  205 ARG A CD  
1369 N NE  . ARG A 188 ? 0.5177 0.5098 0.4161 -0.0080 0.0537  0.0687  205 ARG A NE  
1370 C CZ  . ARG A 188 ? 0.5973 0.5749 0.4806 -0.0002 0.0448  0.0677  205 ARG A CZ  
1371 N NH1 . ARG A 188 ? 0.5052 0.4852 0.3952 0.0040  0.0337  0.0616  205 ARG A NH1 
1372 N NH2 . ARG A 188 ? 0.6025 0.5624 0.4635 0.0035  0.0469  0.0732  205 ARG A NH2 
1373 N N   . THR A 189 ? 0.3393 0.4298 0.3234 -0.0045 0.0508  0.0462  206 THR A N   
1374 C CA  . THR A 189 ? 0.3698 0.4745 0.3725 -0.0059 0.0442  0.0425  206 THR A CA  
1375 C C   . THR A 189 ? 0.3694 0.4873 0.3790 0.0015  0.0449  0.0395  206 THR A C   
1376 O O   . THR A 189 ? 0.3608 0.4847 0.3695 0.0038  0.0539  0.0403  206 THR A O   
1377 C CB  . THR A 189 ? 0.3411 0.4568 0.3606 -0.0164 0.0470  0.0433  206 THR A CB  
1378 O OG1 . THR A 189 ? 0.3137 0.4151 0.3261 -0.0225 0.0460  0.0455  206 THR A OG1 
1379 C CG2 . THR A 189 ? 0.3839 0.5130 0.4195 -0.0171 0.0390  0.0395  206 THR A CG2 
1380 N N   . GLU A 190 ? 0.3667 0.4884 0.3831 0.0055  0.0358  0.0362  207 GLU A N   
1381 C CA  . GLU A 190 ? 0.3643 0.4959 0.3872 0.0135  0.0344  0.0331  207 GLU A CA  
1382 C C   . GLU A 190 ? 0.3209 0.4658 0.3616 0.0119  0.0279  0.0316  207 GLU A C   
1383 O O   . GLU A 190 ? 0.3056 0.4473 0.3480 0.0070  0.0221  0.0321  207 GLU A O   
1384 C CB  . GLU A 190 ? 0.3409 0.4583 0.3496 0.0223  0.0289  0.0310  207 GLU A CB  
1385 C CG  . GLU A 190 ? 0.4675 0.5702 0.4560 0.0241  0.0337  0.0325  207 GLU A CG  
1386 C CD  . GLU A 190 ? 0.5129 0.6125 0.4909 0.0342  0.0355  0.0293  207 GLU A CD  
1387 O OE1 . GLU A 190 ? 0.4429 0.5508 0.4304 0.0401  0.0327  0.0256  207 GLU A OE1 
1388 O OE2 . GLU A 190 ? 0.5070 0.5956 0.4667 0.0363  0.0401  0.0307  207 GLU A OE2 
1389 N N   . ARG A 191 ? 0.3136 0.4733 0.3667 0.0166  0.0289  0.0297  208 ARG A N   
1390 C CA  . ARG A 191 ? 0.3377 0.5093 0.4059 0.0174  0.0216  0.0285  208 ARG A CA  
1391 C C   . ARG A 191 ? 0.3346 0.4982 0.3978 0.0261  0.0146  0.0270  208 ARG A C   
1392 O O   . ARG A 191 ? 0.3039 0.4658 0.3638 0.0339  0.0168  0.0250  208 ARG A O   
1393 C CB  . ARG A 191 ? 0.4183 0.6109 0.5052 0.0180  0.0258  0.0273  208 ARG A CB  
1394 C CG  . ARG A 191 ? 0.4504 0.6555 0.5525 0.0187  0.0171  0.0264  208 ARG A CG  
1395 C CD  . ARG A 191 ? 0.6387 0.8657 0.7618 0.0198  0.0203  0.0249  208 ARG A CD  
1396 N NE  . ARG A 191 ? 0.6513 0.8854 0.7804 0.0124  0.0304  0.0254  208 ARG A NE  
1397 C CZ  . ARG A 191 ? 0.6575 0.8973 0.7951 0.0023  0.0302  0.0260  208 ARG A CZ  
1398 N NH1 . ARG A 191 ? 0.5974 0.8396 0.7397 -0.0011 0.0199  0.0252  208 ARG A NH1 
1399 N NH2 . ARG A 191 ? 0.4955 0.7377 0.6363 -0.0044 0.0407  0.0273  208 ARG A NH2 
1400 N N   . VAL A 192 ? 0.2868 0.4451 0.3497 0.0249  0.0065  0.0278  209 VAL A N   
1401 C CA  . VAL A 192 ? 0.2971 0.4461 0.3562 0.0320  0.0003  0.0271  209 VAL A CA  
1402 C C   . VAL A 192 ? 0.2713 0.4325 0.3435 0.0380  -0.0028 0.0265  209 VAL A C   
1403 O O   . VAL A 192 ? 0.2989 0.4729 0.3820 0.0352  -0.0050 0.0275  209 VAL A O   
1404 C CB  . VAL A 192 ? 0.3345 0.4728 0.3883 0.0283  -0.0055 0.0289  209 VAL A CB  
1405 C CG1 . VAL A 192 ? 0.3114 0.4409 0.3644 0.0351  -0.0110 0.0287  209 VAL A CG1 
1406 C CG2 . VAL A 192 ? 0.3227 0.4488 0.3646 0.0234  -0.0025 0.0292  209 VAL A CG2 
1407 N N   . THR A 193 ? 0.3032 0.4597 0.3745 0.0466  -0.0038 0.0245  210 THR A N   
1408 C CA  . THR A 193 ? 0.3060 0.4709 0.3891 0.0537  -0.0073 0.0240  210 THR A CA  
1409 C C   . THR A 193 ? 0.2948 0.4473 0.3756 0.0585  -0.0141 0.0250  210 THR A C   
1410 O O   . THR A 193 ? 0.2744 0.4320 0.3641 0.0623  -0.0188 0.0267  210 THR A O   
1411 C CB  . THR A 193 ? 0.3019 0.4732 0.3888 0.0608  -0.0015 0.0203  210 THR A CB  
1412 O OG1 . THR A 193 ? 0.3025 0.4585 0.3764 0.0654  -0.0005 0.0174  210 THR A OG1 
1413 C CG2 . THR A 193 ? 0.2796 0.4638 0.3703 0.0559  0.0072  0.0200  210 THR A CG2 
1414 N N   . HIS A 194 ? 0.2789 0.4152 0.3489 0.0585  -0.0150 0.0240  211 HIS A N   
1415 C CA  . HIS A 194 ? 0.2543 0.3782 0.3243 0.0624  -0.0207 0.0248  211 HIS A CA  
1416 C C   . HIS A 194 ? 0.2914 0.4014 0.3516 0.0576  -0.0217 0.0251  211 HIS A C   
1417 O O   . HIS A 194 ? 0.2707 0.3778 0.3222 0.0543  -0.0183 0.0235  211 HIS A O   
1418 C CB  . HIS A 194 ? 0.3078 0.4262 0.3796 0.0716  -0.0215 0.0205  211 HIS A CB  
1419 C CG  . HIS A 194 ? 0.3613 0.4929 0.4432 0.0778  -0.0197 0.0190  211 HIS A CG  
1420 N ND1 . HIS A 194 ? 0.3399 0.4817 0.4216 0.0789  -0.0131 0.0159  211 HIS A ND1 
1421 C CD2 . HIS A 194 ? 0.3329 0.4692 0.4262 0.0835  -0.0234 0.0205  211 HIS A CD2 
1422 C CE1 . HIS A 194 ? 0.3827 0.5358 0.4765 0.0851  -0.0127 0.0149  211 HIS A CE1 
1423 N NE2 . HIS A 194 ? 0.3765 0.5262 0.4773 0.0883  -0.0195 0.0176  211 HIS A NE2 
1424 N N   . ILE A 195 ? 0.2832 0.3843 0.3454 0.0576  -0.0260 0.0274  212 ILE A N   
1425 C CA  . ILE A 195 ? 0.2777 0.3657 0.3337 0.0541  -0.0272 0.0272  212 ILE A CA  
1426 C C   . ILE A 195 ? 0.3272 0.4045 0.3892 0.0586  -0.0314 0.0270  212 ILE A C   
1427 O O   . ILE A 195 ? 0.3292 0.4088 0.3987 0.0619  -0.0332 0.0297  212 ILE A O   
1428 C CB  . ILE A 195 ? 0.3544 0.4444 0.4078 0.0463  -0.0262 0.0309  212 ILE A CB  
1429 C CG1 . ILE A 195 ? 0.3603 0.4381 0.4086 0.0428  -0.0268 0.0303  212 ILE A CG1 
1430 C CG2 . ILE A 195 ? 0.4193 0.5125 0.4783 0.0465  -0.0285 0.0354  212 ILE A CG2 
1431 C CD1 . ILE A 195 ? 0.4330 0.5135 0.4766 0.0352  -0.0245 0.0325  212 ILE A CD1 
1432 N N   . VAL A 196 ? 0.2905 0.3559 0.3498 0.0593  -0.0334 0.0236  213 VAL A N   
1433 C CA  . VAL A 196 ? 0.3453 0.4000 0.4125 0.0630  -0.0376 0.0224  213 VAL A CA  
1434 C C   . VAL A 196 ? 0.4021 0.4467 0.4692 0.0589  -0.0393 0.0221  213 VAL A C   
1435 O O   . VAL A 196 ? 0.3522 0.3941 0.4112 0.0570  -0.0393 0.0192  213 VAL A O   
1436 C CB  . VAL A 196 ? 0.3851 0.4359 0.4528 0.0707  -0.0400 0.0161  213 VAL A CB  
1437 C CG1 . VAL A 196 ? 0.3979 0.4443 0.4541 0.0713  -0.0403 0.0104  213 VAL A CG1 
1438 C CG2 . VAL A 196 ? 0.4475 0.4875 0.5260 0.0742  -0.0446 0.0149  213 VAL A CG2 
1439 N N   . GLU A 197 ? 0.3719 0.4106 0.4486 0.0579  -0.0405 0.0253  214 GLU A N   
1440 C CA  . GLU A 197 ? 0.3832 0.4139 0.4636 0.0538  -0.0413 0.0255  214 GLU A CA  
1441 C C   . GLU A 197 ? 0.4059 0.4259 0.4942 0.0574  -0.0467 0.0197  214 GLU A C   
1442 O O   . GLU A 197 ? 0.3989 0.4147 0.4971 0.0611  -0.0488 0.0194  214 GLU A O   
1443 C CB  . GLU A 197 ? 0.4319 0.4626 0.5185 0.0503  -0.0381 0.0325  214 GLU A CB  
1444 C CG  . GLU A 197 ? 0.4975 0.5219 0.5891 0.0456  -0.0369 0.0335  214 GLU A CG  
1445 C CD  . GLU A 197 ? 0.6012 0.6282 0.6833 0.0414  -0.0355 0.0319  214 GLU A CD  
1446 O OE1 . GLU A 197 ? 0.6163 0.6511 0.6876 0.0402  -0.0336 0.0325  214 GLU A OE1 
1447 O OE2 . GLU A 197 ? 0.8036 0.8247 0.8903 0.0392  -0.0361 0.0302  214 GLU A OE2 
1448 N N   . LYS A 198 ? 0.4932 0.4213 0.4686 0.0608  -0.0244 0.0286  215 LYS A N   
1449 C CA  . LYS A 198 ? 0.5356 0.4529 0.5247 0.0541  -0.0297 0.0262  215 LYS A CA  
1450 C C   . LYS A 198 ? 0.5387 0.4391 0.5126 0.0589  -0.0366 0.0248  215 LYS A C   
1451 O O   . LYS A 198 ? 0.5456 0.4296 0.5227 0.0553  -0.0355 0.0253  215 LYS A O   
1452 C CB  . LYS A 198 ? 0.5852 0.4948 0.5898 0.0454  -0.0209 0.0287  215 LYS A CB  
1453 C CG  . LYS A 198 ? 0.5817 0.5078 0.6054 0.0393  -0.0153 0.0291  215 LYS A CG  
1454 C CD  . LYS A 198 ? 0.7196 0.6379 0.7605 0.0302  -0.0061 0.0312  215 LYS A CD  
1455 C CE  . LYS A 198 ? 0.8011 0.7365 0.8639 0.0235  -0.0021 0.0305  215 LYS A CE  
1456 N NZ  . LYS A 198 ? 0.9968 0.9439 1.0491 0.0283  0.0051  0.0339  215 LYS A NZ  
1457 N N   . PRO A 199 ? 0.4743 0.3787 0.4333 0.0668  -0.0436 0.0226  216 PRO A N   
1458 C CA  . PRO A 199 ? 0.5267 0.4157 0.4710 0.0719  -0.0506 0.0208  216 PRO A CA  
1459 C C   . PRO A 199 ? 0.6061 0.4875 0.5649 0.0664  -0.0592 0.0169  216 PRO A C   
1460 O O   . PRO A 199 ? 0.5795 0.4702 0.5573 0.0605  -0.0624 0.0143  216 PRO A O   
1461 C CB  . PRO A 199 ? 0.5422 0.4409 0.4704 0.0811  -0.0553 0.0190  216 PRO A CB  
1462 C CG  . PRO A 199 ? 0.5097 0.4280 0.4530 0.0775  -0.0556 0.0176  216 PRO A CG  
1463 C CD  . PRO A 199 ? 0.4766 0.3998 0.4342 0.0706  -0.0462 0.0209  216 PRO A CD  
1464 N N   . ALA A 200 ? 0.5583 0.4221 0.5077 0.0688  -0.0636 0.0159  217 ALA A N   
1465 C CA  . ALA A 200 ? 0.5888 0.4447 0.5473 0.0664  -0.0742 0.0109  217 ALA A CA  
1466 C C   . ALA A 200 ? 0.6426 0.5089 0.5956 0.0715  -0.0833 0.0072  217 ALA A C   
1467 O O   . ALA A 200 ? 0.5491 0.4211 0.4835 0.0795  -0.0830 0.0081  217 ALA A O   
1468 C CB  . ALA A 200 ? 0.6356 0.4710 0.5813 0.0700  -0.0775 0.0106  217 ALA A CB  
1469 N N   . PRO A 201 ? 0.6325 0.5012 0.6013 0.0673  -0.0913 0.0028  218 PRO A N   
1470 C CA  . PRO A 201 ? 0.6036 0.4809 0.5652 0.0725  -0.0991 -0.0002 218 PRO A CA  
1471 C C   . PRO A 201 ? 0.6186 0.4873 0.5558 0.0823  -0.1048 -0.0015 218 PRO A C   
1472 O O   . PRO A 201 ? 0.6156 0.4935 0.5397 0.0885  -0.1049 -0.0013 218 PRO A O   
1473 C CB  . PRO A 201 ? 0.6940 0.5692 0.6757 0.0667  -0.1080 -0.0053 218 PRO A CB  
1474 C CG  . PRO A 201 ? 0.7416 0.6182 0.7468 0.0567  -0.1006 -0.0038 218 PRO A CG  
1475 C CD  . PRO A 201 ? 0.6290 0.4954 0.6243 0.0575  -0.0921 0.0006  218 PRO A CD  
1476 N N   . GLU A 202 ? 0.6020 0.4534 0.5335 0.0838  -0.1090 -0.0028 219 GLU A N   
1477 C CA  . GLU A 202 ? 0.6820 0.5241 0.5903 0.0932  -0.1146 -0.0042 219 GLU A CA  
1478 C C   . GLU A 202 ? 0.6500 0.4964 0.5396 0.0996  -0.1066 -0.0003 219 GLU A C   
1479 O O   . GLU A 202 ? 0.6636 0.5071 0.5339 0.1081  -0.1099 -0.0016 219 GLU A O   
1480 C CB  . GLU A 202 ? 0.8535 0.6757 0.7622 0.0927  -0.1210 -0.0068 219 GLU A CB  
1481 C CG  . GLU A 202 ? 0.9520 0.7686 0.8810 0.0868  -0.1303 -0.0120 219 GLU A CG  
1482 C CD  . GLU A 202 ? 1.0224 0.8427 0.9787 0.0757  -0.1244 -0.0110 219 GLU A CD  
1483 O OE1 . GLU A 202 ? 0.7964 0.6181 0.7549 0.0722  -0.1130 -0.0060 219 GLU A OE1 
1484 O OE2 . GLU A 202 ? 1.0606 0.8824 1.0362 0.0707  -0.1311 -0.0156 219 GLU A OE2 
1485 N N   . GLN A 203 ? 0.6417 0.4942 0.5364 0.0962  -0.0963 0.0040  220 GLN A N   
1486 C CA  . GLN A 203 ? 0.6347 0.4901 0.5123 0.1026  -0.0893 0.0071  220 GLN A CA  
1487 C C   . GLN A 203 ? 0.5929 0.4682 0.4746 0.1025  -0.0821 0.0090  220 GLN A C   
1488 O O   . GLN A 203 ? 0.5432 0.4227 0.4133 0.1077  -0.0761 0.0111  220 GLN A O   
1489 C CB  . GLN A 203 ? 0.5629 0.4046 0.4383 0.1007  -0.0835 0.0104  220 GLN A CB  
1490 C CG  . GLN A 203 ? 0.6068 0.4280 0.4767 0.1017  -0.0902 0.0084  220 GLN A CG  
1491 C CD  . GLN A 203 ? 0.6424 0.4493 0.5135 0.0980  -0.0834 0.0121  220 GLN A CD  
1492 O OE1 . GLN A 203 ? 0.6779 0.4894 0.5595 0.0923  -0.0743 0.0157  220 GLN A OE1 
1493 N NE2 . GLN A 203 ? 0.6594 0.4480 0.5193 0.1014  -0.0872 0.0114  220 GLN A NE2 
1494 N N   . ALA A 204 ? 0.5736 0.4611 0.4712 0.0973  -0.0833 0.0079  221 ALA A N   
1495 C CA  . ALA A 204 ? 0.5791 0.4855 0.4821 0.0967  -0.0764 0.0097  221 ALA A CA  
1496 C C   . ALA A 204 ? 0.5230 0.4377 0.4101 0.1057  -0.0769 0.0083  221 ALA A C   
1497 O O   . ALA A 204 ? 0.5094 0.4205 0.3886 0.1097  -0.0837 0.0053  221 ALA A O   
1498 C CB  . ALA A 204 ? 0.4819 0.3984 0.4055 0.0892  -0.0781 0.0085  221 ALA A CB  
1499 N N   . PRO A 205 ? 0.5142 0.4388 0.3955 0.1098  -0.0698 0.0099  222 PRO A N   
1500 C CA  . PRO A 205 ? 0.5228 0.4553 0.3907 0.1184  -0.0700 0.0078  222 PRO A CA  
1501 C C   . PRO A 205 ? 0.5077 0.4528 0.3822 0.1177  -0.0720 0.0058  222 PRO A C   
1502 O O   . PRO A 205 ? 0.4881 0.4351 0.3515 0.1242  -0.0739 0.0034  222 PRO A O   
1503 C CB  . PRO A 205 ? 0.5067 0.4482 0.3720 0.1217  -0.0622 0.0095  222 PRO A CB  
1504 C CG  . PRO A 205 ? 0.5407 0.4859 0.4220 0.1135  -0.0575 0.0125  222 PRO A CG  
1505 C CD  . PRO A 205 ? 0.4777 0.4074 0.3648 0.1071  -0.0614 0.0133  222 PRO A CD  
1506 N N   . THR A 206 ? 0.4399 0.3937 0.3321 0.1102  -0.0707 0.0068  223 THR A N   
1507 C CA  . THR A 206 ? 0.4436 0.4088 0.3434 0.1086  -0.0721 0.0054  223 THR A CA  
1508 C C   . THR A 206 ? 0.4134 0.3785 0.3318 0.0994  -0.0744 0.0060  223 THR A C   
1509 O O   . THR A 206 ? 0.4299 0.3863 0.3549 0.0946  -0.0744 0.0072  223 THR A O   
1510 C CB  . THR A 206 ? 0.4579 0.4421 0.3613 0.1107  -0.0651 0.0058  223 THR A CB  
1511 O OG1 . THR A 206 ? 0.4229 0.4158 0.3418 0.1044  -0.0600 0.0081  223 THR A OG1 
1512 C CG2 . THR A 206 ? 0.4502 0.4352 0.3388 0.1194  -0.0617 0.0049  223 THR A CG2 
1513 N N   . THR A 207 ? 0.4030 0.3777 0.3303 0.0969  -0.0760 0.0049  224 THR A N   
1514 C CA  . THR A 207 ? 0.3833 0.3611 0.3303 0.0882  -0.0777 0.0050  224 THR A CA  
1515 C C   . THR A 207 ? 0.3656 0.3624 0.3249 0.0853  -0.0712 0.0064  224 THR A C   
1516 O O   . THR A 207 ? 0.3733 0.3763 0.3466 0.0800  -0.0732 0.0057  224 THR A O   
1517 C CB  . THR A 207 ? 0.4430 0.4128 0.3908 0.0875  -0.0874 0.0019  224 THR A CB  
1518 O OG1 . THR A 207 ? 0.4271 0.4023 0.3647 0.0929  -0.0881 0.0009  224 THR A OG1 
1519 C CG2 . THR A 207 ? 0.4388 0.3896 0.3768 0.0899  -0.0945 0.0000  224 THR A CG2 
1520 N N   . LEU A 208 ? 0.3617 0.3677 0.3157 0.0892  -0.0638 0.0080  225 LEU A N   
1521 C CA  . LEU A 208 ? 0.3878 0.4122 0.3532 0.0873  -0.0575 0.0089  225 LEU A CA  
1522 C C   . LEU A 208 ? 0.3464 0.3728 0.3224 0.0823  -0.0522 0.0114  225 LEU A C   
1523 O O   . LEU A 208 ? 0.3540 0.3761 0.3211 0.0857  -0.0482 0.0128  225 LEU A O   
1524 C CB  . LEU A 208 ? 0.3733 0.4071 0.3280 0.0951  -0.0531 0.0082  225 LEU A CB  
1525 C CG  . LEU A 208 ? 0.3515 0.4050 0.3183 0.0939  -0.0475 0.0082  225 LEU A CG  
1526 C CD1 . LEU A 208 ? 0.3895 0.4485 0.3663 0.0896  -0.0503 0.0076  225 LEU A CD1 
1527 C CD2 . LEU A 208 ? 0.4379 0.5001 0.3960 0.1018  -0.0433 0.0066  225 LEU A CD2 
1528 N N   . ALA A 209 ? 0.3171 0.3497 0.3115 0.0745  -0.0520 0.0117  226 ALA A N   
1529 C CA  . ALA A 209 ? 0.3372 0.3700 0.3434 0.0687  -0.0470 0.0139  226 ALA A CA  
1530 C C   . ALA A 209 ? 0.3082 0.3589 0.3240 0.0677  -0.0403 0.0150  226 ALA A C   
1531 O O   . ALA A 209 ? 0.3073 0.3708 0.3304 0.0671  -0.0413 0.0137  226 ALA A O   
1532 C CB  . ALA A 209 ? 0.2890 0.3155 0.3114 0.0603  -0.0515 0.0128  226 ALA A CB  
1533 N N   . VAL A 210 ? 0.3690 0.4192 0.3843 0.0676  -0.0334 0.0174  227 VAL A N   
1534 C CA  . VAL A 210 ? 0.2592 0.3245 0.2840 0.0665  -0.0269 0.0185  227 VAL A CA  
1535 C C   . VAL A 210 ? 0.2943 0.3652 0.3407 0.0571  -0.0270 0.0185  227 VAL A C   
1536 O O   . VAL A 210 ? 0.3323 0.3924 0.3859 0.0512  -0.0280 0.0189  227 VAL A O   
1537 C CB  . VAL A 210 ? 0.3300 0.3896 0.3451 0.0699  -0.0200 0.0211  227 VAL A CB  
1538 C CG1 . VAL A 210 ? 0.3397 0.4144 0.3640 0.0693  -0.0135 0.0220  227 VAL A CG1 
1539 C CG2 . VAL A 210 ? 0.3306 0.3844 0.3247 0.0796  -0.0209 0.0204  227 VAL A CG2 
1540 N N   . VAL A 211 ? 0.2487 0.3364 0.3068 0.0555  -0.0260 0.0176  228 VAL A N   
1541 C CA  . VAL A 211 ? 0.2779 0.3727 0.3571 0.0470  -0.0251 0.0174  228 VAL A CA  
1542 C C   . VAL A 211 ? 0.2625 0.3671 0.3461 0.0471  -0.0167 0.0194  228 VAL A C   
1543 O O   . VAL A 211 ? 0.3314 0.4389 0.4025 0.0542  -0.0129 0.0201  228 VAL A O   
1544 C CB  . VAL A 211 ? 0.3035 0.4089 0.3935 0.0447  -0.0307 0.0149  228 VAL A CB  
1545 C CG1 . VAL A 211 ? 0.3942 0.4892 0.4729 0.0478  -0.0389 0.0130  228 VAL A CG1 
1546 C CG2 . VAL A 211 ? 0.3095 0.4322 0.4013 0.0480  -0.0273 0.0146  228 VAL A CG2 
1547 N N   . GLY A 212 ? 0.2741 0.3836 0.3758 0.0397  -0.0140 0.0197  229 GLY A N   
1548 C CA  . GLY A 212 ? 0.2534 0.3703 0.3595 0.0393  -0.0056 0.0217  229 GLY A CA  
1549 C C   . GLY A 212 ? 0.2444 0.3805 0.3552 0.0424  -0.0041 0.0206  229 GLY A C   
1550 O O   . GLY A 212 ? 0.2067 0.3537 0.3332 0.0377  -0.0012 0.0204  229 GLY A O   
1551 N N   . ARG A 213 ? 0.2081 0.3483 0.3058 0.0503  -0.0059 0.0194  230 ARG A N   
1552 C CA  . ARG A 213 ? 0.2482 0.4059 0.3494 0.0544  -0.0044 0.0178  230 ARG A CA  
1553 C C   . ARG A 213 ? 0.2461 0.4011 0.3285 0.0644  -0.0030 0.0174  230 ARG A C   
1554 O O   . ARG A 213 ? 0.2608 0.4081 0.3310 0.0684  -0.0067 0.0165  230 ARG A O   
1555 C CB  . ARG A 213 ? 0.1668 0.3348 0.2770 0.0528  -0.0098 0.0153  230 ARG A CB  
1556 C CG  . ARG A 213 ? 0.1903 0.3617 0.3194 0.0437  -0.0126 0.0149  230 ARG A CG  
1557 C CD  . ARG A 213 ? 0.1886 0.3728 0.3327 0.0402  -0.0079 0.0151  230 ARG A CD  
1558 N NE  . ARG A 213 ? 0.1431 0.3325 0.3060 0.0322  -0.0114 0.0139  230 ARG A NE  
1559 C CZ  . ARG A 213 ? 0.1399 0.3214 0.3127 0.0252  -0.0125 0.0141  230 ARG A CZ  
1560 N NH1 . ARG A 213 ? 0.2100 0.3775 0.3766 0.0243  -0.0094 0.0159  230 ARG A NH1 
1561 N NH2 . ARG A 213 ? 0.1690 0.3564 0.3589 0.0190  -0.0168 0.0120  230 ARG A NH2 
1562 N N   . TYR A 214 ? 0.1959 0.3569 0.2757 0.0688  0.0021  0.0175  231 TYR A N   
1563 C CA  . TYR A 214 ? 0.2434 0.4019 0.3059 0.0791  0.0031  0.0164  231 TYR A CA  
1564 C C   . TYR A 214 ? 0.2462 0.4221 0.3144 0.0842  0.0050  0.0136  231 TYR A C   
1565 O O   . TYR A 214 ? 0.2712 0.4569 0.3525 0.0804  0.0078  0.0139  231 TYR A O   
1566 C CB  . TYR A 214 ? 0.2547 0.3964 0.3019 0.0818  0.0073  0.0195  231 TYR A CB  
1567 C CG  . TYR A 214 ? 0.2536 0.3771 0.2974 0.0760  0.0070  0.0226  231 TYR A CG  
1568 C CD1 . TYR A 214 ? 0.2410 0.3631 0.3000 0.0663  0.0088  0.0244  231 TYR A CD1 
1569 C CD2 . TYR A 214 ? 0.2819 0.3896 0.3079 0.0806  0.0049  0.0231  231 TYR A CD2 
1570 C CE1 . TYR A 214 ? 0.2685 0.3744 0.3265 0.0611  0.0086  0.0265  231 TYR A CE1 
1571 C CE2 . TYR A 214 ? 0.2765 0.3675 0.3005 0.0753  0.0046  0.0256  231 TYR A CE2 
1572 C CZ  . TYR A 214 ? 0.2596 0.3498 0.3001 0.0655  0.0066  0.0272  231 TYR A CZ  
1573 O OH  . TYR A 214 ? 0.3861 0.4599 0.4271 0.0600  0.0061  0.0289  231 TYR A OH  
1574 N N   . VAL A 215 ? 0.2533 0.4327 0.3120 0.0931  0.0033  0.0104  232 VAL A N   
1575 C CA  . VAL A 215 ? 0.2763 0.4686 0.3361 0.1006  0.0047  0.0069  232 VAL A CA  
1576 C C   . VAL A 215 ? 0.2667 0.4473 0.3053 0.1105  0.0048  0.0061  232 VAL A C   
1577 O O   . VAL A 215 ? 0.2916 0.4662 0.3204 0.1145  0.0018  0.0046  232 VAL A O   
1578 C CB  . VAL A 215 ? 0.2736 0.4832 0.3453 0.1021  0.0022  0.0023  232 VAL A CB  
1579 C CG1 . VAL A 215 ? 0.2749 0.4872 0.3437 0.1053  0.0030  -0.0021 232 VAL A CG1 
1580 C CG2 . VAL A 215 ? 0.3039 0.5224 0.3946 0.0921  0.0016  0.0034  232 VAL A CG2 
1581 N N   . LEU A 216 ? 0.2703 0.4467 0.3010 0.1149  0.0083  0.0071  233 LEU A N   
1582 C CA  . LEU A 216 ? 0.2941 0.4557 0.3023 0.1242  0.0086  0.0071  233 LEU A CA  
1583 C C   . LEU A 216 ? 0.3033 0.4735 0.3075 0.1348  0.0087  0.0028  233 LEU A C   
1584 O O   . LEU A 216 ? 0.3272 0.5078 0.3417 0.1336  0.0111  0.0024  233 LEU A O   
1585 C CB  . LEU A 216 ? 0.3415 0.4836 0.3389 0.1205  0.0134  0.0132  233 LEU A CB  
1586 C CG  . LEU A 216 ? 0.3014 0.4338 0.3040 0.1099  0.0132  0.0171  233 LEU A CG  
1587 C CD1 . LEU A 216 ? 0.3553 0.4717 0.3529 0.1052  0.0195  0.0226  233 LEU A CD1 
1588 C CD2 . LEU A 216 ? 0.3452 0.4677 0.3350 0.1138  0.0085  0.0159  233 LEU A CD2 
1589 N N   . GLU A 217 ? 0.3435 0.5089 0.3328 0.1454  0.0055  -0.0010 234 GLU A N   
1590 C CA  . GLU A 217 ? 0.3641 0.5339 0.3462 0.1570  0.0046  -0.0056 234 GLU A CA  
1591 C C   . GLU A 217 ? 0.3778 0.5303 0.3418 0.1601  0.0090  -0.0011 234 GLU A C   
1592 O O   . GLU A 217 ? 0.3526 0.4863 0.3045 0.1561  0.0120  0.0047  234 GLU A O   
1593 C CB  . GLU A 217 ? 0.3549 0.5222 0.3259 0.1662  -0.0007 -0.0115 234 GLU A CB  
1594 C CG  . GLU A 217 ? 0.4515 0.6284 0.4365 0.1570  -0.0040 -0.0161 234 GLU A CG  
1595 C CD  . GLU A 217 ? 0.5703 0.7428 0.5450 0.1621  -0.0085 -0.0222 234 GLU A CD  
1596 O OE1 . GLU A 217 ? 0.5298 0.6919 0.4890 0.1706  -0.0099 -0.0216 234 GLU A OE1 
1597 O OE2 . GLU A 217 ? 0.6507 0.8297 0.6337 0.1574  -0.0105 -0.0276 234 GLU A OE2 
1598 N N   . ALA A 218 ? 0.3797 0.5381 0.3420 0.1673  0.0098  -0.0038 235 ALA A N   
1599 C CA  . ALA A 218 ? 0.3699 0.5116 0.3145 0.1705  0.0151  0.0008  235 ALA A CA  
1600 C C   . ALA A 218 ? 0.4643 0.5830 0.3808 0.1790  0.0144  0.0022  235 ALA A C   
1601 O O   . ALA A 218 ? 0.4794 0.5792 0.3789 0.1798  0.0201  0.0077  235 ALA A O   
1602 C CB  . ALA A 218 ? 0.4635 0.6160 0.4103 0.1782  0.0151  -0.0032 235 ALA A CB  
1603 N N   . ALA A 219 ? 0.4344 0.5535 0.3456 0.1854  0.0082  -0.0026 236 ALA A N   
1604 C CA  . ALA A 219 ? 0.4603 0.5571 0.3451 0.1932  0.0071  -0.0013 236 ALA A CA  
1605 C C   . ALA A 219 ? 0.5155 0.5928 0.3931 0.1835  0.0123  0.0071  236 ALA A C   
1606 O O   . ALA A 219 ? 0.4878 0.5430 0.3418 0.1889  0.0136  0.0100  236 ALA A O   
1607 C CB  . ALA A 219 ? 0.5479 0.6505 0.4323 0.1999  -0.0005 -0.0081 236 ALA A CB  
1608 N N   . ILE A 220 ? 0.4292 0.5135 0.3265 0.1697  0.0152  0.0108  237 ILE A N   
1609 C CA  . ILE A 220 ? 0.4482 0.5149 0.3416 0.1602  0.0198  0.0179  237 ILE A CA  
1610 C C   . ILE A 220 ? 0.4752 0.5231 0.3530 0.1611  0.0280  0.0238  237 ILE A C   
1611 O O   . ILE A 220 ? 0.4152 0.4421 0.2808 0.1581  0.0318  0.0290  237 ILE A O   
1612 C CB  . ILE A 220 ? 0.4254 0.5050 0.3449 0.1460  0.0204  0.0195  237 ILE A CB  
1613 C CG1 . ILE A 220 ? 0.5245 0.5871 0.4435 0.1359  0.0243  0.0257  237 ILE A CG1 
1614 C CG2 . ILE A 220 ? 0.4074 0.5011 0.3430 0.1416  0.0246  0.0199  237 ILE A CG2 
1615 C CD1 . ILE A 220 ? 0.4437 0.4975 0.3571 0.1351  0.0192  0.0253  237 ILE A CD1 
1616 N N   . PHE A 221 ? 0.4958 0.5502 0.3742 0.1650  0.0313  0.0231  238 PHE A N   
1617 C CA  . PHE A 221 ? 0.5146 0.5516 0.3797 0.1647  0.0407  0.0292  238 PHE A CA  
1618 C C   . PHE A 221 ? 0.5485 0.5595 0.3818 0.1750  0.0418  0.0313  238 PHE A C   
1619 O O   . PHE A 221 ? 0.5881 0.5776 0.4100 0.1709  0.0493  0.0380  238 PHE A O   
1620 C CB  . PHE A 221 ? 0.4878 0.5365 0.3568 0.1691  0.0432  0.0273  238 PHE A CB  
1621 C CG  . PHE A 221 ? 0.4298 0.5004 0.3290 0.1577  0.0443  0.0267  238 PHE A CG  
1622 C CD1 . PHE A 221 ? 0.4299 0.4983 0.3442 0.1435  0.0495  0.0317  238 PHE A CD1 
1623 C CD2 . PHE A 221 ? 0.3853 0.4786 0.2983 0.1615  0.0396  0.0207  238 PHE A CD2 
1624 C CE1 . PHE A 221 ? 0.4061 0.4942 0.3480 0.1334  0.0498  0.0308  238 PHE A CE1 
1625 C CE2 . PHE A 221 ? 0.4695 0.5823 0.4097 0.1512  0.0404  0.0202  238 PHE A CE2 
1626 C CZ  . PHE A 221 ? 0.3870 0.4970 0.3411 0.1372  0.0453  0.0254  238 PHE A CZ  
1627 N N   . ASP A 222 ? 0.5498 0.5621 0.3693 0.1884  0.0342  0.0254  239 ASP A N   
1628 C CA  . ASP A 222 ? 0.6640 0.6512 0.4519 0.1994  0.0341  0.0268  239 ASP A CA  
1629 C C   . ASP A 222 ? 0.6743 0.6447 0.4567 0.1930  0.0349  0.0312  239 ASP A C   
1630 O O   . ASP A 222 ? 0.6346 0.5792 0.3936 0.1964  0.0398  0.0361  239 ASP A O   
1631 C CB  . ASP A 222 ? 0.6765 0.6710 0.4546 0.2146  0.0243  0.0181  239 ASP A CB  
1632 C CG  . ASP A 222 ? 0.8808 0.8815 0.6530 0.2252  0.0240  0.0144  239 ASP A CG  
1633 O OD1 . ASP A 222 ? 0.7470 0.7358 0.5093 0.2246  0.0325  0.0199  239 ASP A OD1 
1634 O OD2 . ASP A 222 ? 0.9921 1.0095 0.7703 0.2341  0.0155  0.0057  239 ASP A OD2 
1635 N N   . HIS A 223 ? 0.5742 0.5578 0.3772 0.1840  0.0303  0.0294  240 HIS A N   
1636 C CA  . HIS A 223 ? 0.5501 0.5185 0.3491 0.1780  0.0302  0.0329  240 HIS A CA  
1637 C C   . HIS A 223 ? 0.6059 0.5623 0.4120 0.1651  0.0395  0.0405  240 HIS A C   
1638 O O   . HIS A 223 ? 0.7492 0.6849 0.5442 0.1626  0.0420  0.0447  240 HIS A O   
1639 C CB  . HIS A 223 ? 0.6007 0.5863 0.4176 0.1737  0.0220  0.0282  240 HIS A CB  
1640 C CG  . HIS A 223 ? 0.5632 0.5582 0.3734 0.1860  0.0135  0.0205  240 HIS A CG  
1641 N ND1 . HIS A 223 ? 0.5946 0.5735 0.3813 0.1966  0.0096  0.0188  240 HIS A ND1 
1642 C CD2 . HIS A 223 ? 0.5922 0.6109 0.4168 0.1897  0.0084  0.0136  240 HIS A CD2 
1643 C CE1 . HIS A 223 ? 0.6804 0.6733 0.4682 0.2062  0.0022  0.0109  240 HIS A CE1 
1644 N NE2 . HIS A 223 ? 0.6603 0.6774 0.4713 0.2021  0.0016  0.0076  240 HIS A NE2 
1645 N N   . LEU A 224 ? 0.5362 0.5047 0.3609 0.1570  0.0449  0.0422  241 LEU A N   
1646 C CA  . LEU A 224 ? 0.5480 0.5053 0.3806 0.1452  0.0546  0.0488  241 LEU A CA  
1647 C C   . LEU A 224 ? 0.7013 0.6357 0.5112 0.1502  0.0649  0.0543  241 LEU A C   
1648 O O   . LEU A 224 ? 0.7218 0.6409 0.5335 0.1416  0.0740  0.0602  241 LEU A O   
1649 C CB  . LEU A 224 ? 0.4964 0.4755 0.3580 0.1350  0.0565  0.0480  241 LEU A CB  
1650 C CG  . LEU A 224 ? 0.4365 0.4355 0.3217 0.1278  0.0480  0.0438  241 LEU A CG  
1651 C CD1 . LEU A 224 ? 0.4272 0.4488 0.3371 0.1212  0.0490  0.0421  241 LEU A CD1 
1652 C CD2 . LEU A 224 ? 0.4948 0.4821 0.3870 0.1177  0.0484  0.0467  241 LEU A CD2 
1653 N N   . ARG A 225 ? 0.6864 0.6180 0.4756 0.1639  0.0640  0.0523  242 ARG A N   
1654 C CA  . ARG A 225 ? 0.7805 0.6869 0.5432 0.1703  0.0736  0.0577  242 ARG A CA  
1655 C C   . ARG A 225 ? 0.9370 0.8158 0.6751 0.1747  0.0742  0.0610  242 ARG A C   
1656 O O   . ARG A 225 ? 0.9516 0.8059 0.6737 0.1740  0.0847  0.0676  242 ARG A O   
1657 C CB  . ARG A 225 ? 0.7226 0.6335 0.4692 0.1849  0.0712  0.0539  242 ARG A CB  
1658 C CG  . ARG A 225 ? 0.6894 0.6244 0.4576 0.1814  0.0720  0.0512  242 ARG A CG  
1659 C CD  . ARG A 225 ? 0.7143 0.6486 0.4639 0.1958  0.0719  0.0486  242 ARG A CD  
1660 N NE  . ARG A 225 ? 0.7160 0.6728 0.4878 0.1912  0.0735  0.0465  242 ARG A NE  
1661 C CZ  . ARG A 225 ? 0.6124 0.5961 0.4026 0.1932  0.0643  0.0391  242 ARG A CZ  
1662 N NH1 . ARG A 225 ? 0.6973 0.6892 0.4854 0.2012  0.0531  0.0324  242 ARG A NH1 
1663 N NH2 . ARG A 225 ? 0.6585 0.6614 0.4708 0.1868  0.0667  0.0382  242 ARG A NH2 
1664 N N   . ALA A 226 ? 1.0955 0.9775 0.8303 0.1794  0.0635  0.0564  243 ALA A N   
1665 C CA  . ALA A 226 ? 1.2847 1.1415 0.9982 0.1828  0.0631  0.0592  243 ALA A CA  
1666 C C   . ALA A 226 ? 1.4521 1.3004 1.1806 0.1679  0.0680  0.0640  243 ALA A C   
1667 O O   . ALA A 226 ? 1.5288 1.3512 1.2404 0.1681  0.0730  0.0689  243 ALA A O   
1668 C CB  . ALA A 226 ? 1.1091 0.9731 0.8159 0.1923  0.0500  0.0522  243 ALA A CB  
1669 N N   . THR A 227 ? 1.4008 1.2700 1.1610 0.1554  0.0663  0.0625  244 THR A N   
1670 C CA  . THR A 227 ? 1.4690 1.3329 1.2460 0.1421  0.0680  0.0651  244 THR A CA  
1671 C C   . THR A 227 ? 1.6007 1.4435 1.3758 0.1346  0.0818  0.0725  244 THR A C   
1672 O O   . THR A 227 ? 1.6664 1.5092 1.4416 0.1340  0.0911  0.0753  244 THR A O   
1673 C CB  . THR A 227 ? 1.3893 1.2802 1.1998 0.1314  0.0632  0.0614  244 THR A CB  
1674 O OG1 . THR A 227 ? 1.2135 1.1249 1.0264 0.1385  0.0525  0.0548  244 THR A OG1 
1675 C CG2 . THR A 227 ? 1.3944 1.2805 1.2205 0.1201  0.0612  0.0623  244 THR A CG2 
1676 N N   . THR A 228 ? 1.3245 1.1497 1.0994 0.1286  0.0835  0.0753  245 THR A N   
1677 C CA  . THR A 228 ? 1.1846 0.9884 0.9602 0.1204  0.0969  0.0820  245 THR A CA  
1678 C C   . THR A 228 ? 1.1543 0.9690 0.9651 0.1040  0.0987  0.0816  245 THR A C   
1679 O O   . THR A 228 ? 1.1008 0.8991 0.9182 0.0957  0.1048  0.0849  245 THR A O   
1680 C CB  . THR A 228 ? 0.9753 0.7497 0.7282 0.1241  0.0984  0.0854  245 THR A CB  
1681 N N   . GLU A 234 ? 1.4889 1.3268 1.4144 0.0521  0.1105  0.0796  251 GLU A N   
1682 C CA  . GLU A 234 ? 1.2812 1.1478 1.2213 0.0523  0.1016  0.0747  251 GLU A CA  
1683 C C   . GLU A 234 ? 1.2376 1.1130 1.1565 0.0652  0.0909  0.0721  251 GLU A C   
1684 O O   . GLU A 234 ? 1.2180 1.0893 1.1287 0.0688  0.0814  0.0699  251 GLU A O   
1685 C CB  . GLU A 234 ? 1.2903 1.1701 1.2614 0.0418  0.0927  0.0696  251 GLU A CB  
1686 C CG  . GLU A 234 ? 1.3716 1.2522 1.3722 0.0285  0.1011  0.0698  251 GLU A CG  
1687 C CD  . GLU A 234 ? 1.3472 1.2461 1.3780 0.0201  0.0902  0.0636  251 GLU A CD  
1688 O OE1 . GLU A 234 ? 1.3905 1.2962 1.4173 0.0241  0.0769  0.0599  251 GLU A OE1 
1689 O OE2 . GLU A 234 ? 1.1768 1.0825 1.2345 0.0100  0.0951  0.0622  251 GLU A OE2 
1690 N N   . ILE A 235 ? 1.0552 0.9432 0.9667 0.0719  0.0922  0.0718  252 ILE A N   
1691 C CA  . ILE A 235 ? 0.9593 0.8599 0.8570 0.0831  0.0815  0.0679  252 ILE A CA  
1692 C C   . ILE A 235 ? 0.8908 0.8149 0.8118 0.0781  0.0702  0.0622  252 ILE A C   
1693 O O   . ILE A 235 ? 0.6646 0.6066 0.6080 0.0713  0.0708  0.0605  252 ILE A O   
1694 C CB  . ILE A 235 ? 0.9264 0.8343 0.8115 0.0920  0.0855  0.0683  252 ILE A CB  
1695 C CG1 . ILE A 235 ? 1.0763 0.9589 0.9328 0.0995  0.0959  0.0738  252 ILE A CG1 
1696 C CG2 . ILE A 235 ? 0.7377 0.6632 0.6167 0.1017  0.0734  0.0626  252 ILE A CG2 
1697 C CD1 . ILE A 235 ? 0.9545 0.8276 0.8183 0.0918  0.1108  0.0789  252 ILE A CD1 
1698 N N   . GLN A 236 ? 0.7784 0.7028 0.6925 0.0824  0.0598  0.0591  253 GLN A N   
1699 C CA  . GLN A 236 ? 0.7368 0.6800 0.6697 0.0782  0.0494  0.0541  253 GLN A CA  
1700 C C   . GLN A 236 ? 0.5596 0.5222 0.4877 0.0869  0.0431  0.0502  253 GLN A C   
1701 O O   . GLN A 236 ? 0.5602 0.5181 0.4662 0.0981  0.0412  0.0496  253 GLN A O   
1702 C CB  . GLN A 236 ? 0.8059 0.7384 0.7359 0.0773  0.0419  0.0527  253 GLN A CB  
1703 C CG  . GLN A 236 ? 0.9615 0.8783 0.9032 0.0671  0.0463  0.0551  253 GLN A CG  
1704 C CD  . GLN A 236 ? 0.9432 0.8628 0.8988 0.0619  0.0360  0.0511  253 GLN A CD  
1705 O OE1 . GLN A 236 ? 0.9267 0.8320 0.8714 0.0644  0.0315  0.0509  253 GLN A OE1 
1706 N NE2 . GLN A 236 ? 0.9019 0.8396 0.8809 0.0552  0.0317  0.0478  253 GLN A NE2 
1707 N N   . LEU A 237 ? 0.4968 0.4809 0.4463 0.0818  0.0400  0.0473  254 LEU A N   
1708 C CA  . LEU A 237 ? 0.4645 0.4678 0.4130 0.0889  0.0339  0.0431  254 LEU A CA  
1709 C C   . LEU A 237 ? 0.4717 0.4732 0.4090 0.0950  0.0249  0.0400  254 LEU A C   
1710 O O   . LEU A 237 ? 0.4620 0.4691 0.3865 0.1051  0.0217  0.0373  254 LEU A O   
1711 C CB  . LEU A 237 ? 0.4310 0.4557 0.4055 0.0810  0.0319  0.0407  254 LEU A CB  
1712 C CG  . LEU A 237 ? 0.4026 0.4489 0.3811 0.0865  0.0265  0.0363  254 LEU A CG  
1713 C CD1 . LEU A 237 ? 0.4713 0.5205 0.4362 0.0962  0.0304  0.0362  254 LEU A CD1 
1714 C CD2 . LEU A 237 ? 0.3727 0.4370 0.3772 0.0775  0.0251  0.0347  254 LEU A CD2 
1715 N N   . THR A 238 ? 0.4410 0.4336 0.3826 0.0895  0.0208  0.0400  255 THR A N   
1716 C CA  . THR A 238 ? 0.5017 0.4909 0.4321 0.0952  0.0125  0.0371  255 THR A CA  
1717 C C   . THR A 238 ? 0.5147 0.4906 0.4187 0.1064  0.0134  0.0378  255 THR A C   
1718 O O   . THR A 238 ? 0.4741 0.4548 0.3679 0.1148  0.0076  0.0342  255 THR A O   
1719 C CB  . THR A 238 ? 0.4828 0.4603 0.4201 0.0877  0.0088  0.0375  255 THR A CB  
1720 O OG1 . THR A 238 ? 0.6332 0.6244 0.5938 0.0791  0.0055  0.0355  255 THR A OG1 
1721 C CG2 . THR A 238 ? 0.6143 0.5849 0.5372 0.0940  0.0012  0.0351  255 THR A CG2 
1722 N N   . ASP A 239 ? 0.5781 0.5366 0.4707 0.1071  0.0210  0.0422  256 ASP A N   
1723 C CA  . ASP A 239 ? 0.5971 0.5415 0.4628 0.1186  0.0221  0.0430  256 ASP A CA  
1724 C C   . ASP A 239 ? 0.5261 0.4849 0.3854 0.1284  0.0212  0.0398  256 ASP A C   
1725 O O   . ASP A 239 ? 0.5394 0.4966 0.3822 0.1391  0.0164  0.0366  256 ASP A O   
1726 C CB  . ASP A 239 ? 0.7629 0.6850 0.6175 0.1170  0.0317  0.0489  256 ASP A CB  
1727 C CG  . ASP A 239 ? 0.8352 0.7412 0.6959 0.1080  0.0327  0.0516  256 ASP A CG  
1728 O OD1 . ASP A 239 ? 0.8315 0.7358 0.6919 0.1082  0.0247  0.0490  256 ASP A OD1 
1729 O OD2 . ASP A 239 ? 1.0638 0.9586 0.9298 0.1010  0.0417  0.0560  256 ASP A OD2 
1730 N N   . GLY A 240 ? 0.5320 0.5047 0.4045 0.1251  0.0256  0.0401  257 GLY A N   
1731 C CA  . GLY A 240 ? 0.5333 0.5205 0.4019 0.1344  0.0241  0.0363  257 GLY A CA  
1732 C C   . GLY A 240 ? 0.4875 0.4925 0.3631 0.1380  0.0152  0.0301  257 GLY A C   
1733 O O   . GLY A 240 ? 0.5435 0.5529 0.4078 0.1491  0.0115  0.0258  257 GLY A O   
1734 N N   . ILE A 241 ? 0.4773 0.4925 0.3718 0.1290  0.0120  0.0292  258 ILE A N   
1735 C CA  . ILE A 241 ? 0.4280 0.4592 0.3294 0.1318  0.0049  0.0238  258 ILE A CA  
1736 C C   . ILE A 241 ? 0.4846 0.5048 0.3679 0.1399  -0.0002 0.0216  258 ILE A C   
1737 O O   . ILE A 241 ? 0.4663 0.4956 0.3447 0.1488  -0.0041 0.0165  258 ILE A O   
1738 C CB  . ILE A 241 ? 0.4889 0.5300 0.4119 0.1207  0.0027  0.0238  258 ILE A CB  
1739 C CG1 . ILE A 241 ? 0.4182 0.4745 0.3599 0.1147  0.0067  0.0245  258 ILE A CG1 
1740 C CG2 . ILE A 241 ? 0.4326 0.4837 0.3575 0.1239  -0.0041 0.0191  258 ILE A CG2 
1741 C CD1 . ILE A 241 ? 0.4006 0.4597 0.3617 0.1024  0.0065  0.0262  258 ILE A CD1 
1742 N N   . ALA A 242 ? 0.5025 0.5027 0.3760 0.1373  -0.0001 0.0250  259 ALA A N   
1743 C CA  . ALA A 242 ? 0.5244 0.5124 0.3794 0.1451  -0.0049 0.0230  259 ALA A CA  
1744 C C   . ALA A 242 ? 0.6068 0.5918 0.4432 0.1581  -0.0049 0.0206  259 ALA A C   
1745 O O   . ALA A 242 ? 0.5057 0.4938 0.3338 0.1668  -0.0103 0.0156  259 ALA A O   
1746 C CB  . ALA A 242 ? 0.5582 0.5231 0.4047 0.1406  -0.0037 0.0276  259 ALA A CB  
1747 N N   . ALA A 243 ? 0.5673 0.5452 0.3964 0.1600  0.0011  0.0238  260 ALA A N   
1748 C CA  . ALA A 243 ? 0.5239 0.4976 0.3341 0.1732  0.0006  0.0212  260 ALA A CA  
1749 C C   . ALA A 243 ? 0.5722 0.5697 0.3928 0.1791  -0.0030 0.0145  260 ALA A C   
1750 O O   . ALA A 243 ? 0.5557 0.5547 0.3649 0.1908  -0.0076 0.0090  260 ALA A O   
1751 C CB  . ALA A 243 ? 0.5431 0.5021 0.3419 0.1738  0.0085  0.0267  260 ALA A CB  
1752 N N   . LEU A 244 ? 0.5107 0.5267 0.3536 0.1712  -0.0010 0.0144  261 LEU A N   
1753 C CA  . LEU A 244 ? 0.5837 0.6230 0.4395 0.1756  -0.0040 0.0080  261 LEU A CA  
1754 C C   . LEU A 244 ? 0.5659 0.6141 0.4247 0.1795  -0.0104 0.0021  261 LEU A C   
1755 O O   . LEU A 244 ? 0.5972 0.6577 0.4573 0.1884  -0.0137 -0.0046 261 LEU A O   
1756 C CB  . LEU A 244 ? 0.4884 0.5441 0.3682 0.1649  -0.0006 0.0097  261 LEU A CB  
1757 C CG  . LEU A 244 ? 0.4680 0.5483 0.3644 0.1675  -0.0025 0.0038  261 LEU A CG  
1758 C CD1 . LEU A 244 ? 0.5205 0.6014 0.4060 0.1791  -0.0024 0.0006  261 LEU A CD1 
1759 C CD2 . LEU A 244 ? 0.5153 0.6088 0.4343 0.1558  0.0008  0.0064  261 LEU A CD2 
1760 N N   . LEU A 245 ? 0.6146 0.6559 0.4743 0.1733  -0.0122 0.0041  262 LEU A N   
1761 C CA  . LEU A 245 ? 0.5787 0.6268 0.4403 0.1765  -0.0174 -0.0010 262 LEU A CA  
1762 C C   . LEU A 245 ? 0.6361 0.6795 0.4808 0.1903  -0.0214 -0.0065 262 LEU A C   
1763 O O   . LEU A 245 ? 0.5904 0.6454 0.4399 0.1953  -0.0249 -0.0129 262 LEU A O   
1764 C CB  . LEU A 245 ? 0.5617 0.5974 0.4212 0.1692  -0.0189 0.0026  262 LEU A CB  
1765 C CG  . LEU A 245 ? 0.5161 0.5586 0.3942 0.1567  -0.0177 0.0056  262 LEU A CG  
1766 C CD1 . LEU A 245 ? 0.5415 0.5680 0.4134 0.1520  -0.0205 0.0083  262 LEU A CD1 
1767 C CD2 . LEU A 245 ? 0.6024 0.6663 0.4965 0.1562  -0.0191 0.0010  262 LEU A CD2 
1768 N N   . ARG A 246 ? 0.6439 0.6693 0.4683 0.1966  -0.0207 -0.0044 263 ARG A N   
1769 C CA  . ARG A 246 ? 0.7703 0.7899 0.5775 0.2104  -0.0253 -0.0099 263 ARG A CA  
1770 C C   . ARG A 246 ? 0.7573 0.7931 0.5698 0.2197  -0.0269 -0.0169 263 ARG A C   
1771 O O   . ARG A 246 ? 0.8062 0.8442 0.6119 0.2308  -0.0320 -0.0241 263 ARG A O   
1772 C CB  . ARG A 246 ? 0.7728 0.7659 0.5547 0.2147  -0.0240 -0.0051 263 ARG A CB  
1773 C CG  . ARG A 246 ? 0.8251 0.8020 0.6033 0.2056  -0.0225 0.0013  263 ARG A CG  
1774 C CD  . ARG A 246 ? 0.9053 0.8552 0.6594 0.2093  -0.0204 0.0062  263 ARG A CD  
1775 N NE  . ARG A 246 ? 1.1638 1.0995 0.9172 0.2004  -0.0197 0.0112  263 ARG A NE  
1776 C CZ  . ARG A 246 ? 1.3305 1.2416 1.0646 0.2023  -0.0189 0.0152  263 ARG A CZ  
1777 N NH1 . ARG A 246 ? 1.4016 1.2977 1.1131 0.2129  -0.0183 0.0154  263 ARG A NH1 
1778 N NH2 . ARG A 246 ? 1.3519 1.2525 1.0890 0.1938  -0.0189 0.0188  263 ARG A NH2 
1779 N N   . GLU A 247 ? 0.5373 0.8021 0.6095 0.1200  0.0347  0.0868  264 GLU A N   
1780 C CA  . GLU A 247 ? 0.5094 0.8034 0.5828 0.1143  0.0287  0.0876  264 GLU A CA  
1781 C C   . GLU A 247 ? 0.5197 0.8200 0.5920 0.0998  0.0246  0.0788  264 GLU A C   
1782 O O   . GLU A 247 ? 0.5987 0.9268 0.6748 0.0961  0.0216  0.0791  264 GLU A O   
1783 C CB  . GLU A 247 ? 0.5625 0.8553 0.6308 0.1125  0.0252  0.0890  264 GLU A CB  
1784 C CG  . GLU A 247 ? 0.7190 1.0423 0.7875 0.1053  0.0189  0.0889  264 GLU A CG  
1785 C CD  . GLU A 247 ? 0.7633 1.0795 0.8250 0.0980  0.0152  0.0860  264 GLU A CD  
1786 O OE1 . GLU A 247 ? 0.6409 0.9299 0.6980 0.0997  0.0173  0.0851  264 GLU A OE1 
1787 O OE2 . GLU A 247 ? 0.6897 1.0284 0.7507 0.0902  0.0103  0.0842  264 GLU A OE2 
1788 N N   . ARG A 248 ? 0.4743 0.7501 0.5418 0.0915  0.0248  0.0712  265 ARG A N   
1789 C CA  . ARG A 248 ? 0.4736 0.7516 0.5388 0.0773  0.0213  0.0631  265 ARG A CA  
1790 C C   . ARG A 248 ? 0.4165 0.6740 0.4805 0.0747  0.0244  0.0582  265 ARG A C   
1791 O O   . ARG A 248 ? 0.4179 0.6556 0.4810 0.0819  0.0285  0.0594  265 ARG A O   
1792 C CB  . ARG A 248 ? 0.5138 0.7828 0.5727 0.0679  0.0174  0.0586  265 ARG A CB  
1793 C CG  . ARG A 248 ? 0.6310 0.9156 0.6896 0.0712  0.0148  0.0636  265 ARG A CG  
1794 C CD  . ARG A 248 ? 0.7106 1.0287 0.7727 0.0662  0.0114  0.0639  265 ARG A CD  
1795 N NE  . ARG A 248 ? 0.7767 1.0947 0.8356 0.0506  0.0086  0.0549  265 ARG A NE  
1796 C CZ  . ARG A 248 ? 0.8611 1.1998 0.9229 0.0422  0.0073  0.0512  265 ARG A CZ  
1797 N NH1 . ARG A 248 ? 0.9610 1.3240 1.0293 0.0477  0.0079  0.0554  265 ARG A NH1 
1798 N NH2 . ARG A 248 ? 0.8654 1.1999 0.9237 0.0280  0.0058  0.0430  265 ARG A NH2 
1799 N N   . ASP A 249 ? 0.3688 0.6306 0.4320 0.0638  0.0226  0.0523  266 ASP A N   
1800 C CA  . ASP A 249 ? 0.3561 0.6006 0.4174 0.0598  0.0250  0.0474  266 ASP A CA  
1801 C C   . ASP A 249 ? 0.3221 0.5395 0.3764 0.0545  0.0242  0.0429  266 ASP A C   
1802 O O   . ASP A 249 ? 0.4291 0.6446 0.4798 0.0470  0.0209  0.0402  266 ASP A O   
1803 C CB  . ASP A 249 ? 0.4697 0.7287 0.5323 0.0497  0.0236  0.0432  266 ASP A CB  
1804 C CG  . ASP A 249 ? 0.5433 0.8288 0.6133 0.0547  0.0248  0.0471  266 ASP A CG  
1805 O OD1 . ASP A 249 ? 0.6085 0.8948 0.6824 0.0669  0.0281  0.0525  266 ASP A OD1 
1806 O OD2 . ASP A 249 ? 0.5907 0.8960 0.6627 0.0466  0.0228  0.0445  266 ASP A OD2 
1807 N N   . VAL A 250 ? 0.3543 0.5513 0.4068 0.0584  0.0276  0.0419  267 VAL A N   
1808 C CA  . VAL A 250 ? 0.2551 0.4277 0.3015 0.0537  0.0271  0.0374  267 VAL A CA  
1809 C C   . VAL A 250 ? 0.2896 0.4521 0.3343 0.0502  0.0292  0.0336  267 VAL A C   
1810 O O   . VAL A 250 ? 0.3062 0.4693 0.3537 0.0564  0.0331  0.0350  267 VAL A O   
1811 C CB  . VAL A 250 ? 0.2575 0.4139 0.3023 0.0619  0.0293  0.0397  267 VAL A CB  
1812 C CG1 . VAL A 250 ? 0.2769 0.4097 0.3156 0.0564  0.0285  0.0346  267 VAL A CG1 
1813 C CG2 . VAL A 250 ? 0.3534 0.5211 0.3995 0.0658  0.0274  0.0443  267 VAL A CG2 
1814 N N   . TYR A 251 ? 0.3065 0.4597 0.3467 0.0406  0.0271  0.0291  268 TYR A N   
1815 C CA  . TYR A 251 ? 0.3118 0.4560 0.3495 0.0363  0.0286  0.0258  268 TYR A CA  
1816 C C   . TYR A 251 ? 0.3147 0.4360 0.3469 0.0350  0.0284  0.0231  268 TYR A C   
1817 O O   . TYR A 251 ? 0.2960 0.4093 0.3261 0.0347  0.0265  0.0229  268 TYR A O   
1818 C CB  . TYR A 251 ? 0.2985 0.4521 0.3357 0.0261  0.0269  0.0234  268 TYR A CB  
1819 C CG  . TYR A 251 ? 0.3539 0.5320 0.3968 0.0265  0.0271  0.0254  268 TYR A CG  
1820 C CD1 . TYR A 251 ? 0.3367 0.5236 0.3829 0.0290  0.0300  0.0261  268 TYR A CD1 
1821 C CD2 . TYR A 251 ? 0.4168 0.6107 0.4620 0.0246  0.0245  0.0265  268 TYR A CD2 
1822 C CE1 . TYR A 251 ? 0.3578 0.5686 0.4098 0.0296  0.0302  0.0279  268 TYR A CE1 
1823 C CE2 . TYR A 251 ? 0.4058 0.6252 0.4567 0.0251  0.0245  0.0283  268 TYR A CE2 
1824 C CZ  . TYR A 251 ? 0.4017 0.6292 0.4561 0.0277  0.0273  0.0291  268 TYR A CZ  
1825 O OH  . TYR A 251 ? 0.4405 0.6941 0.5010 0.0284  0.0274  0.0309  268 TYR A OH  
1826 N N   . ALA A 252 ? 0.2780 0.3901 0.3078 0.0342  0.0304  0.0210  269 ALA A N   
1827 C CA  . ALA A 252 ? 0.3283 0.4215 0.3529 0.0321  0.0300  0.0182  269 ALA A CA  
1828 C C   . ALA A 252 ? 0.2897 0.3814 0.3111 0.0245  0.0295  0.0163  269 ALA A C   
1829 O O   . ALA A 252 ? 0.3070 0.4088 0.3302 0.0233  0.0311  0.0166  269 ALA A O   
1830 C CB  . ALA A 252 ? 0.2920 0.3757 0.3163 0.0390  0.0336  0.0175  269 ALA A CB  
1831 N N   . HIS A 253 ? 0.2942 0.3737 0.3112 0.0195  0.0276  0.0146  270 HIS A N   
1832 C CA  . HIS A 253 ? 0.3031 0.3804 0.3169 0.0125  0.0276  0.0137  270 HIS A CA  
1833 C C   . HIS A 253 ? 0.3272 0.3891 0.3361 0.0126  0.0275  0.0125  270 HIS A C   
1834 O O   . HIS A 253 ? 0.2815 0.3328 0.2886 0.0133  0.0259  0.0118  270 HIS A O   
1835 C CB  . HIS A 253 ? 0.3350 0.4145 0.3484 0.0050  0.0259  0.0134  270 HIS A CB  
1836 C CG  . HIS A 253 ? 0.3776 0.4549 0.3881 -0.0020 0.0270  0.0130  270 HIS A CG  
1837 N ND1 . HIS A 253 ? 0.2886 0.3776 0.3007 -0.0049 0.0290  0.0133  270 HIS A ND1 
1838 C CD2 . HIS A 253 ? 0.3219 0.3866 0.3281 -0.0066 0.0269  0.0127  270 HIS A CD2 
1839 C CE1 . HIS A 253 ? 0.3176 0.4004 0.3260 -0.0111 0.0302  0.0132  270 HIS A CE1 
1840 N NE2 . HIS A 253 ? 0.3207 0.3887 0.3256 -0.0120 0.0290  0.0131  270 HIS A NE2 
1841 N N   . ARG A 254 ? 0.3212 0.3835 0.3280 0.0117  0.0293  0.0123  271 ARG A N   
1842 C CA  . ARG A 254 ? 0.3455 0.3969 0.3473 0.0113  0.0294  0.0115  271 ARG A CA  
1843 C C   . ARG A 254 ? 0.3654 0.4107 0.3640 0.0050  0.0280  0.0126  271 ARG A C   
1844 O O   . ARG A 254 ? 0.3259 0.3743 0.3229 0.0005  0.0292  0.0138  271 ARG A O   
1845 C CB  . ARG A 254 ? 0.3297 0.3861 0.3304 0.0122  0.0320  0.0112  271 ARG A CB  
1846 C CG  . ARG A 254 ? 0.2682 0.3303 0.2726 0.0184  0.0346  0.0100  271 ARG A CG  
1847 C CD  . ARG A 254 ? 0.3341 0.4023 0.3376 0.0183  0.0376  0.0093  271 ARG A CD  
1848 N NE  . ARG A 254 ? 0.3250 0.3996 0.3329 0.0241  0.0411  0.0083  271 ARG A NE  
1849 C CZ  . ARG A 254 ? 0.3043 0.3730 0.3120 0.0287  0.0436  0.0057  271 ARG A CZ  
1850 N NH1 . ARG A 254 ? 0.3326 0.3903 0.3360 0.0281  0.0425  0.0036  271 ARG A NH1 
1851 N NH2 . ARG A 254 ? 0.3617 0.4357 0.3736 0.0338  0.0478  0.0051  271 ARG A NH2 
1852 N N   . TYR A 255 ? 0.3451 0.3812 0.3429 0.0046  0.0259  0.0123  272 TYR A N   
1853 C CA  . TYR A 255 ? 0.3478 0.3771 0.3433 -0.0010 0.0254  0.0133  272 TYR A CA  
1854 C C   . TYR A 255 ? 0.3290 0.3511 0.3197 -0.0016 0.0259  0.0148  272 TYR A C   
1855 O O   . TYR A 255 ? 0.3841 0.4049 0.3730 0.0023  0.0258  0.0143  272 TYR A O   
1856 C CB  . TYR A 255 ? 0.3561 0.3774 0.3522 -0.0009 0.0234  0.0124  272 TYR A CB  
1857 C CG  . TYR A 255 ? 0.3514 0.3648 0.3462 0.0044  0.0222  0.0113  272 TYR A CG  
1858 C CD1 . TYR A 255 ? 0.3513 0.3555 0.3425 0.0044  0.0216  0.0118  272 TYR A CD1 
1859 C CD2 . TYR A 255 ? 0.3370 0.3528 0.3343 0.0094  0.0220  0.0098  272 TYR A CD2 
1860 C CE1 . TYR A 255 ? 0.3359 0.3348 0.3261 0.0086  0.0206  0.0102  272 TYR A CE1 
1861 C CE2 . TYR A 255 ? 0.3438 0.3526 0.3400 0.0135  0.0217  0.0081  272 TYR A CE2 
1862 C CZ  . TYR A 255 ? 0.4121 0.4130 0.4048 0.0128  0.0208  0.0079  272 TYR A CZ  
1863 O OH  . TYR A 255 ? 0.5235 0.5190 0.5155 0.0163  0.0207  0.0055  272 TYR A OH  
1864 N N   . ASP A 256 ? 0.3286 0.3461 0.3172 -0.0067 0.0270  0.0168  273 ASP A N   
1865 C CA  . ASP A 256 ? 0.3401 0.3497 0.3241 -0.0069 0.0275  0.0194  273 ASP A CA  
1866 C C   . ASP A 256 ? 0.4208 0.4191 0.4041 -0.0056 0.0257  0.0195  273 ASP A C   
1867 O O   . ASP A 256 ? 0.4033 0.3967 0.3881 -0.0088 0.0259  0.0191  273 ASP A O   
1868 C CB  . ASP A 256 ? 0.4300 0.4392 0.4120 -0.0126 0.0305  0.0221  273 ASP A CB  
1869 C CG  . ASP A 256 ? 0.4926 0.4938 0.4695 -0.0118 0.0313  0.0261  273 ASP A CG  
1870 O OD1 . ASP A 256 ? 0.4616 0.4669 0.4359 -0.0087 0.0309  0.0269  273 ASP A OD1 
1871 O OD2 . ASP A 256 ? 0.5150 0.5062 0.4907 -0.0139 0.0325  0.0284  273 ASP A OD2 
1872 N N   . GLY A 257 ? 0.4444 0.4392 0.4254 -0.0014 0.0242  0.0197  274 GLY A N   
1873 C CA  . GLY A 257 ? 0.4286 0.4139 0.4092 0.0003  0.0225  0.0197  274 GLY A CA  
1874 C C   . GLY A 257 ? 0.3743 0.3604 0.3542 0.0053  0.0205  0.0175  274 GLY A C   
1875 O O   . GLY A 257 ? 0.4274 0.4204 0.4075 0.0073  0.0208  0.0154  274 GLY A O   
1876 N N   . LYS A 258 ? 0.3692 0.3481 0.3482 0.0069  0.0190  0.0180  275 LYS A N   
1877 C CA  . LYS A 258 ? 0.3836 0.3628 0.3618 0.0109  0.0173  0.0156  275 LYS A CA  
1878 C C   . LYS A 258 ? 0.4042 0.3780 0.3856 0.0121  0.0160  0.0122  275 LYS A C   
1879 O O   . LYS A 258 ? 0.3615 0.3280 0.3438 0.0110  0.0154  0.0133  275 LYS A O   
1880 C CB  . LYS A 258 ? 0.4185 0.3956 0.3933 0.0121  0.0165  0.0190  275 LYS A CB  
1881 C CG  . LYS A 258 ? 0.4642 0.4423 0.4386 0.0154  0.0145  0.0162  275 LYS A CG  
1882 C CD  . LYS A 258 ? 0.5987 0.5850 0.5720 0.0167  0.0149  0.0121  275 LYS A CD  
1883 C CE  . LYS A 258 ? 0.6347 0.6222 0.6074 0.0190  0.0132  0.0088  275 LYS A CE  
1884 N NZ  . LYS A 258 ? 0.6479 0.6446 0.6182 0.0194  0.0142  0.0052  275 LYS A NZ  
1885 N N   . ARG A 259 ? 0.3729 0.3497 0.3558 0.0143  0.0161  0.0082  276 ARG A N   
1886 C CA  . ARG A 259 ? 0.4118 0.3837 0.3972 0.0158  0.0153  0.0050  276 ARG A CA  
1887 C C   . ARG A 259 ? 0.4197 0.3895 0.4041 0.0182  0.0144  0.0023  276 ARG A C   
1888 O O   . ARG A 259 ? 0.3733 0.3482 0.3558 0.0195  0.0151  0.0004  276 ARG A O   
1889 C CB  . ARG A 259 ? 0.4505 0.4263 0.4385 0.0174  0.0168  0.0027  276 ARG A CB  
1890 C CG  . ARG A 259 ? 0.5105 0.4809 0.5004 0.0195  0.0166  -0.0004 276 ARG A CG  
1891 C CD  . ARG A 259 ? 0.6251 0.5991 0.6172 0.0221  0.0188  -0.0018 276 ARG A CD  
1892 N NE  . ARG A 259 ? 0.7012 0.6776 0.6925 0.0244  0.0211  -0.0046 276 ARG A NE  
1893 C CZ  . ARG A 259 ? 0.7154 0.6884 0.7076 0.0272  0.0233  -0.0081 276 ARG A CZ  
1894 N NH1 . ARG A 259 ? 0.6265 0.5935 0.6204 0.0285  0.0233  -0.0089 276 ARG A NH1 
1895 N NH2 . ARG A 259 ? 0.8292 0.8046 0.8205 0.0285  0.0262  -0.0112 276 ARG A NH2 
1896 N N   . TYR A 260 ? 0.3580 0.3209 0.3435 0.0184  0.0130  0.0016  277 TYR A N   
1897 C CA  . TYR A 260 ? 0.3137 0.2747 0.2991 0.0204  0.0123  -0.0019 277 TYR A CA  
1898 C C   . TYR A 260 ? 0.3548 0.3114 0.3429 0.0213  0.0131  -0.0057 277 TYR A C   
1899 O O   . TYR A 260 ? 0.3544 0.3059 0.3442 0.0204  0.0126  -0.0048 277 TYR A O   
1900 C CB  . TYR A 260 ? 0.2957 0.2525 0.2808 0.0203  0.0104  0.0004  277 TYR A CB  
1901 C CG  . TYR A 260 ? 0.3170 0.2774 0.2993 0.0201  0.0100  0.0053  277 TYR A CG  
1902 C CD1 . TYR A 260 ? 0.3716 0.3393 0.3514 0.0217  0.0092  0.0051  277 TYR A CD1 
1903 C CD2 . TYR A 260 ? 0.3486 0.3058 0.3307 0.0181  0.0108  0.0100  277 TYR A CD2 
1904 C CE1 . TYR A 260 ? 0.4207 0.3924 0.3974 0.0220  0.0090  0.0104  277 TYR A CE1 
1905 C CE2 . TYR A 260 ? 0.3536 0.3133 0.3329 0.0182  0.0112  0.0152  277 TYR A CE2 
1906 C CZ  . TYR A 260 ? 0.4531 0.4200 0.4296 0.0205  0.0101  0.0157  277 TYR A CZ  
1907 O OH  . TYR A 260 ? 0.4371 0.4070 0.4104 0.0211  0.0105  0.0215  277 TYR A OH  
1908 N N   . ASP A 261 ? 0.3581 0.3164 0.3462 0.0230  0.0149  -0.0100 278 ASP A N   
1909 C CA  . ASP A 261 ? 0.4243 0.3777 0.4145 0.0244  0.0167  -0.0132 278 ASP A CA  
1910 C C   . ASP A 261 ? 0.3956 0.3437 0.3861 0.0244  0.0156  -0.0161 278 ASP A C   
1911 O O   . ASP A 261 ? 0.3354 0.2854 0.3250 0.0246  0.0162  -0.0199 278 ASP A O   
1912 C CB  . ASP A 261 ? 0.4367 0.3928 0.4269 0.0263  0.0203  -0.0165 278 ASP A CB  
1913 C CG  . ASP A 261 ? 0.4729 0.4231 0.4653 0.0284  0.0231  -0.0186 278 ASP A CG  
1914 O OD1 . ASP A 261 ? 0.3971 0.3412 0.3903 0.0281  0.0219  -0.0192 278 ASP A OD1 
1915 O OD2 . ASP A 261 ? 0.4655 0.4169 0.4587 0.0306  0.0268  -0.0196 278 ASP A OD2 
1916 N N   . CYS A 262 ? 0.3668 0.3092 0.3587 0.0236  0.0141  -0.0146 279 CYS A N   
1917 C CA  . CYS A 262 ? 0.3935 0.3310 0.3861 0.0235  0.0130  -0.0170 279 CYS A CA  
1918 C C   . CYS A 262 ? 0.4311 0.3634 0.4250 0.0245  0.0152  -0.0213 279 CYS A C   
1919 O O   . CYS A 262 ? 0.4510 0.3786 0.4459 0.0241  0.0146  -0.0234 279 CYS A O   
1920 C CB  . CYS A 262 ? 0.4006 0.3338 0.3942 0.0220  0.0109  -0.0137 279 CYS A CB  
1921 S SG  . CYS A 262 ? 0.3603 0.2972 0.3523 0.0211  0.0093  -0.0082 279 CYS A SG  
1922 N N   . GLY A 263 ? 0.3637 0.2966 0.3577 0.0259  0.0182  -0.0223 280 GLY A N   
1923 C CA  . GLY A 263 ? 0.4545 0.3817 0.4493 0.0274  0.0215  -0.0258 280 GLY A CA  
1924 C C   . GLY A 263 ? 0.4543 0.3802 0.4487 0.0269  0.0235  -0.0319 280 GLY A C   
1925 O O   . GLY A 263 ? 0.5403 0.4599 0.5355 0.0275  0.0265  -0.0351 280 GLY A O   
1926 N N   . SER A 264 ? 0.4120 0.3444 0.4052 0.0257  0.0223  -0.0335 281 SER A N   
1927 C CA  . SER A 264 ? 0.3669 0.3006 0.3598 0.0243  0.0238  -0.0398 281 SER A CA  
1928 C C   . SER A 264 ? 0.3642 0.3019 0.3571 0.0232  0.0194  -0.0390 281 SER A C   
1929 O O   . SER A 264 ? 0.3755 0.3155 0.3682 0.0235  0.0160  -0.0335 281 SER A O   
1930 C CB  . SER A 264 ? 0.4744 0.4144 0.4657 0.0238  0.0270  -0.0433 281 SER A CB  
1931 O OG  . SER A 264 ? 0.3903 0.3396 0.3797 0.0232  0.0238  -0.0404 281 SER A OG  
1932 N N   . LYS A 265 ? 0.3515 0.2898 0.3450 0.0219  0.0200  -0.0444 282 LYS A N   
1933 C CA  . LYS A 265 ? 0.4136 0.3577 0.4077 0.0216  0.0160  -0.0432 282 LYS A CA  
1934 C C   . LYS A 265 ? 0.3758 0.3310 0.3676 0.0218  0.0138  -0.0405 282 LYS A C   
1935 O O   . LYS A 265 ? 0.3743 0.3327 0.3660 0.0229  0.0103  -0.0351 282 LYS A O   
1936 C CB  . LYS A 265 ? 0.3956 0.3412 0.3910 0.0200  0.0170  -0.0500 282 LYS A CB  
1937 C CG  . LYS A 265 ? 0.5875 0.5229 0.5852 0.0198  0.0181  -0.0518 282 LYS A CG  
1938 C CD  . LYS A 265 ? 0.6036 0.5412 0.6027 0.0177  0.0195  -0.0591 282 LYS A CD  
1939 C CE  . LYS A 265 ? 0.5708 0.5176 0.5685 0.0153  0.0220  -0.0655 282 LYS A CE  
1940 N NZ  . LYS A 265 ? 0.5565 0.5058 0.5559 0.0125  0.0237  -0.0733 282 LYS A NZ  
1941 N N   . ALA A 266 ? 0.3687 0.3295 0.3585 0.0207  0.0165  -0.0442 283 ALA A N   
1942 C CA  . ALA A 266 ? 0.3707 0.3427 0.3579 0.0206  0.0148  -0.0417 283 ALA A CA  
1943 C C   . ALA A 266 ? 0.3919 0.3619 0.3782 0.0222  0.0129  -0.0337 283 ALA A C   
1944 O O   . ALA A 266 ? 0.3663 0.3425 0.3511 0.0230  0.0100  -0.0286 283 ALA A O   
1945 C CB  . ALA A 266 ? 0.4167 0.3938 0.4019 0.0186  0.0189  -0.0477 283 ALA A CB  
1946 N N   . GLY A 267 ? 0.3517 0.3137 0.3389 0.0227  0.0149  -0.0323 284 GLY A N   
1947 C CA  . GLY A 267 ? 0.3666 0.3280 0.3533 0.0235  0.0136  -0.0256 284 GLY A CA  
1948 C C   . GLY A 267 ? 0.3478 0.3053 0.3356 0.0239  0.0104  -0.0204 284 GLY A C   
1949 O O   . GLY A 267 ? 0.4037 0.3638 0.3901 0.0241  0.0088  -0.0149 284 GLY A O   
1950 N N   . MET A 268 ? 0.3707 0.3214 0.3608 0.0240  0.0101  -0.0223 285 MET A N   
1951 C CA  . MET A 268 ? 0.3848 0.3306 0.3764 0.0243  0.0078  -0.0182 285 MET A CA  
1952 C C   . MET A 268 ? 0.3282 0.2804 0.3192 0.0255  0.0056  -0.0157 285 MET A C   
1953 O O   . MET A 268 ? 0.3171 0.2674 0.3081 0.0263  0.0044  -0.0100 285 MET A O   
1954 C CB  . MET A 268 ? 0.3806 0.3184 0.3748 0.0240  0.0084  -0.0215 285 MET A CB  
1955 C CG  . MET A 268 ? 0.4569 0.3902 0.4528 0.0243  0.0066  -0.0184 285 MET A CG  
1956 S SD  . MET A 268 ? 0.6058 0.5302 0.6026 0.0226  0.0073  -0.0154 285 MET A SD  
1957 C CE  . MET A 268 ? 0.4886 0.4079 0.4868 0.0223  0.0089  -0.0211 285 MET A CE  
1958 N N   . PHE A 269 ? 0.3652 0.3251 0.3557 0.0257  0.0053  -0.0201 286 PHE A N   
1959 C CA  . PHE A 269 ? 0.3574 0.3267 0.3471 0.0273  0.0030  -0.0177 286 PHE A CA  
1960 C C   . PHE A 269 ? 0.3184 0.2934 0.3050 0.0281  0.0023  -0.0115 286 PHE A C   
1961 O O   . PHE A 269 ? 0.3344 0.3110 0.3208 0.0303  0.0007  -0.0052 286 PHE A O   
1962 C CB  . PHE A 269 ? 0.4110 0.3900 0.4003 0.0262  0.0033  -0.0247 286 PHE A CB  
1963 C CG  . PHE A 269 ? 0.3024 0.2942 0.2909 0.0279  0.0006  -0.0227 286 PHE A CG  
1964 C CD1 . PHE A 269 ? 0.3784 0.3709 0.3700 0.0297  -0.0012 -0.0218 286 PHE A CD1 
1965 C CD2 . PHE A 269 ? 0.3495 0.3537 0.3344 0.0278  0.0000  -0.0215 286 PHE A CD2 
1966 C CE1 . PHE A 269 ? 0.4039 0.4099 0.3951 0.0320  -0.0038 -0.0192 286 PHE A CE1 
1967 C CE2 . PHE A 269 ? 0.3468 0.3646 0.3308 0.0296  -0.0026 -0.0190 286 PHE A CE2 
1968 C CZ  . PHE A 269 ? 0.3182 0.3372 0.3054 0.0320  -0.0046 -0.0176 286 PHE A CZ  
1969 N N   A GLN A 270 ? 0.3307 0.3085 0.3148 0.0266  0.0039  -0.0129 287 GLN A N   
1970 N N   B GLN A 270 ? 0.3429 0.3207 0.3271 0.0266  0.0039  -0.0129 287 GLN A N   
1971 C CA  A GLN A 270 ? 0.3635 0.3474 0.3444 0.0271  0.0035  -0.0073 287 GLN A CA  
1972 C CA  B GLN A 270 ? 0.3656 0.3493 0.3465 0.0271  0.0035  -0.0074 287 GLN A CA  
1973 C C   A GLN A 270 ? 0.3580 0.3330 0.3394 0.0273  0.0037  -0.0006 287 GLN A C   
1974 C C   B GLN A 270 ? 0.3510 0.3260 0.3325 0.0274  0.0037  -0.0006 287 GLN A C   
1975 O O   A GLN A 270 ? 0.3334 0.3112 0.3127 0.0284  0.0033  0.0057  287 GLN A O   
1976 O O   B GLN A 270 ? 0.3328 0.3105 0.3122 0.0285  0.0032  0.0058  287 GLN A O   
1977 C CB  A GLN A 270 ? 0.3636 0.3531 0.3421 0.0253  0.0056  -0.0109 287 GLN A CB  
1978 C CB  B GLN A 270 ? 0.3669 0.3557 0.3455 0.0252  0.0057  -0.0110 287 GLN A CB  
1979 C CG  A GLN A 270 ? 0.4112 0.4105 0.3884 0.0241  0.0062  -0.0181 287 GLN A CG  
1980 C CG  B GLN A 270 ? 0.4191 0.4157 0.3938 0.0254  0.0054  -0.0060 287 GLN A CG  
1981 C CD  A GLN A 270 ? 0.3749 0.3873 0.3500 0.0252  0.0035  -0.0163 287 GLN A CD  
1982 C CD  B GLN A 270 ? 0.3744 0.3803 0.3470 0.0274  0.0028  -0.0017 287 GLN A CD  
1983 O OE1 A GLN A 270 ? 0.4057 0.4210 0.3793 0.0273  0.0015  -0.0086 287 GLN A OE1 
1984 O OE1 B GLN A 270 ? 0.4197 0.4339 0.3924 0.0277  0.0016  -0.0055 287 GLN A OE1 
1985 N NE2 A GLN A 270 ? 0.2795 0.3002 0.2547 0.0237  0.0037  -0.0233 287 GLN A NE2 
1986 N NE2 B GLN A 270 ? 0.2934 0.2982 0.2644 0.0288  0.0023  0.0064  287 GLN A NE2 
1987 N N   . ALA A 271 ? 0.3414 0.3061 0.3254 0.0261  0.0048  -0.0019 288 ALA A N   
1988 C CA  . ALA A 271 ? 0.3079 0.2645 0.2927 0.0255  0.0054  0.0034  288 ALA A CA  
1989 C C   . ALA A 271 ? 0.3255 0.2790 0.3115 0.0274  0.0045  0.0078  288 ALA A C   
1990 O O   . ALA A 271 ? 0.3658 0.3166 0.3508 0.0277  0.0053  0.0139  288 ALA A O   
1991 C CB  . ALA A 271 ? 0.3782 0.3264 0.3656 0.0236  0.0065  0.0005  288 ALA A CB  
1992 N N   . THR A 272 ? 0.3350 0.2885 0.3231 0.0289  0.0032  0.0048  289 THR A N   
1993 C CA  . THR A 272 ? 0.3330 0.2843 0.3229 0.0316  0.0025  0.0090  289 THR A CA  
1994 C C   . THR A 272 ? 0.3550 0.3156 0.3422 0.0345  0.0017  0.0150  289 THR A C   
1995 O O   . THR A 272 ? 0.3460 0.3026 0.3332 0.0365  0.0027  0.0221  289 THR A O   
1996 C CB  . THR A 272 ? 0.3744 0.3264 0.3673 0.0325  0.0013  0.0038  289 THR A CB  
1997 O OG1 . THR A 272 ? 0.4129 0.3556 0.4078 0.0298  0.0025  -0.0008 289 THR A OG1 
1998 C CG2 . THR A 272 ? 0.3957 0.3463 0.3912 0.0358  0.0007  0.0079  289 THR A CG2 
1999 N N   . VAL A 273 ? 0.3356 0.3086 0.3202 0.0347  0.0003  0.0123  290 VAL A N   
2000 C CA  . VAL A 273 ? 0.3012 0.2854 0.2827 0.0374  -0.0008 0.0179  290 VAL A CA  
2001 C C   . VAL A 273 ? 0.2919 0.2719 0.2705 0.0369  0.0012  0.0245  290 VAL A C   
2002 O O   . VAL A 273 ? 0.3480 0.3269 0.3257 0.0397  0.0018  0.0324  290 VAL A O   
2003 C CB  . VAL A 273 ? 0.3091 0.3078 0.2880 0.0363  -0.0022 0.0121  290 VAL A CB  
2004 C CG1 . VAL A 273 ? 0.3496 0.3613 0.3239 0.0381  -0.0031 0.0176  290 VAL A CG1 
2005 C CG2 . VAL A 273 ? 0.3059 0.3103 0.2876 0.0369  -0.0038 0.0064  290 VAL A CG2 
2006 N N   . ALA A 274 ? 0.3114 0.2886 0.2888 0.0333  0.0026  0.0214  291 ALA A N   
2007 C CA  . ALA A 274 ? 0.3302 0.3058 0.3047 0.0321  0.0045  0.0267  291 ALA A CA  
2008 C C   . ALA A 274 ? 0.3581 0.3208 0.3343 0.0318  0.0069  0.0320  291 ALA A C   
2009 O O   . ALA A 274 ? 0.3526 0.3140 0.3267 0.0330  0.0086  0.0393  291 ALA A O   
2010 C CB  . ALA A 274 ? 0.3911 0.3675 0.3649 0.0284  0.0056  0.0217  291 ALA A CB  
2011 N N   . LEU A 275 ? 0.3269 0.2797 0.3069 0.0298  0.0076  0.0283  292 LEU A N   
2012 C CA  . LEU A 275 ? 0.3480 0.2887 0.3297 0.0286  0.0105  0.0322  292 LEU A CA  
2013 C C   . LEU A 275 ? 0.3443 0.2814 0.3275 0.0328  0.0108  0.0372  292 LEU A C   
2014 O O   . LEU A 275 ? 0.3714 0.2999 0.3547 0.0331  0.0142  0.0431  292 LEU A O   
2015 C CB  . LEU A 275 ? 0.4124 0.3453 0.3972 0.0248  0.0111  0.0266  292 LEU A CB  
2016 C CG  . LEU A 275 ? 0.3527 0.2896 0.3363 0.0214  0.0112  0.0230  292 LEU A CG  
2017 C CD1 . LEU A 275 ? 0.5374 0.4683 0.5239 0.0185  0.0116  0.0182  292 LEU A CD1 
2018 C CD2 . LEU A 275 ? 0.4716 0.4087 0.4528 0.0190  0.0136  0.0271  292 LEU A CD2 
2019 N N   . GLY A 276 ? 0.3244 0.2679 0.3091 0.0360  0.0080  0.0350  293 GLY A N   
2020 C CA  . GLY A 276 ? 0.3573 0.3004 0.3435 0.0410  0.0081  0.0406  293 GLY A CA  
2021 C C   . GLY A 276 ? 0.3492 0.2974 0.3318 0.0444  0.0092  0.0494  293 GLY A C   
2022 O O   . GLY A 276 ? 0.3968 0.3382 0.3803 0.0477  0.0119  0.0567  293 GLY A O   
2023 N N   . ARG A 277 ? 0.3781 0.3381 0.3565 0.0438  0.0074  0.0491  294 ARG A N   
2024 C CA  . ARG A 277 ? 0.4431 0.4090 0.4173 0.0470  0.0085  0.0578  294 ARG A CA  
2025 C C   . ARG A 277 ? 0.4293 0.3824 0.4023 0.0446  0.0134  0.0630  294 ARG A C   
2026 O O   . ARG A 277 ? 0.4831 0.4301 0.4557 0.0480  0.0166  0.0714  294 ARG A O   
2027 C CB  . ARG A 277 ? 0.3949 0.3766 0.3647 0.0459  0.0058  0.0551  294 ARG A CB  
2028 C CG  . ARG A 277 ? 0.4451 0.4360 0.4096 0.0489  0.0063  0.0636  294 ARG A CG  
2029 C CD  . ARG A 277 ? 0.4616 0.4641 0.4260 0.0552  0.0039  0.0686  294 ARG A CD  
2030 N NE  . ARG A 277 ? 0.4702 0.4860 0.4288 0.0581  0.0034  0.0758  294 ARG A NE  
2031 C CZ  . ARG A 277 ? 0.4098 0.4443 0.3650 0.0577  0.0001  0.0724  294 ARG A CZ  
2032 N NH1 . ARG A 277 ? 0.4637 0.5050 0.4205 0.0542  -0.0026 0.0617  294 ARG A NH1 
2033 N NH2 . ARG A 277 ? 0.4168 0.4634 0.3667 0.0608  -0.0002 0.0801  294 ARG A NH2 
2034 N N   . LYS A 278 ? 0.4084 0.3570 0.3811 0.0388  0.0144  0.0578  295 LYS A N   
2035 C CA  . LYS A 278 ? 0.4767 0.4166 0.4476 0.0355  0.0190  0.0617  295 LYS A CA  
2036 C C   . LYS A 278 ? 0.5413 0.4649 0.5155 0.0347  0.0235  0.0643  295 LYS A C   
2037 O O   . LYS A 278 ? 0.4952 0.4112 0.4678 0.0349  0.0283  0.0712  295 LYS A O   
2038 C CB  . LYS A 278 ? 0.4652 0.4070 0.4355 0.0296  0.0187  0.0551  295 LYS A CB  
2039 C CG  . LYS A 278 ? 0.5490 0.4824 0.5183 0.0249  0.0234  0.0574  295 LYS A CG  
2040 C CD  . LYS A 278 ? 0.6085 0.5472 0.5776 0.0200  0.0225  0.0511  295 LYS A CD  
2041 C CE  . LYS A 278 ? 0.6231 0.5558 0.5916 0.0146  0.0270  0.0524  295 LYS A CE  
2042 N NZ  . LYS A 278 ? 0.5075 0.4474 0.4765 0.0106  0.0259  0.0466  295 LYS A NZ  
2043 N N   . TYR A 279 ? 0.4657 0.3832 0.4443 0.0334  0.0228  0.0587  296 TYR A N   
2044 C CA  . TYR A 279 ? 0.4750 0.3768 0.4568 0.0312  0.0276  0.0595  296 TYR A CA  
2045 C C   . TYR A 279 ? 0.5050 0.4014 0.4900 0.0367  0.0285  0.0632  296 TYR A C   
2046 O O   . TYR A 279 ? 0.5085 0.3911 0.4961 0.0354  0.0334  0.0645  296 TYR A O   
2047 C CB  . TYR A 279 ? 0.4928 0.3904 0.4772 0.0250  0.0272  0.0508  296 TYR A CB  
2048 C CG  . TYR A 279 ? 0.5330 0.4340 0.5151 0.0194  0.0277  0.0481  296 TYR A CG  
2049 C CD1 . TYR A 279 ? 0.6155 0.5097 0.5961 0.0156  0.0330  0.0516  296 TYR A CD1 
2050 C CD2 . TYR A 279 ? 0.5098 0.4209 0.4914 0.0180  0.0236  0.0422  296 TYR A CD2 
2051 C CE1 . TYR A 279 ? 0.5846 0.4832 0.5634 0.0105  0.0336  0.0492  296 TYR A CE1 
2052 C CE2 . TYR A 279 ? 0.5672 0.4824 0.5473 0.0136  0.0244  0.0403  296 TYR A CE2 
2053 C CZ  . TYR A 279 ? 0.5868 0.4964 0.5656 0.0097  0.0291  0.0437  296 TYR A CZ  
2054 O OH  . TYR A 279 ? 0.5635 0.4781 0.5409 0.0052  0.0301  0.0419  296 TYR A OH  
2055 N N   . HIS A 280 ? 0.4659 0.3734 0.4511 0.0426  0.0242  0.0646  297 HIS A N   
2056 C CA  . HIS A 280 ? 0.4720 0.3764 0.4609 0.0483  0.0247  0.0680  297 HIS A CA  
2057 C C   . HIS A 280 ? 0.4609 0.3770 0.4479 0.0560  0.0229  0.0760  297 HIS A C   
2058 O O   . HIS A 280 ? 0.4456 0.3616 0.4361 0.0617  0.0232  0.0797  297 HIS A O   
2059 C CB  . HIS A 280 ? 0.4763 0.3828 0.4691 0.0473  0.0210  0.0594  297 HIS A CB  
2060 C CG  . HIS A 280 ? 0.5042 0.4011 0.4986 0.0401  0.0223  0.0518  297 HIS A CG  
2061 N ND1 . HIS A 280 ? 0.4612 0.3441 0.4592 0.0380  0.0264  0.0507  297 HIS A ND1 
2062 C CD2 . HIS A 280 ? 0.4704 0.3707 0.4632 0.0348  0.0203  0.0453  297 HIS A CD2 
2063 C CE1 . HIS A 280 ? 0.4862 0.3654 0.4844 0.0314  0.0264  0.0436  297 HIS A CE1 
2064 N NE2 . HIS A 280 ? 0.5192 0.4088 0.5145 0.0298  0.0228  0.0406  297 HIS A NE2 
2065 N N   . GLY A 281 ? 0.5041 0.4319 0.4861 0.0564  0.0209  0.0786  298 GLY A N   
2066 C CA  . GLY A 281 ? 0.4745 0.4155 0.4541 0.0635  0.0191  0.0865  298 GLY A CA  
2067 C C   . GLY A 281 ? 0.4804 0.4369 0.4622 0.0671  0.0134  0.0828  298 GLY A C   
2068 O O   . GLY A 281 ? 0.5550 0.5213 0.5368 0.0740  0.0123  0.0898  298 GLY A O   
2069 N N   . LEU A 282 ? 0.3837 0.3426 0.3674 0.0626  0.0101  0.0721  299 LEU A N   
2070 C CA  . LEU A 282 ? 0.4061 0.3788 0.3921 0.0647  0.0053  0.0670  299 LEU A CA  
2071 C C   . LEU A 282 ? 0.4000 0.3913 0.3814 0.0634  0.0013  0.0638  299 LEU A C   
2072 O O   . LEU A 282 ? 0.4191 0.4095 0.3973 0.0582  0.0015  0.0593  299 LEU A O   
2073 C CB  . LEU A 282 ? 0.4302 0.3946 0.4205 0.0602  0.0047  0.0570  299 LEU A CB  
2074 C CG  . LEU A 282 ? 0.4665 0.4123 0.4609 0.0603  0.0091  0.0592  299 LEU A CG  
2075 C CD1 . LEU A 282 ? 0.4834 0.4210 0.4807 0.0549  0.0088  0.0496  299 LEU A CD1 
2076 C CD2 . LEU A 282 ? 0.4848 0.4322 0.4830 0.0675  0.0097  0.0655  299 LEU A CD2 
2077 N N   . ILE A 283 ? 0.3782 0.3869 0.3593 0.0680  -0.0020 0.0657  300 ILE A N   
2078 C CA  . ILE A 283 ? 0.3880 0.4163 0.3645 0.0668  -0.0053 0.0629  300 ILE A CA  
2079 C C   . ILE A 283 ? 0.3326 0.3753 0.3119 0.0668  -0.0092 0.0552  300 ILE A C   
2080 O O   . ILE A 283 ? 0.3263 0.3738 0.3094 0.0719  -0.0102 0.0587  300 ILE A O   
2081 C CB  . ILE A 283 ? 0.4552 0.4950 0.4272 0.0722  -0.0053 0.0741  300 ILE A CB  
2082 C CG1 . ILE A 283 ? 0.4929 0.5177 0.4618 0.0715  -0.0008 0.0811  300 ILE A CG1 
2083 C CG2 . ILE A 283 ? 0.3621 0.4241 0.3294 0.0706  -0.0089 0.0703  300 ILE A CG2 
2084 C CD1 . ILE A 283 ? 0.5768 0.6102 0.5409 0.0768  0.0002  0.0929  300 ILE A CD1 
2085 N N   . PRO A 284 ? 0.3778 0.4280 0.3556 0.0612  -0.0109 0.0449  301 PRO A N   
2086 C CA  . PRO A 284 ? 0.3420 0.4065 0.3223 0.0606  -0.0138 0.0371  301 PRO A CA  
2087 C C   . PRO A 284 ? 0.4563 0.5431 0.4349 0.0656  -0.0167 0.0429  301 PRO A C   
2088 O O   . PRO A 284 ? 0.4588 0.5561 0.4320 0.0666  -0.0172 0.0479  301 PRO A O   
2089 C CB  . PRO A 284 ? 0.3650 0.4326 0.3427 0.0536  -0.0137 0.0262  301 PRO A CB  
2090 C CG  . PRO A 284 ? 0.3764 0.4264 0.3526 0.0507  -0.0107 0.0272  301 PRO A CG  
2091 C CD  . PRO A 284 ? 0.3511 0.3967 0.3253 0.0553  -0.0095 0.0394  301 PRO A CD  
2092 N N   . GLU A 285 ? 0.4310 0.5272 0.4141 0.0685  -0.0188 0.0415  302 GLU A N   
2093 C CA  . GLU A 285 ? 0.5851 0.7071 0.5668 0.0725  -0.0222 0.0449  302 GLU A CA  
2094 C C   . GLU A 285 ? 0.5707 0.7085 0.5486 0.0654  -0.0237 0.0337  302 GLU A C   
2095 O O   . GLU A 285 ? 0.5927 0.7238 0.5722 0.0590  -0.0226 0.0220  302 GLU A O   
2096 C CB  . GLU A 285 ? 0.6386 0.7677 0.6268 0.0770  -0.0239 0.0454  302 GLU A CB  
2097 C CG  . GLU A 285 ? 0.6745 0.7882 0.6668 0.0843  -0.0216 0.0564  302 GLU A CG  
2098 C CD  . GLU A 285 ? 0.7300 0.8481 0.7297 0.0881  -0.0228 0.0552  302 GLU A CD  
2099 O OE1 . GLU A 285 ? 0.7087 0.8467 0.7099 0.0862  -0.0260 0.0478  302 GLU A OE1 
2100 O OE2 . GLU A 285 ? 0.7060 0.8076 0.7100 0.0926  -0.0200 0.0613  302 GLU A OE2 
2101 O OXT . GLU A 285 ? 0.5460 0.7029 0.5190 0.0660  -0.0254 0.0362  302 GLU A OXT 
2102 N N   . HIS B 7   ? 1.0497 1.1556 1.0908 -0.0744 0.0520  0.0317  24  HIS B N   
2103 C CA  . HIS B 7   ? 1.1251 1.2255 1.1622 -0.0690 0.0525  0.0168  24  HIS B CA  
2104 C C   . HIS B 7   ? 1.0815 1.1717 1.1153 -0.0693 0.0496  0.0155  24  HIS B C   
2105 O O   . HIS B 7   ? 1.1328 1.2349 1.1634 -0.0660 0.0498  0.0192  24  HIS B O   
2106 C CB  . HIS B 7   ? 0.9169 1.0382 0.9509 -0.0611 0.0563  0.0111  24  HIS B CB  
2107 N N   . HIS B 8   ? 1.0892 1.1578 1.1240 -0.0731 0.0470  0.0106  25  HIS B N   
2108 C CA  . HIS B 8   ? 0.9932 1.0503 1.0248 -0.0725 0.0446  0.0064  25  HIS B CA  
2109 C C   . HIS B 8   ? 0.9233 0.9798 0.9514 -0.0669 0.0458  -0.0086 25  HIS B C   
2110 O O   . HIS B 8   ? 0.9491 0.9974 0.9791 -0.0674 0.0464  -0.0170 25  HIS B O   
2111 C CB  . HIS B 8   ? 0.9125 0.9464 0.9466 -0.0793 0.0413  0.0079  25  HIS B CB  
2112 C CG  . HIS B 8   ? 0.9760 1.0061 1.0115 -0.0838 0.0392  0.0206  25  HIS B CG  
2113 N ND1 . HIS B 8   ? 0.7994 0.8115 0.8345 -0.0867 0.0363  0.0206  25  HIS B ND1 
2114 C CD2 . HIS B 8   ? 1.0572 1.0986 1.0946 -0.0858 0.0395  0.0337  25  HIS B CD2 
2115 C CE1 . HIS B 8   ? 0.8435 0.8553 0.8805 -0.0904 0.0350  0.0331  25  HIS B CE1 
2116 N NE2 . HIS B 8   ? 1.0704 1.0999 1.1088 -0.0901 0.0368  0.0414  25  HIS B NE2 
2117 N N   . VAL B 9   ? 0.6970 0.7623 0.7204 -0.0619 0.0460  -0.0117 26  VAL B N   
2118 C CA  . VAL B 9   ? 0.6431 0.7047 0.6630 -0.0577 0.0462  -0.0257 26  VAL B CA  
2119 C C   . VAL B 9   ? 0.5664 0.6219 0.5832 -0.0574 0.0436  -0.0248 26  VAL B C   
2120 O O   . VAL B 9   ? 0.5115 0.5791 0.5264 -0.0557 0.0435  -0.0169 26  VAL B O   
2121 C CB  . VAL B 9   ? 0.6857 0.7669 0.7023 -0.0510 0.0496  -0.0325 26  VAL B CB  
2122 C CG1 . VAL B 9   ? 0.6608 0.7363 0.6741 -0.0474 0.0496  -0.0474 26  VAL B CG1 
2123 C CG2 . VAL B 9   ? 0.7271 0.8160 0.7472 -0.0509 0.0525  -0.0315 26  VAL B CG2 
2124 N N   . VAL B 10  ? 0.5047 0.5421 0.5212 -0.0588 0.0415  -0.0325 27  VAL B N   
2125 C CA  . VAL B 10  ? 0.4408 0.4708 0.4547 -0.0584 0.0390  -0.0324 27  VAL B CA  
2126 C C   . VAL B 10  ? 0.4270 0.4599 0.4367 -0.0534 0.0396  -0.0457 27  VAL B C   
2127 O O   . VAL B 10  ? 0.4532 0.4744 0.4635 -0.0540 0.0392  -0.0559 27  VAL B O   
2128 C CB  . VAL B 10  ? 0.4567 0.4638 0.4736 -0.0641 0.0361  -0.0305 27  VAL B CB  
2129 C CG1 . VAL B 10  ? 0.3987 0.3999 0.4131 -0.0631 0.0339  -0.0290 27  VAL B CG1 
2130 C CG2 . VAL B 10  ? 0.4741 0.4778 0.4955 -0.0698 0.0357  -0.0188 27  VAL B CG2 
2131 N N   . ARG B 11  ? 0.3816 0.4304 0.3870 -0.0488 0.0404  -0.0456 28  ARG B N   
2132 C CA  . ARG B 11  ? 0.3534 0.4064 0.3544 -0.0443 0.0408  -0.0580 28  ARG B CA  
2133 C C   . ARG B 11  ? 0.3576 0.4118 0.3551 -0.0424 0.0388  -0.0564 28  ARG B C   
2134 O O   . ARG B 11  ? 0.3600 0.4154 0.3538 -0.0394 0.0386  -0.0665 28  ARG B O   
2135 C CB  . ARG B 11  ? 0.4236 0.4976 0.4220 -0.0395 0.0441  -0.0626 28  ARG B CB  
2136 C CG  . ARG B 11  ? 0.5023 0.5968 0.4982 -0.0369 0.0450  -0.0534 28  ARG B CG  
2137 C CD  . ARG B 11  ? 0.5874 0.7032 0.5809 -0.0325 0.0485  -0.0572 28  ARG B CD  
2138 N NE  . ARG B 11  ? 0.6363 0.7712 0.6292 -0.0313 0.0495  -0.0451 28  ARG B NE  
2139 C CZ  . ARG B 11  ? 0.7349 0.8923 0.7247 -0.0269 0.0523  -0.0464 28  ARG B CZ  
2140 N NH1 . ARG B 11  ? 0.7055 0.8691 0.6923 -0.0232 0.0546  -0.0596 28  ARG B NH1 
2141 N NH2 . ARG B 11  ? 0.7130 0.8870 0.7028 -0.0263 0.0528  -0.0340 28  ARG B NH2 
2142 N N   . LYS B 12  ? 0.3902 0.4432 0.3891 -0.0444 0.0374  -0.0439 29  LYS B N   
2143 C CA  . LYS B 12  ? 0.3233 0.3773 0.3197 -0.0426 0.0356  -0.0408 29  LYS B CA  
2144 C C   . LYS B 12  ? 0.3089 0.3403 0.3079 -0.0465 0.0328  -0.0379 29  LYS B C   
2145 O O   . LYS B 12  ? 0.3065 0.3266 0.3098 -0.0511 0.0321  -0.0309 29  LYS B O   
2146 C CB  . LYS B 12  ? 0.3249 0.3962 0.3211 -0.0411 0.0363  -0.0278 29  LYS B CB  
2147 C CG  . LYS B 12  ? 0.3130 0.4096 0.3055 -0.0365 0.0390  -0.0300 29  LYS B CG  
2148 C CD  . LYS B 12  ? 0.3329 0.4463 0.3261 -0.0357 0.0395  -0.0156 29  LYS B CD  
2149 C CE  . LYS B 12  ? 0.4237 0.5635 0.4133 -0.0314 0.0424  -0.0174 29  LYS B CE  
2150 N NZ  . LYS B 12  ? 0.4169 0.5675 0.4008 -0.0267 0.0428  -0.0280 29  LYS B NZ  
2151 N N   . ALA B 13  ? 0.3287 0.3546 0.3252 -0.0446 0.0312  -0.0427 30  ALA B N   
2152 C CA  . ALA B 13  ? 0.3079 0.3137 0.3066 -0.0475 0.0287  -0.0398 30  ALA B CA  
2153 C C   . ALA B 13  ? 0.2845 0.2952 0.2809 -0.0442 0.0276  -0.0353 30  ALA B C   
2154 O O   . ALA B 13  ? 0.3637 0.3876 0.3559 -0.0399 0.0280  -0.0410 30  ALA B O   
2155 C CB  . ALA B 13  ? 0.3395 0.3285 0.3383 -0.0490 0.0275  -0.0518 30  ALA B CB  
2156 N N   . VAL B 14  ? 0.3037 0.3031 0.3031 -0.0466 0.0262  -0.0254 31  VAL B N   
2157 C CA  . VAL B 14  ? 0.2836 0.2857 0.2822 -0.0438 0.0252  -0.0187 31  VAL B CA  
2158 C C   . VAL B 14  ? 0.3265 0.3080 0.3256 -0.0448 0.0232  -0.0235 31  VAL B C   
2159 O O   . VAL B 14  ? 0.3192 0.2814 0.3216 -0.0493 0.0222  -0.0228 31  VAL B O   
2160 C CB  . VAL B 14  ? 0.3222 0.3268 0.3246 -0.0455 0.0254  -0.0028 31  VAL B CB  
2161 C CG1 . VAL B 14  ? 0.3093 0.3132 0.3118 -0.0429 0.0244  0.0044  31  VAL B CG1 
2162 C CG2 . VAL B 14  ? 0.3390 0.3664 0.3407 -0.0441 0.0275  0.0029  31  VAL B CG2 
2163 N N   . PHE B 15  ? 0.2830 0.2692 0.2788 -0.0406 0.0225  -0.0279 32  PHE B N   
2164 C CA  . PHE B 15  ? 0.2924 0.2615 0.2882 -0.0407 0.0207  -0.0322 32  PHE B CA  
2165 C C   . PHE B 15  ? 0.3137 0.2859 0.3099 -0.0376 0.0202  -0.0229 32  PHE B C   
2166 O O   . PHE B 15  ? 0.3300 0.3192 0.3228 -0.0331 0.0205  -0.0235 32  PHE B O   
2167 C CB  . PHE B 15  ? 0.3113 0.2824 0.3032 -0.0385 0.0203  -0.0466 32  PHE B CB  
2168 C CG  . PHE B 15  ? 0.3214 0.2917 0.3132 -0.0407 0.0211  -0.0559 32  PHE B CG  
2169 C CD1 . PHE B 15  ? 0.2868 0.2755 0.2765 -0.0390 0.0230  -0.0577 32  PHE B CD1 
2170 C CD2 . PHE B 15  ? 0.3619 0.3133 0.3557 -0.0444 0.0201  -0.0626 32  PHE B CD2 
2171 C CE1 . PHE B 15  ? 0.3502 0.3378 0.3402 -0.0407 0.0240  -0.0664 32  PHE B CE1 
2172 C CE2 . PHE B 15  ? 0.3064 0.2573 0.3006 -0.0462 0.0210  -0.0708 32  PHE B CE2 
2173 C CZ  . PHE B 15  ? 0.3380 0.3066 0.3305 -0.0443 0.0230  -0.0726 32  PHE B CZ  
2174 N N   . PRO B 16  ? 0.3454 0.3024 0.3455 -0.0397 0.0194  -0.0141 33  PRO B N   
2175 C CA  . PRO B 16  ? 0.3006 0.2591 0.3013 -0.0362 0.0190  -0.0060 33  PRO B CA  
2176 C C   . PRO B 16  ? 0.3631 0.3144 0.3614 -0.0337 0.0178  -0.0152 33  PRO B C   
2177 O O   . PRO B 16  ? 0.3076 0.2397 0.3067 -0.0363 0.0167  -0.0220 33  PRO B O   
2178 C CB  . PRO B 16  ? 0.3282 0.2694 0.3343 -0.0400 0.0187  0.0046  33  PRO B CB  
2179 C CG  . PRO B 16  ? 0.3283 0.2664 0.3362 -0.0451 0.0193  0.0044  33  PRO B CG  
2180 C CD  . PRO B 16  ? 0.3397 0.2796 0.3442 -0.0454 0.0192  -0.0097 33  PRO B CD  
2181 N N   . VAL B 17  ? 0.3026 0.2707 0.2976 -0.0287 0.0179  -0.0159 34  VAL B N   
2182 C CA  . VAL B 17  ? 0.3557 0.3204 0.3477 -0.0261 0.0167  -0.0253 34  VAL B CA  
2183 C C   . VAL B 17  ? 0.3570 0.3284 0.3492 -0.0215 0.0165  -0.0172 34  VAL B C   
2184 O O   . VAL B 17  ? 0.4071 0.3903 0.3956 -0.0178 0.0160  -0.0221 34  VAL B O   
2185 C CB  . VAL B 17  ? 0.3452 0.3236 0.3322 -0.0249 0.0168  -0.0378 34  VAL B CB  
2186 C CG1 . VAL B 17  ? 0.3333 0.3000 0.3208 -0.0292 0.0167  -0.0477 34  VAL B CG1 
2187 C CG2 . VAL B 17  ? 0.3316 0.3355 0.3162 -0.0224 0.0182  -0.0340 34  VAL B CG2 
2188 N N   . ALA B 18  ? 0.3606 0.3260 0.3571 -0.0217 0.0169  -0.0043 35  ALA B N   
2189 C CA  . ALA B 18  ? 0.4322 0.4016 0.4300 -0.0173 0.0169  0.0045  35  ALA B CA  
2190 C C   . ALA B 18  ? 0.4869 0.4318 0.4882 -0.0179 0.0161  0.0062  35  ALA B C   
2191 O O   . ALA B 18  ? 0.4095 0.3525 0.4139 -0.0152 0.0165  0.0167  35  ALA B O   
2192 C CB  . ALA B 18  ? 0.3478 0.3319 0.3482 -0.0162 0.0182  0.0191  35  ALA B CB  
2193 N N   . GLY B 19  ? 0.4821 0.4080 0.4832 -0.0215 0.0152  -0.0039 36  GLY B N   
2194 C CA  . GLY B 19  ? 0.4075 0.3102 0.4118 -0.0223 0.0147  -0.0026 36  GLY B CA  
2195 C C   . GLY B 19  ? 0.4489 0.3519 0.4529 -0.0170 0.0144  -0.0010 36  GLY B C   
2196 O O   . GLY B 19  ? 0.4102 0.3222 0.4103 -0.0141 0.0136  -0.0093 36  GLY B O   
2197 N N   . MET B 20  ? 0.4602 0.3533 0.4687 -0.0155 0.0150  0.0099  37  MET B N   
2198 C CA  . MET B 20  ? 0.4959 0.3883 0.5048 -0.0101 0.0150  0.0124  37  MET B CA  
2199 C C   . MET B 20  ? 0.5026 0.3781 0.5100 -0.0104 0.0139  0.0010  37  MET B C   
2200 O O   . MET B 20  ? 0.4943 0.3758 0.4995 -0.0061 0.0133  -0.0027 37  MET B O   
2201 C CB  . MET B 20  ? 0.5215 0.4056 0.5362 -0.0086 0.0162  0.0267  37  MET B CB  
2202 C CG  . MET B 20  ? 0.5750 0.4785 0.5915 -0.0072 0.0173  0.0394  37  MET B CG  
2203 S SD  . MET B 20  ? 0.9208 0.8165 0.9445 -0.0040 0.0188  0.0569  37  MET B SD  
2204 C CE  . MET B 20  ? 0.8479 0.7498 0.8701 0.0036  0.0187  0.0554  37  MET B CE  
2205 N N   . GLY B 21  ? 0.5325 0.3882 0.5411 -0.0157 0.0134  -0.0046 38  GLY B N   
2206 C CA  . GLY B 21  ? 0.4894 0.3298 0.4965 -0.0164 0.0123  -0.0156 38  GLY B CA  
2207 C C   . GLY B 21  ? 0.5082 0.3417 0.5170 -0.0114 0.0126  -0.0119 38  GLY B C   
2208 O O   . GLY B 21  ? 0.5264 0.3635 0.5324 -0.0082 0.0117  -0.0189 38  GLY B O   
2209 N N   . THR B 22  ? 0.5194 0.3440 0.5329 -0.0102 0.0139  -0.0003 39  THR B N   
2210 C CA  . THR B 22  ? 0.5436 0.3614 0.5592 -0.0049 0.0146  0.0041  39  THR B CA  
2211 C C   . THR B 22  ? 0.5941 0.3933 0.6088 -0.0058 0.0137  -0.0063 39  THR B C   
2212 O O   . THR B 22  ? 0.5599 0.3593 0.5739 -0.0009 0.0137  -0.0081 39  THR B O   
2213 C CB  . THR B 22  ? 0.6268 0.4346 0.6483 -0.0043 0.0162  0.0178  39  THR B CB  
2214 O OG1 . THR B 22  ? 0.7124 0.4984 0.7362 -0.0104 0.0162  0.0159  39  THR B OG1 
2215 C CG2 . THR B 22  ? 0.5805 0.4074 0.6033 -0.0035 0.0170  0.0288  39  THR B CG2 
2216 N N   . ARG B 23  ? 0.5688 0.3525 0.5835 -0.0121 0.0131  -0.0131 40  ARG B N   
2217 C CA  . ARG B 23  ? 0.6488 0.4156 0.6624 -0.0134 0.0122  -0.0235 40  ARG B CA  
2218 C C   . ARG B 23  ? 0.5404 0.3187 0.5494 -0.0115 0.0107  -0.0342 40  ARG B C   
2219 O O   . ARG B 23  ? 0.6268 0.3942 0.6349 -0.0114 0.0100  -0.0423 40  ARG B O   
2220 C CB  . ARG B 23  ? 0.6934 0.4468 0.7069 -0.0208 0.0109  -0.0280 40  ARG B CB  
2221 C CG  . ARG B 23  ? 0.7661 0.5100 0.7816 -0.0227 0.0102  -0.0181 40  ARG B CG  
2222 C CD  . ARG B 23  ? 0.8920 0.6375 0.8997 -0.0274 0.0031  -0.0209 40  ARG B CD  
2223 N NE  . ARG B 23  ? 1.0187 0.7687 1.0283 -0.0326 0.0036  -0.0198 40  ARG B NE  
2224 C CZ  . ARG B 23  ? 1.0811 0.8295 1.0874 -0.0369 -0.0005 -0.0174 40  ARG B CZ  
2225 N NH1 . ARG B 23  ? 0.8844 0.6273 0.8862 -0.0369 -0.0042 -0.0152 40  ARG B NH1 
2226 N NH2 . ARG B 23  ? 1.0894 0.8439 1.0975 -0.0412 -0.0002 -0.0176 40  ARG B NH2 
2227 N N   . PHE B 24  ? 0.5050 0.3047 0.5111 -0.0106 0.0103  -0.0350 41  PHE B N   
2228 C CA  . PHE B 24  ? 0.4637 0.2756 0.4653 -0.0093 0.0088  -0.0453 41  PHE B CA  
2229 C C   . PHE B 24  ? 0.4974 0.3286 0.4974 -0.0029 0.0090  -0.0410 41  PHE B C   
2230 O O   . PHE B 24  ? 0.4230 0.2683 0.4191 -0.0019 0.0078  -0.0485 41  PHE B O   
2231 C CB  . PHE B 24  ? 0.4249 0.2454 0.4241 -0.0140 0.0081  -0.0519 41  PHE B CB  
2232 C CG  . PHE B 24  ? 0.4383 0.2411 0.4388 -0.0203 0.0076  -0.0574 41  PHE B CG  
2233 C CD1 . PHE B 24  ? 0.4869 0.2794 0.4908 -0.0239 0.0086  -0.0502 41  PHE B CD1 
2234 C CD2 . PHE B 24  ? 0.4843 0.2878 0.4800 -0.0213 0.0037  -0.0657 41  PHE B CD2 
2235 C CE1 . PHE B 24  ? 0.4646 0.2523 0.4663 -0.0278 0.0043  -0.0513 41  PHE B CE1 
2236 C CE2 . PHE B 24  ? 0.4911 0.2951 0.4816 -0.0234 -0.0020 -0.0621 41  PHE B CE2 
2237 C CZ  . PHE B 24  ? 0.4684 0.2651 0.4625 -0.0266 -0.0019 -0.0559 41  PHE B CZ  
2238 N N   . LEU B 25  ? 0.4319 0.2649 0.4350 0.0013  0.0104  -0.0290 42  LEU B N   
2239 C CA  . LEU B 25  ? 0.4091 0.2588 0.4111 0.0078  0.0106  -0.0248 42  LEU B CA  
2240 C C   . LEU B 25  ? 0.4790 0.3216 0.4796 0.0104  0.0097  -0.0322 42  LEU B C   
2241 O O   . LEU B 25  ? 0.4843 0.3058 0.4869 0.0091  0.0098  -0.0349 42  LEU B O   
2242 C CB  . LEU B 25  ? 0.4530 0.3040 0.4594 0.0119  0.0125  -0.0097 42  LEU B CB  
2243 C CG  . LEU B 25  ? 0.4644 0.3312 0.4716 0.0111  0.0133  -0.0007 42  LEU B CG  
2244 C CD1 . LEU B 25  ? 0.5145 0.3778 0.5273 0.0140  0.0152  0.0145  42  LEU B CD1 
2245 C CD2 . LEU B 25  ? 0.3896 0.2831 0.3925 0.0137  0.0126  -0.0025 42  LEU B CD2 
2246 N N   . PRO B 26  ? 0.4019 0.2619 0.3992 0.0141  0.0088  -0.0354 43  PRO B N   
2247 C CA  . PRO B 26  ? 0.4576 0.3439 0.4523 0.0163  0.0086  -0.0323 43  PRO B CA  
2248 C C   . PRO B 26  ? 0.3815 0.2801 0.3718 0.0121  0.0074  -0.0416 43  PRO B C   
2249 O O   . PRO B 26  ? 0.3439 0.2645 0.3315 0.0136  0.0073  -0.0398 43  PRO B O   
2250 C CB  . PRO B 26  ? 0.3976 0.2933 0.3908 0.0219  0.0080  -0.0330 43  PRO B CB  
2251 C CG  . PRO B 26  ? 0.4295 0.3074 0.4222 0.0202  0.0070  -0.0432 43  PRO B CG  
2252 C CD  . PRO B 26  ? 0.4610 0.3151 0.4576 0.0171  0.0080  -0.0408 43  PRO B CD  
2253 N N   . ALA B 27  ? 0.3986 0.2840 0.3880 0.0069  0.0064  -0.0517 44  ALA B N   
2254 C CA  . ALA B 27  ? 0.3940 0.2904 0.3796 0.0034  0.0054  -0.0613 44  ALA B CA  
2255 C C   . ALA B 27  ? 0.3462 0.2560 0.3316 0.0022  0.0065  -0.0554 44  ALA B C   
2256 O O   . ALA B 27  ? 0.3870 0.3137 0.3687 0.0014  0.0060  -0.0605 44  ALA B O   
2257 C CB  . ALA B 27  ? 0.4477 0.3263 0.4335 -0.0020 0.0045  -0.0714 44  ALA B CB  
2258 N N   . THR B 28  ? 0.3671 0.2694 0.3563 0.0018  0.0079  -0.0449 45  THR B N   
2259 C CA  . THR B 28  ? 0.4046 0.3196 0.3942 0.0008  0.0090  -0.0380 45  THR B CA  
2260 C C   . THR B 28  ? 0.3923 0.3266 0.3821 0.0060  0.0099  -0.0268 45  THR B C   
2261 O O   . THR B 28  ? 0.3502 0.2942 0.3414 0.0058  0.0111  -0.0182 45  THR B O   
2262 C CB  . THR B 28  ? 0.4040 0.3017 0.3979 -0.0029 0.0100  -0.0320 45  THR B CB  
2263 O OG1 . THR B 28  ? 0.3492 0.2313 0.3471 -0.0007 0.0106  -0.0249 45  THR B OG1 
2264 C CG2 . THR B 28  ? 0.4104 0.2934 0.4039 -0.0088 0.0092  -0.0425 45  THR B CG2 
2265 N N   . LYS B 29  ? 0.3243 0.2654 0.3132 0.0107  0.0095  -0.0262 46  LYS B N   
2266 C CA  . LYS B 29  ? 0.4044 0.3662 0.3935 0.0156  0.0103  -0.0155 46  LYS B CA  
2267 C C   . LYS B 29  ? 0.3986 0.3848 0.3836 0.0147  0.0103  -0.0175 46  LYS B C   
2268 O O   . LYS B 29  ? 0.3922 0.3926 0.3785 0.0162  0.0114  -0.0071 46  LYS B O   
2269 C CB  . LYS B 29  ? 0.3686 0.3365 0.3567 0.0206  0.0097  -0.0157 46  LYS B CB  
2270 C CG  . LYS B 29  ? 0.3767 0.3676 0.3653 0.0256  0.0106  -0.0040 46  LYS B CG  
2271 C CD  . LYS B 29  ? 0.5131 0.5035 0.5033 0.0310  0.0106  0.0004  46  LYS B CD  
2272 C CE  . LYS B 29  ? 0.5063 0.5201 0.4974 0.0363  0.0115  0.0126  46  LYS B CE  
2273 N NZ  . LYS B 29  ? 0.4180 0.4577 0.4039 0.0357  0.0107  0.0087  46  LYS B NZ  
2274 N N   . ALA B 30  ? 0.4083 0.3997 0.3885 0.0122  0.0090  -0.0309 47  ALA B N   
2275 C CA  . ALA B 30  ? 0.4185 0.4332 0.3942 0.0116  0.0089  -0.0349 47  ALA B CA  
2276 C C   . ALA B 30  ? 0.3880 0.3984 0.3623 0.0065  0.0090  -0.0434 47  ALA B C   
2277 O O   . ALA B 30  ? 0.3819 0.4097 0.3520 0.0057  0.0090  -0.0492 47  ALA B O   
2278 C CB  . ALA B 30  ? 0.4496 0.4782 0.4206 0.0134  0.0074  -0.0436 47  ALA B CB  
2279 N N   . MET B 31  ? 0.3720 0.3599 0.3493 0.0030  0.0091  -0.0451 48  MET B N   
2280 C CA  . MET B 31  ? 0.3400 0.3247 0.3167 -0.0017 0.0094  -0.0510 48  MET B CA  
2281 C C   . MET B 31  ? 0.3388 0.3048 0.3205 -0.0043 0.0103  -0.0434 48  MET B C   
2282 O O   . MET B 31  ? 0.3646 0.3143 0.3498 -0.0034 0.0102  -0.0388 48  MET B O   
2283 C CB  . MET B 31  ? 0.3957 0.3729 0.3698 -0.0046 0.0081  -0.0663 48  MET B CB  
2284 C CG  . MET B 31  ? 0.4175 0.3718 0.3940 -0.0056 0.0070  -0.0698 48  MET B CG  
2285 S SD  . MET B 31  ? 0.4628 0.4138 0.4359 -0.0076 0.0052  -0.0865 48  MET B SD  
2286 C CE  . MET B 31  ? 0.6058 0.5787 0.5747 -0.0029 0.0043  -0.0875 48  MET B CE  
2287 N N   . PRO B 32  ? 0.3188 0.2872 0.3013 -0.0073 0.0113  -0.0416 49  PRO B N   
2288 C CA  . PRO B 32  ? 0.3443 0.2945 0.3314 -0.0106 0.0119  -0.0354 49  PRO B CA  
2289 C C   . PRO B 32  ? 0.3671 0.2953 0.3551 -0.0146 0.0109  -0.0451 49  PRO B C   
2290 O O   . PRO B 32  ? 0.3044 0.2327 0.2894 -0.0154 0.0099  -0.0571 49  PRO B O   
2291 C CB  . PRO B 32  ? 0.3896 0.3521 0.3766 -0.0127 0.0131  -0.0321 49  PRO B CB  
2292 C CG  . PRO B 32  ? 0.3437 0.3230 0.3255 -0.0122 0.0129  -0.0427 49  PRO B CG  
2293 C CD  . PRO B 32  ? 0.3492 0.3369 0.3282 -0.0081 0.0119  -0.0457 49  PRO B CD  
2294 N N   . LYS B 33  ? 0.3094 0.3142 0.3302 0.0125  0.0411  0.0146  50  LYS B N   
2295 C CA  . LYS B 33  ? 0.3526 0.3550 0.3642 0.0128  0.0442  0.0086  50  LYS B CA  
2296 C C   . LYS B 33  ? 0.3236 0.3236 0.3210 0.0094  0.0379  0.0070  50  LYS B C   
2297 O O   . LYS B 33  ? 0.3652 0.3673 0.3555 0.0079  0.0382  0.0072  50  LYS B O   
2298 C CB  . LYS B 33  ? 0.4282 0.4249 0.4409 0.0152  0.0492  0.0003  50  LYS B CB  
2299 C CG  . LYS B 33  ? 0.3750 0.3687 0.3764 0.0141  0.0518  -0.0071 50  LYS B CG  
2300 C CD  . LYS B 33  ? 0.3866 0.3853 0.3876 0.0136  0.0564  -0.0048 50  LYS B CD  
2301 C CE  . LYS B 33  ? 0.4987 0.4949 0.4904 0.0121  0.0614  -0.0130 50  LYS B CE  
2302 N NZ  . LYS B 33  ? 0.4382 0.4296 0.4170 0.0095  0.0566  -0.0189 50  LYS B NZ  
2303 N N   . GLU B 34  ? 0.3334 0.3294 0.3276 0.0078  0.0321  0.0059  51  GLU B N   
2304 C CA  . GLU B 34  ? 0.3529 0.3459 0.3360 0.0049  0.0266  0.0043  51  GLU B CA  
2305 C C   . GLU B 34  ? 0.2831 0.2805 0.2636 0.0019  0.0235  0.0107  51  GLU B C   
2306 O O   . GLU B 34  ? 0.3489 0.3445 0.3212 -0.0005 0.0198  0.0101  51  GLU B O   
2307 C CB  . GLU B 34  ? 0.3555 0.3427 0.3378 0.0041  0.0222  0.0014  51  GLU B CB  
2308 C CG  . GLU B 34  ? 0.4096 0.3913 0.3918 0.0065  0.0242  -0.0061 51  GLU B CG  
2309 C CD  . GLU B 34  ? 0.4529 0.4352 0.4460 0.0097  0.0292  -0.0064 51  GLU B CD  
2310 O OE1 . GLU B 34  ? 0.4121 0.3992 0.4142 0.0099  0.0299  -0.0002 51  GLU B OE1 
2311 O OE2 . GLU B 34  ? 0.4337 0.4121 0.4270 0.0117  0.0324  -0.0127 51  GLU B OE2 
2312 N N   . MET B 35  ? 0.3058 0.3093 0.2935 0.0018  0.0252  0.0171  52  MET B N   
2313 C CA  . MET B 35  ? 0.3325 0.3408 0.3174 -0.0012 0.0231  0.0230  52  MET B CA  
2314 C C   . MET B 35  ? 0.3347 0.3474 0.3178 -0.0002 0.0269  0.0243  52  MET B C   
2315 O O   . MET B 35  ? 0.3017 0.3185 0.2823 -0.0024 0.0255  0.0291  52  MET B O   
2316 C CB  . MET B 35  ? 0.3125 0.3262 0.3055 -0.0033 0.0220  0.0302  52  MET B CB  
2317 C CG  . MET B 35  ? 0.3129 0.3235 0.3047 -0.0069 0.0173  0.0302  52  MET B CG  
2318 S SD  . MET B 35  ? 0.3335 0.3401 0.3145 -0.0111 0.0129  0.0288  52  MET B SD  
2319 C CE  . MET B 35  ? 0.2632 0.2778 0.2436 -0.0138 0.0134  0.0362  52  MET B CE  
2320 N N   . LEU B 36  ? 0.3241 0.3360 0.3085 0.0028  0.0322  0.0200  53  LEU B N   
2321 C CA  . LEU B 36  ? 0.3394 0.3548 0.3204 0.0029  0.0359  0.0204  53  LEU B CA  
2322 C C   . LEU B 36  ? 0.2998 0.3134 0.2680 0.0000  0.0319  0.0184  53  LEU B C   
2323 O O   . LEU B 36  ? 0.3110 0.3194 0.2732 -0.0007 0.0288  0.0137  53  LEU B O   
2324 C CB  . LEU B 36  ? 0.3554 0.3698 0.3397 0.0057  0.0434  0.0151  53  LEU B CB  
2325 C CG  . LEU B 36  ? 0.3803 0.3968 0.3797 0.0089  0.0485  0.0176  53  LEU B CG  
2326 C CD1 . LEU B 36  ? 0.4098 0.4252 0.4128 0.0112  0.0572  0.0121  53  LEU B CD1 
2327 C CD2 . LEU B 36  ? 0.4008 0.4248 0.4087 0.0086  0.0480  0.0271  53  LEU B CD2 
2328 N N   . PRO B 37  ? 0.2985 0.3166 0.2631 -0.0016 0.0317  0.0224  54  PRO B N   
2329 C CA  . PRO B 37  ? 0.3626 0.3798 0.3163 -0.0044 0.0278  0.0217  54  PRO B CA  
2330 C C   . PRO B 37  ? 0.4057 0.4226 0.3520 -0.0048 0.0310  0.0165  54  PRO B C   
2331 O O   . PRO B 37  ? 0.3483 0.3669 0.2972 -0.0034 0.0376  0.0140  54  PRO B O   
2332 C CB  . PRO B 37  ? 0.3460 0.3686 0.2997 -0.0062 0.0267  0.0286  54  PRO B CB  
2333 C CG  . PRO B 37  ? 0.3405 0.3679 0.3030 -0.0039 0.0324  0.0312  54  PRO B CG  
2334 C CD  . PRO B 37  ? 0.3304 0.3552 0.3016 -0.0014 0.0342  0.0291  54  PRO B CD  
2335 N N   . VAL B 38  ? 0.3287 0.3435 0.2661 -0.0074 0.0263  0.0150  55  VAL B N   
2336 C CA  . VAL B 38  ? 0.3792 0.3956 0.3072 -0.0098 0.0275  0.0121  55  VAL B CA  
2337 C C   . VAL B 38  ? 0.4404 0.4605 0.3638 -0.0124 0.0235  0.0180  55  VAL B C   
2338 O O   . VAL B 38  ? 0.3895 0.4077 0.3117 -0.0138 0.0175  0.0207  55  VAL B O   
2339 C CB  . VAL B 38  ? 0.3274 0.3396 0.2494 -0.0114 0.0248  0.0069  55  VAL B CB  
2340 C CG1 . VAL B 38  ? 0.4219 0.4372 0.3330 -0.0154 0.0254  0.0046  55  VAL B CG1 
2341 C CG2 . VAL B 38  ? 0.3999 0.4083 0.3271 -0.0087 0.0292  0.0009  55  VAL B CG2 
2342 N N   . VAL B 39  ? 0.4085 0.4336 0.3310 -0.0128 0.0273  0.0201  56  VAL B N   
2343 C CA  . VAL B 39  ? 0.4157 0.4450 0.3354 -0.0148 0.0248  0.0262  56  VAL B CA  
2344 C C   . VAL B 39  ? 0.4350 0.4644 0.3619 -0.0138 0.0222  0.0317  56  VAL B C   
2345 O O   . VAL B 39  ? 0.4996 0.5322 0.4327 -0.0123 0.0255  0.0346  56  VAL B O   
2346 C CB  . VAL B 39  ? 0.4549 0.4845 0.3656 -0.0185 0.0195  0.0272  56  VAL B CB  
2347 C CG1 . VAL B 39  ? 0.4860 0.5200 0.3948 -0.0203 0.0173  0.0337  56  VAL B CG1 
2348 C CG2 . VAL B 39  ? 0.4305 0.4617 0.3329 -0.0209 0.0222  0.0222  56  VAL B CG2 
2349 N N   . ASP B 40  ? 0.3948 0.4209 0.3209 -0.0153 0.0165  0.0335  57  ASP B N   
2350 C CA  . ASP B 40  ? 0.4178 0.4439 0.3492 -0.0159 0.0143  0.0382  57  ASP B CA  
2351 C C   . ASP B 40  ? 0.3821 0.4025 0.3178 -0.0156 0.0117  0.0362  57  ASP B C   
2352 O O   . ASP B 40  ? 0.3604 0.3795 0.2987 -0.0176 0.0092  0.0392  57  ASP B O   
2353 C CB  . ASP B 40  ? 0.4317 0.4595 0.3592 -0.0189 0.0109  0.0429  57  ASP B CB  
2354 C CG  . ASP B 40  ? 0.4705 0.4946 0.3942 -0.0205 0.0064  0.0418  57  ASP B CG  
2355 O OD1 . ASP B 40  ? 0.4757 0.4961 0.3988 -0.0195 0.0057  0.0372  57  ASP B OD1 
2356 O OD2 . ASP B 40  ? 0.5719 0.5970 0.4939 -0.0229 0.0036  0.0459  57  ASP B OD2 
2357 N N   . LYS B 41  ? 0.3777 0.3944 0.3140 -0.0137 0.0125  0.0309  58  LYS B N   
2358 C CA  . LYS B 41  ? 0.3870 0.3978 0.3263 -0.0137 0.0096  0.0285  58  LYS B CA  
2359 C C   . LYS B 41  ? 0.3459 0.3545 0.2893 -0.0108 0.0125  0.0239  58  LYS B C   
2360 O O   . LYS B 41  ? 0.3547 0.3634 0.2954 -0.0093 0.0153  0.0198  58  LYS B O   
2361 C CB  . LYS B 41  ? 0.3636 0.3710 0.2981 -0.0152 0.0056  0.0270  58  LYS B CB  
2362 C CG  . LYS B 41  ? 0.3882 0.3892 0.3263 -0.0153 0.0026  0.0249  58  LYS B CG  
2363 C CD  . LYS B 41  ? 0.3859 0.3843 0.3214 -0.0169 -0.0015 0.0248  58  LYS B CD  
2364 C CE  . LYS B 41  ? 0.4333 0.4333 0.3689 -0.0195 -0.0038 0.0304  58  LYS B CE  
2365 N NZ  . LYS B 41  ? 0.4492 0.4476 0.3839 -0.0210 -0.0079 0.0316  58  LYS B NZ  
2366 N N   . PRO B 42  ? 0.3407 0.3474 0.2906 -0.0104 0.0121  0.0244  59  PRO B N   
2367 C CA  . PRO B 42  ? 0.2826 0.2872 0.2373 -0.0075 0.0148  0.0205  59  PRO B CA  
2368 C C   . PRO B 42  ? 0.3158 0.3150 0.2667 -0.0068 0.0134  0.0144  59  PRO B C   
2369 O O   . PRO B 42  ? 0.3011 0.2969 0.2485 -0.0086 0.0092  0.0140  59  PRO B O   
2370 C CB  . PRO B 42  ? 0.3440 0.3478 0.3051 -0.0088 0.0131  0.0230  59  PRO B CB  
2371 C CG  . PRO B 42  ? 0.3362 0.3431 0.2962 -0.0122 0.0113  0.0284  59  PRO B CG  
2372 C CD  . PRO B 42  ? 0.3649 0.3714 0.3177 -0.0132 0.0096  0.0284  59  PRO B CD  
2373 N N   . LEU B 43  ? 0.3373 0.3358 0.2895 -0.0042 0.0174  0.0099  60  LEU B N   
2374 C CA  . LEU B 43  ? 0.2910 0.2844 0.2397 -0.0038 0.0164  0.0038  60  LEU B CA  
2375 C C   . LEU B 43  ? 0.2861 0.2743 0.2365 -0.0046 0.0115  0.0034  60  LEU B C   
2376 O O   . LEU B 43  ? 0.3383 0.3235 0.2841 -0.0060 0.0079  0.0016  60  LEU B O   
2377 C CB  . LEU B 43  ? 0.3519 0.3443 0.3048 -0.0010 0.0219  -0.0009 60  LEU B CB  
2378 C CG  . LEU B 43  ? 0.3969 0.3927 0.3474 -0.0006 0.0280  -0.0032 60  LEU B CG  
2379 C CD1 . LEU B 43  ? 0.3900 0.3848 0.3491 0.0027  0.0346  -0.0064 60  LEU B CD1 
2380 C CD2 . LEU B 43  ? 0.3935 0.3883 0.3333 -0.0033 0.0269  -0.0075 60  LEU B CD2 
2381 N N   . ILE B 44  ? 0.3126 0.3000 0.2698 -0.0043 0.0113  0.0054  61  ILE B N   
2382 C CA  . ILE B 44  ? 0.3092 0.2912 0.2684 -0.0054 0.0076  0.0041  61  ILE B CA  
2383 C C   . ILE B 44  ? 0.3124 0.2929 0.2683 -0.0085 0.0034  0.0064  61  ILE B C   
2384 O O   . ILE B 44  ? 0.3111 0.2864 0.2669 -0.0093 0.0005  0.0042  61  ILE B O   
2385 C CB  . ILE B 44  ? 0.3027 0.2855 0.2693 -0.0057 0.0083  0.0064  61  ILE B CB  
2386 C CG1 . ILE B 44  ? 0.2667 0.2437 0.2350 -0.0074 0.0051  0.0043  61  ILE B CG1 
2387 C CG2 . ILE B 44  ? 0.2818 0.2703 0.2498 -0.0081 0.0086  0.0129  61  ILE B CG2 
2388 C CD1 . ILE B 44  ? 0.3262 0.2975 0.2936 -0.0053 0.0045  -0.0018 61  ILE B CD1 
2389 N N   . GLN B 45  ? 0.3208 0.3055 0.2750 -0.0102 0.0034  0.0111  62  GLN B N   
2390 C CA  . GLN B 45  ? 0.3644 0.3474 0.3170 -0.0131 0.0001  0.0136  62  GLN B CA  
2391 C C   . GLN B 45  ? 0.3588 0.3405 0.3068 -0.0130 -0.0024 0.0121  62  GLN B C   
2392 O O   . GLN B 45  ? 0.3452 0.3232 0.2948 -0.0146 -0.0056 0.0129  62  GLN B O   
2393 C CB  . GLN B 45  ? 0.3682 0.3561 0.3200 -0.0152 0.0007  0.0191  62  GLN B CB  
2394 C CG  . GLN B 45  ? 0.3842 0.3698 0.3361 -0.0184 -0.0020 0.0217  62  GLN B CG  
2395 C CD  . GLN B 45  ? 0.4285 0.4183 0.3801 -0.0209 -0.0011 0.0267  62  GLN B CD  
2396 O OE1 . GLN B 45  ? 0.3717 0.3657 0.3243 -0.0212 0.0011  0.0286  62  GLN B OE1 
2397 N NE2 . GLN B 45  ? 0.3884 0.3778 0.3392 -0.0230 -0.0028 0.0296  62  GLN B NE2 
2398 N N   . TYR B 46  ? 0.3237 0.3084 0.2667 -0.0117 -0.0008 0.0103  63  TYR B N   
2399 C CA  . TYR B 46  ? 0.3482 0.3323 0.2865 -0.0126 -0.0036 0.0089  63  TYR B CA  
2400 C C   . TYR B 46  ? 0.3407 0.3189 0.2819 -0.0119 -0.0058 0.0051  63  TYR B C   
2401 O O   . TYR B 46  ? 0.2948 0.2709 0.2364 -0.0134 -0.0097 0.0063  63  TYR B O   
2402 C CB  . TYR B 46  ? 0.3490 0.3371 0.2806 -0.0123 -0.0008 0.0061  63  TYR B CB  
2403 C CG  . TYR B 46  ? 0.3583 0.3525 0.2858 -0.0135 0.0011  0.0095  63  TYR B CG  
2404 C CD1 . TYR B 46  ? 0.3290 0.3260 0.2588 -0.0119 0.0058  0.0100  63  TYR B CD1 
2405 C CD2 . TYR B 46  ? 0.3808 0.3786 0.3026 -0.0166 -0.0019 0.0128  63  TYR B CD2 
2406 C CE1 . TYR B 46  ? 0.3577 0.3602 0.2841 -0.0129 0.0077  0.0131  63  TYR B CE1 
2407 C CE2 . TYR B 46  ? 0.3959 0.3993 0.3137 -0.0178 -0.0001 0.0159  63  TYR B CE2 
2408 C CZ  . TYR B 46  ? 0.3847 0.3901 0.3046 -0.0159 0.0049  0.0156  63  TYR B CZ  
2409 O OH  . TYR B 46  ? 0.4148 0.4258 0.3313 -0.0170 0.0070  0.0185  63  TYR B OH  
2410 N N   . ALA B 47  ? 0.2871 0.2627 0.2311 -0.0097 -0.0032 0.0009  64  ALA B N   
2411 C CA  . ALA B 47  ? 0.3099 0.2798 0.2563 -0.0089 -0.0050 -0.0031 64  ALA B CA  
2412 C C   . ALA B 47  ? 0.3114 0.2767 0.2637 -0.0103 -0.0077 -0.0012 64  ALA B C   
2413 O O   . ALA B 47  ? 0.3208 0.2820 0.2751 -0.0109 -0.0107 -0.0023 64  ALA B O   
2414 C CB  . ALA B 47  ? 0.2922 0.2607 0.2406 -0.0062 -0.0013 -0.0078 64  ALA B CB  
2415 N N   . VAL B 48  ? 0.3482 0.3142 0.3039 -0.0113 -0.0064 0.0016  65  VAL B N   
2416 C CA  . VAL B 48  ? 0.3042 0.2656 0.2651 -0.0137 -0.0080 0.0028  65  VAL B CA  
2417 C C   . VAL B 48  ? 0.3461 0.3070 0.3075 -0.0155 -0.0108 0.0063  65  VAL B C   
2418 O O   . VAL B 48  ? 0.3094 0.2652 0.2755 -0.0165 -0.0127 0.0058  65  VAL B O   
2419 C CB  . VAL B 48  ? 0.3503 0.3135 0.3134 -0.0157 -0.0058 0.0053  65  VAL B CB  
2420 C CG1 . VAL B 48  ? 0.3868 0.3458 0.3542 -0.0195 -0.0065 0.0065  65  VAL B CG1 
2421 C CG2 . VAL B 48  ? 0.3921 0.3553 0.3572 -0.0144 -0.0038 0.0026  65  VAL B CG2 
2422 N N   . GLU B 49  ? 0.3452 0.3117 0.3025 -0.0160 -0.0111 0.0101  66  GLU B N   
2423 C CA  . GLU B 49  ? 0.3926 0.3594 0.3513 -0.0179 -0.0140 0.0145  66  GLU B CA  
2424 C C   . GLU B 49  ? 0.3411 0.3062 0.3002 -0.0174 -0.0173 0.0134  66  GLU B C   
2425 O O   . GLU B 49  ? 0.3809 0.3431 0.3464 -0.0187 -0.0197 0.0161  66  GLU B O   
2426 C CB  . GLU B 49  ? 0.3890 0.3627 0.3424 -0.0186 -0.0137 0.0188  66  GLU B CB  
2427 C CG  . GLU B 49  ? 0.4232 0.3982 0.3782 -0.0200 -0.0112 0.0214  66  GLU B CG  
2428 C CD  . GLU B 49  ? 0.4536 0.4355 0.4032 -0.0204 -0.0102 0.0251  66  GLU B CD  
2429 O OE1 . GLU B 49  ? 0.4526 0.4386 0.3965 -0.0197 -0.0109 0.0251  66  GLU B OE1 
2430 O OE2 . GLU B 49  ? 0.5271 0.5103 0.4781 -0.0220 -0.0086 0.0280  66  GLU B OE2 
2431 N N   . GLU B 50  ? 0.3685 0.3352 0.3219 -0.0158 -0.0172 0.0096  67  GLU B N   
2432 C CA  . GLU B 50  ? 0.3544 0.3198 0.3077 -0.0159 -0.0203 0.0081  67  GLU B CA  
2433 C C   . GLU B 50  ? 0.4135 0.3715 0.3746 -0.0153 -0.0211 0.0056  67  GLU B C   
2434 O O   . GLU B 50  ? 0.3554 0.3114 0.3215 -0.0162 -0.0244 0.0078  67  GLU B O   
2435 C CB  . GLU B 50  ? 0.4121 0.3801 0.3574 -0.0149 -0.0187 0.0032  67  GLU B CB  
2436 C CG  . GLU B 50  ? 0.4415 0.4084 0.3854 -0.0156 -0.0218 0.0010  67  GLU B CG  
2437 C CD  . GLU B 50  ? 0.4400 0.4087 0.3761 -0.0151 -0.0191 -0.0050 67  GLU B CD  
2438 O OE1 . GLU B 50  ? 0.3784 0.3512 0.3089 -0.0152 -0.0156 -0.0058 67  GLU B OE1 
2439 O OE2 . GLU B 50  ? 0.3527 0.3184 0.2886 -0.0148 -0.0201 -0.0091 67  GLU B OE2 
2440 N N   . ALA B 51  ? 0.3694 0.3236 0.3321 -0.0138 -0.0182 0.0013  68  ALA B N   
2441 C CA  . ALA B 51  ? 0.3668 0.3140 0.3363 -0.0136 -0.0185 -0.0016 68  ALA B CA  
2442 C C   . ALA B 51  ? 0.4085 0.3523 0.3862 -0.0160 -0.0191 0.0021  68  ALA B C   
2443 O O   . ALA B 51  ? 0.3614 0.3006 0.3458 -0.0163 -0.0208 0.0020  68  ALA B O   
2444 C CB  . ALA B 51  ? 0.3591 0.3040 0.3287 -0.0125 -0.0152 -0.0060 68  ALA B CB  
2445 N N   . VAL B 52  ? 0.3714 0.3173 0.3495 -0.0177 -0.0173 0.0056  69  VAL B N   
2446 C CA  . VAL B 52  ? 0.3629 0.3051 0.3492 -0.0203 -0.0168 0.0087  69  VAL B CA  
2447 C C   . VAL B 52  ? 0.4311 0.3746 0.4219 -0.0206 -0.0204 0.0138  69  VAL B C   
2448 O O   . VAL B 52  ? 0.4078 0.3464 0.4085 -0.0217 -0.0207 0.0151  69  VAL B O   
2449 C CB  . VAL B 52  ? 0.3617 0.3065 0.3465 -0.0226 -0.0140 0.0112  69  VAL B CB  
2450 C CG1 . VAL B 52  ? 0.4604 0.4017 0.4539 -0.0256 -0.0129 0.0146  69  VAL B CG1 
2451 C CG2 . VAL B 52  ? 0.4142 0.3580 0.3967 -0.0234 -0.0109 0.0073  69  VAL B CG2 
2452 N N   . ALA B 53  ? 0.3942 0.3447 0.3784 -0.0200 -0.0229 0.0170  70  ALA B N   
2453 C CA  . ALA B 53  ? 0.3802 0.3335 0.3685 -0.0210 -0.0270 0.0229  70  ALA B CA  
2454 C C   . ALA B 53  ? 0.4625 0.4126 0.4553 -0.0202 -0.0297 0.0214  70  ALA B C   
2455 O O   . ALA B 53  ? 0.4360 0.3865 0.4371 -0.0213 -0.0328 0.0268  70  ALA B O   
2456 C CB  . ALA B 53  ? 0.4154 0.3773 0.3938 -0.0214 -0.0291 0.0260  70  ALA B CB  
2457 N N   . ALA B 54  ? 0.3919 0.3392 0.3804 -0.0185 -0.0288 0.0146  71  ALA B N   
2458 C CA  . ALA B 54  ? 0.4329 0.3769 0.4251 -0.0177 -0.0312 0.0124  71  ALA B CA  
2459 C C   . ALA B 54  ? 0.4148 0.3501 0.4177 -0.0175 -0.0291 0.0096  71  ALA B C   
2460 O O   . ALA B 54  ? 0.4309 0.3625 0.4365 -0.0165 -0.0303 0.0065  71  ALA B O   
2461 C CB  . ALA B 54  ? 0.4291 0.3744 0.4111 -0.0161 -0.0309 0.0061  71  ALA B CB  
2462 N N   . GLY B 55  ? 0.4419 0.3736 0.4503 -0.0189 -0.0256 0.0102  72  GLY B N   
2463 C CA  . GLY B 55  ? 0.4714 0.3946 0.4896 -0.0198 -0.0228 0.0072  72  GLY B CA  
2464 C C   . GLY B 55  ? 0.4309 0.3500 0.4451 -0.0199 -0.0192 0.0000  72  GLY B C   
2465 O O   . GLY B 55  ? 0.4588 0.3708 0.4802 -0.0214 -0.0166 -0.0033 72  GLY B O   
2466 N N   . ILE B 56  ? 0.4355 0.3589 0.4391 -0.0187 -0.0187 -0.0022 73  ILE B N   
2467 C CA  . ILE B 56  ? 0.3946 0.3152 0.3956 -0.0193 -0.0156 -0.0076 73  ILE B CA  
2468 C C   . ILE B 56  ? 0.3897 0.3085 0.3939 -0.0232 -0.0119 -0.0066 73  ILE B C   
2469 O O   . ILE B 56  ? 0.4544 0.3772 0.4572 -0.0244 -0.0114 -0.0023 73  ILE B O   
2470 C CB  . ILE B 56  ? 0.3891 0.3153 0.3802 -0.0169 -0.0156 -0.0092 73  ILE B CB  
2471 C CG1 . ILE B 56  ? 0.4026 0.3302 0.3901 -0.0139 -0.0184 -0.0111 73  ILE B CG1 
2472 C CG2 . ILE B 56  ? 0.4241 0.3483 0.4142 -0.0178 -0.0127 -0.0133 73  ILE B CG2 
2473 C CD1 . ILE B 56  ? 0.4134 0.3345 0.4053 -0.0132 -0.0190 -0.0157 73  ILE B CD1 
2474 N N   . THR B 57  ? 0.3834 0.2963 0.3912 -0.0258 -0.0091 -0.0110 74  THR B N   
2475 C CA  . THR B 57  ? 0.4697 0.3807 0.4791 -0.0309 -0.0050 -0.0113 74  THR B CA  
2476 C C   . THR B 57  ? 0.4091 0.3218 0.4126 -0.0329 -0.0033 -0.0146 74  THR B C   
2477 O O   . THR B 57  ? 0.4213 0.3356 0.4231 -0.0374 -0.0006 -0.0136 74  THR B O   
2478 C CB  . THR B 57  ? 0.4657 0.3683 0.4855 -0.0343 -0.0020 -0.0135 74  THR B CB  
2479 O OG1 . THR B 57  ? 0.4428 0.3405 0.4642 -0.0335 -0.0023 -0.0187 74  THR B OG1 
2480 C CG2 . THR B 57  ? 0.5352 0.4367 0.5635 -0.0326 -0.0036 -0.0089 74  THR B CG2 
2481 N N   . ASP B 58  ? 0.4429 0.3557 0.4435 -0.0299 -0.0049 -0.0179 75  ASP B N   
2482 C CA  . ASP B 58  ? 0.3938 0.3085 0.3904 -0.0316 -0.0037 -0.0201 75  ASP B CA  
2483 C C   . ASP B 58  ? 0.3910 0.3127 0.3818 -0.0269 -0.0055 -0.0185 75  ASP B C   
2484 O O   . ASP B 58  ? 0.3875 0.3087 0.3775 -0.0224 -0.0073 -0.0205 75  ASP B O   
2485 C CB  . ASP B 58  ? 0.4489 0.3575 0.4486 -0.0325 -0.0033 -0.0256 75  ASP B CB  
2486 C CG  . ASP B 58  ? 0.5241 0.4251 0.5304 -0.0377 -0.0004 -0.0282 75  ASP B CG  
2487 O OD1 . ASP B 58  ? 0.5186 0.4191 0.5273 -0.0412 0.0019  -0.0259 75  ASP B OD1 
2488 O OD2 . ASP B 58  ? 0.5034 0.3987 0.5128 -0.0384 0.0002  -0.0329 75  ASP B OD2 
2489 N N   . LEU B 59  ? 0.3518 0.2799 0.3390 -0.0283 -0.0044 -0.0150 76  LEU B N   
2490 C CA  . LEU B 59  ? 0.3105 0.2452 0.2938 -0.0244 -0.0050 -0.0131 76  LEU B CA  
2491 C C   . LEU B 59  ? 0.3684 0.3053 0.3523 -0.0255 -0.0040 -0.0140 76  LEU B C   
2492 O O   . LEU B 59  ? 0.3727 0.3102 0.3573 -0.0310 -0.0028 -0.0131 76  LEU B O   
2493 C CB  . LEU B 59  ? 0.3435 0.2848 0.3239 -0.0250 -0.0043 -0.0079 76  LEU B CB  
2494 C CG  . LEU B 59  ? 0.3582 0.2986 0.3387 -0.0255 -0.0050 -0.0055 76  LEU B CG  
2495 C CD1 . LEU B 59  ? 0.3336 0.2808 0.3107 -0.0265 -0.0042 -0.0004 76  LEU B CD1 
2496 C CD2 . LEU B 59  ? 0.3673 0.3063 0.3470 -0.0211 -0.0074 -0.0067 76  LEU B CD2 
2497 N N   . ILE B 60  ? 0.3114 0.2498 0.2950 -0.0208 -0.0043 -0.0155 77  ILE B N   
2498 C CA  . ILE B 60  ? 0.2884 0.2290 0.2741 -0.0210 -0.0035 -0.0158 77  ILE B CA  
2499 C C   . ILE B 60  ? 0.3279 0.2753 0.3134 -0.0168 -0.0023 -0.0128 77  ILE B C   
2500 O O   . ILE B 60  ? 0.3380 0.2847 0.3222 -0.0119 -0.0020 -0.0150 77  ILE B O   
2501 C CB  . ILE B 60  ? 0.3261 0.2605 0.3139 -0.0191 -0.0043 -0.0213 77  ILE B CB  
2502 C CG1 . ILE B 60  ? 0.3770 0.3042 0.3661 -0.0232 -0.0049 -0.0244 77  ILE B CG1 
2503 C CG2 . ILE B 60  ? 0.3203 0.2575 0.3111 -0.0191 -0.0036 -0.0209 77  ILE B CG2 
2504 C CD1 . ILE B 60  ? 0.3726 0.2932 0.3637 -0.0206 -0.0059 -0.0299 77  ILE B CD1 
2505 N N   . PHE B 61  ? 0.2648 0.2191 0.2519 -0.0192 -0.0013 -0.0077 78  PHE B N   
2506 C CA  . PHE B 61  ? 0.2983 0.2595 0.2870 -0.0158 0.0006  -0.0039 78  PHE B CA  
2507 C C   . PHE B 61  ? 0.3061 0.2698 0.3010 -0.0148 0.0015  -0.0030 78  PHE B C   
2508 O O   . PHE B 61  ? 0.3580 0.3235 0.3553 -0.0196 0.0006  -0.0007 78  PHE B O   
2509 C CB  . PHE B 61  ? 0.3004 0.2683 0.2881 -0.0191 0.0010  0.0023  78  PHE B CB  
2510 C CG  . PHE B 61  ? 0.3501 0.3164 0.3326 -0.0198 0.0004  0.0023  78  PHE B CG  
2511 C CD1 . PHE B 61  ? 0.2932 0.2598 0.2729 -0.0152 0.0010  0.0014  78  PHE B CD1 
2512 C CD2 . PHE B 61  ? 0.3026 0.2672 0.2832 -0.0254 -0.0004 0.0033  78  PHE B CD2 
2513 C CE1 . PHE B 61  ? 0.3181 0.2841 0.2936 -0.0161 0.0001  0.0022  78  PHE B CE1 
2514 C CE2 . PHE B 61  ? 0.3105 0.2738 0.2878 -0.0259 -0.0008 0.0039  78  PHE B CE2 
2515 C CZ  . PHE B 61  ? 0.3171 0.2814 0.2920 -0.0210 -0.0009 0.0037  78  PHE B CZ  
2516 N N   . VAL B 62  ? 0.2795 0.2431 0.2771 -0.0092 0.0035  -0.0051 79  VAL B N   
2517 C CA  . VAL B 62  ? 0.2890 0.2552 0.2943 -0.0074 0.0050  -0.0037 79  VAL B CA  
2518 C C   . VAL B 62  ? 0.3373 0.3117 0.3477 -0.0056 0.0079  0.0025  79  VAL B C   
2519 O O   . VAL B 62  ? 0.3148 0.2897 0.3247 -0.0014 0.0108  0.0011  79  VAL B O   
2520 C CB  . VAL B 62  ? 0.2868 0.2469 0.2930 -0.0027 0.0061  -0.0104 79  VAL B CB  
2521 C CG1 . VAL B 62  ? 0.3009 0.2639 0.3164 -0.0008 0.0081  -0.0084 79  VAL B CG1 
2522 C CG2 . VAL B 62  ? 0.3413 0.2935 0.3430 -0.0047 0.0031  -0.0158 79  VAL B CG2 
2523 N N   . THR B 63  ? 0.3064 0.2878 0.3223 -0.0093 0.0072  0.0095  80  THR B N   
2524 C CA  . THR B 63  ? 0.3225 0.3129 0.3439 -0.0090 0.0092  0.0171  80  THR B CA  
2525 C C   . THR B 63  ? 0.3226 0.3178 0.3565 -0.0059 0.0119  0.0212  80  THR B C   
2526 O O   . THR B 63  ? 0.3204 0.3130 0.3586 -0.0053 0.0114  0.0193  80  THR B O   
2527 C CB  . THR B 63  ? 0.3217 0.3182 0.3412 -0.0162 0.0065  0.0236  80  THR B CB  
2528 O OG1 . THR B 63  ? 0.3656 0.3641 0.3886 -0.0211 0.0042  0.0262  80  THR B OG1 
2529 C CG2 . THR B 63  ? 0.3347 0.3262 0.3437 -0.0196 0.0046  0.0199  80  THR B CG2 
2530 N N   . GLY B 64  ? 0.3322 0.3346 0.3729 -0.0039 0.0149  0.0272  81  GLY B N   
2531 C CA  . GLY B 64  ? 0.3377 0.3461 0.3930 -0.0012 0.0179  0.0331  81  GLY B CA  
2532 C C   . GLY B 64  ? 0.4114 0.4309 0.4732 -0.0042 0.0177  0.0439  81  GLY B C   
2533 O O   . GLY B 64  ? 0.4243 0.4479 0.4810 -0.0108 0.0135  0.0481  81  GLY B O   
2534 N N   . ARG B 65  ? 0.5008 0.5252 0.5738 0.0003  0.0226  0.0482  82  ARG B N   
2535 C CA  . ARG B 65  ? 0.5617 0.5969 0.6404 -0.0028 0.0220  0.0588  82  ARG B CA  
2536 C C   . ARG B 65  ? 0.3886 0.4230 0.4554 -0.0042 0.0216  0.0569  82  ARG B C   
2537 O O   . ARG B 65  ? 0.4378 0.4641 0.4942 -0.0017 0.0227  0.0481  82  ARG B O   
2538 C CB  . ARG B 65  ? 0.6924 0.7341 0.7896 0.0021  0.0275  0.0657  82  ARG B CB  
2539 C CG  . ARG B 65  ? 0.6398 0.6751 0.7406 0.0096  0.0349  0.0583  82  ARG B CG  
2540 C CD  . ARG B 65  ? 0.7381 0.7802 0.8603 0.0138  0.0410  0.0661  82  ARG B CD  
2541 N NE  . ARG B 65  ? 0.7934 0.8470 0.9227 0.0108  0.0397  0.0779  82  ARG B NE  
2542 C CZ  . ARG B 65  ? 0.7475 0.8037 0.8752 0.0118  0.0427  0.0792  82  ARG B CZ  
2543 N NH1 . ARG B 65  ? 0.7131 0.7617 0.8335 0.0158  0.0478  0.0697  82  ARG B NH1 
2544 N NH2 . ARG B 65  ? 0.6336 0.7005 0.7661 0.0080  0.0401  0.0903  82  ARG B NH2 
2545 N N   . ASN B 66  ? 0.4566 0.4998 0.5242 -0.0092 0.0192  0.0655  83  ASN B N   
2546 C CA  . ASN B 66  ? 0.4730 0.5162 0.5295 -0.0116 0.0181  0.0647  83  ASN B CA  
2547 C C   . ASN B 66  ? 0.4263 0.4607 0.4676 -0.0149 0.0144  0.0564  83  ASN B C   
2548 O O   . ASN B 66  ? 0.3387 0.3687 0.3700 -0.0144 0.0146  0.0518  83  ASN B O   
2549 C CB  . ASN B 66  ? 0.5344 0.5764 0.5925 -0.0053 0.0237  0.0623  83  ASN B CB  
2550 C CG  . ASN B 66  ? 0.4902 0.5412 0.5652 -0.0024 0.0280  0.0711  83  ASN B CG  
2551 O OD1 . ASN B 66  ? 0.5436 0.6044 0.6249 -0.0064 0.0258  0.0813  83  ASN B OD1 
2552 N ND2 . ASN B 66  ? 0.4872 0.5349 0.5702 0.0041  0.0343  0.0673  83  ASN B ND2 
2553 N N   . LYS B 67  ? 0.3989 0.3888 0.3463 -0.0579 -0.0658 0.0154  84  LYS B N   
2554 C CA  . LYS B 67  ? 0.4171 0.4001 0.3429 -0.0528 -0.0482 0.0139  84  LYS B CA  
2555 C C   . LYS B 67  ? 0.4439 0.4144 0.3787 -0.0526 -0.0488 0.0038  84  LYS B C   
2556 O O   . LYS B 67  ? 0.3976 0.3689 0.3318 -0.0484 -0.0321 0.0035  84  LYS B O   
2557 C CB  . LYS B 67  ? 0.4615 0.4281 0.3393 -0.0511 -0.0501 0.0127  84  LYS B CB  
2558 C CG  . LYS B 67  ? 0.4965 0.4390 0.3536 -0.0542 -0.0710 0.0022  84  LYS B CG  
2559 C CD  . LYS B 67  ? 0.5488 0.4805 0.3648 -0.0547 -0.0783 0.0040  84  LYS B CD  
2560 C CE  . LYS B 67  ? 0.5841 0.4910 0.3747 -0.0566 -0.0945 -0.0074 84  LYS B CE  
2561 N NZ  . LYS B 67  ? 0.7318 0.6298 0.4945 -0.0598 -0.1107 -0.0056 84  LYS B NZ  
2562 N N   . ARG B 68  ? 0.3902 0.3486 0.3331 -0.0568 -0.0678 -0.0046 85  ARG B N   
2563 C CA  A ARG B 68  ? 0.4798 0.4238 0.4263 -0.0564 -0.0684 -0.0148 85  ARG B CA  
2564 C CA  B ARG B 68  ? 0.4802 0.4240 0.4278 -0.0568 -0.0698 -0.0150 85  ARG B CA  
2565 C C   . ARG B 68  ? 0.3332 0.2920 0.3217 -0.0570 -0.0597 -0.0132 85  ARG B C   
2566 O O   . ARG B 68  ? 0.2916 0.2410 0.2828 -0.0554 -0.0538 -0.0193 85  ARG B O   
2567 C CB  A ARG B 68  ? 0.5988 0.5237 0.5379 -0.0607 -0.0915 -0.0252 85  ARG B CB  
2568 C CB  B ARG B 68  ? 0.5917 0.5194 0.5375 -0.0617 -0.0937 -0.0245 85  ARG B CB  
2569 C CG  A ARG B 68  ? 0.6452 0.5541 0.5409 -0.0604 -0.1007 -0.0273 85  ARG B CG  
2570 C CG  B ARG B 68  ? 0.6412 0.5509 0.5447 -0.0619 -0.1056 -0.0279 85  ARG B CG  
2571 C CD  A ARG B 68  ? 0.6054 0.4885 0.4763 -0.0611 -0.1118 -0.0402 85  ARG B CD  
2572 C CD  B ARG B 68  ? 0.6080 0.5018 0.4742 -0.0574 -0.0950 -0.0327 85  ARG B CD  
2573 N NE  A ARG B 68  ? 0.5929 0.4645 0.4190 -0.0592 -0.1118 -0.0401 85  ARG B NE  
2574 N NE  B ARG B 68  ? 0.5874 0.4580 0.4372 -0.0590 -0.1083 -0.0456 85  ARG B NE  
2575 C CZ  A ARG B 68  ? 0.6568 0.5244 0.4638 -0.0620 -0.1260 -0.0378 85  ARG B CZ  
2576 C CZ  B ARG B 68  ? 0.5877 0.4506 0.4532 -0.0590 -0.1077 -0.0540 85  ARG B CZ  
2577 N NH1 A ARG B 68  ? 0.5861 0.4570 0.4129 -0.0667 -0.1438 -0.0374 85  ARG B NH1 
2578 N NH1 B ARG B 68  ? 0.4883 0.3647 0.3879 -0.0581 -0.0961 -0.0508 85  ARG B NH1 
2579 N NH2 A ARG B 68  ? 0.6583 0.5189 0.4256 -0.0600 -0.1222 -0.0359 85  ARG B NH2 
2580 N NH2 B ARG B 68  ? 0.6480 0.4893 0.4938 -0.0600 -0.1185 -0.0659 85  ARG B NH2 
2581 N N   . ALA B 69  ? 0.3453 0.3272 0.3663 -0.0594 -0.0581 -0.0051 86  ALA B N   
2582 C CA  . ALA B 69  ? 0.3045 0.3025 0.3635 -0.0598 -0.0470 -0.0024 86  ALA B CA  
2583 C C   . ALA B 69  ? 0.2729 0.2747 0.3228 -0.0538 -0.0239 0.0020  86  ALA B C   
2584 O O   . ALA B 69  ? 0.2742 0.2753 0.3397 -0.0528 -0.0155 -0.0004 86  ALA B O   
2585 C CB  . ALA B 69  ? 0.3416 0.3658 0.4353 -0.0632 -0.0483 0.0058  86  ALA B CB  
2586 N N   . ILE B 70  ? 0.3112 0.3169 0.3356 -0.0499 -0.0136 0.0085  87  ILE B N   
2587 C CA  . ILE B 70  ? 0.2819 0.2905 0.2944 -0.0439 0.0080  0.0123  87  ILE B CA  
2588 C C   . ILE B 70  ? 0.3052 0.2890 0.2899 -0.0407 0.0086  0.0023  87  ILE B C   
2589 O O   . ILE B 70  ? 0.3065 0.2888 0.2976 -0.0373 0.0215  0.0008  87  ILE B O   
2590 C CB  . ILE B 70  ? 0.3446 0.3636 0.3355 -0.0410 0.0177  0.0213  87  ILE B CB  
2591 C CG1 . ILE B 70  ? 0.3730 0.4196 0.3960 -0.0432 0.0220  0.0316  87  ILE B CG1 
2592 C CG2 . ILE B 70  ? 0.3640 0.3814 0.3343 -0.0344 0.0382  0.0231  87  ILE B CG2 
2593 C CD1 . ILE B 70  ? 0.3348 0.3998 0.3839 -0.0404 0.0421  0.0376  87  ILE B CD1 
2594 N N   . GLU B 71  ? 0.3134 0.2776 0.2654 -0.0415 -0.0048 -0.0045 88  GLU B N   
2595 C CA  . GLU B 71  ? 0.3475 0.2886 0.2705 -0.0385 -0.0043 -0.0146 88  GLU B CA  
2596 C C   . GLU B 71  ? 0.3556 0.2868 0.3004 -0.0401 -0.0091 -0.0232 88  GLU B C   
2597 O O   . GLU B 71  ? 0.3326 0.2544 0.2710 -0.0361 0.0013  -0.0279 88  GLU B O   
2598 C CB  . GLU B 71  ? 0.4146 0.3374 0.3013 -0.0403 -0.0203 -0.0207 88  GLU B CB  
2599 C CG  . GLU B 71  ? 0.4477 0.3780 0.3081 -0.0388 -0.0156 -0.0123 88  GLU B CG  
2600 C CD  . GLU B 71  ? 0.4939 0.4068 0.3188 -0.0413 -0.0322 -0.0173 88  GLU B CD  
2601 O OE1 . GLU B 71  ? 0.5544 0.4501 0.3755 -0.0441 -0.0478 -0.0275 88  GLU B OE1 
2602 O OE2 . GLU B 71  ? 0.4826 0.3992 0.2831 -0.0406 -0.0297 -0.0111 88  GLU B OE2 
2603 N N   . ASP B 72  ? 0.3173 0.2502 0.2881 -0.0460 -0.0251 -0.0256 89  ASP B N   
2604 C CA  . ASP B 72  ? 0.3344 0.2568 0.3248 -0.0482 -0.0311 -0.0344 89  ASP B CA  
2605 C C   . ASP B 72  ? 0.2937 0.2307 0.3168 -0.0468 -0.0154 -0.0291 89  ASP B C   
2606 O O   . ASP B 72  ? 0.3432 0.2702 0.3779 -0.0470 -0.0150 -0.0357 89  ASP B O   
2607 C CB  . ASP B 72  ? 0.3355 0.2556 0.3434 -0.0550 -0.0527 -0.0390 89  ASP B CB  
2608 C CG  . ASP B 72  ? 0.4460 0.3459 0.4200 -0.0565 -0.0700 -0.0469 89  ASP B CG  
2609 O OD1 . ASP B 72  ? 0.4605 0.3475 0.3982 -0.0524 -0.0647 -0.0498 89  ASP B OD1 
2610 O OD2 . ASP B 72  ? 0.4429 0.3412 0.4266 -0.0617 -0.0885 -0.0500 89  ASP B OD2 
2611 N N   . HIS B 73  ? 0.3105 0.2712 0.3488 -0.0456 -0.0028 -0.0173 90  HIS B N   
2612 C CA  . HIS B 73  ? 0.2666 0.2419 0.3332 -0.0440 0.0134  -0.0116 90  HIS B CA  
2613 C C   . HIS B 73  ? 0.2734 0.2396 0.3191 -0.0369 0.0304  -0.0127 90  HIS B C   
2614 O O   . HIS B 73  ? 0.3141 0.2769 0.3755 -0.0357 0.0374  -0.0150 90  HIS B O   
2615 C CB  . HIS B 73  ? 0.2909 0.2952 0.3802 -0.0449 0.0219  0.0011  90  HIS B CB  
2616 C CG  . HIS B 73  ? 0.2570 0.2779 0.3793 -0.0445 0.0364  0.0071  90  HIS B CG  
2617 N ND1 . HIS B 73  ? 0.2107 0.2366 0.3687 -0.0497 0.0300  0.0052  90  HIS B ND1 
2618 C CD2 . HIS B 73  ? 0.1846 0.2161 0.3078 -0.0393 0.0568  0.0142  90  HIS B CD2 
2619 C CE1 . HIS B 73  ? 0.2620 0.3014 0.4415 -0.0480 0.0460  0.0115  90  HIS B CE1 
2620 N NE2 . HIS B 73  ? 0.2123 0.2552 0.3713 -0.0415 0.0623  0.0170  90  HIS B NE2 
2621 N N   . PHE B 74  ? 0.2924 0.2544 0.3028 -0.0323 0.0371  -0.0114 91  PHE B N   
2622 C CA  . PHE B 74  ? 0.3197 0.2764 0.3123 -0.0253 0.0547  -0.0118 91  PHE B CA  
2623 C C   . PHE B 74  ? 0.3876 0.3165 0.3501 -0.0229 0.0490  -0.0248 91  PHE B C   
2624 O O   . PHE B 74  ? 0.3738 0.2953 0.3318 -0.0180 0.0609  -0.0280 91  PHE B O   
2625 C CB  . PHE B 74  ? 0.3219 0.2929 0.2957 -0.0212 0.0683  -0.0023 91  PHE B CB  
2626 C CG  . PHE B 74  ? 0.2820 0.2814 0.2871 -0.0217 0.0801  0.0104  91  PHE B CG  
2627 C CD1 . PHE B 74  ? 0.3359 0.3453 0.3599 -0.0181 0.0971  0.0149  91  PHE B CD1 
2628 C CD2 . PHE B 74  ? 0.3183 0.3343 0.3349 -0.0259 0.0737  0.0175  91  PHE B CD2 
2629 C CE1 . PHE B 74  ? 0.3400 0.3756 0.3923 -0.0185 0.1049  0.0257  91  PHE B CE1 
2630 C CE2 . PHE B 74  ? 0.3042 0.3472 0.3510 -0.0265 0.0848  0.0286  91  PHE B CE2 
2631 C CZ  . PHE B 74  ? 0.2977 0.3484 0.3557 -0.0217 0.0918  0.0298  91  PHE B CZ  
2632 N N   . ASP B 75  ? 0.4017 0.3149 0.3446 -0.0264 0.0309  -0.0327 92  ASP B N   
2633 C CA  . ASP B 75  ? 0.3828 0.2701 0.2990 -0.0247 0.0248  -0.0458 92  ASP B CA  
2634 C C   . ASP B 75  ? 0.4596 0.3365 0.4004 -0.0267 0.0198  -0.0536 92  ASP B C   
2635 O O   . ASP B 75  ? 0.4757 0.3613 0.4502 -0.0318 0.0126  -0.0511 92  ASP B O   
2636 C CB  . ASP B 75  ? 0.4447 0.3190 0.3343 -0.0284 0.0061  -0.0519 92  ASP B CB  
2637 C CG  . ASP B 75  ? 0.5490 0.4310 0.4105 -0.0267 0.0103  -0.0449 92  ASP B CG  
2638 O OD1 . ASP B 75  ? 0.5269 0.4177 0.3778 -0.0214 0.0284  -0.0390 92  ASP B OD1 
2639 O OD2 . ASP B 75  ? 0.5656 0.4451 0.4160 -0.0308 -0.0047 -0.0450 92  ASP B OD2 
2640 N N   . ALA B 76  ? 0.4097 0.2681 0.3337 -0.0227 0.0237  -0.0631 93  ALA B N   
2641 C CA  . ALA B 76  ? 0.4525 0.2982 0.3967 -0.0244 0.0186  -0.0715 93  ALA B CA  
2642 C C   . ALA B 76  ? 0.4280 0.2649 0.3809 -0.0318 -0.0037 -0.0783 93  ALA B C   
2643 O O   . ALA B 76  ? 0.5486 0.3803 0.4802 -0.0343 -0.0165 -0.0810 93  ALA B O   
2644 C CB  . ALA B 76  ? 0.5242 0.3489 0.4433 -0.0190 0.0240  -0.0825 93  ALA B CB  
2645 N N   . ALA B 77  ? 0.4653 0.3017 0.4513 -0.0357 -0.0085 -0.0804 94  ALA B N   
2646 C CA  . ALA B 77  ? 0.5025 0.3301 0.4991 -0.0426 -0.0293 -0.0879 94  ALA B CA  
2647 C C   . ALA B 77  ? 0.5903 0.3987 0.5935 -0.0428 -0.0319 -0.0991 94  ALA B C   
2648 O O   . ALA B 77  ? 0.5100 0.3234 0.5466 -0.0452 -0.0295 -0.0972 94  ALA B O   
2649 C CB  . ALA B 77  ? 0.4736 0.3220 0.5065 -0.0485 -0.0347 -0.0793 94  ALA B CB  
2650 N N   . PRO B 78  ? 0.6262 0.4126 0.5982 -0.0404 -0.0366 -0.1108 95  PRO B N   
2651 C CA  . PRO B 78  ? 0.6621 0.4291 0.6387 -0.0399 -0.0381 -0.1221 95  PRO B CA  
2652 C C   . PRO B 78  ? 0.6872 0.4520 0.6955 -0.0472 -0.0522 -0.1258 95  PRO B C   
2653 O O   . PRO B 78  ? 0.6652 0.4246 0.6952 -0.0476 -0.0484 -0.1286 95  PRO B O   
2654 C CB  . PRO B 78  ? 0.7129 0.4586 0.6482 -0.0376 -0.0454 -0.1345 95  PRO B CB  
2655 C CG  . PRO B 78  ? 0.7743 0.5296 0.6819 -0.0347 -0.0402 -0.1276 95  PRO B CG  
2656 C CD  . PRO B 78  ? 0.7467 0.5248 0.6776 -0.0384 -0.0415 -0.1146 95  PRO B CD  
2657 N N   . GLU B 79  ? 0.7083 0.4772 0.7200 -0.0532 -0.0687 -0.1261 96  GLU B N   
2658 C CA  . GLU B 79  ? 0.7356 0.5023 0.7762 -0.0605 -0.0833 -0.1307 96  GLU B CA  
2659 C C   . GLU B 79  ? 0.7633 0.5476 0.8457 -0.0626 -0.0741 -0.1214 96  GLU B C   
2660 O O   . GLU B 79  ? 0.6894 0.4666 0.7941 -0.0656 -0.0765 -0.1262 96  GLU B O   
2661 C CB  . GLU B 79  ? 0.8017 0.5727 0.8386 -0.0659 -0.1015 -0.1312 96  GLU B CB  
2662 C CG  . GLU B 79  ? 1.0459 0.8213 1.1168 -0.0739 -0.1162 -0.1333 96  GLU B CG  
2663 C CD  . GLU B 79  ? 1.1900 0.9743 1.2548 -0.0775 -0.1311 -0.1311 96  GLU B CD  
2664 O OE1 . GLU B 79  ? 1.1539 0.9295 1.1870 -0.0757 -0.1367 -0.1337 96  GLU B OE1 
2665 O OE2 . GLU B 79  ? 1.1253 0.9282 1.2144 -0.0806 -0.1345 -0.1246 96  GLU B OE2 
2666 N N   . LEU B 80  ? 0.6273 0.4349 0.7207 -0.0613 -0.0632 -0.1079 97  LEU B N   
2667 C CA  . LEU B 80  ? 0.5625 0.3887 0.6948 -0.0634 -0.0535 -0.0984 97  LEU B CA  
2668 C C   . LEU B 80  ? 0.6201 0.4386 0.7571 -0.0588 -0.0384 -0.0989 97  LEU B C   
2669 O O   . LEU B 80  ? 0.6026 0.4239 0.7707 -0.0622 -0.0369 -0.0978 97  LEU B O   
2670 C CB  . LEU B 80  ? 0.5760 0.4285 0.7154 -0.0621 -0.0434 -0.0842 97  LEU B CB  
2671 C CG  . LEU B 80  ? 0.5178 0.3934 0.6973 -0.0644 -0.0327 -0.0732 97  LEU B CG  
2672 C CD1 . LEU B 80  ? 0.5203 0.4048 0.7333 -0.0733 -0.0473 -0.0742 97  LEU B CD1 
2673 C CD2 . LEU B 80  ? 0.4791 0.3781 0.6581 -0.0610 -0.0187 -0.0599 97  LEU B CD2 
2674 N N   . GLU B 81  ? 0.5691 0.3791 0.6764 -0.0511 -0.0267 -0.1000 98  GLU B N   
2675 C CA  . GLU B 81  ? 0.5819 0.3843 0.6926 -0.0459 -0.0122 -0.1007 98  GLU B CA  
2676 C C   . GLU B 81  ? 0.7823 0.5611 0.8966 -0.0482 -0.0218 -0.1138 98  GLU B C   
2677 O O   . GLU B 81  ? 0.7029 0.4797 0.8409 -0.0486 -0.0157 -0.1130 98  GLU B O   
2678 C CB  . GLU B 81  ? 0.6070 0.4049 0.6832 -0.0372 0.0011  -0.1005 98  GLU B CB  
2679 C CG  . GLU B 81  ? 0.5758 0.3969 0.6487 -0.0344 0.0131  -0.0871 98  GLU B CG  
2680 C CD  . GLU B 81  ? 0.6454 0.4617 0.6860 -0.0257 0.0276  -0.0873 98  GLU B CD  
2681 O OE1 . GLU B 81  ? 0.7184 0.5176 0.7495 -0.0213 0.0325  -0.0954 98  GLU B OE1 
2682 O OE2 . GLU B 81  ? 0.6576 0.4874 0.6828 -0.0232 0.0341  -0.0798 98  GLU B OE2 
2683 N N   . THR B 82  ? 0.7245 0.4852 0.8154 -0.0499 -0.0371 -0.1260 99  THR B N   
2684 C CA  . THR B 82  ? 0.8068 0.5447 0.9000 -0.0524 -0.0474 -0.1395 99  THR B CA  
2685 C C   . THR B 82  ? 0.8233 0.5673 0.9561 -0.0605 -0.0560 -0.1380 99  THR B C   
2686 O O   . THR B 82  ? 0.9217 0.6572 1.0681 -0.0612 -0.0544 -0.1409 99  THR B O   
2687 C CB  . THR B 82  ? 0.8816 0.6020 0.9429 -0.0535 -0.0632 -0.1521 99  THR B CB  
2688 O OG1 . THR B 82  ? 0.8741 0.5863 0.8976 -0.0461 -0.0549 -0.1553 99  THR B OG1 
2689 C CG2 . THR B 82  ? 0.8886 0.5874 0.9560 -0.0574 -0.0758 -0.1660 99  THR B CG2 
2690 N N   . ASP B 83  ? 0.8262 0.5881 0.9744 -0.0663 -0.0645 -0.1315 100 ASP B N   
2691 C CA  . ASP B 83  ? 0.8310 0.6113 1.0061 -0.0714 -0.0686 -0.1233 100 ASP B CA  
2692 C C   . ASP B 83  ? 0.8478 0.6434 1.0510 -0.0703 -0.0537 -0.1123 100 ASP B C   
2693 O O   . ASP B 83  ? 0.8908 0.6887 1.1094 -0.0720 -0.0540 -0.1107 100 ASP B O   
2694 C CB  . ASP B 83  ? 0.8603 0.6611 1.0406 -0.0754 -0.0779 -0.1168 100 ASP B CB  
2695 C CG  . ASP B 83  ? 0.9836 0.8085 1.1926 -0.0788 -0.0786 -0.1068 100 ASP B CG  
2696 O OD1 . ASP B 83  ? 1.0924 0.9152 1.3139 -0.0795 -0.0768 -0.1072 100 ASP B OD1 
2697 O OD2 . ASP B 83  ? 0.8953 0.7417 1.1131 -0.0802 -0.0809 -0.0988 100 ASP B OD2 
2698 N N   . LEU B 84  ? 0.6937 0.5008 0.9034 -0.0675 -0.0401 -0.1043 101 LEU B N   
2699 C CA  . LEU B 84  ? 0.7347 0.5595 0.9704 -0.0662 -0.0255 -0.0924 101 LEU B CA  
2700 C C   . LEU B 84  ? 0.7685 0.5749 1.0029 -0.0624 -0.0175 -0.0971 101 LEU B C   
2701 O O   . LEU B 84  ? 0.7400 0.5567 0.9954 -0.0630 -0.0127 -0.0904 101 LEU B O   
2702 C CB  . LEU B 84  ? 0.6481 0.4894 0.8892 -0.0638 -0.0110 -0.0822 101 LEU B CB  
2703 C CG  . LEU B 84  ? 0.6350 0.5022 0.8842 -0.0671 -0.0153 -0.0733 101 LEU B CG  
2704 C CD1 . LEU B 84  ? 0.4543 0.3384 0.7021 -0.0628 0.0017  -0.0622 101 LEU B CD1 
2705 C CD2 . LEU B 84  ? 0.5937 0.4854 0.8656 -0.0695 -0.0195 -0.0646 101 LEU B CD2 
2706 N N   . GLU B 85  ? 0.8118 0.5919 1.0205 -0.0577 -0.0157 -0.1090 102 GLU B N   
2707 C CA  . GLU B 85  ? 0.9197 0.6808 1.1240 -0.0533 -0.0095 -0.1151 102 GLU B CA  
2708 C C   . GLU B 85  ? 0.8932 0.6494 1.1058 -0.0579 -0.0217 -0.1186 102 GLU B C   
2709 O O   . GLU B 85  ? 0.9239 0.6834 1.1542 -0.0577 -0.0161 -0.1138 102 GLU B O   
2710 C CB  . GLU B 85  ? 1.0010 0.7404 1.1670 -0.0462 -0.0076 -0.1266 102 GLU B CB  
2711 C CG  . GLU B 85  ? 1.0896 0.8066 1.2493 -0.0411 -0.0017 -0.1355 102 GLU B CG  
2712 C CD  . GLU B 85  ? 1.2548 0.9805 1.4336 -0.0367 0.0165  -0.1252 102 GLU B CD  
2713 O OE1 . GLU B 85  ? 1.2744 1.0240 1.4654 -0.0362 0.0267  -0.1112 102 GLU B OE1 
2714 O OE2 . GLU B 85  ? 1.2977 1.0080 1.4784 -0.0335 0.0202  -0.1304 102 GLU B OE2 
2715 N N   . ALA B 86  ? 0.9693 0.7190 1.1696 -0.0622 -0.0380 -0.1264 103 ALA B N   
2716 C CA  . ALA B 86  ? 1.1087 0.8539 1.3157 -0.0667 -0.0487 -0.1300 103 ALA B CA  
2717 C C   . ALA B 86  ? 1.0294 0.7984 1.2682 -0.0702 -0.0457 -0.1175 103 ALA B C   
2718 O O   . ALA B 86  ? 1.1274 0.8924 1.3780 -0.0705 -0.0433 -0.1170 103 ALA B O   
2719 C CB  . ALA B 86  ? 1.1101 0.8519 1.3020 -0.0709 -0.0652 -0.1371 103 ALA B CB  
2720 N N   . LYS B 87  ? 0.8552 0.6496 1.1074 -0.0725 -0.0456 -0.1074 104 LYS B N   
2721 C CA  . LYS B 87  ? 0.8902 0.7099 1.1701 -0.0748 -0.0425 -0.0957 104 LYS B CA  
2722 C C   . LYS B 87  ? 0.8629 0.6903 1.1585 -0.0712 -0.0266 -0.0871 104 LYS B C   
2723 O O   . LYS B 87  ? 0.8309 0.6808 1.1482 -0.0721 -0.0227 -0.0768 104 LYS B O   
2724 C CB  . LYS B 87  ? 0.9248 0.7694 1.2112 -0.0767 -0.0459 -0.0880 104 LYS B CB  
2725 C CG  . LYS B 87  ? 0.9145 0.7530 1.1863 -0.0801 -0.0617 -0.0957 104 LYS B CG  
2726 C CD  . LYS B 87  ? 0.8883 0.7504 1.1651 -0.0811 -0.0649 -0.0882 104 LYS B CD  
2727 C CE  . LYS B 87  ? 0.8432 0.7296 1.1424 -0.0818 -0.0629 -0.0786 104 LYS B CE  
2728 N NZ  . LYS B 87  ? 0.9072 0.8143 1.2077 -0.0815 -0.0663 -0.0725 104 LYS B NZ  
2729 N N   . GLY B 88  ? 0.7543 0.5645 1.0381 -0.0662 -0.0171 -0.0909 105 GLY B N   
2730 C CA  . GLY B 88  ? 0.7645 0.5814 1.0619 -0.0621 -0.0013 -0.0826 105 GLY B CA  
2731 C C   . GLY B 88  ? 0.7692 0.6161 1.0827 -0.0610 0.0092  -0.0684 105 GLY B C   
2732 O O   . GLY B 88  ? 0.7049 0.5669 1.0367 -0.0593 0.0186  -0.0590 105 GLY B O   
2733 N N   . LYS B 89  ? 0.8822 0.7384 1.1882 -0.0615 0.0078  -0.0667 106 LYS B N   
2734 C CA  . LYS B 89  ? 0.7967 0.6820 1.1151 -0.0599 0.0178  -0.0535 106 LYS B CA  
2735 C C   . LYS B 89  ? 0.7345 0.6144 1.0430 -0.0546 0.0337  -0.0514 106 LYS B C   
2736 O O   . LYS B 89  ? 0.6747 0.5565 0.9717 -0.0542 0.0357  -0.0511 106 LYS B O   
2737 C CB  . LYS B 89  ? 0.8417 0.7418 1.1578 -0.0633 0.0072  -0.0521 106 LYS B CB  
2738 C CG  . LYS B 89  ? 0.9297 0.8322 1.2509 -0.0677 -0.0081 -0.0554 106 LYS B CG  
2739 C CD  . LYS B 89  ? 1.0668 0.9911 1.4079 -0.0667 -0.0050 -0.0460 106 LYS B CD  
2740 C CE  . LYS B 89  ? 1.0876 1.0387 1.4330 -0.0621 0.0039  -0.0340 106 LYS B CE  
2741 N NZ  . LYS B 89  ? 1.1624 1.1315 1.5178 -0.0598 0.0041  -0.0265 106 LYS B NZ  
2742 N N   . HIS B 90  ? 0.9200 0.6817 0.8348 -0.0094 0.1051  -0.0159 107 HIS B N   
2743 C CA  . HIS B 90  ? 0.9158 0.6738 0.8338 -0.0044 0.0975  -0.0209 107 HIS B CA  
2744 C C   . HIS B 90  ? 0.8518 0.6000 0.7622 0.0060  0.0924  -0.0178 107 HIS B C   
2745 O O   . HIS B 90  ? 0.7752 0.5288 0.6908 0.0102  0.0865  -0.0209 107 HIS B O   
2746 C CB  . HIS B 90  ? 0.9697 0.7098 0.8840 -0.0060 0.0958  -0.0257 107 HIS B CB  
2747 C CG  . HIS B 90  ? 1.0481 0.7983 0.9711 -0.0161 0.0999  -0.0298 107 HIS B CG  
2748 N ND1 . HIS B 90  ? 1.0964 0.8402 1.0142 -0.0228 0.1064  -0.0275 107 HIS B ND1 
2749 C CD2 . HIS B 90  ? 1.0864 0.8543 1.0232 -0.0209 0.0986  -0.0360 107 HIS B CD2 
2750 C CE1 . HIS B 90  ? 1.0534 0.8094 0.9814 -0.0311 0.1088  -0.0323 107 HIS B CE1 
2751 N NE2 . HIS B 90  ? 1.1282 0.8992 1.0679 -0.0300 0.1041  -0.0375 107 HIS B NE2 
2752 N N   . GLU B 91  ? 0.8328 0.5664 0.7306 0.0099  0.0946  -0.0120 108 GLU B N   
2753 C CA  . GLU B 91  ? 0.8459 0.5711 0.7367 0.0197  0.0900  -0.0091 108 GLU B CA  
2754 C C   . GLU B 91  ? 0.7676 0.5137 0.6664 0.0214  0.0892  -0.0070 108 GLU B C   
2755 O O   . GLU B 91  ? 0.7474 0.4945 0.6471 0.0277  0.0834  -0.0077 108 GLU B O   
2756 C CB  . GLU B 91  ? 0.9107 0.6168 0.7864 0.0231  0.0929  -0.0033 108 GLU B CB  
2757 C CG  . GLU B 91  ? 1.1301 0.8162 0.9968 0.0194  0.0953  -0.0041 108 GLU B CG  
2758 C CD  . GLU B 91  ? 1.3819 1.0501 1.2329 0.0220  0.0986  0.0020  108 GLU B CD  
2759 O OE1 . GLU B 91  ? 1.3216 0.9951 1.1699 0.0264  0.0995  0.0066  108 GLU B OE1 
2760 O OE2 . GLU B 91  ? 1.3960 1.0449 1.2372 0.0195  0.1001  0.0022  108 GLU B OE2 
2761 N N   . LEU B 92  ? 0.7287 0.4914 0.6329 0.0156  0.0948  -0.0046 109 LEU B N   
2762 C CA  . LEU B 92  ? 0.7362 0.5195 0.6485 0.0167  0.0938  -0.0028 109 LEU B CA  
2763 C C   . LEU B 92  ? 0.6951 0.4931 0.6195 0.0143  0.0893  -0.0080 109 LEU B C   
2764 O O   . LEU B 92  ? 0.6587 0.4645 0.5863 0.0185  0.0847  -0.0075 109 LEU B O   
2765 C CB  . LEU B 92  ? 0.6820 0.4805 0.5979 0.0107  0.1007  0.0000  109 LEU B CB  
2766 C CG  . LEU B 92  ? 0.8329 0.6232 0.7383 0.0133  0.1051  0.0055  109 LEU B CG  
2767 C CD1 . LEU B 92  ? 0.7623 0.5708 0.6733 0.0067  0.1118  0.0069  109 LEU B CD1 
2768 C CD2 . LEU B 92  ? 0.7573 0.5438 0.6573 0.0230  0.1009  0.0092  109 LEU B CD2 
2769 N N   . LEU B 93  ? 0.6559 0.4583 0.5871 0.0073  0.0907  -0.0130 110 LEU B N   
2770 C CA  . LEU B 93  ? 0.6469 0.4641 0.5897 0.0046  0.0867  -0.0183 110 LEU B CA  
2771 C C   . LEU B 93  ? 0.6631 0.4706 0.6030 0.0117  0.0793  -0.0207 110 LEU B C   
2772 O O   . LEU B 93  ? 0.5806 0.4008 0.5269 0.0127  0.0751  -0.0221 110 LEU B O   
2773 C CB  . LEU B 93  ? 0.6927 0.5132 0.6420 -0.0035 0.0893  -0.0239 110 LEU B CB  
2774 C CG  . LEU B 93  ? 0.6596 0.4970 0.6216 -0.0075 0.0858  -0.0301 110 LEU B CG  
2775 C CD1 . LEU B 93  ? 0.6599 0.5208 0.6304 -0.0097 0.0859  -0.0279 110 LEU B CD1 
2776 C CD2 . LEU B 93  ? 0.8048 0.6451 0.7727 -0.0157 0.0893  -0.0352 110 LEU B CD2 
2777 N N   . ALA B 94  ? 0.6519 0.4368 0.5816 0.0167  0.0776  -0.0213 111 ALA B N   
2778 C CA  . ALA B 94  ? 0.6802 0.4553 0.6066 0.0239  0.0706  -0.0240 111 ALA B CA  
2779 C C   . ALA B 94  ? 0.6218 0.3994 0.5451 0.0304  0.0678  -0.0194 111 ALA B C   
2780 O O   . ALA B 94  ? 0.6640 0.4463 0.5905 0.0334  0.0622  -0.0220 111 ALA B O   
2781 C CB  . ALA B 94  ? 0.6951 0.4444 0.6100 0.0285  0.0695  -0.0248 111 ALA B CB  
2782 N N   . LEU B 95  ? 0.6711 0.4456 0.5878 0.0323  0.0716  -0.0128 112 LEU B N   
2783 C CA  . LEU B 95  ? 0.7115 0.4882 0.6251 0.0386  0.0690  -0.0083 112 LEU B CA  
2784 C C   . LEU B 95  ? 0.6269 0.4260 0.5514 0.0354  0.0670  -0.0089 112 LEU B C   
2785 O O   . LEU B 95  ? 0.6265 0.4277 0.5517 0.0394  0.0615  -0.0095 112 LEU B O   
2786 C CB  . LEU B 95  ? 0.7080 0.4799 0.6139 0.0402  0.0742  -0.0019 112 LEU B CB  
2787 C CG  . LEU B 95  ? 0.7563 0.5272 0.6568 0.0475  0.0723  0.0033  112 LEU B CG  
2788 C CD1 . LEU B 95  ? 0.9021 0.6535 0.7926 0.0561  0.0675  0.0034  112 LEU B CD1 
2789 C CD2 . LEU B 95  ? 0.8214 0.5926 0.7171 0.0465  0.0787  0.0083  112 LEU B CD2 
2790 N N   . VAL B 96  ? 0.5897 0.4054 0.5226 0.0278  0.0713  -0.0091 113 VAL B N   
2791 C CA  . VAL B 96  ? 0.6074 0.4447 0.5505 0.0241  0.0696  -0.0096 113 VAL B CA  
2792 C C   . VAL B 96  ? 0.5796 0.4215 0.5287 0.0228  0.0640  -0.0155 113 VAL B C   
2793 O O   . VAL B 96  ? 0.5173 0.3684 0.4695 0.0239  0.0596  -0.0151 113 VAL B O   
2794 C CB  . VAL B 96  ? 0.5578 0.4115 0.5090 0.0158  0.0754  -0.0096 113 VAL B CB  
2795 C CG1 . VAL B 96  ? 0.5446 0.4199 0.5062 0.0115  0.0732  -0.0108 113 VAL B CG1 
2796 C CG2 . VAL B 96  ? 0.6252 0.4774 0.5710 0.0173  0.0804  -0.0040 113 VAL B CG2 
2797 N N   . ARG B 97  ? 0.5697 0.4047 0.5200 0.0206  0.0638  -0.0211 114 ARG B N   
2798 C CA  . ARG B 97  ? 0.6115 0.4526 0.5683 0.0191  0.0587  -0.0277 114 ARG B CA  
2799 C C   . ARG B 97  ? 0.5967 0.4261 0.5469 0.0271  0.0526  -0.0281 114 ARG B C   
2800 O O   . ARG B 97  ? 0.5409 0.3791 0.4962 0.0263  0.0479  -0.0320 114 ARG B O   
2801 C CB  . ARG B 97  ? 0.5354 0.3727 0.4957 0.0150  0.0599  -0.0343 114 ARG B CB  
2802 C CG  . ARG B 97  ? 0.5725 0.4257 0.5419 0.0058  0.0652  -0.0353 114 ARG B CG  
2803 C CD  . ARG B 97  ? 0.6928 0.5418 0.6656 0.0014  0.0666  -0.0418 114 ARG B CD  
2804 N NE  . ARG B 97  ? 0.6909 0.5589 0.6745 -0.0077 0.0706  -0.0439 114 ARG B NE  
2805 C CZ  . ARG B 97  ? 0.8572 0.7237 0.8441 -0.0131 0.0738  -0.0481 114 ARG B CZ  
2806 N NH1 . ARG B 97  ? 0.7055 0.5521 0.6860 -0.0104 0.0729  -0.0511 114 ARG B NH1 
2807 N NH2 . ARG B 97  ? 0.7269 0.6122 0.7237 -0.0213 0.0776  -0.0495 114 ARG B NH2 
2808 N N   . ASP B 98  ? 0.5975 0.4077 0.5364 0.0344  0.0527  -0.0244 115 ASP B N   
2809 C CA  . ASP B 98  ? 0.6195 0.4192 0.5522 0.0421  0.0468  -0.0249 115 ASP B CA  
2810 C C   . ASP B 98  ? 0.6229 0.4306 0.5552 0.0446  0.0443  -0.0202 115 ASP B C   
2811 O O   . ASP B 98  ? 0.6035 0.4057 0.5321 0.0500  0.0391  -0.0210 115 ASP B O   
2812 C CB  . ASP B 98  ? 0.7753 0.5511 0.6956 0.0495  0.0472  -0.0227 115 ASP B CB  
2813 C CG  . ASP B 98  ? 0.9457 0.7101 0.8606 0.0570  0.0408  -0.0256 115 ASP B CG  
2814 O OD1 . ASP B 98  ? 0.8570 0.6250 0.7772 0.0557  0.0369  -0.0327 115 ASP B OD1 
2815 O OD2 . ASP B 98  ? 0.9247 0.6783 0.8308 0.0640  0.0396  -0.0210 115 ASP B OD2 
2816 N N   . ILE B 99  ? 0.5447 0.3656 0.4808 0.0409  0.0475  -0.0157 116 ILE B N   
2817 C CA  . ILE B 99  ? 0.5114 0.3393 0.4470 0.0433  0.0443  -0.0116 116 ILE B CA  
2818 C C   . ILE B 99  ? 0.5680 0.4046 0.5088 0.0415  0.0385  -0.0160 116 ILE B C   
2819 O O   . ILE B 99  ? 0.5670 0.4002 0.5036 0.0460  0.0339  -0.0144 116 ILE B O   
2820 C CB  . ILE B 99  ? 0.5069 0.3499 0.4473 0.0389  0.0481  -0.0072 116 ILE B CB  
2821 C CG1 . ILE B 99  ? 0.5659 0.4004 0.5003 0.0412  0.0538  -0.0029 116 ILE B CG1 
2822 C CG2 . ILE B 99  ? 0.5071 0.3575 0.4473 0.0410  0.0441  -0.0034 116 ILE B CG2 
2823 C CD1 . ILE B 99  ? 0.5239 0.3742 0.4637 0.0366  0.0580  0.0003  116 ILE B CD1 
2824 N N   . LEU B 100 ? 0.5248 0.3728 0.4744 0.0345  0.0386  -0.0220 117 LEU B N   
2825 C CA  . LEU B 100 ? 0.5546 0.4118 0.5098 0.0317  0.0335  -0.0277 117 LEU B CA  
2826 C C   . LEU B 100 ? 0.5753 0.4286 0.5336 0.0302  0.0335  -0.0356 117 LEU B C   
2827 O O   . LEU B 100 ? 0.5327 0.3978 0.4994 0.0231  0.0360  -0.0393 117 LEU B O   
2828 C CB  . LEU B 100 ? 0.5170 0.3963 0.4812 0.0237  0.0334  -0.0274 117 LEU B CB  
2829 C CG  . LEU B 100 ? 0.5735 0.4641 0.5425 0.0201  0.0280  -0.0322 117 LEU B CG  
2830 C CD1 . LEU B 100 ? 0.5454 0.4288 0.5069 0.0258  0.0233  -0.0284 117 LEU B CD1 
2831 C CD2 . LEU B 100 ? 0.5760 0.4891 0.5546 0.0107  0.0287  -0.0328 117 LEU B CD2 
2832 N N   . PRO B 101 ? 0.5438 0.3813 0.4958 0.0368  0.0303  -0.0386 118 PRO B N   
2833 C CA  . PRO B 101 ? 0.4982 0.3307 0.4526 0.0363  0.0294  -0.0466 118 PRO B CA  
2834 C C   . PRO B 101 ? 0.4977 0.3493 0.4635 0.0291  0.0272  -0.0541 118 PRO B C   
2835 O O   . PRO B 101 ? 0.4788 0.3446 0.4487 0.0259  0.0246  -0.0540 118 PRO B O   
2836 C CB  . PRO B 101 ? 0.5153 0.3301 0.4608 0.0453  0.0248  -0.0482 118 PRO B CB  
2837 C CG  . PRO B 101 ? 0.6277 0.4329 0.5642 0.0509  0.0257  -0.0398 118 PRO B CG  
2838 C CD  . PRO B 101 ? 0.5563 0.3786 0.4981 0.0455  0.0274  -0.0349 118 PRO B CD  
2839 N N   . ALA B 102 ? 0.5423 0.3931 0.5125 0.0268  0.0279  -0.0610 119 ALA B N   
2840 C CA  . ALA B 102 ? 0.6100 0.4798 0.5918 0.0194  0.0267  -0.0687 119 ALA B CA  
2841 C C   . ALA B 102 ? 0.5814 0.4587 0.5656 0.0201  0.0206  -0.0744 119 ALA B C   
2842 O O   . ALA B 102 ? 0.5316 0.4290 0.5245 0.0131  0.0195  -0.0778 119 ALA B O   
2843 C CB  . ALA B 102 ? 0.6641 0.5283 0.6489 0.0182  0.0280  -0.0754 119 ALA B CB  
2844 N N   . HIS B 103 ? 0.5435 0.4058 0.5200 0.0282  0.0166  -0.0756 120 HIS B N   
2845 C CA  . HIS B 103 ? 0.5701 0.4391 0.5484 0.0291  0.0108  -0.0817 120 HIS B CA  
2846 C C   . HIS B 103 ? 0.4998 0.3757 0.4757 0.0284  0.0090  -0.0759 120 HIS B C   
2847 O O   . HIS B 103 ? 0.4909 0.3712 0.4668 0.0292  0.0042  -0.0800 120 HIS B O   
2848 C CB  . HIS B 103 ? 0.5263 0.3764 0.4975 0.0384  0.0070  -0.0863 120 HIS B CB  
2849 C CG  . HIS B 103 ? 0.4976 0.3284 0.4568 0.0468  0.0069  -0.0786 120 HIS B CG  
2850 N ND1 . HIS B 103 ? 0.5962 0.4137 0.5489 0.0492  0.0115  -0.0710 120 HIS B ND1 
2851 C CD2 . HIS B 103 ? 0.5835 0.4065 0.5359 0.0532  0.0028  -0.0777 120 HIS B CD2 
2852 C CE1 . HIS B 103 ? 0.5709 0.3735 0.5134 0.0567  0.0103  -0.0656 120 HIS B CE1 
2853 N NE2 . HIS B 103 ? 0.5935 0.3988 0.5356 0.0594  0.0050  -0.0695 120 HIS B NE2 
2854 N N   . VAL B 104 ? 0.4743 0.3513 0.4479 0.0267  0.0125  -0.0668 121 VAL B N   
2855 C CA  . VAL B 104 ? 0.4242 0.3042 0.3938 0.0271  0.0108  -0.0601 121 VAL B CA  
2856 C C   . VAL B 104 ? 0.4338 0.3335 0.4106 0.0180  0.0129  -0.0570 121 VAL B C   
2857 O O   . VAL B 104 ? 0.4383 0.3430 0.4194 0.0141  0.0175  -0.0556 121 VAL B O   
2858 C CB  . VAL B 104 ? 0.4767 0.3381 0.4358 0.0350  0.0126  -0.0515 121 VAL B CB  
2859 C CG1 . VAL B 104 ? 0.4378 0.3028 0.3932 0.0351  0.0110  -0.0443 121 VAL B CG1 
2860 C CG2 . VAL B 104 ? 0.4707 0.3122 0.4217 0.0442  0.0101  -0.0542 121 VAL B CG2 
2861 N N   . ASN B 105 ? 0.4096 0.3193 0.3866 0.0148  0.0095  -0.0555 122 ASN B N   
2862 C CA  . ASN B 105 ? 0.3970 0.3242 0.3792 0.0068  0.0105  -0.0518 122 ASN B CA  
2863 C C   . ASN B 105 ? 0.3737 0.2960 0.3484 0.0096  0.0088  -0.0431 122 ASN B C   
2864 O O   . ASN B 105 ? 0.4228 0.3316 0.3896 0.0164  0.0058  -0.0415 122 ASN B O   
2865 C CB  . ASN B 105 ? 0.3879 0.3343 0.3780 -0.0016 0.0076  -0.0589 122 ASN B CB  
2866 C CG  . ASN B 105 ? 0.3858 0.3301 0.3716 0.0002  0.0021  -0.0613 122 ASN B CG  
2867 O OD1 . ASN B 105 ? 0.3703 0.3165 0.3519 -0.0010 -0.0004 -0.0560 122 ASN B OD1 
2868 N ND2 . ASN B 105 ? 0.4390 0.3787 0.4255 0.0035  -0.0001 -0.0696 122 ASN B ND2 
2869 N N   . CYS B 106 ? 0.3647 0.2975 0.3417 0.0049  0.0105  -0.0374 123 CYS B N   
2870 C CA  . CYS B 106 ? 0.4036 0.3330 0.3740 0.0072  0.0081  -0.0295 123 CYS B CA  
2871 C C   . CYS B 106 ? 0.3498 0.2978 0.3248 -0.0019 0.0064  -0.0280 123 CYS B C   
2872 O O   . CYS B 106 ? 0.4070 0.3704 0.3906 -0.0093 0.0085  -0.0318 123 CYS B O   
2873 C CB  . CYS B 106 ? 0.5097 0.4284 0.4750 0.0133  0.0116  -0.0221 123 CYS B CB  
2874 S SG  . CYS B 106 ? 0.5822 0.5115 0.5546 0.0086  0.0177  -0.0207 123 CYS B SG  
2875 N N   . LEU B 107 ? 0.3116 0.2575 0.2806 -0.0012 0.0023  -0.0230 124 LEU B N   
2876 C CA  . LEU B 107 ? 0.3580 0.3186 0.3291 -0.0089 0.0003  -0.0197 124 LEU B CA  
2877 C C   . LEU B 107 ? 0.3661 0.3178 0.3291 -0.0040 -0.0020 -0.0109 124 LEU B C   
2878 O O   . LEU B 107 ? 0.3505 0.2856 0.3059 0.0045  -0.0032 -0.0083 124 LEU B O   
2879 C CB  . LEU B 107 ? 0.3871 0.3582 0.3601 -0.0161 -0.0040 -0.0248 124 LEU B CB  
2880 C CG  . LEU B 107 ? 0.4086 0.3701 0.3745 -0.0131 -0.0089 -0.0257 124 LEU B CG  
2881 C CD1 . LEU B 107 ? 0.4719 0.4304 0.4302 -0.0136 -0.0131 -0.0179 124 LEU B CD1 
2882 C CD2 . LEU B 107 ? 0.3509 0.3262 0.3226 -0.0209 -0.0107 -0.0344 124 LEU B CD2 
2883 N N   . TYR B 108 ? 0.3393 0.3022 0.3037 -0.0094 -0.0030 -0.0064 125 TYR B N   
2884 C CA  . TYR B 108 ? 0.3570 0.3133 0.3146 -0.0051 -0.0052 0.0019  125 TYR B CA  
2885 C C   . TYR B 108 ? 0.3541 0.3161 0.3080 -0.0109 -0.0110 0.0048  125 TYR B C   
2886 O O   . TYR B 108 ? 0.3331 0.3110 0.2923 -0.0203 -0.0116 0.0026  125 TYR B O   
2887 C CB  . TYR B 108 ? 0.3123 0.2759 0.2744 -0.0052 -0.0009 0.0051  125 TYR B CB  
2888 C CG  . TYR B 108 ? 0.3273 0.2855 0.2925 -0.0007 0.0051  0.0024  125 TYR B CG  
2889 C CD1 . TYR B 108 ? 0.3344 0.2760 0.2931 0.0090  0.0064  0.0056  125 TYR B CD1 
2890 C CD2 . TYR B 108 ? 0.3542 0.3233 0.3282 -0.0063 0.0095  -0.0033 125 TYR B CD2 
2891 C CE1 . TYR B 108 ? 0.3054 0.2413 0.2659 0.0126  0.0118  0.0034  125 TYR B CE1 
2892 C CE2 . TYR B 108 ? 0.3584 0.3211 0.3345 -0.0026 0.0148  -0.0056 125 TYR B CE2 
2893 C CZ  . TYR B 108 ? 0.3889 0.3349 0.3579 0.0067  0.0160  -0.0020 125 TYR B CZ  
2894 O OH  . TYR B 108 ? 0.4294 0.3686 0.3994 0.0097  0.0213  -0.0040 125 TYR B OH  
2895 N N   . ILE B 109 ? 0.3071 0.2560 0.2519 -0.0054 -0.0154 0.0098  126 ILE B N   
2896 C CA  . ILE B 109 ? 0.3291 0.2797 0.2683 -0.0100 -0.0215 0.0138  126 ILE B CA  
2897 C C   . ILE B 109 ? 0.3911 0.3312 0.3229 -0.0030 -0.0241 0.0219  126 ILE B C   
2898 O O   . ILE B 109 ? 0.3711 0.2963 0.2981 0.0066  -0.0236 0.0237  126 ILE B O   
2899 C CB  . ILE B 109 ? 0.4045 0.3482 0.3386 -0.0108 -0.0256 0.0106  126 ILE B CB  
2900 C CG1 . ILE B 109 ? 0.4600 0.4110 0.4012 -0.0144 -0.0227 0.0015  126 ILE B CG1 
2901 C CG2 . ILE B 109 ? 0.4409 0.3902 0.3704 -0.0188 -0.0313 0.0137  126 ILE B CG2 
2902 C CD1 . ILE B 109 ? 0.5380 0.4845 0.4751 -0.0157 -0.0267 -0.0027 126 ILE B CD1 
2903 N N   . ARG B 110 ? 0.3665 0.3138 0.2966 -0.0079 -0.0275 0.0267  127 ARG B N   
2904 C CA  . ARG B 110 ? 0.4945 0.4326 0.4176 -0.0015 -0.0310 0.0342  127 ARG B CA  
2905 C C   . ARG B 110 ? 0.4803 0.4059 0.3932 -0.0004 -0.0378 0.0373  127 ARG B C   
2906 O O   . ARG B 110 ? 0.4402 0.3710 0.3510 -0.0089 -0.0416 0.0367  127 ARG B O   
2907 C CB  . ARG B 110 ? 0.4755 0.4261 0.4007 -0.0065 -0.0322 0.0382  127 ARG B CB  
2908 C CG  . ARG B 110 ? 0.5376 0.5056 0.4735 -0.0125 -0.0266 0.0342  127 ARG B CG  
2909 C CD  . ARG B 110 ? 0.5527 0.5181 0.4936 -0.0056 -0.0201 0.0320  127 ARG B CD  
2910 N NE  . ARG B 110 ? 0.4681 0.4502 0.4190 -0.0114 -0.0148 0.0286  127 ARG B NE  
2911 C CZ  . ARG B 110 ? 0.4878 0.4710 0.4449 -0.0091 -0.0084 0.0246  127 ARG B CZ  
2912 N NH1 . ARG B 110 ? 0.4202 0.3888 0.3742 -0.0014 -0.0064 0.0232  127 ARG B NH1 
2913 N NH2 . ARG B 110 ? 0.4524 0.4512 0.4185 -0.0148 -0.0040 0.0218  127 ARG B NH2 
2914 N N   . GLN B 111 ? 0.4365 0.3459 0.3427 0.0098  -0.0394 0.0406  128 GLN B N   
2915 C CA  . GLN B 111 ? 0.4919 0.3891 0.3879 0.0111  -0.0465 0.0445  128 GLN B CA  
2916 C C   . GLN B 111 ? 0.5170 0.4172 0.4090 0.0084  -0.0514 0.0510  128 GLN B C   
2917 O O   . GLN B 111 ? 0.5312 0.4374 0.4267 0.0108  -0.0495 0.0534  128 GLN B O   
2918 C CB  . GLN B 111 ? 0.4513 0.3304 0.3414 0.0231  -0.0469 0.0460  128 GLN B CB  
2919 C CG  . GLN B 111 ? 0.5210 0.3960 0.4103 0.0319  -0.0459 0.0504  128 GLN B CG  
2920 C CD  . GLN B 111 ? 0.6073 0.4648 0.4901 0.0434  -0.0468 0.0518  128 GLN B CD  
2921 O OE1 . GLN B 111 ? 0.4705 0.3192 0.3504 0.0451  -0.0471 0.0487  128 GLN B OE1 
2922 N NE2 . GLN B 111 ? 0.5201 0.3728 0.4004 0.0513  -0.0476 0.0561  128 GLN B NE2 
2923 N N   . SER B 112 ? 0.5226 0.4192 0.4072 0.0027  -0.0578 0.0535  129 SER B N   
2924 C CA  . SER B 112 ? 0.6281 0.5273 0.5083 -0.0008 -0.0631 0.0596  129 SER B CA  
2925 C C   . SER B 112 ? 0.6789 0.5655 0.5532 0.0102  -0.0664 0.0654  129 SER B C   
2926 O O   . SER B 112 ? 0.6691 0.5603 0.5430 0.0104  -0.0686 0.0695  129 SER B O   
2927 C CB  . SER B 112 ? 0.6759 0.5725 0.5481 -0.0098 -0.0696 0.0612  129 SER B CB  
2928 O OG  . SER B 112 ? 0.6506 0.5298 0.5145 -0.0043 -0.0732 0.0620  129 SER B OG  
2929 N N   . ALA B 113 ? 0.6397 0.5105 0.5090 0.0195  -0.0672 0.0655  130 ALA B N   
2930 C CA  . ALA B 113 ? 0.6791 0.5371 0.5426 0.0306  -0.0706 0.0703  130 ALA B CA  
2931 C C   . ALA B 113 ? 0.6317 0.4766 0.4934 0.0400  -0.0683 0.0679  130 ALA B C   
2932 O O   . ALA B 113 ? 0.5692 0.4125 0.4317 0.0371  -0.0664 0.0636  130 ALA B O   
2933 C CB  . ALA B 113 ? 0.6886 0.5370 0.5413 0.0289  -0.0798 0.0762  130 ALA B CB  
2934 N N   . PRO B 114 ? 0.7551 0.5909 0.6143 0.0515  -0.0687 0.0704  131 PRO B N   
2935 C CA  . PRO B 114 ? 0.7780 0.6006 0.6346 0.0609  -0.0669 0.0685  131 PRO B CA  
2936 C C   . PRO B 114 ? 0.7877 0.5947 0.6342 0.0623  -0.0737 0.0703  131 PRO B C   
2937 O O   . PRO B 114 ? 0.9109 0.7062 0.7502 0.0691  -0.0792 0.0743  131 PRO B O   
2938 C CB  . PRO B 114 ? 0.8402 0.6612 0.6979 0.0714  -0.0653 0.0707  131 PRO B CB  
2939 C CG  . PRO B 114 ? 0.8776 0.7027 0.7330 0.0695  -0.0707 0.0754  131 PRO B CG  
2940 C CD  . PRO B 114 ? 0.8639 0.7023 0.7231 0.0565  -0.0706 0.0746  131 PRO B CD  
2941 N N   . LEU B 115 ? 0.6972 0.5048 0.5434 0.0549  -0.0737 0.0669  132 LEU B N   
2942 C CA  . LEU B 115 ? 0.7162 0.5112 0.5534 0.0537  -0.0797 0.0677  132 LEU B CA  
2943 C C   . LEU B 115 ? 0.6785 0.4647 0.5150 0.0591  -0.0772 0.0632  132 LEU B C   
2944 O O   . LEU B 115 ? 0.7606 0.5398 0.5917 0.0560  -0.0808 0.0620  132 LEU B O   
2945 C CB  . LEU B 115 ? 0.7032 0.5065 0.5396 0.0401  -0.0826 0.0672  132 LEU B CB  
2946 C CG  . LEU B 115 ? 0.7420 0.5510 0.5761 0.0342  -0.0870 0.0725  132 LEU B CG  
2947 C CD1 . LEU B 115 ? 0.6329 0.4527 0.4676 0.0200  -0.0880 0.0708  132 LEU B CD1 
2948 C CD2 . LEU B 115 ? 0.8206 0.6132 0.6435 0.0394  -0.0951 0.0784  132 LEU B CD2 
2949 N N   . GLY B 116 ? 0.6776 0.4646 0.5195 0.0663  -0.0709 0.0605  133 GLY B N   
2950 C CA  . GLY B 116 ? 0.6482 0.4258 0.4888 0.0727  -0.0687 0.0567  133 GLY B CA  
2951 C C   . GLY B 116 ? 0.5601 0.3465 0.4073 0.0671  -0.0635 0.0502  133 GLY B C   
2952 O O   . GLY B 116 ? 0.5907 0.3910 0.4438 0.0574  -0.0618 0.0481  133 GLY B O   
2953 N N   . LEU B 117 ? 0.3935 0.3840 0.3959 -0.0598 -0.0376 0.0205  134 LEU B N   
2954 C CA  . LEU B 117 ? 0.3965 0.3957 0.3965 -0.0545 -0.0305 0.0213  134 LEU B CA  
2955 C C   . LEU B 117 ? 0.3824 0.3916 0.3771 -0.0574 -0.0286 0.0246  134 LEU B C   
2956 O O   . LEU B 117 ? 0.3499 0.3635 0.3418 -0.0540 -0.0240 0.0242  134 LEU B O   
2957 C CB  . LEU B 117 ? 0.4192 0.4255 0.4238 -0.0510 -0.0276 0.0207  134 LEU B CB  
2958 C CG  . LEU B 117 ? 0.3858 0.4004 0.3897 -0.0452 -0.0218 0.0215  134 LEU B CG  
2959 C CD1 . LEU B 117 ? 0.3724 0.3795 0.3750 -0.0403 -0.0193 0.0193  134 LEU B CD1 
2960 C CD2 . LEU B 117 ? 0.3914 0.4110 0.3988 -0.0430 -0.0206 0.0215  134 LEU B CD2 
2961 N N   . GLY B 118 ? 0.4066 0.4205 0.4004 -0.0637 -0.0319 0.0274  135 GLY B N   
2962 C CA  . GLY B 118 ? 0.3914 0.4159 0.3800 -0.0677 -0.0297 0.0302  135 GLY B CA  
2963 C C   . GLY B 118 ? 0.4644 0.4837 0.4453 -0.0709 -0.0302 0.0306  135 GLY B C   
2964 O O   . GLY B 118 ? 0.3589 0.3873 0.3361 -0.0705 -0.0252 0.0302  135 GLY B O   
2965 N N   . HIS B 119 ? 0.3723 0.3770 0.3512 -0.0741 -0.0365 0.0307  136 HIS B N   
2966 C CA  . HIS B 119 ? 0.4314 0.4291 0.4023 -0.0771 -0.0378 0.0311  136 HIS B CA  
2967 C C   . HIS B 119 ? 0.3847 0.3820 0.3563 -0.0692 -0.0319 0.0274  136 HIS B C   
2968 O O   . HIS B 119 ? 0.3647 0.3655 0.3299 -0.0701 -0.0288 0.0270  136 HIS B O   
2969 C CB  . HIS B 119 ? 0.4665 0.4474 0.4369 -0.0815 -0.0471 0.0316  136 HIS B CB  
2970 C CG  . HIS B 119 ? 0.4802 0.4523 0.4413 -0.0856 -0.0499 0.0327  136 HIS B CG  
2971 N ND1 . HIS B 119 ? 0.5270 0.5024 0.4774 -0.0947 -0.0515 0.0370  136 HIS B ND1 
2972 C CD2 . HIS B 119 ? 0.4495 0.4099 0.4097 -0.0824 -0.0515 0.0300  136 HIS B CD2 
2973 C CE1 . HIS B 119 ? 0.5414 0.5072 0.4841 -0.0972 -0.0542 0.0371  136 HIS B CE1 
2974 N NE2 . HIS B 119 ? 0.5287 0.4850 0.4776 -0.0894 -0.0544 0.0328  136 HIS B NE2 
2975 N N   . ALA B 120 ? 0.3996 0.3930 0.3785 -0.0618 -0.0305 0.0243  137 ALA B N   
2976 C CA  . ALA B 120 ? 0.3702 0.3625 0.3503 -0.0543 -0.0255 0.0211  137 ALA B CA  
2977 C C   . ALA B 120 ? 0.3508 0.3579 0.3305 -0.0511 -0.0189 0.0207  137 ALA B C   
2978 O O   . ALA B 120 ? 0.3635 0.3723 0.3407 -0.0485 -0.0155 0.0186  137 ALA B O   
2979 C CB  . ALA B 120 ? 0.3797 0.3661 0.3672 -0.0483 -0.0251 0.0185  137 ALA B CB  
2980 N N   . VAL B 121 ? 0.3396 0.3581 0.3228 -0.0514 -0.0173 0.0221  138 VAL B N   
2981 C CA  . VAL B 121 ? 0.3700 0.4033 0.3550 -0.0482 -0.0117 0.0209  138 VAL B CA  
2982 C C   . VAL B 121 ? 0.3447 0.3857 0.3230 -0.0542 -0.0100 0.0208  138 VAL B C   
2983 O O   . VAL B 121 ? 0.4010 0.4491 0.3794 -0.0510 -0.0055 0.0174  138 VAL B O   
2984 C CB  . VAL B 121 ? 0.3229 0.3663 0.3132 -0.0477 -0.0112 0.0224  138 VAL B CB  
2985 C CG1 . VAL B 121 ? 0.3472 0.4072 0.3399 -0.0460 -0.0065 0.0207  138 VAL B CG1 
2986 C CG2 . VAL B 121 ? 0.3689 0.4068 0.3649 -0.0413 -0.0117 0.0218  138 VAL B CG2 
2987 N N   . LEU B 122 ? 0.3704 0.4101 0.3427 -0.0635 -0.0138 0.0243  139 LEU B N   
2988 C CA  . LEU B 122 ? 0.3813 0.4278 0.3451 -0.0712 -0.0123 0.0247  139 LEU B CA  
2989 C C   . LEU B 122 ? 0.4047 0.4436 0.3625 -0.0706 -0.0117 0.0225  139 LEU B C   
2990 O O   . LEU B 122 ? 0.3443 0.3932 0.2979 -0.0727 -0.0072 0.0199  139 LEU B O   
2991 C CB  . LEU B 122 ? 0.4336 0.4765 0.3913 -0.0819 -0.0182 0.0299  139 LEU B CB  
2992 C CG  . LEU B 122 ? 0.4894 0.5387 0.4362 -0.0927 -0.0177 0.0318  139 LEU B CG  
2993 C CD1 . LEU B 122 ? 0.4064 0.4771 0.3549 -0.0931 -0.0097 0.0286  139 LEU B CD1 
2994 C CD2 . LEU B 122 ? 0.4982 0.5412 0.4406 -0.1024 -0.0252 0.0376  139 LEU B CD2 
2995 N N   . THR B 123 ? 0.3971 0.4194 0.3553 -0.0674 -0.0159 0.0224  140 THR B N   
2996 C CA  . THR B 123 ? 0.4067 0.4209 0.3601 -0.0659 -0.0157 0.0200  140 THR B CA  
2997 C C   . THR B 123 ? 0.3916 0.4163 0.3489 -0.0585 -0.0084 0.0148  140 THR B C   
2998 O O   . THR B 123 ? 0.3860 0.4105 0.3379 -0.0591 -0.0065 0.0121  140 THR B O   
2999 C CB  . THR B 123 ? 0.3880 0.3843 0.3449 -0.0617 -0.0206 0.0197  140 THR B CB  
3000 O OG1 . THR B 123 ? 0.4289 0.4148 0.3825 -0.0691 -0.0285 0.0234  140 THR B OG1 
3001 C CG2 . THR B 123 ? 0.4147 0.4030 0.3686 -0.0585 -0.0200 0.0166  140 THR B CG2 
3002 N N   . ALA B 124 ? 0.3315 0.3652 0.2980 -0.0516 -0.0049 0.0131  141 ALA B N   
3003 C CA  . ALA B 124 ? 0.3468 0.3893 0.3195 -0.0436 0.0006  0.0079  141 ALA B CA  
3004 C C   . ALA B 124 ? 0.3257 0.3874 0.2982 -0.0465 0.0057  0.0046  141 ALA B C   
3005 O O   . ALA B 124 ? 0.3553 0.4252 0.3333 -0.0405 0.0099  -0.0011 141 ALA B O   
3006 C CB  . ALA B 124 ? 0.3346 0.3769 0.3175 -0.0351 0.0008  0.0077  141 ALA B CB  
3007 N N   . ALA B 125 ? 0.3717 0.4411 0.3386 -0.0559 0.0054  0.0074  142 ALA B N   
3008 C CA  . ALA B 125 ? 0.4125 0.5020 0.3802 -0.0593 0.0110  0.0035  142 ALA B CA  
3009 C C   . ALA B 125 ? 0.3623 0.4585 0.3276 -0.0588 0.0156  -0.0030 142 ALA B C   
3010 O O   . ALA B 125 ? 0.3636 0.4760 0.3373 -0.0544 0.0208  -0.0096 142 ALA B O   
3011 C CB  . ALA B 125 ? 0.4233 0.5176 0.3825 -0.0718 0.0094  0.0081  142 ALA B CB  
3012 N N   . PRO B 126 ? 0.3667 0.4517 0.3220 -0.0625 0.0138  -0.0022 143 PRO B N   
3013 C CA  . PRO B 126 ? 0.4375 0.5307 0.3907 -0.0621 0.0187  -0.0092 143 PRO B CA  
3014 C C   . PRO B 126 ? 0.4113 0.5074 0.3778 -0.0490 0.0214  -0.0160 143 PRO B C   
3015 O O   . PRO B 126 ? 0.4149 0.5237 0.3844 -0.0472 0.0264  -0.0237 143 PRO B O   
3016 C CB  . PRO B 126 ? 0.3937 0.4701 0.3337 -0.0678 0.0143  -0.0058 143 PRO B CB  
3017 C CG  . PRO B 126 ? 0.3976 0.4622 0.3311 -0.0750 0.0077  0.0026  143 PRO B CG  
3018 C CD  . PRO B 126 ? 0.3246 0.3903 0.2701 -0.0681 0.0069  0.0043  143 PRO B CD  
3019 N N   . ALA B 127 ? 0.3875 0.4720 0.3618 -0.0401 0.0181  -0.0135 144 ALA B N   
3020 C CA  . ALA B 127 ? 0.3800 0.4656 0.3666 -0.0282 0.0195  -0.0189 144 ALA B CA  
3021 C C   . ALA B 127 ? 0.4293 0.5294 0.4284 -0.0230 0.0213  -0.0216 144 ALA B C   
3022 O O   . ALA B 127 ? 0.4377 0.5447 0.4478 -0.0145 0.0230  -0.0281 144 ALA B O   
3023 C CB  . ALA B 127 ? 0.4174 0.4830 0.4055 -0.0219 0.0149  -0.0149 144 ALA B CB  
3024 N N   . VAL B 128 ? 0.4110 0.5154 0.4095 -0.0276 0.0202  -0.0170 145 VAL B N   
3025 C CA  . VAL B 128 ? 0.4039 0.5207 0.4143 -0.0227 0.0210  -0.0191 145 VAL B CA  
3026 C C   . VAL B 128 ? 0.4031 0.5426 0.4175 -0.0264 0.0263  -0.0260 145 VAL B C   
3027 O O   . VAL B 128 ? 0.4222 0.5741 0.4498 -0.0195 0.0278  -0.0324 145 VAL B O   
3028 C CB  . VAL B 128 ? 0.3658 0.4770 0.3744 -0.0257 0.0173  -0.0114 145 VAL B CB  
3029 C CG1 . VAL B 128 ? 0.3569 0.4832 0.3762 -0.0229 0.0182  -0.0134 145 VAL B CG1 
3030 C CG2 . VAL B 128 ? 0.4321 0.5239 0.4402 -0.0206 0.0128  -0.0067 145 VAL B CG2 
3031 N N   . GLY B 129 ? 0.4291 0.5745 0.4325 -0.0376 0.0288  -0.0253 146 GLY B N   
3032 C CA  . GLY B 129 ? 0.4884 0.6569 0.4956 -0.0422 0.0345  -0.0323 146 GLY B CA  
3033 C C   . GLY B 129 ? 0.4493 0.6280 0.4641 -0.0426 0.0340  -0.0306 146 GLY B C   
3034 O O   . GLY B 129 ? 0.5057 0.6746 0.5161 -0.0454 0.0299  -0.0223 146 GLY B O   
3035 N N   . ASN B 130 ? 0.4487 0.6483 0.4755 -0.0404 0.0382  -0.0394 147 ASN B N   
3036 C CA  . ASN B 130 ? 0.6477 0.8595 0.6838 -0.0401 0.0379  -0.0395 147 ASN B CA  
3037 C C   . ASN B 130 ? 0.6197 0.8301 0.6723 -0.0265 0.0343  -0.0423 147 ASN B C   
3038 O O   . ASN B 130 ? 0.6794 0.9065 0.7465 -0.0221 0.0358  -0.0501 147 ASN B O   
3039 C CB  . ASN B 130 ? 0.5456 0.7825 0.5846 -0.0477 0.0447  -0.0478 147 ASN B CB  
3040 C CG  . ASN B 130 ? 0.7598 1.0064 0.7997 -0.0543 0.0448  -0.0443 147 ASN B CG  
3041 O OD1 . ASN B 130 ? 0.7489 0.9822 0.7806 -0.0579 0.0403  -0.0342 147 ASN B OD1 
3042 N ND2 . ASN B 130 ? 1.0745 1.3450 1.1244 -0.0566 0.0499  -0.0534 147 ASN B ND2 
3043 N N   . GLU B 131 ? 0.5541 0.7441 0.6043 -0.0204 0.0290  -0.0359 148 GLU B N   
3044 C CA  . GLU B 131 ? 0.5254 0.7107 0.5884 -0.0087 0.0245  -0.0367 148 GLU B CA  
3045 C C   . GLU B 131 ? 0.4046 0.5751 0.4626 -0.0088 0.0193  -0.0266 148 GLU B C   
3046 O O   . GLU B 131 ? 0.3335 0.4914 0.3788 -0.0148 0.0184  -0.0196 148 GLU B O   
3047 C CB  . GLU B 131 ? 0.4200 0.5937 0.4857 -0.0002 0.0228  -0.0393 148 GLU B CB  
3048 C CG  . GLU B 131 ? 0.5191 0.7040 0.5901 0.0016  0.0271  -0.0498 148 GLU B CG  
3049 C CD  . GLU B 131 ? 0.5182 0.6897 0.5934 0.0110  0.0239  -0.0514 148 GLU B CD  
3050 O OE1 . GLU B 131 ? 0.4151 0.5719 0.4927 0.0174  0.0182  -0.0457 148 GLU B OE1 
3051 O OE2 . GLU B 131 ? 0.5471 0.7229 0.6227 0.0115  0.0272  -0.0584 148 GLU B OE2 
3052 N N   . PRO B 132 ? 0.3802 0.5514 0.4483 -0.0021 0.0153  -0.0260 149 PRO B N   
3053 C CA  . PRO B 132 ? 0.3291 0.4851 0.3923 -0.0014 0.0103  -0.0170 149 PRO B CA  
3054 C C   . PRO B 132 ? 0.3162 0.4530 0.3741 0.0026  0.0079  -0.0139 149 PRO B C   
3055 O O   . PRO B 132 ? 0.3290 0.4644 0.3920 0.0087  0.0081  -0.0188 149 PRO B O   
3056 C CB  . PRO B 132 ? 0.3675 0.5302 0.4436 0.0054  0.0064  -0.0186 149 PRO B CB  
3057 C CG  . PRO B 132 ? 0.4395 0.6125 0.5286 0.0125  0.0073  -0.0284 149 PRO B CG  
3058 C CD  . PRO B 132 ? 0.4062 0.5908 0.4913 0.0059  0.0143  -0.0340 149 PRO B CD  
3059 N N   . PHE B 133 ? 0.3236 0.4459 0.3719 -0.0009 0.0056  -0.0063 150 PHE B N   
3060 C CA  . PHE B 133 ? 0.3050 0.4093 0.3475 0.0014  0.0040  -0.0035 150 PHE B CA  
3061 C C   . PHE B 133 ? 0.3295 0.4215 0.3682 0.0009  0.0000  0.0034  150 PHE B C   
3062 O O   . PHE B 133 ? 0.2973 0.3935 0.3351 -0.0030 -0.0011 0.0066  150 PHE B O   
3063 C CB  . PHE B 133 ? 0.2798 0.3792 0.3123 -0.0050 0.0067  -0.0034 150 PHE B CB  
3064 C CG  . PHE B 133 ? 0.2906 0.3892 0.3148 -0.0142 0.0065  0.0015  150 PHE B CG  
3065 C CD1 . PHE B 133 ? 0.2864 0.3996 0.3106 -0.0202 0.0086  0.0005  150 PHE B CD1 
3066 C CD2 . PHE B 133 ? 0.2999 0.3833 0.3170 -0.0171 0.0037  0.0066  150 PHE B CD2 
3067 C CE1 . PHE B 133 ? 0.2706 0.3818 0.2873 -0.0289 0.0074  0.0055  150 PHE B CE1 
3068 C CE2 . PHE B 133 ? 0.3025 0.3846 0.3135 -0.0252 0.0023  0.0106  150 PHE B CE2 
3069 C CZ  . PHE B 133 ? 0.3207 0.4161 0.3314 -0.0310 0.0038  0.0105  150 PHE B CZ  
3070 N N   . ALA B 134 ? 0.2729 0.3504 0.3095 0.0046  -0.0020 0.0051  151 ALA B N   
3071 C CA  . ALA B 134 ? 0.3036 0.3693 0.3358 0.0035  -0.0050 0.0106  151 ALA B CA  
3072 C C   . ALA B 134 ? 0.2672 0.3223 0.2907 -0.0022 -0.0041 0.0126  151 ALA B C   
3073 O O   . ALA B 134 ? 0.3062 0.3589 0.3269 -0.0033 -0.0021 0.0103  151 ALA B O   
3074 C CB  . ALA B 134 ? 0.2673 0.3232 0.3023 0.0101  -0.0079 0.0113  151 ALA B CB  
3075 N N   . VAL B 135 ? 0.2950 0.3445 0.3149 -0.0059 -0.0060 0.0165  152 VAL B N   
3076 C CA  . VAL B 135 ? 0.2819 0.3200 0.2959 -0.0105 -0.0064 0.0178  152 VAL B CA  
3077 C C   . VAL B 135 ? 0.3488 0.3771 0.3617 -0.0094 -0.0082 0.0199  152 VAL B C   
3078 O O   . VAL B 135 ? 0.3080 0.3398 0.3219 -0.0095 -0.0098 0.0222  152 VAL B O   
3079 C CB  . VAL B 135 ? 0.2767 0.3191 0.2879 -0.0179 -0.0071 0.0194  152 VAL B CB  
3080 C CG1 . VAL B 135 ? 0.3144 0.3446 0.3214 -0.0221 -0.0086 0.0197  152 VAL B CG1 
3081 C CG2 . VAL B 135 ? 0.2624 0.3153 0.2731 -0.0206 -0.0051 0.0177  152 VAL B CG2 
3082 N N   . LEU B 136 ? 0.2985 0.3147 0.3090 -0.0088 -0.0079 0.0189  153 LEU B N   
3083 C CA  . LEU B 136 ? 0.2869 0.2942 0.2958 -0.0090 -0.0089 0.0202  153 LEU B CA  
3084 C C   . LEU B 136 ? 0.2891 0.2874 0.2955 -0.0135 -0.0087 0.0184  153 LEU B C   
3085 O O   . LEU B 136 ? 0.3183 0.3111 0.3243 -0.0131 -0.0081 0.0161  153 LEU B O   
3086 C CB  . LEU B 136 ? 0.2763 0.2771 0.2862 -0.0034 -0.0091 0.0201  153 LEU B CB  
3087 C CG  . LEU B 136 ? 0.3215 0.3293 0.3357 0.0020  -0.0107 0.0212  153 LEU B CG  
3088 C CD1 . LEU B 136 ? 0.3321 0.3471 0.3509 0.0059  -0.0093 0.0177  153 LEU B CD1 
3089 C CD2 . LEU B 136 ? 0.3470 0.3456 0.3605 0.0051  -0.0130 0.0232  153 LEU B CD2 
3090 N N   . LEU B 137 ? 0.3128 0.3101 0.3183 -0.0177 -0.0096 0.0190  154 LEU B N   
3091 C CA  . LEU B 137 ? 0.2920 0.2819 0.2973 -0.0220 -0.0099 0.0161  154 LEU B CA  
3092 C C   . LEU B 137 ? 0.3159 0.2978 0.3201 -0.0214 -0.0087 0.0150  154 LEU B C   
3093 O O   . LEU B 137 ? 0.3378 0.3215 0.3401 -0.0228 -0.0086 0.0168  154 LEU B O   
3094 C CB  . LEU B 137 ? 0.3243 0.3192 0.3306 -0.0273 -0.0117 0.0160  154 LEU B CB  
3095 C CG  . LEU B 137 ? 0.3105 0.3154 0.3174 -0.0284 -0.0129 0.0183  154 LEU B CG  
3096 C CD1 . LEU B 137 ? 0.3747 0.3828 0.3833 -0.0339 -0.0152 0.0178  154 LEU B CD1 
3097 C CD2 . LEU B 137 ? 0.3583 0.3621 0.3645 -0.0283 -0.0131 0.0177  154 LEU B CD2 
3098 N N   . ALA B 138 ? 0.3320 0.3049 0.3366 -0.0199 -0.0078 0.0123  155 ALA B N   
3099 C CA  . ALA B 138 ? 0.3255 0.2911 0.3287 -0.0191 -0.0064 0.0118  155 ALA B CA  
3100 C C   . ALA B 138 ? 0.3481 0.3127 0.3508 -0.0249 -0.0057 0.0095  155 ALA B C   
3101 O O   . ALA B 138 ? 0.3297 0.2909 0.3294 -0.0261 -0.0043 0.0101  155 ALA B O   
3102 C CB  . ALA B 138 ? 0.3008 0.2573 0.3053 -0.0163 -0.0056 0.0089  155 ALA B CB  
3103 N N   . ASP B 139 ? 0.3137 0.2816 0.3195 -0.0290 -0.0068 0.0065  156 ASP B N   
3104 C CA  . ASP B 139 ? 0.3843 0.3534 0.3912 -0.0347 -0.0061 0.0028  156 ASP B CA  
3105 C C   . ASP B 139 ? 0.3893 0.3646 0.3913 -0.0367 -0.0054 0.0066  156 ASP B C   
3106 O O   . ASP B 139 ? 0.4004 0.3759 0.4008 -0.0415 -0.0037 0.0041  156 ASP B O   
3107 C CB  . ASP B 139 ? 0.3562 0.3280 0.3686 -0.0380 -0.0088 -0.0011 156 ASP B CB  
3108 C CG  . ASP B 139 ? 0.4468 0.4111 0.4652 -0.0397 -0.0095 -0.0083 156 ASP B CG  
3109 O OD1 . ASP B 139 ? 0.4519 0.4101 0.4699 -0.0390 -0.0069 -0.0107 156 ASP B OD1 
3110 O OD2 . ASP B 139 ? 0.4656 0.4301 0.4898 -0.0420 -0.0131 -0.0118 156 ASP B OD2 
3111 N N   . ASP B 140 ? 0.3252 0.3061 0.3251 -0.0336 -0.0069 0.0121  157 ASP B N   
3112 C CA  . ASP B 140 ? 0.3473 0.3325 0.3423 -0.0346 -0.0072 0.0164  157 ASP B CA  
3113 C C   . ASP B 140 ? 0.3993 0.3778 0.3903 -0.0312 -0.0070 0.0198  157 ASP B C   
3114 O O   . ASP B 140 ? 0.3186 0.2973 0.3106 -0.0255 -0.0085 0.0229  157 ASP B O   
3115 C CB  . ASP B 140 ? 0.3792 0.3736 0.3752 -0.0328 -0.0095 0.0200  157 ASP B CB  
3116 C CG  . ASP B 140 ? 0.4295 0.4307 0.4282 -0.0375 -0.0103 0.0176  157 ASP B CG  
3117 O OD1 . ASP B 140 ? 0.4486 0.4484 0.4478 -0.0424 -0.0093 0.0132  157 ASP B OD1 
3118 O OD2 . ASP B 140 ? 0.5003 0.5086 0.5013 -0.0365 -0.0121 0.0195  157 ASP B OD2 
3119 N N   . LEU B 141 ? 0.3471 0.3199 0.3340 -0.0351 -0.0053 0.0187  158 LEU B N   
3120 C CA  . LEU B 141 ? 0.3341 0.2993 0.3166 -0.0330 -0.0058 0.0223  158 LEU B CA  
3121 C C   . LEU B 141 ? 0.4059 0.3738 0.3821 -0.0347 -0.0085 0.0282  158 LEU B C   
3122 O O   . LEU B 141 ? 0.3627 0.3338 0.3342 -0.0413 -0.0077 0.0279  158 LEU B O   
3123 C CB  . LEU B 141 ? 0.3488 0.3063 0.3295 -0.0371 -0.0027 0.0185  158 LEU B CB  
3124 C CG  . LEU B 141 ? 0.3726 0.3204 0.3505 -0.0345 -0.0032 0.0214  158 LEU B CG  
3125 C CD1 . LEU B 141 ? 0.4779 0.4204 0.4544 -0.0404 0.0006  0.0165  158 LEU B CD1 
3126 C CD2 . LEU B 141 ? 0.4863 0.4323 0.4575 -0.0342 -0.0068 0.0286  158 LEU B CD2 
3127 N N   . ILE B 142 ? 0.3911 0.3581 0.3677 -0.0288 -0.0122 0.0331  159 ILE B N   
3128 C CA  . ILE B 142 ? 0.3976 0.3667 0.3694 -0.0294 -0.0164 0.0388  159 ILE B CA  
3129 C C   . ILE B 142 ? 0.4061 0.3653 0.3737 -0.0278 -0.0198 0.0434  159 ILE B C   
3130 O O   . ILE B 142 ? 0.4181 0.3732 0.3907 -0.0211 -0.0214 0.0435  159 ILE B O   
3131 C CB  . ILE B 142 ? 0.3954 0.3738 0.3732 -0.0241 -0.0192 0.0401  159 ILE B CB  
3132 C CG1 . ILE B 142 ? 0.4128 0.4004 0.3940 -0.0268 -0.0165 0.0363  159 ILE B CG1 
3133 C CG2 . ILE B 142 ? 0.4951 0.4740 0.4685 -0.0243 -0.0246 0.0460  159 ILE B CG2 
3134 C CD1 . ILE B 142 ? 0.4399 0.4374 0.4268 -0.0226 -0.0186 0.0373  159 ILE B CD1 
3135 N N   . ASP B 143 ? 0.3674 0.3225 0.3254 -0.0344 -0.0215 0.0473  160 ASP B N   
3136 C CA  . ASP B 143 ? 0.3918 0.3362 0.3438 -0.0347 -0.0260 0.0530  160 ASP B CA  
3137 C C   . ASP B 143 ? 0.4714 0.4174 0.4208 -0.0334 -0.0332 0.0592  160 ASP B C   
3138 O O   . ASP B 143 ? 0.5019 0.4526 0.4448 -0.0395 -0.0336 0.0608  160 ASP B O   
3139 C CB  . ASP B 143 ? 0.4685 0.4066 0.4100 -0.0447 -0.0228 0.0530  160 ASP B CB  
3140 C CG  . ASP B 143 ? 0.4638 0.3892 0.3976 -0.0465 -0.0276 0.0593  160 ASP B CG  
3141 O OD1 . ASP B 143 ? 0.4979 0.4167 0.4374 -0.0392 -0.0308 0.0605  160 ASP B OD1 
3142 O OD2 . ASP B 143 ? 0.4543 0.3763 0.3761 -0.0560 -0.0282 0.0628  160 ASP B OD2 
3143 N N   . ALA B 144 ? 0.4410 0.3836 0.3964 -0.0253 -0.0392 0.0618  161 ALA B N   
3144 C CA  . ALA B 144 ? 0.4495 0.3952 0.4064 -0.0222 -0.0467 0.0662  161 ALA B CA  
3145 C C   . ALA B 144 ? 0.5095 0.4449 0.4685 -0.0169 -0.0551 0.0706  161 ALA B C   
3146 O O   . ALA B 144 ? 0.4810 0.4111 0.4457 -0.0119 -0.0546 0.0684  161 ALA B O   
3147 C CB  . ALA B 144 ? 0.4114 0.3703 0.3798 -0.0156 -0.0453 0.0620  161 ALA B CB  
3148 N N   . ASP B 145 ? 0.4753 0.4076 0.4303 -0.0179 -0.0637 0.0767  162 ASP B N   
3149 C CA  . ASP B 145 ? 0.5175 0.4393 0.4758 -0.0127 -0.0736 0.0809  162 ASP B CA  
3150 C C   . ASP B 145 ? 0.5409 0.4697 0.5166 -0.0007 -0.0755 0.0757  162 ASP B C   
3151 O O   . ASP B 145 ? 0.5555 0.4772 0.5382 0.0053  -0.0797 0.0750  162 ASP B O   
3152 C CB  . ASP B 145 ? 0.5963 0.5130 0.5463 -0.0169 -0.0835 0.0887  162 ASP B CB  
3153 C CG  . ASP B 145 ? 0.7203 0.6288 0.6513 -0.0299 -0.0822 0.0943  162 ASP B CG  
3154 O OD1 . ASP B 145 ? 0.7193 0.6230 0.6445 -0.0349 -0.0756 0.0927  162 ASP B OD1 
3155 O OD2 . ASP B 145 ? 0.7487 0.6560 0.6703 -0.0356 -0.0878 0.0998  162 ASP B OD2 
3156 N N   . THR B 146 ? 0.4796 0.4229 0.4629 0.0024  -0.0726 0.0715  163 THR B N   
3157 C CA  A THR B 146 ? 0.4760 0.4292 0.4755 0.0123  -0.0722 0.0651  163 THR B CA  
3158 C CA  B THR B 146 ? 0.4754 0.4285 0.4748 0.0122  -0.0722 0.0651  163 THR B CA  
3159 C C   . THR B 146 ? 0.3939 0.3573 0.3956 0.0115  -0.0612 0.0588  163 THR B C   
3160 O O   . THR B 146 ? 0.4089 0.3781 0.4043 0.0053  -0.0564 0.0590  163 THR B O   
3161 C CB  A THR B 146 ? 0.4551 0.4173 0.4624 0.0162  -0.0787 0.0652  163 THR B CB  
3162 C CB  B THR B 146 ? 0.4557 0.4179 0.4630 0.0162  -0.0787 0.0652  163 THR B CB  
3163 O OG1 A THR B 146 ? 0.5209 0.4723 0.5288 0.0185  -0.0907 0.0703  163 THR B OG1 
3164 O OG1 B THR B 146 ? 0.4364 0.4070 0.4372 0.0101  -0.0748 0.0663  163 THR B OG1 
3165 C CG2 A THR B 146 ? 0.4665 0.4427 0.4899 0.0245  -0.0759 0.0572  163 THR B CG2 
3166 C CG2 B THR B 146 ? 0.5167 0.4672 0.5221 0.0170  -0.0912 0.0716  163 THR B CG2 
3167 N N   . PRO B 147 ? 0.4147 0.3800 0.4249 0.0172  -0.0576 0.0533  164 PRO B N   
3168 C CA  . PRO B 147 ? 0.4264 0.3995 0.4371 0.0155  -0.0482 0.0481  164 PRO B CA  
3169 C C   . PRO B 147 ? 0.3688 0.3560 0.3818 0.0140  -0.0457 0.0464  164 PRO B C   
3170 O O   . PRO B 147 ? 0.3736 0.3700 0.3956 0.0189  -0.0492 0.0448  164 PRO B O   
3171 C CB  . PRO B 147 ? 0.4174 0.3922 0.4386 0.0232  -0.0471 0.0424  164 PRO B CB  
3172 C CG  . PRO B 147 ? 0.4536 0.4162 0.4762 0.0268  -0.0543 0.0452  164 PRO B CG  
3173 C CD  . PRO B 147 ? 0.3861 0.3453 0.4048 0.0246  -0.0623 0.0515  164 PRO B CD  
3174 N N   . VAL B 148 ? 0.3218 0.3113 0.3280 0.0073  -0.0398 0.0461  165 VAL B N   
3175 C CA  . VAL B 148 ? 0.3697 0.3715 0.3773 0.0049  -0.0381 0.0453  165 VAL B CA  
3176 C C   . VAL B 148 ? 0.3446 0.3582 0.3627 0.0100  -0.0358 0.0400  165 VAL B C   
3177 O O   . VAL B 148 ? 0.3520 0.3766 0.3757 0.0115  -0.0375 0.0393  165 VAL B O   
3178 C CB  . VAL B 148 ? 0.3648 0.3660 0.3643 -0.0030 -0.0329 0.0451  165 VAL B CB  
3179 C CG1 . VAL B 148 ? 0.4365 0.4504 0.4394 -0.0049 -0.0304 0.0429  165 VAL B CG1 
3180 C CG2 . VAL B 148 ? 0.3937 0.3876 0.3829 -0.0093 -0.0355 0.0499  165 VAL B CG2 
3181 N N   . LEU B 149 ? 0.3409 0.3531 0.3619 0.0125  -0.0320 0.0360  166 LEU B N   
3182 C CA  . LEU B 149 ? 0.3595 0.3835 0.3894 0.0163  -0.0295 0.0308  166 LEU B CA  
3183 C C   . LEU B 149 ? 0.3616 0.3919 0.4019 0.0232  -0.0347 0.0291  166 LEU B C   
3184 O O   . LEU B 149 ? 0.3355 0.3795 0.3833 0.0248  -0.0336 0.0254  166 LEU B O   
3185 C CB  . LEU B 149 ? 0.3269 0.3472 0.3573 0.0178  -0.0252 0.0268  166 LEU B CB  
3186 C CG  . LEU B 149 ? 0.3228 0.3561 0.3587 0.0185  -0.0211 0.0216  166 LEU B CG  
3187 C CD1 . LEU B 149 ? 0.2837 0.3225 0.3146 0.0114  -0.0177 0.0225  166 LEU B CD1 
3188 C CD2 . LEU B 149 ? 0.3520 0.3821 0.3895 0.0212  -0.0182 0.0173  166 LEU B CD2 
3189 N N   . LYS B 150 ? 0.3216 0.3420 0.3629 0.0270  -0.0408 0.0315  167 LYS B N   
3190 C CA  . LYS B 150 ? 0.3857 0.4112 0.4383 0.0338  -0.0474 0.0297  167 LYS B CA  
3191 C C   . LYS B 150 ? 0.3795 0.4129 0.4330 0.0319  -0.0507 0.0321  167 LYS B C   
3192 O O   . LYS B 150 ? 0.3588 0.4049 0.4237 0.0360  -0.0523 0.0277  167 LYS B O   
3193 C CB  . LYS B 150 ? 0.3843 0.3955 0.4373 0.0375  -0.0550 0.0328  167 LYS B CB  
3194 C CG  . LYS B 150 ? 0.4277 0.4428 0.4947 0.0455  -0.0634 0.0300  167 LYS B CG  
3195 C CD  . LYS B 150 ? 0.5556 0.5847 0.6370 0.0517  -0.0598 0.0201  167 LYS B CD  
3196 C CE  . LYS B 150 ? 0.6483 0.6811 0.7465 0.0606  -0.0688 0.0155  167 LYS B CE  
3197 N NZ  . LYS B 150 ? 0.6611 0.7142 0.7739 0.0646  -0.0650 0.0053  167 LYS B NZ  
3198 N N   . GLN B 151 ? 0.3904 0.4174 0.4325 0.0255  -0.0516 0.0384  168 GLN B N   
3199 C CA  . GLN B 151 ? 0.3624 0.3969 0.4047 0.0233  -0.0547 0.0406  168 GLN B CA  
3200 C C   . GLN B 151 ? 0.3903 0.4412 0.4385 0.0224  -0.0489 0.0358  168 GLN B C   
3201 O O   . GLN B 151 ? 0.3872 0.4491 0.4444 0.0253  -0.0517 0.0336  168 GLN B O   
3202 C CB  . GLN B 151 ? 0.3529 0.3789 0.3811 0.0155  -0.0550 0.0471  168 GLN B CB  
3203 C CG  . GLN B 151 ? 0.3997 0.4088 0.4194 0.0142  -0.0601 0.0526  168 GLN B CG  
3204 C CD  . GLN B 151 ? 0.4234 0.4260 0.4284 0.0051  -0.0585 0.0575  168 GLN B CD  
3205 O OE1 . GLN B 151 ? 0.4022 0.4116 0.4040 0.0008  -0.0578 0.0586  168 GLN B OE1 
3206 N NE2 . GLN B 151 ? 0.4093 0.3994 0.4057 0.0017  -0.0575 0.0598  168 GLN B NE2 
3207 N N   . LEU B 152 ? 0.3208 0.3733 0.3645 0.0184  -0.0412 0.0339  169 LEU B N   
3208 C CA  . LEU B 152 ? 0.3496 0.4164 0.3971 0.0161  -0.0360 0.0302  169 LEU B CA  
3209 C C   . LEU B 152 ? 0.3792 0.4580 0.4392 0.0218  -0.0350 0.0234  169 LEU B C   
3210 O O   . LEU B 152 ? 0.3385 0.4315 0.4050 0.0213  -0.0339 0.0205  169 LEU B O   
3211 C CB  . LEU B 152 ? 0.3542 0.4175 0.3937 0.0104  -0.0296 0.0300  169 LEU B CB  
3212 C CG  . LEU B 152 ? 0.3439 0.3965 0.3724 0.0045  -0.0296 0.0347  169 LEU B CG  
3213 C CD1 . LEU B 152 ? 0.3768 0.4294 0.4010 -0.0009 -0.0241 0.0330  169 LEU B CD1 
3214 C CD2 . LEU B 152 ? 0.3678 0.4235 0.3940 0.0017  -0.0332 0.0383  169 LEU B CD2 
3215 N N   . ILE B 153 ? 0.3871 0.4611 0.4509 0.0267  -0.0350 0.0202  170 ILE B N   
3216 C CA  . ILE B 153 ? 0.3852 0.4713 0.4614 0.0319  -0.0336 0.0125  170 ILE B CA  
3217 C C   . ILE B 153 ? 0.4229 0.5177 0.5117 0.0373  -0.0400 0.0100  170 ILE B C   
3218 O O   . ILE B 153 ? 0.3840 0.4952 0.4829 0.0385  -0.0379 0.0037  170 ILE B O   
3219 C CB  . ILE B 153 ? 0.3303 0.4082 0.4082 0.0364  -0.0332 0.0096  170 ILE B CB  
3220 C CG1 . ILE B 153 ? 0.3582 0.4330 0.4269 0.0313  -0.0260 0.0093  170 ILE B CG1 
3221 C CG2 . ILE B 153 ? 0.4113 0.5008 0.5048 0.0436  -0.0346 0.0010  170 ILE B CG2 
3222 C CD1 . ILE B 153 ? 0.4091 0.4719 0.4760 0.0344  -0.0257 0.0084  170 ILE B CD1 
3223 N N   . ASP B 154 ? 0.3726 0.4566 0.4610 0.0402  -0.0482 0.0147  171 ASP B N   
3224 C CA  . ASP B 154 ? 0.3861 0.4768 0.4872 0.0456  -0.0558 0.0124  171 ASP B CA  
3225 C C   . ASP B 154 ? 0.3744 0.4783 0.4771 0.0419  -0.0546 0.0125  171 ASP B C   
3226 O O   . ASP B 154 ? 0.4008 0.5183 0.5175 0.0459  -0.0568 0.0065  171 ASP B O   
3227 C CB  . ASP B 154 ? 0.4645 0.5388 0.5623 0.0480  -0.0659 0.0189  171 ASP B CB  
3228 C CG  . ASP B 154 ? 0.4672 0.5302 0.5681 0.0533  -0.0691 0.0175  171 ASP B CG  
3229 O OD1 . ASP B 154 ? 0.5076 0.5780 0.6171 0.0571  -0.0648 0.0098  171 ASP B OD1 
3230 O OD2 . ASP B 154 ? 0.5494 0.5964 0.6439 0.0533  -0.0762 0.0241  171 ASP B OD2 
3231 N N   . VAL B 155 ? 0.3605 0.4610 0.4501 0.0344  -0.0514 0.0185  172 VAL B N   
3232 C CA  . VAL B 155 ? 0.4017 0.5153 0.4929 0.0305  -0.0494 0.0181  172 VAL B CA  
3233 C C   . VAL B 155 ? 0.3919 0.5218 0.4897 0.0291  -0.0416 0.0109  172 VAL B C   
3234 O O   . VAL B 155 ? 0.3635 0.5090 0.4716 0.0298  -0.0415 0.0063  172 VAL B O   
3235 C CB  . VAL B 155 ? 0.4099 0.5162 0.4863 0.0226  -0.0476 0.0254  172 VAL B CB  
3236 C CG1 . VAL B 155 ? 0.4330 0.5527 0.5117 0.0187  -0.0462 0.0250  172 VAL B CG1 
3237 C CG2 . VAL B 155 ? 0.4299 0.5207 0.4982 0.0226  -0.0548 0.0323  172 VAL B CG2 
3238 N N   . ALA B 156 ? 0.3544 0.4812 0.4462 0.0267  -0.0353 0.0097  173 ALA B N   
3239 C CA  . ALA B 156 ? 0.3724 0.5135 0.4675 0.0236  -0.0279 0.0038  173 ALA B CA  
3240 C C   . ALA B 156 ? 0.4584 0.6143 0.5699 0.0297  -0.0284 -0.0054 173 ALA B C   
3241 O O   . ALA B 156 ? 0.4497 0.6228 0.5677 0.0271  -0.0245 -0.0106 173 ALA B O   
3242 C CB  . ALA B 156 ? 0.3907 0.5235 0.4764 0.0207  -0.0226 0.0042  173 ALA B CB  
3243 N N   . VAL B 157 ? 0.4295 0.5793 0.5484 0.0374  -0.0332 -0.0082 174 VAL B N   
3244 C CA  . VAL B 157 ? 0.4832 0.6466 0.6202 0.0442  -0.0348 -0.0182 174 VAL B CA  
3245 C C   . VAL B 157 ? 0.5172 0.6910 0.6658 0.0466  -0.0404 -0.0201 174 VAL B C   
3246 O O   . VAL B 157 ? 0.4948 0.6876 0.6567 0.0476  -0.0379 -0.0290 174 VAL B O   
3247 C CB  . VAL B 157 ? 0.5472 0.6989 0.6896 0.0521  -0.0404 -0.0199 174 VAL B CB  
3248 C CG1 . VAL B 157 ? 0.5889 0.7541 0.7528 0.0603  -0.0442 -0.0311 174 VAL B CG1 
3249 C CG2 . VAL B 157 ? 0.4956 0.6403 0.6289 0.0501  -0.0342 -0.0201 174 VAL B CG2 
3250 N N   . ALA B 158 ? 0.4250 0.5869 0.5689 0.0473  -0.0480 -0.0122 175 ALA B N   
3251 C CA  . ALA B 158 ? 0.4857 0.6557 0.6413 0.0505  -0.0549 -0.0139 175 ALA B CA  
3252 C C   . ALA B 158 ? 0.5164 0.7023 0.6720 0.0442  -0.0493 -0.0151 175 ALA B C   
3253 O O   . ALA B 158 ? 0.6039 0.8061 0.7748 0.0468  -0.0506 -0.0224 175 ALA B O   
3254 C CB  . ALA B 158 ? 0.3691 0.5216 0.5171 0.0515  -0.0646 -0.0044 175 ALA B CB  
3255 N N   . ARG B 159 ? 0.5419 0.7235 0.6817 0.0359  -0.0437 -0.0084 176 ARG B N   
3256 C CA  . ARG B 159 ? 0.4992 0.6932 0.6375 0.0292  -0.0396 -0.0079 176 ARG B CA  
3257 C C   . ARG B 159 ? 0.4710 0.6784 0.6086 0.0234  -0.0296 -0.0131 176 ARG B C   
3258 O O   . ARG B 159 ? 0.5070 0.7258 0.6440 0.0172  -0.0260 -0.0132 176 ARG B O   
3259 C CB  . ARG B 159 ? 0.4522 0.6333 0.5746 0.0234  -0.0408 0.0024  176 ARG B CB  
3260 C CG  . ARG B 159 ? 0.4943 0.6617 0.6146 0.0275  -0.0503 0.0081  176 ARG B CG  
3261 C CD  . ARG B 159 ? 0.5425 0.7054 0.6523 0.0217  -0.0520 0.0155  176 ARG B CD  
3262 N NE  . ARG B 159 ? 0.5382 0.6905 0.6465 0.0248  -0.0615 0.0204  176 ARG B NE  
3263 C CZ  . ARG B 159 ? 0.5740 0.7327 0.6898 0.0267  -0.0678 0.0202  176 ARG B CZ  
3264 N NH1 . ARG B 159 ? 0.5308 0.7073 0.6582 0.0266  -0.0654 0.0144  176 ARG B NH1 
3265 N NH2 . ARG B 159 ? 0.6053 0.7521 0.7168 0.0284  -0.0770 0.0258  176 ARG B NH2 
3266 N N   . GLN B 160 ? 0.4682 0.5968 0.6268 0.0547  -0.0399 0.0708  177 GLN B N   
3267 C CA  . GLN B 160 ? 0.5684 0.7239 0.7526 0.0573  -0.0378 0.0682  177 GLN B CA  
3268 C C   . GLN B 160 ? 0.5207 0.6981 0.7208 0.0480  -0.0401 0.0636  177 GLN B C   
3269 O O   . GLN B 160 ? 0.4342 0.6354 0.6553 0.0515  -0.0483 0.0680  177 GLN B O   
3270 C CB  . GLN B 160 ? 0.6055 0.7763 0.8068 0.0717  -0.0448 0.0777  177 GLN B CB  
3271 C CG  . GLN B 160 ? 0.6816 0.8360 0.8727 0.0820  -0.0399 0.0806  177 GLN B CG  
3272 C CD  . GLN B 160 ? 0.8811 1.0499 1.0879 0.0968  -0.0476 0.0911  177 GLN B CD  
3273 O OE1 . GLN B 160 ? 0.7827 0.9605 0.9963 0.1000  -0.0585 0.0986  177 GLN B OE1 
3274 N NE2 . GLN B 160 ? 0.8840 1.0557 1.0971 0.1058  -0.0420 0.0915  177 GLN B NE2 
3275 N N   . GLY B 161 ? 0.4436 0.6118 0.6329 0.0359  -0.0328 0.0547  178 GLY B N   
3276 C CA  . GLY B 161 ? 0.3591 0.5469 0.5624 0.0271  -0.0337 0.0496  178 GLY B CA  
3277 C C   . GLY B 161 ? 0.3121 0.4886 0.5029 0.0146  -0.0235 0.0393  178 GLY B C   
3278 O O   . GLY B 161 ? 0.3343 0.4875 0.5058 0.0124  -0.0158 0.0362  178 GLY B O   
3279 N N   . SER B 162 ? 0.2337 0.4274 0.4368 0.0066  -0.0232 0.0341  179 SER B N   
3280 C CA  . SER B 162 ? 0.2937 0.4788 0.4864 -0.0057 -0.0142 0.0246  179 SER B CA  
3281 C C   . SER B 162 ? 0.2968 0.4593 0.4661 -0.0120 -0.0155 0.0253  179 SER B C   
3282 O O   . SER B 162 ? 0.2755 0.4358 0.4415 -0.0082 -0.0250 0.0323  179 SER B O   
3283 C CB  . SER B 162 ? 0.2395 0.4502 0.4524 -0.0116 -0.0139 0.0193  179 SER B CB  
3284 O OG  . SER B 162 ? 0.2380 0.4690 0.4712 -0.0060 -0.0121 0.0184  179 SER B OG  
3285 N N   . VAL B 163 ? 0.2708 0.4163 0.4237 -0.0216 -0.0059 0.0181  180 VAL B N   
3286 C CA  . VAL B 163 ? 0.2548 0.3776 0.3840 -0.0280 -0.0057 0.0185  180 VAL B CA  
3287 C C   . VAL B 163 ? 0.2832 0.4057 0.4087 -0.0409 0.0025  0.0094  180 VAL B C   
3288 O O   . VAL B 163 ? 0.3022 0.4231 0.4281 -0.0459 0.0124  0.0024  180 VAL B O   
3289 C CB  . VAL B 163 ? 0.3111 0.4037 0.4162 -0.0248 -0.0021 0.0216  180 VAL B CB  
3290 C CG1 . VAL B 163 ? 0.3145 0.3838 0.3946 -0.0316 -0.0015 0.0220  180 VAL B CG1 
3291 C CG2 . VAL B 163 ? 0.3865 0.4796 0.4952 -0.0111 -0.0106 0.0313  180 VAL B CG2 
3292 N N   . LEU B 164 ? 0.2656 0.3884 0.3864 -0.0463 -0.0016 0.0095  181 LEU B N   
3293 C CA  . LEU B 164 ? 0.2266 0.3462 0.3407 -0.0583 0.0059  0.0019  181 LEU B CA  
3294 C C   . LEU B 164 ? 0.3023 0.3916 0.3871 -0.0628 0.0094  0.0027  181 LEU B C   
3295 O O   . LEU B 164 ? 0.3138 0.3923 0.3867 -0.0588 0.0016  0.0093  181 LEU B O   
3296 C CB  . LEU B 164 ? 0.2870 0.4263 0.4143 -0.0613 -0.0004 0.0011  181 LEU B CB  
3297 C CG  . LEU B 164 ? 0.3152 0.4840 0.4705 -0.0550 -0.0079 0.0035  181 LEU B CG  
3298 C CD1 . LEU B 164 ? 0.3058 0.4893 0.4700 -0.0599 -0.0126 0.0018  181 LEU B CD1 
3299 C CD2 . LEU B 164 ? 0.2785 0.4631 0.4512 -0.0542 -0.0013 -0.0014 181 LEU B CD2 
3300 N N   . GLY B 165 ? 0.2677 0.3438 0.3411 -0.0714 0.0210  -0.0039 182 GLY B N   
3301 C CA  . GLY B 165 ? 0.3412 0.3905 0.3877 -0.0773 0.0252  -0.0036 182 GLY B CA  
3302 C C   . GLY B 165 ? 0.3750 0.4296 0.4194 -0.0834 0.0224  -0.0051 182 GLY B C   
3303 O O   . GLY B 165 ? 0.3622 0.4362 0.4221 -0.0889 0.0248  -0.0109 182 GLY B O   
3304 N N   . VAL B 166 ? 0.3538 0.3905 0.3782 -0.0821 0.0173  0.0003  183 VAL B N   
3305 C CA  . VAL B 166 ? 0.3109 0.3500 0.3305 -0.0873 0.0141  -0.0009 183 VAL B CA  
3306 C C   . VAL B 166 ? 0.4204 0.4301 0.4097 -0.0921 0.0192  0.0000  183 VAL B C   
3307 O O   . VAL B 166 ? 0.4118 0.3995 0.3839 -0.0890 0.0214  0.0038  183 VAL B O   
3308 C CB  . VAL B 166 ? 0.3508 0.4022 0.3791 -0.0800 -0.0004 0.0054  183 VAL B CB  
3309 C CG1 . VAL B 166 ? 0.3646 0.4467 0.4238 -0.0765 -0.0044 0.0041  183 VAL B CG1 
3310 C CG2 . VAL B 166 ? 0.3621 0.3976 0.3774 -0.0707 -0.0080 0.0142  183 VAL B CG2 
3311 N N   . GLN B 167 ? 0.4413 0.4506 0.4239 -0.0992 0.0208  -0.0034 184 GLN B N   
3312 C CA  . GLN B 167 ? 0.4391 0.4217 0.3925 -0.1027 0.0235  -0.0015 184 GLN B CA  
3313 C C   . GLN B 167 ? 0.4666 0.4551 0.4176 -0.1054 0.0177  -0.0021 184 GLN B C   
3314 O O   . GLN B 167 ? 0.4187 0.4299 0.3893 -0.1082 0.0166  -0.0066 184 GLN B O   
3315 C CB  . GLN B 167 ? 0.5139 0.4806 0.4541 -0.1120 0.0388  -0.0070 184 GLN B CB  
3316 C CG  . GLN B 167 ? 0.5690 0.5487 0.5181 -0.1222 0.0473  -0.0155 184 GLN B CG  
3317 C CD  . GLN B 167 ? 0.7425 0.7052 0.6776 -0.1317 0.0626  -0.0203 184 GLN B CD  
3318 O OE1 . GLN B 167 ? 0.8283 0.7725 0.7516 -0.1310 0.0677  -0.0185 184 GLN B OE1 
3319 N NE2 . GLN B 167 ? 0.6620 0.6320 0.5998 -0.1406 0.0700  -0.0267 184 GLN B NE2 
3320 N N   . GLU B 168 ? 0.4867 0.4534 0.4124 -0.1043 0.0142  0.0024  185 GLU B N   
3321 C CA  . GLU B 168 ? 0.4651 0.4322 0.3831 -0.1073 0.0097  0.0015  185 GLU B CA  
3322 C C   . GLU B 168 ? 0.5286 0.4953 0.4433 -0.1180 0.0224  -0.0064 185 GLU B C   
3323 O O   . GLU B 168 ? 0.5215 0.4728 0.4237 -0.1233 0.0344  -0.0087 185 GLU B O   
3324 C CB  . GLU B 168 ? 0.5768 0.5184 0.4660 -0.1036 0.0037  0.0081  185 GLU B CB  
3325 C CG  . GLU B 168 ? 0.5964 0.5399 0.4886 -0.0929 -0.0110 0.0162  185 GLU B CG  
3326 C CD  . GLU B 168 ? 0.6497 0.6146 0.5587 -0.0904 -0.0237 0.0167  185 GLU B CD  
3327 O OE1 . GLU B 168 ? 0.6151 0.5831 0.5213 -0.0966 -0.0223 0.0121  185 GLU B OE1 
3328 O OE2 . GLU B 168 ? 0.6681 0.6468 0.5933 -0.0826 -0.0347 0.0215  185 GLU B OE2 
3329 N N   . VAL B 169 ? 0.4899 0.4741 0.4166 -0.1211 0.0198  -0.0104 186 VAL B N   
3330 C CA  . VAL B 169 ? 0.4920 0.4767 0.4153 -0.1306 0.0309  -0.0175 186 VAL B CA  
3331 C C   . VAL B 169 ? 0.5269 0.5079 0.4383 -0.1313 0.0246  -0.0171 186 VAL B C   
3332 O O   . VAL B 169 ? 0.4784 0.4643 0.3926 -0.1250 0.0110  -0.0126 186 VAL B O   
3333 C CB  . VAL B 169 ? 0.5229 0.5349 0.4751 -0.1345 0.0362  -0.0243 186 VAL B CB  
3334 C CG1 . VAL B 169 ? 0.4548 0.4687 0.4167 -0.1339 0.0424  -0.0250 186 VAL B CG1 
3335 C CG2 . VAL B 169 ? 0.5053 0.5421 0.4803 -0.1297 0.0244  -0.0236 186 VAL B CG2 
3336 N N   . PRO B 170 ? 0.5367 0.5083 0.4340 -0.1388 0.0342  -0.0215 187 PRO B N   
3337 C CA  . PRO B 170 ? 0.6063 0.5746 0.4922 -0.1396 0.0289  -0.0219 187 PRO B CA  
3338 C C   . PRO B 170 ? 0.5281 0.5234 0.4395 -0.1381 0.0206  -0.0244 187 PRO B C   
3339 O O   . PRO B 170 ? 0.5842 0.6007 0.5194 -0.1406 0.0254  -0.0290 187 PRO B O   
3340 C CB  . PRO B 170 ? 0.6381 0.5954 0.5093 -0.1484 0.0435  -0.0272 187 PRO B CB  
3341 C CG  . PRO B 170 ? 0.6969 0.6592 0.5794 -0.1531 0.0559  -0.0308 187 PRO B CG  
3342 C CD  . PRO B 170 ? 0.6309 0.5936 0.5213 -0.1468 0.0505  -0.0261 187 PRO B CD  
3343 N N   . ARG B 171 ? 0.5067 0.5009 0.4124 -0.1341 0.0082  -0.0214 188 ARG B N   
3344 C CA  . ARG B 171 ? 0.5395 0.5584 0.4693 -0.1324 -0.0005 -0.0231 188 ARG B CA  
3345 C C   . ARG B 171 ? 0.5916 0.6248 0.5333 -0.1394 0.0092  -0.0310 188 ARG B C   
3346 O O   . ARG B 171 ? 0.5233 0.5811 0.4916 -0.1390 0.0071  -0.0336 188 ARG B O   
3347 C CB  . ARG B 171 ? 0.6059 0.6185 0.5246 -0.1285 -0.0146 -0.0194 188 ARG B CB  
3348 C CG  . ARG B 171 ? 0.4975 0.5346 0.4407 -0.1270 -0.0240 -0.0210 188 ARG B CG  
3349 C CD  . ARG B 171 ? 0.4553 0.4874 0.3910 -0.1220 -0.0402 -0.0161 188 ARG B CD  
3350 N NE  . ARG B 171 ? 0.4692 0.5034 0.4119 -0.1146 -0.0500 -0.0089 188 ARG B NE  
3351 C CZ  . ARG B 171 ? 0.5338 0.5909 0.5044 -0.1104 -0.0578 -0.0068 188 ARG B CZ  
3352 N NH1 . ARG B 171 ? 0.4320 0.5115 0.4261 -0.1128 -0.0573 -0.0111 188 ARG B NH1 
3353 N NH2 . ARG B 171 ? 0.5408 0.5981 0.5157 -0.1034 -0.0662 0.0001  188 ARG B NH2 
3354 N N   . GLU B 172 ? 0.5752 0.5937 0.4979 -0.1456 0.0206  -0.0347 189 GLU B N   
3355 C CA  . GLU B 172 ? 0.6167 0.6478 0.5493 -0.1522 0.0307  -0.0420 189 GLU B CA  
3356 C C   . GLU B 172 ? 0.5533 0.6039 0.5107 -0.1547 0.0389  -0.0458 189 GLU B C   
3357 O O   . GLU B 172 ? 0.6571 0.7253 0.6306 -0.1586 0.0443  -0.0515 189 GLU B O   
3358 C CB  . GLU B 172 ? 0.6695 0.6792 0.5755 -0.1582 0.0425  -0.0445 189 GLU B CB  
3359 C CG  . GLU B 172 ? 0.9466 0.9361 0.8257 -0.1563 0.0357  -0.0417 189 GLU B CG  
3360 C CD  . GLU B 172 ? 0.8832 0.8518 0.7424 -0.1508 0.0277  -0.0342 189 GLU B CD  
3361 O OE1 . GLU B 172 ? 0.8089 0.7681 0.6635 -0.1509 0.0335  -0.0318 189 GLU B OE1 
3362 O OE2 . GLU B 172 ? 0.8710 0.8328 0.7196 -0.1463 0.0152  -0.0307 189 GLU B OE2 
3363 N N   . ASP B 173 ? 0.5917 0.6391 0.5520 -0.1525 0.0401  -0.0429 190 ASP B N   
3364 C CA  . ASP B 173 ? 0.5523 0.6155 0.5333 -0.1551 0.0483  -0.0467 190 ASP B CA  
3365 C C   . ASP B 173 ? 0.5262 0.6125 0.5345 -0.1492 0.0394  -0.0451 190 ASP B C   
3366 O O   . ASP B 173 ? 0.4835 0.5836 0.5095 -0.1505 0.0452  -0.0481 190 ASP B O   
3367 C CB  . ASP B 173 ? 0.5944 0.6391 0.5615 -0.1571 0.0569  -0.0454 190 ASP B CB  
3368 C CG  . ASP B 173 ? 0.7399 0.7671 0.6864 -0.1651 0.0702  -0.0487 190 ASP B CG  
3369 O OD1 . ASP B 173 ? 0.7348 0.7628 0.6758 -0.1686 0.0728  -0.0518 190 ASP B OD1 
3370 O OD2 . ASP B 173 ? 0.7954 0.8070 0.7305 -0.1676 0.0782  -0.0479 190 ASP B OD2 
3371 N N   . THR B 174 ? 0.5276 0.6186 0.5402 -0.1427 0.0255  -0.0404 191 THR B N   
3372 C CA  . THR B 174 ? 0.4330 0.5435 0.4698 -0.1364 0.0174  -0.0376 191 THR B CA  
3373 C C   . THR B 174 ? 0.4505 0.5887 0.5152 -0.1384 0.0207  -0.0429 191 THR B C   
3374 O O   . THR B 174 ? 0.4094 0.5639 0.4946 -0.1342 0.0176  -0.0416 191 THR B O   
3375 C CB  . THR B 174 ? 0.4151 0.5263 0.4521 -0.1296 0.0018  -0.0315 191 THR B CB  
3376 O OG1 . THR B 174 ? 0.4286 0.5439 0.4645 -0.1321 -0.0017 -0.0340 191 THR B OG1 
3377 C CG2 . THR B 174 ? 0.4386 0.5248 0.4510 -0.1261 -0.0026 -0.0254 191 THR B CG2 
3378 N N   . ARG B 175 ? 0.5027 0.6468 0.5687 -0.1441 0.0266  -0.0486 192 ARG B N   
3379 C CA  . ARG B 175 ? 0.5037 0.6587 0.5859 -0.1325 0.0278  -0.0492 192 ARG B CA  
3380 C C   . ARG B 175 ? 0.5505 0.7034 0.6357 -0.1290 0.0358  -0.0506 192 ARG B C   
3381 O O   . ARG B 175 ? 0.5978 0.7559 0.6937 -0.1185 0.0347  -0.0496 192 ARG B O   
3382 C CB  . ARG B 175 ? 0.6225 0.7762 0.6998 -0.1318 0.0306  -0.0525 192 ARG B CB  
3383 C CG  . ARG B 175 ? 0.7202 0.8808 0.8113 -0.1185 0.0284  -0.0507 192 ARG B CG  
3384 C CD  . ARG B 175 ? 0.8767 1.0371 0.9645 -0.1172 0.0296  -0.0531 192 ARG B CD  
3385 N NE  . ARG B 175 ? 0.8708 1.0344 0.9606 -0.1174 0.0209  -0.0510 192 ARG B NE  
3386 C CZ  . ARG B 175 ? 0.7440 0.9038 0.8216 -0.1266 0.0206  -0.0541 192 ARG B CZ  
3387 N NH1 . ARG B 175 ? 0.9655 1.1167 1.0268 -0.1373 0.0297  -0.0589 192 ARG B NH1 
3388 N NH2 . ARG B 175 ? 0.7738 0.9365 0.8544 -0.1252 0.0108  -0.0519 192 ARG B NH2 
3389 N N   . LYS B 176 ? 0.4653 0.6082 0.5395 -0.1380 0.0435  -0.0525 193 LYS B N   
3390 C CA  . LYS B 176 ? 0.4585 0.5990 0.5354 -0.1348 0.0501  -0.0541 193 LYS B CA  
3391 C C   . LYS B 176 ? 0.4812 0.6289 0.5711 -0.1294 0.0450  -0.0504 193 LYS B C   
3392 O O   . LYS B 176 ? 0.5059 0.6541 0.6009 -0.1245 0.0482  -0.0512 193 LYS B O   
3393 C CB  . LYS B 176 ? 0.5041 0.6279 0.5629 -0.1461 0.0615  -0.0572 193 LYS B CB  
3394 C CG  . LYS B 176 ? 0.6223 0.7377 0.6679 -0.1504 0.0690  -0.0613 193 LYS B CG  
3395 C CD  . LYS B 176 ? 0.7952 0.8904 0.8208 -0.1611 0.0805  -0.0629 193 LYS B CD  
3396 C CE  . LYS B 176 ? 0.8568 0.9423 0.8669 -0.1664 0.0876  -0.0662 193 LYS B CE  
3397 N NZ  . LYS B 176 ? 0.9177 0.9802 0.9053 -0.1761 0.0988  -0.0662 193 LYS B NZ  
3398 N N   . TYR B 177 ? 0.4186 0.5725 0.5141 -0.1300 0.0363  -0.0463 194 TYR B N   
3399 C CA  . TYR B 177 ? 0.3539 0.5118 0.4571 -0.1291 0.0336  -0.0434 194 TYR B CA  
3400 C C   . TYR B 177 ? 0.3664 0.5390 0.4871 -0.1183 0.0214  -0.0380 194 TYR B C   
3401 O O   . TYR B 177 ? 0.3628 0.5398 0.4870 -0.1141 0.0143  -0.0360 194 TYR B O   
3402 C CB  . TYR B 177 ? 0.4313 0.5657 0.5114 -0.1303 0.0319  -0.0388 194 TYR B CB  
3403 C CG  . TYR B 177 ? 0.4962 0.6077 0.5531 -0.1377 0.0432  -0.0417 194 TYR B CG  
3404 C CD1 . TYR B 177 ? 0.5201 0.6265 0.5762 -0.1415 0.0537  -0.0451 194 TYR B CD1 
3405 C CD2 . TYR B 177 ? 0.4380 0.5327 0.4735 -0.1408 0.0433  -0.0409 194 TYR B CD2 
3406 C CE1 . TYR B 177 ? 0.4691 0.5543 0.5042 -0.1487 0.0643  -0.0474 194 TYR B CE1 
3407 C CE2 . TYR B 177 ? 0.5668 0.6404 0.5807 -0.1475 0.0542  -0.0431 194 TYR B CE2 
3408 C CZ  . TYR B 177 ? 0.5196 0.5889 0.5340 -0.1515 0.0646  -0.0462 194 TYR B CZ  
3409 O OH  . TYR B 177 ? 0.6500 0.6986 0.6439 -0.1585 0.0756  -0.0480 194 TYR B OH  
3410 N N   . GLY B 178 ? 0.5167 0.5579 0.4424 -0.0694 -0.0247 0.0189  195 GLY B N   
3411 C CA  . GLY B 178 ? 0.4807 0.5147 0.4248 -0.0723 -0.0270 0.0185  195 GLY B CA  
3412 C C   . GLY B 178 ? 0.4363 0.4633 0.3779 -0.0866 -0.0428 0.0128  195 GLY B C   
3413 O O   . GLY B 178 ? 0.4059 0.4407 0.3405 -0.0914 -0.0545 0.0134  195 GLY B O   
3414 N N   . ILE B 179 ? 0.4166 0.4296 0.3636 -0.0935 -0.0424 0.0073  196 ILE B N   
3415 C CA  . ILE B 179 ? 0.3905 0.3985 0.3336 -0.1075 -0.0563 0.0009  196 ILE B CA  
3416 C C   . ILE B 179 ? 0.3738 0.3833 0.3389 -0.1108 -0.0620 0.0014  196 ILE B C   
3417 O O   . ILE B 179 ? 0.3816 0.3847 0.3599 -0.1068 -0.0513 0.0015  196 ILE B O   
3418 C CB  . ILE B 179 ? 0.3846 0.3766 0.3121 -0.1151 -0.0511 -0.0086 196 ILE B CB  
3419 C CG1 . ILE B 179 ? 0.4585 0.4501 0.3640 -0.1114 -0.0458 -0.0087 196 ILE B CG1 
3420 C CG2 . ILE B 179 ? 0.4440 0.4342 0.3687 -0.1299 -0.0654 -0.0156 196 ILE B CG2 
3421 C CD1 . ILE B 179 ? 0.4449 0.4479 0.3383 -0.1156 -0.0598 -0.0066 196 ILE B CD1 
3422 N N   . VAL B 180 ? 0.4129 0.4308 0.3822 -0.1177 -0.0781 0.0023  197 VAL B N   
3423 C CA  . VAL B 180 ? 0.3968 0.4191 0.3874 -0.1207 -0.0849 0.0035  197 VAL B CA  
3424 C C   . VAL B 180 ? 0.4146 0.4312 0.4037 -0.1342 -0.0922 -0.0051 197 VAL B C   
3425 O O   . VAL B 180 ? 0.4208 0.4370 0.3931 -0.1422 -0.1000 -0.0094 197 VAL B O   
3426 C CB  . VAL B 180 ? 0.3972 0.4340 0.3961 -0.1185 -0.0971 0.0109  197 VAL B CB  
3427 C CG1 . VAL B 180 ? 0.4566 0.5009 0.4589 -0.1063 -0.0890 0.0178  197 VAL B CG1 
3428 C CG2 . VAL B 180 ? 0.5343 0.5746 0.5174 -0.1254 -0.1101 0.0106  197 VAL B CG2 
3429 N N   . ALA B 181 ? 0.4139 0.4271 0.4204 -0.1370 -0.0888 -0.0079 198 ALA B N   
3430 C CA  . ALA B 181 ? 0.4102 0.4240 0.4213 -0.1504 -0.0977 -0.0156 198 ALA B CA  
3431 C C   . ALA B 181 ? 0.4825 0.5117 0.5123 -0.1502 -0.1106 -0.0094 198 ALA B C   
3432 O O   . ALA B 181 ? 0.3950 0.4272 0.4430 -0.1422 -0.1058 -0.0035 198 ALA B O   
3433 C CB  . ALA B 181 ? 0.4457 0.4455 0.4646 -0.1547 -0.0843 -0.0236 198 ALA B CB  
3434 N N   . SER B 182 ? 0.3870 0.4265 0.4122 -0.1565 -0.1252 -0.0100 199 SER B N   
3435 C CA  . SER B 182 ? 0.5153 0.5681 0.5546 -0.1478 -0.1318 -0.0025 199 SER B CA  
3436 C C   . SER B 182 ? 0.5187 0.5802 0.5572 -0.1511 -0.1392 -0.0067 199 SER B C   
3437 O O   . SER B 182 ? 0.5010 0.5604 0.5250 -0.1580 -0.1405 -0.0140 199 SER B O   
3438 C CB  . SER B 182 ? 0.4266 0.4833 0.4582 -0.1376 -0.1340 0.0067  199 SER B CB  
3439 O OG  . SER B 182 ? 0.5386 0.5924 0.5480 -0.1391 -0.1358 0.0051  199 SER B OG  
3440 N N   . GLN B 183 ? 0.5723 0.6450 0.6260 -0.1456 -0.1440 -0.0014 200 GLN B N   
3441 C CA  . GLN B 183 ? 0.6674 0.7521 0.7222 -0.1475 -0.1520 -0.0031 200 GLN B CA  
3442 C C   . GLN B 183 ? 0.6466 0.7387 0.6998 -0.1381 -0.1578 0.0075  200 GLN B C   
3443 O O   . GLN B 183 ? 0.5340 0.6258 0.5973 -0.1302 -0.1559 0.0152  200 GLN B O   
3444 C CB  . GLN B 183 ? 0.6621 0.7541 0.7377 -0.1514 -0.1519 -0.0075 200 GLN B CB  
3445 C CG  . GLN B 183 ? 0.7225 0.8061 0.8010 -0.1628 -0.1452 -0.0193 200 GLN B CG  
3446 C CD  . GLN B 183 ? 0.7788 0.8602 0.8397 -0.1720 -0.1468 -0.0293 200 GLN B CD  
3447 O OE1 . GLN B 183 ? 0.7411 0.8332 0.7931 -0.1711 -0.1548 -0.0285 200 GLN B OE1 
3448 N NE2 . GLN B 183 ? 0.8004 0.8673 0.8563 -0.1811 -0.1383 -0.0386 200 GLN B NE2 
3449 N N   . PRO B 184 ? 0.6524 0.7509 0.6938 -0.1390 -0.1644 0.0082  201 PRO B N   
3450 C CA  . PRO B 184 ? 0.6161 0.7189 0.6554 -0.1310 -0.1690 0.0189  201 PRO B CA  
3451 C C   . PRO B 184 ? 0.6135 0.7255 0.6719 -0.1257 -0.1720 0.0251  201 PRO B C   
3452 O O   . PRO B 184 ? 0.6230 0.7446 0.6937 -0.1292 -0.1746 0.0209  201 PRO B O   
3453 C CB  . PRO B 184 ? 0.6253 0.7350 0.6500 -0.1348 -0.1756 0.0173  201 PRO B CB  
3454 C CG  . PRO B 184 ? 0.6727 0.7757 0.6854 -0.1432 -0.1720 0.0064  201 PRO B CG  
3455 C CD  . PRO B 184 ? 0.6586 0.7590 0.6862 -0.1475 -0.1671 -0.0005 201 PRO B CD  
3456 N N   . VAL B 185 ? 0.6028 0.7115 0.6637 -0.1175 -0.1710 0.0347  202 VAL B N   
3457 C CA  . VAL B 185 ? 0.5533 0.6701 0.6289 -0.1117 -0.1746 0.0423  202 VAL B CA  
3458 C C   . VAL B 185 ? 0.5586 0.6781 0.6265 -0.1078 -0.1802 0.0514  202 VAL B C   
3459 O O   . VAL B 185 ? 0.5978 0.7268 0.6761 -0.1043 -0.1853 0.0576  202 VAL B O   
3460 C CB  . VAL B 185 ? 0.5173 0.6282 0.6067 -0.1055 -0.1681 0.0459  202 VAL B CB  
3461 C CG1 . VAL B 185 ? 0.5609 0.6715 0.6613 -0.1090 -0.1632 0.0385  202 VAL B CG1 
3462 C CG2 . VAL B 185 ? 0.5745 0.6742 0.6538 -0.1020 -0.1627 0.0489  202 VAL B CG2 
3463 N N   . ASP B 186 ? 0.5749 0.6863 0.6259 -0.1081 -0.1790 0.0530  203 ASP B N   
3464 C CA  . ASP B 186 ? 0.5807 0.6943 0.6219 -0.1061 -0.1843 0.0610  203 ASP B CA  
3465 C C   . ASP B 186 ? 0.5308 0.6364 0.5510 -0.1099 -0.1820 0.0574  203 ASP B C   
3466 O O   . ASP B 186 ? 0.5795 0.6802 0.5936 -0.1143 -0.1775 0.0485  203 ASP B O   
3467 C CB  . ASP B 186 ? 0.5125 0.6224 0.5624 -0.0991 -0.1836 0.0716  203 ASP B CB  
3468 C CG  . ASP B 186 ? 0.5535 0.6501 0.5997 -0.0972 -0.1757 0.0716  203 ASP B CG  
3469 O OD1 . ASP B 186 ? 0.5075 0.5972 0.5387 -0.1005 -0.1719 0.0667  203 ASP B OD1 
3470 O OD2 . ASP B 186 ? 0.5983 0.6927 0.6571 -0.0923 -0.1732 0.0766  203 ASP B OD2 
3471 N N   . ALA B 187 ? 0.5717 0.6760 0.5810 -0.1082 -0.1848 0.0647  204 ALA B N   
3472 C CA  . ALA B 187 ? 0.6049 0.7045 0.5938 -0.1121 -0.1837 0.0616  204 ALA B CA  
3473 C C   . ALA B 187 ? 0.6151 0.7015 0.5965 -0.1126 -0.1748 0.0572  204 ALA B C   
3474 O O   . ALA B 187 ? 0.5272 0.6096 0.4940 -0.1167 -0.1722 0.0508  204 ALA B O   
3475 C CB  . ALA B 187 ? 0.6031 0.7043 0.5833 -0.1097 -0.1884 0.0717  204 ALA B CB  
3476 N N   . ARG B 188 ? 0.5723 0.6530 0.5635 -0.1084 -0.1700 0.0603  205 ARG B N   
3477 C CA  . ARG B 188 ? 0.5737 0.6453 0.5584 -0.1083 -0.1617 0.0565  205 ARG B CA  
3478 C C   . ARG B 188 ? 0.5093 0.5803 0.5069 -0.1069 -0.1564 0.0517  205 ARG B C   
3479 O O   . ARG B 188 ? 0.5059 0.5719 0.4975 -0.1073 -0.1498 0.0475  205 ARG B O   
3480 C CB  . ARG B 188 ? 0.5397 0.6059 0.5214 -0.1054 -0.1593 0.0635  205 ARG B CB  
3481 C CG  . ARG B 188 ? 0.6112 0.6749 0.5758 -0.1076 -0.1620 0.0677  205 ARG B CG  
3482 C CD  . ARG B 188 ? 0.7360 0.7932 0.6971 -0.1064 -0.1584 0.0731  205 ARG B CD  
3483 N NE  . ARG B 188 ? 0.8561 0.9103 0.8009 -0.1089 -0.1605 0.0774  205 ARG B NE  
3484 C CZ  . ARG B 188 ? 0.9078 0.9579 0.8359 -0.1118 -0.1559 0.0726  205 ARG B CZ  
3485 N NH1 . ARG B 188 ? 0.7492 0.7976 0.6741 -0.1124 -0.1490 0.0638  205 ARG B NH1 
3486 N NH2 . ARG B 188 ? 0.9814 1.0294 0.8958 -0.1138 -0.1581 0.0774  205 ARG B NH2 
3487 N N   . THR B 189 ? 0.4512 0.5280 0.4662 -0.1051 -0.1590 0.0527  206 THR B N   
3488 C CA  . THR B 189 ? 0.4295 0.5063 0.4590 -0.1031 -0.1538 0.0497  206 THR B CA  
3489 C C   . THR B 189 ? 0.4924 0.5731 0.5271 -0.1078 -0.1554 0.0427  206 THR B C   
3490 O O   . THR B 189 ? 0.5107 0.5981 0.5459 -0.1109 -0.1617 0.0418  206 THR B O   
3491 C CB  . THR B 189 ? 0.4354 0.5153 0.4824 -0.0972 -0.1542 0.0563  206 THR B CB  
3492 O OG1 . THR B 189 ? 0.4584 0.5340 0.5004 -0.0944 -0.1525 0.0619  206 THR B OG1 
3493 C CG2 . THR B 189 ? 0.4122 0.4932 0.4747 -0.0946 -0.1484 0.0534  206 THR B CG2 
3494 N N   . GLU B 190 ? 0.4633 0.5408 0.5020 -0.1091 -0.1495 0.0376  207 GLU B N   
3495 C CA  . GLU B 190 ? 0.5261 0.6051 0.5706 -0.1151 -0.1496 0.0303  207 GLU B CA  
3496 C C   . GLU B 190 ? 0.5141 0.5933 0.5766 -0.1124 -0.1441 0.0305  207 GLU B C   
3497 O O   . GLU B 190 ? 0.4211 0.4985 0.4863 -0.1067 -0.1392 0.0345  207 GLU B O   
3498 C CB  . GLU B 190 ? 0.5923 0.6647 0.6201 -0.1219 -0.1472 0.0231  207 GLU B CB  
3499 C CG  . GLU B 190 ? 0.5838 0.6555 0.5923 -0.1236 -0.1509 0.0234  207 GLU B CG  
3500 C CD  . GLU B 190 ? 0.6862 0.7573 0.6840 -0.1324 -0.1527 0.0145  207 GLU B CD  
3501 O OE1 . GLU B 190 ? 0.6224 0.6922 0.6276 -0.1383 -0.1505 0.0072  207 GLU B OE1 
3502 O OE2 . GLU B 190 ? 0.7473 0.8191 0.7297 -0.1338 -0.1558 0.0144  207 GLU B OE2 
3503 N N   . ARG B 191 ? 0.4421 0.5244 0.5171 -0.1167 -0.1446 0.0259  208 ARG B N   
3504 C CA  . ARG B 191 ? 0.4922 0.5741 0.5848 -0.1152 -0.1387 0.0258  208 ARG B CA  
3505 C C   . ARG B 191 ? 0.4183 0.4921 0.5062 -0.1223 -0.1332 0.0198  208 ARG B C   
3506 O O   . ARG B 191 ? 0.4544 0.5248 0.5350 -0.1313 -0.1344 0.0121  208 ARG B O   
3507 C CB  . ARG B 191 ? 0.5614 0.6505 0.6719 -0.1167 -0.1408 0.0242  208 ARG B CB  
3508 C CG  . ARG B 191 ? 0.4578 0.5465 0.5877 -0.1139 -0.1339 0.0256  208 ARG B CG  
3509 C CD  . ARG B 191 ? 0.6912 0.7869 0.8385 -0.1162 -0.1350 0.0233  208 ARG B CD  
3510 N NE  . ARG B 191 ? 0.8468 0.9517 0.9933 -0.1135 -0.1429 0.0263  208 ARG B NE  
3511 C CZ  . ARG B 191 ? 0.8194 0.9283 0.9728 -0.1047 -0.1440 0.0340  208 ARG B CZ  
3512 N NH1 . ARG B 191 ? 0.7920 0.8985 0.9557 -0.0977 -0.1376 0.0382  208 ARG B NH1 
3513 N NH2 . ARG B 191 ? 0.7329 0.8485 0.8830 -0.1031 -0.1512 0.0375  208 ARG B NH2 
3514 N N   . VAL B 192 ? 0.3379 0.4093 0.4300 -0.1185 -0.1269 0.0232  209 VAL B N   
3515 C CA  . VAL B 192 ? 0.4048 0.4670 0.4916 -0.1230 -0.1187 0.0192  209 VAL B CA  
3516 C C   . VAL B 192 ? 0.4198 0.4773 0.5235 -0.1249 -0.1107 0.0155  209 VAL B C   
3517 O O   . VAL B 192 ? 0.3673 0.4310 0.4910 -0.1199 -0.1091 0.0200  209 VAL B O   
3518 C CB  . VAL B 192 ? 0.3801 0.4418 0.4615 -0.1115 -0.1082 0.0241  209 VAL B CB  
3519 C CG1 . VAL B 192 ? 0.3765 0.4264 0.4484 -0.1091 -0.0933 0.0200  209 VAL B CG1 
3520 C CG2 . VAL B 192 ? 0.3899 0.4559 0.4554 -0.1107 -0.1151 0.0271  209 VAL B CG2 
3521 N N   . THR B 193 ? 0.3710 0.4166 0.4663 -0.1321 -0.1041 0.0070  210 THR B N   
3522 C CA  . THR B 193 ? 0.4049 0.4422 0.5138 -0.1349 -0.0936 0.0023  210 THR B CA  
3523 C C   . THR B 193 ? 0.4075 0.4294 0.5090 -0.1282 -0.0746 0.0013  210 THR B C   
3524 O O   . THR B 193 ? 0.3960 0.4111 0.5111 -0.1253 -0.0625 0.0014  210 THR B O   
3525 C CB  . THR B 193 ? 0.4780 0.5136 0.5857 -0.1506 -0.1000 -0.0083 210 THR B CB  
3526 O OG1 . THR B 193 ? 0.4575 0.4839 0.5416 -0.1567 -0.0988 -0.0154 210 THR B OG1 
3527 C CG2 . THR B 193 ? 0.4270 0.4805 0.5421 -0.1548 -0.1174 -0.0066 210 THR B CG2 
3528 N N   . HIS B 194 ? 0.3967 0.4127 0.4767 -0.1258 -0.0712 0.0004  211 HIS B N   
3529 C CA  . HIS B 194 ? 0.3685 0.3708 0.4402 -0.1185 -0.0529 0.0002  211 HIS B CA  
3530 C C   . HIS B 194 ? 0.4097 0.4163 0.4627 -0.1113 -0.0534 0.0043  211 HIS B C   
3531 O O   . HIS B 194 ? 0.3725 0.3871 0.4152 -0.1158 -0.0671 0.0041  211 HIS B O   
3532 C CB  . HIS B 194 ? 0.4964 0.4804 0.5591 -0.1283 -0.0443 -0.0108 211 HIS B CB  
3533 C CG  . HIS B 194 ? 0.5275 0.5073 0.6063 -0.1393 -0.0447 -0.0178 211 HIS B CG  
3534 N ND1 . HIS B 194 ? 0.5021 0.4909 0.5828 -0.1532 -0.0606 -0.0245 211 HIS B ND1 
3535 C CD2 . HIS B 194 ? 0.5445 0.5130 0.6380 -0.1389 -0.0304 -0.0194 211 HIS B CD2 
3536 C CE1 . HIS B 194 ? 0.5084 0.4928 0.6045 -0.1616 -0.0566 -0.0307 211 HIS B CE1 
3537 N NE2 . HIS B 194 ? 0.5015 0.4724 0.6058 -0.1534 -0.0380 -0.0279 211 HIS B NE2 
3538 N N   . ILE B 195 ? 0.3348 0.3367 0.3832 -0.1000 -0.0380 0.0083  212 ILE B N   
3539 C CA  . ILE B 195 ? 0.3374 0.3437 0.3675 -0.0934 -0.0363 0.0112  212 ILE B CA  
3540 C C   . ILE B 195 ? 0.3838 0.3761 0.4040 -0.0873 -0.0178 0.0099  212 ILE B C   
3541 O O   . ILE B 195 ? 0.3745 0.3585 0.4063 -0.0819 -0.0042 0.0117  212 ILE B O   
3542 C CB  . ILE B 195 ? 0.3363 0.3609 0.3739 -0.0827 -0.0385 0.0206  212 ILE B CB  
3543 C CG1 . ILE B 195 ? 0.3504 0.3818 0.3693 -0.0779 -0.0378 0.0225  212 ILE B CG1 
3544 C CG2 . ILE B 195 ? 0.4792 0.5062 0.5325 -0.0710 -0.0246 0.0269  212 ILE B CG2 
3545 C CD1 . ILE B 195 ? 0.5286 0.5786 0.5524 -0.0734 -0.0456 0.0284  212 ILE B CD1 
3546 N N   . VAL B 196 ? 0.3579 0.3462 0.3568 -0.0885 -0.0168 0.0067  213 VAL B N   
3547 C CA  . VAL B 196 ? 0.3663 0.3400 0.3543 -0.0830 0.0009  0.0050  213 VAL B CA  
3548 C C   . VAL B 196 ? 0.3812 0.3647 0.3530 -0.0741 0.0036  0.0096  213 VAL B C   
3549 O O   . VAL B 196 ? 0.3722 0.3630 0.3311 -0.0799 -0.0087 0.0075  213 VAL B O   
3550 C CB  . VAL B 196 ? 0.4476 0.4018 0.4254 -0.0966 0.0019  -0.0071 213 VAL B CB  
3551 C CG1 . VAL B 196 ? 0.4543 0.4131 0.4147 -0.1073 -0.0135 -0.0129 213 VAL B CG1 
3552 C CG2 . VAL B 196 ? 0.5336 0.4703 0.5014 -0.0899 0.0225  -0.0086 213 VAL B CG2 
3553 N N   . GLU B 197 ? 0.4427 0.4267 0.4147 -0.0599 0.0204  0.0162  214 GLU B N   
3554 C CA  . GLU B 197 ? 0.5095 0.5073 0.4685 -0.0498 0.0242  0.0215  214 GLU B CA  
3555 C C   . GLU B 197 ? 0.4757 0.4588 0.4150 -0.0504 0.0338  0.0164  214 GLU B C   
3556 O O   . GLU B 197 ? 0.4392 0.4050 0.3793 -0.0465 0.0496  0.0155  214 GLU B O   
3557 C CB  . GLU B 197 ? 0.4979 0.5100 0.4683 -0.0328 0.0366  0.0325  214 GLU B CB  
3558 C CG  . GLU B 197 ? 0.6944 0.7274 0.6533 -0.0237 0.0379  0.0377  214 GLU B CG  
3559 C CD  . GLU B 197 ? 0.6314 0.6811 0.5890 -0.0312 0.0201  0.0362  214 GLU B CD  
3560 O OE1 . GLU B 197 ? 0.6127 0.6644 0.5845 -0.0370 0.0097  0.0358  214 GLU B OE1 
3561 O OE2 . GLU B 197 ? 0.6832 0.7425 0.6257 -0.0318 0.0168  0.0353  214 GLU B OE2 
3562 N N   . LYS B 198 ? 0.4537 0.4426 0.3755 -0.0558 0.0247  0.0131  215 LYS B N   
3563 C CA  . LYS B 198 ? 0.5506 0.5293 0.4521 -0.0559 0.0326  0.0087  215 LYS B CA  
3564 C C   . LYS B 198 ? 0.5356 0.4877 0.4328 -0.0648 0.0394  -0.0011 215 LYS B C   
3565 O O   . LYS B 198 ? 0.5595 0.4979 0.4514 -0.0577 0.0572  -0.0012 215 LYS B O   
3566 C CB  . LYS B 198 ? 0.6293 0.6173 0.5277 -0.0383 0.0491  0.0174  215 LYS B CB  
3567 C CG  . LYS B 198 ? 0.6242 0.6411 0.5232 -0.0314 0.0425  0.0248  215 LYS B CG  
3568 C CD  . LYS B 198 ? 0.7300 0.7601 0.6241 -0.0145 0.0583  0.0329  215 LYS B CD  
3569 C CE  . LYS B 198 ? 0.8353 0.8959 0.7283 -0.0104 0.0512  0.0377  215 LYS B CE  
3570 N NZ  . LYS B 198 ? 0.7680 0.8432 0.6807 -0.0077 0.0462  0.0427  215 LYS B NZ  
3571 N N   . PRO B 199 ? 0.4552 0.4003 0.3545 -0.0805 0.0263  -0.0096 216 PRO B N   
3572 C CA  . PRO B 199 ? 0.4699 0.3916 0.3647 -0.0910 0.0327  -0.0208 216 PRO B CA  
3573 C C   . PRO B 199 ? 0.4936 0.4070 0.3647 -0.0944 0.0365  -0.0275 216 PRO B C   
3574 O O   . PRO B 199 ? 0.5547 0.4811 0.4122 -0.0946 0.0271  -0.0258 216 PRO B O   
3575 C CB  . PRO B 199 ? 0.4784 0.4030 0.3804 -0.1070 0.0144  -0.0275 216 PRO B CB  
3576 C CG  . PRO B 199 ? 0.4502 0.3962 0.3475 -0.1069 -0.0029 -0.0219 216 PRO B CG  
3577 C CD  . PRO B 199 ? 0.4635 0.4225 0.3669 -0.0900 0.0051  -0.0101 216 PRO B CD  
3578 N N   . ALA B 200 ? 0.5839 0.4746 0.4502 -0.0979 0.0508  -0.0357 217 ALA B N   
3579 C CA  . ALA B 200 ? 0.5804 0.4612 0.4242 -0.1050 0.0525  -0.0450 217 ALA B CA  
3580 C C   . ALA B 200 ? 0.6019 0.4906 0.4377 -0.1225 0.0309  -0.0534 217 ALA B C   
3581 O O   . ALA B 200 ? 0.5669 0.4573 0.4150 -0.1329 0.0203  -0.0574 217 ALA B O   
3582 C CB  . ALA B 200 ? 0.5886 0.4417 0.4301 -0.1076 0.0723  -0.0541 217 ALA B CB  
3583 N N   . PRO B 201 ? 0.7213 0.6157 0.5367 -0.1258 0.0242  -0.0559 218 PRO B N   
3584 C CA  . PRO B 201 ? 0.5587 0.4633 0.3662 -0.1407 0.0032  -0.0614 218 PRO B CA  
3585 C C   . PRO B 201 ? 0.6138 0.5083 0.4238 -0.1572 -0.0009 -0.0745 218 PRO B C   
3586 O O   . PRO B 201 ? 0.5899 0.4963 0.4072 -0.1666 -0.0180 -0.0754 218 PRO B O   
3587 C CB  . PRO B 201 ? 0.6276 0.5343 0.4108 -0.1405 0.0031  -0.0632 218 PRO B CB  
3588 C CG  . PRO B 201 ? 0.6837 0.5930 0.4668 -0.1229 0.0174  -0.0533 218 PRO B CG  
3589 C CD  . PRO B 201 ? 0.7944 0.6896 0.5937 -0.1150 0.0346  -0.0519 218 PRO B CD  
3590 N N   . GLU B 202 ? 0.6113 0.4846 0.4165 -0.1610 0.0153  -0.0848 219 GLU B N   
3591 C CA  . GLU B 202 ? 0.6222 0.4858 0.4296 -0.1781 0.0135  -0.0993 219 GLU B CA  
3592 C C   . GLU B 202 ? 0.6284 0.4936 0.4607 -0.1804 0.0111  -0.0978 219 GLU B C   
3593 O O   . GLU B 202 ? 0.6058 0.4707 0.4428 -0.1960 0.0043  -0.1088 219 GLU B O   
3594 C CB  . GLU B 202 ? 0.7034 0.5409 0.5014 -0.1803 0.0351  -0.1106 219 GLU B CB  
3595 C CG  . GLU B 202 ? 0.8777 0.7104 0.6509 -0.1775 0.0412  -0.1133 219 GLU B CG  
3596 C CD  . GLU B 202 ? 1.0252 0.8611 0.7964 -0.1568 0.0512  -0.0987 219 GLU B CD  
3597 O OE1 . GLU B 202 ? 0.7387 0.5754 0.5274 -0.1439 0.0587  -0.0878 219 GLU B OE1 
3598 O OE2 . GLU B 202 ? 1.1010 0.9402 0.8529 -0.1536 0.0517  -0.0981 219 GLU B OE2 
3599 N N   . GLN B 203 ? 0.5847 0.4529 0.4329 -0.1655 0.0168  -0.0848 220 GLN B N   
3600 C CA  . GLN B 203 ? 0.5851 0.4530 0.4578 -0.1656 0.0180  -0.0825 220 GLN B CA  
3601 C C   . GLN B 203 ? 0.5498 0.4406 0.4359 -0.1603 0.0013  -0.0705 220 GLN B C   
3602 O O   . GLN B 203 ? 0.5416 0.4342 0.4487 -0.1578 0.0025  -0.0663 220 GLN B O   
3603 C CB  . GLN B 203 ? 0.5306 0.3805 0.4127 -0.1521 0.0421  -0.0774 220 GLN B CB  
3604 C CG  . GLN B 203 ? 0.5520 0.3757 0.4235 -0.1577 0.0609  -0.0897 220 GLN B CG  
3605 C CD  . GLN B 203 ? 0.5613 0.3653 0.4399 -0.1431 0.0867  -0.0837 220 GLN B CD  
3606 O OE1 . GLN B 203 ? 0.5425 0.3548 0.4289 -0.1251 0.0919  -0.0686 220 GLN B OE1 
3607 N NE2 . GLN B 203 ? 0.5919 0.3699 0.4682 -0.1507 0.1039  -0.0957 220 GLN B NE2 
3608 N N   . ALA B 204 ? 0.5384 0.5313 0.3583 -0.1960 -0.0403 -0.0374 221 ALA B N   
3609 C CA  . ALA B 204 ? 0.4844 0.4890 0.3198 -0.1875 -0.0402 -0.0343 221 ALA B CA  
3610 C C   . ALA B 204 ? 0.4873 0.5112 0.3294 -0.1876 -0.0479 -0.0311 221 ALA B C   
3611 O O   . ALA B 204 ? 0.4879 0.5120 0.3207 -0.1892 -0.0528 -0.0291 221 ALA B O   
3612 C CB  . ALA B 204 ? 0.5527 0.5467 0.3862 -0.1787 -0.0365 -0.0318 221 ALA B CB  
3613 N N   . PRO B 205 ? 0.4534 0.4935 0.3110 -0.1861 -0.0492 -0.0306 222 PRO B N   
3614 C CA  . PRO B 205 ? 0.4795 0.5385 0.3439 -0.1866 -0.0567 -0.0277 222 PRO B CA  
3615 C C   . PRO B 205 ? 0.4799 0.5416 0.3451 -0.1790 -0.0595 -0.0230 222 PRO B C   
3616 O O   . PRO B 205 ? 0.4425 0.5140 0.3062 -0.1805 -0.0663 -0.0205 222 PRO B O   
3617 C CB  . PRO B 205 ? 0.4899 0.5637 0.3718 -0.1855 -0.0559 -0.0285 222 PRO B CB  
3618 C CG  . PRO B 205 ? 0.4721 0.5358 0.3583 -0.1800 -0.0484 -0.0296 222 PRO B CG  
3619 C CD  . PRO B 205 ? 0.4833 0.5260 0.3538 -0.1834 -0.0441 -0.0323 222 PRO B CD  
3620 N N   . THR B 206 ? 0.4399 0.4931 0.3074 -0.1708 -0.0546 -0.0216 223 THR B N   
3621 C CA  . THR B 206 ? 0.4731 0.5269 0.3406 -0.1632 -0.0567 -0.0172 223 THR B CA  
3622 C C   . THR B 206 ? 0.4079 0.4429 0.2686 -0.1582 -0.0499 -0.0176 223 THR B C   
3623 O O   . THR B 206 ? 0.4907 0.5132 0.3465 -0.1611 -0.0443 -0.0213 223 THR B O   
3624 C CB  . THR B 206 ? 0.4675 0.5387 0.3531 -0.1562 -0.0587 -0.0140 223 THR B CB  
3625 O OG1 . THR B 206 ? 0.4131 0.4801 0.3078 -0.1502 -0.0519 -0.0149 223 THR B OG1 
3626 C CG2 . THR B 206 ? 0.5015 0.5913 0.3968 -0.1613 -0.0637 -0.0147 223 THR B CG2 
3627 N N   . THR B 207 ? 0.4498 0.4829 0.3106 -0.1504 -0.0503 -0.0138 224 THR B N   
3628 C CA  . THR B 207 ? 0.4427 0.4599 0.2996 -0.1440 -0.0439 -0.0136 224 THR B CA  
3629 C C   . THR B 207 ? 0.4788 0.5040 0.3514 -0.1343 -0.0419 -0.0109 224 THR B C   
3630 O O   . THR B 207 ? 0.4502 0.4665 0.3214 -0.1271 -0.0387 -0.0090 224 THR B O   
3631 C CB  . THR B 207 ? 0.5296 0.5349 0.3710 -0.1435 -0.0454 -0.0118 224 THR B CB  
3632 O OG1 . THR B 207 ? 0.4907 0.5082 0.3344 -0.1411 -0.0525 -0.0074 224 THR B OG1 
3633 C CG2 . THR B 207 ? 0.5073 0.5012 0.3322 -0.1530 -0.0457 -0.0152 224 THR B CG2 
3634 N N   . LEU B 208 ? 0.4317 0.4735 0.3194 -0.1339 -0.0436 -0.0108 225 LEU B N   
3635 C CA  . LEU B 208 ? 0.4487 0.4996 0.3526 -0.1251 -0.0418 -0.0085 225 LEU B CA  
3636 C C   . LEU B 208 ? 0.4577 0.5027 0.3678 -0.1243 -0.0345 -0.0118 225 LEU B C   
3637 O O   . LEU B 208 ? 0.4651 0.5168 0.3806 -0.1298 -0.0342 -0.0147 225 LEU B O   
3638 C CB  . LEU B 208 ? 0.5202 0.5930 0.4367 -0.1254 -0.0483 -0.0064 225 LEU B CB  
3639 C CG  . LEU B 208 ? 0.6293 0.7147 0.5620 -0.1163 -0.0490 -0.0029 225 LEU B CG  
3640 C CD1 . LEU B 208 ? 0.5747 0.6532 0.5021 -0.1092 -0.0498 0.0011  225 LEU B CD1 
3641 C CD2 . LEU B 208 ? 0.5974 0.7041 0.5411 -0.1185 -0.0559 -0.0014 225 LEU B CD2 
3642 N N   . ALA B 209 ? 0.4165 0.4489 0.3258 -0.1177 -0.0285 -0.0114 226 ALA B N   
3643 C CA  . ALA B 209 ? 0.4690 0.4929 0.3819 -0.1171 -0.0212 -0.0145 226 ALA B CA  
3644 C C   . ALA B 209 ? 0.4091 0.4420 0.3391 -0.1091 -0.0184 -0.0129 226 ALA B C   
3645 O O   . ALA B 209 ? 0.3776 0.4152 0.3130 -0.1014 -0.0198 -0.0092 226 ALA B O   
3646 C CB  . ALA B 209 ? 0.4743 0.4765 0.3743 -0.1158 -0.0157 -0.0157 226 ALA B CB  
3647 N N   . VAL B 210 ? 0.3994 0.4342 0.3375 -0.1110 -0.0144 -0.0159 227 VAL B N   
3648 C CA  . VAL B 210 ? 0.4142 0.4555 0.3678 -0.1038 -0.0108 -0.0150 227 VAL B CA  
3649 C C   . VAL B 210 ? 0.4066 0.4319 0.3570 -0.0969 -0.0043 -0.0145 227 VAL B C   
3650 O O   . VAL B 210 ? 0.4891 0.4982 0.4300 -0.0997 0.0004  -0.0173 227 VAL B O   
3651 C CB  . VAL B 210 ? 0.3927 0.4401 0.3548 -0.1088 -0.0085 -0.0185 227 VAL B CB  
3652 C CG1 . VAL B 210 ? 0.3724 0.4266 0.3505 -0.1016 -0.0046 -0.0176 227 VAL B CG1 
3653 C CG2 . VAL B 210 ? 0.4085 0.4718 0.3738 -0.1157 -0.0148 -0.0190 227 VAL B CG2 
3654 N N   . VAL B 211 ? 0.3447 0.3748 0.3041 -0.0878 -0.0038 -0.0111 228 VAL B N   
3655 C CA  . VAL B 211 ? 0.3404 0.3572 0.2994 -0.0804 0.0026  -0.0105 228 VAL B CA  
3656 C C   . VAL B 211 ? 0.4319 0.4556 0.4068 -0.0763 0.0069  -0.0112 228 VAL B C   
3657 O O   . VAL B 211 ? 0.4526 0.4917 0.4386 -0.0788 0.0047  -0.0119 228 VAL B O   
3658 C CB  . VAL B 211 ? 0.4616 0.4764 0.4181 -0.0728 0.0008  -0.0063 228 VAL B CB  
3659 C CG1 . VAL B 211 ? 0.4978 0.5092 0.4398 -0.0777 -0.0047 -0.0054 228 VAL B CG1 
3660 C CG2 . VAL B 211 ? 0.4075 0.4397 0.3803 -0.0661 -0.0017 -0.0030 228 VAL B CG2 
3661 N N   . GLY B 212 ? 0.3726 0.3845 0.3482 -0.0702 0.0132  -0.0111 229 GLY B N   
3662 C CA  . GLY B 212 ? 0.3875 0.4033 0.3766 -0.0667 0.0180  -0.0121 229 GLY B CA  
3663 C C   . GLY B 212 ? 0.3093 0.3407 0.3143 -0.0590 0.0166  -0.0089 229 GLY B C   
3664 O O   . GLY B 212 ? 0.3524 0.3802 0.3640 -0.0514 0.0212  -0.0077 229 GLY B O   
3665 N N   . ARG B 213 ? 0.3150 0.3638 0.3264 -0.0610 0.0104  -0.0075 230 ARG B N   
3666 C CA  . ARG B 213 ? 0.3052 0.3707 0.3328 -0.0546 0.0085  -0.0048 230 ARG B CA  
3667 C C   . ARG B 213 ? 0.2828 0.3658 0.3183 -0.0609 0.0039  -0.0060 230 ARG B C   
3668 O O   . ARG B 213 ? 0.3025 0.3891 0.3307 -0.0667 -0.0016 -0.0061 230 ARG B O   
3669 C CB  . ARG B 213 ? 0.2723 0.3405 0.2986 -0.0482 0.0045  -0.0003 230 ARG B CB  
3670 C CG  . ARG B 213 ? 0.2812 0.3332 0.3002 -0.0413 0.0086  0.0013  230 ARG B CG  
3671 C CD  . ARG B 213 ? 0.3009 0.3526 0.3317 -0.0338 0.0144  0.0017  230 ARG B CD  
3672 N NE  . ARG B 213 ? 0.2821 0.3203 0.3070 -0.0265 0.0175  0.0040  230 ARG B NE  
3673 C CZ  . ARG B 213 ? 0.3355 0.3545 0.3485 -0.0272 0.0224  0.0023  230 ARG B CZ  
3674 N NH1 . ARG B 213 ? 0.3308 0.3415 0.3366 -0.0347 0.0247  -0.0017 230 ARG B NH1 
3675 N NH2 . ARG B 213 ? 0.3780 0.3861 0.3867 -0.0201 0.0249  0.0045  230 ARG B NH2 
3676 N N   . TYR B 214 ? 0.2728 0.3662 0.3226 -0.0599 0.0063  -0.0072 231 TYR B N   
3677 C CA  . TYR B 214 ? 0.2975 0.4079 0.3561 -0.0657 0.0024  -0.0086 231 TYR B CA  
3678 C C   . TYR B 214 ? 0.2414 0.3682 0.3187 -0.0596 0.0025  -0.0070 231 TYR B C   
3679 O O   . TYR B 214 ? 0.2657 0.3888 0.3497 -0.0526 0.0075  -0.0063 231 TYR B O   
3680 C CB  . TYR B 214 ? 0.2853 0.3914 0.3416 -0.0736 0.0056  -0.0131 231 TYR B CB  
3681 C CG  . TYR B 214 ? 0.2729 0.3605 0.3119 -0.0794 0.0075  -0.0155 231 TYR B CG  
3682 C CD1 . TYR B 214 ? 0.2965 0.3662 0.3286 -0.0756 0.0133  -0.0158 231 TYR B CD1 
3683 C CD2 . TYR B 214 ? 0.3366 0.4250 0.3671 -0.0888 0.0038  -0.0177 231 TYR B CD2 
3684 C CE1 . TYR B 214 ? 0.3338 0.3865 0.3506 -0.0808 0.0152  -0.0181 231 TYR B CE1 
3685 C CE2 . TYR B 214 ? 0.3606 0.4322 0.3758 -0.0942 0.0057  -0.0201 231 TYR B CE2 
3686 C CZ  . TYR B 214 ? 0.3276 0.3814 0.3361 -0.0901 0.0115  -0.0203 231 TYR B CZ  
3687 O OH  . TYR B 214 ? 0.3885 0.4255 0.3823 -0.0955 0.0135  -0.0228 231 TYR B OH  
3688 N N   . VAL B 215 ? 0.2684 0.4134 0.3541 -0.0623 -0.0032 -0.0064 232 VAL B N   
3689 C CA  . VAL B 215 ? 0.2374 0.4000 0.3416 -0.0592 -0.0033 -0.0060 232 VAL B CA  
3690 C C   . VAL B 215 ? 0.2853 0.4577 0.3925 -0.0683 -0.0051 -0.0093 232 VAL B C   
3691 O O   . VAL B 215 ? 0.2686 0.4467 0.3706 -0.0743 -0.0109 -0.0094 232 VAL B O   
3692 C CB  . VAL B 215 ? 0.2476 0.4244 0.3604 -0.0535 -0.0089 -0.0019 232 VAL B CB  
3693 C CG1 . VAL B 215 ? 0.2756 0.4699 0.4078 -0.0502 -0.0085 -0.0018 232 VAL B CG1 
3694 C CG2 . VAL B 215 ? 0.3454 0.5120 0.4536 -0.0449 -0.0078 0.0016  232 VAL B CG2 
3695 N N   . LEU B 216 ? 0.2472 0.4212 0.3625 -0.0695 -0.0002 -0.0121 233 LEU B N   
3696 C CA  . LEU B 216 ? 0.3507 0.5308 0.4672 -0.0786 -0.0008 -0.0157 233 LEU B CA  
3697 C C   . LEU B 216 ? 0.2757 0.4730 0.4105 -0.0773 0.0000  -0.0164 233 LEU B C   
3698 O O   . LEU B 216 ? 0.2629 0.4601 0.4070 -0.0708 0.0047  -0.0159 233 LEU B O   
3699 C CB  . LEU B 216 ? 0.2912 0.4544 0.3979 -0.0831 0.0048  -0.0191 233 LEU B CB  
3700 C CG  . LEU B 216 ? 0.3176 0.4617 0.4061 -0.0846 0.0053  -0.0191 233 LEU B CG  
3701 C CD1 . LEU B 216 ? 0.3330 0.4606 0.4148 -0.0876 0.0119  -0.0223 233 LEU B CD1 
3702 C CD2 . LEU B 216 ? 0.3039 0.4514 0.3831 -0.0921 -0.0011 -0.0194 233 LEU B CD2 
3703 N N   . GLU B 217 ? 0.2520 0.4636 0.3914 -0.0837 -0.0045 -0.0177 234 GLU B N   
3704 C CA  . GLU B 217 ? 0.3198 0.5470 0.4754 -0.0843 -0.0035 -0.0192 234 GLU B CA  
3705 C C   . GLU B 217 ? 0.3117 0.5311 0.4666 -0.0885 0.0027  -0.0230 234 GLU B C   
3706 O O   . GLU B 217 ? 0.2680 0.4734 0.4097 -0.0942 0.0043  -0.0252 234 GLU B O   
3707 C CB  . GLU B 217 ? 0.3186 0.5629 0.4787 -0.0903 -0.0101 -0.0196 234 GLU B CB  
3708 C CG  . GLU B 217 ? 0.3672 0.6224 0.5321 -0.0851 -0.0161 -0.0156 234 GLU B CG  
3709 C CD  . GLU B 217 ? 0.4944 0.7681 0.6658 -0.0904 -0.0228 -0.0158 234 GLU B CD  
3710 O OE1 . GLU B 217 ? 0.4224 0.6950 0.5846 -0.0988 -0.0260 -0.0176 234 GLU B OE1 
3711 O OE2 . GLU B 217 ? 0.5265 0.8160 0.7128 -0.0858 -0.0249 -0.0140 234 GLU B OE2 
3712 N N   . ALA B 218 ? 0.3232 0.4853 0.3629 -0.1713 0.0341  0.0242  235 ALA B N   
3713 C CA  . ALA B 218 ? 0.3562 0.5148 0.3836 -0.1766 0.0347  0.0275  235 ALA B CA  
3714 C C   . ALA B 218 ? 0.3707 0.5109 0.3822 -0.1950 0.0252  0.0365  235 ALA B C   
3715 O O   . ALA B 218 ? 0.3859 0.5156 0.3816 -0.2027 0.0221  0.0401  235 ALA B O   
3716 C CB  . ALA B 218 ? 0.3980 0.5679 0.4350 -0.1669 0.0427  0.0273  235 ALA B CB  
3717 N N   . ALA B 219 ? 0.3868 0.5198 0.4004 -0.2020 0.0194  0.0404  236 ALA B N   
3718 C CA  . ALA B 219 ? 0.4520 0.5626 0.4483 -0.2185 0.0082  0.0491  236 ALA B CA  
3719 C C   . ALA B 219 ? 0.4379 0.5237 0.4141 -0.2269 -0.0032 0.0497  236 ALA B C   
3720 O O   . ALA B 219 ? 0.4785 0.5384 0.4353 -0.2395 -0.0146 0.0571  236 ALA B O   
3721 C CB  . ALA B 219 ? 0.4256 0.5334 0.4286 -0.2224 0.0042  0.0516  236 ALA B CB  
3722 N N   . ILE B 220 ? 0.4385 0.5280 0.4172 -0.2189 -0.0020 0.0411  237 ILE B N   
3723 C CA  . ILE B 220 ? 0.4295 0.4868 0.3857 -0.2066 -0.0149 0.0357  237 ILE B CA  
3724 C C   . ILE B 220 ? 0.4644 0.5070 0.4023 -0.2039 -0.0176 0.0377  237 ILE B C   
3725 O O   . ILE B 220 ? 0.4575 0.4675 0.3730 -0.1999 -0.0316 0.0372  237 ILE B O   
3726 C CB  . ILE B 220 ? 0.4137 0.4791 0.3761 -0.1882 -0.0118 0.0230  237 ILE B CB  
3727 C CG1 . ILE B 220 ? 0.5556 0.5897 0.4958 -0.1747 -0.0254 0.0157  237 ILE B CG1 
3728 C CG2 . ILE B 220 ? 0.4023 0.4940 0.3754 -0.1788 0.0024  0.0178  237 ILE B CG2 
3729 C CD1 . ILE B 220 ? 0.5030 0.5140 0.4353 -0.1774 -0.0389 0.0159  237 ILE B CD1 
3730 N N   . PHE B 221 ? 0.4496 0.5157 0.3966 -0.2053 -0.0047 0.0394  238 PHE B N   
3731 C CA  . PHE B 221 ? 0.4649 0.5192 0.3956 -0.2008 -0.0062 0.0401  238 PHE B CA  
3732 C C   . PHE B 221 ? 0.5421 0.5667 0.4519 -0.2147 -0.0192 0.0505  238 PHE B C   
3733 O O   . PHE B 221 ? 0.4722 0.4677 0.3595 -0.2081 -0.0306 0.0492  238 PHE B O   
3734 C CB  . PHE B 221 ? 0.4473 0.5344 0.3935 -0.2023 0.0106  0.0412  238 PHE B CB  
3735 C CG  . PHE B 221 ? 0.4445 0.5570 0.4069 -0.1867 0.0222  0.0306  238 PHE B CG  
3736 C CD1 . PHE B 221 ? 0.4314 0.5318 0.3840 -0.1682 0.0179  0.0200  238 PHE B CD1 
3737 C CD2 . PHE B 221 ? 0.4148 0.5602 0.4011 -0.1866 0.0360  0.0299  238 PHE B CD2 
3738 C CE1 . PHE B 221 ? 0.3951 0.5191 0.3616 -0.1548 0.0286  0.0103  238 PHE B CE1 
3739 C CE2 . PHE B 221 ? 0.3944 0.5574 0.3933 -0.1688 0.0444  0.0199  238 PHE B CE2 
3740 C CZ  . PHE B 221 ? 0.3477 0.5060 0.3379 -0.1593 0.0431  0.0114  238 PHE B CZ  
3741 N N   . ASP B 222 ? 0.5823 0.6133 0.4988 -0.2340 -0.0184 0.0605  239 ASP B N   
3742 C CA  . ASP B 222 ? 0.6175 0.6207 0.5138 -0.2491 -0.0310 0.0711  239 ASP B CA  
3743 C C   . ASP B 222 ? 0.6560 0.6202 0.5318 -0.2438 -0.0497 0.0689  239 ASP B C   
3744 O O   . ASP B 222 ? 0.6329 0.5654 0.4848 -0.2469 -0.0629 0.0734  239 ASP B O   
3745 C CB  . ASP B 222 ? 0.7119 0.7315 0.6209 -0.2647 -0.0266 0.0792  239 ASP B CB  
3746 C CG  . ASP B 222 ? 0.8479 0.8957 0.7693 -0.2602 -0.0131 0.0794  239 ASP B CG  
3747 O OD1 . ASP B 222 ? 0.6836 0.7309 0.5968 -0.2595 -0.0101 0.0801  239 ASP B OD1 
3748 O OD2 . ASP B 222 ? 0.9256 0.9936 0.8643 -0.2573 -0.0065 0.0784  239 ASP B OD2 
3749 N N   . HIS B 223 ? 0.5914 0.5568 0.4758 -0.2354 -0.0516 0.0617  240 HIS B N   
3750 C CA  . HIS B 223 ? 0.6188 0.5487 0.4849 -0.2299 -0.0693 0.0588  240 HIS B CA  
3751 C C   . HIS B 223 ? 0.6354 0.5457 0.4850 -0.2101 -0.0763 0.0490  240 HIS B C   
3752 O O   . HIS B 223 ? 0.7148 0.5901 0.5430 -0.2069 -0.0932 0.0483  240 HIS B O   
3753 C CB  . HIS B 223 ? 0.6008 0.5394 0.4816 -0.2280 -0.0688 0.0544  240 HIS B CB  
3754 C CG  . HIS B 223 ? 0.5805 0.5321 0.4743 -0.2477 -0.0655 0.0640  240 HIS B CG  
3755 N ND1 . HIS B 223 ? 0.6475 0.5750 0.5276 -0.2636 -0.0778 0.0738  240 HIS B ND1 
3756 C CD2 . HIS B 223 ? 0.5496 0.5362 0.4688 -0.2544 -0.0514 0.0652  240 HIS B CD2 
3757 C CE1 . HIS B 223 ? 0.6261 0.5750 0.5228 -0.2752 -0.0705 0.0795  240 HIS B CE1 
3758 N NE2 . HIS B 223 ? 0.6122 0.5968 0.5327 -0.2663 -0.0544 0.0734  240 HIS B NE2 
3759 N N   . LEU B 224 ? 0.5529 0.4850 0.4117 -0.1967 -0.0644 0.0411  241 LEU B N   
3760 C CA  . LEU B 224 ? 0.5719 0.4874 0.4151 -0.1785 -0.0705 0.0316  241 LEU B CA  
3761 C C   . LEU B 224 ? 0.7064 0.6045 0.5310 -0.1821 -0.0754 0.0375  241 LEU B C   
3762 O O   . LEU B 224 ? 0.7473 0.6220 0.5538 -0.1690 -0.0856 0.0311  241 LEU B O   
3763 C CB  . LEU B 224 ? 0.4848 0.4304 0.3445 -0.1628 -0.0558 0.0206  241 LEU B CB  
3764 C CG  . LEU B 224 ? 0.5193 0.4804 0.3950 -0.1561 -0.0518 0.0127  241 LEU B CG  
3765 C CD1 . LEU B 224 ? 0.4935 0.4889 0.3872 -0.1452 -0.0350 0.0048  241 LEU B CD1 
3766 C CD2 . LEU B 224 ? 0.4500 0.3837 0.3102 -0.1437 -0.0669 0.0037  241 LEU B CD2 
3767 N N   . ARG B 225 ? 0.6441 0.5545 0.4732 -0.1990 -0.0681 0.0489  242 ARG B N   
3768 C CA  . ARG B 225 ? 0.7274 0.6189 0.5371 -0.2051 -0.0742 0.0560  242 ARG B CA  
3769 C C   . ARG B 225 ? 0.8334 0.6842 0.6191 -0.2154 -0.0943 0.0636  242 ARG B C   
3770 O O   . ARG B 225 ? 0.9153 0.7387 0.6787 -0.2139 -0.1055 0.0656  242 ARG B O   
3771 C CB  . ARG B 225 ? 0.6980 0.6165 0.5197 -0.2210 -0.0600 0.0657  242 ARG B CB  
3772 C CG  . ARG B 225 ? 0.6768 0.6335 0.5202 -0.2120 -0.0410 0.0594  242 ARG B CG  
3773 C CD  . ARG B 225 ? 0.6309 0.6105 0.4822 -0.2256 -0.0287 0.0680  242 ARG B CD  
3774 N NE  . ARG B 225 ? 0.6674 0.6833 0.5396 -0.2157 -0.0108 0.0612  242 ARG B NE  
3775 C CZ  . ARG B 225 ? 0.6244 0.6745 0.5224 -0.2194 0.0028  0.0604  242 ARG B CZ  
3776 N NH1 . ARG B 225 ? 0.5778 0.6334 0.4850 -0.2341 0.0018  0.0664  242 ARG B NH1 
3777 N NH2 . ARG B 225 ? 0.5732 0.6528 0.4881 -0.2083 0.0174  0.0532  242 ARG B NH2 
3778 N N   . ALA B 226 ? 1.0768 0.9229 0.8666 -0.2262 -0.0994 0.0680  243 ALA B N   
3779 C CA  . ALA B 226 ? 1.1614 0.9682 0.9287 -0.2354 -0.1193 0.0746  243 ALA B CA  
3780 C C   . ALA B 226 ? 1.2724 1.0477 1.0229 -0.2169 -0.1353 0.0639  243 ALA B C   
3781 O O   . ALA B 226 ? 1.4304 1.1677 1.1564 -0.2194 -0.1535 0.0675  243 ALA B O   
3782 C CB  . ALA B 226 ? 1.0074 0.8208 0.7855 -0.2518 -0.1191 0.0817  243 ALA B CB  
3783 N N   . THR B 227 ? 1.3021 1.0928 1.0651 -0.1984 -0.1291 0.0507  244 THR B N   
3784 C CA  . THR B 227 ? 1.3143 1.0806 1.0651 -0.1806 -0.1430 0.0389  244 THR B CA  
3785 C C   . THR B 227 ? 1.4257 1.1641 1.1533 -0.1685 -0.1551 0.0341  244 THR B C   
3786 O O   . THR B 227 ? 1.3418 1.0784 1.0672 -0.1483 -0.1573 0.0204  244 THR B O   
3787 C CB  . THR B 227 ? 1.1719 0.9660 0.9422 -0.1637 -0.1313 0.0253  244 THR B CB  
3788 N N   . GLU B 234 ? 1.5962 1.3149 1.2936 -0.0245 -0.1833 -0.0727 251 GLU B N   
3789 C CA  . GLU B 234 ? 1.3280 1.0885 1.0501 -0.0286 -0.1608 -0.0712 251 GLU B CA  
3790 C C   . GLU B 234 ? 1.3317 1.1000 1.0663 -0.0488 -0.1553 -0.0573 251 GLU B C   
3791 O O   . GLU B 234 ? 1.2991 1.0539 1.0317 -0.0524 -0.1649 -0.0572 251 GLU B O   
3792 C CB  . GLU B 234 ? 1.3251 1.1070 1.0574 -0.0118 -0.1550 -0.0882 251 GLU B CB  
3793 C CG  . GLU B 234 ? 1.3374 1.1254 1.0642 0.0076  -0.1535 -0.1024 251 GLU B CG  
3794 C CD  . GLU B 234 ? 1.2888 1.1087 1.0304 0.0203  -0.1416 -0.1167 251 GLU B CD  
3795 O OE1 . GLU B 234 ? 1.2105 1.0411 0.9631 0.0162  -0.1387 -0.1175 251 GLU B OE1 
3796 O OE2 . GLU B 234 ? 1.1050 0.9396 0.8471 0.0337  -0.1348 -0.1267 251 GLU B OE2 
3797 N N   . ILE B 235 ? 1.2630 1.0535 1.0103 -0.0617 -0.1400 -0.0461 252 ILE B N   
3798 C CA  . ILE B 235 ? 1.1064 0.9104 0.8686 -0.0801 -0.1323 -0.0341 252 ILE B CA  
3799 C C   . ILE B 235 ? 1.1169 0.9488 0.8991 -0.0751 -0.1217 -0.0419 252 ILE B C   
3800 O O   . ILE B 235 ? 0.9204 0.7811 0.7158 -0.0660 -0.1074 -0.0493 252 ILE B O   
3801 C CB  . ILE B 235 ? 1.0902 0.9132 0.8616 -0.0942 -0.1185 -0.0216 252 ILE B CB  
3802 C CG1 . ILE B 235 ? 1.2513 1.0444 1.0015 -0.1023 -0.1303 -0.0122 252 ILE B CG1 
3803 C CG2 . ILE B 235 ? 0.8054 0.6480 0.5956 -0.1113 -0.1091 -0.0118 252 ILE B CG2 
3804 C CD1 . ILE B 235 ? 1.0965 0.8842 0.8352 -0.0885 -0.1313 -0.0190 252 ILE B CD1 
3805 N N   . GLN B 236 ? 0.9698 0.7932 0.7542 -0.0821 -0.1284 -0.0395 253 GLN B N   
3806 C CA  . GLN B 236 ? 0.9180 0.7627 0.7188 -0.0782 -0.1214 -0.0466 253 GLN B CA  
3807 C C   . GLN B 236 ? 0.7714 0.6432 0.5936 -0.0939 -0.1066 -0.0361 253 GLN B C   
3808 O O   . GLN B 236 ? 0.6758 0.5401 0.4975 -0.1107 -0.1085 -0.0228 253 GLN B O   
3809 C CB  . GLN B 236 ? 1.0264 0.8457 0.8170 -0.0760 -0.1380 -0.0509 253 GLN B CB  
3810 C CG  . GLN B 236 ? 1.1249 0.9247 0.8988 -0.0567 -0.1511 -0.0659 253 GLN B CG  
3811 C CD  . GLN B 236 ? 1.2404 1.0211 1.0078 -0.0533 -0.1655 -0.0720 253 GLN B CD  
3812 O OE1 . GLN B 236 ? 1.1907 0.9651 0.9620 -0.0667 -0.1688 -0.0632 253 GLN B OE1 
3813 N NE2 . GLN B 236 ? 1.2119 0.9841 0.9695 -0.0352 -0.1741 -0.0877 253 GLN B NE2 
3814 N N   . LEU B 237 ? 0.6556 0.5599 0.4966 -0.0885 -0.0918 -0.0422 254 LEU B N   
3815 C CA  . LEU B 237 ? 0.5976 0.5279 0.4598 -0.1023 -0.0787 -0.0335 254 LEU B CA  
3816 C C   . LEU B 237 ? 0.6058 0.5242 0.4699 -0.1140 -0.0869 -0.0275 254 LEU B C   
3817 O O   . LEU B 237 ? 0.5807 0.5061 0.4541 -0.1304 -0.0827 -0.0158 254 LEU B O   
3818 C CB  . LEU B 237 ? 0.5368 0.5009 0.4172 -0.0935 -0.0636 -0.0420 254 LEU B CB  
3819 C CG  . LEU B 237 ? 0.5236 0.5169 0.4276 -0.1055 -0.0498 -0.0351 254 LEU B CG  
3820 C CD1 . LEU B 237 ? 0.4418 0.4432 0.3509 -0.1186 -0.0426 -0.0230 254 LEU B CD1 
3821 C CD2 . LEU B 237 ? 0.5098 0.5332 0.4285 -0.0950 -0.0366 -0.0446 254 LEU B CD2 
3822 N N   . THR B 238 ? 0.5768 0.4769 0.4316 -0.1058 -0.0993 -0.0357 255 THR B N   
3823 C CA  . THR B 238 ? 0.6483 0.5352 0.5036 -0.1159 -0.1082 -0.0308 255 THR B CA  
3824 C C   . THR B 238 ? 0.6346 0.4998 0.4802 -0.1324 -0.1166 -0.0168 255 THR B C   
3825 O O   . THR B 238 ? 0.5818 0.4480 0.4352 -0.1467 -0.1171 -0.0082 255 THR B O   
3826 C CB  . THR B 238 ? 0.6312 0.4971 0.4738 -0.1034 -0.1223 -0.0423 255 THR B CB  
3827 O OG1 . THR B 238 ? 0.7448 0.6339 0.5988 -0.0918 -0.1139 -0.0542 255 THR B OG1 
3828 C CG2 . THR B 238 ? 0.7858 0.6330 0.6255 -0.1138 -0.1336 -0.0367 255 THR B CG2 
3829 N N   . ASP B 239 ? 0.7180 0.5629 0.5460 -0.1311 -0.1238 -0.0143 256 ASP B N   
3830 C CA  . ASP B 239 ? 0.7298 0.5544 0.5473 -0.1479 -0.1316 -0.0004 256 ASP B CA  
3831 C C   . ASP B 239 ? 0.6182 0.4700 0.4534 -0.1641 -0.1166 0.0109  256 ASP B C   
3832 O O   . ASP B 239 ? 0.6487 0.4964 0.4865 -0.1812 -0.1191 0.0217  256 ASP B O   
3833 C CB  . ASP B 239 ? 0.8381 0.6373 0.6334 -0.1429 -0.1416 -0.0001 256 ASP B CB  
3834 C CG  . ASP B 239 ? 1.0366 0.8075 0.8136 -0.1267 -0.1580 -0.0118 256 ASP B CG  
3835 O OD1 . ASP B 239 ? 0.9848 0.7433 0.7598 -0.1255 -0.1675 -0.0152 256 ASP B OD1 
3836 O OD2 . ASP B 239 ? 1.2322 0.9940 0.9970 -0.1147 -0.1615 -0.0180 256 ASP B OD2 
3837 N N   . GLY B 240 ? 0.6011 0.4818 0.4494 -0.1590 -0.1008 0.0080  257 GLY B N   
3838 C CA  . GLY B 240 ? 0.6013 0.5103 0.4680 -0.1731 -0.0861 0.0173  257 GLY B CA  
3839 C C   . GLY B 240 ? 0.5314 0.4580 0.4173 -0.1811 -0.0810 0.0190  257 GLY B C   
3840 O O   . GLY B 240 ? 0.5140 0.4466 0.4075 -0.1983 -0.0788 0.0295  257 GLY B O   
3841 N N   . ILE B 241 ? 0.5488 0.4832 0.4421 -0.1690 -0.0797 0.0085  258 ILE B N   
3842 C CA  . ILE B 241 ? 0.5317 0.4832 0.4435 -0.1758 -0.0749 0.0097  258 ILE B CA  
3843 C C   . ILE B 241 ? 0.5042 0.4319 0.4080 -0.1886 -0.0880 0.0173  258 ILE B C   
3844 O O   . ILE B 241 ? 0.5493 0.4888 0.4661 -0.2033 -0.0839 0.0253  258 ILE B O   
3845 C CB  . ILE B 241 ? 0.5753 0.5380 0.4943 -0.1604 -0.0719 -0.0033 258 ILE B CB  
3846 C CG1 . ILE B 241 ? 0.4981 0.4897 0.4289 -0.1510 -0.0566 -0.0091 258 ILE B CG1 
3847 C CG2 . ILE B 241 ? 0.4236 0.3964 0.3578 -0.1676 -0.0708 -0.0021 258 ILE B CG2 
3848 C CD1 . ILE B 241 ? 0.5355 0.5310 0.4644 -0.1327 -0.0563 -0.0234 258 ILE B CD1 
3849 N N   . ALA B 242 ? 0.5789 0.4726 0.4610 -0.1831 -0.1044 0.0146  259 ALA B N   
3850 C CA  . ALA B 242 ? 0.6025 0.4709 0.4749 -0.1952 -0.1181 0.0220  259 ALA B CA  
3851 C C   . ALA B 242 ? 0.6589 0.5265 0.5304 -0.2149 -0.1168 0.0364  259 ALA B C   
3852 O O   . ALA B 242 ? 0.5983 0.4653 0.4754 -0.2296 -0.1191 0.0442  259 ALA B O   
3853 C CB  . ALA B 242 ? 0.6227 0.4533 0.4701 -0.1856 -0.1365 0.0169  259 ALA B CB  
3854 N N   . ALA B 243 ? 0.6415 0.5090 0.5055 -0.2158 -0.1136 0.0398  260 ALA B N   
3855 C CA  . ALA B 243 ? 0.6367 0.5068 0.5005 -0.2352 -0.1111 0.0532  260 ALA B CA  
3856 C C   . ALA B 243 ? 0.6153 0.5243 0.5060 -0.2451 -0.0942 0.0568  260 ALA B C   
3857 O O   . ALA B 243 ? 0.5652 0.4786 0.4616 -0.2629 -0.0938 0.0665  260 ALA B O   
3858 C CB  . ALA B 243 ? 0.6485 0.5111 0.4984 -0.2330 -0.1110 0.0552  260 ALA B CB  
3859 N N   . LEU B 244 ? 0.5715 0.5091 0.4792 -0.2334 -0.0805 0.0487  261 LEU B N   
3860 C CA  . LEU B 244 ? 0.5628 0.5375 0.4967 -0.2410 -0.0650 0.0508  261 LEU B CA  
3861 C C   . LEU B 244 ? 0.6368 0.6147 0.5820 -0.2486 -0.0675 0.0528  261 LEU B C   
3862 O O   . LEU B 244 ? 0.5902 0.5901 0.5509 -0.2489 -0.0571 0.0566  261 LEU B O   
3863 C CB  . LEU B 244 ? 0.5081 0.5085 0.4561 -0.2251 -0.0524 0.0404  261 LEU B CB  
3864 C CG  . LEU B 244 ? 0.5239 0.5632 0.4992 -0.2305 -0.0363 0.0413  261 LEU B CG  
3865 C CD1 . LEU B 244 ? 0.5896 0.6409 0.5677 -0.2347 -0.0280 0.0487  261 LEU B CD1 
3866 C CD2 . LEU B 244 ? 0.5751 0.6348 0.5610 -0.2137 -0.0262 0.0305  261 LEU B CD2 
3867 N N   . LEU B 245 ? 0.7123 0.6693 0.6491 -0.2418 -0.0789 0.0474  262 LEU B N   
3868 C CA  . LEU B 245 ? 0.7434 0.7019 0.6897 -0.2454 -0.0813 0.0484  262 LEU B CA  
3869 C C   . LEU B 245 ? 0.7104 0.6652 0.6548 -0.2546 -0.0823 0.0589  262 LEU B C   
3870 O O   . LEU B 245 ? 0.7541 0.7248 0.7135 -0.2540 -0.0762 0.0600  262 LEU B O   
3871 C CB  . LEU B 245 ? 0.6518 0.5815 0.5837 -0.2387 -0.0966 0.0421  262 LEU B CB  
3872 C CG  . LEU B 245 ? 0.6786 0.6161 0.6153 -0.2200 -0.0937 0.0289  262 LEU B CG  
3873 C CD1 . LEU B 245 ? 0.6907 0.5973 0.6099 -0.2116 -0.1095 0.0231  262 LEU B CD1 
3874 C CD2 . LEU B 245 ? 0.7196 0.6859 0.6806 -0.2223 -0.0833 0.0271  262 LEU B CD2 
3875 N N   . ARG B 246 ? 0.7263 0.6602 0.6518 -0.2629 -0.0903 0.0661  263 ARG B N   
3876 C CA  . ARG B 246 ? 0.7723 0.7013 0.6931 -0.2724 -0.0929 0.0756  263 ARG B CA  
3877 C C   . ARG B 246 ? 0.7755 0.7373 0.7136 -0.2739 -0.0772 0.0784  263 ARG B C   
3878 O O   . ARG B 246 ? 0.9013 0.8655 0.8400 -0.2807 -0.0774 0.0842  263 ARG B O   
3879 C CB  . ARG B 246 ? 0.8700 0.7645 0.7633 -0.2802 -0.1075 0.0821  263 ARG B CB  
3880 C CG  . ARG B 246 ? 0.9021 0.7618 0.7775 -0.2752 -0.1241 0.0768  263 ARG B CG  
3881 C CD  . ARG B 246 ? 1.0583 0.8798 0.9053 -0.2806 -0.1406 0.0824  263 ARG B CD  
3882 N NE  . ARG B 246 ? 1.2291 1.0180 1.0604 -0.2717 -0.1569 0.0745  263 ARG B NE  
3883 C CZ  . ARG B 246 ? 1.3260 1.0763 1.1322 -0.2721 -0.1749 0.0768  263 ARG B CZ  
3884 N NH1 . ARG B 246 ? 1.2846 1.0223 1.0771 -0.2828 -0.1797 0.0881  263 ARG B NH1 
3885 N NH2 . ARG B 246 ? 1.3183 1.0448 1.1130 -0.2582 -0.1875 0.0668  263 ARG B NH2 
3886 N N   . GLU B 247 ? 0.7441 0.7736 0.8089 -0.1679 -0.1031 0.0367  264 GLU B N   
3887 C CA  . GLU B 247 ? 0.7119 0.7551 0.8016 -0.1664 -0.1005 0.0399  264 GLU B CA  
3888 C C   . GLU B 247 ? 0.6578 0.7166 0.7619 -0.1646 -0.1082 0.0443  264 GLU B C   
3889 O O   . GLU B 247 ? 0.6823 0.7537 0.8098 -0.1675 -0.1110 0.0467  264 GLU B O   
3890 C CB  . GLU B 247 ? 0.7650 0.8040 0.8525 -0.1588 -0.0889 0.0401  264 GLU B CB  
3891 C CG  . GLU B 247 ? 0.9102 0.9616 1.0216 -0.1568 -0.0844 0.0433  264 GLU B CG  
3892 C CD  . GLU B 247 ? 0.9186 0.9669 1.0255 -0.1481 -0.0754 0.0444  264 GLU B CD  
3893 O OE1 . GLU B 247 ? 0.8400 0.8763 0.9267 -0.1438 -0.0721 0.0425  264 GLU B OE1 
3894 O OE2 . GLU B 247 ? 0.8231 0.8809 0.9474 -0.1458 -0.0718 0.0471  264 GLU B OE2 
3895 N N   . ARG B 248 ? 0.5743 0.6319 0.6651 -0.1601 -0.1120 0.0454  265 ARG B N   
3896 C CA  . ARG B 248 ? 0.5751 0.6464 0.6780 -0.1567 -0.1175 0.0498  265 ARG B CA  
3897 C C   . ARG B 248 ? 0.5255 0.5943 0.6141 -0.1587 -0.1276 0.0502  265 ARG B C   
3898 O O   . ARG B 248 ? 0.5033 0.5586 0.5703 -0.1614 -0.1287 0.0467  265 ARG B O   
3899 C CB  . ARG B 248 ? 0.6033 0.6766 0.7061 -0.1471 -0.1094 0.0516  265 ARG B CB  
3900 C CG  . ARG B 248 ? 0.6633 0.7342 0.7727 -0.1444 -0.0982 0.0507  265 ARG B CG  
3901 C CD  . ARG B 248 ? 0.7650 0.8486 0.9012 -0.1470 -0.0976 0.0531  265 ARG B CD  
3902 N NE  . ARG B 248 ? 0.7386 0.8365 0.8902 -0.1431 -0.1010 0.0576  265 ARG B NE  
3903 C CZ  . ARG B 248 ? 0.7633 0.8641 0.9165 -0.1355 -0.0951 0.0595  265 ARG B CZ  
3904 N NH1 . ARG B 248 ? 0.7985 0.8890 0.9390 -0.1308 -0.0860 0.0576  265 ARG B NH1 
3905 N NH2 . ARG B 248 ? 0.7837 0.8978 0.9521 -0.1328 -0.0988 0.0636  265 ARG B NH2 
3906 N N   . ASP B 249 ? 0.4742 0.5551 0.5744 -0.1574 -0.1349 0.0544  266 ASP B N   
3907 C CA  . ASP B 249 ? 0.5322 0.6106 0.6187 -0.1591 -0.1447 0.0553  266 ASP B CA  
3908 C C   . ASP B 249 ? 0.4915 0.5621 0.5580 -0.1518 -0.1397 0.0548  266 ASP B C   
3909 O O   . ASP B 249 ? 0.4525 0.5287 0.5256 -0.1442 -0.1333 0.0567  266 ASP B O   
3910 C CB  . ASP B 249 ? 0.5875 0.6812 0.6937 -0.1601 -0.1546 0.0604  266 ASP B CB  
3911 C CG  . ASP B 249 ? 0.6046 0.7051 0.7299 -0.1664 -0.1599 0.0607  266 ASP B CG  
3912 O OD1 . ASP B 249 ? 0.6484 0.7405 0.7669 -0.1732 -0.1606 0.0571  266 ASP B OD1 
3913 O OD2 . ASP B 249 ? 0.7574 0.8694 0.9025 -0.1624 -0.1612 0.0637  266 ASP B OD2 
3914 N N   . VAL B 250 ? 0.4686 0.5260 0.5111 -0.1544 -0.1427 0.0521  267 VAL B N   
3915 C CA  . VAL B 250 ? 0.4667 0.5158 0.4899 -0.1484 -0.1385 0.0514  267 VAL B CA  
3916 C C   . VAL B 250 ? 0.4099 0.4546 0.4186 -0.1523 -0.1483 0.0522  267 VAL B C   
3917 O O   . VAL B 250 ? 0.4014 0.4381 0.3996 -0.1601 -0.1549 0.0502  267 VAL B O   
3918 C CB  . VAL B 250 ? 0.4108 0.4443 0.4159 -0.1467 -0.1289 0.0464  267 VAL B CB  
3919 C CG1 . VAL B 250 ? 0.3820 0.4079 0.3701 -0.1404 -0.1245 0.0457  267 VAL B CG1 
3920 C CG2 . VAL B 250 ? 0.4913 0.5278 0.5096 -0.1434 -0.1199 0.0458  267 VAL B CG2 
3921 N N   . TYR B 251 ? 0.3995 0.4483 0.4064 -0.1470 -0.1493 0.0552  268 TYR B N   
3922 C CA  . TYR B 251 ? 0.4294 0.4737 0.4219 -0.1499 -0.1582 0.0567  268 TYR B CA  
3923 C C   . TYR B 251 ? 0.4176 0.4493 0.3874 -0.1450 -0.1511 0.0544  268 TYR B C   
3924 O O   . TYR B 251 ? 0.3880 0.4189 0.3590 -0.1380 -0.1406 0.0531  268 TYR B O   
3925 C CB  . TYR B 251 ? 0.4582 0.5179 0.4687 -0.1484 -0.1662 0.0626  268 TYR B CB  
3926 C CG  . TYR B 251 ? 0.4781 0.5509 0.5135 -0.1532 -0.1732 0.0650  268 TYR B CG  
3927 C CD1 . TYR B 251 ? 0.4947 0.5656 0.5287 -0.1617 -0.1851 0.0653  268 TYR B CD1 
3928 C CD2 . TYR B 251 ? 0.4817 0.5675 0.5420 -0.1490 -0.1672 0.0666  268 TYR B CD2 
3929 C CE1 . TYR B 251 ? 0.4843 0.5650 0.5417 -0.1625 -0.1869 0.0665  268 TYR B CE1 
3930 C CE2 . TYR B 251 ? 0.5372 0.6341 0.6213 -0.1527 -0.1714 0.0683  268 TYR B CE2 
3931 C CZ  . TYR B 251 ? 0.5210 0.6147 0.6035 -0.1579 -0.1797 0.0679  268 TYR B CZ  
3932 O OH  . TYR B 251 ? 0.6105 0.7134 0.7165 -0.1585 -0.1802 0.0687  268 TYR B OH  
3933 N N   . ALA B 252 ? 0.5071 0.5280 0.4561 -0.1490 -0.1570 0.0539  269 ALA B N   
3934 C CA  . ALA B 252 ? 0.5103 0.5186 0.4373 -0.1452 -0.1508 0.0520  269 ALA B CA  
3935 C C   . ALA B 252 ? 0.4084 0.4195 0.3312 -0.1453 -0.1587 0.0562  269 ALA B C   
3936 O O   . ALA B 252 ? 0.4575 0.4708 0.3813 -0.1517 -0.1707 0.0586  269 ALA B O   
3937 C CB  . ALA B 252 ? 0.5152 0.5035 0.4162 -0.1509 -0.1490 0.0466  269 ALA B CB  
3938 N N   . HIS B 253 ? 0.4230 0.4340 0.3420 -0.1382 -0.1525 0.0573  270 HIS B N   
3939 C CA  . HIS B 253 ? 0.4242 0.4383 0.3404 -0.1377 -0.1595 0.0616  270 HIS B CA  
3940 C C   . HIS B 253 ? 0.4782 0.4769 0.3695 -0.1355 -0.1534 0.0595  270 HIS B C   
3941 O O   . HIS B 253 ? 0.4174 0.4146 0.3088 -0.1285 -0.1419 0.0575  270 HIS B O   
3942 C CB  . HIS B 253 ? 0.4913 0.5242 0.4330 -0.1308 -0.1589 0.0665  270 HIS B CB  
3943 C CG  . HIS B 253 ? 0.4739 0.5108 0.4146 -0.1302 -0.1664 0.0714  270 HIS B CG  
3944 N ND1 . HIS B 253 ? 0.3985 0.4405 0.3444 -0.1361 -0.1802 0.0753  270 HIS B ND1 
3945 C CD2 . HIS B 253 ? 0.5039 0.5402 0.4393 -0.1244 -0.1622 0.0731  270 HIS B CD2 
3946 C CE1 . HIS B 253 ? 0.4965 0.5406 0.4399 -0.1338 -0.1843 0.0794  270 HIS B CE1 
3947 N NE2 . HIS B 253 ? 0.4962 0.5367 0.4329 -0.1268 -0.1732 0.0781  270 HIS B NE2 
3948 N N   . ARG B 254 ? 0.4865 0.4741 0.3574 -0.1414 -0.1612 0.0602  271 ARG B N   
3949 C CA  . ARG B 254 ? 0.5464 0.5182 0.3921 -0.1403 -0.1559 0.0585  271 ARG B CA  
3950 C C   . ARG B 254 ? 0.5587 0.5403 0.4137 -0.1336 -0.1550 0.0631  271 ARG B C   
3951 O O   . ARG B 254 ? 0.5840 0.5687 0.4381 -0.1360 -0.1651 0.0676  271 ARG B O   
3952 C CB  . ARG B 254 ? 0.5325 0.4873 0.3512 -0.1495 -0.1649 0.0578  271 ARG B CB  
3953 C CG  . ARG B 254 ? 0.6041 0.5450 0.4077 -0.1567 -0.1649 0.0526  271 ARG B CG  
3954 C CD  . ARG B 254 ? 0.7929 0.7171 0.5695 -0.1664 -0.1756 0.0525  271 ARG B CD  
3955 N NE  . ARG B 254 ? 0.7708 0.7063 0.5613 -0.1720 -0.1914 0.0567  271 ARG B NE  
3956 C CZ  . ARG B 254 ? 0.8810 0.8170 0.6760 -0.1786 -0.1976 0.0549  271 ARG B CZ  
3957 N NH1 . ARG B 254 ? 0.8217 0.7462 0.6060 -0.1809 -0.1897 0.0490  271 ARG B NH1 
3958 N NH2 . ARG B 254 ? 0.8737 0.8225 0.6877 -0.1817 -0.2101 0.0591  271 ARG B NH2 
3959 N N   . TYR B 255 ? 0.5202 0.5062 0.3841 -0.1253 -0.1431 0.0619  272 TYR B N   
3960 C CA  . TYR B 255 ? 0.4709 0.4665 0.3449 -0.1184 -0.1408 0.0658  272 TYR B CA  
3961 C C   . TYR B 255 ? 0.5614 0.5421 0.4107 -0.1194 -0.1398 0.0657  272 TYR B C   
3962 O O   . TYR B 255 ? 0.5280 0.4899 0.3525 -0.1238 -0.1368 0.0617  272 TYR B O   
3963 C CB  . TYR B 255 ? 0.4916 0.4944 0.3806 -0.1094 -0.1284 0.0641  272 TYR B CB  
3964 C CG  . TYR B 255 ? 0.5015 0.4884 0.3734 -0.1080 -0.1171 0.0584  272 TYR B CG  
3965 C CD1 . TYR B 255 ? 0.5371 0.5136 0.3940 -0.1053 -0.1103 0.0573  272 TYR B CD1 
3966 C CD2 . TYR B 255 ? 0.5690 0.5502 0.4391 -0.1100 -0.1132 0.0540  272 TYR B CD2 
3967 C CE1 . TYR B 255 ? 0.5522 0.5134 0.3940 -0.1043 -0.0997 0.0520  272 TYR B CE1 
3968 C CE2 . TYR B 255 ? 0.5806 0.5466 0.4355 -0.1088 -0.1030 0.0488  272 TYR B CE2 
3969 C CZ  . TYR B 255 ? 0.6021 0.5584 0.4436 -0.1059 -0.0962 0.0478  272 TYR B CZ  
3970 O OH  . TYR B 255 ? 0.6714 0.6125 0.4994 -0.1047 -0.0855 0.0425  272 TYR B OH  
3971 N N   . ASP B 256 ? 0.5285 0.5173 0.3849 -0.1156 -0.1422 0.0704  273 ASP B N   
3972 C CA  . ASP B 256 ? 0.5220 0.4990 0.3588 -0.1148 -0.1393 0.0710  273 ASP B CA  
3973 C C   . ASP B 256 ? 0.5312 0.5096 0.3739 -0.1062 -0.1248 0.0689  273 ASP B C   
3974 O O   . ASP B 256 ? 0.5123 0.5072 0.3790 -0.0996 -0.1222 0.0710  273 ASP B O   
3975 C CB  . ASP B 256 ? 0.6138 0.5992 0.4562 -0.1155 -0.1503 0.0776  273 ASP B CB  
3976 C CG  . ASP B 256 ? 0.7389 0.7111 0.5598 -0.1151 -0.1480 0.0787  273 ASP B CG  
3977 O OD1 . ASP B 256 ? 0.7819 0.7428 0.5901 -0.1121 -0.1355 0.0747  273 ASP B OD1 
3978 O OD2 . ASP B 256 ? 0.9233 0.8965 0.7407 -0.1178 -0.1587 0.0837  273 ASP B OD2 
3979 N N   . GLY B 257 ? 0.5261 0.4871 0.3477 -0.1063 -0.1154 0.0645  274 GLY B N   
3980 C CA  . GLY B 257 ? 0.6237 0.5854 0.4516 -0.0983 -0.1019 0.0623  274 GLY B CA  
3981 C C   . GLY B 257 ? 0.5587 0.5014 0.3672 -0.0995 -0.0912 0.0560  274 GLY B C   
3982 O O   . GLY B 257 ? 0.5826 0.5142 0.3774 -0.1057 -0.0931 0.0528  274 GLY B O   
3983 N N   . LYS B 258 ? 0.5337 0.4732 0.3432 -0.0934 -0.0793 0.0541  275 LYS B N   
3984 C CA  . LYS B 258 ? 0.5945 0.5158 0.3872 -0.0936 -0.0675 0.0482  275 LYS B CA  
3985 C C   . LYS B 258 ? 0.5623 0.4907 0.3741 -0.0873 -0.0592 0.0451  275 LYS B C   
3986 O O   . LYS B 258 ? 0.5177 0.4587 0.3493 -0.0798 -0.0548 0.0465  275 LYS B O   
3987 C CB  . LYS B 258 ? 0.6295 0.5405 0.4097 -0.0915 -0.0593 0.0480  275 LYS B CB  
3988 C CG  . LYS B 258 ? 0.6889 0.5804 0.4525 -0.0916 -0.0458 0.0419  275 LYS B CG  
3989 C CD  . LYS B 258 ? 0.8051 0.6775 0.5419 -0.1007 -0.0489 0.0388  275 LYS B CD  
3990 C CE  . LYS B 258 ? 0.9994 0.8487 0.7142 -0.1021 -0.0352 0.0330  275 LYS B CE  
3991 N NZ  . LYS B 258 ? 1.2125 1.0401 0.8948 -0.1123 -0.0394 0.0309  275 LYS B NZ  
3992 N N   . ARG B 259 ? 0.4978 0.4174 0.3027 -0.0906 -0.0572 0.0409  276 ARG B N   
3993 C CA  . ARG B 259 ? 0.5147 0.4390 0.3354 -0.0856 -0.0506 0.0380  276 ARG B CA  
3994 C C   . ARG B 259 ? 0.5184 0.4277 0.3301 -0.0827 -0.0369 0.0328  276 ARG B C   
3995 O O   . ARG B 259 ? 0.5667 0.4573 0.3553 -0.0881 -0.0333 0.0293  276 ARG B O   
3996 C CB  . ARG B 259 ? 0.5497 0.4732 0.3691 -0.0908 -0.0566 0.0365  276 ARG B CB  
3997 C CG  . ARG B 259 ? 0.5707 0.4946 0.4015 -0.0866 -0.0495 0.0329  276 ARG B CG  
3998 C CD  . ARG B 259 ? 0.6389 0.5587 0.4644 -0.0928 -0.0547 0.0311  276 ARG B CD  
3999 N NE  . ARG B 259 ? 0.6897 0.6058 0.5216 -0.0892 -0.0469 0.0273  276 ARG B NE  
4000 C CZ  . ARG B 259 ? 0.7049 0.6038 0.5217 -0.0915 -0.0399 0.0222  276 ARG B CZ  
4001 N NH1 . ARG B 259 ? 0.7251 0.6076 0.5177 -0.0980 -0.0393 0.0200  276 ARG B NH1 
4002 N NH2 . ARG B 259 ? 0.7197 0.6168 0.5452 -0.0874 -0.0335 0.0194  276 ARG B NH2 
4003 N N   . TYR B 260 ? 0.4490 0.3660 0.2793 -0.0746 -0.0293 0.0322  277 TYR B N   
4004 C CA  . TYR B 260 ? 0.4417 0.3468 0.2695 -0.0710 -0.0163 0.0272  277 TYR B CA  
4005 C C   . TYR B 260 ? 0.4148 0.3230 0.2555 -0.0682 -0.0146 0.0249  277 TYR B C   
4006 O O   . TYR B 260 ? 0.4271 0.3510 0.2893 -0.0631 -0.0177 0.0274  277 TYR B O   
4007 C CB  . TYR B 260 ? 0.4128 0.3229 0.2522 -0.0638 -0.0087 0.0281  277 TYR B CB  
4008 C CG  . TYR B 260 ? 0.4777 0.3840 0.3042 -0.0662 -0.0097 0.0304  277 TYR B CG  
4009 C CD1 . TYR B 260 ? 0.4718 0.3925 0.3061 -0.0660 -0.0192 0.0360  277 TYR B CD1 
4010 C CD2 . TYR B 260 ? 0.5107 0.3978 0.3162 -0.0689 -0.0008 0.0272  277 TYR B CD2 
4011 C CE1 . TYR B 260 ? 0.4922 0.4086 0.3138 -0.0683 -0.0207 0.0385  277 TYR B CE1 
4012 C CE2 . TYR B 260 ? 0.5162 0.3986 0.3084 -0.0713 -0.0016 0.0295  277 TYR B CE2 
4013 C CZ  . TYR B 260 ? 0.5324 0.4293 0.3324 -0.0710 -0.0120 0.0353  277 TYR B CZ  
4014 O OH  . TYR B 260 ? 0.5607 0.4519 0.3464 -0.0735 -0.0134 0.0379  277 TYR B OH  
4015 N N   . ASP B 261 ? 0.4858 0.3783 0.3128 -0.0716 -0.0095 0.0202  278 ASP B N   
4016 C CA  . ASP B 261 ? 0.5244 0.4173 0.3616 -0.0692 -0.0074 0.0178  278 ASP B CA  
4017 C C   . ASP B 261 ? 0.4845 0.3766 0.3352 -0.0610 0.0035  0.0156  278 ASP B C   
4018 O O   . ASP B 261 ? 0.4888 0.3656 0.3304 -0.0609 0.0135  0.0112  278 ASP B O   
4019 C CB  . ASP B 261 ? 0.5391 0.4151 0.3562 -0.0764 -0.0065 0.0137  278 ASP B CB  
4020 C CG  . ASP B 261 ? 0.5946 0.4714 0.4217 -0.0745 -0.0058 0.0117  278 ASP B CG  
4021 O OD1 . ASP B 261 ? 0.5411 0.4272 0.3884 -0.0669 -0.0029 0.0125  278 ASP B OD1 
4022 O OD2 . ASP B 261 ? 0.6645 0.5326 0.4793 -0.0808 -0.0086 0.0097  278 ASP B OD2 
4023 N N   . CYS B 262 ? 0.3970 0.3050 0.2704 -0.0542 0.0017  0.0184  279 CYS B N   
4024 C CA  . CYS B 262 ? 0.4282 0.3363 0.3164 -0.0463 0.0108  0.0166  279 CYS B CA  
4025 C C   . CYS B 262 ? 0.4524 0.3567 0.3488 -0.0434 0.0137  0.0138  279 CYS B C   
4026 O O   . CYS B 262 ? 0.4476 0.3535 0.3594 -0.0365 0.0195  0.0127  279 CYS B O   
4027 C CB  . CYS B 262 ? 0.3704 0.2958 0.2784 -0.0401 0.0079  0.0207  279 CYS B CB  
4028 S SG  . CYS B 262 ? 0.4097 0.3388 0.3101 -0.0421 0.0063  0.0239  279 CYS B SG  
4029 N N   . GLY B 263 ? 0.4525 0.3509 0.3388 -0.0487 0.0098  0.0126  280 GLY B N   
4030 C CA  . GLY B 263 ? 0.5320 0.4244 0.4235 -0.0464 0.0131  0.0098  280 GLY B CA  
4031 C C   . GLY B 263 ? 0.5123 0.3881 0.3978 -0.0451 0.0250  0.0047  280 GLY B C   
4032 O O   . GLY B 263 ? 0.5395 0.4106 0.4326 -0.0417 0.0286  0.0025  280 GLY B O   
4033 N N   . SER B 264 ? 0.5000 0.3657 0.3715 -0.0478 0.0313  0.0028  281 SER B N   
4034 C CA  . SER B 264 ? 0.4782 0.3279 0.3452 -0.0462 0.0441  -0.0021 281 SER B CA  
4035 C C   . SER B 264 ? 0.4643 0.3168 0.3406 -0.0411 0.0514  -0.0019 281 SER B C   
4036 O O   . SER B 264 ? 0.5041 0.3663 0.3813 -0.0412 0.0470  0.0016  281 SER B O   
4037 C CB  . SER B 264 ? 0.5150 0.3452 0.3539 -0.0548 0.0479  -0.0059 281 SER B CB  
4038 O OG  . SER B 264 ? 0.4962 0.3235 0.3199 -0.0590 0.0476  -0.0048 281 SER B OG  
4039 N N   . LYS B 265 ? 0.4450 0.2630 0.3344 0.0422  0.0256  0.0003  282 LYS B N   
4040 C CA  . LYS B 265 ? 0.4941 0.3241 0.3836 0.0439  0.0337  0.0001  282 LYS B CA  
4041 C C   . LYS B 265 ? 0.5227 0.3454 0.3972 0.0414  0.0344  -0.0024 282 LYS B C   
4042 O O   . LYS B 265 ? 0.4418 0.2748 0.3178 0.0382  0.0374  -0.0006 282 LYS B O   
4043 C CB  . LYS B 265 ? 0.5693 0.4014 0.4595 0.0523  0.0405  -0.0023 282 LYS B CB  
4044 C CG  . LYS B 265 ? 0.6568 0.5002 0.5637 0.0547  0.0412  0.0009  282 LYS B CG  
4045 C CD  . LYS B 265 ? 0.7917 0.6345 0.6991 0.0633  0.0466  -0.0018 282 LYS B CD  
4046 C CE  . LYS B 265 ? 0.6644 0.5115 0.5648 0.0675  0.0549  -0.0047 282 LYS B CE  
4047 N NZ  . LYS B 265 ? 0.7333 0.5738 0.6293 0.0761  0.0586  -0.0090 282 LYS B NZ  
4048 N N   . ALA B 266 ? 0.5101 0.3152 0.3701 0.0427  0.0315  -0.0066 283 ALA B N   
4049 C CA  . ALA B 266 ? 0.4799 0.2773 0.3249 0.0401  0.0318  -0.0091 283 ALA B CA  
4050 C C   . ALA B 266 ? 0.5285 0.3270 0.3747 0.0316  0.0261  -0.0059 283 ALA B C   
4051 O O   . ALA B 266 ? 0.4942 0.2968 0.3357 0.0283  0.0282  -0.0055 283 ALA B O   
4052 C CB  . ALA B 266 ? 0.5012 0.2793 0.3311 0.0434  0.0293  -0.0143 283 ALA B CB  
4053 N N   . GLY B 267 ? 0.4721 0.2666 0.3242 0.0279  0.0187  -0.0038 284 GLY B N   
4054 C CA  . GLY B 267 ? 0.4526 0.2482 0.3063 0.0200  0.0130  -0.0010 284 GLY B CA  
4055 C C   . GLY B 267 ? 0.4563 0.2709 0.3227 0.0171  0.0161  0.0030  284 GLY B C   
4056 O O   . GLY B 267 ? 0.4619 0.2794 0.3260 0.0119  0.0152  0.0041  284 GLY B O   
4057 N N   . MET B 268 ? 0.4228 0.2504 0.3029 0.0203  0.0197  0.0051  285 MET B N   
4058 C CA  . MET B 268 ? 0.4810 0.3271 0.3738 0.0179  0.0228  0.0088  285 MET B CA  
4059 C C   . MET B 268 ? 0.4093 0.2607 0.2959 0.0190  0.0297  0.0078  285 MET B C   
4060 O O   . MET B 268 ? 0.4019 0.2629 0.2927 0.0145  0.0301  0.0103  285 MET B O   
4061 C CB  . MET B 268 ? 0.4250 0.2833 0.3331 0.0217  0.0255  0.0110  285 MET B CB  
4062 C CG  . MET B 268 ? 0.4972 0.3751 0.4183 0.0204  0.0297  0.0144  285 MET B CG  
4063 S SD  . MET B 268 ? 0.6391 0.5283 0.5773 0.0150  0.0235  0.0189  285 MET B SD  
4064 C CE  . MET B 268 ? 0.5551 0.4454 0.5014 0.0209  0.0246  0.0192  285 MET B CE  
4065 N N   . PHE B 269 ? 0.4432 0.2892 0.3204 0.0250  0.0351  0.0043  286 PHE B N   
4066 C CA  . PHE B 269 ? 0.4448 0.2949 0.3145 0.0262  0.0416  0.0032  286 PHE B CA  
4067 C C   . PHE B 269 ? 0.4441 0.2867 0.3023 0.0204  0.0383  0.0027  286 PHE B C   
4068 O O   . PHE B 269 ? 0.4365 0.2883 0.2957 0.0172  0.0409  0.0047  286 PHE B O   
4069 C CB  . PHE B 269 ? 0.4968 0.3405 0.3573 0.0339  0.0472  -0.0011 286 PHE B CB  
4070 C CG  . PHE B 269 ? 0.4882 0.3366 0.3406 0.0358  0.0543  -0.0025 286 PHE B CG  
4071 C CD1 . PHE B 269 ? 0.5239 0.3887 0.3854 0.0383  0.0613  -0.0004 286 PHE B CD1 
4072 C CD2 . PHE B 269 ? 0.4840 0.3208 0.3196 0.0348  0.0539  -0.0057 286 PHE B CD2 
4073 C CE1 . PHE B 269 ? 0.5547 0.4246 0.4088 0.0398  0.0679  -0.0013 286 PHE B CE1 
4074 C CE2 . PHE B 269 ? 0.5180 0.3600 0.3459 0.0363  0.0605  -0.0067 286 PHE B CE2 
4075 C CZ  . PHE B 269 ? 0.4700 0.3288 0.3074 0.0388  0.0675  -0.0044 286 PHE B CZ  
4076 N N   . GLN B 270 ? 0.4498 0.2760 0.2975 0.0185  0.0322  0.0004  287 GLN B N   
4077 C CA  . GLN B 270 ? 0.5324 0.3514 0.3693 0.0128  0.0289  0.0001  287 GLN B CA  
4078 C C   . GLN B 270 ? 0.4472 0.2745 0.2939 0.0055  0.0242  0.0043  287 GLN B C   
4079 O O   . GLN B 270 ? 0.4371 0.2656 0.2790 0.0010  0.0238  0.0052  287 GLN B O   
4080 C CB  . GLN B 270 ? 0.5661 0.3654 0.3894 0.0125  0.0233  -0.0034 287 GLN B CB  
4081 C CG  . GLN B 270 ? 0.6886 0.4780 0.4985 0.0190  0.0276  -0.0084 287 GLN B CG  
4082 C CD  . GLN B 270 ? 0.7504 0.5452 0.5519 0.0206  0.0349  -0.0096 287 GLN B CD  
4083 O OE1 . GLN B 270 ? 0.6130 0.4130 0.4127 0.0154  0.0350  -0.0074 287 GLN B OE1 
4084 N NE2 . GLN B 270 ? 0.5446 0.3381 0.3408 0.0280  0.0409  -0.0132 287 GLN B NE2 
4085 N N   . ALA B 271 ? 0.4583 0.2914 0.3187 0.0043  0.0205  0.0068  288 ALA B N   
4086 C CA  . ALA B 271 ? 0.4744 0.3182 0.3462 -0.0019 0.0169  0.0106  288 ALA B CA  
4087 C C   . ALA B 271 ? 0.4295 0.2900 0.3090 -0.0019 0.0230  0.0130  288 ALA B C   
4088 O O   . ALA B 271 ? 0.4047 0.2702 0.2857 -0.0072 0.0213  0.0150  288 ALA B O   
4089 C CB  . ALA B 271 ? 0.4880 0.3362 0.3733 -0.0024 0.0124  0.0127  288 ALA B CB  
4090 N N   . THR B 272 ? 0.3932 0.2622 0.2778 0.0039  0.0299  0.0129  289 THR B N   
4091 C CA  . THR B 272 ? 0.3847 0.2692 0.2761 0.0040  0.0358  0.0152  289 THR B CA  
4092 C C   . THR B 272 ? 0.4161 0.2970 0.2947 0.0022  0.0383  0.0142  289 THR B C   
4093 O O   . THR B 272 ? 0.4055 0.2955 0.2882 -0.0020 0.0386  0.0169  289 THR B O   
4094 C CB  . THR B 272 ? 0.3837 0.2767 0.2814 0.0111  0.0430  0.0149  289 THR B CB  
4095 O OG1 . THR B 272 ? 0.4945 0.3920 0.4050 0.0122  0.0404  0.0163  289 THR B OG1 
4096 C CG2 . THR B 272 ? 0.4383 0.3473 0.3425 0.0115  0.0496  0.0173  289 THR B CG2 
4097 N N   . VAL B 273 ? 0.4211 0.2887 0.2841 0.0052  0.0397  0.0105  290 VAL B N   
4098 C CA  . VAL B 273 ? 0.4251 0.2891 0.2750 0.0034  0.0421  0.0095  290 VAL B CA  
4099 C C   . VAL B 273 ? 0.4220 0.2815 0.2693 -0.0044 0.0352  0.0111  290 VAL B C   
4100 O O   . VAL B 273 ? 0.4514 0.3180 0.2994 -0.0084 0.0361  0.0135  290 VAL B O   
4101 C CB  . VAL B 273 ? 0.4634 0.3135 0.2971 0.0084  0.0444  0.0047  290 VAL B CB  
4102 C CG1 . VAL B 273 ? 0.4681 0.3122 0.2868 0.0056  0.0451  0.0036  290 VAL B CG1 
4103 C CG2 . VAL B 273 ? 0.4492 0.3057 0.2853 0.0161  0.0521  0.0032  290 VAL B CG2 
4104 N N   . ALA B 274 ? 0.4582 0.3059 0.3028 -0.0068 0.0280  0.0100  291 ALA B N   
4105 C CA  . ALA B 274 ? 0.4567 0.2975 0.2963 -0.0139 0.0212  0.0109  291 ALA B CA  
4106 C C   . ALA B 274 ? 0.4397 0.2936 0.2937 -0.0193 0.0184  0.0150  291 ALA B C   
4107 O O   . ALA B 274 ? 0.4170 0.2723 0.2687 -0.0244 0.0165  0.0166  291 ALA B O   
4108 C CB  . ALA B 274 ? 0.5013 0.3267 0.3354 -0.0149 0.0142  0.0087  291 ALA B CB  
4109 N N   . LEU B 275 ? 0.4062 0.2692 0.2752 -0.0184 0.0174  0.0167  292 LEU B N   
4110 C CA  . LEU B 275 ? 0.3725 0.2485 0.2559 -0.0230 0.0146  0.0202  292 LEU B CA  
4111 C C   . LEU B 275 ? 0.3838 0.2752 0.2743 -0.0221 0.0210  0.0225  292 LEU B C   
4112 O O   . LEU B 275 ? 0.4030 0.3022 0.2997 -0.0270 0.0190  0.0250  292 LEU B O   
4113 C CB  . LEU B 275 ? 0.4004 0.2814 0.2972 -0.0225 0.0111  0.0212  292 LEU B CB  
4114 C CG  . LEU B 275 ? 0.4453 0.3138 0.3382 -0.0256 0.0031  0.0201  292 LEU B CG  
4115 C CD1 . LEU B 275 ? 0.6412 0.4931 0.5193 -0.0227 0.0029  0.0168  292 LEU B CD1 
4116 C CD2 . LEU B 275 ? 0.5659 0.4428 0.4740 -0.0248 0.0006  0.0217  292 LEU B CD2 
4117 N N   . GLY B 276 ? 0.3934 0.2889 0.2828 -0.0161 0.0285  0.0217  293 GLY B N   
4118 C CA  . GLY B 276 ? 0.4313 0.3401 0.3250 -0.0155 0.0346  0.0238  293 GLY B CA  
4119 C C   . GLY B 276 ? 0.4685 0.3735 0.3514 -0.0197 0.0343  0.0243  293 GLY B C   
4120 O O   . GLY B 276 ? 0.3984 0.3138 0.2878 -0.0232 0.0348  0.0273  293 GLY B O   
4121 N N   . ARG B 277 ? 0.4271 0.3168 0.2937 -0.0197 0.0330  0.0214  294 ARG B N   
4122 C CA  . ARG B 277 ? 0.4952 0.3805 0.3509 -0.0242 0.0320  0.0219  294 ARG B CA  
4123 C C   . ARG B 277 ? 0.4538 0.3395 0.3153 -0.0317 0.0243  0.0242  294 ARG B C   
4124 O O   . ARG B 277 ? 0.4375 0.3309 0.3022 -0.0358 0.0242  0.0271  294 ARG B O   
4125 C CB  . ARG B 277 ? 0.4422 0.3105 0.2791 -0.0226 0.0316  0.0180  294 ARG B CB  
4126 C CG  . ARG B 277 ? 0.4660 0.3288 0.2901 -0.0275 0.0304  0.0184  294 ARG B CG  
4127 C CD  . ARG B 277 ? 0.4609 0.3328 0.2817 -0.0252 0.0382  0.0194  294 ARG B CD  
4128 N NE  . ARG B 277 ? 0.5186 0.3840 0.3254 -0.0291 0.0374  0.0194  294 ARG B NE  
4129 C CZ  . ARG B 277 ? 0.5287 0.3827 0.3188 -0.0267 0.0392  0.0159  294 ARG B CZ  
4130 N NH1 . ARG B 277 ? 0.5005 0.3470 0.2852 -0.0204 0.0415  0.0117  294 ARG B NH1 
4131 N NH2 . ARG B 277 ? 0.5203 0.3694 0.2988 -0.0310 0.0379  0.0164  294 ARG B NH2 
4132 N N   . LYS B 278 ? 0.5083 0.3862 0.3717 -0.0335 0.0177  0.0232  295 LYS B N   
4133 C CA  . LYS B 278 ? 0.5245 0.3998 0.3901 -0.0405 0.0099  0.0247  295 LYS B CA  
4134 C C   . LYS B 278 ? 0.4674 0.3586 0.3505 -0.0434 0.0086  0.0281  295 LYS B C   
4135 O O   . LYS B 278 ? 0.4551 0.3491 0.3397 -0.0488 0.0054  0.0301  295 LYS B O   
4136 C CB  . LYS B 278 ? 0.5098 0.3730 0.3729 -0.0414 0.0032  0.0226  295 LYS B CB  
4137 C CG  . LYS B 278 ? 0.5707 0.4322 0.4380 -0.0484 -0.0052 0.0240  295 LYS B CG  
4138 C CD  . LYS B 278 ? 0.5615 0.4091 0.4234 -0.0492 -0.0115 0.0218  295 LYS B CD  
4139 C CE  . LYS B 278 ? 0.5951 0.4411 0.4610 -0.0560 -0.0199 0.0231  295 LYS B CE  
4140 N NZ  . LYS B 278 ? 0.5943 0.4270 0.4546 -0.0570 -0.0260 0.0212  295 LYS B NZ  
4141 N N   . TYR B 279 ? 0.4350 0.3369 0.3317 -0.0400 0.0107  0.0288  296 TYR B N   
4142 C CA  . TYR B 279 ? 0.4043 0.3208 0.3181 -0.0427 0.0087  0.0316  296 TYR B CA  
4143 C C   . TYR B 279 ? 0.4539 0.3856 0.3760 -0.0403 0.0155  0.0339  296 TYR B C   
4144 O O   . TYR B 279 ? 0.4364 0.3805 0.3719 -0.0429 0.0140  0.0364  296 TYR B O   
4145 C CB  . TYR B 279 ? 0.4060 0.3257 0.3313 -0.0414 0.0053  0.0312  296 TYR B CB  
4146 C CG  . TYR B 279 ? 0.4525 0.3595 0.3723 -0.0448 -0.0025 0.0297  296 TYR B CG  
4147 C CD1 . TYR B 279 ? 0.5436 0.4495 0.4650 -0.0512 -0.0091 0.0306  296 TYR B CD1 
4148 C CD2 . TYR B 279 ? 0.4820 0.3779 0.3950 -0.0418 -0.0034 0.0273  296 TYR B CD2 
4149 C CE1 . TYR B 279 ? 0.5177 0.4122 0.4340 -0.0544 -0.0162 0.0293  296 TYR B CE1 
4150 C CE2 . TYR B 279 ? 0.4875 0.3715 0.3951 -0.0451 -0.0106 0.0261  296 TYR B CE2 
4151 C CZ  . TYR B 279 ? 0.4993 0.3830 0.4087 -0.0515 -0.0169 0.0271  296 TYR B CZ  
4152 O OH  . TYR B 279 ? 0.5034 0.3758 0.4078 -0.0549 -0.0242 0.0260  296 TYR B OH  
4153 N N   . HIS B 280 ? 0.4312 0.3623 0.3453 -0.0357 0.0228  0.0331  297 HIS B N   
4154 C CA  . HIS B 280 ? 0.4540 0.3995 0.3758 -0.0330 0.0297  0.0353  297 HIS B CA  
4155 C C   . HIS B 280 ? 0.4775 0.4217 0.3874 -0.0324 0.0351  0.0356  297 HIS B C   
4156 O O   . HIS B 280 ? 0.4162 0.3726 0.3317 -0.0304 0.0410  0.0377  297 HIS B O   
4157 C CB  . HIS B 280 ? 0.4175 0.3679 0.3454 -0.0263 0.0345  0.0342  297 HIS B CB  
4158 C CG  . HIS B 280 ? 0.4341 0.3868 0.3737 -0.0266 0.0297  0.0341  297 HIS B CG  
4159 N ND1 . HIS B 280 ? 0.4336 0.4012 0.3903 -0.0276 0.0290  0.0366  297 HIS B ND1 
4160 C CD2 . HIS B 280 ? 0.4466 0.3891 0.3834 -0.0260 0.0253  0.0320  297 HIS B CD2 
4161 C CE1 . HIS B 280 ? 0.4018 0.3688 0.3656 -0.0277 0.0245  0.0360  297 HIS B CE1 
4162 N NE2 . HIS B 280 ? 0.4230 0.3749 0.3752 -0.0268 0.0221  0.0334  297 HIS B NE2 
4163 N N   . GLY B 281 ? 0.4572 0.3875 0.3511 -0.0340 0.0334  0.0337  298 GLY B N   
4164 C CA  . GLY B 281 ? 0.4940 0.4237 0.3764 -0.0336 0.0384  0.0341  298 GLY B CA  
4165 C C   . GLY B 281 ? 0.4455 0.3777 0.3233 -0.0265 0.0470  0.0324  298 GLY B C   
4166 O O   . GLY B 281 ? 0.4749 0.4112 0.3463 -0.0258 0.0522  0.0334  298 GLY B O   
4167 N N   . LEU B 282 ? 0.4283 0.3576 0.3082 -0.0211 0.0482  0.0298  299 LEU B N   
4168 C CA  . LEU B 282 ? 0.4448 0.3764 0.3215 -0.0138 0.0561  0.0279  299 LEU B CA  
4169 C C   . LEU B 282 ? 0.4735 0.3900 0.3317 -0.0112 0.0571  0.0238  299 LEU B C   
4170 O O   . LEU B 282 ? 0.4499 0.3526 0.3013 -0.0125 0.0515  0.0214  299 LEU B O   
4171 C CB  . LEU B 282 ? 0.4440 0.3796 0.3324 -0.0093 0.0566  0.0272  299 LEU B CB  
4172 C CG  . LEU B 282 ? 0.4497 0.4004 0.3569 -0.0115 0.0553  0.0309  299 LEU B CG  
4173 C CD1 . LEU B 282 ? 0.4677 0.4205 0.3857 -0.0080 0.0542  0.0301  299 LEU B CD1 
4174 C CD2 . LEU B 282 ? 0.4292 0.3948 0.3416 -0.0100 0.0624  0.0336  299 LEU B CD2 
4175 N N   . ILE B 283 ? 0.4401 0.3597 0.2905 -0.0074 0.0643  0.0230  300 ILE B N   
4176 C CA  . ILE B 283 ? 0.4493 0.3564 0.2814 -0.0051 0.0660  0.0192  300 ILE B CA  
4177 C C   . ILE B 283 ? 0.4644 0.3745 0.2942 0.0032  0.0739  0.0165  300 ILE B C   
4178 O O   . ILE B 283 ? 0.4570 0.3812 0.2933 0.0054  0.0802  0.0186  300 ILE B O   
4179 C CB  . ILE B 283 ? 0.5044 0.4122 0.3269 -0.0098 0.0666  0.0210  300 ILE B CB  
4180 C CG1 . ILE B 283 ? 0.4783 0.3829 0.3034 -0.0181 0.0585  0.0237  300 ILE B CG1 
4181 C CG2 . ILE B 283 ? 0.5251 0.4202 0.3278 -0.0071 0.0687  0.0166  300 ILE B CG2 
4182 C CD1 . ILE B 283 ? 0.5588 0.4652 0.3761 -0.0232 0.0587  0.0261  300 ILE B CD1 
4183 N N   . PRO B 284 ? 0.4557 0.3532 0.2761 0.0078  0.0738  0.0117  301 PRO B N   
4184 C CA  . PRO B 284 ? 0.5165 0.4167 0.3343 0.0160  0.0812  0.0088  301 PRO B CA  
4185 C C   . PRO B 284 ? 0.6000 0.5067 0.4089 0.0173  0.0881  0.0088  301 PRO B C   
4186 O O   . PRO B 284 ? 0.6041 0.5059 0.4014 0.0133  0.0867  0.0089  301 PRO B O   
4187 C CB  . PRO B 284 ? 0.5178 0.4005 0.3247 0.0194  0.0782  0.0035  301 PRO B CB  
4188 C CG  . PRO B 284 ? 0.5487 0.4232 0.3594 0.0139  0.0692  0.0046  301 PRO B CG  
4189 C CD  . PRO B 284 ? 0.5559 0.4365 0.3691 0.0062  0.0666  0.0089  301 PRO B CD  
4190 N N   . GLU B 285 ? 0.6093 0.5281 0.4243 0.0228  0.0955  0.0092  302 GLU B N   
4191 C CA  . GLU B 285 ? 0.7490 0.6731 0.5543 0.0257  0.1028  0.0082  302 GLU B CA  
4192 C C   . GLU B 285 ? 0.8589 0.7707 0.6507 0.0323  0.1047  0.0018  302 GLU B C   
4193 O O   . GLU B 285 ? 0.7624 0.6686 0.5581 0.0374  0.1040  -0.0012 302 GLU B O   
4194 C CB  . GLU B 285 ? 0.7347 0.6771 0.5516 0.0288  0.1099  0.0112  302 GLU B CB  
4195 C CG  . GLU B 285 ? 0.7858 0.7407 0.6152 0.0223  0.1082  0.0174  302 GLU B CG  
4196 C CD  . GLU B 285 ? 0.9160 0.8886 0.7582 0.0256  0.1149  0.0204  302 GLU B CD  
4197 O OE1 . GLU B 285 ? 0.9436 0.9197 0.7822 0.0325  0.1218  0.0178  302 GLU B OE1 
4198 O OE2 . GLU B 285 ? 0.7962 0.7793 0.6525 0.0215  0.1130  0.0251  302 GLU B OE2 
4199 O OXT . GLU B 285 ? 0.8174 0.7248 0.5946 0.0326  0.1069  -0.0005 302 GLU B OXT 
4200 N N   . GLY C .   ? 0.9190 0.7596 0.9503 0.0057  0.1093  -0.1138 401 GLY A N   
4201 C CA  . GLY C .   ? 0.8490 0.6965 0.8919 0.0130  0.0991  -0.1219 401 GLY A CA  
4202 C C   . GLY C .   ? 0.8230 0.6630 0.8653 0.0190  0.0984  -0.1260 401 GLY A C   
4203 O O   . GLY C .   ? 0.8405 0.6820 0.8725 0.0209  0.0969  -0.1332 401 GLY A O   
4204 O OXT . GLY C .   ? 0.7976 0.6299 0.8497 0.0220  0.0993  -0.1223 401 GLY A OXT 
4205 N N   . GLY D .   ? 0.7808 0.7040 0.7665 -0.0225 0.0927  -0.1344 402 GLY A N   
4206 C CA  . GLY D .   ? 0.7749 0.6991 0.7591 -0.0168 0.0879  -0.1434 402 GLY A CA  
4207 C C   . GLY D .   ? 0.7761 0.7082 0.7450 -0.0193 0.0872  -0.1502 402 GLY A C   
4208 O O   . GLY D .   ? 0.7745 0.7153 0.7416 -0.0237 0.0865  -0.1492 402 GLY A O   
4209 O OXT . GLY D .   ? 0.7787 0.7088 0.7368 -0.0170 0.0872  -0.1571 402 GLY A OXT 
4222 N N   . GLY G .   ? 0.6962 0.7595 1.2935 0.2348  -0.2278 -0.3725 401 GLY B N   
4223 C CA  . GLY G .   ? 0.6475 0.7033 1.2259 0.2294  -0.2186 -0.3647 401 GLY B CA  
4224 C C   . GLY G .   ? 0.6424 0.6936 1.2341 0.2291  -0.2166 -0.3549 401 GLY B C   
4225 O O   . GLY G .   ? 0.6128 0.6572 1.2113 0.2318  -0.2161 -0.3515 401 GLY B O   
4226 O OXT . GLY G .   ? 0.6818 0.7361 1.2779 0.2260  -0.2154 -0.3501 401 GLY B OXT 
4227 N N   . GLY H .   ? 0.7938 0.9005 1.2578 0.2019  -0.2125 -0.4049 402 GLY B N   
4228 C CA  . GLY H .   ? 0.7878 0.8958 1.2593 0.1989  -0.2105 -0.3968 402 GLY B CA  
4229 C C   . GLY H .   ? 0.6635 0.7806 1.1314 0.1953  -0.2110 -0.3988 402 GLY B C   
4230 O O   . GLY H .   ? 0.6195 0.7390 1.0955 0.1930  -0.2102 -0.3927 402 GLY B O   
4231 O OXT . GLY H .   ? 0.6226 0.7450 1.0796 0.1945  -0.2122 -0.4066 402 GLY B OXT 
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